|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
140-815 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 1464.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITG 219
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 220 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 299
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 300 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDH 379
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 380 AMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKG 459
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 460 QSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMF 539
Cdd:cd14927 321 QSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 540 VLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPDKKRKY 619
Cdd:cd14927 401 ILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRKY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 620 QAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKKAASFQTVSQL 699
Cdd:cd14927 481 EAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDSTEDPKSGVKEKRKKAASFQTVSQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 700 HKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAI 779
Cdd:cd14927 561 HKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAI 640
|
650 660 670
....*....|....*....|....*....|....*.
gi 578836100 780 PDDTFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14927 641 PDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
140-815 |
0e+00 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 1357.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITG 219
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 220 ESGAGKTVNTKRVIQYFAIVAALGdgpgkKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 299
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASS-----KKKKESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 300 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDH 379
Cdd:cd01377 156 TGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 380 AMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKG 459
Cdd:cd01377 236 AFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 460 QSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMF 539
Cdd:cd01377 316 QNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 540 VLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKP-LGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPrpdKKRK 618
Cdd:cd01377 396 VLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKP---KPKK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 619 YQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGScsteppKSGVKEKRKKAASFQTVSQ 698
Cdd:cd01377 473 SEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEES------GGGGGKKKKKGGSFRTVSQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 699 LHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSA 778
Cdd:cd01377 547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
|
650 660 670
....*....|....*....|....*....|....*..
gi 578836100 779 IPDDtFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd01377 627 IPKG-FDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
140-815 |
0e+00 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 1152.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITG 219
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 220 ESGAGKTVNTKRVIQYFAIVAALGDgPGKKAqflatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 299
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIE-SKKKL--------GALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 300 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKpELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDH 379
Cdd:cd14929 152 RGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 380 AMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKG 459
Cdd:cd14929 231 AMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 460 QSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMF 539
Cdd:cd14929 311 QNIEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 540 VLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPDKKrKY 619
Cdd:cd14929 391 VLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKK-KF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 620 QAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPpkSGVKeKRKKAASFQTVSQL 699
Cdd:cd14929 470 EAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSAIQ--FGEK-KRKKGASFQTVASL 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 700 HKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAI 779
Cdd:cd14929 547 HKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTF 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 578836100 780 PDDTFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14929 627 PKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
141-815 |
0e+00 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 1142.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 141 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITGE 220
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 221 SGAGKTVNTKRVIQYFAIVAALGDgPGKKAQflaTKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 300
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGD-LAKKKD---SKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 301 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDHA 380
Cdd:cd14913 158 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 381 MDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQ 460
Cdd:cd14913 238 IDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 461 SVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFV 540
Cdd:cd14913 318 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 541 LEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPDKKRKyQ 620
Cdd:cd14913 398 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRA-E 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 621 AHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAgscSTEPPKSGVKEKRKKAASFQTVSQLH 700
Cdd:cd14913 477 AHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFA---TADADSGKKKVAKKKGSSFQTVSALF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 701 KENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIP 780
Cdd:cd14913 554 RENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIP 633
|
650 660 670
....*....|....*....|....*....|....*
gi 578836100 781 DDTFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14913 634 EGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
141-815 |
0e+00 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 1075.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 141 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITGE 220
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 221 SGAGKTVNTKRVIQYFAIVAALGDgPGKKAQflaTKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 300
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGD-RSKKDQ---TPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 301 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDHA 380
Cdd:cd14917 158 GKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 381 MDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQ 460
Cdd:cd14917 238 FDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 461 SVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFV 540
Cdd:cd14917 318 NVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 541 LEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRpDKKRKYQ 620
Cdd:cd14917 398 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPR-NIKGKPE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 621 AHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGScstEPPKSGVKEKRKKAASFQTVSQLH 700
Cdd:cd14917 477 AHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGA---DAPIEKGKGKAKKGSSFQTVSALH 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 701 KENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIP 780
Cdd:cd14917 554 RENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIP 633
|
650 660 670
....*....|....*....|....*....|....*
gi 578836100 781 DDTFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14917 634 EGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
141-815 |
0e+00 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 1057.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 141 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITGE 220
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 221 SGAGKTVNTKRVIQYFAIVAALGDGPGKKaqfLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 300
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAIGDRSKKE---NPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 301 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDHA 380
Cdd:cd14916 159 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 381 MDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQ 460
Cdd:cd14916 239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 461 SVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFV 540
Cdd:cd14916 319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 541 LEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRpDKKRKYQ 620
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPR-NVKGKQE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 621 AHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSgvKEKRKKAASFQTVSQLH 700
Cdd:cd14916 478 AHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKG--KGGKKKGSSFQTVSALH 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 701 KENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIP 780
Cdd:cd14916 556 RENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIP 635
|
650 660 670
....*....|....*....|....*....|....*
gi 578836100 781 DDTFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14916 636 EGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
129-815 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1054.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 129 EDMAMMTHLNEASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLR 208
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 209 NRDNQSMLITGESGAGKTVNTKRVIQYFAIVAALGDGpgkkaqflatKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSR 288
Cdd:pfam00063 82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSGSA----------GNVGRLEEQILQSNPILEAFGNAKTVRNNNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 289 FGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmNPYDYHFCSQ-GVITVDN 367
Cdd:pfam00063 152 FGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLT-NPKDYHYLSQsGCYTIDG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 368 MNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHP 447
Cdd:pfam00063 231 IDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 448 RVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFT 526
Cdd:pfam00063 311 RIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDvKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 527 NEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIE-KPLGILSILEEECMFPKASDASFRAKLYDNHaGKS 605
Cdd:pfam00063 391 NEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKH 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 606 PNFQQPRPdkkrKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVK- 684
Cdd:pfam00063 469 PHFQKPRL----QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSt 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 685 EKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLY 764
Cdd:pfam00063 545 PKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITF 624
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 578836100 765 TDFRQRYRILNPSAIPDDtFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:pfam00063 625 QEFVQRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
141-815 |
0e+00 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 1030.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 141 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITGE 220
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 221 SGAGKTVNTKRVIQYFAIVAALGDgpgKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 300
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGD---KKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 301 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDHA 380
Cdd:cd14923 159 GKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 381 MDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQ 460
Cdd:cd14923 239 IDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 461 SVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFV 540
Cdd:cd14923 319 NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 541 LEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPdKKRKYQ 620
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKP-AKGKAE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 621 AHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGscsTEPPKSGVKEK--RKKAASFQTVSQ 698
Cdd:cd14923 478 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAG---AEAGDSGGSKKggKKKGSSFQTVSA 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 699 LHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSA 778
Cdd:cd14923 555 VFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASA 634
|
650 660 670
....*....|....*....|....*....|....*..
gi 578836100 779 IPDDTFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14923 635 IPEGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
121-827 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 1022.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 121 NPPRFDLLEDMAMMTHLNEASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVAD 200
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 201 NAYNDMLRNRDNQSMLITGESGAGKTVNTKRVIQYFAivaALGDGPGKKaqflatktgGTLEDQIIEANPAMEAFGNAKT 280
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLA---SVSGSNTEV---------GSVEDQILESNPILEAFGNAKT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 281 LRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMnPYDYHFCSQ 360
Cdd:smart00242 149 LRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 361 G-VITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEA-DGTESADKAAYLMGVSSG 438
Cdd:smart00242 228 GgCLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTvKDKEELSNAAELLGVDPE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 439 DLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSF 518
Cdd:smart00242 308 ELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 519 EQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIE-KPLGILSILEEECMFPKASDASFRAKL 597
Cdd:smart00242 388 EQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 598 YDNHaGKSPNFQQPRpdkkRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGScste 677
Cdd:smart00242 467 NQHH-KKHPHFSKPK----KKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSN---- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 678 ppksgvKEKRKKaasFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQG 757
Cdd:smart00242 538 ------AGSKKR---FQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAG 608
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 758 FPNRLLYTDFRQRYRILNPSAIPDDTfMDSRKATEKLLGSLDLDHTQYQFGHTKVFFKAGLLGVLEELRD 827
Cdd:smart00242 609 FPYRLPFDEFLQRYRVLLPDTWPPWG-GDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
141-815 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 1020.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 141 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITGE 220
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 221 SGAGKTVNTKRVIQYFAIVAALGDGpgKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 300
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEK--KKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 301 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDHA 380
Cdd:cd14910 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 381 MDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQ 460
Cdd:cd14910 240 IEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 461 SVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFV 540
Cdd:cd14910 320 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 541 LEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPdKKRKYQ 620
Cdd:cd14910 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKP-AKGKVE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 621 AHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLyenYAGSCSTEPPKSGVKE-KRKKAASFQTVSQL 699
Cdd:cd14910 479 AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALL---FSGAAAAEAEEGGGKKgGKKKGSSFQTVSAL 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 700 HKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAI 779
Cdd:cd14910 556 FRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAI 635
|
650 660 670
....*....|....*....|....*....|....*.
gi 578836100 780 PDDTFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14910 636 PEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
141-815 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 1018.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 141 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITGE 220
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 221 SGAGKTVNTKRVIQYFAIVAALGDGpgKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 300
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEK--KKEEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 301 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDHA 380
Cdd:cd14915 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 381 MDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQ 460
Cdd:cd14915 240 VDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 461 SVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFV 540
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 541 LEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPdKKRKYQ 620
Cdd:cd14915 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKP-AKGKAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 621 AHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYEnyAGSCSTEPPKSGVKEKRKKAASFQTVSQLH 700
Cdd:cd14915 479 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFS--GGQTAEAEGGGGKKGGKKKGSSFQTVSALF 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 701 KENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIP 780
Cdd:cd14915 557 RENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 636
|
650 660 670
....*....|....*....|....*....|....*
gi 578836100 781 DDTFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14915 637 EGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
142-815 |
0e+00 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 1014.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 142 VLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITGES 221
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 222 GAGKTVNTKRVIQYFAIVAALGDgpgkKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPSG 301
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGE----KKKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 302 KLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDHAM 381
Cdd:cd14918 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 382 DILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQS 461
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 462 VEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVL 541
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 542 EQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPdKKRKYQA 621
Cdd:cd14918 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKV-VKGKAEA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 622 HFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAgscSTEPPKSGVKEKRKKAASFQTVSQLHK 701
Cdd:cd14918 478 HFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYA---SAEADSGAKKGAKKKGSSFQTVSALFR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 702 ENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPD 781
Cdd:cd14918 555 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPE 634
|
650 660 670
....*....|....*....|....*....|....
gi 578836100 782 DTFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14918 635 GQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
140-815 |
0e+00 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 1009.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITG 219
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 220 ESGAGKTVNTKRVIQYFAIVAALGdgpgkKAQFLATktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 299
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTG-----KQSSDGK---GSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 300 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDH 379
Cdd:cd14934 153 TGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 380 AMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKG 459
Cdd:cd14934 233 AFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 460 QSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMF 539
Cdd:cd14934 313 QNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 540 VLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPDKKRKY 619
Cdd:cd14934 393 VLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKGP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 620 QAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENyagscstEPPKSGVKeKRKKAASFQTVSQL 699
Cdd:cd14934 473 EAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKE-------EEAPAGSK-KQKRGSSFMTVSNF 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 700 HKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAI 779
Cdd:cd14934 545 YREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVI 624
|
650 660 670
....*....|....*....|....*....|....*.
gi 578836100 780 PDDtFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14934 625 PQG-FVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
141-815 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 1006.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 141 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITGE 220
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 221 SGAGKTVNTKRVIQYFAIVAALGDGpgKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 300
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEK--KKEEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 301 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDHA 380
Cdd:cd14912 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 381 MDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQ 460
Cdd:cd14912 240 IDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 461 SVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFV 540
Cdd:cd14912 320 TVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 541 LEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPdKKRKYQ 620
Cdd:cd14912 400 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKV-VKGKAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 621 AHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENyAGSCSTEPPKSGVKE-KRKKAASFQTVSQL 699
Cdd:cd14912 479 AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSG-AQTAEGASAGGGAKKgGKKKGSSFQTVSAL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 700 HKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAI 779
Cdd:cd14912 558 FRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAI 637
|
650 660 670
....*....|....*....|....*....|....*.
gi 578836100 780 PDDTFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14912 638 PEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
140-815 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 1003.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITG 219
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 220 ESGAGKTVNTKRVIQYFAIVAAlgdgPGKKAQflATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 299
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGA----SKKTDE--AAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 300 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDH 379
Cdd:cd14909 155 TGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 380 AMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKG 459
Cdd:cd14909 235 AFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 460 QSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMF 539
Cdd:cd14909 315 RNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 540 VLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPDKKRKY 619
Cdd:cd14909 395 VLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 620 QAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGscSTEPPKSGVKEKRKKAASFQTVSQL 699
Cdd:cd14909 475 AAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAG--QSGGGEQAKGGRGKKGGGFATVSSA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 700 HKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAI 779
Cdd:cd14909 553 YKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGI 632
|
650 660 670
....*....|....*....|....*....|....*.
gi 578836100 780 PDDTfmDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14909 633 QGEE--DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
65-1148 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 882.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 65 KVHTIPW-DGKKRVWV--PDEQDAYVEAEVKSEATGGRVTVETKDQKVLMVREaelqpMNPPRFDLLEDMAMMTHLNEAS 141
Cdd:COG5022 7 EVGSGCWiPDEEKGWIwaEIIKEAFNKGKVTEEGKKEDGESVSVKKKVLGNDR-----IKLPKFDGVDDLTELSYLNEPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 142 VLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITGES 221
Cdd:COG5022 82 VLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 222 GAGKTVNTKRVIQYFAIVAAlGDGPGKkaqflatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPSG 301
Cdd:COG5022 162 GAGKTENAKRIMQYLASVTS-SSTVEI----------SSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 302 KLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmNPYDYHFCSQG-VITVDNMNDGEELIATDHA 380
Cdd:COG5022 231 EICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQ-NPKDYIYLSQGgCDKIDGIDDAKEFKITLDA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 381 MDILGFSVDEKCACYKIVGALLHFGNMKFKqKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQ 460
Cdd:COG5022 310 LKTIGIDEEEQDQIFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 461 SVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFV 540
Cdd:COG5022 389 NLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 541 LEQEEYKREGIDWVFIDFgLDLQPCIDLIEK--PLGILSILEEECMFPKASDASFRAKLYDN-HAGKSPNFQqprpdKKR 617
Cdd:COG5022 469 LEQEEYVKEGIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFK-----KSR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 618 KYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYagscsteppksgvkEKRKKAASFQTVS 697
Cdd:COG5022 543 FRDNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDE--------------ENIESKGRFPTLG 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 698 QLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPS 777
Cdd:COG5022 609 SRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPS 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 778 AIPDDTFM---DSRKATEKLLGSLDLDHTQYQFGHTKVFFKAGLLGVLEELRDQRLAKVLTLLQARSRGRLMRLEYQRLL 854
Cdd:COG5022 689 KSWTGEYTwkeDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQAL 768
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 855 GGRDALFTIQWNIRAFNAVKNWSWMKLFFKMKPLLRSAQAEEELAALRAELRGLRGALaAAEAKRQELEETHVSITQEKN 934
Cdd:COG5022 769 KRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTI-KREKKLRETEEVEFSLKAEVL 847
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 935 DLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLEDEEEVNAdLAARRRKLEDECTELKKDID-----DLELT 1009
Cdd:COG5022 848 IQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISS-LKLVNLELESEIIELKKSLSsdlieNLEFK 926
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1010 LAKAEKEKQATEN-KVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLE 1088
Cdd:COG5022 927 TELIARLKKLLNNiDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSK 1006
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578836100 1089 QEKKLRMDTERAKRKLEGDLKLTQE----SVADAAQDKQQLEEKLKKK-DSELSQLSLRVEDEQL 1148
Cdd:COG5022 1007 QYGALQESTKQLKELPVEVAELQSAskiiSSESTELSILKPLQKLKGLlLLENNQLQARYKALKL 1071
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
140-815 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 843.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDS-PPHIYAVADNAYNDMLRNRDNQSMLIT 218
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSADlPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 219 GESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQflatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 298
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSA-------SSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 299 PSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMNPYDYHF----CSQGVITVDNMNDGEEL 374
Cdd:cd00124 154 PTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylNSSGCDRIDGVDDAEEF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 375 IATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREE--QAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVG 452
Cdd:cd00124 234 QELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 453 NEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQF--FIGVLDIAGFEIFEFNSFEQLCINFTNEKL 530
Cdd:cd00124 314 GETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEStsFIGILDIFGFENFEVNSFEQLCINYANEKL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 531 QQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIE-KPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFq 609
Cdd:cd00124 394 QQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFF- 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 610 qprpDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSqnrllatlyenyagscsteppksgvkekrkk 689
Cdd:cd00124 472 ----SKKRKAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSG------------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 690 aASFqtvsqlhKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQ 769
Cdd:cd00124 517 -SQF-------RSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLK 588
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 578836100 770 RYRILNPSAIPDDtFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd00124 589 RYRILAPGATEKA-SDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
140-815 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 803.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITG 219
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 220 ESGAGKTVNTKRVIQYFAIVAAL---GDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIH 296
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkpkGSGAVPHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 297 FGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmNPYDYHFCSQGVITVDNMNDGEELIA 376
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 377 TDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYV 456
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 457 TKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFN 535
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 536 QHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAgKSPNFqqprpdK 615
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHS-MHPKF------M 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 616 KRKYQ--AHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVK-EKRKKAAS 692
Cdd:cd14911 473 KTDFRgvADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQfGARTRKGM 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 693 FQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYR 772
Cdd:cd14911 553 FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 632
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 578836100 773 ILNPSAIPDDtFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14911 633 LLTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
140-815 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 786.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITG 219
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 220 ESGAGKTVNTKRVIQYFAIVAALGDGpGKKAQFLatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 299
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKG-RKDHNIP-----GELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 300 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQ-DMLLLSMNpyDYHFCSQGVITVDNMNDGEELIATD 378
Cdd:cd14920 155 TGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKsDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 379 HAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTK 458
Cdd:cd14920 233 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 459 GQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQH 537
Cdd:cd14920 313 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 538 MFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPL---GILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQPRpd 614
Cdd:cd14920 393 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPR-- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 615 kKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENY-----AGSCSTEPPKSGVKEKRKK 689
Cdd:cd14920 470 -QLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdrivgLDQVTGMTETAFGSAYKTK 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 690 AASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQ 769
Cdd:cd14920 549 KGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 578836100 770 RYRILNPSAIPdDTFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14920 629 RYEILTPNAIP-KGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
140-815 |
0e+00 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 734.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITG 219
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 220 ESGAGKTVNTKRVIQYFAIVAAlgDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 299
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVAS--SFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 300 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmNPYDYHFCSQGVITVDNMNDGEELIATDH 379
Cdd:cd14932 159 NGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLE-DYSKYRFLSNGNVTIPGQQDKELFAETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 380 AMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKG 459
Cdd:cd14932 238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 460 QSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHM 538
Cdd:cd14932 318 QTQEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 539 FVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPL---GILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQPrpdK 615
Cdd:cd14932 398 FILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQ-GNNPKFQKP---K 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 616 KRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENY---------AGSCSTEppkSGVKEK 686
Cdd:cd14932 474 KLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVdrivgldkvAGMGESL---HGAFKT 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 687 RKkaASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTD 766
Cdd:cd14932 551 RK--GMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 578836100 767 FRQRYRILNPSAIPDDtFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14932 629 FRQRYEILTPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
141-815 |
0e+00 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 722.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 141 SVLHNLRQRYA-RWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITG 219
Cdd:cd01380 2 AVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 220 ESGAGKTVNTKRVIQYFAIVAALGDGpgkkaqflatKTGgtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 299
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSG----------ETQ--VEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 300 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGR-KPELQDmLLLSMNPYDYHFCSQGVITVDNMNDGEELIATD 378
Cdd:cd01380 150 NYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAAsLPELKE-LHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 379 HAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTK 458
Cdd:cd01380 229 KALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 459 GQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQF--FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQ 536
Cdd:cd01380 309 PLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhsFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 537 HMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGK-SPNFQQPRPDK 615
Cdd:cd01380 389 HVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 616 KRkyqahFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRllatlyenyagscsteppksgvkekrKKaasfqT 695
Cdd:cd01380 468 TA-----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR--------------------------KK-----T 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 696 VSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILN 775
Cdd:cd01380 512 VGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLL 591
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 578836100 776 PSAipDDTFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd01380 592 PSK--EWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
140-815 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 711.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITG 219
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 220 ESGAGKTVNTKRVIQYFAIVAAlgDGPGKKaqflATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 299
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVAS--SHKGKK----DTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 300 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQ-DMLLLSMNpyDYHFCSQGVITVDNMNDGEELIATD 378
Cdd:cd14921 155 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRsDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 379 HAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTK 458
Cdd:cd14921 233 EAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 459 GQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQH 537
Cdd:cd14921 313 AQTKEQADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 538 MFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPL---GILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQPrpd 614
Cdd:cd14921 393 MFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKP--- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 615 KKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYEN---------YAGSCSTEPPKSgvke 685
Cdd:cd14921 469 KQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDvdrivgldqMAKMTESSLPSA---- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 686 KRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYT 765
Cdd:cd14921 545 SKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQ 624
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 578836100 766 DFRQRYRILNPSAIPDDtFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14921 625 EFRQRYEILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
140-815 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 697.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITG 219
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 220 ESGAGKTVNTKRVIQYFAIVAAlgDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 299
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVAS--SHKTKKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 300 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmNPYDYHFCSQGVITVDNMNDGEELIATDH 379
Cdd:cd15896 159 NGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLE-NYNNYRFLSNGNVTIPGQQDKDLFTETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 380 AMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKG 459
Cdd:cd15896 238 AFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 460 QSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHM 538
Cdd:cd15896 318 QTQEQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 539 FVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPL---GILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQPrpdK 615
Cdd:cd15896 398 FILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKP---K 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 616 KRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEpPKSGVKEK----RKKAA 691
Cdd:cd15896 474 KLKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLD-KVSGMSEMpgafKTRKG 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 692 SFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRY 771
Cdd:cd15896 553 MFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 632
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 578836100 772 RILNPSAIPDDtFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd15896 633 EILTPNAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
140-815 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 693.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITG 219
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 220 ESGAGKTVNTKRVIQYFAIVAAlgDGPGKKAQflatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 299
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVAS--SHKSKKDQ-------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 300 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmnPYD-YHFCSQGVITVDNMNDGEELIATD 378
Cdd:cd14919 152 NGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLE--PYNkYRFLSNGHVTIPGQQDKDMFQETM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 379 HAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTK 458
Cdd:cd14919 230 EAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 459 GQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQH 537
Cdd:cd14919 310 AQTKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 538 MFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPL---GILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQPrpd 614
Cdd:cd14919 390 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKP--- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 615 KKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYEN---------YAGSCSTEPPksGVKE 685
Cdd:cd14919 466 KQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriigldqVAGMSETALP--GAFK 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 686 KRKkaASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYT 765
Cdd:cd14919 544 TRK--GMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQ 621
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 578836100 766 DFRQRYRILNPSAIPDDtFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14919 622 EFRQRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
140-815 |
0e+00 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 682.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITG 219
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 220 ESGAGKTVNTKRVIQYFAIVAALGDG---PGkkaqflatkTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIH 296
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGrkePG---------VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 297 FGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMNPYdYHFCSQGVITVDNmNDGEELIA 376
Cdd:cd14930 152 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 377 TDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYV 456
Cdd:cd14930 230 TLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 457 TKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDtKLPRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFF 534
Cdd:cd14930 310 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 535 NQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPL---GILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQP 611
Cdd:cd14930 389 NHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 612 RpdkKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKS---GVKEKRK 688
Cdd:cd14930 468 R---HLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSlgdGPPGGRP 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 689 KAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFR 768
Cdd:cd14930 545 RRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFR 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 578836100 769 QRYRILNPSAIPDDtFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14930 625 QRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
140-815 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 668.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITG 219
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 220 ESGAGKTVNTKRVIQYFAIVAalgdgpGKKAqflatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 299
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAIS------GQHS---------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 300 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMnPYDYHFCSQG-VITVDNMNDGEELIATD 378
Cdd:cd01381 146 NGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGD-ASDYYYLTQGnCLTCEGRDDAAEFADIR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 379 HAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQRE--EQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYV 456
Cdd:cd01381 225 SAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 457 TKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFF---IGVLDIAGFEIFEFNSFEQLCINFTNEKLQQF 533
Cdd:cd01381 305 VSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 534 FNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLI-EKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSpNFQQPr 612
Cdd:cd01381 385 FVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNK-NYLKP- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 613 pdkKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSteppksgvkEKRKKAas 692
Cdd:cd01381 462 ---KSDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGS---------ETRKKS-- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 693 fQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYR 772
Cdd:cd01381 528 -PTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYR 606
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 578836100 773 ILNPSaIPDDTFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd01381 607 VLVPG-IPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
141-815 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 658.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 141 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITGE 220
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 221 SGAGKTVNTKRVIQYFAIVAalGDGPGKkaqflatktGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 300
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVS--GGSESE---------VERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 301 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDHA 380
Cdd:cd01378 151 GEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 381 MDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADgTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEY---VT 457
Cdd:cd01378 231 MKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 458 KGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQ-FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQ 536
Cdd:cd01378 310 VPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 537 hmFVL--EQEEYKREGIDWVFIDFgLDLQPCIDLIE-KPLGILSILEEECMFP-KASDASFRAKLydNHAGKSPNFQQPR 612
Cdd:cd01378 390 --LTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL--NQLFSNHPHFECP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 613 PDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYEnyagscstEPPKSGVKeKRKKAAS 692
Cdd:cd01378 465 SGHFELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFP--------EGVDLDSK-KRPPTAG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 693 FQTvsqlhKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYR 772
Cdd:cd01378 536 TKF-----KNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYK 610
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 578836100 773 ILNPSAIPDDTfMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd01378 611 LLSPKTWPAWD-GTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
141-815 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 649.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 141 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITGE 220
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 221 SGAGKTVNTKRVIQYFAIVaalgdgpgkkaqflaTKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 300
Cdd:cd14883 82 SGAGKTETTKLILQYLCAV---------------TNNHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDAS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 301 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRK--PELQDMLLLSmNPYDYHFCSQ-GVITVDNMNDGEELIAT 377
Cdd:cd14883 147 GHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKEKLKLG-EPEDYHYLNQsGCIRIDNINDKKDFDHL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 378 DHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAE-ADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYV 456
Cdd:cd14883 226 RLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 457 TKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQ 536
Cdd:cd14883 306 EIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 537 HMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIEK-PLGILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQPrpdK 615
Cdd:cd14883 386 YVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKP---D 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 616 KRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATL--YENYAGSCSTEPPKSGVKEKRKKAASF 693
Cdd:cd14883 461 RRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELftYPDLLALTGLSISLGGDTTSRGTSKGK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 694 QTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRI 773
Cdd:cd14883 541 PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLC 620
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 578836100 774 LNPSAIPDDTfMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14883 621 LDPRARSADH-KETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
141-815 |
0e+00 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 631.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 141 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKgkRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITGE 220
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 221 SGAGKTVNTKRVIQYfaiVAALGDGpgkkaqflatktGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 300
Cdd:cd01383 80 SGAGKTETAKIAMQY---LAALGGG------------SSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 301 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMnPYDYHFCSQ-GVITVDNMNDGEELIATDH 379
Cdd:cd01383 145 GKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS-ASEYKYLNQsNCLTIDGVDDAKKFHELKE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 380 AMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKG 459
Cdd:cd01383 224 ALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 460 QSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDT-KLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHM 538
Cdd:cd01383 304 LTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 539 FVLEQEEYKREGIDWVFIDFgLDLQPCIDLIE-KPLGILSILEEECMFPKASDASFRAKLyDNHAGKSPNFqqprpdKKR 617
Cdd:cd01383 384 FKLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCF------KGE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 618 KYQAhFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSgvkeKRKKAASF-QTV 696
Cdd:cd01383 456 RGGA-FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFASKMLDASRKALPLT----KASGSDSQkQSV 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 697 SQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNP 776
Cdd:cd01383 531 ATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLP 610
|
650 660 670
....*....|....*....|....*....|....*....
gi 578836100 777 SAIPDDTfmDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd01383 611 EDVSASQ--DPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
140-815 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 594.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLIT 218
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 219 GESGAGKTVNTKRVIQYFAIVAALGDGPGKkaqflatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 298
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGGRAVTEGR-----------SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 299 PSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmNPYDYHFCSQ-GVITVDNMNDGEELIAT 377
Cdd:cd01384 150 DAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLK-DPKQFHYLNQsKCFELDGVDDAEEYRAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 378 DHAMDILGFSVDEKCACYKIVGALLHFGNMKFKqkqreEQAEADGTESADK--------AAYLMGVSSGDLLKGLLHpRV 449
Cdd:cd01384 229 RRAMDVVGISEEEQDAIFRVVAAILHLGNIEFS-----KGEEDDSSVPKDEksefhlkaAAELLMCDEKALEDALCK-RV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 450 RVG-NEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNE 528
Cdd:cd01384 303 IVTpDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 529 KLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIE-KPLGILSILEEECMFPKASDASFRAKLYDNHAGKspn 607
Cdd:cd01384 383 KLQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDH--- 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 608 fqqPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDplneTVVP----IFQKSQNRLLATLYenyagscstePPKSGv 683
Cdd:cd01384 459 ---KRFSKPKLSRTDFTIDHYAGDVTYQTDLFLDKNKD----YVVAehqaLLNASKCPFVAGLF----------PPLPR- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 684 kEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLL 763
Cdd:cd01384 521 -EGTSSSSKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKP 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 578836100 764 YTDFRQRYRILNPSAipDDTFMDSRKATEKLLGSLDLDhtQYQFGHTKVFFK 815
Cdd:cd01384 600 FEEFLDRFGLLAPEV--LKGSDDEKAACKKILEKAGLK--GYQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
140-815 |
0e+00 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 569.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLIT 218
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 219 GESGAGKTVNTKRVIQYfaivaaLGDGPGKKAqflatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 298
Cdd:cd01382 81 GESGAGKTESTKYILRY------LTESWGSGA--------GPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 299 PSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLsmnpydyhfcsqgVITVDNMNDgeeLIATD 378
Cdd:cd01382 147 EKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLK-------------DPLLDDVGD---FIRMD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 379 HAMDILGFSVDEKCACYKIVGALLHFGNMKFkqkqrEEQAE---------ADGTESADKAAYLMGVSSGDLLKGLLHpRV 449
Cdd:cd01382 211 KAMKKIGLSDEEKLDIFRVVAAVLHLGNIEF-----EENGSdsgggcnvkPKSEQSLEYAAELLGLDQDELRVSLTT-RV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 450 RVGNEYVTKGQS------VEQVVFAVGALAKATYDRLFRWLVSRINQTldtkLPRQ---FFIGVLDIAGFEIFEFNSFEQ 520
Cdd:cd01382 285 MQTTRGGAKGTVikvplkVEEANNARDALAKAIYSKLFDHIVNRINQC----IPFEtssYFIGVLDIAGFEYFEVNSFEQ 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 521 LCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIE-KPLGILSILEEECMFPKASDASFRAKLYD 599
Cdd:cd01382 361 FCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 600 NHAgKSPNFQQPRPDKKRKYQA-----HFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYEnyagsc 674
Cdd:cd01382 440 KHK-NHFRLSIPRKSKLKIHRNlrddeGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFE------ 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 675 STEPPKSGVKEKRKKaASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRIC 754
Cdd:cd01382 513 SSTNNNKDSKQKAGK-LSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLM 591
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578836100 755 RQGFPNRLLYTDFRQRYRILNPSAIPDdtfMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd01382 592 QGGFPSRTSFHDLYNMYKKYLPPKLAR---LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
140-815 |
3.61e-179 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 559.39 E-value: 3.61e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLR----NRDNQS 214
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 215 MLITGESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLAT----KTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFG 290
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAASeaieQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 291 KFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmNPYDYHFCSQGVITVDNMND 370
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQ-TPVEYFYLRGECSSIPSCDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 371 GEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGT-ESADKAAYLMGVSSGDLLKGLLHPRV 449
Cdd:cd14890 240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 450 RVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEK 529
Cdd:cd14890 320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 530 LQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIE-KPLGILSILE--EECMFPKASDAS--FRAKLYDNHAGK 604
Cdd:cd14890 400 LQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFItlDDCWRFKGEEANkkFVSQLHASFGRK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 605 S------------PNFQQPRPDKKRkyqaHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLlatlyenyag 672
Cdd:cd14890 479 SgsggtrrgssqhPHFVHPKFDADK----QFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSI---------- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 673 scsteppksgvkekRKKAASFQTVSQLHkenlnKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIR 752
Cdd:cd14890 545 --------------REVSVGAQFRTQLQ-----ELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQ 605
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578836100 753 ICRQGFPNRLLYTDFRQRYRILNPSAIPDDTFMdsrkatEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14890 606 IRQQGFALREEHDSFFYDFQVLLPTAENIEQLV------AVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
140-815 |
1.11e-177 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 554.77 E-value: 1.11e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITG 219
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 220 ESGAGKTVNTKRVIQYFAIVAAlgdgpgkkaqflatKTGGtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 299
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAG--------------STNG-VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 300 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMnpyDYHFCSQ-GVITVDNMNDGEELIATD 378
Cdd:cd14872 146 RGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSA---AYGYLSLsGCIEVEGVDDVADFEEVV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 379 HAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESAD---KAAYLMGVSSGDLLKGLLHPRVRVgney 455
Cdd:cd14872 223 LAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDvlkEVATLLGVDAATLEEALTSRLMEI---- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 456 vtKGQ-------SVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTN 527
Cdd:cd14872 299 --KGCdptriplTPAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 528 EKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEK-PLGILSILEEECMFPKASDASFRAKLYDNHAGKSp 606
Cdd:cd14872 377 EKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 607 NFQqprPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYenyagscstePPKSGvKEK 686
Cdd:cd14872 455 TFV---YAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF----------PPSEG-DQK 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 687 RKKAasfqTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTD 766
Cdd:cd14872 521 TSKV----TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHER 596
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 578836100 767 FRQRYRILnPSAIPDDTFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14872 597 FLKRYRFL-VKTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
140-815 |
6.07e-173 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 542.75 E-value: 6.07e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRRSDSPpHIYAVADNAYNDMLRNRDNQSMLIT 218
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFIQPSISKSP-HVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 219 GESGAGKTVNTKRVIQYFAIVAALgdgpgkkaqflATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF- 297
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSE-----------DIKKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFs 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 298 --------GPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSG-----------------------RKPELQDML 346
Cdd:cd14888 149 klkskrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAareakntglsyeendeklakgadAKPISIDMS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 347 L-LSMNPYDYHFCSqGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQA---EADG 422
Cdd:cd14888 229 SfEPHLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASC 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 423 TESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFF 501
Cdd:cd14888 308 TDDLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 502 IGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLI-EKPLGILSILE 580
Cdd:cd14888 388 CGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLD 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 581 EECMFPKASDASFRAKLYDNHAGKSpnfqqpRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQN 660
Cdd:cd14888 467 EECFVPGGKDQGLCNKLCQKHKGHK------RFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKN 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 661 RLLATLYENYAGSCSTEPPksgvkEKRKkaasFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLH 740
Cdd:cd14888 541 PFISNLFSAYLRRGTDGNT-----KKKK----FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNE 611
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578836100 741 QLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPsaipddtfmdsrkatekllGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14888 612 QLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN-------------------GEGKKQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
141-815 |
7.57e-173 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 541.10 E-value: 7.57e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 141 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITGE 220
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 221 SGAGKTVNTKRVIQYFAivaalgdgpgkkaqFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 300
Cdd:cd01379 82 SGAGKTESANLLVQQLT--------------VLGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTST 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 301 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQ-DMLLLSMNPYDYHFCSQGVITVDNMNDG---EELIA 376
Cdd:cd01379 148 GAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDIVNNSgnrEKFEE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 377 TDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQ----AEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVG 452
Cdd:cd01379 228 IEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVTR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 453 NEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL--DTKLP-RQFFIGVLDIAGFEIFEFNSFEQLCINFTNEK 529
Cdd:cd01379 308 GETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASdEPLSIGILDIFGFENFQKNSFEQLCINIANEQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 530 LQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCID-LIEKPLGILSILEEECMFPKASDASFRAKLYDNHagKSPNF 608
Cdd:cd01379 388 IQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI--KSKYY 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 609 QQPRPDkkrkyQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLAtlyenyagscsteppksgvkekrk 688
Cdd:cd01379 465 WRPKSN-----ALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR------------------------ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 689 kaasfQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFR 768
Cdd:cd01379 516 -----QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFL 590
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 578836100 769 QRYRILNPSAipDDTFMDSRKATEKLLGSLDLDHtqYQFGHTKVFFK 815
Cdd:cd01379 591 KRYYFLAFKW--NEEVVANRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
140-815 |
1.20e-172 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 541.67 E-value: 1.20e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLIT 218
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 219 GESGAGKTVNTKRVIQYFAIVAA-LGDGPGKKaqflatktggtledqIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 297
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAGgLNDSTIKK---------------IIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 298 GPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmNPYDYHFcSQGVITVDNMNDGEELIAT 377
Cdd:cd14903 146 DKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSA-NECAYTG-ANKTIKIEGMSDRKHFART 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 378 DHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAE--ADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEY 455
Cdd:cd14903 224 KEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 456 VTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFN 535
Cdd:cd14903 304 YTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 536 QHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPDK 615
Cdd:cd14903 384 QDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 616 krkyqAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRK--KAASF 693
Cdd:cd14903 463 -----TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRrgGALTT 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 694 QTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRI 773
Cdd:cd14903 538 TTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 578836100 774 LNPSAipDDTFMDSRKATEKLLGSLDLDH-TQYQFGHTKVFFK 815
Cdd:cd14903 618 FLPEG--RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
140-815 |
7.12e-168 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 528.21 E-value: 7.12e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLIT 218
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 219 GESGAGKTVNTKRVIQYFAIVA--ALGDGPGKKAQflatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIH 296
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISqqSLELSLKEKTS--------CVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 297 FGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmNPYDYHFCSQ-GVITVDNMNDGEELI 375
Cdd:cd14873 153 ICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-TPENYHYLNQsGCVEDKTISDQESFR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 376 ATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFkqkqreeqAEADGTESADK-----AAYLMGVSSGDLLKGLLHPRVR 450
Cdd:cd14873 232 EVITAMEVMQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKtalgrSAELLGLDPTQLTDALTQRSMF 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 451 VGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKlpRQF-FIGVLDIAGFEIFEFNSFEQLCINFTNEK 529
Cdd:cd14873 304 LRGEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGK--EDFkSIGILDIFGFENFEVNHFEQFNINYANEK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 530 LQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAgkspnfQ 609
Cdd:cd14873 382 LQEYFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHA------N 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 610 QPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKk 689
Cdd:cd14873 455 NHFYVKPRVAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRP- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 690 aasfqTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQ 769
Cdd:cd14873 534 -----TVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYK 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 578836100 770 RYRILNPSAIPDDtfmDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14873 609 RYKVLMRNLALPE---DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
140-813 |
6.11e-167 |
|
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276866 [Multi-domain] Cd Length: 655 Bit Score: 525.89 E-value: 6.11e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAY------KGKRRSDSPPHIYAVADNAYNDMLRNRD-- 211
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 212 --NQSMLITGESGAGKTVNTKRVIQYFAIVAAlgdgpgKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRF 289
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSS------ATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 290 GKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKP-ELQDMLLLSMNPYDYHFCSQGVITVDNM 368
Cdd:cd14901 155 GKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSdELHALGLTHVEEYKYLNSSQCYDRRDGV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 369 NDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAY-LMGVSSGDLLKGLLHP 447
Cdd:cd14901 235 DDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRAACdLLGLDMDVLEKTLCTR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 448 RVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLP--RQFFIGVLDIAGFEIFEFNSFEQLCINF 525
Cdd:cd14901 315 EIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 526 TNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgldlqP----CIDLIE-KPLGILSILEEECMFPKASDASFRAKLYDN 600
Cdd:cd14901 395 ANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 601 HAGKSP----NFQQPRpdkkrkyqAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATlyenyagscst 676
Cdd:cd14901 470 LAKHASfsvsKLQQGK--------RQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS----------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 677 eppksgvkekrkkaasfqTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQ 756
Cdd:cd14901 531 ------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRS 592
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578836100 757 GFPNRLLYTDFRQRYRILNPSaIPDDTFMdSRKATEKLLGSLDL------DHTQYQFGHTKVF 813
Cdd:cd14901 593 GYPVRFPHDAFVHTYSCLAPD-GASDTWK-VNELAERLMSQLQHselnieHLPPFQVGKTKVF 653
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
140-815 |
1.23e-166 |
|
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276838 [Multi-domain] Cd Length: 657 Bit Score: 525.09 E-value: 1.23e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITG 219
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 220 ESGAGKTVNTKRVIQYFAIVAalgdgpgKKAQFLATktggtleDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgP 299
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN-------QRRNNLVT-------EQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-E 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 300 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLsMNPYDYHFCSQG-VITVDNMNDGEELIATD 378
Cdd:cd01387 146 GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGL-QEAEKYFYLNQGgNCEIAGKSDADDFRRLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 379 HAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQRE---EQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEY 455
Cdd:cd01387 225 AAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRER 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 456 VTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFN 535
Cdd:cd01387 305 IFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 536 QHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLI-EKPLGILSILEEECMFPKASDASFRAKLYDNHAgKSPNFQQPRPD 614
Cdd:cd01387 385 KHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHHA-LNELYSKPRMP 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 615 kkrkyQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKKAASFQ 694
Cdd:cd01387 463 -----LPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKAPPRLGKGRFVTMKPRTP 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 695 TVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRIL 774
Cdd:cd01387 538 TVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 578836100 775 NPSAIPDDTFMDSRKAT-EKLLGSLDLDhtQYQFGHTKVFFK 815
Cdd:cd01387 618 VALKLPRPAPGDMCVSLlSRLCTVTPKD--MYRLGATKVFLR 657
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
140-815 |
1.11e-163 |
|
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 518.47 E-value: 1.11e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITG 219
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 220 ESGAGKTVNTKRVIQYFAivaalgdgpgkkaqFLATKTGGT-LEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 298
Cdd:cd01385 81 ESGSGKTESTNFLLHHLT--------------ALSQKGYGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 299 PSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGrKPELQDMLLLSMNPYDYHFCSQ-GVITVDNMNDGEELIAT 377
Cdd:cd01385 147 ENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAG-ASEEERKELHLKQPEDYHYLNQsDCYTLEGEDEKYEFERL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 378 DHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQK--QREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEY 455
Cdd:cd01385 226 KQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGET 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 456 VTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL----DTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQ 531
Cdd:cd01385 306 LILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 532 QFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIE-KPLGILSILEEECMFPKASDASFRAKlYDNHAGKSPNFQQ 610
Cdd:cd01385 386 YYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEK 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 611 PrpdkKRKYQAhFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATL--------------------YENY 670
Cdd:cd01385 464 P----QVMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELigidpvavfrwavlraffraMAAF 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 671 AGSCS-----TEPP---------KSGVKEKRKKAASfqTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAF 736
Cdd:cd01385 539 REAGRrraqrTAGHsltlhdrttKSLLHLHKKKKPP--SVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDE 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 737 LVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIpddtfmDSRKATEK-LLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd01385 617 LVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGL------ISSKEDIKdFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
140-815 |
3.13e-160 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 507.76 E-value: 3.13e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKG--KRRSDSPPHIYAVADNAYNDMLRNR----DN 212
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPlLYDVPGFDSQRKeeATASSPPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 213 QSMLITGESGAGKTVNTKRVIQYFAIVAALGDGPgkKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKF 292
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKGA--STSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 293 IRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKpELQDMLLLSMNPYDYHFCSQG-VITVDNMNDG 371
Cdd:cd14892 159 IQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLD-ANENAALELTPAESFLFLNQGnCVEVDGVDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 372 EELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQ--KQREEQAEADGTESADKAAYLMGVSSGDLLKGLLhPRV 449
Cdd:cd14892 238 TEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnaDDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLV-TQT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 450 RVGneyvTKGQSVE------QVVFAVGALAKATYDRLFRWLVSRIN-----QTL-----DTKLPRQFFIGVLDIAGFEIF 513
Cdd:cd14892 317 TST----ARGSVLEikltarEAKNALDALCKYLYGELFDWLISRINachkqQTSgvtggAASPTFSPFIGILDIFGFEIM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 514 EFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIEK-PLGILSILEEECMFP-KASDA 591
Cdd:cd14892 393 PTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 592 SFRAKLYDNHAGKSPNFQQPRPDKKrkyqaHFEVVHYAGVVPYSIVGWLEKNKDPLnetvvpifqksQNRLLATLyenya 671
Cdd:cd14892 472 QLLTIYHQTHLDKHPHYAKPRFECD-----EFVLRHYAGDVTYDVHGFLAKNNDNL-----------HDDLRDLL----- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 672 gscsteppksgvkEKRKKaasFQTvsqlhkeNLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGI 751
Cdd:cd14892 531 -------------RSSSK---FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVV 587
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578836100 752 RICRQGFPNRLLYTDFRQRYRIL-------NPSAIPDDTFMDSRKATEKLLGSLDLDhtQYQFGHTKVFFK 815
Cdd:cd14892 588 RIRREGFPIRRQFEEFYEKFWPLarnkagvAASPDACDATTARKKCEEIVARALERE--NFQLGRTKVFLR 656
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
140-815 |
2.67e-153 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 487.66 E-value: 2.67e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKR-RSDSPPHIYAVADNAYNDMLRNRDNQSMLIT 218
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 219 GESGAGKTVNTKRVIQYFAivaalgdgpgkkaqFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 298
Cdd:cd14897 81 GESGAGKTESTKYMIKHLM--------------KLSPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 299 PSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmNPYDYHFCSQGVITVDNMNDGEELiatD 378
Cdd:cd14897 147 ENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLE-DPDCHRILRDDNRNRPVFNDSEEL---E 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 379 H----------AMDILGFSVDEKCACYKIVGALLHFGNMKFkqkqrEEQAEADGTESADK-----AAYLMGVSSGDLLKG 443
Cdd:cd14897 223 YyrqmfhdltnIMKLIGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 444 LLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDtklPRQFF--------IGVLDIAGFEIFEF 515
Cdd:cd14897 298 LISNVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLW---PDKDFqimtrgpsIGILDMSGFENFKI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 516 NSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLI-EKPLGILSILEEECMFPKASDASFR 594
Cdd:cd14897 375 NSFDQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLV 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 595 AKLyDNHAGKSPNFQQPRPDkkrkyQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYagsc 674
Cdd:cd14897 454 QKL-NKYCGESPRYVASPGN-----RVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSY---- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 675 steppksgvkekrkkaasfqtvsqlHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRIC 754
Cdd:cd14897 524 -------------------------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIR 578
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578836100 755 RQGFPNRLLYTDFRQRYRILNPSaiPDDTFMDSRKATEKLLGSLDLDhtQYQFGHTKVFFK 815
Cdd:cd14897 579 RDGYPIRIKYEDFVKRYKEICDF--SNKVRSDDLGKCQKILKTAGIK--GYQFGKTKVFLK 635
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
140-815 |
5.40e-146 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 468.74 E-value: 5.40e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRRSDS--------PPHIYAVADNAYNDMLRNR 210
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQNGeyfdikkePPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 211 DNQSMLITGESGAGKTVNTKRVIQYFAIVAA--------LGDGPGKKAQFLATKTggtLEDQIIEANPAMEAFGNAKTLR 282
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevLTLTSSIRATSKSTKS---IEQKILSCNPILEAFGNAKTVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 283 NDNSSRFGKFIRIHFG-PSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPE-LQDMLL---LSMNPYDYHF 357
Cdd:cd14907 158 NDNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQlLQQLGLknqLSGDRYDYLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 358 CSqGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQ--REEQAEADGTESADKAAYLMGV 435
Cdd:cd14907 238 KS-NCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 436 SSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL------DTKLPRQFF--IGVLDI 507
Cdd:cd14907 317 DEEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekDQQLFQNKYlsIGLLDI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 508 AGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVF--IDFgLDLQPCIDLIEK-PLGILSILEEECM 584
Cdd:cd14907 397 FGFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 585 FPKASDASFRAKLYDNHAGKSpNFQQPRPDKKRKyqahFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLA 664
Cdd:cd14907 476 LATGTDEKLLNKIKKQHKNNS-KLIFPNKINKDT----FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIIS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 665 TLYENYAGSCSTEPPKSGVKEKRKKaasfqTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRC 744
Cdd:cd14907 551 SIFSGEDGSQQQNQSKQKKSQKKDK-----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRY 625
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578836100 745 NGVLEGIRICRQGFPNRLLYTDFRQRYRILNpsaipddtfmdsrkatekllgsldldhTQYQFGHTKVFFK 815
Cdd:cd14907 626 LGVLESIRVRKQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
140-815 |
2.74e-145 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 466.06 E-value: 2.74e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYA----RwmIYTYSGLFCVTINPYKWLPvytASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRD---N 212
Cdd:cd14891 1 AGILHNLEERSKldnqR--PYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 213 QSMLITGESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKT----GGTLEDQIIEANPAMEAFGNAKTLRNDNSSR 288
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKrklsVTSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 289 FGKFIRIHFGPSG-KLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmNPYDYHFCSQ-GVITVD 366
Cdd:cd14891 156 FGKFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLL-SPEDFIYLNQsGCVSDD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 367 NMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKA----AYLMGVSSGDLLK 442
Cdd:cd14891 235 NIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAEIASESDKEAlataAELLGVDEEALEK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 443 GLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTK---LPrqfFIGVLDIAGFEIFE-FNSF 518
Cdd:cd14891 315 VITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDpdpLP---YIGVLDIFGFESFEtKNDF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 519 EQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLI-EKPLGILSILEEECMFPKASDASFRAKL 597
Cdd:cd14891 392 EQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 598 YDNHAgKSPNFQQPRPDKKRKyqaHFEVVHYAGVVPYSIVGWLEKNKDplnetvvpIFQKSQNRLLATlyenyagscste 677
Cdd:cd14891 471 HKTHK-RHPCFPRPHPKDMRE---MFIVKHYAGTVSYTIGSFIDKNND--------IIPEDFEDLLAS------------ 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 678 ppksgvkekrkkAASFQTVSQlhkenlnKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQG 757
Cdd:cd14891 527 ------------SAKFSDQMQ-------ELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVG 587
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578836100 758 FPNRLLYTDFRQRYRILNPSAI------PDDTFmdsrkaTEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14891 588 LPTRVTYAELVDVYKPVLPPSVtrlfaeNDRTL------TQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
142-815 |
2.53e-142 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 458.22 E-value: 2.53e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 142 VLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDML----RNRDNQSMLI 217
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 218 TGESGAGKTVNTKRVIQyfaivaalgdgpgkkaQFLATKTGGT-LEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIH 296
Cdd:cd14889 83 SGESGAGKTESTKLLLR----------------QIMELCRGNSqLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 297 FgPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLsMNPYDYHFCSQGVITVDNMND-GEELI 375
Cdd:cd14889 147 F-RNGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGL-LDPGKYRYLNNGAGCKREVQYwKKKYD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 376 ATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREE-QAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNE 454
Cdd:cd14889 225 EVCNAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 455 YVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLdtkLPRQFF------IGVLDIAGFEIFEFNSFEQLCINFTNE 528
Cdd:cd14889 305 QIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL---APKDDSsvelreIGILDIFGFENFAVNRFEQACINLANE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 529 KLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDL-IEKPLGILSILEEECMFPKASDASFRAKLyDNHAGKSPN 607
Cdd:cd14889 382 QLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSY 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 608 FQqprpdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSG---VK 684
Cdd:cd14889 460 YG-----KSRSKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKlpqAG 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 685 EKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLY 764
Cdd:cd14889 535 SDNFNSTRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSF 614
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 578836100 765 TDFRQRYRIL-NPSAIPDDtfmdsRKATEKLLGSLDLdhTQYQFGHTKVFFK 815
Cdd:cd14889 615 AEFAERYKILlCEPALPGT-----KQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
141-774 |
1.29e-140 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 452.45 E-value: 1.29e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 141 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAY-----------KGKRRSDSPPHIYAVADNAYNDMLR 208
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 209 NRD----NQSMLITGESGAGKTVNTKRVIQYFAIVAAlgdgPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRND 284
Cdd:cd14900 82 GLNgvmsDQSILVSGESGSGKTESTKFLMEYLAQAGD----NNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRND 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 285 NSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMlllsmnpydyhfcsqgvit 364
Cdd:cd14900 158 NSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKR------------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 365 vDNMNDgeeliaTDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTE-------SADKAAYLMGVSS 437
Cdd:cd14900 219 -DMYRR------VMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDlapssiwSRDAAATLLSVDA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 438 GDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL-----DTKLPRQFFIGVLDIAGFEI 512
Cdd:cd14900 292 TKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 513 FEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLI-EKPLGILSILEEECMFPKASDA 591
Cdd:cd14900 372 FPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIsQRPTGILSLIDEECVMPKGSDT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 592 SFRAKLYdNHAGKSPNFQQPRPDKKRkyqAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQksqnrllatlyenYA 671
Cdd:cd14900 451 TLASKLY-RACGSHPRFSASRIQRAR---GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFV-------------YG 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 672 GScsteppksgvkekrkkaasfqtvsqlHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGI 751
Cdd:cd14900 514 LQ--------------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAV 567
|
650 660
....*....|....*....|...
gi 578836100 752 RICRQGFPNRLLYTDFRQRYRIL 774
Cdd:cd14900 568 RVARAGFPIRLLHDEFVARYFSL 590
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
895-1972 |
2.18e-139 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 463.88 E-value: 2.18e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 895 EEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSER 974
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 975 LEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQ 1054
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1055 ALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKKDS 1134
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1135 ELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGCR 1214
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1215 KREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASA 1294
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1295 EKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLSRGKALAAQSLEELRRQLEEESKA 1374
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1375 KSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAiQRTEELEEAKKKLALRLQEAEEGVE 1454
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1455 AANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLR 1534
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1535 HGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQLEL 1614
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1615 SQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRL 1694
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1695 MQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLN 1774
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1775 QKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAAL 1854
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1855 RGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEA 1934
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 578836100 1935 EQQANTNLAKYRKAQHELDDAEERADMAETQANKLRAR 1972
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
140-815 |
9.46e-138 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 445.16 E-value: 9.46e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLIT 218
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 219 GESGAGKTVNTKRVIQYFAIVAAlgdgpGKKAQFLAtktggtledQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 298
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG-----GRKDKTIA---------KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 299 PSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSG-RKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIAT 377
Cdd:cd14904 147 GRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFAST 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 378 DHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGtESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVT 457
Cdd:cd14904 227 QKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNG-SQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 458 KGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQF-FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQ 536
Cdd:cd14904 306 VPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 537 HMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHA--GKSPNFQQPRPD 614
Cdd:cd14904 386 DVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQtkKDNESIDFPKVK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 615 KkrkyqAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKKAASFQ 694
Cdd:cd14904 465 R-----TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAPSETKEGKSGKGTKAPKSLGSQ 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 695 tvsqlHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRIL 774
Cdd:cd14904 540 -----FKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIM 614
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 578836100 775 NPSAIPDDtfmDSRKATEKLLGSLDLDHT-QYQFGHTKVFFK 815
Cdd:cd14904 615 FPPSMHSK---DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
140-815 |
6.21e-135 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 438.57 E-value: 6.21e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYK--GKRRS---DSP----PHIYAVADNAYNDMLRN- 209
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 210 RDNQSMLITGESGAGKTVNTKRVIQYfaiVAALGDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRF 289
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLY---LTTLGNGEEGAPNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 290 GKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSG------RKPELQDMLLLSMN-PYDYHFCSQG- 361
Cdd:cd14908 158 GKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGgdeeehEKYEFHDGITGGLQlPNEFHYTGQGg 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 362 VITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAY---LMGVSSG 438
Cdd:cd14908 238 APDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARvakLLGVDVD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 439 DLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL--DTKLPRQFFIGVLDIAGFEIFEFN 516
Cdd:cd14908 318 KLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 517 SFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIE-KPLGILSILEEECMFP-KASDASFR 594
Cdd:cd14908 398 SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 595 AKLYDNHAgksPNFQQPRPDKKR-------KYQAHFEVVHYAGVVPYSI-VGWLEKNKDPLNETVVPIFQKSQNrllatl 666
Cdd:cd14908 477 SRLYETYL---PEKNQTHSENTRfeatsiqKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFESGQQ------ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 667 yenyagscsteppksgvkekrkkaasfqtvsqlHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNG 746
Cdd:cd14908 548 ---------------------------------FKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGG 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 747 VLEGIRICRQGFPNRLLYTDFRQRYRILNPSaIPDDT---FMDSRKATEKLLGSLDLD-----------------HTQYQ 806
Cdd:cd14908 595 VLEAVRVARSGYPVRLPHKDFFKRYRMLLPL-IPEVVlswSMERLDPQKLCVKKMCKDlvkgvlspamvsmknipEDTMQ 673
|
....*....
gi 578836100 807 FGHTKVFFK 815
Cdd:cd14908 674 LGKSKVFMR 682
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
140-777 |
2.99e-134 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 437.79 E-value: 2.99e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYK--------GKRRSDSPPHIYAVADNAYNDMLRN- 209
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKPe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 210 RDNQSMLITGESGAGKTVNTKRVIQYFAIVA---ALGDGPGKKAQFLATktggtledQIIEANPAMEAFGNAKTLRNDNS 286
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGrdqSSTEQEGSDAVEIGK--------RILQTNPILESFGNAQTIRNDNS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 287 SRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLS-MNPYDYH---FCSQGV 362
Cdd:cd14902 153 SRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQkGGKYELLnsyGPSFAR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 363 ITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESA---DKAAYLMGVSSGD 439
Cdd:cd14902 233 KRAVADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGVDVDK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 440 LLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFF---------IGVLDIAGF 510
Cdd:cd14902 313 LETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSIsdedeelatIGILDIFGF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 511 EIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIE-KPLGILSILEEECMFPKAS 589
Cdd:cd14902 393 ESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 590 DASFRAKLYDNHAGkspnfqqprpdkkrkyQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATL--Y 667
Cdd:cd14902 472 NQALSTKFYRYHGG----------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIgaD 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 668 ENYAGSCStepPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGV 747
Cdd:cd14902 536 ENRDSPGA---DNGAAGRRRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGV 612
|
650 660 670
....*....|....*....|....*....|
gi 578836100 748 LEGIRICRQGFPNRLLYTDFRQRYRILNPS 777
Cdd:cd14902 613 LEAVRIARHGYSVRLAHASFIELFSGFKCF 642
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
130-868 |
1.07e-133 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 439.85 E-value: 1.07e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 130 DMAMMTHLNEASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDS-PPHIYAVADNAYNDMLR 208
Cdd:PTZ00014 100 DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDKlPPHVFTTARRALENLHG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 209 NRDNQSMLITGESGAGKTVNTKRVIQYFAivaalgdgPGKKAQflatkTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSR 288
Cdd:PTZ00014 180 VKKSQTIIVSGESGAGKTEATKQIMRYFA--------SSKSGN-----MDLKIQNAIMAANPVLEAFGNAKTIRNNNSSR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 289 FGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDML-LLSMNpyDYHFCSQGVITVDN 367
Cdd:PTZ00014 247 FGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYkLKSLE--EYKYINPKCLDVPG 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 368 MNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEA-----DGTESADKAAYLMGVSSGDLLK 442
Cdd:PTZ00014 325 IDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDAaaisdESLEVFNEACELLFLDYESLKK 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 443 GLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLC 522
Cdd:PTZ00014 405 ELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLF 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 523 INFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLI-EKPLGILSILEEECMFPKASDASFRAKLYDNH 601
Cdd:PTZ00014 485 INITNEMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLcGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNL 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 602 AgKSPNFQQPRPDKKRKyqahFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYEnyagscsteppks 681
Cdd:PTZ00014 564 K-NNPKYKPAKVDSNKN----FVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFE------------- 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 682 GVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNR 761
Cdd:PTZ00014 626 GVEVEKGKLAKGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYR 705
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 762 LLYTDFRQRYRILNPSAIPDDTfMDSRKATEKLLGSLDLDHTQYQFGHTKVFFKAGLLGVLEELRDQRLAKVLTLLQARS 841
Cdd:PTZ00014 706 RTFAEFLSQFKYLDLAVSNDSS-LDPKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQREKLAAWEPLVSVLE 784
|
730 740
....*....|....*....|....*...
gi 578836100 842 rGRLMRLEYQRLLGGR-DALFTIQWNIR 868
Cdd:PTZ00014 785 -ALILKIKKKRKVRKNiKSLVRIQAHLR 811
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
141-815 |
2.39e-125 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 412.04 E-value: 2.39e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 141 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTasvVAAYKGKRRSDS--PPHIYAVADNAYNDMLR-------NR 210
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEMPGWTalPPHVFSIAEGAYRSLRRrlhepgaSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 211 DNQSMLITGESGAGKTVNTKRVIQYFAIVAAlgdgpGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFG 290
Cdd:cd14895 79 KNQTILVSGESGAGKTETTKFIMNYLAESSK-----HTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 291 KFIRIHFGP-----SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLL-SMNPYDYHFCSQGVIT 364
Cdd:cd14895 154 KFVRMFFEGheldtSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLeLLSAQEFQYISGGQCY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 365 V--DNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESA---------------- 426
Cdd:cd14895 234 QrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvqq 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 427 --DKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINqtldTKLP-RQF--- 500
Cdd:cd14895 314 hlDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVN----SASPqRQFaln 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 501 -----------FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDlQPCIDLI 569
Cdd:cd14895 390 pnkaankdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEML 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 570 E-KPLGILSILEEECMFPKASDASFRAKLYDNHAGKSpNFQQPRPDKKrkyQAHFEVVHYAGVVPYSIVGWLEKNKDPLN 648
Cdd:cd14895 469 EqRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHS-NFSASRTDQA---DVAFQIHHYAGAVRYQAEGFCEKNKDQPN 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 649 ETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKKA--ASFQTVSQLhKENLNKLMTNLRATQPHFVRCIVPNE 726
Cdd:cd14895 545 AELFSVLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSvlSSVGIGSQF-KQQLASLLDVVQQTQTHYIRCIKPND 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 727 NKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTfmdsrkATEKLLGSLDLDHTqyQ 806
Cdd:cd14895 624 ESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDA------TASALIETLKVDHA--E 695
|
....*....
gi 578836100 807 FGHTKVFFK 815
Cdd:cd14895 696 LGKTRVFLR 704
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
140-815 |
5.81e-125 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 408.78 E-value: 5.81e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITG 219
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 220 ESGAGKTVNTKRVIQYFAIvaalgdgpgkkaqfLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgP 299
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSS--------------LYQDQTEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHL-Q 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 300 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmNPYDYHFCSQG-VITVDNMNDGEELIATD 378
Cdd:cd14896 146 HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQ-GPETYYYLNQGgACRLQGKEDAQDFEGLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 379 HAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESAD--KAAYLMGVSSgDLLKGLLHPRVRVGN-EY 455
Cdd:cd14896 225 KALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEihTAARLLQVPP-ERLEGAVTHRVTETPyGR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 456 VTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFF--IGVLDIAGFEIFEFNSFEQLCINFTNEKLQQF 533
Cdd:cd14896 304 VSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 534 FNQHMFVLEQEEYKREGIDWVFIDfGLDLQPCIDLI-EKPLGILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQPR 612
Cdd:cd14896 384 SSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQ 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 613 ---PDkkrkyqahFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENyagscstEPPKSGVKEKRKK 689
Cdd:cd14896 462 lplPV--------FTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQE-------AEPQYGLGQGKPT 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 690 AAS-FQtvsqlhkENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFR 768
Cdd:cd14896 527 LASrFQ-------QSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFL 599
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 578836100 769 QRYRILNPSAIPDdtFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14896 600 ARFGALGSERQEA--LSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
140-815 |
2.05e-123 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 404.76 E-value: 2.05e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDS-PPHIYAVADNAYNDMLRNRDNQSMLIT 218
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLTKlPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 219 GESGAGKTVNTKRVIQYFAivaalgdgpgkkaqflATKTG---GTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 295
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA----------------SAKSGnmdLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 296 HFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDML-LLSMNPYDY--HFCSQgVITVDNMNDGE 372
Cdd:cd14876 145 DVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYhLLGLKEYKFlnPKCLD-VPGIDDVADFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 373 ELIATDHAMdilGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADK-----AAYLMGVSSGDLLKGLLHP 447
Cdd:cd14876 224 EVLESLKSM---GLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVDDAAAISNESLevfkeACSLLFLDPEALKRELTVK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 448 RVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTN 527
Cdd:cd14876 301 VTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 528 EKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCID-LIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGkSP 606
Cdd:cd14876 381 EMLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKS-NG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 607 NFQQPRPDKKRKyqahFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYEnyagscsteppksGVKEK 686
Cdd:cd14876 459 KFKPAKVDSNIN----FIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFE-------------GVVVE 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 687 RKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTD 766
Cdd:cd14876 522 KGKIAKGSLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEE 601
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 578836100 767 FRQRYRILNPSAIPDDTfMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14876 602 FLYQFKFLDLGIANDKS-LDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
140-772 |
1.43e-116 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 387.53 E-value: 1.43e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYK-------GKRRSDS---PPHIYAVADNAYNDMLR 208
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhnsqfGDRVTSTdprEPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 209 NRDNQSMLITGESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLA---TKTGGTLEDQIIEANPAMEAFGNAKTLRNDN 285
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISppaSPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 286 SSRFGKFIRIHF-GPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGR----KPELQDMLLLSMNPYDYHFCSQ 360
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 361 GVITV--DNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQ--KQREEQAEADGTESA---------- 426
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 427 DKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL-------------- 492
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 493 -DTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIE- 570
Cdd:cd14899 401 vDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEh 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 571 KPLGILSILEEECMFPKASDASFRAKLYDNHAGKS--PNFQQPrPDKKRKYQahFEVVHYAGVVPYSIVGWLEKNKDPLN 648
Cdd:cd14899 480 RPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNshPHFRSA-PLIQRTTQ--FVVAHYAGCVTYTIDGFLAKNKDSFC 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 649 ETVVPIFQKSQNRLLATL-----YENYAGSCSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIV 723
Cdd:cd14899 557 ESAAQLLAGSSNPLIQALaagsnDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIK 636
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 578836100 724 PNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYR 772
Cdd:cd14899 637 PNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
140-777 |
1.36e-113 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 378.94 E-value: 1.36e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRRSDSP-PHIYAVADNAYNDMLRNRDNQSMLI 217
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQNKSPiPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 218 TGESGAGKTVNTKRVIQYfaIVAALGDGPGKKAQflATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 297
Cdd:cd14906 81 SGESGSGKTEASKTILQY--LINTSSSNQQQNNN--NNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 298 -GPSGKLASADIDSYLLEKSRvIFQLPGER--SYHVYYQILSGRKPELQDMLLLSMNPYDYHF--CSQGVITV------- 365
Cdd:cd14906 157 rSSDGKIDGASIETYLLEKSR-ISHRPDNInlSYHIFYYLVYGASKDERSKWGLNNDPSKYRYldARDDVISSfksqssn 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 366 --DNMNDGEELIAT----DHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQ---REEQAEADGTESADKAAYLMGVS 436
Cdd:cd14906 236 knSNHNNKTESIESfqllKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 437 SGDLLKGLLHPRVRVGNE--YVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQ-----------FFIG 503
Cdd:cd14906 316 ESVFKQALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSNdlaggsnkknnLFIG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 504 VLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIE-KPLGILSILEEE 582
Cdd:cd14906 396 VLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 583 CMFPKASDASFRAKlYDNHAGKSPNFQQPRPDKkrkyqAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRL 662
Cdd:cd14906 475 CIMPKGSEQSLLEK-YNKQYHNTNQYYQRTLAK-----GTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFL 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 663 LATLYENYagscSTEPPKSgvkekRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQL 742
Cdd:cd14906 549 KKSLFQQQ----ITSTTNT-----TKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQL 619
|
650 660 670
....*....|....*....|....*....|....*
gi 578836100 743 RCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPS 777
Cdd:cd14906 620 RNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
140-813 |
2.90e-113 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 376.11 E-value: 2.90e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRR-SDSPPHIYAVADNAYNDMLRNRD--NQSM 215
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 216 LITGESGAGKTVNTKRVIQYFAIVAAlgdgpgKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 295
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAA------SPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 296 HFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSG---------RKPELQDMLLLSmNPydyhfcsqgvitvD 366
Cdd:cd14880 155 QLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGasaderlqwHLPEGAAFSWLP-NP-------------E 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 367 NMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQA---EADGTESADKAAYLMGVSSGDLLKG 443
Cdd:cd14880 221 RNLEEDCFEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLET 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 444 LlhpRVRVgneyVTKGQsvEQVVFAV-----------GALAKATYDRLFRWLVSRINQTLDTKLPR-QFFIGVLDIAGFE 511
Cdd:cd14880 301 L---QIRT----IRAGK--QQQVFKKpcsraecdtrrDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 512 IFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIE-KPLGILSILEEECMFPKASD 590
Cdd:cd14880 372 SFPENSLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIEgSPISICSLINEECRLNRPSS 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 591 ASFRAKLYDNHAGKSPNFQQPRPDKKrkyqAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENY 670
Cdd:cd14880 451 AAQLQTRIESALAGNPCLGHNKLSRE----PSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPAN 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 671 AGSCSTEPPKSgvkekRKKAASFQTVSQLhKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEG 750
Cdd:cd14880 527 PEEKTQEEPSG-----QSRAPVLTVVSKF-KASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVET 600
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578836100 751 IRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTFMDSRKATEKLLGSLdldhtqyQFGHTKVF 813
Cdd:cd14880 601 IHISAAGFPIRVSHQNFVERYKLLRRLRPHTSSGPHSPYPAKGLSEPV-------HCGRTKVF 656
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
140-815 |
4.64e-112 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 372.30 E-value: 4.64e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRRS-----DSPPHIYAVADNAYNDMLRNRDNQ 213
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 214 SMLITGESGAGKTVNTKRVIQYFAIVAALGDGPGKKAqflatktggtledqIIEANPAMEAFGNAKTLRNDNSSRFGKFI 293
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSSTDVQSL--------------ILGSNPLLESFGNAKTLRNNNSSRFGKFI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 294 RIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDML-LLSMNPYDYHFCSQgVITVDNMNDGE 372
Cdd:cd14886 147 KLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLgFKSLESYNFLNASK-CYDAPGIDDQK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 373 ELIATDHAMDILgFSVDEKCACYKIVGALLHFGNMKFKQKQR---EEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRV 449
Cdd:cd14886 226 EFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 450 RVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEK 529
Cdd:cd14886 305 VINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANER 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 530 LQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIEKP-LGILSILEEECMFPKASDASFRAKLydNHAGKSPNF 608
Cdd:cd14886 385 LQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC--KSKIKNNSF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 609 QqprPDKKRkyQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYagscstePPKSGVKEKRK 688
Cdd:cd14886 462 I---PGKGS--QCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDI-------PNEDGNMKGKF 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 689 KAASFQTvsqlhkeNLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFR 768
Cdd:cd14886 530 LGSTFQL-------SIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFF 602
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 578836100 769 QRYRILNP-SAIPDDTFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14886 603 HRNKILIShNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
140-815 |
5.40e-110 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 367.41 E-value: 5.40e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITG 219
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 220 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKaqflatktggtleDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 299
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSV-------------EKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 300 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMNPYDYHFcsqGVITVDNMNDGEELIA--- 376
Cdd:cd01386 148 AGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSF---GIVPLQKPEDKQKAAAafs 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 377 -TDHAMDILGFSVDEKCACYKIVGALLHFGN---MKFKQKQREEQAEadgTESADKAAYLMGVSSGDLLK---------G 443
Cdd:cd01386 225 kLQAAMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFAR---PEWAQRAAYLLGCTLEELSSaifkhhlsgG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 444 LLHPRVRVGNEYVTKGQSVEQVVFAVGAL---AKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFN---- 516
Cdd:cd01386 302 PQQSTTSSGQESPARSSSGGPKLTGVEALegfAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqr 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 517 --SFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDwvfIDFGLD---LQPCIDLIEKPL---------------GIL 576
Cdd:cd01386 382 gaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVE---VDFDLPelsPGALVALIDQAPqqalvrsdlrdedrrGLL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 577 SILEEECMFPKASDASFRAKLYdNHAGKSPNFQQPRPDKKRKYQAHFEVVHYAGV--VPYSIVGWLEKNK-DPLNETVVP 653
Cdd:cd01386 459 WLLDEEALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLRRSEGPLQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQ 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 654 IFQKSQNRLlatlyenyagscsteppkSGVKekrKKAASFQTvsqlhKENLNKLMTNLRATQPHFVRCIVPNENKTPGV- 732
Cdd:cd01386 538 LLQESQKET------------------AAVK---RKSPCLQI-----KFQVDALIDTLRRTGLHFVHCLLPQHNAGKDEr 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 733 -----------MDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPS----AIPDDTFMDSRKATEKLLGS 797
Cdd:cd01386 592 stsspaagdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPltkkLGLNSEVADERKAVEELLEE 671
|
730
....*....|....*...
gi 578836100 798 LDLDHTQYQFGHTKVFFK 815
Cdd:cd01386 672 LDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
140-815 |
7.85e-109 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 363.36 E-value: 7.85e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMI-YTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDS-PPHIYAVADNAYNDM-LRNRDNQSML 216
Cdd:cd14875 1 ATLLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 217 ITGESGAGKTVNTKRVIQYFaivaalgdgpGKKAQFLATKTGG-TLEDQIIE----ANPAMEAFGNAKTLRNDNSSRFGK 291
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYL----------GQLSYMHSSNTSQrSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 292 FIRIHFGP-SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMNPYDYHfCSQGVIT-----V 365
Cdd:cd14875 151 YIKLYFDPtSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYK-CLNGGNTfvrrgV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 366 DN--MNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESAdKAAYLMGVSSGDLLKG 443
Cdd:cd14875 230 DGktLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFL-TACRLLQLDPAKLREC 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 444 LLhprVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKL--PRQFFIGVLDIAGFEIFEFNSFEQL 521
Cdd:cd14875 309 FL---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGdcSGCKYIGLLDIFGFENFTRNSFEQL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 522 CINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIE-KPLGILSILEEECMFPKASDASFRAKLYDN 600
Cdd:cd14875 386 CINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQ 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 601 HAGKSPNFQQPrpdkKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYenyagscSTEPpk 680
Cdd:cd14875 465 WANKSPYFVLP----KSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLL-------STEK-- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 681 sgVKEKRKkaasfQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPN 760
Cdd:cd14875 532 --GLARRK-----QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPV 604
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 761 RLLYTDF-RQRYRILNPSAIPDDTFMDSRKATEKLLGS----LDLDHTQYQFGHTKVFFK 815
Cdd:cd14875 605 RRPIEQFcRYFYLIMPRSTASLFKQEKYSEAAKDFLAYyqrlYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
140-815 |
1.11e-99 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 336.40 E-value: 1.11e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAY---KGKRRSDSPPHIYAVADNAYNDMLRNRDNQSML 216
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 217 ITGESGAGKTVNTKRVIQYFAivaalgdgpgkkaqFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIH 296
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLT--------------CRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 297 FGPSGK-LASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmNPYDYHFCSQG----VITVDNMNDG 371
Cdd:cd14878 147 FCERKKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLN-NLCAHRYLNQTmredVSTAERSLNR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 372 EELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRV 451
Cdd:cd14878 226 EKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 452 GNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL----DTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTN 527
Cdd:cd14878 306 KGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 528 EKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLI-EKPLGILSILEEECMFPKASDASFRAKLY------DN 600
Cdd:cd14878 386 EKMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDFFfQKPSGFLSLLDEESQMIWSVEPNLPKKLQsllessNT 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 601 HAGKSPNFQQPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENyagscsteppk 680
Cdd:cd14878 466 NAVYSPMKDGNGNVALKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQS----------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 681 sgvkekrkKAASfqTVSQLHKeNLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPN 760
Cdd:cd14878 535 --------KLVT--IASQLRK-SLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPV 603
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 578836100 761 RLLYTDFRQRYRILNPSAIpddtfMDSRKATEKLLGSLDLDHTQ---YQFGHTKVFFK 815
Cdd:cd14878 604 RLSFSDFLSRYKPLADTLL-----GEKKKQSAEERCRLVLQQCKlqgWQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
140-815 |
6.20e-97 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 328.13 E-value: 6.20e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYtasvVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITG 219
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 220 ESGAGKTVNTKRVIQYFaivaalgdgpgkkaqFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 299
Cdd:cd14937 77 ESGSGKTEASKLVIKYY---------------LSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 300 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDML-LLSMNPYDYHFCSQGVI-TVDNMNDGEELIAT 377
Cdd:cd14937 142 YQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYkIRSENEYKYIVNKNVVIpEIDDAKDFGNLMIS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 378 DHAMDIlgfsVDEKCACYKIVGALLHFGNMKFKQ-----KQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVG 452
Cdd:cd14937 222 FDKMNM----HDMKDDLFLTLSGLLLLGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 453 NEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQ 532
Cdd:cd14937 298 NQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 533 FFNQHMFVLEQEEYKREGIDWVFIDFGLDlQPCIDLIEKPLGILSILEEECMFPKASDASFrAKLYDNHAGKSPNFQQpr 612
Cdd:cd14937 378 IYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESI-VSVYTNKFSKHEKYAS-- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 613 pdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTeppksgvkeKRKKAAS 692
Cdd:cd14937 454 --TKKDINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESL---------GRKNLIT 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 693 FQtvsqlHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRIcRQGFPNRLLYTDFRQRYR 772
Cdd:cd14937 523 FK-----YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFE 596
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 578836100 773 ILNPSAIPDDTFMDSRKATEKLLGSLDLDhtQYQFGHTKVFFK 815
Cdd:cd14937 597 YLDYSTSKDSSLTDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
141-778 |
1.55e-95 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 321.85 E-value: 1.55e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 141 SVLHNLRQRYARWMIYTYSGLFCVTINPYKwlPVYTASVVAAYKgKRRSDSPPHIYAVADNAYNDMLRNrDNQSMLITGE 220
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVH-GNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 221 SGAGKTVNTKRVIQYFaivaalgdgpgkkaqFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgpS 300
Cdd:cd14898 78 SGSGKTENAKLVIKYL---------------VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--D 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 301 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLlsmnpyDYHFCSQGVITVDNMNdgEELIATDHA 380
Cdd:cd14898 141 GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI------DTSSTAGNKESIVQLS--EKYKMTCSA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 381 MDILG---FSVDEKCACykivgALLHFGNMKFKQkqrEEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVT 457
Cdd:cd14898 213 MKSLGianFKSIEDCLL-----GILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 458 KGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQffIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQH 537
Cdd:cd14898 285 VFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKK 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 538 MFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKL--YDNHAGKSpnfqqprpdk 615
Cdd:cd14898 363 MFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIkkYLNGFINT---------- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 616 krKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNetVVPIfqksQNRLLATlyenyagscsteppksgvKEKRKKAASFqt 695
Cdd:cd14898 432 --KARDKIKVSHYAGDVEYDLRDFLDKNREKGQ--LLIF----KNLLIND------------------EGSKEDLVKY-- 483
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 696 vsqlHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILN 775
Cdd:cd14898 484 ----FKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILG 559
|
...
gi 578836100 776 PSA 778
Cdd:cd14898 560 ITL 562
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
137-814 |
1.15e-84 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 292.53 E-value: 1.15e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 137 LNEASVLHNLRQRYARWMIYTY---SGLfcVTINPYKWLPVYTASVVAAYKGKRRSDS-------PPHIYAVADNAYNDM 206
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGSEYYDTTsgskeplPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 207 LRNRDNQSMLITGESGAGKTVNTKRVIQyfaivaalgdgpgkkaQFL----ATKTGGTLEDQIIEANPAMEAFGNAKTLR 282
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLR----------------QLLrlssHSKKGTKLSSQISAAEFVLDSFGNAKTLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 283 NDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIfQLP-GERSYHVYYQILSGRKPELQDMLLLSmNPYDY-----H 356
Cdd:cd14879 143 NPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVA-SVPtGERNFHVFYYLLAGASPEERQHLGLD-DPSDYallasY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 357 FCSQGVITVDNmNDGEELiatDH---AMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQ--REEQAEADGTESADKAAY 431
Cdd:cd14879 221 GCHPLPLGPGS-DDAEGF---QElktALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVKNTDVLDIVAA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 432 LMGVSSGDLLKGLLHPRVRVGNEYVTkgqsveqvVF--AVGA------LAKATYDRLFRWLVSRINQTL-DTKLPRQFFI 502
Cdd:cd14879 297 FLGVSPEDLETSLTYKTKLVRKELCT--------VFldPEGAaaqrdeLARTLYSLLFAWVVETINQKLcAPEDDFATFI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 503 GVLDIAGFEIF---EFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLI-EKPLGILSI 578
Cdd:cd14879 369 SLLDFPGFQNRsstGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGI 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 579 LEEEC-MFPKASDASFRAKLYDNHAGKSPnFQQPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVpifqk 657
Cdd:cd14879 448 LDDQTrRMPKKTDEQMLEALRKRFGNHSS-FIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFV----- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 658 sqnrllaTLyenyagscsteppksgvkekrkkaasFQTVSQLhKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFL 737
Cdd:cd14879 522 -------NL--------------------------LRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRR 567
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578836100 738 VLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYrilnpsaIPDDTFMDSRKATEKLLGSLDLDHTQYQFGHTKVFF 814
Cdd:cd14879 568 VKAQIRSLGLPELAARLRVEYVVSLEHAEFCERY-------KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
140-815 |
1.39e-84 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 294.63 E-value: 1.39e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYA--------RWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRD 211
Cdd:cd14887 1 PNLLENLYQRYNkayinkenRNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 212 NQSMLITGESGAGKTVNTKRVIQYFAIVAALGDGPGKKaqflatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGK 291
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQ----------GLEARLLQSGPVLEAFGNAHTVLNANSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 292 FIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRK-PELQDMLLLSMNPYDYhfcsqgvitvdnmnD 370
Cdd:cd14887 151 MLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVaAATQKSSAGEGDPEST--------------D 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 371 GEELIAtdhAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADG---------------------------- 422
Cdd:cd14887 217 LRRITA---AMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKltsvsvgceetaadrshssevkclssgl 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 423 --TESADK----AAYLMGVSSGD-----LLKGLLHPRVRVGNEYVTkgqsVEQVVFAVGALAKATYDRLFRWLVSRINQT 491
Cdd:cd14887 294 kvTEASRKhlktVARLLGLPPGVegeemLRLALVSRSVRETRSFFD----LDGAAAARDAACKNLYSRAFDAVVARINAG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 492 L-------------DTKLPRQF-FIGVLDIAGFEIFE---FNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGidwV 554
Cdd:cd14887 370 LqrsakpsesdsdeDTPSTTGTqTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEG---V 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 555 FID-----FGLDLQPCIDLIEKP------------------------LGILSILEEE-CMFPKASDASFRAKLYDNHAGK 604
Cdd:cd14887 447 FQNqdcsaFPFSFPLASTLTSSPsstspfsptpsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNK 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 605 ----SPNFQQPRPDKKRKyQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVvpifqksqnrllatlyENYAGSCSTEPPK 680
Cdd:cd14887 527 niinSAKYKNITPALSRE-NLEFTVSHFACDVTYDARDFCRANREATSDEL----------------ERLFLACSTYTRL 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 681 SGVKEKRKKAA---SFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQG 757
Cdd:cd14887 590 VGSKKNSGVRAissRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADG 669
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 578836100 758 FPNRLLYTDFRQRYRILNPSAIPDdtFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14887 670 FPCRLPYVELWRRYETKLPMALRE--ALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
140-763 |
2.12e-82 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 286.80 E-value: 2.12e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRRSDS-------PPHIYAVADNAYNDMLRNRD 211
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 212 NQSMLITGESGAGKTVNTKRVIQYFAIVaalgdgpgkKAQFLATKtggtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGK 291
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI---------QTDSQMTE----RIDKLIYINNILESMSNATTIKNNNSSRCGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 292 FIRIHF---------GPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMNPYDYHFCSQGV 362
Cdd:cd14884 148 INLLIFeeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 363 ------------ITVDNMNDGEELIATD--------HAMDILGFSVDEKCACYKIVGALLHFGNMKFKQkqreeqaeadg 422
Cdd:cd14884 228 shqkrsvkgtlrLGSDSLDPSEEEKAKDeknfvallHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA----------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 423 tesadkAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQT----------L 492
Cdd:cd14884 297 ------AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNvlkckekdesD 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 493 DTKLPR--QFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIE 570
Cdd:cd14884 371 NEDIYSinEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIA 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 571 KPLGIL-SILEEECMFPKASDASFRAKLYDNH----------AGKSPNFQQPRPDKKRKYQAH-FEVVHYAGVVPYSIVG 638
Cdd:cd14884 450 KIFRRLdDITKLKNQGQKKTDDHFFRYLLNNErqqqlegkvsYGFVLNHDADGTAKKQNIKKNiFFIRHYAGLVTYRINN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 639 WLEKNKDPLNETVVPIFQKSQNRllaTLYENYAGscsteppksgvkekrKKAASFQTVSQLHKENLNKLMTNLRATQPHF 718
Cdd:cd14884 530 WIDKNSDKIETSIETLISCSSNR---FLREANNG---------------GNKGNFLSVSKKYIKELDNLFTQLQSTDMYY 591
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 578836100 719 VRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLL 763
Cdd:cd14884 592 IRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
140-779 |
2.74e-75 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 264.43 E-value: 2.74e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 140 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYkgkrrsdsppHIYAVADNAYNDMLRNRDNQSMLI-T 218
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNAESIVfG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 219 GESGAGKTVNTKRVIQYfaivaaLGDGPGKKaqfLATKTGGTLEDQIieanpamEAFGNAKTLRNDNSSRFGKFIRIHFG 298
Cdd:cd14874 71 GESGSGKSYNAFQVFKY------LTSQPKSK---VTTKHSSAIESVF-------KSFGCAKTLKNDEATRFGCSIDLLYK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 299 PSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmNPYDYHFCSQGVITVDNMNDGEELIATD 378
Cdd:cd14874 135 RNVLTGLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIK-GLQKFFYINQGNSTENIQSDVNHFKHLE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 379 HAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQR---EEQAEADGTESADK-AAYLMGVSSGDLLKGLLhPRVRVGNE 454
Cdd:cd14874 214 DALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNpnvEQDVVEIGNMSEVKwVAFLLEVDFDQLVNFLL-PKSEDGTT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 455 YvtkgqSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLpRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFF 534
Cdd:cd14874 293 I-----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPL-HTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 535 NQHMFVLEQEEYKREGIDwvfIDF----GLDLQPCIDLI-EKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSpNFQ 609
Cdd:cd14874 367 VKHSFHDQLVDYAKDGIS---VDYkvpnSIENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRS-SYG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 610 QPRpdkkRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEppksgvkekrkk 689
Cdd:cd14874 443 KAR----NKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDM------------ 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 690 aasFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQ 769
Cdd:cd14874 507 ---IVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFAR 583
|
650
....*....|
gi 578836100 770 RYRILNPSAI 779
Cdd:cd14874 584 QYRCLLPGDI 593
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
213-814 |
2.55e-73 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 258.89 E-value: 2.55e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 213 QSMLITGESGAGKTVNTKRVI-QYFAIVaalGDGPGKKA-QFLATktggtledqiieANPAMEAFGNAKTLRNDNSSRFG 290
Cdd:cd14881 69 QAIILSGTSGSGKTYASMLLLrQLFDVA---GGGPETDAfKHLAA------------AFTVLRSLGSAKTATNSESSRIG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 291 KFIRIHFgPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLS-MNPYDYHFCSQGVITVDNMN 369
Cdd:cd14881 134 HFIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgYSPANLRYLSHGDTRQNEAE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 370 DGEELIATDHAMDILGFS-VDekcaCYKIVGALLHFGNMKFKQKQREEQAEADGTEsADKAAYLMGVSSGDLLKGLlhpR 448
Cdd:cd14881 213 DAARFQAWKACLGILGIPfLD----VVRVLAAVLLLGNVQFIDGGGLEVDVKGETE-LKSVAALLGVSGAALFRGL---T 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 449 VRVGNeyvTKGQSVEQVV------FAVGALAKATYDRLFRWLVSRINQ------TLDTKlPRQFFIGVLDIAGFEIFEFN 516
Cdd:cd14881 285 TRTHN---ARGQLVKSVCdanmsnMTRDALAKALYCRTVATIVRRANSlkrlgsTLGTH-ATDGFIGILDMFGFEDPKPS 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 517 SFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDW-VFIDFgLDLQPCIDLIEK-PLGILSILEEECMfPKASDASFR 594
Cdd:cd14881 361 QLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCeVEVDY-VDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYV 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 595 AKLYDNHAGkSPNFQQPRPDKKRKyqahFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSqnrllatlyenyagSC 674
Cdd:cd14881 439 AKIKVQHRQ-NPRLFEAKPQDDRM----FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQ--------------NC 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 675 STeppksgvkekrkkaaSFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRIC 754
Cdd:cd14881 500 NF---------------GFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLM 564
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578836100 755 RQGFPNRLLYTDFRQRYRILNPSAIP---DDTFMDSRKATEKLLGSLDLDH-----TQYQFGHTKVFF 814
Cdd:cd14881 565 AGGYPHRMRFKAFNARYRLLAPFRLLrrvEEKALEDCALILQFLEAQPPSKlssvsTSWALGKRHIFL 632
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
141-815 |
3.21e-66 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 238.10 E-value: 3.21e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 141 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITGE 220
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 221 SGAGKTVNTKRVIQYFAIvaaLGDGPGKKAQflatktggtledQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 300
Cdd:cd14882 82 SYSGKTTNARLLIKHLCY---LGDGNRGATG------------RVESSIKAILALVNAGTPLNADSTRCILQYQLTFGST 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 301 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPE--LQDMLLLSMNPYDYHFCSQGV-------ITVDNMNDG 371
Cdd:cd14882 147 GKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQnrLKEYNLKAGRNYRYLRIPPEVppsklkyRRDDPEGNV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 372 EELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREeqAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRV 451
Cdd:cd14882 227 ERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYCLIK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 452 GNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLdtKLPRQFF-----IGVLDIAGFEIFEFNSFEQLCINFT 526
Cdd:cd14882 305 GGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKM--SFPRAVFgdkysISIHDMFGFECFHRNRLEQLMVNTL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 527 NEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCID-LIEKPLGILSILEEecmfpkASDASFRAKLYDN--HAG 603
Cdd:cd14882 383 NEQMQYHYNQRIFISEMLEMEEEDIPTINLRF-YDNKTAVDqLMTKPDGLFYIIDD------ASRSCQDQNYIMDriKEK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 604 KSPNFqqprpdkKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENyagscsteppkSGV 683
Cdd:cd14882 456 HSQFV-------KKHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-----------SQV 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 684 KEKRKKAASFQTVSQlhkENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLL 763
Cdd:cd14882 518 RNMRTLAATFRATSL---ELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIP 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 578836100 764 YTDFRQRYRILnpsAIPDDTFMDSRKATEKLLgSLDLDHTQYQFGHTKVFFK 815
Cdd:cd14882 595 FQEFLRRYQFL---AFDFDETVEMTKDNCRLL-LIRLKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
143-814 |
8.76e-66 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 239.10 E-value: 8.76e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 143 LHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRR----------SDSPPHIYAVADNAYNDMLRNRDN 212
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 213 QSMLITGESGAGKTVNTKRVIQYfaiVAALGDGPGKKAQFL-ATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGK 291
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQY---LCEIGDETEPRPDSEgASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 292 FIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSG--RKPELQDMLLLSMNPYDYHFCSQGVITVDNMN 369
Cdd:cd14893 161 MISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGvqHDPTLRDSLEMNKCVNEFVMLKQADPLATNFA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 370 dgeeLIATDHAMDILGFSV-----DEKCACYKIVGALLHFGNMKF--KQKQREEQAEADGTESADKAAYLMGVSSGDLLK 442
Cdd:cd14893 241 ----LDARDYRDLMSSFSAlrirkNQRVEIVRIVAALLHLGNVDFvpDPEGGKSVGGANSTTVSDAQSCALKDPAQILLA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 443 GLL---HPRV------------RVGNEYVT--KGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPR------- 498
Cdd:cd14893 317 AKLlevEPVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRyeksniv 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 499 --QFFIGVLDIAGFEIFE--FNSFEQLCINFTNEKLQQFFNQHMFV-----LEQEEYKREG--IDWVFIDFGLDLQPCID 567
Cdd:cd14893 397 inSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrlTVNSNVDITSEQEKCLQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 568 LIE-KPLGILSILEEECMFPKASDASFRAKLY---DNHAGKS-PN----FQQPRPDKKRKYQAHFEVVHYAGVVPYSIVG 638
Cdd:cd14893 477 LFEdKPFGIFDLLTENCKVRLPNDEDFVNKLFsgnEAVGGLSrPNmgadTTNEYLAPSKDWRLLFIVQHHCGKVTYNGKG 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 639 WLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKKAASFQTVSQLHKENLN------------- 705
Cdd:cd14893 557 LSSKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynqa 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 706 -KLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRilnpsaipddTF 784
Cdd:cd14893 637 dALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK----------NV 706
|
730 740 750
....*....|....*....|....*....|....
gi 578836100 785 MDSRKATEKLLGSLD----LDHTQYQFGHTKVFF 814
Cdd:cd14893 707 CGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
141-767 |
1.66e-60 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 221.89 E-value: 1.66e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 141 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRrsDSPPHIYAVADNAYNDMLRNRDNQSMLITG 219
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRR--GLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 220 ESGAGKTVNTKRVIQYFAIVAAlgdgpgKKAQFLatktggtlEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 299
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTDL------SRSKYL--------RDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 300 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmNPYDYHFCSQ-GVITVDNMNDGEELIATD 378
Cdd:cd14905 146 YGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLG-DINSYHYLNQgGSISVESIDDNRVFDRLK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 379 HAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQreEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTK 458
Cdd:cd14905 225 MSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKN--GKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVEN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 459 GQSveqvvfavgaLAKATYDRLFRWLVSRINQTLDtklPRQF--FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQ 536
Cdd:cd14905 303 RDS----------LARSLYSALFHWIIDFLNSKLK---PTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 537 HMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKplgILSILEEECMFPKASDASFRAKLYD----NHA-GKSPNfqqp 611
Cdd:cd14905 370 TVLKQEQREYQTERIPWMTPISFKDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKLQNflsrHHLfGKKPN---- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 612 rpdkkrkyqaHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLL----------ATLYE--------NYAG- 672
Cdd:cd14905 443 ----------KFGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLfsrdgvfninATVAElnqmfdakNTAKk 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 673 ----------SCSTEPPKSGVKEKRKK----------------AASFQTVSqlhkeNLNKLMTNlRATQPHFVRCIVPNE 726
Cdd:cd14905 513 splsivkvllSCGSNNPNNVNNPNNNSgggggggnsgggsgsgGSTYTTYS-----STNKAINN-SNCDFHFIRCIKPNS 586
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 578836100 727 NKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFP----NRLLYTDF 767
Cdd:cd14905 587 KKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
162-295 |
7.17e-56 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 191.79 E-value: 7.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 162 FCVTINPYKWLPVYTASVV-AAYKGKRRSDSPPHIYAVADNAYNDMLRNRDNQSMLITGESGAGKTVNTKRVIQYFAIVA 240
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 578836100 241 ALGDGPGK-KAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 295
Cdd:cd01363 81 FNGINKGEtEGWVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
141-813 |
1.61e-47 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 183.50 E-value: 1.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 141 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRS-DSPPHIYAVADNAYNDMLRNRDNQSMLITG 219
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIeDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 220 ESGAGKTVNTKRVIQYFA---------IVAALGDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFG 290
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAyqvkgsrrlPTNLNDQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 291 KFIRIHFgPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmNPYDYHFCSQGVITVDNMND 370
Cdd:cd14938 162 KFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLK-NIENYSMLNNEKGFEKFSDY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 371 GEELIATDHAMDILGFSVDEKCACYKIVGALLHFGN-------------MKFKQKQRE----------EQAEADGTESAD 427
Cdd:cd14938 240 SGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLDENV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 428 KAAYLmgvsSGDLLKGLLHPRVR------VGNEYV-TKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL-DTKLPRQ 499
Cdd:cd14938 320 KNLLL----ACKLLSFDIETFVKyfttnyIFNDSIlIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCtQLQNINI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 500 F--FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCID-LIEKPLGIL 576
Cdd:cd14938 396 NtnYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNlLVGPTEGSL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 577 -SILEEECMfPKASDASFRAKLYDNHAGKSPNFQQpRPDKKRKYQAhFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIF 655
Cdd:cd14938 476 fSLLENVST-KTIFDKSNLHSSIIRKFSRNSKYIK-KDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 656 QKSQNRLLATLYENY----AGSCSTEPPKSGVKE-----KRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNE 726
Cdd:cd14938 553 KQSENEYMRQFCMFYnydnSGNIVEEKRRYSIQSalklfKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNE 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 727 NKTP-GVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPsaipddtfmDSRKATEKLLGSLDLDHTQY 805
Cdd:cd14938 633 SKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEW 703
|
....*...
gi 578836100 806 QFGHTKVF 813
Cdd:cd14938 704 MIGNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1228-1979 |
8.80e-27 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 119.78 E-value: 8.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1228 EEAALRHEATVAALRRKQAEgAAELGEQVDSLQRVRQKLEK---EKSELR--------MEVDDLAANVETLTRAKASAEK 1296
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDI-LNELERQLKSLERQAEKAERykeLKAELRelelallvLRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1297 LCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKEcliSQLSRGKALAAQSLEELRRQLEEESKAKS 1376
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE---QQKQILRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1377 ALAHAVQALrhdcDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEAdaiqRTEELEEAKKKLALRLQEAE---EGV 1453
Cdd:TIGR02168 331 KLDELAEEL----AELEEKLEELKEELESLEAELEELEAELEELESRLEE----LEEQLETLRSKVAQLELQIAslnNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1454 EAANAKCSSLEKAKLRLQTESEDVTLELERATSAA-----AALDKKQRHLERALEERRRQEEEMQRELEAAQRESRGLGT 1528
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaelEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1529 ELFRLR---HGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALE-----------GEKSEIQAALE 1594
Cdd:TIGR02168 483 ELAQLQarlDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEaalggrlqavvVENLNAAKKAI 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1595 EAEGALELEETKTLRIQLELSQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLD--------AETRArnEALRLKKK 1666
Cdd:TIGR02168 563 AFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvVDDLD--NALELAKK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1667 MEGDLN------DLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAA 1740
Cdd:TIGR02168 641 LRPGYRivtldgDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1741 LEQGERSRRLAEQELLEA-------TERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAM 1813
Cdd:TIGR02168 721 LEELSRQISALRKDLARLeaeveqlEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1814 MAEELKKEQD--------------TSAHLERMKKTLEQTVRELQARLEEAEQAALRGgKKQVQKLEAKVRELEAELDAEQ 1879
Cdd:TIGR02168 801 LREALDELRAeltllneeaanlreRLESLERRIAATERRLEDLEEQIEELSEDIESL-AAEIEELEELIEELESELEALL 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1880 KKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYR-KAQHELDDAEER 1958
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEAL 959
|
810 820
....*....|....*....|....*..
gi 578836100 1959 ADMAETQANKLRARTR------DALGP 1979
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKrlenkiKELGP 986
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
979-1944 |
1.38e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 115.92 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 979 EEVNADLAarrrKLEDECTELKKDIDDLELTLAKAEK--EKQATENKVKN--LTEEMAALDESVARLTKEKKALQEAHQQ 1054
Cdd:TIGR02168 182 ERTRENLD----RLEDILNELERQLKSLERQAEKAERykELKAELRELELalLVLRLEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1055 ALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLrmdteraKRKLEGDLKLTQESVADAAQDKQQLEEKLKKKDS 1134
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE-------ISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1135 ELSQLSLRVedeqllgAQMQKKIKELQARAEELEEELEAEraararvEKQRAEAARELEELSERLEEAGGASAGQREGCR 1214
Cdd:TIGR02168 331 KLDELAEEL-------AELEEKLEELKEELESLEAELEEL-------EAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1215 KREAELGRLRRELEEAALRHEatvaalrrKQAEGAAELGEQVDSLQRvrQKLEKEKSELRMEVDDLAANVETLTRAKASA 1294
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRE--------RLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERLEEALEEL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1295 EKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKE-------CLISQLS----RGKAL-AAQSLE 1362
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSglsgilgVLSELISvdegYEAAIeAALGGR 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1363 ELRRQLEEESKAKSALAHAVQALRHDCDLLreqheeeaEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKKKL 1442
Cdd:TIGR02168 547 LQAVVVENLNAAKKAIAFLKQNELGRVTFL--------PLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1443 ALRLQeaeeGVEAANAKCSSLEKAKlRLQTESEDVTLELERATSAAAAldkkqrhleraleerrrqeeemqreleAAQRE 1522
Cdd:TIGR02168 619 SYLLG----GVLVVDDLDNALELAK-KLRPGYRIVTLDGDLVRPGGVI---------------------------TGGSA 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1523 SRGLGTeLFRlrhgheealealetlKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQaaleeaegalel 1602
Cdd:TIGR02168 667 KTNSSI-LER---------------RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLR------------ 718
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1603 eeTKTLRIQLELSQVKAEVDRkLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLElqlghat 1682
Cdd:TIGR02168 719 --KELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE------- 788
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1683 RQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERL 1762
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1763 NLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVREL 1842
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1843 QARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQS 1922
Cdd:TIGR02168 949 YSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
970 980
....*....|....*....|..
gi 578836100 1923 KVKSykrQFEEAEQQANTNLAK 1944
Cdd:TIGR02168 1029 EARE---RFKDTFDQVNENFQR 1047
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
888-1443 |
1.75e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 115.42 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 888 LLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGK 967
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 968 VKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKA 1047
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1048 LQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLEE 1127
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1128 KLKKKDSELSQLSLRVEDEqllgAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASA 1207
Cdd:COG1196 471 EAALLEAALAELLEELAEA----AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAA 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1208 GQREGCRKREAELGRLRRELEEAALRhEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETL 1287
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKAAKAG-RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1288 TRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLSRGKALAAQSLEELRRQ 1367
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578836100 1368 LEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQwrSKYEADAIQRteELEEAKKKLA 1443
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELP--EPPDLEELER--ELERLEREIE 777
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1418-1979 |
1.26e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 112.72 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1418 AQWRSKYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRH 1497
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1498 LERALEERRRQEEEMQRELEAAQRESRGLGTELfrlrhghEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEK 1577
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEEL-------EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1578 TKKALEGEKSEIQAALEEAEGALELEETKTLRIQLELSQVKAEVDRKLAEKDEECANLRRNHQRAVEslQASLDAETRAR 1657
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE--AAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1658 NEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDeEQRLAAELHEQAQALERRASLLAAELEEL 1737
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL-EGVKAALLLAGLRGLAGAVAVLIGVEAAY 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1738 RAALEQ--GERSRRLAEQELLEATERLNLLHSQNTG------LLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAIT 1809
Cdd:COG1196 537 EAALEAalAAALQNIVVEDDEVAAAAIEYLKAAKAGratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYY 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1810 DAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKgV 1889
Cdd:COG1196 617 VLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE-L 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1890 RKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAkyrKAQHELDDAEERADMAETQANKL 1969
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE---EEALEELPEPPDLEELERELERL 772
|
570
....*....|
gi 578836100 1970 RARtRDALGP 1979
Cdd:COG1196 773 ERE-IEALGP 781
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
896-1456 |
2.03e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.95 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 896 EELAALRAELRGLRgaLAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERL 975
Cdd:COG1196 220 EELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 976 EDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQA 1055
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1056 LGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKKDSE 1135
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1136 LSQLSLRVEDEQLLGAQMQKKIKELQAraeeleeeleaeraararvekQRAEAARELEELSERLEEAGGASAGQREgcRK 1215
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLE---------------------ELAEAAARLLLLLEAEADYEGFLEGVKA--AL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1216 REAELGRLRRELEEAALRHEATVAALRrkQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASAE 1295
Cdd:COG1196 515 LLAGLRGLAGAVAVLIGVEAAYEAALE--AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1296 KLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLSRGKALAAQSLEELRRQLEEESKAK 1375
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1376 SALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKKKLALRLQEAEEGVEA 1455
Cdd:COG1196 673 ALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA 752
|
.
gi 578836100 1456 A 1456
Cdd:COG1196 753 L 753
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
884-1792 |
5.74e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 110.53 E-value: 5.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 884 KMKPLLRSAQAEEELAALRAELRGLRGALAAA--EAKRQELEEThvsiTQEKNDLALQLQAEQDNLADAEERChlliksk 961
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELKAELRELELALLVLrlEELREELEEL----QEELKEAEEELEELTAELQELEEKL------- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 962 VQLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARL 1041
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1042 TKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLEcslEQEKKLRMDTERAKRKLEgdlkltqesvadaaqd 1121
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE---LQIASLNNEIERLEARLE---------------- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1122 kqQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQkkIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEE 1201
Cdd:TIGR02168 411 --RLEDRRERLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1202 AGGasagqregcrkREAELGRLRRELEEAAlrheATVAALRRKQAEGAAELGeQVDSLQRVRQKLEKEKSE-LRMEVDDL 1280
Cdd:TIGR02168 487 LQA-----------RLDSLERLQENLEGFS----EGVKALLKNQSGLSGILG-VLSELISVDEGYEAAIEAaLGGRLQAV 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1281 AanVETLTRAKASAEKLcrtYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEekecLISQLSRGKALAAqs 1360
Cdd:TIGR02168 551 V--VENLNAAKKAIAFL---KQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKD----LVKFDPKLRKALS-- 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1361 leelrrqleeeskakSALAHAV------QALRhdcdlLREQHEEEAEAQAELQRLLSKANAeVAQWRSKYEADAIQRTEE 1434
Cdd:TIGR02168 620 ---------------YLLGGVLvvddldNALE-----LAKKLRPGYRIVTLDGDLVRPGGV-ITGGSAKTNSSILERRRE 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1435 LEEAKKKLAlrlqEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQR 1514
Cdd:TIGR02168 679 IEELEEKIE----ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1515 ELEAAQRESRGLGTELfrlrhghEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALE 1594
Cdd:TIGR02168 755 ELTELEAEIEELEERL-------EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1595 EAEGALELEETKTLRIQLELSQVKAEVDrKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDL 1674
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIE-SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1675 ELQLGHATRQATEAQAATRLMQAQLKEEQAGRDE-EQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRR---- 1749
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgp 986
|
890 900 910 920
....*....|....*....|....*....|....*....|....*.
gi 578836100 1750 ---LAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEE 1792
Cdd:TIGR02168 987 vnlAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
967-1561 |
3.53e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.10 E-value: 3.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 967 KVKELSERLEdEEEVNAdLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKK 1046
Cdd:COG1196 214 RYRELKEELK-ELEAEL-LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1047 ALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLE 1126
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1127 EKLKKKDSELSQLSLRVEDEQllgaqmqKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAggas 1206
Cdd:COG1196 372 AELAEAEEELEELAEELLEAL-------RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE---- 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1207 agqregcRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEkekSELRMEVDDLAANVET 1286
Cdd:COG1196 441 -------EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL---LLLEAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1287 LTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESgelsrllEEKECLISQLSRGKALAAQSLEELRR 1366
Cdd:COG1196 511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE-------VAAAAIEYLKAAKAGRATFLPLDKIR 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1367 QLEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSK-YEADAIQRTEELEEAKKKLALR 1445
Cdd:COG1196 584 ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVtLAGRLREVTLEGEGGSAGGSLT 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1446 LQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQRESRG 1525
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
570 580 590
....*....|....*....|....*....|....*.
gi 578836100 1526 LGTELFRLRHGHEEALEALETLKRENKNLQEEISDL 1561
Cdd:COG1196 744 EEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1265-1877 |
9.78e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.56 E-value: 9.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1265 KLEKEKSELRME--------VDD----LAANVETLTRAKASAEKLcRTYEDQLSEAKI-----KVEELQRQLADASTQRG 1327
Cdd:COG1196 171 KERKEEAERKLEateenlerLEDilgeLERQLEPLERQAEKAERY-RELKEELKELEAellllKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1328 RLQTESGELSRLLEEKECLISQLsrgkalaaqsleelRRQLEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQ 1407
Cdd:COG1196 250 ELEAELEELEAELAELEAELEEL--------------RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1408 RLLSKANAEVAQWRSKyEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSA 1487
Cdd:COG1196 316 ERLEELEEELAELEEE-LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1488 AAALDKKQRHLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSL 1567
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1568 SGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQLELSQVKAEVDRKLAEKDEECANLRrnhqRAVESLQ 1647
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA----LAAALQN 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1648 ASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRA 1727
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1728 SLLAAelEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKA 1807
Cdd:COG1196 631 RLEAA--LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE 708
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1808 ITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDA 1877
Cdd:COG1196 709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1228-1960 |
6.18e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 104.45 E-value: 6.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1228 EEAalRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDlAANVETLTRAKAS--AEKLCRTYEDQL 1305
Cdd:PTZ00121 1101 EEA--KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAED-AKRVEIARKAEDArkAEEARKAEDAKK 1177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1306 SEAKIKVEELQRqladASTQRGRLQTESGELSRLLEEkECLISQLSRgkalAAQSLEELRRQLEEESKAKSALAHAVQAL 1385
Cdd:PTZ00121 1178 AEAARKAEEVRK----AEELRKAEDARKAEAARKAEE-ERKAEEARK----AEDAKKAEAVKKAEEAKKDAEEAKKAEEE 1248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1386 RHDCDLLREQHEEEaeaqaelqrllskanAEVAQWRSKYEADAIQRTEELEEAK-KKLALRLQEAEEGVEAANAKCSSLE 1464
Cdd:PTZ00121 1249 RNNEEIRKFEEARM---------------AHFARRQAAIKAEEARKADELKKAEeKKKADEAKKAEEKKKADEAKKKAEE 1313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1465 KAKlrlqteSEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEAL 1544
Cdd:PTZ00121 1314 AKK------ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA 1387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1545 ETLKR--ENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEgeksEIQAALEEAEGALELEETKTLRIQLELSQvKAEVD 1622
Cdd:PTZ00121 1388 EEKKKadEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE----EKKKADEAKKKAEEAKKADEAKKKAEEAK-KAEEA 1462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1623 RKLAEKDEECANLRRNHQRAVESLQASLDAEtRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAAtrlmQAQLKEE 1702
Cdd:PTZ00121 1463 KKKAEEAKKADEAKKKAEEAKKADEAKKKAE-EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA----EEAKKAD 1537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1703 QAGRDEEQRLAAELheqaqaleRRAsllaaelEELRAALEqgersRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEAD 1782
Cdd:PTZ00121 1538 EAKKAEEKKKADEL--------KKA-------EELKKAEE-----KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1783 LAQLSGEVEEAAQERREAEEKAKKAitdaammaEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGG--KKQ 1860
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKA--------EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAeeAKK 1669
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1861 VQKLEAKVRELEAElDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQAN- 1939
Cdd:PTZ00121 1670 AEEDKKKAEEAKKA-EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEe 1748
|
730 740
....*....|....*....|...
gi 578836100 1940 --TNLAKYRKAQHELDDAEERAD 1960
Cdd:PTZ00121 1749 akKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1674-1982 |
1.17e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.09 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1674 LELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQ 1753
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1754 ELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKK 1833
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1834 TLEQTVRELQARLEEAEQAALRgGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARM 1913
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAE-LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578836100 1914 QDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDALGPKLS 1982
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1435-1977 |
2.11e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 98.86 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1435 LEEA--------KKKLAL-RLQEAEEGVEAANAKCSSLEKAKLRLQTESE------DVTLELERATSAAAALDKKQRHLE 1499
Cdd:COG1196 161 IEEAagiskykeRKEEAErKLEATEENLERLEDILGELERQLEPLERQAEkaeryrELKEELKELEAELLLLKLRELEAE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1500 RALEERRRQEEEMQreLEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTK 1579
Cdd:COG1196 241 LEELEAELEELEAE--LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1580 KALEGEKSEIQAALEEAEGALELEETKTLRIQLELSQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNE 1659
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1660 ALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLA-AELEELR 1738
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEeAALLEAA 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1739 AALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLE------ADLAQLSGEVEEAAQERREAEEKAK--KAITD 1810
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglagavAVLIGVEAAYEAALEAALAAALQNIvvEDDEV 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1811 AAMMAEELKKEQD--------TSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKH 1882
Cdd:COG1196 559 AAAAIEYLKAAKAgratflplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1883 AEALKGVRK---------------HERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRK 1947
Cdd:COG1196 639 AVTLAGRLRevtlegeggsaggslTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
570 580 590
....*....|....*....|....*....|
gi 578836100 1948 AQHELDDAEERADMAETQANKLRARTRDAL 1977
Cdd:COG1196 719 EELEEEALEEQLEAEREELLEELLEEEELL 748
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1142-1956 |
5.59e-20 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 97.55 E-value: 5.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1142 RVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEaarelEELSERLEEAGGASAGQREGCRKREAE-- 1219
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQE-----QLQAETELCAEAEEMRARLAARKQELEei 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1220 LGRLRRELEEAALRHEAtVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLtrakasaeklcr 1299
Cdd:pfam01576 77 LHELESRLEEEEERSQQ-LQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLL------------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1300 tyEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLsrgkalaaqsleelRRQLEEESKAKSALA 1379
Cdd:pfam01576 144 --EDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDL--------------EERLKKEEKGRQELE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1380 HAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELeEAKKKLALRLQEAEEGVEAANAK 1459
Cdd:pfam01576 208 KAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNAL-KKIRELEAQISELQEDLESERAA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1460 CSSLEKAKLRLQTESEDVTLELERA--TSAAAALDKKQRHLERALEErrrqeeemqrelEAAQRESRGLGTELFRLRHGH 1537
Cdd:pfam01576 287 RNKAEKQRRDLGEELEALKTELEDTldTTAAQQELRSKREQEVTELK------------KALEEETRSHEAQLQEMRQKH 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1538 EEAL----EALETLKRENKN-------LQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEETK 1606
Cdd:pfam01576 355 TQALeeltEQLEQAKRNKANlekakqaLESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEK 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1607 TLRIQLELSQVKA---EVDRKLAEKDEECANLRRNHQRAVESLQasldAETRARNEALRLKKKMEGDLNDLELQLGH--A 1681
Cdd:pfam01576 435 LSKLQSELESVSSllnEAEGKNIKLSKDVSSLESQLQDTQELLQ----EETRQKLNLSTRLRQLEDERNSLQEQLEEeeE 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1682 TRQATEAQAATrlMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATER 1761
Cdd:pfam01576 511 AKRNVERQLST--LQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVD 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1762 LNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDT----------------- 1824
Cdd:pfam01576 589 LDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAkeelertnkqlraemed 668
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1825 ----------SAH-LERMKKTLEQTVRELQARLEE-------AEQAALR---------------------GGKKQVQKLE 1865
Cdd:pfam01576 669 lvsskddvgkNVHeLERSKRALEQQVEEMKTQLEEledelqaTEDAKLRlevnmqalkaqferdlqardeQGEEKRRQLV 748
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1866 AKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKY 1945
Cdd:pfam01576 749 KQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQS 828
|
890
....*....|.
gi 578836100 1946 RKAQHELDDAE 1956
Cdd:pfam01576 829 KESEKKLKNLE 839
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
265-755 |
9.77e-19 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 93.27 E-value: 9.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 265 IIEANPAMEAFGNAKTLRNDNSSRFGKF--IRIHFGPSG---KLASADIDSYLLEKSRVIFQL------PGERSYHVYYQ 333
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 334 ILSGRKPELQDMLLLSMNPYDYHFCSQ------------GVITVDNM--NDGEELIATDHAMDILGFSVDEKCACYKIVG 399
Cdd:cd14894 329 MVAGVNAFPFMRLLAKELHLDGIDCSAltylgrsdhklaGFVSKEDTwkKDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 400 ALLHFGNMKFKQKQREEQAEADGT---ESADKAAYLMGVSSGDLLKGLLHPR-VRVGNEYVTKGQSVE--QVVFAVGALA 473
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsVSLQSTSETFEVTLEkgQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 474 KATYDRLFRWLVSRINQTL----------------DTKLPRQF-FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQ 536
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEATkmsalstdgnkhqmdsNASAPEAVsLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYAREEQ 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 537 ----------HMFVLEQEEykregiDWVFIdfgldlqpcidlIEKPLGILSILEEECMFPKASDAS----------FRAK 596
Cdd:cd14894 569 viavayssrpHLTARDSEK------DVLFI------------YEHPLGVFASLEELTILHQSENMNaqqeekrnklFVRN 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 597 LYDNHAGKSPNFQQPRPDKKRKYQAHFEVV-----HYAGVVPYSIVGWLEKNKDPL-NETVVPIFQKSQNRLLATLYENY 670
Cdd:cd14894 631 IYDRNSSRLPEPPRVLSNAKRHTPVLLNVLpfvipHTRGNVIYDANDFVKKNSDFVyANLLVGLKTSNSSHFCRMLNESS 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 671 AGSCSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEG 750
Cdd:cd14894 711 QLGWSPNTNRSMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQ 790
|
....*
gi 578836100 751 IRICR 755
Cdd:cd14894 791 MEICR 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1657-1988 |
1.19e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 93.08 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1657 RNEALRLKKKMEGDLN-------DLELQLGHATRQATEAQAAtrlmqAQLKEEQAGRDEEQRLAA--ELHEQAQALERRA 1727
Cdd:COG1196 174 KEEAERKLEATEENLErledilgELERQLEPLERQAEKAERY-----RELKEELKELEAELLLLKlrELEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1728 SLLAAELEELRAaleqgersrrlaEQELLEAT-ERLNLLHSQNTGLLNQKKK----LEADLAQLSGEVEEAAQERREAEE 1802
Cdd:COG1196 249 EELEAELEELEA------------ELAELEAElEELRLELEELELELEEAQAeeyeLLAELARLEQDIARLEERRRELEE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1803 KAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRggkkqvqkLEAKVRELEAELDAEQKKH 1882
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE--------AEAELAEAEEELEELAEEL 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1883 AEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMA 1962
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
330 340
....*....|....*....|....*.
gi 578836100 1963 ETQANKLRARTRDALGPKLSLSPQHK 1988
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLL 494
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
966-1851 |
4.01e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 91.67 E-value: 4.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 966 GKVKELSERLEDEEEVNADLAARRRKLEDEcTELKKDIDDLELTLAKAE-----KEKQATENKVKNLTEEMAALDESVAR 1040
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRRE-REKAERYQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1041 LTKEKKALQEAHQQALGDLQAEEDRVSALTKAK-LRLEQQVEDLECSLEQekklrmdterakrkLEGDLKLTQESVADAA 1119
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqLRVKEKIGELEAEIAS--------------LERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1120 QDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAeeleeeleaeraararvEKQRAEAARELEelserl 1199
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL-----------------EDLRAELEEVDK------ 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1200 eeaggASAGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAaELGEQVDSLQRVRQKLEKEKSELRMEVDD 1279
Cdd:TIGR02169 379 -----EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA-DLNAAIAGIEAKINELEEEKEDKALEIKK 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1280 LAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKEC-------LISQLSR 1352
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGS 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1353 GKALAAQSLeelrrqleeeskaKSALAHAVQALRHDCDLLreqheeeaeaQAELQRLLSKANAEVAQWRSKYEADAIQRT 1432
Cdd:TIGR02169 533 VGERYATAI-------------EVAAGNRLNNVVVEDDAV----------AKEAIELLKRRKAGRATFLPLNKMRDERRD 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1433 EEL--EEAKKKLALRLQEAEEGVEAANAKC-------SSLEKAKlRLQTESEDVTLE---LERATS------AAAALDKK 1494
Cdd:TIGR02169 590 LSIlsEDGVIGFAVDLVEFDPKYEPAFKYVfgdtlvvEDIEAAR-RLMGKYRMVTLEgelFEKSGAmtggsrAPRGGILF 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1495 QRHLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQE 1574
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1575 LEktkKALEGEKSEIQaaleeaegaleleetktlriqlELSQVKAEVDRKLAEKDEECANLRR--NHQRaVESLQASLDA 1652
Cdd:TIGR02169 749 LE---QEIENVKSELK----------------------ELEARIEELEEDLHKLEEALNDLEArlSHSR-IPEIQAELSK 802
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1653 --ETRARNEAlRLkKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQA-------L 1723
Cdd:TIGR02169 803 leEEVSRIEA-RL-REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEleaalrdL 880
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1724 ERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAA-----QERR 1798
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELsledvQAEL 960
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....
gi 578836100 1799 EAEEKAKKAITDAAMMA-EELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQ 1851
Cdd:TIGR02169 961 QRVEEEIRALEPVNMLAiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1217-1972 |
4.86e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 88.20 E-value: 4.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1217 EAELGRLRRELEEAALRHEATVAALRrkqaegaaELGEQVDSLQRVRQKLEKEKsELRMEVDDLAANVetLTRAKASAEK 1296
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIID--------EKRQQLERLRREREKAERYQ-ALLKEKREYEGYE--LLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1297 LCRTYEDQLSEAKIKVEELQRQLADastqrgrLQTESGELSRLLEEKECLISQLSRGKALAAQSLeelrrqleeeskaks 1376
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISE-------LEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEK--------------- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1377 alahavqalrhdcdllreqheeeaeaqaelqrlLSKANAEVAQWRSKyEADAIQRTEELEEAKKKLALRLQEAEEGVEAA 1456
Cdd:TIGR02169 296 ---------------------------------IGELEAEIASLERS-IAEKERELEDAEERLAKLEAEIDKLLAEIEEL 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1457 NAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLRHG 1536
Cdd:TIGR02169 342 EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEE 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1537 HEEALEALETLKRENKNLQEEISDLTDQVSlsgKSIQELEKTKKALEGEKSEIqaaleeaegalELEETKTLRIQLELSQ 1616
Cdd:TIGR02169 422 LADLNAAIAGIEAKINELEEEKEDKALEIK---KQEWKLEQLAADLSKYEQEL-----------YDLKEEYDRVEKELSK 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1617 VKAEVDRKLAEKDE---------------------------ECANLRRNHQRAVES-----LQASLDAETRARNEALRLK 1664
Cdd:TIGR02169 488 LQRELAEAEAQARAseervrggraveevlkasiqgvhgtvaQLGSVGERYATAIEVaagnrLNNVVVEDDAVAKEAIELL 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1665 KKMEG-------------------------------DLNDLELQLGHATRQA-------TEAQAATRLM--------QAQ 1698
Cdd:TIGR02169 568 KRRKAgratflplnkmrderrdlsilsedgvigfavDLVEFDPKYEPAFKYVfgdtlvvEDIEAARRLMgkyrmvtlEGE 647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1699 LKEEQ----AGRDEEQRL---AAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTG 1771
Cdd:TIGR02169 648 LFEKSgamtGGSRAPRGGilfSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1772 LLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMkkTLEQTVRELQARLEEAEq 1851
Cdd:TIGR02169 728 LEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR--LSHSRIPEIQAELSKLE- 804
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1852 aalrggkKQVQKLEAKVRELEAELDAE-------QKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKV 1924
Cdd:TIGR02169 805 -------EEVSRIEARLREIEQKLNRLtlekeylEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 578836100 1925 KSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRAR 1972
Cdd:TIGR02169 878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1421-1976 |
5.78e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 87.89 E-value: 5.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1421 RSKYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANaKCSSLEKAKLRLQTESEDVTLELERATSA-----AAALDKKQ 1495
Cdd:PTZ00121 1170 RKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAAR-KAEEERKAEEARKAEDAKKAEAVKKAEEAkkdaeEAKKAEEE 1248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1496 RHLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLrhghEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQEL 1575
Cdd:PTZ00121 1249 RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA----EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKA 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1576 EKTKKALEGEKSEIQAALEEAEGALELEETKtlRIQLELSQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETR 1655
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAA--ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1656 ARNEALRLKKKMEGDLNDLELQL-GHATRQATEAQAATRlmQAQLKEEQAGRDEEQRLAAELHEQAQAlERRASLLAAEL 1734
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKkAEEKKKADEAKKKAE--EAKKADEAKKKAEEAKKAEEAKKKAEE-AKKADEAKKKA 1479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1735 EELRAAleqgERSRRLAEQELLEATERlnllhsqntgllnQKKKLEADLAQLSGEVEEA--AQERREAEEKAKkaiTDAA 1812
Cdd:PTZ00121 1480 EEAKKA----DEAKKKAEEAKKKADEA-------------KKAAEAKKKADEAKKAEEAkkADEAKKAEEAKK---ADEA 1539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1813 MMAEELKKEQDTSaHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKgvRKH 1892
Cdd:PTZ00121 1540 KKAEEKKKADELK-KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK--KAE 1616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1893 ERRVK-ELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEE----AEQQANTNLAKYRKAQhELDDAEERADMAETQAN 1967
Cdd:PTZ00121 1617 EAKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkikAAEEAKKAEEDKKKAE-EAKKAEEDEKKAAEALK 1695
|
....*....
gi 578836100 1968 KLRARTRDA 1976
Cdd:PTZ00121 1696 KEAEEAKKA 1704
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
959-1848 |
5.02e-16 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 84.64 E-value: 5.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 959 KSKVQLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESV 1038
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1039 ARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLeQQVEDLECSLEQEKKlrmdtERAKRKLEGDLKLTQESvada 1118
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKL-QEEELKLLAKEEEEL-----KSELLKLERRKVDDEEK---- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1119 aqdKQQLEEKLKKKDSELSQLSlrvedEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSER 1198
Cdd:pfam02463 316 ---LKESEKEKKKAEKELKKEK-----EEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLS 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1199 LEEAGGASAGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVD 1278
Cdd:pfam02463 388 SAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1279 DLAANVETLTRAKASAEKLcrtyEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLSRGKALAA 1358
Cdd:pfam02463 468 KKSEDLLKETQLVKLQEQL----ELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKV 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1359 QSLEELRRQLEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEA 1438
Cdd:pfam02463 544 AISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAK 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1439 KKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLeleratSAAAALDKKQRHLERALEERRRQEEEMQRELEA 1518
Cdd:pfam02463 624 VVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEV------KASLSELTKELLEIQELQEKAESELAKEEILRR 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1519 AQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSgKSIQELEKTKKALEGEKSEIQAALEEAEG 1598
Cdd:pfam02463 698 QLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDE-EEEEEEKSRLKKEEKEEEKSELSLKEKEL 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1599 ALELEETKTLRIQLELSQVKAEVDRKLAEKDEEC-ANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQ 1677
Cdd:pfam02463 777 AEEREKTEKLKVEEEKEEKLKAQEEELRALEEELkEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEEL 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1678 LGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALErrasllaaelEELRAALEQGERSRRLAEQELLE 1757
Cdd:pfam02463 857 ERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELE----------EESQKLNLLEEKENEIEERIKEE 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1758 ATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERM----KK 1833
Cdd:pfam02463 927 AEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLeeekKK 1006
|
890
....*....|....*
gi 578836100 1834 TLEQTVRELQARLEE 1848
Cdd:pfam02463 1007 LIRAIIEETCQRLKE 1021
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1105-1971 |
1.04e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.04 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1105 EGDLKLTQESVADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQ 1184
Cdd:PTZ00121 1078 DFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIA 1157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1185 RAEAARELEELSERLEEAGGASAGQREGCRKREAELgrlrRELEEAALRHEATVAALRRKQAEG-AAELGEQVDSLQRVR 1263
Cdd:PTZ00121 1158 RKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEEL----RKAEDARKAEAARKAEEERKAEEArKAEDAKKAEAVKKAE 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1264 QKLEKEKSELRMEvdDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRqladASTQRGRLQTESGELSRLLEEK 1343
Cdd:PTZ00121 1234 EAKKDAEEAKKAE--EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK----AEEKKKADEAKKAEEKKKADEA 1307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1344 ECLISQLSRGKALAAQSLEELRRQLEEESKAKSAlahavqalrhdcdllreqheeeaeaqaelqrllsKANAEVAQWRSK 1423
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEA----------------------------------KKAAEAAKAEAE 1353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1424 YEADAIQRTEELEEAKKKlalRLQEAEEGVEAANAKCSSLEKAKlRLQTESEDVTLELERATSAAAAldKKQRHLERALE 1503
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEK---KKEEAKKKADAAKKKAEEKKKAD-EAKKKAEEDKKKADELKKAAAA--KKKADEAKKKA 1427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1504 ERRRQEEEMQRELEAAQRESrglgtelfRLRHGHEEALEALETLKRENKNLQEEisdltdqvslsgksiqelEKTKKALE 1583
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKAD--------EAKKKAEEAKKAEEAKKKAEEAKKAD------------------EAKKKAEE 1481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1584 GEKSEiqaaleeaegaleleetkTLRIQLELSQVKAEVDRKLAEKDEECANLRRNhQRAVESLQASLDAETRARNEALRL 1663
Cdd:PTZ00121 1482 AKKAD------------------EAKKKAEEAKKKADEAKKAAEAKKKADEAKKA-EEAKKADEAKKAEEAKKADEAKKA 1542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1664 KKKMEGDlndlELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQ 1743
Cdd:PTZ00121 1543 EEKKKAD----ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1744 GERSRRL-AEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQ 1822
Cdd:PTZ00121 1619 KIKAEELkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA 1698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1823 DTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHE----RRVKE 1898
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKaeeiRKEKE 1778
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578836100 1899 LAYQAEEDRKNLARMQDlVDKlqsKVKSYKRQFEEAEQQANTNlAKYRKAQHELDDAE--ERADMAETQANKLRA 1971
Cdd:PTZ00121 1779 AVIEEELDEEDEKRRME-VDK---KIKDIFDNFANIIEGGKEG-NLVINDSKEMEDSAikEVADSKNMQLEEADA 1848
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1171-1958 |
1.68e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.81 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1171 LEAERAARARVEKQRAEAARELEELSERLEEAggasAGQREGCRKREAELGRLR-RELEEAALRHEATVAALRRKQAEgA 1249
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERL----RREREKAERYQALLKEKReYEGYELLKEKEALERQKEAIERQ-L 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1250 AELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLT-----RAKASAEKL---CRTYEDQLSEAKIKVEELQRQLAD 1321
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGeeeqlRVKEKIGELeaeIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1322 ASTQRGRLQTESGELSRLLEEKECLISQLSRGKALAAQSLEELRRQLEEESKAKSALAHAVQALRHDCDLLREQHEEEAE 1401
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1402 AQAELQRLLSKANAEVAQWRSKYeADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLEL 1481
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAI-AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1482 ERATSAAAALDKKQRhlerALEERRRQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEA-----LETLKRENKNLQE 1556
Cdd:TIGR02169 486 SKLQRELAEAEAQAR----ASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVaagnrLNNVVVEDDAVAK 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1557 EISDLTDQVSLSGKSIQELEKTKKALegekseiqaaleeaegaleleetKTLRIQLELSQVKAEVDrkLAEKDEECANLR 1636
Cdd:TIGR02169 562 EAIELLKRRKAGRATFLPLNKMRDER-----------------------RDLSILSEDGVIGFAVD--LVEFDPKYEPAF 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1637 RNHQR---AVESLQA-----------SLDAE-----------TRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAA 1691
Cdd:TIGR02169 617 KYVFGdtlVVEDIEAarrlmgkyrmvTLEGElfeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSE 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1692 TRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTG 1771
Cdd:TIGR02169 697 LRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1772 LLNQKKKLEADLAQlsGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEE--A 1849
Cdd:TIGR02169 777 LEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSieK 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1850 EQAALRGGKK----QVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVK 1925
Cdd:TIGR02169 855 EIENLNGKKEeleeELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
|
810 820 830
....*....|....*....|....*....|...
gi 578836100 1926 SYKRQFEEaEQQANTNLAKYRKAQHELDDAEER 1958
Cdd:TIGR02169 935 EIEDPKGE-DEEIPEEELSLEDVQAELQRVEEE 966
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1618-1980 |
2.16e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.41 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1618 KAEVDRKLAEKDEECANLRRNHQ-RAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQ 1696
Cdd:PTZ00121 1116 KAEEAKKKAEDARKAEEARKAEDaRKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRK 1195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1697 AQ--LKEEQAGRDEEQRLAAEL--HEQAQALE--RRASLLAAELEELRAALEQ--GERSRRLAEQELLEATERLNLLHSQ 1768
Cdd:PTZ00121 1196 AEdaRKAEAARKAEEERKAEEArkAEDAKKAEavKKAEEAKKDAEEAKKAEEErnNEEIRKFEEARMAHFARRQAAIKAE 1275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1769 NTGLLNQKKKLE----ADLAQLSGEVEEAAQERREAEEK-----AKKAITDAAMMAEELKKEQdtsahlERMKKTLEQTV 1839
Cdd:PTZ00121 1276 EARKADELKKAEekkkADEAKKAEEKKKADEAKKKAEEAkkadeAKKKAEEAKKKADAAKKKA------EEAKKAAEAAK 1349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1840 RELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDK 1919
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEE 1429
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578836100 1920 LQsKVKSYKRQFEEAEQ--QANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDALGPK 1980
Cdd:PTZ00121 1430 KK-KADEAKKKAEEAKKadEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
963-1326 |
4.30e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.17 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 963 QLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLT 1042
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1043 KEKKALqeahqqalgdlqaeEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDK 1122
Cdd:TIGR02168 761 AEIEEL--------------EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1123 QQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEA 1202
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1203 GGASAGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAA 1282
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGP 986
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 578836100 1283 -NVETLTRAKASAEK---LCRTYEDqLSEAKIKVEELQRQLADASTQR 1326
Cdd:TIGR02168 987 vNLAAIEEYEELKERydfLTAQKED-LTEAKETLEEAIEEIDREARER 1033
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1480-1981 |
1.36e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.49 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1480 ELERATSAAAAL----DKKQRHLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQ 1555
Cdd:COG4913 243 ALEDAREQIELLepirELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1556 EEISDLTDQV-SLSGKSIQELEKTKKALEGEKSEIQaaleeaegaleleetktlRIQLELSQVKAEVDRKLAEKDEECAN 1634
Cdd:COG4913 323 EELDELEAQIrGNGGDRLEQLEREIERLERELEERE------------------RRRARLEALLAALGLPLPASAEEFAA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1635 LRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAA 1714
Cdd:COG4913 385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFVG 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1715 EL------HEQAQ-ALER-----RASLL--AAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNqkkKLE 1780
Cdd:COG4913 465 ELievrpeEERWRgAIERvlggfALTLLvpPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAG---KLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1781 ADLAQLSGEVEEAAQERR--------EAEEKAKKAITDAAMM-----AEELKKEQDTSAHL------ERMKKTLEQTVRE 1841
Cdd:COG4913 542 FKPHPFRAWLEAELGRRFdyvcvdspEELRRHPRAITRAGQVkgngtRHEKDDRRRIRSRYvlgfdnRAKLAALEAELAE 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1842 LQARLEEAEQaalrggkkQVQKLEAKVRELEAELDAEQK--KHAEALKGVRKHERRVKELayqaEEDRKNLARMQDLVDK 1919
Cdd:COG4913 622 LEEELAEAEE--------RLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAEL----EAELERLDASSDDLAA 689
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578836100 1920 LQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDALGPKL 1981
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
894-1585 |
2.06e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 76.26 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 894 AEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKV-QLEGKVKELS 972
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIaSLERSIAEKE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 973 ERLEDeeevnadLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAH 1052
Cdd:TIGR02169 315 RELED-------AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1053 QQalgdlqaeedRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGdlklTQESVADAAQDKQQLEEKLKKK 1132
Cdd:TIGR02169 388 KD----------YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG----IEAKINELEEEKEDKALEIKKQ 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1133 DSELSQLSLRVEDEqllgaqmQKKIKELQARAEELEEELEAERAARARVEKQRaEAARELEELSERLEEAGGASagqREG 1212
Cdd:TIGR02169 454 EWKLEQLAADLSKY-------EQELYDLKEEYDRVEKELSKLQRELAEAEAQA-RASEERVRGGRAVEEVLKAS---IQG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1213 CRKREAELGRLRRE----LEEAA---------------------LRHE----ATVAALRRKQAEG--------------A 1249
Cdd:TIGR02169 523 VHGTVAQLGSVGERyataIEVAAgnrlnnvvveddavakeaielLKRRkagrATFLPLNKMRDERrdlsilsedgvigfA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1250 AELGE-----------------QVDSLQRVRQKLEK-----------EKS------------------ELRMEVDDLAAN 1283
Cdd:TIGR02169 603 VDLVEfdpkyepafkyvfgdtlVVEDIEAARRLMGKyrmvtlegelfEKSgamtggsraprggilfsrSEPAELQRLRER 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1284 VETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLSRGKALAAQSLEE 1363
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1364 LRRQLEEESKAKSALAHAVQALRHDcdllreqheEEAEAQAELQRLLSKANAEVAQWRSkyeadaiqRTEELEEAKKKLA 1443
Cdd:TIGR02169 763 LEARIEELEEDLHKLEEALNDLEAR---------LSHSRIPEIQAELSKLEEEVSRIEA--------RLREIEQKLNRLT 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1444 LRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQRES 1523
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578836100 1524 RGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTdQVSLSGKSIQELEKTKKALEGE 1585
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE-EIPEEELSLEDVQAELQRVEEE 966
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1425-1972 |
2.19e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.86 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1425 EADAIQRTEELEEA---------KKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESE------DVTLELERATSAAA 1489
Cdd:TIGR02168 151 EAKPEERRAIFEEAagiskykerRKETERKLERTRENLDRLEDILNELERQLKSLERQAEkaerykELKAELRELELALL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1490 ALDKKQRHLERALEERRRQEEEMQreLEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQvslsg 1569
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEE--LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ----- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1570 ksIQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQLELSQVKAEVDRkLAEKDEECANLRRNHQRAVESLQAS 1649
Cdd:TIGR02168 304 --KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES-LEAELEELEAELEELESRLEELEEQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1650 LDAETRARNEALRLKKKMEGDLNDLELQL----GHATRQATEAQAATRLMQAQLKEEQAGRDEEqrLAAELHEQAQALER 1725
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLerleDRRERLQQEIEELLKKLEEAELKELQAELEE--LEEELEELQEELER 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1726 raslLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHS---QNTGLLNQKKKLEADLAQLSG-------------- 1788
Cdd:TIGR02168 459 ----LEEALEELREELEEAEQALDAAERELAQLQARLDSLERlqeNLEGFSEGVKALLKNQSGLSGilgvlselisvdeg 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1789 ---EVEEAAQERREA-----EEKAKKAI--------TDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQA 1852
Cdd:TIGR02168 535 yeaAIEAALGGRLQAvvvenLNAAKKAIaflkqnelGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1853 ----------------------------------------ALRGG----------------KKQVQKLEAKV-------R 1869
Cdd:TIGR02168 615 rkalsyllggvlvvddldnalelakklrpgyrivtldgdlVRPGGvitggsaktnssilerRREIEELEEKIeeleekiA 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1870 ELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQ 1949
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
650 660
....*....|....*....|...
gi 578836100 1950 HELDDAEERADMAETQANKLRAR 1972
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEE 797
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1431-1980 |
3.08e-13 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 75.60 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1431 RTEELEEAKKKLALRLQEAEEgveaanaKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEE 1510
Cdd:pfam01576 69 RKQELEEILHELESRLEEEEE-------RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDIL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1511 EMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQ 1590
Cdd:pfam01576 142 LLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1591 AALEEAEGALELEETKTLRIQLELSQVKAEVDRKLAEKDEECANLRRnHQRAVESLQASLDAETRARNEALRLKKKMEGD 1670
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRE-LEAQISELQEDLESERAARNKAEKQRRDLGEE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1671 LNDLELQL-----GHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLA----------AELHEQ--------------AQ 1721
Cdd:pfam01576 301 LEALKTELedtldTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQemrqkhtqalEELTEQleqakrnkanlekaKQ 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1722 ALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEA-------- 1793
Cdd:pfam01576 381 ALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAegknikls 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1794 ------------AQERREAEEKAKKAIT--------DAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQA- 1852
Cdd:pfam01576 461 kdvsslesqlqdTQELLQEETRQKLNLStrlrqledERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTl 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1853 -ALRGGKKQVQkleakvRELEAELDAEQKKHAEALKGVRKHERRVKEL------AYQAEEDRKNLARMQDLVDKLQSKVK 1925
Cdd:pfam01576 541 eALEEGKKRLQ------RELEALTQQLEEKAAAYDKLEKTKNRLQQELddllvdLDHQRQLVSNLEKKQKKFDQMLAEEK 614
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 578836100 1926 SYKRQFEE----AEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDALGPK 1980
Cdd:pfam01576 615 AISARYAEerdrAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSK 673
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
893-1344 |
3.32e-13 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 75.21 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 893 QAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADaeerchllikskvqLEGKVKELS 972
Cdd:pfam01576 542 ALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSN--------------LEKKQKKFD 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 973 ERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAAL-------DESVARLTKEK 1045
Cdd:pfam01576 608 QMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLvsskddvGKNVHELERSK 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1046 KALQEAHQQALGDLQAEEDRVSALTKAKLRLE-----------------------------QQVEDLECSLEQEKKLRMD 1096
Cdd:pfam01576 688 RALEQQVEEMKTQLEELEDELQATEDAKLRLEvnmqalkaqferdlqardeqgeekrrqlvKQVRELEAELEDERKQRAQ 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1097 TERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERA 1176
Cdd:pfam01576 768 AVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQE 847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1177 ARARVEKQRAEAARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEG---AAELG 1253
Cdd:pfam01576 848 DLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVeqlTTELA 927
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1254 EQVDSLQRV---RQKLEKEKSELRMEVDDLAANV----------------------ETLTRAKASAEKLCRTYEDQLSEA 1308
Cdd:pfam01576 928 AERSTSQKSesaRQQLERQNKELKAKLQEMEGTVkskfkssiaaleakiaqleeqlEQESRERQAANKLVRRTEKKLKEV 1007
|
490 500 510
....*....|....*....|....*....|....*.
gi 578836100 1309 KIKVEELQRQLADASTQRGRLQTESGELSRLLEEKE 1344
Cdd:pfam01576 1008 LLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAE 1043
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1619-1975 |
3.63e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 75.49 E-value: 3.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1619 AEVDRKLAEKDEECANLRRNHQRA---VESLQASLDAETRARNEALRLKKkMEGDLNDLELQLGHATRQATEAQAATRLM 1695
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLdliIDEKRQQLERLRREREKAERYQA-LLKEKREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1696 Q-AQLKEEQAGRDEE-QRLAAELHEQAQAL-----------ERRASLLAAELEELRAALEQGERSRRLAEQELLEATERL 1762
Cdd:TIGR02169 245 QlASLEEELEKLTEEiSELEKRLEEIEQLLeelnkkikdlgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1763 NLLHSQNTGLLNQKKKLEADL-------AQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDtsaHLERMKKTL 1835
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIeeerkrrDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE---KLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1836 EQTVRELQARLEEAeqaalrggkkqvQKLEAKVRELEAELDAEQKKHAEAlkgvrkhERRVKELAYQAEEDRKNLARMQD 1915
Cdd:TIGR02169 402 NELKRELDRLQEEL------------QRLSEELADLNAAIAGIEAKINEL-------EEEKEDKALEIKKQEWKLEQLAA 462
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1916 LVDKLQSKVKSYKrqfeeaeqqantnlAKYRKAQHELDDAEERADMAETQANKLRARTRD 1975
Cdd:TIGR02169 463 DLSKYEQELYDLK--------------EEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1532-1978 |
1.29e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.15 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1532 RLRHGHEEALEALETL--KRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGAleleetktlr 1609
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQieEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER---------- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1610 iQLELSQVKAEVDrKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLghATRQATEAQ 1689
Cdd:PRK02224 250 -REELETLEAEIE-DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARR--EELEDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1690 AATRLMQ----AQLKEEQAGRDEEQrlAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLL 1765
Cdd:PRK02224 326 LRDRLEEcrvaAQAHNEEAESLRED--ADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1766 HSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAitdAAMMAE----ELKKEQDTSAHLERMKKTLEQtVRE 1841
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEA---EALLEAgkcpECGQPVEGSPHVETIEEDRER-VEE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1842 LQARLEEAEQaalrggkkQVQKLEAKVRELEAELDAEqkKHAEALKGVRKH-ERRVKELAYQAEEDRKNLARMQDLVDKL 1920
Cdd:PRK02224 480 LEAELEDLEE--------EVEEVEERLERAEDLVEAE--DRIERLEERREDlEELIAERRETIEEKRERAEELRERAAEL 549
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578836100 1921 QSKVKSYKRQFEEAEQQANT---NLAKYRKAQHELDDAEERADMAETQANkLRARTRDALG 1978
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEareEVAELNSKLAELKERIESLERIRTLLA-AIADAEDEIE 609
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
72-117 |
1.94e-12 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 63.22 E-value: 1.94e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 578836100 72 DGKKRVWVPDEQDAYVEAEVKSEaTGGRVTVETKDQKVLMVREAEL 117
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEE-EGDKVTVETEDGKTVTVKKDDV 45
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
962-1344 |
1.17e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.48 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 962 VQLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARL 1041
Cdd:TIGR02169 642 VTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEI 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1042 TKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLklTQESVADAAQD 1121
Cdd:TIGR02169 722 EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAE 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1122 KQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEE 1201
Cdd:TIGR02169 800 LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1202 AGGASAGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEgAAELGEQVDSLQRVRQKLEKEKSELrMEVDDLA 1281
Cdd:TIGR02169 880 LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK-LEALEEELSEIEDPKGEDEEIPEEE-LSLEDVQ 957
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578836100 1282 ANVETLTRAkasaeklCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKE 1344
Cdd:TIGR02169 958 AELQRVEEE-------IRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
889-1161 |
1.21e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.48 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 889 LRSAQAEEELAALRAELRGLRGALAAAEAKRQELEEthvsitqekndlalQLQAEQDNLADAEERCHLLIKSKVQLEGKV 968
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSSLQSELRRIEN--------------RLDELSQELSDASRKIGEIEKEIEQLEQEE 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 969 KELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATE-----NKVKNLTEEMAALDESVARLTK 1043
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEarlshSRIPEIQAELSKLEEEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1044 EKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQ 1123
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD 892
|
250 260 270
....*....|....*....|....*....|....*...
gi 578836100 1124 QLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQ 1161
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1421-1972 |
1.32e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.09 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1421 RSKYEADAIQRTEELEEakkklalRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRhler 1500
Cdd:PRK03918 177 RIERLEKFIKRTENIEE-------LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEK---- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1501 aleerrrqeeemqrELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLqEEISDLTDQVSLSGKSIQELEKTKK 1580
Cdd:PRK03918 246 --------------ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1581 ALEGEKSEIQAALEEAEGALELEETKTLRIQlELSQVKAEVDRKLA--EKDEECANLRRNHQRAVESLQASLDAET---- 1654
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEelEERHELYEEAKAKKEELERLKKRLTGLTpekl 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1655 -RARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAA-TRLMQAQLKEEQAGR----DEEQRLAAELHEQAQALERRAS 1728
Cdd:PRK03918 390 eKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAiEELKKAKGKCPVCGRelteEHRKELLEEYTAELKRIEKELK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1729 LLAAELEELRAALEQGERsrrlaeqeLLEATERLNLLHSqntgLLNQKKKLEADLAQLSGE-VEEAAQERREAEEKAKKA 1807
Cdd:PRK03918 470 EIEEKERKLRKELRELEK--------VLKKESELIKLKE----LAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKL 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1808 ITDAAMMAEELKKEQDtsahLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEaELDAEQKKHAEALK 1887
Cdd:PRK03918 538 KGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAEK 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1888 GVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNL-----AKYRKAQHELDDAEERADMA 1962
Cdd:PRK03918 613 ELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEylelsRELAGLRAELEELEKRREEI 692
|
570
....*....|
gi 578836100 1963 ETQANKLRAR 1972
Cdd:PRK03918 693 KKTLEKLKEE 702
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1122-1972 |
2.46e-11 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 69.23 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1122 KQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEE 1201
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1202 AGGASAGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLA 1281
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1282 ANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRL----QTESGELSRLLEEKECLISQLSRGKALA 1357
Cdd:pfam02463 328 KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELlakkKLESERLSSAAKLKEEELELKSEEEKEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1358 AQSLEELRRQLEEESKAKSALAHAVQALRHDCDLLR-----EQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRT 1432
Cdd:pfam02463 408 QLLLELARQLEDLLKEEKKEELEILEEEEESIELKQgklteEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1433 EELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEM 1512
Cdd:pfam02463 488 LLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLV 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1513 QRELEA---AQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEktKKALEGEKSEI 1589
Cdd:pfam02463 568 RALTELplgARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTEL--TKLKESAKAKE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1590 QAALEEAEGALELEETKTLRIQLELSQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALrLKKKMEG 1669
Cdd:pfam02463 646 SGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKL-EAEELLA 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1670 DLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRR 1749
Cdd:pfam02463 725 DRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELR 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1750 LAEQELLeatERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLE 1829
Cdd:pfam02463 805 ALEEELK---EEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEE 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1830 RMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKN 1909
Cdd:pfam02463 882 QKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEER 961
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578836100 1910 LARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQhELDDAEERADMAETQANKLRAR 1972
Cdd:pfam02463 962 NKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLE-EEKKKLIRAIIEETCQRLKEFL 1023
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
961-1343 |
3.08e-11 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 68.00 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 961 KVQLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVAR 1040
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1041 LTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQ 1120
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1121 DKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAAreleelserle 1200
Cdd:pfam07888 193 EFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELS----------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1201 eaggASAGQREgcrKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSEL-RMEVdd 1279
Cdd:pfam07888 262 ----SMAAQRD---RTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELqRLEE-- 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578836100 1280 lAANVETLTRAKASAE----KLCRTYedQLSEAKIKVEELQRQLADASTQRGRLQTESGEL---SRLLEEK 1343
Cdd:pfam07888 333 -RLQEERMEREKLEVElgreKDCNRV--QLSESRRELQELKASLRVAQKEKEQLQAEKQELleyIRQLEQR 400
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1263-1920 |
6.21e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 68.07 E-value: 6.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1263 RQKLEKEKSELRMEVDDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLaDASTQRGRLQTESGELSRLLEE 1342
Cdd:TIGR00618 193 HGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR-EAQEEQLKKQQLLKQLRARIEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1343 KECLISQLSRGK-------------ALAAQSLEELRRQLEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQRL 1409
Cdd:TIGR00618 272 LRAQEAVLEETQerinrarkaaplaAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLH 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1410 -----LSKANAEVAQWRSKYE------------ADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQT 1472
Cdd:TIGR00618 352 sqeihIRDAHEVATSIREISCqqhtltqhihtlQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKK 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1473 ESEdvtLELERATSAAAALDKkqrhLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENK 1552
Cdd:TIGR00618 432 QQE---LQQRYAELCAAAITC----TAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPC 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1553 NLQEEISDLTDQVSLSGKS------IQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQLELSQVKaevdRKLA 1626
Cdd:TIGR00618 505 PLCGSCIHPNPARQDIDNPgpltrrMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILT----QCDN 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1627 EKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLmqAQLKEEQAGR 1706
Cdd:TIGR00618 581 RSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTAL--HALQLTLTQE 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1707 DEEQRLAAELHEQAQALERRASLLAA---ELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEAD- 1782
Cdd:TIGR00618 659 RVREHALSIRVLPKELLASRQLALQKmqsEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARe 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1783 --LAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEEL-KKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKK 1859
Cdd:TIGR00618 739 daLNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDI 818
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578836100 1860 QVQKLEAKVRELEAELDAEQKKHAeALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKL 1920
Cdd:TIGR00618 819 LNLQCETLVQEEEQFLSRLEEKSA-TLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
892-1092 |
8.06e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 66.33 E-value: 8.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 892 AQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKEL 971
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 972 SERLED------------------EEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAA 1033
Cdd:COG4942 103 KEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578836100 1034 LDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKK 1092
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
914-1352 |
8.72e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.86 E-value: 8.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 914 AAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLEDEEEVNADLAARRRKLE 993
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 994 DECTELKKDIDDLEltlAKAEKEKQATENKVKnlTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAK 1073
Cdd:PTZ00121 1391 KKADEAKKKAEEDK---KKADELKKAAAAKKK--ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK 1465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1074 LRLEQQVEDLECSLEQEKKlrmdTERAKRKLEgdlkltqESVADAAQDKQQLEEKlkKKDSELSQLSLRVEDEQLLGAQM 1153
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKK----ADEAKKKAE-------EAKKKADEAKKAAEAK--KKADEAKKAEEAKKADEAKKAEE 1532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1154 QKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAALR 1233
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1234 HEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRA----KASAEKLCRTYEDQ--LSE 1307
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKaeedKKKAEEAKKAEEDEkkAAE 1692
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 578836100 1308 AKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLSR 1352
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1408-1958 |
1.15e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.25 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1408 RLLSKANAEVAQWRSkyeADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTES-EDVTLELERATS 1486
Cdd:COG4913 276 YLRAALRLWFAQRRL---ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1487 AAAALDKKQRHLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLRHGHEEAL----EALETLKRENKNLQEEISDLT 1562
Cdd:COG4913 353 ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALaeaeAALRDLRRELRELEAEIASLE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1563 DQVSLSGksiQELEKTKKALEGEkseiqaaleeaegalELEETKTLRIQLELSQVKAE-------VDRKL---------A 1626
Cdd:COG4913 433 RRKSNIP---ARLLALRDALAEA---------------LGLDEAELPFVGELIEVRPEeerwrgaIERVLggfaltllvP 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1627 EKDEECAN--LRRNHQRA---VESLQASLDAETRARNEALRLKKKMEGDLND----LELQLGH-------ATRQA--TEA 1688
Cdd:COG4913 495 PEHYAAALrwVNRLHLRGrlvYERVRTGLPDPERPRLDPDSLAGKLDFKPHPfrawLEAELGRrfdyvcvDSPEElrRHP 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1689 QAATRlmQAQLKEEQAGR--DEEQRLAAELHEQAQALERRAsLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLH 1766
Cdd:COG4913 575 RAITR--AGQVKGNGTRHekDDRRRIRSRYVLGFDNRAKLA-ALEAELAELEEELAEAEERLEALEAELDALQERREALQ 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1767 SqntglLNQKKKLEADLAQLSGEVEEAAQERREAeEKAKKAITDAAMMAEELKKEQDTsahLERMKKTLEQTVRELQARL 1846
Cdd:COG4913 652 R-----LAEYSWDEIDVASAEREIAELEAELERL-DASSDDLAALEEQLEELEAELEE---LEEELDELKGEIGRLEKEL 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1847 EEAEQaalrggkkQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNL-ARMQDLVDKLQSKVK 1925
Cdd:COG4913 723 EQAEE--------ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALrARLNRAEEELERAMR 794
|
570 580 590
....*....|....*....|....*....|...
gi 578836100 1926 SYKRQFEEAEQQANTNLAKYRKAQHELDDAEER 1958
Cdd:COG4913 795 AFNREWPAETADLDADLESLPEYLALLDRLEED 827
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1633-1857 |
1.22e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.56 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1633 ANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAgrdEEQRL 1712
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK---EIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1713 AAELHEQAQALERRASLLAAELEELRAAL-------EQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQ 1785
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLALllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578836100 1786 LSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGG 1857
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
888-1356 |
3.04e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.45 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 888 LLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEEThvsiTQEKNDLALQLQAEQDNLADAEERchllikskvqlegk 967
Cdd:PRK02224 243 LEEHEERREELETLEAEIEDLRETIAETEREREELAEE----VRDLRERLEELEEERDDLLAEAGL-------------- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 968 vkelsERLEDEeevnaDLAARRRKLEDECTELKKDIDDLELTLakaekekQATENKVKNLTEEMAALDESVARLTKEKKA 1047
Cdd:PRK02224 305 -----DDADAE-----AVEARREELEDRDEELRDRLEECRVAA-------QAHNEEAESLREDADDLEERAEELREEAAE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1048 LQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSL---EQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQ 1124
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLgnaEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1125 L-------------------------EEKLKKKDSELSQLSLRVED--------EQL--LGAQMQKKIKELQARAEELEE 1169
Cdd:PRK02224 448 LleagkcpecgqpvegsphvetieedRERVEELEAELEDLEEEVEEveerleraEDLveAEDRIERLEERREDLEELIAE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1170 ELEAERAARARVEKQRAEAARELEELSERLEEAGGAsAGQREGCRKREAELGRLRRELEEA--ALRHEATVAALRRKQAE 1247
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAEA-EEEAEEAREEVAELNSKLAELKERieSLERIRTLLAAIADAED 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1248 GAAELGEQVDSLQRV----RQKLEKE---KSELRMEVDDlaANVETLTRAKASAEklcrTYEDQLSEakiKVEELQRQLA 1320
Cdd:PRK02224 607 EIERLREKREALAELnderRERLAEKrerKRELEAEFDE--ARIEEAREDKERAE----EYLEQVEE---KLDELREERD 677
|
490 500 510
....*....|....*....|....*....|....*.
gi 578836100 1321 DASTQRGRLQTESGELSRLLEEKECLISQLSRGKAL 1356
Cdd:PRK02224 678 DLQAEIGAVENELEELEELRERREALENRVEALEAL 713
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1636-1989 |
3.77e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1636 RRNHQRAVESLQASLDaetraRNEALRLKKKMEGDLNDLELQLGHATRQAT--EAQAATRLMQAQLKEEQAGRDEEQRLA 1713
Cdd:PTZ00121 1062 AKAHVGQDEGLKPSYK-----DFDFDAKEDNRADEATEEAFGKAEEAKKTEtgKAEEARKAEEAKKKAEDARKAEEARKA 1136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1714 AE---LHEQAQALERRASLLAAELEELRAAleqgERSRRLAEQELLEATERLnllhsqntglLNQKKKLEADLAQLSGEV 1790
Cdd:PTZ00121 1137 EDarkAEEARKAEDAKRVEIARKAEDARKA----EEARKAEDAKKAEAARKA----------EEVRKAEELRKAEDARKA 1202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1791 EEA--AQERREAEEkAKKAitDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAkv 1868
Cdd:PTZ00121 1203 EAArkAEEERKAEE-ARKA--EDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA-- 1277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1869 RELEAELDAEQKKHAEALKGVRKhERRVKELAYQAEEDRKnlarmqdlVDKLQSKVKSYKRQFEEAEqqantnlakyRKA 1948
Cdd:PTZ00121 1278 RKADELKKAEEKKKADEAKKAEE-KKKADEAKKKAEEAKK--------ADEAKKKAEEAKKKADAAK----------KKA 1338
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 578836100 1949 QHELDDAEERADMAETQANKLRARTRDALGPKLSLSPQHKE 1989
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
886-1715 |
4.06e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 65.38 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 886 KPLLRSAQAEEELAALRAELRGLRGALAAA-----EAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKS 960
Cdd:pfam02463 200 LKLKEQAKKALEYYQLKEKLELEEEYLLYLdylklNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 961 KVQLEGKVKELSERLEDEEEVNADLAARRRKLEDEctELKKDIDDLELTLAKAEKEKQATENKVKnlteemaALDESVAR 1040
Cdd:pfam02463 280 EKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE--KLKESEKEKKKAEKELKKEKEEIEELEK-------ELKELEIK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1041 LTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLEcsleqEKKLRMDTERAKRKLEGDLKLTQESVADAAQ 1120
Cdd:pfam02463 351 REAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE-----EELELKSEEEKEAQLLLELARQLEDLLKEEK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1121 DKQQLEEKLKKKDSELSQLSLRvEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLE 1200
Cdd:pfam02463 426 KEELEILEEEEESIELKQGKLT-EEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESK 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1201 EAGGASAGQREGCRKREAELGRLRRELEEAALRHEAtvaalrrkqAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDL 1280
Cdd:pfam02463 505 ARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVEN---------YKVAISTAVIVEVSATADEVEERQKLVRALTELPL 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1281 AAN-VETLTRAKASAEKLCRTYE--DQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLSRGKALA 1357
Cdd:pfam02463 576 GARkLRLLIPKLKLPLKSIAVLEidPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLE 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1358 AQSLEELRRQLEEESKAKSALAHAVQalrhdcDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADaiqrtEELEE 1437
Cdd:pfam02463 656 EGLAEKSEVKASLSELTKELLEIQEL------QEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEA-----EELLA 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1438 AKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELE 1517
Cdd:pfam02463 725 DRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELR 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1518 AAQREsRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAE 1597
Cdd:pfam02463 805 ALEEE-LKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQK 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1598 GALE-LEETKTLRIQLELSQVKAEVDRKLAEKDEECANLRRNH---QRAVESLQASLDAETRARNEALRLKKKMEGDLND 1673
Cdd:pfam02463 884 LKDElESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEaeiLLKYEEEPEELLLEEADEKEKEENNKEEEEERNK 963
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 578836100 1674 LELQLghatRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAE 1715
Cdd:pfam02463 964 RLLLA----KEELGKVNLMAIEEFEEKEERYNKDELEKERLE 1001
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1516-1972 |
4.93e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.70 E-value: 4.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1516 LEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEE 1595
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1596 AEGALELEETKTLRIQlELSQVKAEVDRKLAEKDEECANLRRNHQRaVESLQASLDAETRARnealRLKKKMEGDLNDLE 1675
Cdd:PRK03918 240 IEELEKELESLEGSKR-KLEEKIRELEERIEELKKEIEELEEKVKE-LKELKEKAEEYIKLS----EFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1676 LQLGHATRQATEAQAatRLMQAQLKEEQAG-----RDEEQRLAAELHEQAQALERRASLLaAELEELRAAL-----EQGE 1745
Cdd:PRK03918 314 KRLSRLEEEINGIEE--RIKELEEKEERLEelkkkLKELEKRLEELEERHELYEEAKAKK-EELERLKKRLtgltpEKLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1746 RSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSG--------------------------EVEEAAQERRE 1799
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkelleeytaELKRIEKELKE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1800 AEEKAKKAITDAAMMAEELKKEQDtsahLERMKKTLEQtVRELQARL-----EEAEQAA--LRGGKKQVQKLEAKVRELE 1872
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESE----LIKLKELAEQ-LKELEEKLkkynlEELEKKAeeYEKLKEKLIKLKGEIKSLK 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1873 AELDAEQ---KKHAEALKGVRKHERRVKELAYQAEEdrKNLARMQDLVDKLQSKVKSYKRQFE--EAEQQANTNLAKYRK 1947
Cdd:PRK03918 546 KELEKLEelkKKLAELEKKLDELEEELAELLKELEE--LGFESVEELEERLKELEPFYNEYLElkDAEKELEREEKELKK 623
|
490 500
....*....|....*....|....*
gi 578836100 1948 AQHELDDAEERADMAETQANKLRAR 1972
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKE 648
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
889-1322 |
6.56e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.55 E-value: 6.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 889 LRSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQL-QAEQDNLADAEERCHLLIKSKVQLEGK 967
Cdd:COG4913 281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 968 VKELSERLED----EEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTK 1043
Cdd:COG4913 361 RARLEALLAAlglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1044 EKKALQEAHQQALG-------------DLQAEEDR-----VSALTKAKLRL---EQQVEDLECSLEQEK-KLRMDTERAK 1101
Cdd:COG4913 441 RLLALRDALAEALGldeaelpfvgeliEVRPEEERwrgaiERVLGGFALTLlvpPEHYAAALRWVNRLHlRGRLVYERVR 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1102 RklegdlklTQESVADAAQDKQQLEEKLKKKDSELS-----QLSLR-----VEDEQ------------------------ 1147
Cdd:COG4913 521 T--------GLPDPERPRLDPDSLAGKLDFKPHPFRawleaELGRRfdyvcVDSPEelrrhpraitragqvkgngtrhek 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1148 ----------LLGAQMQKKIKELqaraeeleeeleaeraararvEKQRAEAARELEELSERLEEAggasAGQREGCRKRE 1217
Cdd:COG4913 593 ddrrrirsryVLGFDNRAKLAAL---------------------EAELAELEEELAEAEERLEAL----EAELDALQERR 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1218 AELGRLrRELEEAALRHEATVAALRRKQAE-GAAELG-EQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASAE 1295
Cdd:COG4913 648 EALQRL-AEYSWDEIDVASAEREIAELEAElERLDASsDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726
|
490 500
....*....|....*....|....*..
gi 578836100 1296 KLCRTYEDQLSEAKIKVEELQRQLADA 1322
Cdd:COG4913 727 EELDELQDRLEAAEDLARLELRALLEE 753
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
883-1329 |
6.68e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 6.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 883 FKMKPLLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEEthvsitqekndlalqlqaeqdnladaeerchlLIKSKV 962
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE--------------------------------LKKKLK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 963 QLEGKVKELSERLEDEEEVNAdLAARRRKLEDECTELkkDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLT 1042
Cdd:PRK03918 349 ELEKRLEELEERHELYEEAKA-KKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1043 KEKKALQEAHQQ--ALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESvaDAAQ 1120
Cdd:PRK03918 426 KAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLK--ELAE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1121 DKQQLEEKLKKKDSE-----------LSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAA 1189
Cdd:PRK03918 504 QLKELEEKLKKYNLEelekkaeeyekLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELG 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1190 RELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEgAAELGEQVDSLQRV-----RQ 1264
Cdd:PRK03918 584 FESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKR-LEELRKELEELEKKyseeeYE 662
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578836100 1265 KLEKEKSELRMEVDDLAANVETLTRAKASAEKLCRTYEDQL---SEAKIKVEELQRQLADASTQRGRL 1329
Cdd:PRK03918 663 ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELeerEKAKKELEKLEKALERVEELREKV 730
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
967-1189 |
7.44e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 7.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 967 KVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKK 1046
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1047 ALQEAHQQALGDLQaeedRVSALTKAKLRLEQQ-VEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQL 1125
Cdd:COG4942 101 AQKEELAELLRALY----RLGRQPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578836100 1126 EEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAA 1189
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1410-1988 |
9.94e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 63.97 E-value: 9.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1410 LSKANAEVAQWRSKYEADAIQRTEELEEAKKKLalrlqEAEEgveaanakcssleKAKLRLQTESEDVTLELERATSAAA 1489
Cdd:pfam05483 83 LYKEAEKIKKWKVSIEAELKQKENKLQENRKII-----EAQR-------------KAIQELQFENEKVSLKLEEEIQENK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1490 ALDKKQ---RHLERALEERRRQEEEMQRELEAAQRESRGLGTEL--------------------------FRLRHGHEEA 1540
Cdd:pfam05483 145 DLIKENnatRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLnnniekmilafeelrvqaenarlemhFKLKEDHEKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1541 LEALETLKRENKNLQEEISDLTDQVSLSGKSIQEL-----EKTKKALE-GEKSEIQAALEEAEGALELEETKTLR----- 1609
Cdd:pfam05483 225 QHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLtflleESRDKANQlEEKTKLQDENLKELIEKKDHLTKELEdikms 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1610 IQLELSQVKA-EVDRKLAEK-------DEECANLRRNHQRAVESLQAS-LDAETRARNEALRL-KKKMEGDLNDLELQLG 1679
Cdd:pfam05483 305 LQRSMSTQKAlEEDLQIATKticqlteEKEAQMEELNKAKAAHSFVVTeFEATTCSLEELLRTeQQRLEKNEDQLKIITM 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1680 HATRQATEAQAATRL----------MQAQLKEEQAGRDEE---QRLAAELHEQAQALERRASLLAAELEELRAALEQGER 1746
Cdd:pfam05483 385 ELQKKSSELEEMTKFknnkeveleeLKKILAEDEKLLDEKkqfEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKT 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1747 SRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSA 1826
Cdd:pfam05483 465 SEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEM 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1827 HL----ERMKKTLEQTVRELQARLEEAEQAAlRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQ 1902
Cdd:pfam05483 545 NLrdelESVREEFIQKGDEVKCKLDKSEENA-RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1903 AEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRA----RTRDALG 1978
Cdd:pfam05483 624 GSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKeidkRCQHKIA 703
|
650
....*....|
gi 578836100 1979 PKLSLSPQHK 1988
Cdd:pfam05483 704 EMVALMEKHK 713
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1695-1975 |
1.01e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 64.04 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1695 MQAQLKEEQAGRDEEQRLAAELHE----QAQALERRASL---------LAAELEELRAALEQgeRSRRLaEQELLEATER 1761
Cdd:pfam01576 7 MQAKEEELQKVKERQQKAESELKElekkHQQLCEEKNALqeqlqaeteLCAEAEEMRARLAA--RKQEL-EEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1762 LNLLHSQNTGLLNQKKKLEADLAQLSG--EVEEAAQERREAEekakKAITDAAM--MAEELKKEQDTSAHLERMKKTLEQ 1837
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEqlDEEEAARQKLQLE----KVTTEAKIkkLEEDILLLEDQNSKLSKERKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1838 TVRELQARLEEAEQAALRGGKKQvQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLV 1917
Cdd:pfam01576 160 RISEFTSNLAEEEEKAKSLSKLK-NKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 578836100 1918 DKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRD 1975
Cdd:pfam01576 239 AKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRD 296
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1410-1840 |
1.17e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1410 LSKANAEVAQWRSKYE--ADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCS--SLEKAKLRLQTESEDVTLELERAT 1485
Cdd:COG4717 73 LKELEEELKEAEEKEEeyAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1486 SAAAALDKKQRHLERALEERRRQEEEMQRELE----AAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDL 1561
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEqlslATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1562 TDQVsLSGKSIQELEKTKK---------ALEGEKSEIQAALEEAEGALELEETKTLRIQLELSQVKAEVDRKLAEKDEEC 1632
Cdd:COG4717 233 ENEL-EAAALEERLKEARLllliaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1633 AnLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLmQAQLKEEQAGRDEEQRL 1712
Cdd:COG4717 312 A-LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI-AALLAEAGVEDEEELRA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1713 AAELHEQAQALERRASLLAAELEELRAALEQGERSRRLA--EQELLEATERLNLLHSQNTGLLNQKKKLEADLAQL--SG 1788
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELAELEAELEQLeeDG 469
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 578836100 1789 EVEEAAQERREAEEKAKKAITD--AAMMAEELKKEQDTSAHLERMKKTLEQTVR 1840
Cdd:COG4717 470 ELAELLQELEELKAELRELAEEwaALKLALELLEEAREEYREERLPPVLERASE 523
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
892-1145 |
1.36e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.55 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 892 AQAEEELAALRAELRG-----LRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEG 966
Cdd:TIGR02169 775 HKLEEALNDLEARLSHsripeIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 967 KVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESvarltkekk 1046
Cdd:TIGR02169 855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK--------- 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1047 alqeahqqalgdLQAEEDRVSALTKAKLRLEQQVEDlECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLE 1126
Cdd:TIGR02169 926 ------------LEALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELK 992
|
250
....*....|....*....
gi 578836100 1127 EKLKKKDSELSQLSLRVED 1145
Cdd:TIGR02169 993 EKRAKLEEERKAILERIEE 1011
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
888-1352 |
1.75e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 888 LLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLAlQLQAEQDNLADAEERCHLliksKVQLEGK 967
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE-KLEKLLQLLPLYQELEAL----EAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 968 VKELsERLEDEEEVNADLAARRRKLEDECTELKKDIDDLEltlakaEKEKQATENKVKNLTEEMAALDESVARLTKEKKA 1047
Cdd:COG4717 145 PERL-EELEERLEELRELEEELEELEAELAELQEELEELL------EQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1048 LQEAHQQalgdlqaeedrvsaltkaklrLEQQVEDLECSLEQEKKlrmdtERAKRKLEGDLKLTQESVADAAQDKQQLEE 1127
Cdd:COG4717 218 AQEELEE---------------------LEEELEQLENELEAAAL-----EERLKEARLLLLIAAALLALLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1128 KLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGAsa 1207
Cdd:COG4717 272 ILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL-- 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1208 gqregcRKREAELGRLRRELEEAALRHEATvAALRRKQAEGAAELGEQVDSLQRvRQKLEKEKSELRMEVDDLAANVETL 1287
Cdd:COG4717 350 ------QELLREAEELEEELQLEELEQEIA-ALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEEL 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578836100 1288 TRAKASAEklcrtYEDQLSEAKIKVEELQRQLADASTQRGRLQTE------SGELSRLLEEKECLISQLSR 1352
Cdd:COG4717 422 LEALDEEE-----LEEELEELEEELEELEEELEELREELAELEAEleqleeDGELAELLQELEELKAELRE 487
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
892-1342 |
1.76e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 892 AQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQekndLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKEL 971
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE----LEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 972 SERLEDEEEVNADlAARRRKLEDECTELKKDIDDLELTLAKAE----------KEKQATENKVKNLTEEMAALDESVARL 1041
Cdd:PRK03918 279 EEKVKELKELKEK-AEEYIKLSEFYEEYLDELREIEKRLSRLEeeingieeriKELEEKEERLEELKKKLKELEKRLEEL 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1042 TKEKKALQEA---------HQQALGDLQAE--EDRVSALTKAKLRLEQQVEDLE---CSLEQEKKLRMDT----ERAKRK 1103
Cdd:PRK03918 358 EERHELYEEAkakkeelerLKKRLTGLTPEklEKELEELEKAKEEIEEEISKITariGELKKEIKELKKAieelKKAKGK 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1104 L------------EGDLKLTQESVADAAQDKQQLEEKLKKKDSELSQLS--LRVEDEQLLGAQMQKKIKELQARAEELEE 1169
Cdd:PRK03918 438 CpvcgrelteehrKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEkvLKKESELIKLKELAEQLKELEEKLKKYNL 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1170 ELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGC----RKREAELGRLRRELEEAALRHEATVaALRRKQ 1245
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELekklDELEEELAELLKELEELGFESVEEL-EERLKE 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1246 AEGA----AELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASAEKLCRTY-EDQLSEAKIKVEELQRQLA 1320
Cdd:PRK03918 597 LEPFyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYsEEEYEELREEYLELSRELA 676
|
490 500
....*....|....*....|..
gi 578836100 1321 DASTQRGRLQTESGELSRLLEE 1342
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLEK 698
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
896-1090 |
2.14e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.01 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 896 EELAALRAELRGLRGALAAAEAKR---QELEETHVSITQEKNDLA-LQLQAEQDNLADAEERCHLLIKSKVQLEGKVKEL 971
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIellEPIRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 972 SERLEDEEEVNADLAARRRKLEDECTELK-KDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQE 1050
Cdd:COG4913 308 EAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 578836100 1051 AHQQALGDLQAEEDRVS-ALTKAKLRLEQQVEDLEcSLEQE 1090
Cdd:COG4913 388 EAAALLEALEEELEALEeALAEAEAALRDLRRELR-ELEAE 427
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
964-1483 |
2.19e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.75 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 964 LEGKVKELSERLEDEEEVNADLAARRRKLED----------ECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAA 1033
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEvleeheerreELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1034 LDESVARLTKEkkalqeahqQALGDLQAE--EDRVSALTKAKLRLEQQVEDLECSLEQ-EKKLRMDTERAKRkLEGDLKL 1110
Cdd:PRK02224 291 LEEERDDLLAE---------AGLDDADAEavEARREELEDRDEELRDRLEECRVAAQAhNEEAESLREDADD-LEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1111 TQESVADAAQDKQQLEEKLKKKDSELSQLSLRVEDeqllgaqmqkkikelqaraeeleeeleaeraararVEKQRAEAAR 1190
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEIEELEEEIEE-----------------------------------LRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1191 ELEELSERLEEAggasAGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEkek 1270
Cdd:PRK02224 406 DLGNAEDFLEEL----REERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVE--- 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1271 sELRMEVDDLAANVETLTRAKASAEKLCRTyEDQLSEAKIKVEELQRQLADastQRGRLQTESGELSRLLEEKECLISQl 1350
Cdd:PRK02224 479 -ELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLEELIAE---RRETIEEKRERAEELRERAAELEAE- 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1351 SRGKALAAQSLEELRRQLEEESKA----KSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLlsKANAEVAQWRSKYEA 1426
Cdd:PRK02224 553 AEEKREAAAEAEEEAEEAREEVAElnskLAELKERIESLERIRTLLAAIADAEDEIERLREKR--EALAELNDERRERLA 630
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578836100 1427 DAIQRTEELEEAKKKLAL-----RLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELER 1483
Cdd:PRK02224 631 EKRERKRELEAEFDEARIeeareDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1430-1934 |
2.32e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1430 QRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLqTESEDVTLELERATSAAAALDK---KQRHLERALEERR 1506
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI-EELEKELESLEGSKRKLEEKIReleERIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1507 RQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEK 1586
Cdd:PRK03918 279 EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1587 SEIQAALEEAEGALELEETKTLRIQLELSQVKAEVDrKLAEKDEECANLRRNhqraVESLQASLDAETRARNEALRLKKK 1666
Cdd:PRK03918 359 ERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE-ELEKAKEEIEEEISK----ITARIGELKKEIKELKKAIEELKK 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1667 MEGD----------------LNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLL 1730
Cdd:PRK03918 434 AKGKcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLK 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1731 AAELEELRAALEQGERSRRLAEQ------ELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGE--------VEEAAQE 1796
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKEKLIKlkgeikSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEleelgfesVEELEER 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1797 RREAEE------KAKKAITDAAMMAEELKKEQDT----SAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEA 1866
Cdd:PRK03918 594 LKELEPfyneylELKDAEKELEREEKELKKLEEEldkaFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSR 673
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578836100 1867 KVRELEAELDAEQKKHAEALKGVRKHERRVKELAyQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEA 1934
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTLEKLKEELEERE-KAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1696-1934 |
2.32e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1696 QAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHsqntgllNQ 1775
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE-------KE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1776 KKKLEADLAQLSGEVEEAAqerREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEE--AEQAA 1853
Cdd:COG4942 92 IAELRAELEAQKEELAELL---RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAElaALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1854 LRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKgvrKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEE 1933
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
.
gi 578836100 1934 A 1934
Cdd:COG4942 246 A 246
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1671-1970 |
2.83e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1671 LNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLlaAELEELRAALEQGERSRRL 1750
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREI--AELEAELERLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1751 AEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAammAEELKKEQDTSAHLER 1830
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL---LEERFAAALGDAVERE 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1831 MKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQK--KHAEALKGVR--KHERRVKELayqaeED 1906
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEylALLDRLEEDGlpEYEERFKEL-----LN 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1907 RKNLARMQDLVDKLQSKVKSYKRQFE-------------------EAEQQANTNLAKYRKAQHELDDAEERADMAETQAN 1967
Cdd:COG4913 842 ENSIEFVADLLSKLRRAIREIKERIDplndslkripfgpgrylrlEARPRPDPEVREFRQELRAVTSGASLFDEELSEAR 921
|
...
gi 578836100 1968 KLR 1970
Cdd:COG4913 922 FAA 924
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1712-1940 |
3.28e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.93 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1712 LAAELHEQAQALERRAslLAAELEELR-------AALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLA 1784
Cdd:COG4942 9 LLLALAAAAQADAAAE--AEAELEQLQqeiaeleKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1785 QLSGEVEEAAQERREAEEKAKKAITDAAMMAE----ELKKEQDTSAHLERMKKTLEQTVRELQARLEEAeQAALRGGKKQ 1860
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL-RADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1861 VQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANT 1940
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
894-1083 |
3.97e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 894 AEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLA--LQLQAEQDNLADAEERCHllikskvqlegkvkEL 971
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIA--------------EL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 972 SERLEDEEEVNADLAARRRKLEdectELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKA---- 1047
Cdd:COG4913 674 EAELERLDASSDDLAALEEQLE----ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelra 749
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 578836100 1048 -LQEAHQQALGDLQAE------EDRVSALTKAKLRLEQQVEDL 1083
Cdd:COG4913 750 lLEERFAAALGDAVERelrenlEERIDALRARLNRAEEELERA 792
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
950-1644 |
6.20e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.70 E-value: 6.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 950 AEERCHLLIKSKVQlEGKVKELSERLEDEEEVNAdlaARRRKLEDECTELKKDIDDLELTLA-KAEKEKQATENKV---K 1025
Cdd:PTZ00121 1148 AEDAKRVEIARKAE-DARKAEEARKAEDAKKAEA---ARKAEEVRKAEELRKAEDARKAEAArKAEEERKAEEARKaedA 1223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1026 NLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQ--QVEDLECSLEQEKKLRMDTERAKRK 1103
Cdd:PTZ00121 1224 KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEarKADELKKAEEKKKADEAKKAEEKKK 1303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1104 LEgDLKLTQESVADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEEleaeraararvEK 1183
Cdd:PTZ00121 1304 AD-EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA-----------EK 1371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1184 QRAEAARELEELSERLEEAGGASAGQREGCR-KREAElgRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRV 1262
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEdKKKAD--ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA 1449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1263 RQKLEKEKSelrmevddlAANVETLTRAKASAEKLCRTYED--QLSEAKIKVEELQRQlADASTQRGRLQTESGELSRLL 1340
Cdd:PTZ00121 1450 KKKAEEAKK---------AEEAKKKAEEAKKADEAKKKAEEakKADEAKKKAEEAKKK-ADEAKKAAEAKKKADEAKKAE 1519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1341 EEKECLISQLSRGKALAAQSLEELRRQLEEESKAKSALAHAVQalRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQW 1420
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEE--KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1421 RSKYEADAIQRTEEL---EEAKKKlALRLQEAEEgveaANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRH 1497
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAkkaEEAKIK-AEELKKAEE----EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE 1672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1498 LERALEERRRQEEEMQRELEAAQRESRGlGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEK 1577
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEE-AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578836100 1578 TkkalEGEKSEIQAALEEAEGALELEETKTLRIQLElsQVKAEVDRKLAEKDEECANLRRNHQRAVE 1644
Cdd:PTZ00121 1752 D----EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE--ELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1223-1910 |
6.84e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 61.29 E-value: 6.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1223 LRRELEEAALRHEAtVAALRRKQAEGAAELGEQvdsLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASAEKLC---- 1298
Cdd:pfam15921 115 LQTKLQEMQMERDA-MADIRRRESQSQEDLRNQ---LQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLqeir 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1299 ------------RTYE-DQLSEAKIK-----VEELQRQL-ADASTQRGRLQTESGELSRLLEEK----ECLISQ-LSRGK 1354
Cdd:pfam15921 191 silvdfeeasgkKIYEhDSMSTMHFRslgsaISKILRELdTEISYLKGRIFPVEDQLEALKSESqnkiELLLQQhQDRIE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1355 ALAAQSLEELRRQLEEESKAKSAlAHAVQALrhdcdlLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEE 1434
Cdd:pfam15921 271 QLISEHEVEITGLTEKASSARSQ-ANSIQSQ------LEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDK 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1435 LEEAKKKLALRLQEAEEG--------VEAANAKcSSLEKAKLRLQTESEDVTLELE-------RATSAAAALDkkqrHLE 1499
Cdd:pfam15921 344 IEELEKQLVLANSELTEArterdqfsQESGNLD-DQLQKLLADLHKREKELSLEKEqnkrlwdRDTGNSITID----HLR 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1500 RALEERRRQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTK 1579
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTV 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1580 KALEGEKSEIQAALEEAEGALELEETKT-LRIQlELSQVKAEVDR-------------KLAEKDEECANLRRNhqraVES 1645
Cdd:pfam15921 499 SDLTASLQEKERAIEATNAEITKLRSRVdLKLQ-ELQHLKNEGDHlrnvqtecealklQMAEKDKVIEILRQQ----IEN 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1646 LQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGR-------DEEQRLAAELHE 1718
Cdd:pfam15921 574 MTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKvklvnagSERLRAVKDIKQ 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1719 QAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERR 1798
Cdd:pfam15921 654 ERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQ 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1799 EaEEKAKKAITDAAMMAEELKKEQDTSAHLER--MKKTLEQTVRELQARLEEAEQAA--LRGGKKQVQKLEAKVRELEAE 1874
Cdd:pfam15921 734 K-QITAKRGQIDALQSKIQFLEEAMTNANKEKhfLKEEKNKLSQELSTVATEKNKMAgeLEVLRSQERRLKEKVANMEVA 812
|
730 740 750
....*....|....*....|....*....|....*.
gi 578836100 1875 LDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNL 1910
Cdd:pfam15921 813 LDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKEL 848
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
963-1161 |
1.34e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 963 QLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLT 1042
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1043 KEKK----ALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADA 1118
Cdd:COG4942 104 EELAellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 578836100 1119 AQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQ 1161
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1516-1959 |
1.44e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1516 LEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEE 1595
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1596 aegaleleetktlriqLELSQVKAEVDRKLAEKDEECANLR------RNHQRAVESLQASLDAETRARNEALR-LKKKME 1668
Cdd:COG4717 128 ----------------LPLYQELEALEAELAELPERLEELEerleelRELEEELEELEAELAELQEELEELLEqLSLATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1669 GDLNDLELQLGHATRQATEAQAATRLMQAQLK--EEQAGRDEEQRLAAELHEQAQALERRASLLAA-------------- 1732
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEelEEELEQLENELEAAALEERLKEARLLLLIAAAllallglggsllsl 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1733 ---------------------------ELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQ 1785
Cdd:COG4717 272 iltiagvlflvlgllallflllarekaSLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1786 LSGEVEEAAQERR-EAEEKAKKAITDAAMMA--EELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQvq 1862
Cdd:COG4717 352 LLREAEELEEELQlEELEQEIAALLAEAGVEdeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE-- 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1863 kLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELayqaEEDrknlarmqDLVDKLQSKVKSYKRQFEEAEQQAntnl 1942
Cdd:COG4717 430 -LEEELEELEEELEELEEELEELREELAELEAELEQL----EED--------GELAELLQELEELKAELRELAEEW---- 492
|
490
....*....|....*..
gi 578836100 1943 AKYRKAQHELDDAEERA 1959
Cdd:COG4717 493 AALKLALELLEEAREEY 509
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1727-1968 |
1.49e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1727 ASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKK 1806
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1807 AITDAAMMAEELKKEQDTSAHLER-MKKTLEQTVRELQARLEEAEQAALRGG--KKQVQKLEAKVRELEAELDAEQKKHA 1883
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRaLYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1884 EALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAE 1963
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
....*
gi 578836100 1964 TQANK 1968
Cdd:COG4942 248 FAALK 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1734-1978 |
1.80e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1734 LEELRAALEQGERSRRlAEQELLEATERLNLLhsqntgllnqkkkleADLAQLSGEVEEAAQERREAEE-----KAKKAI 1808
Cdd:COG4913 224 FEAADALVEHFDDLER-AHEALEDAREQIELL---------------EPIRELAERYAAARERLAELEYlraalRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1809 TDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQkleakvrELEAELDAEQKKHAEALKG 1888
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLE-------QLEREIERLERELEERERR 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1889 VRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELddAEERADMAETQAN- 1967
Cdd:COG4913 361 RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL--EAEIASLERRKSNi 438
|
250
....*....|....*.
gi 578836100 1968 -----KLRARTRDALG 1978
Cdd:COG4913 439 parllALRDALAEALG 454
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1730-1970 |
2.11e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 58.00 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1730 LAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAIT 1809
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1810 DAAMMAEELKKEQDTSAHLERMKKTLEQ--------------------TVRELQARLEEAEQAAlrggkkqvqKLEAKVR 1869
Cdd:COG1340 93 ELDELRKELAELNKAGGSIDKLRKEIERlewrqqtevlspeeekelveKIKELEKELEKAKKAL---------EKNEKLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1870 ELEAELDAEQKKhaealkgVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQ 1949
Cdd:COG1340 164 ELRAELKELRKE-------AEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQ 236
|
250 260
....*....|....*....|.
gi 578836100 1950 HELDDAEERADMAETQANKLR 1970
Cdd:COG1340 237 KELRELRKELKKLRKKQRALK 257
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1655-1954 |
2.29e-08 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 59.53 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1655 RARNEALRLKKKMEGDLNDLELQLGHATRQATEAQaatrlmqaqlkEEQAGRDEEQRLAAELHEQAQALERRAS---LLA 1731
Cdd:PLN02939 59 RSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSS-----------DDDHNRASMQRDEAIAAIDNEQQTNSKDgeqLSD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1732 AELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAE------EKAK 1805
Cdd:PLN02939 128 FQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEileeqlEKLR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1806 KAIT-----------------------------DAAMMAEELKKEQDTS---AHLERMKKTLEQTVRELQARLEEAEQAA 1853
Cdd:PLN02939 208 NELLirgateglcvhslskeldvlkeenmllkdDIQFLKAELIEVAETEervFKLEKERSLLDASLRELESKFIVAQEDV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1854 LRGGKKQVQKLEAKVRELEAELDAEQKKHAEA---LKGVRKHERRVKELAYQAEEdrKNLARMQ-DLVDKLQSKVKSYKR 1929
Cdd:PLN02939 288 SKLSPLQYDCWWEKVENLQDLLDRATNQVEKAalvLDQNQDLRDKVDKLEASLKE--ANVSKFSsYKVELLQQKLKLLEE 365
|
330 340
....*....|....*....|....*
gi 578836100 1930 QFEEAEQQANTNLAKYRKAQHELDD 1954
Cdd:PLN02939 366 RLQASDHEIHSYIQLYQESIKEFQD 390
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
892-1296 |
3.10e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 892 AQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKN--DLALQLQAEQDNLADAEERCHllikskvQLEGKVK 969
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLE-------ELEERLE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 970 ELSERLEDEEEVNADLAARRRKLEDECT-----------ELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESV 1038
Cdd:COG4717 157 ELRELEEELEELEAELAELQEELEELLEqlslateeelqDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1039 ARLTKEKKALQE-----------AHQQALGDLQAEEDRVSA---------------LTKAKLRLEQQVEDLECSLEQEKK 1092
Cdd:COG4717 237 EAAALEERLKEArlllliaaallALLGLGGSLLSLILTIAGvlflvlgllallfllLAREKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1093 LRMDTERAKRKLEGDLKLTQESVADA---AQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELqaraeelee 1169
Cdd:COG4717 317 EEEELEELLAALGLPPDLSPEELLELldrIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEEL--------- 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1170 eLEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEaalrheaTVAALRRKQAEGA 1249
Cdd:COG4717 388 -RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEE-------ELEELREELAELE 459
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 578836100 1250 AELG--EQVDSLQRVRQKLEKEKSELRMEVDDLAAN---VETLTRAKASAEK 1296
Cdd:COG4717 460 AELEqlEEDGELAELLQELEELKAELRELAEEWAALklaLELLEEAREEYRE 511
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1427-1940 |
3.80e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1427 DAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKkqrhleraleerr 1506
Cdd:PRK02224 283 DLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRE------------- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1507 rqeeemqrelEAAQRESR--GLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEG 1584
Cdd:PRK02224 350 ----------DADDLEERaeELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1585 EKSEIQAALeeaegaleleetKTLRIQL-ELSQVKAEVDRKLAE-KDEECAnlrrnhQRAVESLQASLDAETRARNEalr 1662
Cdd:PRK02224 420 ERDELRERE------------AELEATLrTARERVEEAEALLEAgKCPECG------QPVEGSPHVETIEEDRERVE--- 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1663 lkkKMEGDLNDLELQlghatrQATEAQAATRLMQAQLKEEQAGRDEEQR-----LAAELHEQAQALERRASLLAAELEEL 1737
Cdd:PRK02224 479 ---ELEAELEDLEEE------VEEVEERLERAEDLVEAEDRIERLEERRedleeLIAERRETIEEKRERAEELRERAAEL 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1738 RAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEaDLAQLSGEVEEAAQERREAEEKAKKaitdaamMAEE 1817
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREA-------LAEL 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1818 LKKEQDTSAHLERMKKTLEQTVRElqARLEEAEQAALRgGKKQVQKLEAKVRELEAELDAEQKkhaeALKGVrkhERRVK 1897
Cdd:PRK02224 622 NDERRERLAEKRERKRELEAEFDE--ARIEEAREDKER-AEEYLEQVEEKLDELREERDDLQA----EIGAV---ENELE 691
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 578836100 1898 ELayqaEEDRKNLARMQDLVDKLQSkvksykrQFEEAEQQANT 1940
Cdd:PRK02224 692 EL----EELRERREALENRVEALEA-------LYDEAEELESM 723
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
968-1583 |
4.82e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 4.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 968 VKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNL---TEEMAALDESVARLTKE 1044
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELeelKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1045 KKALQEahqqalgDLQAEEDRVSALTKAKLRLEQQVEDLEcSLEQE-------KKLRMDTERAKRKLEGDL-------KL 1110
Cdd:PRK03918 254 KRKLEE-------KIRELEERIEELKKEIEELEEKVKELK-ELKEKaeeyiklSEFYEEYLDELREIEKRLsrleeeiNG 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1111 TQESVADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAAR 1190
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1191 ELEELSerleeaggasaGQREGCRKREAELGRLRRELEEA-----ALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQK 1265
Cdd:PRK03918 406 EISKIT-----------ARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEK 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1266 LEKEKSELRmEVDDLAANVETLTRAKASAEKLcRTYEDQLSeaKIKVEELQRQLADASTQRGRLQTESGELSRLLEEkec 1345
Cdd:PRK03918 475 ERKLRKELR-ELEKVLKKESELIKLKELAEQL-KELEEKLK--KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE--- 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1346 lisqLSRGKALaaqsleelrrqleeeSKAKSALAHAVQALRhdcdllreqheeeaeaqaelqRLLSKANAEVAQWRSKYE 1425
Cdd:PRK03918 548 ----LEKLEEL---------------KKKLAELEKKLDELE---------------------EELAELLKELEELGFESV 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1426 ADAIQRTEELEEAKKKLaLRLQEAEEGVEaanakcsSLEKAKLRLQTESEDVTLELERATSAAAALDKKqrhleraleER 1505
Cdd:PRK03918 588 EELEERLKELEPFYNEY-LELKDAEKELE-------REEKELKKLEEELDKAFEELAETEKRLEELRKE---------LE 650
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578836100 1506 RRQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTdqvslsgKSIQELEKTKKALE 1583
Cdd:PRK03918 651 ELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE-------KAKKELEKLEKALE 721
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1712-1949 |
6.46e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.72 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1712 LAAELHEQAQALERRASLLAAELEELRAALEQgersrrlAEQELLEATERLNLLHSQNtgllnQKKKLEADLAQLSGEVE 1791
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEE-------AEAALEEFRQKNGLVDLSE-----EAKLLLQQLSELESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1792 EAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAhlermKKTLEQTVRELQARLEEAEQaalRGGKK--QVQKLEAKVR 1869
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPDALPELLQSPV-----IQQLRAQLAELEAELAELSA---RYTPNhpDVIALRAQIA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1870 ELEAELDAEQKKHAEALKG-VRKHERRVKELAYQAEEDRKNLARMQdlvdKLQSKVKSYKRQFEEAEQQANTNLAKYRKA 1948
Cdd:COG3206 302 ALRAQLQQEAQRILASLEAeLEALQAREASLQAQLAQLEARLAELP----ELEAELRRLEREVEVARELYESLLQRLEEA 377
|
.
gi 578836100 1949 Q 1949
Cdd:COG3206 378 R 378
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
884-1068 |
1.04e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.93 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 884 KMKPLLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERchllikskvq 963
Cdd:COG1579 5 DLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 964 lEGKVKELSERLEDEEEVNAdlaarrrkledecteLKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTK 1043
Cdd:COG1579 75 -IKKYEEQLGNVRNNKEYEA---------------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138
|
170 180
....*....|....*....|....*
gi 578836100 1044 EKKALQEAHQQALGDLQAEEDRVSA 1068
Cdd:COG1579 139 ELEEKKAELDEELAELEAELEELEA 163
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
934-1160 |
1.19e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.95 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 934 NDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKA 1013
Cdd:TIGR04523 310 KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1014 EKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKL 1093
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQ 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578836100 1094 RMDTERAKRKLEGDLKLTQESVADAAQD-------KQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKEL 1160
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKELKSKEKElkklneeKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1639-1946 |
2.02e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 56.29 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1639 HQRAVESLQASldaETRARNEALRLKKKMEGDLNDLELQlghatRQATEAQAATrlmQAQLKEEQAGRDEEQRLAAE--- 1715
Cdd:pfam17380 280 HQKAVSERQQQ---EKFEKMEQERLRQEKEEKAREVERR-----RKLEEAEKAR---QAEMDRQAAIYAEQERMAMErer 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1716 ------LHEQAQALER-RASLLAAELEELRA----ALEQGERSRRLAEQelLEATERLNLLHSQNTGLLNQKKKleaDLA 1784
Cdd:pfam17380 349 elerirQEERKRELERiRQEEIAMEISRMRElerlQMERQQKNERVRQE--LEAARKVKILEEERQRKIQQQKV---EME 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1785 QLSGEVEEAAQE--RREAEEKAKKAitdAAMMAEELKKEQDT----SAHLERMKKTLE-QTVRELQARLEEAE----QAA 1853
Cdd:pfam17380 424 QIRAEQEEARQRevRRLEEERAREM---ERVRLEEQERQQQVerlrQQEEERKRKKLElEKEKRDRKRAEEQRrkilEKE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1854 LRGGKKQVQKLEAKVRELEAELD------AEQKKHAEALKGVRKHE-----RRVKELAYQAEEDRKNLARMQDLVDKLQS 1922
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKEMEerqkaiYEEERRREAEEERRKQQemeerRRIQEQMRKATEERSRLEAMEREREMMRQ 580
|
330 340
....*....|....*....|....*
gi 578836100 1923 KVKSYKRQFE-EAEQQANTNLAKYR 1946
Cdd:pfam17380 581 IVESEKARAEyEATTPITTIKPIYR 605
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1707-1878 |
2.07e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.16 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1707 DEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNllhsQNTGLLNQKKKLEaDLAQL 1786
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK----KYEEQLGNVRNNK-EYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1787 SGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQdtsAHLERMKKTLEQTVRELQARLEEAEqaalrggkKQVQKLEA 1866
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELE---AELAELEAELEEKKAELDEELAELE--------AELEELEA 163
|
170
....*....|..
gi 578836100 1867 KVRELEAELDAE 1878
Cdd:COG1579 164 EREELAAKIPPE 175
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
896-1290 |
2.71e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 56.11 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 896 EELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLAdaeerchlLIKSKVQLEGK-------V 968
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLN--------LVQTALRQQEKieryqedL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 969 KELSERLEDEEEVNADLAARRrkledectelkkdiddleltlAKAEKEKQATENKVKNLTEEMA----ALDESVARLTKE 1044
Cdd:COG3096 357 EELTERLEEQEEVVEEAAEQL---------------------AEAEARLEAAEEEVDSLKSQLAdyqqALDVQQTRAIQY 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1045 KKALQ---EAHQQ-ALGDLQAE--EDRVSALtkaKLRLEQQVEDLecsLEQEKKLRmDTERAKRKLEGDLKLTQESV--- 1115
Cdd:COG3096 416 QQAVQaleKARALcGLPDLTPEnaEDYLAAF---RAKEQQATEEV---LELEQKLS-VADAARRQFEKAYELVCKIAgev 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1116 --ADAAQDKQQL-------------EEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARAR 1180
Cdd:COG3096 489 erSQAWQTARELlrryrsqqalaqrLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1181 VEKQRAEAAReleelserleeaggasagQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQ 1260
Cdd:COG3096 569 LEEQAAEAVE------------------QRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTA 630
|
410 420 430
....*....|....*....|....*....|
gi 578836100 1261 RVRQKLEKEKsELRMEVDDLAANVETLTRA 1290
Cdd:COG3096 631 AMQQLLERER-EATVERDELAARKQALESQ 659
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1224-1955 |
4.16e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 55.34 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1224 RRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQrvrqKLEKEKSELRMEVDDLAANVETLTRAKASAEKLCRtYED 1303
Cdd:COG3096 280 RRELSERALELRRELFGARRQLAEEQYRLVEMARELE----ELSARESDLEQDYQAASDHLNLVQTALRQQEKIER-YQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1304 QLSEAKIKVEELQRQLADASTQRGRLQTEsgeLSRLLEEKECLISQLS-RGKALAAQSLEelrrqleeeskaksALAH-- 1380
Cdd:COG3096 355 DLEELTERLEEQEEVVEEAAEQLAEAEAR---LEAAEEEVDSLKSQLAdYQQALDVQQTR--------------AIQYqq 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1381 AVQALRHDCDLLREQHeeeaeaqaelqrlLSKANAEvaQWRSKYEADAIQRTEELEEAKKKLAL------RLQEAEEGVE 1454
Cdd:COG3096 418 AVQALEKARALCGLPD-------------LTPENAE--DYLAAFRAKEQQATEEVLELEQKLSVadaarrQFEKAYELVC 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1455 AANAKCS---SLEKAKLRLQTESEDVTLeLERATSAAAALDKKQRhleraleerrrqeeemqreLEAAQRESRGLGTELF 1531
Cdd:COG3096 483 KIAGEVErsqAWQTARELLRRYRSQQAL-AQRLQQLRAQLAELEQ-------------------RLRQQQNAERLLEEFC 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1532 RLRHGHEEALEALETLKREnknLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAA----------------LEE 1595
Cdd:COG3096 543 QRIGQQLDAAEELEELLAE---LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlaaqdalerlreQSG 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1596 AEGALELEETKTLRIQLE-LSQVKAEVDRKLAEKDEECANLRRNHQ----------RAVESLQASLDAETR--------- 1655
Cdd:COG3096 620 EALADSQEVTAAMQQLLErEREATVERDELAARKQALESQIERLSQpggaedprllALAERLGGVLLSEIYddvtledap 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1656 --------ARNE--------ALRLKKKMEGDLNDLELQLGHAT------RQATEAQAA--TRLMQAQLKEE--------- 1702
Cdd:COG3096 700 yfsalygpARHAivvpdlsaVKEQLAGLEDCPEDLYLIEGDPDsfddsvFDAEELEDAvvVKLSDRQWRYSrfpevplfg 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1703 QAGRdeEQRLAaELHEQAQALERRASLLAAELEELRAALEQGER--SRRLA-------EQELLEATERLNllhsqntgll 1773
Cdd:COG3096 780 RAAR--EKRLE-ELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvGGHLAvafapdpEAELAALRQRRS---------- 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1774 nqkkKLEADLAQLSGEVEEAAQERREAEEKA---KKAITDAAMMAEElkkeqdtsahlermkkTLEQTVRELQARLEEAE 1850
Cdd:COG3096 847 ----ELERELAQHRAQEQQLRQQLDQLKEQLqllNKLLPQANLLADE----------------TLADRLEELREELDAAQ 906
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1851 QAA-------------------LRGGKKQVQKLEAKVRELEAELDaEQKKHAEALKGVRKherRVKELAYQAEEDRknLA 1911
Cdd:COG3096 907 EAQafiqqhgkalaqleplvavLQSDPEQFEQLQADYLQAKEQQR-RLKQQIFALSEVVQ---RRPHFSYEDAVGL--LG 980
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 578836100 1912 RMQDLVDKLqskvksyKRQFEEAEQQANTNLAKYRKAQHELDDA 1955
Cdd:COG3096 981 ENSDLNEKL-------RARLEQAEEARREAREQLRQAQAQYSQY 1017
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
983-1212 |
4.35e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 983 ADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAE 1062
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1063 EDRVS---ALTKAK---------LRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLEEKLK 1130
Cdd:COG3883 99 GGSVSyldVLLGSEsfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1131 KKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQR 1210
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAA 258
|
..
gi 578836100 1211 EG 1212
Cdd:COG3883 259 AG 260
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1712-1909 |
5.43e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1712 LAAELHEQAQALE----RRASLLAAELEELRAALEQGERSrrlaEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLs 1787
Cdd:COG4717 47 LLERLEKEADELFkpqgRKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEKL- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1788 gEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAK 1867
Cdd:COG4717 122 -EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 578836100 1868 VRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKN 1909
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1706-1891 |
6.41e-07 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 54.31 E-value: 6.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1706 RDEEQRLAaELHEQAQALERRASLLAAELEEL-RAALEQGE------RSRRLAE-QELLEATER-LNLLHSQNTGLLNQ- 1775
Cdd:COG0497 168 RALKKELE-ELRADEAERARELDLLRFQLEELeAAALQPGEeeeleeERRRLSNaEKLREALQEaLEALSGGEGGALDLl 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1776 ---KKKLEaDLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELkkEQDTS---------AHLERMKKTLEQTVRELQ 1843
Cdd:COG0497 247 gqaLRALE-RLAEYDPSLAELAERLESALIELEEAASELRRYLDSL--EFDPErleeveerlALLRRLARKYGVTVEELL 323
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 578836100 1844 ARLEEAEQ--AALRGGKKQVQKLEAKVRELEAELDAEqkkhAEALKGVRK 1891
Cdd:COG0497 324 AYAEELRAelAELENSDERLEELEAELAEAEAELLEA----AEKLSAARK 369
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1632-1938 |
1.11e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 54.04 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1632 CANLRRNHQRAvESLQASLDAETRARNEALRLKKKMEgdlndLELQLGHATRQATEAQAATRLMQAQLKEEQAG------ 1705
Cdd:PRK10246 585 CASLNITLQPQ-DDIQPWLDAQEEHERQLRLLSQRHE-----LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGyaltlp 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1706 -----------RDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLN 1774
Cdd:PRK10246 659 qedeeaswlatRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQ 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1775 QKKKLEADLAQlsgeveeaAQERREAEEKAKKAITDAAMMAEELKKEqdTSAHLERMKKTLEQTVRELQARLEEAEQAal 1854
Cdd:PRK10246 739 QDVLEAQRLQK--------AQAQFDTALQASVFDDQQAFLAALLDEE--TLTQLEQLKQNLENQRQQAQTLVTQTAQA-- 806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1855 rggkkQVQKLEAKVRELEAELDAEQKKHAEAL--KGVRKHERRVKELAYQAEEDRKNLARMQDLVdklqskvksykRQFE 1932
Cdd:PRK10246 807 -----LAQHQQHRPDGLDLTVTVEQIQQELAQlaQQLRENTTRQGEIRQQLKQDADNRQQQQALM-----------QQIA 870
|
....*.
gi 578836100 1933 EAEQQA 1938
Cdd:PRK10246 871 QATQQV 876
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1828-1949 |
1.13e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 53.05 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1828 LERMKK-TLEQTVRELQARLEEAE------QAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALkgvrkheRRVKELA 1900
Cdd:PRK09039 71 LERQGNqDLQDSVANLRASLSAAEaersrlQALLAELAGAGAAAEGRAGELAQELDSEKQVSARAL-------AQVELLN 143
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 578836100 1901 YQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAkyRKAQ 1949
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALA--QRVQ 190
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
1789-1900 |
1.58e-06 |
|
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 462259 [Multi-domain] Cd Length: 353 Bit Score: 52.68 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1789 EVEEAAQERREAEEKAKKAITDAAMMAEELkkeqdtsahlERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEaKV 1868
Cdd:pfam07767 206 EAEKKRLKEEEKLERVLEKIAESAATAEAR----------EEKRKTKAQRNKEKRRKEEEREAKEEKALKKKLAQLE-RL 274
|
90 100 110
....*....|....*....|....*....|..
gi 578836100 1869 RELEAELDAEQKKHAEALKGVRKHERRVKELA 1900
Cdd:pfam07767 275 KEIAKEIAEKEKEREEKAEARKREKRKKKKEE 306
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1018-1274 |
1.92e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1018 QATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLEcslEQEKKLRMDT 1097
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE---AELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1098 ERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQAraeeleeeleaeraA 1177
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRA--------------D 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1178 RARVEKQRAEAAReleelserleeaggasagQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGA---AELGE 1254
Cdd:COG4942 159 LAELAALRAELEA------------------ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAaelAELQQ 220
|
250 260
....*....|....*....|
gi 578836100 1255 QVDSLQRVRQKLEKEKSELR 1274
Cdd:COG4942 221 EAEELEALIARLEAEAAAAA 240
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
697-724 |
2.18e-06 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 49.65 E-value: 2.18e-06
10 20
....*....|....*....|....*...
gi 578836100 697 SQLHKENLNKLMTNLRATQPHFVRCIVP 724
Cdd:cd01363 143 FEIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1532-1852 |
2.43e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.82 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1532 RLRHGHEEALEALE---TLKRENKNLQEEISD----LTDQVSLSGKSIQELEKTKkaLEGEKSEIQAALEEAEGALELEE 1604
Cdd:pfam17380 300 RLRQEKEEKAREVErrrKLEEAEKARQAEMDRqaaiYAEQERMAMERERELERIR--QEERKRELERIRQEEIAMEISRM 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1605 TKTLRIQLELSQ----VKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQlgh 1680
Cdd:pfam17380 378 RELERLQMERQQknerVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE--- 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1681 atrQATEAQAATRLMQaqlkEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELleaTE 1760
Cdd:pfam17380 455 ---EQERQQQVERLRQ----QEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEM---EE 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1761 RLNLLHSQntgllnqkkkleadlaqlsgeveeaaQERREAEEKAKKA--ITDAAMMAEELKKEQDTSAHLERMKKTleqt 1838
Cdd:pfam17380 525 RQKAIYEE--------------------------ERRREAEEERRKQqeMEERRRIQEQMRKATEERSRLEAMERE---- 574
|
330
....*....|....
gi 578836100 1839 vRELQARLEEAEQA 1852
Cdd:pfam17380 575 -REMMRQIVESEKA 587
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1774-1975 |
3.02e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1774 NQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQ-- 1851
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAel 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1852 AALRGG-KKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQ 1930
Cdd:COG4942 100 EAQKEElAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 578836100 1931 FEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRD 1975
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
886-1590 |
3.12e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 52.74 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 886 KPLLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEkndlaLQLQAEQDNL---ADAEERCHLLIKSKV 962
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQS-----LATRLELDGFergPFSERQIKNFHTLVI 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 963 Q-LEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAE-------KEKQATENKVKNLTEEMAAL 1034
Cdd:TIGR00606 401 ErQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQeelkfviKELQQLEGSSDRILELDQEL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1035 DESVARLTK-EKKALQEAHQQALGDLQAEEdrvSALTKAKLRLEQQVEDLECSLEQEKKL------RMDTERAKRKLEGD 1107
Cdd:TIGR00606 481 RKAERELSKaEKNSLTETLKKEVKSLQNEK---ADLDRKLRKLDQEMEQLNHHTTTRTQMemltkdKMDKDEQIRKIKSR 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1108 LKLTQESVADAAQDKQQLEEKLKKKDSELSQLSLRVedeqllgAQMQKKIKELQARAEELEEELEAERAARARVEKQRAE 1187
Cdd:TIGR00606 558 HSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRL-------AKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1188 AAreleelserleeaggasagqreGCRKREAELGRLRRELEEAAlRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLE 1267
Cdd:TIGR00606 631 VC----------------------GSQDEESDLERLKEEIEKSS-KQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVF 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1268 KEKSELRMEVDDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVE----ELQRQLADASTQRGRLQTESGELSRL---L 1340
Cdd:TIGR00606 688 QTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPgrqsIIDLKEKEIPELRNKLQKVNRDIQRLkndI 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1341 EEKECLISQLSRGKALAA--------------QSLEELRRQLEEESKAKSA-LAHAVQALRHDCDLLREQHEEEAEAQAE 1405
Cdd:TIGR00606 768 EEQETLLGTIMPEEESAKvcltdvtimerfqmELKDVERKIAQQAAKLQGSdLDRTVQQVNQEKQEKQHELDTVVSKIEL 847
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1406 LQRLLSKANAEVAQWRSKYE---------ADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESED 1476
Cdd:TIGR00606 848 NRKLIQDQQEQIQHLKSKTNelkseklqiGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEE 927
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1477 VTLELEraTSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQE 1556
Cdd:TIGR00606 928 LISSKE--TSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQ 1005
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 578836100 1557 EI-------SDLTDQVSLSGKS--IQELEKTKKALEGEKSEIQ 1590
Cdd:TIGR00606 1006 DIdtqkiqeRWLQDNLTLRKREneLKEVEEELKQHLKEMGQMQ 1048
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1245-1489 |
3.24e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1245 QAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADAST 1324
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1325 QRGRLQTESGELSRLLEekecLISQLSRGKALAAQSLEELRRQLEEESKAKS-ALAHAVQALRHDCDLLREQHEEEAEAQ 1403
Cdd:COG4942 98 ELEAQKEELAELLRALY----RLGRQPPLALLLSPEDFLDAVRRLQYLKYLApARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1404 AELQRLLskanAEVAQWRSKYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANakcsSLEKAKLRLQTESEDVTLELER 1483
Cdd:COG4942 174 AELEALL----AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE----ELEALIARLEAEAAAAAERTPA 245
|
....*.
gi 578836100 1484 ATSAAA 1489
Cdd:COG4942 246 AGFAAL 251
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1609-1817 |
3.33e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1609 RIQLELSQVKAEVDRkLAEKDEECANLRRNHQRA--VESLQASLDAETRARnEALRLKKKME---GDLNDLELQLGHATR 1683
Cdd:COG4913 239 RAHEALEDAREQIEL-LEPIRELAERYAAARERLaeLEYLRAALRLWFAQR-RLELLEAELEelrAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1684 QATEAQAATRLMQAQLkeEQAGRDEEQRLAAELH---EQAQALERRASLLAAELEELRAALEQGERS----RRLAEQELL 1756
Cdd:COG4913 317 RLDALREELDELEAQI--RGNGGDRLEQLEREIErleRELEERERRRARLEALLAALGLPLPASAEEfaalRAEAAALLE 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578836100 1757 EATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERR---EAEEKAKKAITDAAMMAEE 1817
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSnipARLLALRDALAEALGLDEA 458
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1706-1980 |
3.59e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.26 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1706 RDEEQRLAAELhEQAQALERRAslLAAE---LEELRAALEQGERSRRLAEQELLEATERLNLLHsqnTGLLNQKK----- 1777
Cdd:COG3096 280 RRELSERALEL-RRELFGARRQ--LAEEqyrLVEMARELEELSARESDLEQDYQAASDHLNLVQ---TALRQQEKieryq 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1778 ----KLEADLAQLSGEVEEAAQERREAEEKAKKAITDaammAEELK----------KEQDTSA--------HLERMKKTL 1835
Cdd:COG3096 354 edleELTERLEEQEEVVEEAAEQLAEAEARLEAAEEE----VDSLKsqladyqqalDVQQTRAiqyqqavqALEKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1836 EQTvrELQARLEEAEQAALRGgkkQVQKLEAKVRELEAEL---DAEQKKHAEALKGVRKH----ER-----RVKELAYQA 1903
Cdd:COG3096 430 GLP--DLTPENAEDYLAAFRA---KEQQATEEVLELEQKLsvaDAARRQFEKAYELVCKIagevERsqawqTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1904 EEDRKNLARMQDLVDKLQ------SKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRA------ 1971
Cdd:COG3096 505 RSQQALAQRLQQLRAQLAeleqrlRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEqrselr 584
|
....*....
gi 578836100 1972 RTRDALGPK 1980
Cdd:COG3096 585 QQLEQLRAR 593
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
937-1561 |
3.78e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.15 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 937 ALQLQAEQDNLADAEERCHLLIKSKVQLEgkvKELSERLEDEEEVNADLAARRRKLEDECTELKkdiddleltlAKAEKE 1016
Cdd:pfam12128 243 FTKLQQEFNTLESAELRLSHLHFGYKSDE---TLIASRQEERQETSAELNQLLRTLDDQWKEKR----------DELNGE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1017 KQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQAL----GDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKK 1092
Cdd:pfam12128 310 LSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLpswqSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNN 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1093 L---RMDTERAKRKLEGDLKLTQESvadaaQDKQQLEEKLKkkdSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEE 1169
Cdd:pfam12128 390 RdiaGIKDKLAKIREARDRQLAVAE-----DDLQALESELR---EQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1170 ELEAERAARARVEKQRAE---AARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAALRHEA---TVAALRR 1243
Cdd:pfam12128 462 LLLQLENFDERIERAREEqeaANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPqagTLLHFLR 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1244 KQAEGAAE-LGEQVDSLQRVRQKLEKEKSEL----------------RMEVDDLAANVETLTRAKASAEKLCRT------ 1300
Cdd:pfam12128 542 KEAPDWEQsIGKVISPELLHRTDLDPEVWDGsvggelnlygvkldlkRIDVPEWAASEEELRERLDKAEEALQSarekqa 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1301 -YEDQLSEAKIKVEELQRQLADASTQrgrLQTESGELSRLLEEKECLisQLSRGKALAAQSLEELRRQLEEESKAKSALA 1379
Cdd:pfam12128 622 aAEEQLVQANGELEKASREETFARTA---LKNARLDLRRLFDEKQSE--KDKKNKALAERKDSANERLNSLEAQLKQLDK 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1380 HAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKKKlalrlQEAEEGVEaanak 1459
Cdd:pfam12128 697 KHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKR-----DLASLGVD----- 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1460 csslEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQRESRGlgtELFRLRHGHEE 1539
Cdd:pfam12128 767 ----PDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQ---QLARLIADTKL 839
|
650 660
....*....|....*....|..
gi 578836100 1540 ALEALETLKRENKNLQEEISDL 1561
Cdd:pfam12128 840 RRAKLEMERKASEKQQVRLSEN 861
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1721-1972 |
3.87e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1721 QALERRASLLAAE---------LEELRAALEQGERSRRLAEQELLEATERLNLLhsqNTGLLNQKK---------KLEAD 1782
Cdd:PRK04863 287 EALELRRELYTSRrqlaaeqyrLVEMARELAELNEAESDLEQDYQAASDHLNLV---QTALRQQEKieryqadleELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1783 LAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRelqaRLEEAEQA------ALRG 1856
Cdd:PRK04863 364 LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQ----ALERAKQLcglpdlTADN 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1857 GKKQVQKLEAKVREL-EAELDAEQK---------KHAEALKGVRK---------HERRVKELAYQAEEDRKNLARMQDLV 1917
Cdd:PRK04863 440 AEDWLEEFQAKEQEAtEELLSLEQKlsvaqaahsQFEQAYQLVRKiagevsrseAWDVARELLRRLREQRHLAEQLQQLR 519
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578836100 1918 DKLQ------SKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRAR 1972
Cdd:PRK04863 520 MRLSeleqrlRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARER 580
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1540-1754 |
4.44e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1540 ALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQLELSQVKA 1619
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1620 EVDRKLAEKDEECANLRRNHQRAVESL----QASLDAETRAR-----NEALR-LKKKMEGDLNDLELQLGHATRQATEAQ 1689
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQylkylAPARReQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578836100 1690 AATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQE 1754
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1790-1929 |
4.57e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.78 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1790 VEEAAQERREAE--EKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEqaalrggkKQVQKLEAK 1867
Cdd:COG2433 378 IEEALEELIEKElpEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKD--------ERIERLERE 449
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578836100 1868 VRELEAELDAEQKKHAEalkgVRKHERRVKELayqaeedRKNLARMQDLVDKLQSKVKSYKR 1929
Cdd:COG2433 450 LSEARSEERREIRKDRE----ISRLDREIERL-------ERELEEERERIEELKRKLERLKE 500
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1112-1338 |
4.59e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1112 QESVADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAarE 1191
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL--R 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1192 LEELSERLEEAGGASAGQREGCRKREAELgrLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKS 1271
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALL--LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578836100 1272 ELRMEVDDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSR 1338
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
888-1145 |
4.60e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.10 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 888 LLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEethvsitQEKNDLalqlqaeQDNLADAEERCHLLIKSKVQLEGK 967
Cdd:pfam01576 825 LAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQ-------QERDEL-------ADEIASGASGKSALQDEKRRLEAR 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 968 VKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVArlTKEKKA 1047
Cdd:pfam01576 891 IAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK--SKFKSS 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1048 LQEahqqalgdlqaeedrvsaltkaklrLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLEE 1127
Cdd:pfam01576 969 IAA-------------------------LEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKD 1023
|
250
....*....|....*...
gi 578836100 1128 KLKKKDSELSQLSLRVED 1145
Cdd:pfam01576 1024 QAEKGNSRMKQLKRQLEE 1041
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1606-1966 |
6.42e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.49 E-value: 6.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1606 KTLRIQLELSQVKAEVDRKLAEKDEECANLRRNHQRAVESLQasldaetRARNeALRLKKKME---GDLNDLELQLGHAT 1682
Cdd:COG3096 296 GARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLN-------LVQT-ALRQQEKIEryqEDLEELTERLEEQE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1683 RQATEAQ-----AATRLMQA---------QLKEEQAGRDEEQRLAAELHEQAQALERRASLLAA----------ELEELR 1738
Cdd:COG3096 368 EVVEEAAeqlaeAEARLEAAeeevdslksQLADYQQALDVQQTRAIQYQQAVQALEKARALCGLpdltpenaedYLAAFR 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1739 AALEQGERSRRLAEQELLEATERlnllHSQNtgllnqKKKLEAdLAQLSGEVEeaaqeRREAEEKAKKAITDAammaeel 1818
Cdd:COG3096 448 AKEQQATEEVLELEQKLSVADAA----RRQF------EKAYEL-VCKIAGEVE-----RSQAWQTARELLRRY------- 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1819 kkeqdtsahlermkktleqtvRELQARLEeaeqaalrggkkQVQKLEAKVRELEAELDAEQKKhaealkgvrkhERRVKE 1898
Cdd:COG3096 505 ---------------------RSQQALAQ------------RLQQLRAQLAELEQRLRQQQNA-----------ERLLEE 540
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578836100 1899 LAYQAEEDRKNlarmQDLVDKLQSKVKSykrQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQA 1966
Cdd:COG3096 541 FCQRIGQQLDA----AEELEELLAELEA---QLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARA 601
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
895-1121 |
6.48e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 895 EEELAALRAELRglrgalaAAEAKRQELEETH--VSITQEKNDLALQLQAEQDNLADAEERchlliksKVQLEGKVKELS 972
Cdd:COG3206 181 EEQLPELRKELE-------EAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAE-------LAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 973 ERLEDEEEVNADLAArrrklEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAh 1052
Cdd:COG3206 247 AQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEA- 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1053 qqalgDLQAEEDRVSALTKAKLRLEQQVEDLEcSLEQE-KKLRMDTERAKRKLEGDLKLTQESVADAAQD 1121
Cdd:COG3206 321 -----ELEALQAREASLQAQLAQLEARLAELP-ELEAElRRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1705-1948 |
7.04e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 7.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1705 GRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGER--SRRLA-------EQELLEATERLNllhsqntgllnq 1775
Cdd:PRK04863 780 GRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRfiGSHLAvafeadpEAELRQLNRRRV------------ 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1776 kkKLEADLAQLsgevEEAAQERREAEEKAKKAITDaammaeeLKKEQDTSAHLERmkKTLEQTVRELQARLEEAEQAAL- 1854
Cdd:PRK04863 848 --ELERALADH----ESQEQQQRSQLEQAKEGLSA-------LNRLLPRLNLLAD--ETLADRVEEIREQLDEAEEAKRf 912
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1855 --RGGKK--QVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAY--------QAEEDRKNLARMQDLVDKLQS 1922
Cdd:PRK04863 913 vqQHGNAlaQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEvvqrrahfSYEDAAEMLAKNSDLNEKLRQ 992
|
250 260
....*....|....*....|....*.
gi 578836100 1923 KVKSYKRQFEEAEQQANTNLAKYRKA 1948
Cdd:PRK04863 993 RLEQAEQERTRAREQLRQAQAQLAQY 1018
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1217-1933 |
7.30e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 51.38 E-value: 7.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1217 EAELGRLRRELEEaalrHEATVAALRRKQAEGAAELGEQVDSLQ-RVRQKLEKEKSELRMEVDDLAANVETLTRAKASAe 1295
Cdd:pfam12128 257 ELRLSHLHFGYKS----DETLIASRQEERQETSAELNQLLRTLDdQWKEKRDELNGELSAADAAVAKDRSELEALEDQH- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1296 klcRTYEDQ-LSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLS-RGKALAAQSLEELRRQLEEESK 1373
Cdd:pfam12128 332 ---GAFLDAdIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKeQNNRDIAGIKDKLAKIREARDR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1374 AKSALAHAVQALrhdCDLLREQHEEEAEAQAELQRLLSKANAEVaqwrsKYEADAIQRTEELEEAKKKLALRLQEAEEGV 1453
Cdd:pfam12128 409 QLAVAEDDLQAL---ESELREQLEAGKLEFNEEEYRLKSRLGEL-----KLRLNQATATPELLLQLENFDERIERAREEQ 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1454 EAANAKCSSLEKAKLRLQTESEDVTLELERATsaAAALDKKQRHLERALEERRRQEEEMQRELEAAQ--RESRG--LGTE 1529
Cdd:pfam12128 481 EAANAEVERLQSELRQARKRRDQASEALRQAS--RRLEERQSALDELELQLFPQAGTLLHFLRKEAPdwEQSIGkvISPE 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1530 LFRLRHGHEEALEAleTLKRENK----NLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQaaleeaegaleleet 1605
Cdd:pfam12128 559 LLHRTDLDPEVWDG--SVGGELNlygvKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQA--------------- 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1606 ktlRIQLELSQVKAEVDR-KLAEKDEECA--NLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHAT 1682
Cdd:pfam12128 622 ---AAEEQLVQANGELEKaSREETFARTAlkNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKH 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1683 RQATEAQAATRLmQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELraaleQGERSRRLAEQELLEATErl 1762
Cdd:pfam12128 699 QAWLEEQKEQKR-EARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKAL-----ETWYKRDLASLGVDPDVI-- 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1763 nllhsqntgllnqkKKLEADLAQLSGEVEEAAQERREAEEKAKkaitdaaMMAEELKKEQDtsaHLERMKKTLEQTVREL 1842
Cdd:pfam12128 771 --------------AKLKREIRTLERKIERIAVRRQEVLRYFD-------WYQETWLQRRP---RLATQLSNIERAISEL 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1843 QARLEEAEQAAlrggKKQVQKLEakvRELEAeLDAEQKKHAEALKGVRKHERRVKELA--YQAEEDRKNLARMQDLVDKL 1920
Cdd:pfam12128 827 QQQLARLIADT----KLRRAKLE---MERKA-SEKQQVRLSENLRGLRCEMSKLATLKedANSEQAQGSIGERLAQLEDL 898
|
730
....*....|...
gi 578836100 1921 QSKVKSYKRQFEE 1933
Cdd:pfam12128 899 KLKRDYLSESVKK 911
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1798-1939 |
8.94e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.55 E-value: 8.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1798 REAEEKAKKAITDAAMMAEELKKEQDTSA--HLERMKKTLEQTVRE-------LQARLEEAEQA---ALRGGKKQVQKLE 1865
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAkeEIHKLRNEFEKELRErrnelqkLEKRLLQKEENldrKLELLEKREEELE 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578836100 1866 AKVRELEAELDAEQKKHAEALKGVRKHERRVKELA-YQAEEDRKNLarMQDLVDKLQSKVKSYKRQFE-EAEQQAN 1939
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEELIEEQLQELERISgLTAEEAKEIL--LEKVEEEARHEAAVLIKEIEeEAKEEAD 187
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1678-1905 |
1.01e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1678 LGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLA--AELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQEL 1755
Cdd:COG3883 2 LALALAAPTPAFADPQIQAKQKELSELQAELEAAQAelDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1756 LEATERLN------------------LLHSQNTG-LLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKaitdaammAE 1816
Cdd:COG3883 82 EERREELGeraralyrsggsvsyldvLLGSESFSdFLDRLSALSKIADADADLLEELKADKAELEAKKAE--------LE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1817 ELKKEqdtsahLERMKKTLEQTVRELQARLEEAeQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRV 1896
Cdd:COG3883 154 AKLAE------LEALKAELEAAKAELEAQQAEQ-EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
....*....
gi 578836100 1897 KELAYQAEE 1905
Cdd:COG3883 227 AAAAAAAAA 235
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
889-1148 |
1.20e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 889 LRSAQAEEELAALRA--ELRGLRGALAAAEAKRQEleethvsitqEKNDLALQlQAEQdnLADAEERCHLLIKSKVQLEG 966
Cdd:PTZ00121 1539 AKKAEEKKKADELKKaeELKKAEEKKKAEEAKKAE----------EDKNMALR-KAEE--AKKAEEARIEEVMKLYEEEK 1605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 967 KVKELSERLEDEEEVNADlaaRRRKLEDECTELKKDIDDLELTLAKAEKEKQATE-NKVKnlTEEMAALDESVARLTKEK 1045
Cdd:PTZ00121 1606 KMKAEEAKKAEEAKIKAE---ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEeNKIK--AAEEAKKAEEDKKKAEEA 1680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1046 KALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDK--Q 1123
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKkiA 1760
|
250 260
....*....|....*....|....*
gi 578836100 1124 QLEEKLKKKDSELSQLSLRVEDEQL 1148
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1526-1871 |
1.26e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.89 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1526 LGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALegekseiqaaleeaegaleleET 1605
Cdd:pfam07888 85 LKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTL---------------------TQ 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1606 KTLRIQLELSQVKAEVDRKLAEKDEEcanlrrnhQRAVESLQASLDAetrARNEALRLKKKMEGDLNDLELQLGHATR-Q 1684
Cdd:pfam07888 144 RVLERETELERMKERAKKAGAQRKEE--------EAERKQLQAKLQQ---TEEELRSLSKEFQELRNSLAQRDTQVLQlQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1685 ATEAQAATRLMQAQLKEEQAGRDEEQrlAAELHEQAQALERRASLLAAELEEL------------RAALEQGERSRRLAE 1752
Cdd:pfam07888 213 DTITTLTQKLTTAHRKEAENEALLEE--LRSLQERLNASERKVEGLGEELSSMaaqrdrtqaelhQARLQAAQLTLQLAD 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1753 QELLEATERLNlLHSQNTGLLNQKKKLEADLAQLSGEV---EEAAQERREAEEKAKKaitdaammaeELKKEQDTSahle 1829
Cdd:pfam07888 291 ASLALREGRAR-WAQERETLQQSAEADKDRIEKLSAELqrlEERLQEERMEREKLEV----------ELGREKDCN---- 355
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 578836100 1830 rmKKTLEQTVRELQARleeaeQAALRGGKKQVQKLEAKVREL 1871
Cdd:pfam07888 356 --RVQLSESRRELQEL-----KASLRVAQKEKEQLQAEKQEL 390
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
891-1073 |
1.45e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 891 SAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERchlLIKSKVQLEGKVKE 970
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE---IAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 971 LSERL------------------------------------EDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAE 1014
Cdd:COG3883 88 LGERAralyrsggsvsyldvllgsesfsdfldrlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578836100 1015 KEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAK 1073
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
927-1448 |
1.63e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.11 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 927 VSITQEKN---DLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDI 1003
Cdd:pfam05483 247 IQITEKENkmkDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1004 DDLeltlaKAEKEKQATE-NKVKN----LTEEMAALDESVARLTKEKKALQEAHQQALG----DLQAEEDRVSALTKAKL 1074
Cdd:pfam05483 327 CQL-----TEEKEAQMEElNKAKAahsfVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEEMTKFKN 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1075 RLEQQVEDLECSLEQEKKLrMDTERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKkkdselSQLSLRVEDEQLLGAQMQ 1154
Cdd:pfam05483 402 NKEVELEELKKILAEDEKL-LDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLE------IQLTAIKTSEEHYLKEVE 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1155 KKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGCRK----REAELgRLRRELE-- 1228
Cdd:pfam05483 475 DLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQienlEEKEM-NLRDELEsv 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1229 -EAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASAEKLCRTYEDQLSE 1307
Cdd:pfam05483 554 rEEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNA 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1308 AKIKVEELQRQLADASTQRGRLQT---ESGELSRLLEEKecLISQLSRGKALAAQSLEELRRQLEEESKAKSALAHAVQA 1384
Cdd:pfam05483 634 YEIKVNKLELELASAKQKFEEIIDnyqKEIEDKKISEEK--LLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEK 711
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578836100 1385 LRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELE---EAKKKLALRLQE 1448
Cdd:pfam05483 712 HKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEiekEEKEKLKMEAKE 778
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
892-1971 |
1.74e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 50.21 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 892 AQAEEELAALRAELRGLrgalaAAEAKRQELEETHVSITQEKndlALQLQAEqdnlADAEErchLLIKSKVQLEgKVKEL 971
Cdd:NF041483 174 AEAEQALAAARAEAERL-----AEEARQRLGSEAESARAEAE---AILRRAR----KDAER---LLNAASTQAQ-EATDH 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 972 SERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEK---QATENKVKNLTEEMAALD-------ESVARL 1041
Cdd:NF041483 238 AEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAEKvvaEAKEAAAKQLASAESANEqrtrtakEEIARL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1042 ----TKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQvedlECSLEQEKKLRMDTERAKRKLEGDLKLTQESVAD 1117
Cdd:NF041483 318 vgeaTKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAA----EDTAAQLAKAARTAEEVLTKASEDAKATTRAAAE 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1118 AAqdkqqlEEKLKKKDSELSQLSLRVED--EQLLGA------QMQKKIKELQARAEELE-EELEAERAARARVEKQRAEA 1188
Cdd:NF041483 394 EA------ERIRREAEAEADRLRGEAADqaEQLKGAakddtkEYRAKTVELQEEARRLRgEAEQLRAEAVAEGERIRGEA 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1189 ARELEELSERLEEA-----GGASAGQREGCRKREAELGRLRRELEEAA--LRHEATvAALRRKQAEGAAELGEQVDSLQR 1261
Cdd:NF041483 468 RREAVQQIEEAARTaeellTKAKADADELRSTATAESERVRTEAIERAttLRRQAE-ETLERTRAEAERLRAEAEEQAEE 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1262 VRQKLEKEKSELRMEVDDLAAN-----VETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTqrgRLQTESGEL 1336
Cdd:NF041483 547 VRAAAERAARELREETERAIAArqaeaAEELTRLHTEAEERLTAAEEALADARAEAERIRREAAEETE---RLRTEAAER 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1337 SRLLEEKECLISQLSRGKALAAQSleelrrqleeeskAKSALAHAVqALRHDCDLLREQHEEEAEAQAELQRLlsKANAE 1416
Cdd:NF041483 624 IRTLQAQAEQEAERLRTEAAADAS-------------AARAEGENV-AVRLRSEAAAEAERLKSEAQESADRV--RAEAA 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1417 VAQWRSKYEAdaiqrTEELEEAKKKLALRLQEAEEGVEAANAKCSSlEKAKLRLQTEsedvtlelERATSAAAALDKKQR 1496
Cdd:NF041483 688 AAAERVGTEA-----AEALAAAQEEAARRRREAEETLGSARAEADQ-ERERAREQSE--------ELLASARKRVEEAQA 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1497 HLERALEERRRQEEEMQRELEAAQRESRGLGTELfrlrhgHEEAlealetlkrenknlQEEISDLTDQVSLSGksiqelE 1576
Cdd:NF041483 754 EAQRLVEEADRRATELVSAAEQTAQQVRDSVAGL------QEQA--------------EEEIAGLRSAAEHAA------E 807
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1577 KTKKALEGEKSEIQAALEEAEGALELEETKTLR-IQLELSQVKAEVDRKLAEKDEECANLR--------RNHQRAVESLQ 1647
Cdd:NF041483 808 RTRTEAQEEADRVRSDAYAERERASEDANRLRReAQEETEAAKALAERTVSEAIAEAERLRsdaseyaqRVRTEASDTLA 887
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1648 ASLDAETRARNEALRLKKKMEGDL-NDLELQLGHATRQATEAQAATRLMQAQLKEEqaGRDEEQRLAAELHEQAQALERR 1726
Cdd:NF041483 888 SAEQDAARTRADAREDANRIRSDAaAQADRLIGEATSEAERLTAEARAEAERLRDE--ARAEAERVRADAAAQAEQLIAE 965
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1727 ASllaAELEELRA--------ALEQGERSRRLAEQELLEATERLNLLHSQntgllnqkKKLEADlAQLSGEVEEAAQERR 1798
Cdd:NF041483 966 AT---GEAERLRAeaaetvgsAQQHAERIRTEAERVKAEAAAEAERLRTE--------AREEAD-RTLDEARKDANKRRS 1033
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1799 EAEEKAKKAITDAAMMAEELKKEQDTSAhLERMKKTLEQTVRELQARLEEAEQ---AALRGGKKQVQKLEAKVREL--EA 1873
Cdd:NF041483 1034 EAAEQADTLITEAAAEADQLTAKAQEEA-LRTTTEAEAQADTMVGAARKEAERivaEATVEGNSLVEKARTDADELlvGA 1112
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1874 ELDAEQ-KKHAEALKgvRKHERRVKELAYQAEedRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANT------------ 1940
Cdd:NF041483 1113 RRDATAiRERAEELR--DRITGEIEELHERAR--RESAEQMKSAGERCDALVKAAEEQLAEAEAKAKElvsdanseaskv 1188
|
1130 1140 1150
....*....|....*....|....*....|.
gi 578836100 1941 NLAKYRKAQHELDDAEERADMAETQANKLRA 1971
Cdd:NF041483 1189 RIAAVKKAEGLLKEAEQKKAELVREAEKIKA 1219
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1671-1945 |
1.92e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.91 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1671 LNDLELQLGHATRQATEAQAATRLMQAQLKE--EQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQgersr 1748
Cdd:PRK11281 17 FLLLCLSSAFARAASNGDLPTEADVQAQLDAlnKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQ----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1749 rlAEQELLEATERLNLLHSQNTGLLNQK------KKLEADLAQLSGEVEEAAQERREAE----------EKAKKAITDAA 1812
Cdd:PRK11281 92 --APAKLRQAQAELEALKDDNDEETRETlstlslRQLESRLAQTLDQLQNAQNDLAEYNsqlvslqtqpERAQAALYANS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1813 MMAEELKKEqdtsahLERMKKTLEQTVRELQARLeEAEQAALRGGKKQVQKLEAKVRELeaeLDAEQKKHAEALKGVRKH 1892
Cdd:PRK11281 170 QRLQQIRNL------LKGGKVGGKALRPSQRVLL-QAEQALLNAQNDLQRKSLEGNTQL---QDLLQKQRDYLTARIQRL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 578836100 1893 ERRVKELayQAEEDRKNLARMQDLVDKLQSKVKSYKRQ---FEEAEQQANTNLAKY 1945
Cdd:PRK11281 240 EHQLQLL--QEAINSKRLTLSEKTVQEAQSQDEAARIQanpLVAQELEINLQLSQR 293
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1789-1966 |
2.07e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.56 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1789 EVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEE----AEQAALRGGKKQVQKL 1864
Cdd:pfam15709 349 EVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERkqrlQLQAAQERARQQQEEF 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1865 EAKVRELeaeldaEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQdlvdklQSKVKSYKRQFEEAEQqantnlak 1944
Cdd:pfam15709 429 RRKLQEL------QRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMA------EEERLEYQRQKQEAEE-------- 488
|
170 180
....*....|....*....|..
gi 578836100 1945 yrKAQHElddAEERADMAETQA 1966
Cdd:pfam15709 489 --KARLE---AEERRQKEEEAA 505
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
916-1161 |
2.07e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.63 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 916 EAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLEDEEEVNADLAARRRKLEDE 995
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 996 CTELKKDIDDLELTLAKAEKEKQATE-------NKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSA 1068
Cdd:TIGR04523 112 IKNDKEQKNKLEVELNKLEKQKKENKknidkflTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1069 LTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRK---LEGDLKLTQesvadaaQDKQQLEEKLKKKDSELSQLSLRVED 1145
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQnnqLKDNIEKKQ-------QEINEKTTEISNTQTQLNQLKDEQNK 264
|
250
....*....|....*.
gi 578836100 1146 EQllgAQMQKKIKELQ 1161
Cdd:TIGR04523 265 IK---KQLSEKQKELE 277
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
890-1701 |
2.15e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.58 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 890 RSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVS----ITQEKNDLALQLQAEQDNLADAEERCHLLIkskvQLE 965
Cdd:TIGR00618 98 RSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLkldyKTFTRVVLLPQGEFAQFLKAKSKEKKELLM----NLF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 966 GKvkELSERLEDEEEVNADLAARRRKLEDECTELKKDidDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEK 1045
Cdd:TIGR00618 174 PL--DQYTQLALMEFAKKKSLHGKAELLTLRSQLLTL--CTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1046 KALQEAH--QQALGDLQAEEDRVSALTKaklRLEQQVEdlecsleqekklRMDTERAKRKLEGDLKLTQESVADAAQDKQ 1123
Cdd:TIGR00618 250 EAQEEQLkkQQLLKQLRARIEELRAQEA---VLEETQE------------RINRARKAAPLAAHIKAVTQIEQQAQRIHT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1124 QLEEKLKKKDSELSQLSLRVEDEQLLGAQmQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELeelserleeag 1203
Cdd:TIGR00618 315 ELQSKMRSRAKLLMKRAAHVKQQSSIEEQ-RRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIH----------- 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1204 gASAGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAAN 1283
Cdd:TIGR00618 383 -TLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHL 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1284 VETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTES-----GELSRLLEEKECLISQLSRGKALAA 1358
Cdd:TIGR00618 462 QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIhpnpaRQDIDNPGPLTRRMQRGEQTYAQLE 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1359 QSLEELRRQLEEESKAKSALAHAVQALRHDCDLLreqheeeaeaqaELQRLLSKANAEVAQwrsKYEADAIQRTEELEEA 1438
Cdd:TIGR00618 542 TSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIL------------TQCDNRSKEDIPNLQ---NITVRLQDLTEKLSEA 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1439 KKKLALRLQEAEEGVEAANAKcssLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERA-LEERRRQEEEMQRELE 1517
Cdd:TIGR00618 607 EDMLACEQHALLRKLQPEQDL---QDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSiRVLPKELLASRQLALQ 683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1518 AAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQE-------EISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQ 1590
Cdd:TIGR00618 684 KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEienasssLGSDLAAREDALNQSLKELMHQARTVLKARTEAH 763
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1591 AALEEAEGALELEETKTLRIQLELS---QVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKM 1667
Cdd:TIGR00618 764 FNNNEEVTAALQTGAELSHLAAEIQffnRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSAT 843
|
810 820 830
....*....|....*....|....*....|....
gi 578836100 1668 EGDLNDLELQLGHATRQATEAQAATRLMQAQLKE 1701
Cdd:TIGR00618 844 LGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
895-1360 |
2.44e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.73 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 895 EEELAALRAELRGLRGALAAAEAKR--QELEETHVSIT---QEKNDLALQLQAEQDNLADAEErchlliKSKVQLEGKVK 969
Cdd:pfam15921 244 EDQLEALKSESQNKIELLLQQHQDRieQLISEHEVEITgltEKASSARSQANSIQSQLEIIQE------QARNQNSMYMR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 970 ELSERLEDEEEVNADLAARRRKLEDECTELKKD--IDDLELTLAKAEKEKQATENkvKNLTEEMAALdesVARLTKEKKA 1047
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQLQKL---LADLHKREKE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1048 LQEAHQQ--------------------ALGDLQAEEDRVSALTKA-----KLRLEQQVEDLEC---SLEQEKKLRMDTER 1099
Cdd:pfam15921 393 LSLEKEQnkrlwdrdtgnsitidhlrrELDDRNMEVQRLEALLKAmksecQGQMERQMAAIQGkneSLEKVSSLTAQLES 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1100 AK---RKLEGDL---KLTQES----VADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEE 1169
Cdd:pfam15921 473 TKemlRKVVEELtakKMTLESsertVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEA 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1170 ELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREgcrkREAELGRLRRELEEAALRHEATVAALRRKQAEGA 1249
Cdd:pfam15921 553 LKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQ----LEKEINDRRLELQEFKILKDKKDAKIRELEARVS 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1250 AELGEQVDSLQRVRQKLEKEKsELRMEVDDLAANVET----LTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQ 1325
Cdd:pfam15921 629 DLELEKVKLVNAGSERLRAVK-DIKQERDQLLNEVKTsrneLNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSE 707
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 578836100 1326 ----RGRLQTESGELSRLLEEKECLISQLS--RGKALAAQS 1360
Cdd:pfam15921 708 leqtRNTLKSMEGSDGHAMKVAMGMQKQITakRGQIDALQS 748
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1751-1967 |
2.54e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1751 AEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLER 1830
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1831 MK--KTLEQTVRELQA--RLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEED 1906
Cdd:COG3883 108 LLgsESFSDFLDRLSAlsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578836100 1907 RKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQAN 1967
Cdd:COG3883 188 SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
822-1344 |
2.60e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.33 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 822 LEELRDQRLAK--VLTLLQAR--SRGRLMRLEYQRLLGGRDALFTIQWNIRafnavKNWSWMKlffKMKPLLRSAQAE-E 896
Cdd:pfam05483 337 MEELNKAKAAHsfVVTEFEATtcSLEELLRTEQQRLEKNEDQLKIITMELQ-----KKSSELE---EMTKFKNNKEVElE 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 897 ELAALRAELRGLRGALAAAEAKRQELEEThvsitqeKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLE 976
Cdd:pfam05483 409 ELKKILAEDEKLLDEKKQFEKIAEELKGK-------EQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 977 DEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQAL 1056
Cdd:pfam05483 482 KEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKG 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1057 GDLQAEEDRVsaltkaklrlEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKKDSEL 1136
Cdd:pfam05483 562 DEVKCKLDKS----------EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQL 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1137 SQLSLRVEDEQLLGAQMQKKIKEL-QARAEELEEELEAERAARARVEKQRAEAareleelserleeaggasagqregcrk 1215
Cdd:pfam05483 632 NAYEIKVNKLELELASAKQKFEEIiDNYQKEIEDKKISEEKLLEEVEKAKAIA--------------------------- 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1216 reAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVddlaanvetltrakasae 1295
Cdd:pfam05483 685 --DEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAAL------------------ 744
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 578836100 1296 klcrtyEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKE 1344
Cdd:pfam05483 745 ------EIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
949-1121 |
2.79e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 949 DAEERCHLLIKSKVQLEGKVKELSERLEDEEEVNADLAARRRKL----------------EDECTELKKDIDDLELT--- 1009
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdeidvasaEREIAELEAELERLDASsdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1010 LAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKL--RLEQQVEDlecsl 1087
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLeeRFAAALGD----- 761
|
170 180 190
....*....|....*....|....*....|....
gi 578836100 1088 EQEKKLRMDTERAKRKLEGDLKLTQESVADAAQD 1121
Cdd:COG4913 762 AVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1538-1975 |
2.84e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.25 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1538 EEALEALETLKRENKNLQ----EEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQLE 1613
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIdkflTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1614 LSQVKA--EVDRKLAEKDEECANLRRNHQRAVESLQAsldaetrarnealrlkkkmegDLNDLELQLGHATRQATEAQAA 1691
Cdd:TIGR04523 203 LSNLKKkiQKNKSLESQISELKKQNNQLKDNIEKKQQ---------------------EINEKTTEISNTQTQLNQLKDE 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1692 TRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELE-----ELRAALEQGERSRRLAEQELLEATERLNLLH 1766
Cdd:TIGR04523 262 QNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLN 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1767 SQNTGLLNQKKKLEADLAQLsgeveeaaqeRREAEEKAKKAitdaammaEELKKEQDTsaHLERMKKtLEQTVRELQARL 1846
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEK----------QRELEEKQNEI--------EKLKKENQS--YKQEIKN-LESQINDLESKI 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1847 EEAEqaalrggkKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKS 1926
Cdd:TIGR04523 401 QNQE--------KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV 472
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 578836100 1927 YKRQfeeaeqqantnlakYRKAQHELDDAEERADMAETQANKLRARTRD 1975
Cdd:TIGR04523 473 LSRS--------------INKIKQNLEQKQKELKSKEKELKKLNEEKKE 507
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1547-1934 |
4.48e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1547 LKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAAleeaegaleleetktlriqlelsqvKAEVDRKLA 1626
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESE-------------------------NSEKQRELE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1627 EKDEECANLRRNHQRAVESLQasldaetrarnealrlkkKMEGDLNDLELQLGHATRQATEAQAATRLMQA--QLKEEQA 1704
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEIK------------------NLESQINDLESKIQNQEKLNQQKDEQIKKLQQekELLEKEI 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1705 GRDEEQRLAA-----ELHEQAQALE-------RRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGL 1772
Cdd:TIGR04523 429 ERLKETIIKNnseikDLTNQDSVKEliiknldNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1773 LNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQdtsahlermkktLEQTVRELQARLEEAEQA 1852
Cdd:TIGR04523 509 EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN------------LEKEIDEKNKEIEELKQT 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1853 ALRGGKKQVQKlEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFE 1932
Cdd:TIGR04523 577 QKSLKKKQEEK-QELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIK 655
|
..
gi 578836100 1933 EA 1934
Cdd:TIGR04523 656 EI 657
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1694-1904 |
4.51e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.04 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1694 LMQAQLKEEQAGRDEE-QRLAAELHEQAQ--ALERRASL-LAAELEELRAALEQGErsrrlAEQElleaterlnllhsqn 1769
Cdd:PRK09039 39 VAQFFLSREISGKDSAlDRLNSQIAELADllSLERQGNQdLQDSVANLRASLSAAE-----AERS--------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1770 tgllnqkkKLEADLAQLSGEVEEAAQerreaeekakkaitDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLeEA 1849
Cdd:PRK09039 99 --------RLQALLAELAGAGAAAEG--------------RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQL-AA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578836100 1850 EQAALRGGKKQVQKLEAKVRELEAELDAeqkkhaeALKgvrkheRRVKELA-YQAE 1904
Cdd:PRK09039 156 LEAALDASEKRDRESQAKIADLGRRLNV-------ALA------QRVQELNrYRSE 198
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
887-1161 |
4.61e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.80 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 887 PLLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQ----------------EKNDLALQLQAEQDNLADA 950
Cdd:COG3096 776 PLFGRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvgghlavafapdpeaELAALRQRRSELERELAQH 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 951 EERCHLL------IKSKVQLEGKV---------KELSERLED-EEEVNADLAARR---------RKLEDECTELKKD--- 1002
Cdd:COG3096 856 RAQEQQLrqqldqLKEQLQLLNKLlpqanlladETLADRLEElREELDAAQEAQAfiqqhgkalAQLEPLVAVLQSDpeq 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1003 IDDLELTLAKAEKEKQATENKVKNLTEEMA-----ALDESVARLTkEKKALQEAHQQALgdLQAEEDRvsalTKAKLRLE 1077
Cdd:COG3096 936 FEQLQADYLQAKEQQRRLKQQIFALSEVVQrrphfSYEDAVGLLG-ENSDLNEKLRARL--EQAEEAR----REAREQLR 1008
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1078 QQVEDLECSLE--------QEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKKDSELSQLS---LRVEDE 1146
Cdd:COG3096 1009 QAQAQYSQYNQvlaslkssRDAKQQTLQELEQELEELGVQADAEAEERARIRRDELHEELSQNRSRRSQLEkqlTRCEAE 1088
|
330
....*....|....*
gi 578836100 1147 QllgAQMQKKIKELQ 1161
Cdd:COG3096 1089 M---DSLQKRLRKAE 1100
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1463-1962 |
4.63e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.81 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1463 LEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAA------QRESRGLGTELFRLRH- 1535
Cdd:TIGR00618 196 AELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQeeqlkkQQLLKQLRARIEELRAq 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1536 --GHEEALEALEtLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEET-KTLRIQL 1612
Cdd:TIGR00618 276 eaVLEETQERIN-RARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLlQTLHSQE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1613 ELSQVKAEVDRK-LAEKDEECANLRRNHQRA-------------------VESLQASLDAETRARN----EALRLKKKME 1668
Cdd:TIGR00618 355 IHIRDAHEVATSiREISCQQHTLTQHIHTLQqqkttltqklqslckeldiLQREQATIDTRTSAFRdlqgQLAHAKKQQE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1669 GDLNDLELQLGHATRQATEAQAATRLMQaqlKEEQAGRDEEQRLAAELHEQAQALERRAsllaaelEELRAALEQGERSR 1748
Cdd:TIGR00618 435 LQQRYAELCAAAITCTAQCEKLEKIHLQ---ESAQSLKEREQQLQTKEQIHLQETRKKA-------VVLARLLELQEEPC 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1749 RLAEQELLEATERLNLLHSQNT-----GLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMA-------- 1815
Cdd:TIGR00618 505 PLCGSCIHPNPARQDIDNPGPLtrrmqRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTqcdnrske 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1816 ---------EELKKEQDTSAHLERMKKTLEQT-VRELQARLEEAEQAALRGGKKQVQKLE--AKVRELEAELDAEQKKHA 1883
Cdd:TIGR00618 585 dipnlqnitVRLQDLTEKLSEAEDMLACEQHAlLRKLQPEQDLQDVRLHLQQCSQELALKltALHALQLTLTQERVREHA 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1884 EALKGVRKHERRVKELAYQAEE--------DRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRK----AQHE 1951
Cdd:TIGR00618 665 LSIRVLPKELLASRQLALQKMQsekeqltyWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAredaLNQS 744
|
570
....*....|.
gi 578836100 1952 LDDAEERADMA 1962
Cdd:TIGR00618 745 LKELMHQARTV 755
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1612-1907 |
4.86e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 48.47 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1612 LELSQVKAEVDRKLAE--------KDEECANLRRNHQRAVESLQASLDAETRaRNEALRLKKKMEGDLNDLELQLGHATR 1683
Cdd:NF033838 135 LEPGKKVAEATKKVEEaekkakdqKEEDRRNYPTNTYKTLELEIAESDVEVK-KAELELVKEEAKEPRDEEKIKQAKAKV 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1684 QATEAQAaTRLMQAQLKEEQAGRDEEQRLAAELHEQAqalerrasllaaelEELRAALEQGE---RSRRLAEQELLEATE 1760
Cdd:NF033838 214 ESKKAEA-TRLEKIKTDREKAEEEAKRRADAKLKEAV--------------EKNVATSEQDKpkrRAKRGVLGEPATPDK 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1761 RLNLLHSQNTGLlnQKKKLEADLAQLSGEVEEAAQERREAEEKAKKaitdaammaeelKKEQDTSAHLERMKKTLEQTVR 1840
Cdd:NF033838 279 KENDAKSSDSSV--GEETLPSPSLKPEKKVAEAEKKVEEAKKKAKD------------QKEEDRRNYPTNTYKTLELEIA 344
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578836100 1841 ELQARLEEAEQAALRGGKKQVQKlEAKVRELEAELDAeqkKHAEA--LKGVRKHERRVKELAYQ--AEEDR 1907
Cdd:NF033838 345 ESDVKVKEAELELVKEEAKEPRN-EEKIKQAKAKVES---KKAEAtrLEKIKTDRKKAEEEAKRkaAEEDK 411
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1782-1978 |
4.94e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.92 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1782 DLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQdtSAHLERMKKTLEQTVRELQARleEAEQAALRGGKKQV 1861
Cdd:TIGR02794 44 DPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQR--AAEQARQKELEQRAAAEKAAK--QAEQAAKQAEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1862 QKLEAKVRELeaeldAEQKKHAEALKGVRKHErrvkELAYQAEEDRKN-----------LARMQDLVDKLQSKVKSYKRQ 1930
Cdd:TIGR02794 120 QAEEAKAKQA-----AEAKAKAEAEAERKAKE----EAAKQAEEEAKAkaaaeakkkaeEAKKKAEAEAKAKAEAEAKAK 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 578836100 1931 FEEAEQQANTNLAKYRKAQHELDDAE-ERADMAETQANKLRARTRDALG 1978
Cdd:TIGR02794 191 AEEAKAKAEAAKAKAAAEAAAKAEAEaAAAAAAEAERKADEAELGDIFG 239
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1684-1881 |
5.23e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 46.95 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1684 QATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQ----ALERRASLLA---AELEELRAALEQGERSRRLAEQELL 1756
Cdd:pfam00261 9 ELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQlleeELERTEERLAealEKLEEAEKAADESERGRKVLENRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1757 EATERLNLLHSQntglLNQKKKLEADLAQLSGEVEE----AAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLE--- 1829
Cdd:pfam00261 89 KDEEKMEILEAQ----LKEAKEIAEEADRKYEEVARklvvVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEase 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578836100 1830 ----RMKKTLEQTVRELQARLEEAEQAAlRGGKKQVQKLEAKVRELEAELDAEQKK 1881
Cdd:pfam00261 165 ekasEREDKYEEQIRFLTEKLKEAETRA-EFAERSVQKLEKEVDRLEDELEAEKEK 219
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1620-1821 |
5.87e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 48.02 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1620 EVDRKLAEKdEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDlndlelqlghaTRQATEAQAATRLMQAQL 1699
Cdd:pfam15709 349 EVERKRREQ-EEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEE-----------ERQRQEEEERKQRLQLQA 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1700 KEEQAGRDEEqrlaaELHEQAQALERRAsllaaELEELRAALEQGERSRRLAEQeLLEATERLNLLHSQNTGLLNQKKKL 1779
Cdd:pfam15709 417 AQERARQQQE-----EFRRKLQELQRKK-----QQEEAERAEAEKQRQKELEMQ-LAEEQKRLMEMAEEERLEYQRQKQE 485
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 578836100 1780 EADLAQLsgeveEAAQERREAEEKAKKAITDAAMMAEELKKE 1821
Cdd:pfam15709 486 AEEKARL-----EAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1552-1977 |
5.91e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.50 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1552 KNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQLELSQVKAEVDRKLA--EKD 1629
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNdiEEQ 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1630 EECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNdlELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEE 1709
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAA--KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELN 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1710 QRLAAELHEQAQALERRASLLAAELEELRAALeqgERSRRLAEQELLEATErlnlLHSQNTGLLNQKKKLEADLAQLSGE 1789
Cdd:TIGR00606 849 RKLIQDQQEQIQHLKSKTNELKSEKLQIGTNL---QRRQQFEEQLVELSTE----VQSLIREIKDAKEQDSPLETFLEKD 921
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1790 VEEAAQERREAEEKAKKAITDAAMMAEELKK--------EQDTSAHLERMKKTLEQTVRELQARLEEAEQaalrggkkQV 1861
Cdd:TIGR00606 922 QQEKEELISSKETSNKKAQDKVNDIKEKVKNihgymkdiENKIQDGKDDYLKQKETELNTVNAQLEECEK--------HQ 993
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1862 QKLEAKVRELEAELDAeQKKHAEALKG---VRKHERRVKELAYQAEEDRKNLARMQdlvdKLQSKVKSYKRQFEEAEQQA 1938
Cdd:TIGR00606 994 EKINEDMRLMRQDIDT-QKIQERWLQDnltLRKRENELKEVEEELKQHLKEMGQMQ----VLQMKQEHQKLEENIDLIKR 1068
|
410 420 430
....*....|....*....|....*....|....*....
gi 578836100 1939 NTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDAL 1977
Cdd:TIGR00606 1069 NHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMM 1107
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1643-1853 |
6.59e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1643 VESLQASLDAetrARNEALRLKKKMegDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQA 1722
Cdd:COG3206 184 LPELRKELEE---AEAALEEFRQKN--GLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1723 LERrasllAAELEELRAALEQgersrrlAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREA-- 1800
Cdd:COG3206 259 LLQ-----SPVIQQLRAQLAE-------LEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEAlq 326
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578836100 1801 --EEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAA 1853
Cdd:COG3206 327 arEASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAE 381
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1635-1923 |
6.69e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 47.11 E-value: 6.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1635 LRRNHQRAVESL--QASLDAETRA----RNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDE 1708
Cdd:pfam15905 61 LKKKSQKNLKESkdQKELEKEIRAlvqeRGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNEL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1709 EQRLAAELHEQaqaleRRASLLAAELEELRAALEQGERSRRLAEQEL---LEATERlNLLHSQntgllnqkkkleADLAQ 1785
Cdd:pfam15905 141 LKAKFSEDGTQ-----KKMSSLSMELMKLRNKLEAKMKEVMAKQEGMegkLQVTQK-NLEHSK------------GKVAQ 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1786 LSG---EVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAAlrggKKQVQ 1862
Cdd:pfam15905 203 LEEklvSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQEL----SKQIK 278
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578836100 1863 KLEAKVRELEAELDAEQKKHAEalkgvrKHERRVKELayqaEEDRKNLARMQDLVDKLQSK 1923
Cdd:pfam15905 279 DLNEKCKLLESEKEELLREYEE------KEQTLNAEL----EELKEKLTLEEQEHQKLQQK 329
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1433-1881 |
6.91e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1433 EELEEAKKKLA---LRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQE 1509
Cdd:TIGR04523 314 SELKNQEKKLEeiqNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1510 EEMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGE---- 1585
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQlkvl 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1586 KSEIQAALEEAEGALELEETKTLRIqLELSQVKAEVDRKLAEKDEECANLRRNhQRAVESLQASLDAETRARNEALrLKK 1665
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEKEL-KKLNEEKKELEEKVKDLTKKISSLKEK-IEKLESEKKEKESKISDLEDEL-NKD 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1666 KMEGDLNDLELQLGHATRQATeaqaatrlmqaQLKEEQAGRDEEQRlaaELHEQAQALERRASLLAAELEELRAALEQGE 1745
Cdd:TIGR04523 551 DFELKKENLEKEIDEKNKEIE-----------ELKQTQKSLKKKQE---EKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1746 RSRRLAEQElleaTERLNllhSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKK-EQDT 1824
Cdd:TIGR04523 617 KELEKAKKE----NEKLS---SIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDwLKEL 689
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 578836100 1825 SAHLErmKKTLEQTVRELQARLEEAEqaalrggkKQVQKLEAKVRELEAELDAEQKK 1881
Cdd:TIGR04523 690 SLHYK--KYITRMIRIKDLPKLEEKY--------KEIEKELKKLDEFSKELENIIKN 736
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
958-1296 |
1.11e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.43 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 958 IKSKVQLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLteemaaldes 1037
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI---------- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1038 vaRLTKEKKALQEAHQQalgDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKltqESVAD 1117
Cdd:pfam17380 354 --RQEERKRELERIRQE---EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKV---EMEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1118 AAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSE 1197
Cdd:pfam17380 426 RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERK 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1198 RLEEaggasagqrEGCRKREAelgrLRRELEEaalRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKeKSELRMEV 1277
Cdd:pfam17380 506 QAMI---------EEERKRKL----LEKEMEE---RQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRK-ATEERSRL 568
|
330
....*....|....*....
gi 578836100 1278 DDLAANVETLTRAKASAEK 1296
Cdd:pfam17380 569 EAMEREREMMRQIVESEKA 587
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1542-1853 |
1.12e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 47.26 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1542 EALETLKRENKNLQEEISDLTDQVSLSgKSIQELEKTKKALEGEKseiqaaleeaegaleleetktlriqlELSQVKAEV 1621
Cdd:COG5185 282 ENANNLIKQFENTKEKIAEYTKSIDIK-KATESLEEQLAAAEAEQ--------------------------ELEESKRET 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1622 DRKLAEKDEECANLRRNHQRAVESLQAslDAETRARNEALRLKKKMegdLNDLELQLgHATRQATEAQaatrlMQAQLKE 1701
Cdd:COG5185 335 ETGIQNLTAEIEQGQESLTENLEAIKE--EIENIVGEVELSKSSEE---LDSFKDTI-ESTKESLDEI-----PQNQRGY 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1702 EQagrdeeqrlaaelhEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNllhsqntglLNQKKKLEA 1781
Cdd:COG5185 404 AQ--------------EILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELN---------KVMREADEE 460
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578836100 1782 DLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELK-KEQDTSAHLERMKKTLEQTVRELQARLEEAEQAA 1853
Cdd:COG5185 461 SQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKaTLEKLRAKLERQLEGVRSKLDQVAESLKDFMRAR 533
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
897-1089 |
1.16e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 897 ELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSkvQLEGKVKELSERlE 976
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--LLEERFAAALGD-A 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 977 DEEEVNADLAARRRKLEdecTELKKDIDDLELTLAKAekeKQATENKVKNLTEEMAALDESVARLT------------KE 1044
Cdd:COG4913 763 VERELRENLEERIDALR---ARLNRAEEELERAMRAF---NREWPAETADLDADLESLPEYLALLDrleedglpeyeeRF 836
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 578836100 1045 KKALQEAHQQALGDLQaeedrvSALTKAKLRLEQQVEDLECSLEQ 1089
Cdd:COG4913 837 KELLNENSIEFVADLL------SKLRRAIREIKERIDPLNDSLKR 875
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1782-1952 |
1.26e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1782 DLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAalrggkkqv 1861
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ--------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1862 QKLEAKVRELEA---ELDAEQKKHAEAlkgvrkhERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQA 1938
Cdd:COG1579 82 LGNVRNNKEYEAlqkEIESLKRRISDL-------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
170
....*....|....
gi 578836100 1939 NTNLAKYRKAQHEL 1952
Cdd:COG1579 155 EAELEELEAEREEL 168
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1614-1790 |
1.33e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1614 LSQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRlkKKMEGDLNDLELQLGHATRQATEAQAATR 1693
Cdd:COG3206 217 LLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVI--QQLRAQLAELEAELAELSARYTPNHPDVI 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1694 LMQAQLKE-EQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERsrrlAEQELLEATERLNLLHSQNTGL 1772
Cdd:COG3206 295 ALRAQIAAlRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE----LEAELRRLEREVEVARELYESL 370
|
170
....*....|....*...
gi 578836100 1773 LNQKKKLEADLAQLSGEV 1790
Cdd:COG3206 371 LQRLEEARLAEALTVGNV 388
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
892-1160 |
1.45e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 892 AQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLE------ 965
Cdd:PRK04863 275 MRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEkieryq 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 966 GKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDL--------------------------------------E 1007
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELksqladyqqaldvqqtraiqyqqavqalerakqlcglpD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1008 LTLAKAEKEKQATENKVKNLTEEMAALDE--SVARLTKEK--KALQ------------EAHQQALGDL-QAEEDRVSALT 1070
Cdd:PRK04863 435 LTADNAEDWLEEFQAKEQEATEELLSLEQklSVAQAAHSQfeQAYQlvrkiagevsrsEAWDVARELLrRLREQRHLAEQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1071 KAKLRleQQVEDLECSLEQEKKLrmdtERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLG 1150
Cdd:PRK04863 515 LQQLR--MRLSELEQRLRQQQRA----ERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQL 588
|
330
....*....|
gi 578836100 1151 AQMQKKIKEL 1160
Cdd:PRK04863 589 EQLQARIQRL 598
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1734-1974 |
1.57e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 46.93 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1734 LEELRAALEQGERSRRLAEQELLEATER-----LNLLHSQNTGLLNQK---------KKLEADLAQLSGEVEEAAQERRE 1799
Cdd:NF033838 71 LSEIQKSLDKRKHTQNVALNKKLSDIKTeylyeLNVLKEKSEAELTSKtkkeldaafEQFKKDTLEPGKKVAEATKKVEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1800 AEEKAKKaitdaammaeelKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKlEAKVRELEAELDAEQ 1879
Cdd:NF033838 151 AEKKAKD------------QKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKEEAKEPRD-EEKIKQAKAKVESKK 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1880 KKhAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQF---EEAEQQANTNLAKYR---------- 1946
Cdd:NF033838 218 AE-ATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGvlgEPATPDKKENDAKSSdssvgeetlp 296
|
250 260 270
....*....|....*....|....*....|..
gi 578836100 1947 ----KAQHELDDAEERADMAETQANKLRARTR 1974
Cdd:NF033838 297 spslKPEKKVAEAEKKVEEAKKKAKDQKEEDR 328
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1699-1968 |
1.74e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 46.85 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1699 LKEEQAGRDEEQRLAAELHE-QAQALERRASL--LAAELEELRAALEQGERSRRLAE-------------QELLEATERL 1762
Cdd:PLN03188 938 LEEELASLMHEHKLLKEKYEnHPEVLRTKIELkrVQDELEHYRNFYDMGEREVLLEEiqdlrsqlqyyidSSLPSARKRN 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1763 NLLHSQNTGLLNQKKKLEAdlaqLSGEVEEAAQERREAEE-KAKKAITDAAMMAEELKKEQDTSAHL-ERMKKTLEqTVR 1840
Cdd:PLN03188 1018 SLLKLTYSCEPSQAPPLNT----IPESTDESPEKKLEQERlRWTEAESKWISLAEELRTELDASRALaEKQKHELD-TEK 1092
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1841 ELQARLEEAEQAALRGGKKQVQK----------LEAKVRELEAELDAEQKKHAEAlkGVRKHERR--------VKELAYQ 1902
Cdd:PLN03188 1093 RCAEELKEAMQMAMEGHARMLEQyadleekhiqLLARHRRIQEGIDDVKKAAARA--GVRGAESKfinalaaeISALKVE 1170
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578836100 1903 AEEDRKNLarmQDLVDKLQSKVksykRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANK 1968
Cdd:PLN03188 1171 REKERRYL---RDENKSLQAQL----RDTAEAVQAAGELLVRLKEAEEALTVAQKRAMDAEQEAAE 1229
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
911-1352 |
1.82e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 46.66 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 911 ALAAAEAKRQELEETHvsitQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLEDEEEVNADLAARRR 990
Cdd:pfam05557 32 LEKKASALKRQLDRES----DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 991 KLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQ---------------- 1054
Cdd:pfam05557 108 CLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRikelefeiqsqeqdse 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1055 ALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKlTQESVADAAQDKQQLEEKLK--KK 1132
Cdd:pfam05557 188 IVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEK-YREEAATLELEKEKLEQELQswVK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1133 DSELSQLSLRVEDEqllgaqMQKKIKELQARAEELEEELEAERAARARVEKQRAEAAREleelserleeaggasagqreg 1212
Cdd:pfam05557 267 LAQDTGLNLRSPED------LSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQE--------------------- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1213 CRKREAELGRLRRELEeaalRHEATVAALRR------KQAEGAAELGEQVDS---LQRVRQKLEKEKSELRMEVDDLAAN 1283
Cdd:pfam05557 320 LAQYLKKIEDLNKKLK----RHKALVRRLQRrvllltKERDGYRAILESYDKeltMSNYSPQLLERIEEAEDMTQKMQAH 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578836100 1284 VETLTRAKASAEKLCRTYEDQLS--EAKIKVEELQRQLADASTQ-------RGRLQTESGELSRLLEEKECLISQLSR 1352
Cdd:pfam05557 396 NEEMEAQLSVAEEELGGYKQQAQtlERELQALRQQESLADPSYSkeevdslRRKLETLELERQRLREQKNELEMELER 473
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1410-1852 |
1.85e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 46.56 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1410 LSKANAEVAQWRSKYEADAIQRT---EELEEAKK---KLALRLQEAEegVEAANAKCSSlEKAKLRLQTESEDVT----- 1478
Cdd:pfam05701 44 LEKVQEEIPEYKKQSEAAEAAKAqvlEELESTKRlieELKLNLERAQ--TEEAQAKQDS-ELAKLRVEEMEQGIAdeasv 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1479 -----LELERATSAAAALDKK----------QRHLERALEERRRQEEEMQRELEAAQRESR--GLGTELFRLRHGHEEA- 1540
Cdd:pfam05701 121 aakaqLEVAKARHAAAVAELKsvkeeleslrKEYASLVSERDIAIKRAEEAVSASKEIEKTveELTIELIATKESLESAh 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1541 ---LEALE--------------TLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGALELE 1603
Cdd:pfam05701 201 aahLEAEEhrigaalareqdklNWEKELKQAEEELQRLNQQLLSAKDLKSKLETASALLLDLKAELAAYMESKLKEEADG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1604 ETKTLRIQLELSQVKAEVDRKLAE--------KDEecANLRRNhqrAVESLQASLDAEtRARNEALRLKKKMEG-DLNDL 1674
Cdd:pfam05701 281 EGNEKKTSTSIQAALASAKKELEEvkaniekaKDE--VNCLRV---AAASLRSELEKE-KAELASLRQREGMASiAVSSL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1675 ELQLGHATRQATEAQAAtrlmqaqlkeEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGER-------- 1746
Cdd:pfam05701 355 EAELNRTKSEIALVQAK----------EKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQakaaastv 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1747 -SRRLAEQELLEAT---ERLNLLHSQntGLLNQKKKLEADLAQLSG--------EVEEAAQERREAEEKAKKAITDAAMM 1814
Cdd:pfam05701 425 eSRLEAVLKEIEAAkasEKLALAAIK--ALQESESSAESTNQEDSPrgvtlsleEYYELSKRAHEAEELANKRVAEAVSQ 502
|
490 500 510
....*....|....*....|....*....|....*....
gi 578836100 1815 AEELKKEQDTS-AHLERMKKTLEQTVRELQARLEEAEQA 1852
Cdd:pfam05701 503 IEEAKESELRSlEKLEEVNREMEERKEALKIALEKAEKA 541
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
964-1144 |
1.86e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.74 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 964 LEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTK 1043
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1044 EKKALQE---AHQQALGDLQ---AEEDRV-SALTKAKLRLEQQVEDlecSLEQEKKLRMDTERAKRKLEGDLKLTQESVA 1116
Cdd:pfam10174 423 RVKSLQTdssNTDTALTTLEealSEKERIiERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELTEKESSLI 499
|
170 180
....*....|....*....|....*...
gi 578836100 1117 DAAQDKQQLEEKLKKKDSELSQLSLRVE 1144
Cdd:pfam10174 500 DLKEHASSLASSGLKKDSKLKSLEIAVE 527
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
900-1155 |
2.00e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 46.28 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 900 ALRAELRGLRGALAAAEAKRQELEETHVSITQE-----KNDLALQLQAEQDNLADAEERCHLLIKSKVQLE----GKVKE 970
Cdd:pfam07111 112 AGQAEAEGLRAALAGAEMVRKNLEEGSQRELEEiqrlhQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkraGEAKQ 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 971 LSERLEDEEEVNADLAARRRKLEDECT---ELKKDIDDL---ELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKE 1044
Cdd:pfam07111 192 LAEAQKEAELLRKQLSKTQEELEAQVTlveSLRKYVGEQvppEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVR 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1045 KK------ALQEAHQ----QALGDLQAEEDRvsaltKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQES 1114
Cdd:pfam07111 272 VQslthmlALQEEELtrkiQPSDSLEPEFPK-----KCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQ 346
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 578836100 1115 VADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQK 1155
Cdd:pfam07111 347 VTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQE 387
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
988-1139 |
2.01e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 46.17 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 988 RRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKE----KKALQEAhQQALGDLQAEE 1063
Cdd:pfam05667 329 LQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQykvkKKTLDLL-PDAEENIAKLQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1064 DRVSALTKAKLRLEQQ-----VEDLEcSLEQEKKLRMDTE-RAKRKLEgDLKLTQESVadaaqdkQQLEEKLKKKDSELS 1137
Cdd:pfam05667 408 ALVDASAQRLVELAGQwekhrVPLIE-EYRALKEAKSNKEdESQRKLE-EIKELREKI-------KEVAEEAKQKEELYK 478
|
..
gi 578836100 1138 QL 1139
Cdd:pfam05667 479 QL 480
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1640-1956 |
2.09e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 46.54 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1640 QRAVESLQASLDAETRARNEAL-----RLKKKMEGDLNDLELQLGHATRQATEAQ--AATRLMQAQLKEEQAGRDEEQRL 1712
Cdd:NF033838 68 EKILSEIQKSLDKRKHTQNVALnkklsDIKTEYLYELNVLKEKSEAELTSKTKKEldAAFEQFKKDTLEPGKKVAEATKK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1713 AAELHEQA--QALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERlnllHSQNTGLLNQ-KKKLEADLAQLSgE 1789
Cdd:NF033838 148 VEEAEKKAkdQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKEEAK----EPRDEEKIKQaKAKVESKKAEAT-R 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1790 VEEAAQERREAEEKAKKaiTDAAMMAEELKKEQDTSAHlERMKKTLEQTVRELQARLEEAEQAAlRGGKKQVQKLEAKVR 1869
Cdd:NF033838 223 LEKIKTDREKAEEEAKR--RADAKLKEAVEKNVATSEQ-DKPKRRAKRGVLGEPATPDKKENDA-KSSDSSVGEETLPSP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1870 ELEAEldaeqKKHAEALKGVRKHERRVKElayQAEEDRKNLA--RMQDL---VDKLQSKVKSYKRQF--EEAEQQANTNL 1942
Cdd:NF033838 299 SLKPE-----KKVAEAEKKVEEAKKKAKD---QKEEDRRNYPtnTYKTLeleIAESDVKVKEAELELvkEEAKEPRNEEK 370
|
330
....*....|....
gi 578836100 1943 AKYRKAQHELDDAE 1956
Cdd:NF033838 371 IKQAKAKVESKKAE 384
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
976-1161 |
2.46e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 976 EDEEEVN---ADLAARRRKLEDEctelkkdiddleltLAKAEKEKQATENKVKNLTEEMAALDEsvaRLTKEKKALQEAH 1052
Cdd:PRK00409 513 EDKEKLNeliASLEELERELEQK--------------AEEAEALLKEAEKLKEELEEKKEKLQE---EEDKLLEEAEKEA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1053 QQALGDLQAEEDRVsaltkakLRLEQQVEDLECSLEQEKKLrmdtERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKK 1132
Cdd:PRK00409 576 QQAIKEAKKEADEI-------IKELRQLQKGGYASVKAHEL----IEARKRLNKANEKKEKKKKKQKEKQEELKVGDEVK 644
|
170 180 190
....*....|....*....|....*....|....*.
gi 578836100 1133 DSELSQ----LSLRVEDE---QLLGAQMQKKIKELQ 1161
Cdd:PRK00409 645 YLSLGQkgevLSIPDDKEaivQAGIMKMKVPLSDLE 680
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1516-1728 |
2.55e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1516 LEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEE 1595
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1596 AEGALELEETKTlRIQLELSQ-------VKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAEtraRNEALRLKKKME 1668
Cdd:COG4942 109 LLRALYRLGRQP-PLALLLSPedfldavRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE---RAELEALLAELE 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578836100 1669 GDLNDLELQLghATRQATEAQAATRLM--QAQLKEEQAGRDEEQRLAAELHEQAQALERRAS 1728
Cdd:COG4942 185 EERAALEALK--AERQKLLARLEKELAelAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1683-1876 |
2.80e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.57 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1683 RQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATErl 1762
Cdd:PRK09510 81 RKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAA-- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1763 nllhsqntgllnQKKKLEADLAQLSgevEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVREL 1842
Cdd:PRK09510 159 ------------AAKKAAAEAKKKA---EAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....*..
gi 578836100 1843 QARLEEAE---QAALRGGKKQVQKLEAKVRELEAELD 1876
Cdd:PRK09510 224 KAAAAKAAaeaKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1024-1497 |
2.92e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1024 VKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLEcslEQEKKLRMDTERAKRK 1103
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELE---AELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1104 LEgdlkltqesVADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQaraEELEEELEAERAARARVEK 1183
Cdd:COG4717 125 LQ---------LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA---ELQEELEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1184 QRAEAARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVR 1263
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1264 QKLEKeksELRMEVDDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEK 1343
Cdd:COG4717 273 LTIAG---VLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1344 ECLISQLSRgkalAAQSLEELRRQLEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSK 1423
Cdd:COG4717 350 QELLREAEE----LEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1424 YEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLE------KAKLRLQTESEDVTLELERATSAAAALDKKQRH 1497
Cdd:COG4717 426 DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEedgelaELLQELEELKAELRELAEEWAALKLALELLEEA 505
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1539-1769 |
2.96e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1539 EALEA-LETLKRENKNLQEEISDLTDQV------SLSGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQ 1611
Cdd:PRK11281 83 EQLKQqLAQAPAKLRQAQAELEALKDDNdeetreTLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQ 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1612 LELS---QVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARnealrlKKKMEGD--LNDL-ELQLGHATRQA 1685
Cdd:PRK11281 163 AALYansQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQ------RKSLEGNtqLQDLlQKQRDYLTARI 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1686 TEAQAATRLMQAQLKEEQAGRDEEQrlAAELHEQAQALERRA-SLLAAELEelraaleqgeRSRRLAeQELLEATERLNL 1764
Cdd:PRK11281 237 QRLEHQLQLLQEAINSKRLTLSEKT--VQEAQSQDEAARIQAnPLVAQELE----------INLQLS-QRLLKATEKLNT 303
|
....*
gi 578836100 1765 LHSQN 1769
Cdd:PRK11281 304 LTQQN 308
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1009-1210 |
2.99e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1009 TLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSAL----TKAKLRLEQQVEDLE 1084
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLqaeiAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1085 CSLEQEKKLRMDTERAKRKLEGD---------------LKLTQESVADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLL 1149
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSEsfsdfldrlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578836100 1150 GAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQR 1210
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1539-1972 |
3.01e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 45.79 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1539 EALEALETLKRENKNLQEEISDLTDQVSLSG----KSIQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQlEL 1614
Cdd:pfam05701 32 QTVERRKLVELELEKVQEEIPEYKKQSEAAEaakaQVLEELESTKRLIEELKLNLERAQTEEAQAKQDSELAKLRVE-EM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1615 SQVKAEVDRKLAEkdEECANLRRNHQRAVESLQAsldaetrARNEALRLKKKMEGDLNDLELqlghATRQATEAQAATRL 1694
Cdd:pfam05701 111 EQGIADEASVAAK--AQLEVAKARHAAAVAELKS-------VKEELESLRKEYASLVSERDI----AIKRAEEAVSASKE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1695 MQAQLKEeqagrdeeqrLAAELHEQAQALER-RASLLAAELEELRAALEQGERSRRLaEQELLEATERLNLLHSQNTGLL 1773
Cdd:pfam05701 178 IEKTVEE----------LTIELIATKESLESaHAAHLEAEEHRIGAALAREQDKLNW-EKELKQAEEELQRLNQQLLSAK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1774 NQKKKLEA------DL-AQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKE-QDTSAHLERMK---KTLEQTVREL 1842
Cdd:pfam05701 247 DLKSKLETasalllDLkAELAAYMESKLKEEADGEGNEKKTSTSIQAALASAKKElEEVKANIEKAKdevNCLRVAAASL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1843 QARLEEaEQAALRGGKKQVQKLEAKVRELEAELDaeqkkhaealkgvrkheRRVKELAYQAEEDRKNLARMQDLVDKLQs 1922
Cdd:pfam05701 327 RSELEK-EKAELASLRQREGMASIAVSSLEAELN-----------------RTKSEIALVQAKEKEAREKMVELPKQLQ- 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 578836100 1923 kvksykrqfeEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRAR 1972
Cdd:pfam05701 388 ----------QAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESR 427
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1647-1807 |
3.03e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.34 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1647 QASLDAETRARNEAL-RLKKKMeGDLNDLeLQLGHATRQATEAQAATrlMQAQLKEEQAGRDEEQRLAAELHEQAQALER 1725
Cdd:PRK09039 41 QFFLSREISGKDSALdRLNSQI-AELADL-LSLERQGNQDLQDSVAN--LRASLSAAEAERSRLQALLAELAGAGAAAEG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1726 RASLLAAELEELRAaleQGERSRRLAEqelleaterlnllhsqntgLLNQkkKLEADLAQLsGEVEEA--AQERREAEEK 1803
Cdd:PRK09039 117 RAGELAQELDSEKQ---VSARALAQVE-------------------LLNQ--QIAALRRQL-AALEAAldASEKRDRESQ 171
|
....
gi 578836100 1804 AKKA 1807
Cdd:PRK09039 172 AKIA 175
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1720-1875 |
3.16e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.62 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1720 AQALER-RASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERR 1798
Cdd:COG2433 379 EEALEElIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEER 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1799 EAEEKAKkaitdaammaeELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAA---LRGGKKQVQKLEA----KVREL 1871
Cdd:COG2433 459 REIRKDR-----------EISRLDREIERLERELEEERERIEELKRKLERLKELWkleHSGELVPVKVVEKftkeAIRRL 527
|
....
gi 578836100 1872 EAEL 1875
Cdd:COG2433 528 EEEY 531
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1775-1887 |
3.53e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 45.25 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1775 QKKKLEADLAQLSGEV--EEAAQERREAEEKAK----KAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEE 1848
Cdd:COG2268 224 EEAELEQEREIETARIaeAEAELAKKKAEERREaetaRAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREE 303
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 578836100 1849 AEQAALRGGKKQVQKLEAKVRElEAELDAEQ---KKHAEALK 1887
Cdd:COG2268 304 AELEADVRKPAEAEKQAAEAEA-EAEAEAIRakgLAEAEGKR 344
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
962-1149 |
3.64e-04 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 45.61 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 962 VQLEGKVKELSERLEDEEEVNADLAAR-------RRKLEDECTELKKDIDDLELTLAKA----EKEKQATENKVKNLTEE 1030
Cdd:pfam09726 398 VRLEQDIKKLKAELQASRQTEQELRSQissltslERSLKSELGQLRQENDLLQTKLHNAvsakQKDKQTVQQLEKRLKAE 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1031 MAALDESVARLTKEKKALQEahqqalgdlqaEEDrvsalTKAKLRLEQQVEDLECSlEQEKKLRMDTERAKRKLEGDLKL 1110
Cdd:pfam09726 478 QEARASAEKQLAEEKKRKKE-----------EEA-----TAARAVALAAASRGECT-ESLKQRKRELESEIKKLTHDIKL 540
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 578836100 1111 TQESVADAAQDKQQLEE-KLKKKDSE--LSQLSLRVEDEQLL 1149
Cdd:pfam09726 541 KEEQIRELEIKVQELRKyKESEKDTEvlMSALSAMQDKNQHL 582
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1735-1972 |
3.92e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1735 EELRAALEQgersrrLAEQELLEATERLNLLHSQNT-GLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKaitdaam 1813
Cdd:PRK11281 39 ADVQAQLDA------LNKQKLLEAEDKLVQQDLEQTlALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEA------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1814 maeeLKKEQDTSAhlermKKTLE-QTVRELQARLEEAE------QAALRGGKKQVQKLEAKVRELEAELDAEQKKHAE-- 1884
Cdd:PRK11281 106 ----LKDDNDEET-----RETLStLSLRQLESRLAQTLdqlqnaQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQir 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1885 -ALKGVR------KHERRVK---ELAY---QAEEDRKNLA---RMQDLvDKLQSKVKSYKRQFEEAEQQANTNL--AKYR 1946
Cdd:PRK11281 177 nLLKGGKvggkalRPSQRVLlqaEQALlnaQNDLQRKSLEgntQLQDL-LQKQRDYLTARIQRLEHQLQLLQEAinSKRL 255
|
250 260
....*....|....*....|....*..
gi 578836100 1947 K-AQHELDDAEERADMAETQANKLRAR 1972
Cdd:PRK11281 256 TlSEKTVQEAQSQDEAARIQANPLVAQ 282
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
983-1132 |
4.51e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 983 ADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEmaaLDESVARLTKEKKALQEAH-QQALGDLQA 1061
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE---IEEVEARIKKYEEQLGNVRnNKEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578836100 1062 EEDrvsALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKK 1132
Cdd:COG1579 97 EIE---SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1690-1976 |
4.76e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1690 AATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQN 1769
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1770 TGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEA 1849
Cdd:COG4372 104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1850 EQAALRggkkqvqkLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKR 1929
Cdd:COG4372 184 ALDELL--------KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 578836100 1930 QFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDA 1976
Cdd:COG4372 256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLL 302
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1716-1955 |
4.80e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 43.94 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1716 LHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQ 1795
Cdd:pfam06008 10 ALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1796 ERREAEEKAKKAITDAAMMAEELkkEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAEL 1875
Cdd:pfam06008 90 AIKNLIDNIKEINEKVATLGEND--FALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1876 DAEQKKHAEALKGV-RKHERRVKEL--------AYQAEEDRKNLARMQDLVDKLQSK--VKSYKRQFEEAEQQANTNLAK 1944
Cdd:pfam06008 168 QEENKALANALRDSlAEYEAKLSDLrellreaaAKTRDANRLNLANQANLREFQRKKeeVSEQKNQLEETLKTARDSLDA 247
|
250
....*....|.
gi 578836100 1945 YRKAQHELDDA 1955
Cdd:pfam06008 248 ANLLLQEIDDA 258
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1042-1897 |
4.86e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.42 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1042 TKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSL--------EQEKKLRMDTERAKRKLEGDLKLTQE 1113
Cdd:TIGR00606 247 LDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMekvfqgtdEQLNDLYHNHQRTVREKERELVDCQR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1114 SVADAAQDKQQLEEKLKKKDSELSQLSLRVE--DEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARE 1191
Cdd:TIGR00606 327 ELEKLNKERRLLNQEKTELLVEQGRLQLQADrhQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1192 LEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGaAELGEQVDSLQRVRQKLEKEKS 1271
Cdd:TIGR00606 407 AKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKEL-QQLEGSSDRILELDQELRKAER 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1272 ELRMEvdDLAANVETLTRAKASaeklcrtyedqLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLS 1351
Cdd:TIGR00606 486 ELSKA--EKNSLTETLKKEVKS-----------LQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIR 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1352 RGKALAAQ---SLEELRRQLEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSK----- 1423
Cdd:TIGR00606 553 KIKSRHSDeltSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvc 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1424 ----YEADAIQRTEELEEAKKKLALRLQEAE------EGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAaldK 1493
Cdd:TIGR00606 633 gsqdEESDLERLKEEIEKSSKQRAMLAGATAvysqfiTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAP---D 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1494 KQRHLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLRhgheealealETLKRENKNLQEEISDLTDQVSLSGKSIQ 1573
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELR----------NKLQKVNRDIQRLKNDIEEQETLLGTIMP 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1574 ELEKTKKALE--GEKSEIQAALEEAEGALELEETKTLRIQLELSQvkAEVDRKLAEKDEEcanLRRNHQRAVESLQASLD 1651
Cdd:TIGR00606 780 EEESAKVCLTdvTIMERFQMELKDVERKIAQQAAKLQGSDLDRTV--QQVNQEKQEKQHE---LDTVVSKIELNRKLIQD 854
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1652 aetraRNEALRLKKKMEGDLNDLELQLGHATRQATEaqaatrlMQAQLKEEQAgrdEEQRLAAELHEQAQALERRASLLA 1731
Cdd:TIGR00606 855 -----QQEQIQHLKSKTNELKSEKLQIGTNLQRRQQ-------FEEQLVELST---EVQSLIREIKDAKEQDSPLETFLE 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1732 AELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLN--------QKKKLEADLAQLSGEVEEAAQERREAEEK 1803
Cdd:TIGR00606 920 KDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENkiqdgkddYLKQKETELNTVNAQLEECEKHQEKINED 999
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1804 AKKAITDAAMMAEELKKEQDtsaHLERMKKtlEQTVRELQarlEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHA 1883
Cdd:TIGR00606 1000 MRLMRQDIDTQKIQERWLQD---NLTLRKR--ENELKEVE---EELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHV 1071
|
890
....*....|....
gi 578836100 1884 EALKGVRKHERRVK 1897
Cdd:TIGR00606 1072 LALGRQKGYEKEIK 1085
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
978-1161 |
5.97e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 978 EEEVNADL--AARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQA 1055
Cdd:PRK11281 38 EADVQAQLdaLNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1056 LGDLQAEEdrvsaltkaklrLEQQVEDLECSLEQEKK-----------LRMDTERAkrklegdlkltQESVADAAQDKQQ 1124
Cdd:PRK11281 118 LSTLSLRQ------------LESRLAQTLDQLQNAQNdlaeynsqlvsLQTQPERA-----------QAALYANSQRLQQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 578836100 1125 LEEKLK-----KKDSELSQLSLRVEDEQLLGAQMQKKIKELQ 1161
Cdd:PRK11281 175 IRNLLKggkvgGKALRPSQRVLLQAEQALLNAQNDLQRKSLE 216
|
|
| FUSC |
pfam04632 |
Fusaric acid resistance protein family; This family includes a conserved region found in two ... |
1678-1869 |
6.46e-04 |
|
Fusaric acid resistance protein family; This family includes a conserved region found in two proteins associated with fusaric acid resistance, from Burkholderia cepacia and Klebsiella oxytoca. These proteins are likely to be membrane transporter proteins.
Pssm-ID: 428044 [Multi-domain] Cd Length: 655 Bit Score: 44.58 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1678 LGHATRQATEA--QAATRLMQAQLKEEQAGRDEEQRLAAeLHEQAQALERRASLLAAELEELRAaleqgeRSRRLAE--Q 1753
Cdd:pfam04632 153 VGPALRARLRArlRDALRLAAAALAGAPGAEAFEAARLR-LAADILALEALRSHAAFESPRGRA------RARALRRllA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1754 ELLEATERLNLLHSQ----NTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAkkAITDAAMMAEELKKEQDTSAhle 1829
Cdd:pfam04632 226 RMLALLPRLRSLARLlarlRTEGAGTVPELAALLDELAAWEAALAAEALQAALAA--LRARLRALRPALPLDFDTAA--- 300
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 578836100 1830 rmkkTLEQTVRELQARLEEAEQ--AALRGGKKQVQKLEAKVR 1869
Cdd:pfam04632 301 ----ELLARLADLLAELAEALAscRALRHPIAQGARPARLAR 338
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1613-1917 |
6.49e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1613 ELSQVKAEVDRKLAEKDEEcanlRRNHQRAVESLQASLDAETRARNEALRLkkkmegDLNDLELQLGHATRQATEAQAAT 1692
Cdd:COG3096 840 ALRQRRSELERELAQHRAQ----EQQLRQQLDQLKEQLQLLNKLLPQANLL------ADETLADRLEELREELDAAQEAQ 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1693 RLMQAQlkeeqagrdeeQRLAAELHEQAQALERRAsllaAELEELRAALEQGERSRRLAEQELLEATE----RLNLLHSQ 1768
Cdd:COG3096 910 AFIQQH-----------GKALAQLEPLVAVLQSDP----EQFEQLQADYLQAKEQQRRLKQQIFALSEvvqrRPHFSYED 974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1769 NTGLLNQKKKLEADLAQlsgEVEEAAQERREAEEKAKKAItdaammaeelKKEQDTSAHLERMKKTLEQTVRELQARLEE 1848
Cdd:COG3096 975 AVGLLGENSDLNEKLRA---RLEQAEEARREAREQLRQAQ----------AQYSQYNQVLASLKSSRDAKQQTLQELEQE 1041
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578836100 1849 AEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLV 1917
Cdd:COG3096 1042 LEELGVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQV 1110
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1609-1936 |
6.56e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1609 RIQLELSQVKAEVDRKLAEKDEECANLRRNhQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEA 1688
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQA-RSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1689 QAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQ 1768
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1769 NTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEE 1848
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1849 AEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYK 1928
Cdd:COG4372 281 AALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLS 360
|
....*...
gi 578836100 1929 RQFEEAEQ 1936
Cdd:COG4372 361 KGAEAGVA 368
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1841-1978 |
6.90e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 6.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1841 ELQARLEEAEQAaLRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDL--VD 1918
Cdd:COG1579 14 ELDSELDRLEHR-LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeYE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1919 KLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDALG 1978
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1263-1496 |
7.20e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1263 RQKLEKEKSELRMEVDDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEE 1342
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1343 KECLISQLSRgkaLAAQSLEELRRQLEEESKAKSALAHAVQALRHdcdllreqheeeaeaqaelqrllskanaeVAQWRS 1422
Cdd:COG4942 102 QKEELAELLR---ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKY-----------------------------LAPARR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578836100 1423 KYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQR 1496
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1609-1867 |
7.73e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1609 RIQLELSQVKA-EVDRKLAEKDEECANLRRNHQRAVESLQASldaetrarNEALRLKKKME---GDLNDLELQLGHAT-- 1682
Cdd:PRK04863 299 RRQLAAEQYRLvEMARELAELNEAESDLEQDYQAASDHLNLV--------QTALRQQEKIEryqADLEELEERLEEQNev 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1683 ------------RQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAE----------LEELRAA 1740
Cdd:PRK04863 371 veeadeqqeeneARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQLCGLPdltadnaedwLEEFQAK 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1741 LEQGERSRRLAEQ------------------------------------ELLEATERLNLLHSQNTGLLNQKKKLEADLA 1784
Cdd:PRK04863 451 EQEATEELLSLEQklsvaqaahsqfeqayqlvrkiagevsrseawdvarELLRRLREQRHLAEQLQQLRMRLSELEQRLR 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1785 QlsgeveEAAQER--REAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQaalrggkkQVQ 1862
Cdd:PRK04863 531 Q------QQRAERllAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQA--------RIQ 596
|
....*
gi 578836100 1863 KLEAK 1867
Cdd:PRK04863 597 RLAAR 601
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1002-1115 |
9.05e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.30 E-value: 9.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1002 DIDDLELTLAKAEKEKQATENkvknltEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVE 1081
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKK------EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG 485
|
90 100 110
....*....|....*....|....*....|....
gi 578836100 1082 DLEcslEQEKKLrmdtERAKRKLEGDLKLTQESV 1115
Cdd:COG0542 486 KIP---ELEKEL----AELEEELAELAPLLREEV 512
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
896-1130 |
9.13e-04 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 44.28 E-value: 9.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 896 EELAALRAELRGLRGALAAAEA--------KRQELEETHVSITQEKNDLALQLQAE-QDN------LADAEERchlLIKS 960
Cdd:pfam15070 53 QELETSLAELKNQAAVPPAEEEqppagpseEEQRLQEEAEQLQKELEALAGQLQAQvQDNeqlsrlNQEQEQR---LLEL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 961 KVQLEGKVKELSERLEDEEEVNADLA------ARRRKLEDECTEL-----KKDIDDLELTLA-KAEKE-KQATENKVKNL 1027
Cdd:pfam15070 130 ERAAERWGEQAEDRKQILEDMQSDRAtisralSQNRELKEQLAELqngfvKLTNENMELTSAlQSEQHvKKELAKKLGQL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1028 TEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVedlecsLEQEKKL-RMDTERAKRKLEG 1106
Cdd:pfam15070 210 QEELGELKETLELKSQEAQSLQEQRDQYLAHLQQYVAAYQQLASEKEELHKQY------LLQTQLMdRLQHEEVQGKVAA 283
|
250 260
....*....|....*....|....*....
gi 578836100 1107 D-----LKLTQESVADAAQDKQQLEEKLK 1130
Cdd:pfam15070 284 EmarqeLQETQERLEALTQQNQQLQAQLS 312
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
920-1282 |
9.36e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 920 QELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLEDEEEVNADLAARRRKLEDECTEL 999
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1000 KKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQ 1079
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1080 VEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKE 1159
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1160 LQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAALRHEATVA 1239
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 578836100 1240 ALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAA 1282
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
968-1354 |
9.49e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 9.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 968 VKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEK----------QATENKVKNLTEEMAALDES 1037
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLlklelllsnlKKKIQKNKSLESQISELKKQ 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1038 VARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLK-LTQESVA 1116
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdLNNQKEQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1117 DAAQD-KQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEaareleel 1195
Cdd:TIGR04523 307 DWNKElKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE-------- 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1196 serleeaggaSAGQREGCRKREAELGRLRRELEeaalrheatvaalrrKQAEGAAELGEQVDSLQRVRQKLEKEKSELRM 1275
Cdd:TIGR04523 379 ----------NQSYKQEIKNLESQINDLESKIQ---------------NQEKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578836100 1276 EVDDLAANVETLTRAKASAEKlcrtyedQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLSRGK 1354
Cdd:TIGR04523 434 TIIKNNSEIKDLTNQDSVKEL-------IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1777-1951 |
1.04e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 41.87 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1777 KKLEADLAQLSGEVEEAAQERREAEEKAKKAITdAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRG 1856
Cdd:pfam01442 7 DELSTYAEELQEQLGPVAQELVDRLEKETEALR-ERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEELRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1857 GKKQVQKLEAKVRELEAELDAEQKKHAEALKGVrkherrvkeLAYQAEEDRKNLA-RMQDLVDKLQSKVKSYKRQFEEAE 1935
Cdd:pfam01442 86 LNADAEELQEKLAPYGEELRERLEQNVDALRAR---------LAPYAEELRQKLAeRLEELKESLAPYAEEVQAQLSQRL 156
|
170
....*....|....*.
gi 578836100 1936 QQANTNLAKYRKAQHE 1951
Cdd:pfam01442 157 QELREKLEPQAEDLRE 172
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
893-1083 |
1.06e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 893 QAEEELAALRaELRGLRGALAAAEAKRQELEEthvsitqeknDLALQLQAEQdNLADAEERCHLLIKSKVQLEGKVKELS 972
Cdd:PRK04863 497 VARELLRRLR-EQRHLAEQLQQLRMRLSELEQ----------RLRQQQRAER-LLAEFCKRLGKNLDDEDELEQLQEELE 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 973 ERLEDEEEVNADLAARRRKLEDECTELKKDIDdlelTLAKAEKEKQATENKVKNLTEEMAALDESVARLTkekkALQEAH 1052
Cdd:PRK04863 565 ARLESLSESVSEARERRMALRQQLEQLQARIQ----RLAARAPAWLAAQDALARLREQSGEEFEDSQDVT----EYMQQL 636
|
170 180 190
....*....|....*....|....*....|.
gi 578836100 1053 QQALGDLQAEEDRVSAltkAKLRLEQQVEDL 1083
Cdd:PRK04863 637 LERERELTVERDELAA---RKQALDEEIERL 664
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1671-1812 |
1.08e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1671 LNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERR-----ASLLAA----ELEELRAAL 1741
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyeEQLGNVrnnkEYEALQKEI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578836100 1742 EQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAA 1812
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
895-1159 |
1.08e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 895 EEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSER 974
Cdd:pfam07888 79 ESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKER 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 975 LEDeeevnadLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLT------------ 1042
Cdd:pfam07888 159 AKK-------AGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTqklttahrkeae 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1043 -----KEKKALQE---AHQQA-------LGDLQAEEDRVSA-LTKAKLRLEQ---QVEDLECSLEQEK--------KLRM 1095
Cdd:pfam07888 232 neallEELRSLQErlnASERKveglgeeLSSMAAQRDRTQAeLHQARLQAAQltlQLADASLALREGRarwaqereTLQQ 311
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578836100 1096 DTERAKRKLE---GDLKLTQESVADAAQDKQQLEEKL-KKKDSELSQLSLRVEDEQLLGAQMQKKIKE 1159
Cdd:pfam07888 312 SAEADKDRIEklsAELQRLEERLQEERMEREKLEVELgREKDCNRVQLSESRRELQELKASLRVAQKE 379
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1695-1875 |
1.37e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 43.90 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1695 MQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQgERSRRLAEQELLEATERLNllhsqntglln 1774
Cdd:pfam13166 298 AISSLLAQLPAVSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRALEA-KRKDPFKSIELDSVDAKIE----------- 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1775 QKKKLEADLAQLSGEVEEAAQERREAEEKAKKAItdAAMMAEELKKEQDTsahLERMKKTLEQTVRELQARLEEAEqaal 1854
Cdd:pfam13166 366 SINDLVASINELIAKHNEITDNFEEEKNKAKKKL--RLHLVEEFKSEIDE---YKDKYAGLEKAINSLEKEIKNLE---- 436
|
170 180
....*....|....*....|.
gi 578836100 1855 rggkKQVQKLEAKVRELEAEL 1875
Cdd:pfam13166 437 ----AEIKKLREEIKELEAQL 453
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1563-1977 |
1.42e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1563 DQVSLSGKSIQELEKTKKALegeKSEIQAALEEAEGALELEETKTLRIQLELSQVKAEVDrklaEKDEECANLRRNHQRa 1642
Cdd:pfam15921 310 NQNSMYMRQLSDLESTVSQL---RSELREAKRMYEDKIEELEKQLVLANSELTEARTERD----QFSQESGNLDDQLQK- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1643 veslqasLDAETRARNEALRLKKKMEGDLNDLE----LQLGHATRQA----TEAQAATRLMQAqLKEEQAGRDEEQrlAA 1714
Cdd:pfam15921 382 -------LLADLHKREKELSLEKEQNKRLWDRDtgnsITIDHLRRELddrnMEVQRLEALLKA-MKSECQGQMERQ--MA 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1715 ELHEQAQALERRASL---LAAELEELRAALEQgersrRLAEQELLEATERLnlLHSQNTGLLNQKKKLEA---DLAQLSG 1788
Cdd:pfam15921 452 AIQGKNESLEKVSSLtaqLESTKEMLRKVVEE-----LTAKKMTLESSERT--VSDLTASLQEKERAIEAtnaEITKLRS 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1789 EVEEAAQER---REAEEKAKKAITDAA----MMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQV 1861
Cdd:pfam15921 525 RVDLKLQELqhlKNEGDHLRNVQTECEalklQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRL 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1862 Q---------KLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELayqaEEDRknlarmqdlvDKLQSKVKSYKRQFE 1932
Cdd:pfam15921 605 ElqefkilkdKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDI----KQER----------DQLLNEVKTSRNELN 670
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 578836100 1933 EAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDAL 1977
Cdd:pfam15921 671 SLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
1648-1884 |
1.54e-03 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 43.83 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1648 ASLDAETRARNEALRLKKKME-GDLNDLELQLGHATRQATEAQAAT------RLMQAQLKEEQAGRDEEQRLAAELHEQA 1720
Cdd:PRK14900 779 AVADPALRDLLQAGELARVHRvAGVEGSRLVVAAATAPAPQSAVGVgpgfevRVPLAGVIDLAAETARVDKEIGKVDQDL 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1721 QALERR---ASLLAaeleelRAALEQGERSRRLAEQelleaterlnllhsqntgLLNQKKKLEADLAQLSGEVEEAAQER 1797
Cdd:PRK14900 859 AVLERKlqnPSFVQ------NAPPAVVEKDRARAEE------------------LREKRGKLEAHRAMLSGSEANSARRD 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1798 REAEEKAKKAITDAAmmAEELKKEQDTSAhLERMKKTLEqTVRELQARLEEAEQAALRGGKKQVQK-LEAKVRELEAELD 1876
Cdd:PRK14900 915 TMEIQNEQKPTQDGP--AAEAQPAQENTV-VESAEKAVA-AVSEAAQQAATAVASGIEKVAEAVRKtVRRSVKKAAATRA 990
|
....*...
gi 578836100 1877 AEQKKHAE 1884
Cdd:PRK14900 991 AMKKKVAK 998
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1702-1911 |
1.64e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1702 EQAGRDEEQRLAAELHEQAQalERRASLLAAELEELRAALEQgeRSRRLaEQELLEATErlnllhsqntgllnQKKklea 1781
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQR--KKKEQQQAEELQQKQAAEQE--RLKQL-EKERLAAQE--------------QKK---- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1782 dlaqlsgEVEEAAQERRE----AEEKAKKAITDAAMMAE-ELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRG 1856
Cdd:PRK09510 119 -------QAEEAAKQAALkqkqAEEAAAKAAAAAKAKAEaEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578836100 1857 GKKQVQKLEAKvreleAELDAEQKKHAEALKgvrKHERRVKELAYQAEEDRKNLA 1911
Cdd:PRK09510 192 AAKAAAEAKKK-----AEAEAKKKAAAEAKK---KAAAEAKAAAAKAAAEAKAAA 238
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
995-1130 |
1.77e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 42.41 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 995 ECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKL 1074
Cdd:COG4026 129 EYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKRL 208
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578836100 1075 ----RLEQQVEDL-ECSLEQEKKLRMDTERAKrklEGDLKLTQESVadAAQDKQQLEEKLK 1130
Cdd:COG4026 209 levfSLEELWKELfPEELPEEDFIYFATENLK---PGKIIVGQGYI--AAESKEDAEEWLK 264
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1217-1379 |
1.89e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1217 EAELGRLRRELEEAALRHEATVAALRRKQAEgAAELGEQVDSLQrvrQKLEKEKSELRMEV------------------- 1277
Cdd:COG3883 36 QAELDALQAELEELNEEYNELQAELEALQAE-IDKLQAEIAEAE---AEIEERREELGERAralyrsggsvsyldvllgs 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1278 ---DDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLSRGK 1354
Cdd:COG3883 112 esfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191
|
170 180
....*....|....*....|....*
gi 578836100 1355 ALAAQSLEELRRQLEEESKAKSALA 1379
Cdd:COG3883 192 AAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1546-1975 |
1.97e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 43.13 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1546 TLKRENKNLQEEISDLTdqvslsgKSIQELEKTKKALEgekseiqaaleeaegaleleetktlriqLELSQVKAEVDRKL 1625
Cdd:pfam13166 86 TLGEESIEIQEKIAKLK-------KEIKDHEEKLDAAE----------------------------ANLQKLDKEKEKLE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1626 AEKDEECAnlRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDlelqlghatrqateaqAATRLMQAQLKEEQAG 1705
Cdd:pfam13166 131 ADFLDECW--KKIKRKKNSALSEALNGFKYEANFKSRLLREIEKDNFN----------------AGVLLSDEDRKAALAT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1706 RDEEQR----------LAAELHEQAQALERRASLLAAELEELRaaleqgersRRLAEQELLEATERLNLLHSQNTGLLNQ 1775
Cdd:pfam13166 193 VFSDNKpeiapltfnvIDFDALEKAEILIQKVIGKSSAIEELI---------KNPDLADWVEQGLELHKAHLDTCPFCGQ 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1776 ------KKKLEadlAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEA 1849
Cdd:pfam13166 264 plpaerKAALE---AHFDDEFTEFQNRLQKLIEKVESAISSLLAQLPAVSDLASLLSAFELDVEDIESEAEVLNSQLDGL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1850 EQAALRGGKKQVQKLEAKVreLEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARmqDLVDKLQSKVKSYKR 1929
Cdd:pfam13166 341 RRALEAKRKDPFKSIELDS--VDAKIESINDLVASINELIAKHNEITDNFEEEKNKAKKKLRL--HLVEEFKSEIDEYKD 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 578836100 1930 QFEEAEQQANtnlakyrKAQHELDDAEERADMAETQANKLRARTRD 1975
Cdd:pfam13166 417 KYAGLEKAIN-------SLEKEIKNLEAEIKKLREEIKELEAQLRD 455
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1832-1967 |
2.06e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.73 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1832 KKTLEQTVRELQARLEEAEQ------AALRGGKKQVQKLEAKVRELEAE----LDAEQKKHA-EALKGVRKHERRVKELA 1900
Cdd:COG1842 25 EKMLDQAIRDMEEDLVEARQalaqviANQKRLERQLEELEAEAEKWEEKarlaLEKGREDLArEALERKAELEAQAEALE 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578836100 1901 YQAEEDRKNLARMQDLVDKLQSKVKSYKRQFE---------EAEQQANTNLAKYR--KAQHELDDAEERADMAETQAN 1967
Cdd:COG1842 105 AQLAQLEEQVEKLKEALRQLESKLEELKAKKDtlkarakaaKAQEKVNEALSGIDsdDATSALERMEEKIEEMEARAE 182
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
971-1297 |
2.09e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 971 LSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQE 1050
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1051 AHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSL-EQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLEEKL 1129
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIaEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1130 KKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQ 1209
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1210 REGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTR 1289
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
....*...
gi 578836100 1290 AKASAEKL 1297
Cdd:COG4372 349 GLLDNDVL 356
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
887-1484 |
2.16e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 887 PLLRSAQAEEELAALRA-------ELRGLRGALAAAEAKRQELEEthvsitqekndlALQL--------------QAEQD 945
Cdd:COG3096 432 PDLTPENAEDYLAAFRAkeqqateEVLELEQKLSVADAARRQFEK------------AYELvckiageversqawQTARE 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 946 NLADAEERCHLLiKSKVQLEGKVKELSERLEDEEEVnadlaarRRKLEDECTELKKDIDD-LELTLAKAEKEkqatenkv 1024
Cdd:COG3096 500 LLRRYRSQQALA-QRLQQLRAQLAELEQRLRQQQNA-------ERLLEEFCQRIGQQLDAaEELEELLAELE-------- 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1025 knltEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLrmdTERAKRKL 1104
Cdd:COG3096 564 ----AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEV---TAAMQQLL 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1105 EGDLKLTQESvADAAQDKQQLEEKLKK-------KDSELSQLSLR--------------VED----EQLLGAQMQKKIKE 1159
Cdd:COG3096 637 EREREATVER-DELAARKQALESQIERlsqpggaEDPRLLALAERlggvllseiyddvtLEDapyfSALYGPARHAIVVP 715
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1160 LQARAEELEEELEAERAARARVEKQrAEAARELEELSERLEEAGGASAGQRE------------GCRKREAELGRLRREL 1227
Cdd:COG3096 716 DLSAVKEQLAGLEDCPEDLYLIEGD-PDSFDDSVFDAEELEDAVVVKLSDRQwrysrfpevplfGRAAREKRLEELRAER 794
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1228 EEAALRH---------------------------------EATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELR 1274
Cdd:COG3096 795 DELAEQYakasfdvqklqrlhqafsqfvgghlavafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQ 874
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1275 M-----------EVDDLAANVETLTRAKASAE----------KLCRTYEDQLS---EAKIKVEELQRQLADASTQRGRLQ 1330
Cdd:COG3096 875 LlnkllpqanllADETLADRLEELREELDAAQeaqafiqqhgKALAQLEPLVAvlqSDPEQFEQLQADYLQAKEQQRRLK 954
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1331 TESGELSRLLEEKECLISQLSRGKALAAQSLEElrrqleeesKAKSALAHAVQALRHDCDLLREQHEEeaeaqaelqrlL 1410
Cdd:COG3096 955 QQIFALSEVVQRRPHFSYEDAVGLLGENSDLNE---------KLRARLEQAEEARREAREQLRQAQAQ-----------Y 1014
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1411 SKANAEVAQWRSKYEA------DAIQRTEELE-----EAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTL 1479
Cdd:COG3096 1015 SQYNQVLASLKSSRDAkqqtlqELEQELEELGvqadaEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQK 1094
|
....*
gi 578836100 1480 ELERA 1484
Cdd:COG3096 1095 RLRKA 1099
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1095-1559 |
2.17e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1095 MDTERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAE 1174
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1175 RAARARVEKQRAEAARELEELserleeaggasagQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGE 1254
Cdd:COG4717 126 QLLPLYQELEALEAELAELPE-------------RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1255 QVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASAEKlcrtyEDQLSEAKIKVEELQRQLADASTQRGRLQTESG 1334
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-----ELEAAALEERLKEARLLLLIAAALLALLGLGGS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1335 ELSRLLEEKE----------CLISQLSRGKALAAQSLEELRRQLEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQA 1404
Cdd:COG4717 268 LLSLILTIAGvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1405 ELQRLLSKANAEVAQwrskyeadaIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERA 1484
Cdd:COG4717 348 ELQELLREAEELEEE---------LQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGEL 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578836100 1485 TSAAAALDKKQrhLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLRHGHE--EALEALETLKRENKNLQEEIS 1559
Cdd:COG4717 419 EELLEALDEEE--LEEELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWA 493
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1774-1982 |
2.43e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.53 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1774 NQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAA 1853
Cdd:TIGR02794 61 PAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1854 LRggkKQVQKLEAKvreleAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEE 1933
Cdd:TIGR02794 141 ER---KAKEEAAKQ-----AEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAK 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 578836100 1934 AEQQANTNLAKYRKAQHELDDAEERADMA-ETQANKLRARTRDALGPKLS 1982
Cdd:TIGR02794 213 AEAEAAAAAAAEAERKADEAELGDIFGLAsGSNAEKQGGARGAAAGSEVD 262
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1779-1872 |
2.43e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 42.18 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1779 LEADLAQLSGEVE-EAAQERREAEEKAKKAITDAAMMAEELKKEQDTS--AHLERMKKTLEQTVRELQARLEEA------ 1849
Cdd:cd16269 187 LQADQALTEKEKEiEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSyeEHLRQLKEKMEEERENLLKEQERAlesklk 266
|
90 100
....*....|....*....|....*
gi 578836100 1850 EQAAL--RGGKKQVQKLEAKVRELE 1872
Cdd:cd16269 267 EQEALleEGFKEQAELLQEEIRSLK 291
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1026-1253 |
2.43e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1026 NLTEEMAALDESVARLTKEKKALQEAHQQALGDLQA--EEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRK 1103
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1104 LEGDLKLTQESVADAAQDK--QQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARV 1181
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEA 324
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578836100 1182 EKQRAEAARELEELSErleeaggasaGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELG 1253
Cdd:COG3206 325 LQAREASLQAQLAQLE----------ARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVG 386
|
|
| COG4646 |
COG4646 |
Adenine-specific DNA methylase, N12 class [Replication, recombination and repair]; |
1214-1888 |
2.45e-03 |
|
Adenine-specific DNA methylase, N12 class [Replication, recombination and repair];
Pssm-ID: 443684 [Multi-domain] Cd Length: 1711 Bit Score: 42.93 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1214 RKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKAS 1293
Cdd:COG4646 1005 RQEEILEEQIAEILKAIKELKAVVRKRFTVKQLESTKKLGAGKLKQLDLLALKDLDVPWEPLDVDQLFGRGSRQGNNNFL 1084
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1294 AEKLCRTYEDQLSEAKIKVEELQRQLA-DASTQRGRLQTESGELSRLLEEKECLISQLSRGKALAAQSLEELRRQLEEES 1372
Cdd:COG4646 1085 VTKMRNVAGLAFSDAAKLSDYFGKQRYrDELTAGKGVVVATGTDESNLMYELYTAQAYLQLLLLGKQGLTNFDTWASTLE 1164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1373 KAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKKKLALRLQEAE-- 1450
Cdd:COG4646 1165 ELVTAAELAPERTAYRANTREAKAVNLPEEDVMIKEAEDAKTADELLLPTPEKISGGVATKPSEVQKELLEELEERAAiv 1244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1451 -----EGVEAANAKCSSLEKAKLRLQTesEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQRESRG 1525
Cdd:COG4646 1245 rkndgEPDRDNMLVITDDGRKAALDQR--LDIKTLPDDEGSLVALCVTNIDRIWEDNPESKLTQLVFCDLSTPKGDGTFN 1322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1526 LGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEET 1605
Cdd:COG4646 1323 DLEDIREKLIEEEIAELEIAFIHLALDDQEKAELFARDRLGAVEKLRISTAKMGAGTNVRLLLEATHDLDVPWRPRDAEQ 1402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1606 KTLRIQLELSQVKAEV----------DRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLE 1675
Cdd:COG4646 1403 RAGRGRRQGNENEEVEeiryvtentfDAYLWQAAETKQKFIAQIMTSKSPVRSLEDVDEAALSYAERKALAAGRPKEKEK 1482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1676 LQLGHATRQATEAQAATR----LMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLA 1751
Cdd:COG4646 1483 MDLDIEVLKLKLLDAAALeqlyAEEDKLRKSYLDEEEALEERIEAATKDLRLARAASQEEADEQESASKEAAAGEKKAAA 1562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1752 EQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAkkaitdAAMMAEELKKEQDTSAHLERM 1831
Cdd:COG4646 1563 AELLAALQAAGLIVLDGGRTPRGEKGGGLLARALLEAATLLLPIEEAEGSEGA------DATGDRRTGAAAEIELAAEAL 1636
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 578836100 1832 KKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKG 1888
Cdd:COG4646 1637 ILNLAERLERALRDGAEEEEIAPRELEAALKEEAALLARAGELAELELDKADLEAEL 1693
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1775-1976 |
2.48e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.01 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1775 QKKKLEADLAQLSGEVEEAAQERREAE--EKAKKAitdaammAEELKKEQD--TSAHLERMK----KTLEQTVRELQARL 1846
Cdd:PRK05035 442 EQEKKKAEEAKARFEARQARLEREKAAreARHKKA-------AEARAAKDKdaVAAALARVKakkaAATQPIVIKAGARP 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1847 EEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGV--RKHERRVKELAYQAEEDRKNLARMQDLVDklqSKV 1924
Cdd:PRK05035 515 DNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAkaKKAAQQAANAEAEEEVDPKKAAVAAAIAR---AKA 591
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578836100 1925 KSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDA 1976
Cdd:PRK05035 592 KKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDP 643
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1770-1978 |
2.60e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 41.63 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1770 TGLLNQKKKLEADLAQLSGEVEEAAQERREAEEK---AKKAITDAAMMAEEL-KKEQDTSAHLERMKKTLEQTVRELQAR 1845
Cdd:pfam06008 8 TGALPAPYKINYNLENLTKQLQEYLSPENAHKIQieiLEKELSSLAQETEELqKKATQTLAKAQQVNAESERTLGHAKEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1846 LEEAEQAAlrggkKQVQKLEAKVRELEAELDAE-----QKKHAEALKGVRkhERRVKELAYQAEEDRKNLARMQDLVDKL 1920
Cdd:pfam06008 88 AEAIKNLI-----DNIKEINEKVATLGENDFALpssdlSRMLAEAQRMLG--EIRSRDFGTQLQNAEAELKAAQDLLSRI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578836100 1921 QSKVKSYKRQFEEAEQQANTNLAKYrkaQHELDDAEERADMAET---QANKLRARTRDALG 1978
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEY---EAKLSDLRELLREAAAktrDANRLNLANQANLR 218
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
893-1211 |
2.67e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 893 QAEEELAALRAELRGLRGALaaaEAKRQELEETHVSITQEKNdlalQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELS 972
Cdd:COG4372 35 KALFELDKLQEELEQLREEL---EQAREELEQLEEELEQARS----ELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 973 ERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAH 1052
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1053 QQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKK 1132
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578836100 1133 DSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQRE 1211
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1733-1866 |
2.70e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1733 ELEELRAALEQgerSRRLAEQELLEATErlnllhsqntgLLNQKKKLEADLAQLSGEVEEA-AQERREAEEKAKKAItda 1811
Cdd:PRK00409 517 KLNELIASLEE---LERELEQKAEEAEA-----------LLKEAEKLKEELEEKKEKLQEEeDKLLEEAEKEAQQAI--- 579
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578836100 1812 ammaEELKKEQD----TSAHLERMKKTL--EQTVRELQARLEEAEQAALRGGKKQVQKLEA 1866
Cdd:PRK00409 580 ----KEAKKEADeiikELRQLQKGGYASvkAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1821-1903 |
2.75e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.02 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1821 EQDTSAHLERMKKTLEQTVRELQARLEEAEQAA--LRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKherRVKE 1898
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALAEAQQqeLVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQ---KRKE 220
|
....*
gi 578836100 1899 LAYQA 1903
Cdd:PRK11448 221 ITDQA 225
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
892-1352 |
3.04e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 892 AQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKndlALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKEL 971
Cdd:pfam12128 297 DQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDAD---IETAAADQEQLPSWQSELENLEERLKALTGKHQDV 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 972 SERLEdeeevnadlaaRRRKLEDEctELKKDIDDLELTLAK----AEKEKQATENKVKNLTEEM-AALDESVARLTKEKK 1046
Cdd:pfam12128 374 TAKYN-----------RRRSKIKE--QNNRDIAGIKDKLAKireaRDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEY 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1047 ALQEAhqqaLGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKL--------EGDLKLTQES--VA 1116
Cdd:pfam12128 441 RLKSR----LGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELrqarkrrdQASEALRQASrrLE 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1117 DAAQDKQQLEEKLKKKDSEL-----------SQLSLRVEDEQLLG----------------------------------A 1151
Cdd:pfam12128 517 ERQSALDELELQLFPQAGTLlhflrkeapdwEQSIGKVISPELLHrtdldpevwdgsvggelnlygvkldlkridvpewA 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1152 QMQKkikELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAA 1231
Cdd:pfam12128 597 ASEE---ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKAL 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1232 LRHEATVAALRRKQAEGAAELGEQvdsLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKasaeklcrtyEDQLSEAKIK 1311
Cdd:pfam12128 674 AERKDSANERLNSLEAQLKQLDKK---HQAWLEEQKEQKREARTEKQAYWQVVEGALDAQ----------LALLKAAIAA 740
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 578836100 1312 VEE-LQRQLADASTQRGR----LQTESGELSRLLEEKECLISQLSR 1352
Cdd:pfam12128 741 RRSgAKAELKALETWYKRdlasLGVDPDVIAKLKREIRTLERKIER 786
|
|
| PTZ00332 |
PTZ00332 |
paraflagellar rod protein; Provisional |
1533-1973 |
3.06e-03 |
|
paraflagellar rod protein; Provisional
Pssm-ID: 240364 [Multi-domain] Cd Length: 589 Bit Score: 42.64 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1533 LRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQEleKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQL 1612
Cdd:PTZ00332 146 LRRSQLDATQLAQVPTATLKNIEDIMNVTQIQNALASTDDQI--KTQLAQLEKTNEIQNVAMHDGEMQVAEEQMWTKVQL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1613 E--LSQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARnealRLKKKMEGDLNDLELQLGHATRQatEAQA 1690
Cdd:PTZ00332 224 QerLIELVADKFRLIGKCEEENKSFSKIHEVQKQANQETSQMKDAKR----RLKQRCETDLKHIHDAIQKADLE--DAEA 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1691 ATRLMQAQLKEEQAGRDEEQRlAAELHEQAQALERRASLLAAE-LEELRAALEQGERS--RRLAEQELLEATerlnllhS 1767
Cdd:PTZ00332 298 MKRYATNKEKSERFIRENEDR-QEEAWNKIQDLERQLQRLGTErFEEVKRRIEENDREekRRVEYQQFLEVA-------G 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1768 QNTGLLnQKKKLEADLA-QLSGEVEEAAQERREAEeKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARL 1846
Cdd:PTZ00332 370 QHKKLL-ELTVYNCDLAlRCTGLVEELVSEGCAAV-KARHDKTNQDLAALRLQVHKEHLEYFRMLYLTLGSLIYKKEKRL 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1847 EEAEqaalrggkKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRV-KELAYQAEEDRKNLARMQDLVDKLQSKVK 1925
Cdd:PTZ00332 448 EEID--------RNIRTTHIQLEFCVETFDPNAKKHADMKKELYKLRQGVeEELAMLKEKQAQALEMFKESEEALDAAGI 519
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 578836100 1926 SYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKlRART 1973
Cdd:PTZ00332 520 EFVHPVDENNEEVLTRRSKMVEYRSHLAKQEEVKIAAEREEIK-RARL 566
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
902-1161 |
3.55e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.48 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 902 RAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQ----DNLADAEERCHLLIKSKVQLEGKVKELSERLEd 977
Cdd:PRK10246 379 REQLRQWQQQLTHAEQKLNALPAITLTLTADEVAAALAQHAEQrplrQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQT- 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 978 eeEVNADLAARRRKLEDE---------CTELKKDIDDLE----------------------------LTLAKAEKEKQAT 1020
Cdd:PRK10246 458 --QRNAALNEMRQRYKEKtqqladvktICEQEARIKDLEaqraqlqagqpcplcgstshpaveayqaLEPGVNQSRLDAL 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1021 ENKVKNLTEEMAAL-------------DESVAR-LTKEKKALQEAHQQ---ALGDLQAEEDRVSALTKAKLRLEQQVEDL 1083
Cdd:PRK10246 536 EKEVKKLGEEGAALrgqldaltkqlqrDESEAQsLRQEEQALTQQWQAvcaSLNITLQPQDDIQPWLDAQEEHERQLRLL 615
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578836100 1084 ECSLEQEKKLRmDTERAKRKLEGDLKLTQESVADAAqdkQQLEEKLKKKDSELSQLSLRvEDEQLLGAQMQKKIKELQ 1161
Cdd:PRK10246 616 SQRHELQGQIA-AHNQQIIQYQQQIEQRQQQLLTAL---AGYALTLPQEDEEASWLATR-QQEAQSWQQRQNELTALQ 688
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1753-1976 |
4.09e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.98 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1753 QELLEATERLNLL--HSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAK------KAITDAAMMA---EELKKE 1821
Cdd:COG0497 135 QSLLDPDAQRELLdaFAGLEELLEEYREAYRAWRALKKELEELRADEAERARELDllrfqlEELEAAALQPgeeEELEEE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1822 QDTSAHLERmkktLEQTVRELQARLEEAEQAALRggkkQVQKLEAKVRELeAELDAEQKKHAEALKGVRkheRRVKELAY 1901
Cdd:COG0497 215 RRRLSNAEK----LREALQEALEALSGGEGGALD----LLGQALRALERL-AEYDPSLAELAERLESAL---IELEEAAS 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1902 Q-------AEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAeqqantnLAKYRKAQHEL---DDAEERADMAETQANKLRA 1971
Cdd:COG0497 283 ElrryldsLEFDPERLEEVEERLALLRRLARKYGVTVEEL-------LAYAEELRAELaelENSDERLEELEAELAEAEA 355
|
....*
gi 578836100 1972 RTRDA 1976
Cdd:COG0497 356 ELLEA 360
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1431-1976 |
4.19e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.04 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1431 RTEELEEAKKKLALRLQEAEEGVE-AANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKK---QRHLERALEERR 1506
Cdd:pfam05557 10 RLSQLQNEKKQMELEHKRARIELEkKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQaelNRLKKKYLEALN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1507 RQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEK 1586
Cdd:pfam05557 90 KKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1587 SEIQA-ALEEAEGALELEETKTlrIQLELSQVkAEVDRKLAEKDEECANLRRNH------QRAVESLQASLDAETRARNE 1659
Cdd:pfam05557 170 QRIKElEFEIQSQEQDSEIVKN--SKSELARI-PELEKELERLREHNKHLNENIenklllKEEVEDLKRKLEREEKYREE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1660 ALRL---KKKMEGDLNDLElQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQrlaAELHEQAQALERRASLLAAELEE 1736
Cdd:pfam05557 247 AATLeleKEKLEQELQSWV-KLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEEN---SSLTSSARQLEKARRELEQELAQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1737 LRAALEQgERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAE 1816
Cdd:pfam05557 323 YLKKIED-LNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1817 ELKKEQDTSAHLERMKKTLEqtvRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDaeqkkhaealkgvrKHERRV 1896
Cdd:pfam05557 402 QLSVAEEELGGYKQQAQTLE---RELQALRQQESLADPSYSKEEVDSLRRKLETLELERQ--------------RLREQK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1897 KELAYQAEedRKNLARMQDLVDklqSKV--------KSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERAD-------- 1960
Cdd:pfam05557 465 NELEMELE--RRCLQGDYDPKK---TKVlhlsmnpaAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLrlpettst 539
|
570
....*....|....*.
gi 578836100 1961 MAETQANKLRARTRDA 1976
Cdd:pfam05557 540 MNFKEVLDLRKELESA 555
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
964-1161 |
4.24e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 964 LEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDI----DDLELTLAKAEKEKQATENKVKNLTEEMAALDESVA 1039
Cdd:PHA02562 193 IQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIkaeiEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1040 RLTKEKKALQEAHQ--QALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKlRMDterakrklegdlkltqeSVAD 1117
Cdd:PHA02562 273 QFQKVIKMYEKGGVcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEE-IMD-----------------EFNE 334
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 578836100 1118 AAQDKQQLEEKLKKKDSELSQLSLRVEDeqllgaqMQKKIKELQ 1161
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLITLVDKAKK-------VKAAIEELQ 371
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
915-1120 |
4.32e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 915 AEAKRQELEETHVSITQEKNdlalqlqaeqdnlADAEErchllIKSKVQLEGKVKELSERLEDEEEVNAdlaaRRRKLED 994
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAK-------------KEAEA-----IKKEALLEAKEEIHKLRNEFEKELRE----RRNELQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 995 ECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDesvarltKEKKALQEAHQQALGDLQaeedRVSALTKAKL 1074
Cdd:PRK12704 87 LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE-------KKEEELEELIEEQLQELE----RISGLTAEEA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 578836100 1075 RlEQQVEDLECSLEQEKKLRMDTERAKRKLEGDlKLTQESVADAAQ 1120
Cdd:PRK12704 156 K-EILLEKVEEEARHEAAVLIKEIEEEAKEEAD-KKAKEILAQAIQ 199
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1301-1747 |
4.35e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 41.82 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1301 YEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLSRGKALAAQSLEELRRQLEEESKAKSALAH 1380
Cdd:COG5278 81 YEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1381 AVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKC 1460
Cdd:COG5278 161 LALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALAL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1461 SSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLRHGHEEA 1540
Cdd:COG5278 241 ALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1541 LEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQLELSQVKAE 1620
Cdd:COG5278 321 AAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1621 VDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQLK 1700
Cdd:COG5278 401 AAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAA 480
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 578836100 1701 EEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERS 1747
Cdd:COG5278 481 AAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALAS 527
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1730-1813 |
4.44e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.25 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1730 LAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSgevEEAAQERREAEEKAKKAIT 1809
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQ---EKAAETSQERKQKRKEITD 223
|
....
gi 578836100 1810 DAAM 1813
Cdd:PRK11448 224 QAAK 227
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1696-1847 |
4.56e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.20 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1696 QAQLKEEQAgRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGErsrrlaeQELLEATERLNLLHSQNTGLLNQ 1775
Cdd:cd22656 107 TDDEELEEA-KKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQ-------TALETLEKALKDLLTDEGGAIAR 178
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578836100 1776 K--KKLEADLAQLSgevEEAAQERREAEEKAKKAITDAammAEELKKEQDTSAHLERMKKTLEQTVRELQARLE 1847
Cdd:cd22656 179 KeiKDLQKELEKLN---EEYAAKLKAKIDELKALIADD---EAKLAAALRLIADLTAADTDLDNLLALIGPAIP 246
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1655-1963 |
5.04e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.78 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1655 RARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAEL 1734
Cdd:pfam02029 14 RAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1735 EELRAALEQGERSRRLAEQELLEATE----RLNLLHSQNTGLLN---QKKKLEADLAQLSGEVEEAAQERREAEEKAKKA 1807
Cdd:pfam02029 94 ADEKESVAERKENNEEEENSSWEKEEkrdsRLGRYKEEETEIREkeyQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTEN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1808 ITDAAMMAEELKKEQDTSahlERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEalK 1887
Cdd:pfam02029 174 FAKEEVKDEKIKKEKKVK---YESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAE--Q 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578836100 1888 GVRKHERRVKELAYQ-AEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQantnlAKYRKAQHELDDAEERADMAE 1963
Cdd:pfam02029 249 KLEELRRRRQEKESEeFEKLRQKQQEAELELEELKKKREERRKLLEEEEQR-----RKQEEAERKLREEEEKRRMKE 320
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1609-1743 |
5.23e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.19 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1609 RIQLELSQVKAEVDRKLAEKDEECANLRRNHQRA-----VESLQASLDaetRARNEALRLKKKMEGDL---NDLElqlgH 1680
Cdd:COG1566 80 DLQAALAQAEAQLAAAEAQLARLEAELGAEAEIAaaeaqLAAAQAQLD---LAQRELERYQALYKKGAvsqQELD----E 152
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578836100 1681 ATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQAlerrasllAAELEELRAALEQ 1743
Cdd:COG1566 153 ARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQA--------EAALAQAELNLAR 207
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1686-1868 |
5.89e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.87 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1686 TEAQAATRLMQAQLKEEQAgrdEEQRLAAELhEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELleATERLNLL 1765
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAQA---QVARLQAEL-DRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQL--AQAQIDLA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1766 HSQNT---GLLNQKKKLEAD--LAQLSGEVEEAAQERREAEEKAKKAITD-AAMMAEELKKEQDTSAhlermkkTLEQTV 1839
Cdd:pfam00529 128 RRRVLapiGGISRESLVTAGalVAQAQANLLATVAQLDQIYVQITQSAAEnQAEVRSELSGAQLQIA-------EAEAEL 200
|
170 180
....*....|....*....|....*....
gi 578836100 1840 RELQARLEEAEQAALRGGKkqVQKLEAKV 1868
Cdd:pfam00529 201 KLAKLDLERTEIRAPVDGT--VAFLSVTV 227
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1826-1981 |
6.03e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1826 AHLERMKKTLEQTVRELQARLEEAEqAALRGGKKQVQKLEAKVRELEAELDAEQ---KKHAEALKGVRKhERRVKELAYQ 1902
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALE-ARLEAAKTELEDLEKEIKRLELEIEEVEariKKYEEQLGNVRN-NKEYEALQKE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578836100 1903 AEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDALGPKL 1981
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPEL 176
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1078-1668 |
6.09e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1078 QQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLEEKlkkkDSELSQLSLRVEDEQLLGAQMQKKI 1157
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL----KEEIEELEKELESLEGSKRKLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1158 KELQARAEELEEELEAERAARARVEKQRAEAareleelserleeaggasagqregcrKREAELGRLRRELEEAALRHEAT 1237
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKELKEKA--------------------------EEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1238 VAALRRkQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKA--------SAEKLCRTYED---QLS 1306
Cdd:PRK03918 316 LSRLEE-EINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAkkeelerlKKRLTGLTPEKlekELE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1307 EAKIKVEELQRQLADASTQRGRLQTESGELSRLLEE-----KEC-----LISQLSRGKALAAQSleelrrqlEEESKAKS 1376
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakGKCpvcgrELTEEHRKELLEEYT--------AELKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1377 ALAHAVQALRHdcdlLREQHEEEAEAQAELQRLLskanaevaqwRSKYEADAIqrtEELEEAKKKLALrlqeaeEGVEAA 1456
Cdd:PRK03918 467 ELKEIEEKERK----LRKELRELEKVLKKESELI----------KLKELAEQL---KELEEKLKKYNL------EELEKK 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1457 NAKCSSLEKAKLRLQTESEDVTLELERatsaAAALDKKQRHLERALEERRRQEEEMQRELEAAQRES-RGLGTELFRLRH 1535
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELEK----LEELKKKLAELEKKLDELEEELAELLKELEELGFESvEELEERLKELEP 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1536 GHEEALEA------LETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLR 1609
Cdd:PRK03918 600 FYNEYLELkdaekeLEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLR 679
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 578836100 1610 IQLELSQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKME 1668
Cdd:PRK03918 680 AELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1264-1817 |
6.13e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.63 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1264 QKLEKEKSELRMEVDDLAANVETLT------RAKASAEKLCRTYEDQLSEAKIK--VEELQRQLADASTQRGRLQTESGE 1335
Cdd:pfam05483 172 KKYEYEREETRQVYMDLNNNIEKMIlafeelRVQAENARLEMHFKLKEDHEKIQhlEEEYKKEINDKEKQVSLLLIQITE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1336 -------LSRLLEEKECLISQLSRGKALAAQSLEELRRQLEEESKAKSALAHAVQ-------ALRHDCDLLREQHEEEAE 1401
Cdd:pfam05483 252 kenkmkdLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQrsmstqkALEEDLQIATKTICQLTE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1402 AQAELQRLLSKANAEVAQWRSKYEADAI----------QRTEELEEAKKKLALRLQ----EAEEGVEAANAKCSSLEKAK 1467
Cdd:pfam05483 332 EKEAQMEELNKAKAAHSFVVTEFEATTCsleellrteqQRLEKNEDQLKIITMELQkkssELEEMTKFKNNKEVELEELK 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1468 L--------------------RLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQRESRGLG 1527
Cdd:pfam05483 412 KilaedeklldekkqfekiaeELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELT 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1528 TELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEETKT 1607
Cdd:pfam05483 492 AHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKS 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1608 LRIQLELSQVKAEVDRKLAEKDEECANLRR---NHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQ 1684
Cdd:pfam05483 572 EENARSIEYEVLKKEKQMKILENKCNNLKKqieNKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQK 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1685 ATEaqaatrLMQAQLKEEQAGRDEEQRLAAELhEQAQALERRASLLAAELE-----ELRAALEQGERSRRLAEQELLEAT 1759
Cdd:pfam05483 652 FEE------IIDNYQKEIEDKKISEEKLLEEV-EKAKAIADEAVKLQKEIDkrcqhKIAEMVALMEKHKHQYDKIIEERD 724
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578836100 1760 ERLNLLHSQNTGLLNQKKKLEADLAQLSGEV----EEAAQERREAEEKAKKAITDAAMMAEE 1817
Cdd:pfam05483 725 SELGLYKNKEQEQSSAKAALEIELSNIKAELlslkKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1779-1958 |
6.80e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.26 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1779 LEADLAQLSGEVEEAAQE-RREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAeqaalRGG 1857
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEhKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELN-----RLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1858 KKQVQKLEAKVRELEA-ELDAEQKKHaeALKGvrkherRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQ 1936
Cdd:pfam05557 82 KKYLEALNKKLNEKESqLADAREVIS--CLKN------ELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQ 153
|
170 180
....*....|....*....|..
gi 578836100 1937 QantnLAKYRKAQHELDDAEER 1958
Cdd:pfam05557 154 L----RQNLEKQQSSLAEAEQR 171
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1795-1966 |
6.92e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.95 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1795 QERREAEEKAKKAITDAAMMAEELKKEQDtsahlermkktleqtvrELQARLEEAEQAALRGGKKQVQKLEAKVRELEAE 1874
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQA-----------------AEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1875 LDAE--QKKHAEALKGVRKHE-RRVKELAYQAEEDRKNLArmqdlvdKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHE 1951
Cdd:PRK09510 132 KQAEeaAAKAAAAAKAKAEAEaKRAAAAAKKAAAEAKKKA-------EAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAE 204
|
170
....*....|....*
gi 578836100 1952 LDDAEERADMAETQA 1966
Cdd:PRK09510 205 AEAKKKAAAEAKKKA 219
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
999-1160 |
7.11e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.89 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 999 LKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKAlQEAHQQALGDLQAeedRVSALTKAKLRLEQ 1078
Cdd:pfam13851 31 LKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLEN-YEKDKQSLKNLKA---RLKVLEKELKDLKW 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1079 QVEDLECSLEQekklrMDTERakrkleGDLKLTQESVADAAQDK------------QQLEEKLKKKDSELSQLSLRVEDE 1146
Cdd:pfam13851 107 EHEVLEQRFEK-----VERER------DELYDKFEAAIQDVQQKtglknlllekklQALGETLEKKEAQLNEVLAAANLD 175
|
170
....*....|....
gi 578836100 1147 QLLGAQMQKKIKEL 1160
Cdd:pfam13851 176 PDALQAVTEKLEDV 189
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
833-1145 |
7.41e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 833 VLTLLQARSRGrLMRLEyqRLLGGRDALfTIQWNIRAFNAVKNWSWMKLFFKMKplLRSAQAEEELAALRAELrGLRGAL 912
Cdd:PLN02939 144 ILLLNQARLQA-LEDLE--KILTEKEAL-QGKINILEMRLSETDARIKLAAQEK--IHVEILEEQLEKLRNEL-LIRGAT 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 913 AAAEAKRQELEethVSITQEKN----DLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLEDEEEVNADLAAR 988
Cdd:PLN02939 217 EGLCVHSLSKE---LDVLKEENmllkDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 989 R-----RKLE--------------------DECTELKKDIDDLELTLAKAEKEKQATEnKVKNLTEEMAALDESVARLTK 1043
Cdd:PLN02939 294 QydcwwEKVEnlqdlldratnqvekaalvlDQNQDLRDKVDKLEASLKEANVSKFSSY-KVELLQQKLKLLEERLQASDH 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1044 EKKALQEAHQQALGDLQaeeDRVSALTK--AKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLegdlkltqesvadAAQD 1121
Cdd:PLN02939 373 EIHSYIQLYQESIKEFQ---DTLSKLKEesKKRSLEHPADDMPSEFWSRILLLIDGWLLEKKI-------------SNND 436
|
330 340
....*....|....*....|....
gi 578836100 1122 KQQLEEKLKKKDSELSQLSLRVED 1145
Cdd:PLN02939 437 AKLLREMVWKRDGRIREAYLSCKG 460
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
895-1043 |
7.53e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 895 EEELAALRAELRGLRGALAAAEAKRQELEEthvSITQEKNDLAlQLQAEQDNLADAEERchlLIKSKVQLEGKVKELSER 974
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQD---SVANLRASLS-AAEAERSRLQALLAE---LAGAGAAAEGRAGELAQE 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 975 LEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEM-AALDESVARLTK 1043
Cdd:PRK09039 125 LDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLnVALAQRVQELNR 194
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
1730-1885 |
7.98e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 38.82 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1730 LAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKait 1809
Cdd:pfam12718 5 LKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNENLTRK--- 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578836100 1810 dAAMMAEELKKEQdtsahlERMKKTLEQtVRELQARLEEAEqaalrggkKQVQKLEAKVRELEAELDAEQKKHAEA 1885
Cdd:pfam12718 82 -IQLLEEELEESD------KRLKETTEK-LRETDVKAEHLE--------RKVQALEQERDEWEKKYEELEEKYKEA 141
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1685-1958 |
8.08e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.35 E-value: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1685 ATEAQAATrlMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNL 1764
Cdd:pfam10174 335 AKEQRAAI--LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1765 LHSQNTGLLNQKKKLEAD-------LAQLsgevEEAAQERREAEEKAKKAItdaammAEELKKEQDTSAHLERMKKTLEQ 1837
Cdd:pfam10174 413 KDKQLAGLKERVKSLQTDssntdtaLTTL----EEALSEKERIIERLKEQR------EREDRERLEELESLKKENKDLKE 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1838 TVRELQARLEEAEQAAL-----------RGGKKqvqklEAKVRELEAELdaeQKKHAEALKGVRKHERrvkelAYQAEED 1906
Cdd:pfam10174 483 KVSALQPELTEKESSLIdlkehasslasSGLKK-----DSKLKSLEIAV---EQKKEECSKLENQLKK-----AHNAEEA 549
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 578836100 1907 RKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEER 1958
Cdd:pfam10174 550 VRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKK 601
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1668-1800 |
8.35e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1668 EGDLNDLELQLGHATRQATEAQAATRlmQAQLKEEQAgRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGErs 1747
Cdd:PRK10636 509 DGDLEDYQQWLSDVQKQENQTDEAPK--ENNANSAQA-RKDQKRREAELRTQTQPLRKEIARLEKEMEKLNAQLAQAE-- 583
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 578836100 1748 RRLAEQELLEATERLNLlhsqnTGLLNQKKKLEADLAqlsgEVEEA---AQERREA 1800
Cdd:PRK10636 584 EKLGDSELYDQSRKAEL-----TACLQQQASAKSGLE----ECEMAwleAQEQLEQ 630
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1613-1826 |
8.48e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1613 ELSQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAAT 1692
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1693 RLMQAQLKEEQAGR--------DEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNl 1764
Cdd:COG3883 107 VLLGSESFSDFLDRlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA- 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578836100 1765 lhsqntGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSA 1826
Cdd:COG3883 186 ------QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
908-1104 |
8.59e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 908 LRGALAAAEAKRQELEEthvsitqekndlalQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLED-----EEEVN 982
Cdd:PRK04863 990 LRQRLEQAEQERTRARE--------------QLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDlgvpaDSGAE 1055
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 983 ADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDE----------SVARLTKEKKALQEAH 1052
Cdd:PRK04863 1056 ERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREqvvnakagwcAVLRLVKDNGVERRLH 1135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578836100 1053 QQALGDLQAEEDRvSALTKAKLRLEQQVEDLEcSLEQEKKLRMDTERAKRKL 1104
Cdd:PRK04863 1136 RRELAYLSADELR-SMSDKALGALRLAVADNE-HLRDVLRLSEDPKRPERKV 1185
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1640-1768 |
8.65e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.48 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1640 QRAVESLQASLDAETRARNEALRLKK---KMEGDLNDLELQLGHATRQATEAQAATRLMQAQLKeeQAGRDEEQR--LAA 1714
Cdd:pfam00529 57 QAALDSAEAQLAKAQAQVARLQAELDrlqALESELAISRQDYDGATAQLRAAQAAVKAAQAQLA--QAQIDLARRrvLAP 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578836100 1715 E--------LHEQAQALERRASLLA--AELEELRAALEQGER-SRRLAEQELLEATERLNLLHSQ 1768
Cdd:pfam00529 135 IggisreslVTAGALVAQAQANLLAtvAQLDQIYVQITQSAAeNQAEVRSELSGAQLQIAEAEAE 199
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1107-1296 |
9.53e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1107 DLKLTQESVADAAQDKQQLEEkLKKKDSELSQLSLRVE--DEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQ 1184
Cdd:COG4913 236 DLERAHEALEDAREQIELLEP-IRELAERYAAARERLAelEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578836100 1185 RAEAARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQ 1264
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE 394
|
170 180 190
....*....|....*....|....*....|..
gi 578836100 1265 KLEKEKSELRMEVDDLAANVETLTRAKASAEK 1296
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| |
