|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
1-564 |
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: 1168.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMN 80
Cdd:cd14927 133 MEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMN 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAY 160
Cdd:cd14927 213 PYDYHFCSQGVTTVDNMDDGEELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAY 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 161 LMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFE 240
Cdd:cd14927 293 LMGVSSADLLKGLLHPRVKVGNEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 241 IFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKvrrlrlsdvggphsysfcsq 320
Cdd:cd14927 373 IFEFNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEK-------------------- 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 321 PLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETV 400
Cdd:cd14927 433 PLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETV 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 401 VPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPG 480
Cdd:cd14927 513 VAIFQKSQNKLLATLYENYVGSDSTEDPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPG 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 481 VMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTFMDSRKATEKLLGSLDLDHTQYQFGHTK 560
Cdd:cd14927 593 VMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIPDDKFVDSRKATEKLLGSLDIDHTQYQFGHTK 672
|
....
gi 768017794 561 VFFK 564
Cdd:cd14927 673 VFFK 676
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
1-564 |
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: 1077.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMN 80
Cdd:cd01377 128 LEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGD 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAY 160
Cdd:cd01377 208 PSYYFFLSQGELTIDGVDDAEEFKLTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAH 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 161 LMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFE 240
Cdd:cd01377 288 LLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 241 IFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKvrrlrlsdvggphsysfcsQ 320
Cdd:cd01377 368 IFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEK-------------------P 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 321 PLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPrpdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETV 400
Cdd:cd01377 429 NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKP---KPKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENV 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 401 VPIFQKSQNRLLATLYENYAGScsteppKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPG 480
Cdd:cd01377 506 VALLKKSSDPLVASLFKDYEES------GGGGGKKKKKGGSFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPG 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 481 VMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDtFMDSRKATEKLLGSLDLDHTQYQFGHTK 560
Cdd:cd01377 580 KIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKG-FDDGKAACEKILKALQLDPELYRIGNTK 658
|
....
gi 768017794 561 VFFK 564
Cdd:cd01377 659 VFFK 662
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
1-564 |
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: 925.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKpELQDMLLLSMN 80
Cdd:cd14929 124 LEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSAN 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAY 160
Cdd:cd14929 203 PSDFHFCSCGAVAVESLDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAF 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 161 LMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFE 240
Cdd:cd14929 283 LMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 241 IFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKvrrlrlsdvggphsysfcsq 320
Cdd:cd14929 363 ILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEK-------------------- 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 321 PLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPDKKrKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETV 400
Cdd:cd14929 423 PMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKK-KFEAHFELVHYAGVVPYNISGWLEKNKDLLNETV 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 401 VPIFQKSQNRLLATLYENYAGSCSTEPpkSGVKeKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPG 480
Cdd:cd14929 502 VAVFQKSSNRLLASLFENYISTDSAIQ--FGEK-KRKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPG 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 481 VMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTFMDSRKATEKLLGSLDLDHTQYQFGHTK 560
Cdd:cd14929 579 VLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKFVSSRKAAEELLGSLEIDHTQYRFGITK 658
|
....
gi 768017794 561 VFFK 564
Cdd:cd14929 659 VFFK 662
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
1-564 |
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: 918.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMN 80
Cdd:cd14913 129 LEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTN 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAY 160
Cdd:cd14913 209 PYDYPFISQGEILVASIDDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAY 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 161 LMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFE 240
Cdd:cd14913 289 LMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFE 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 241 IFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKvrrlrlsdvggphsysfcsq 320
Cdd:cd14913 369 IFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEK-------------------- 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 321 PLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPDKKRKyQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETV 400
Cdd:cd14913 429 PMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRA-EAHFSLIHYAGTVDYSVSGWLEKNKDPLNETV 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 401 VPIFQKSQNRLLATLYENYAgscSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPG 480
Cdd:cd14913 508 VGLYQKSSNRLLAHLYATFA---TADADSGKKKVAKKKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPG 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 481 VMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTFMDSRKATEKLLGSLDLDHTQYQFGHTK 560
Cdd:cd14913 585 AMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDSKKACEKLLASIDIDHTQYKFGHTK 664
|
....
gi 768017794 561 VFFK 564
Cdd:cd14913 665 VFFK 668
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
1-564 |
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: 864.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMN 80
Cdd:cd14917 129 LEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNN 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAY 160
Cdd:cd14917 209 PYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAY 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 161 LMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFE 240
Cdd:cd14917 289 LMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFE 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 241 IFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKvrrlrlsdvggphsysfcsq 320
Cdd:cd14917 369 IFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEK-------------------- 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 321 PLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRpDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETV 400
Cdd:cd14917 429 PMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPR-NIKGKPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETV 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 401 VPIFQKSQNRLLATLYENYAGScstEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPG 480
Cdd:cd14917 508 VGLYQKSSLKLLSNLFANYAGA---DAPIEKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPG 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 481 VMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTFMDSRKATEKLLGSLDLDHTQYQFGHTK 560
Cdd:cd14917 585 VMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTK 664
|
....
gi 768017794 561 VFFK 564
Cdd:cd14917 665 VFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
1-564 |
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: 846.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMN 80
Cdd:cd14916 130 LEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNN 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAY 160
Cdd:cd14916 210 PYDYAFVSQGEVSVASIDDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAY 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 161 LMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFE 240
Cdd:cd14916 290 LMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 241 IFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKvrrlrlsdvggphsysfcsq 320
Cdd:cd14916 370 IFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEK-------------------- 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 321 PLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRpDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETV 400
Cdd:cd14916 430 PMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPR-NVKGKQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETV 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 401 VPIFQKSQNRLLATLYENYAGSCSTEPPKSgvKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPG 480
Cdd:cd14916 509 VGLYQKSSLKLMATLFSTYASADTGDSGKG--KGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPG 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 481 VMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTFMDSRKATEKLLGSLDLDHTQYQFGHTK 560
Cdd:cd14916 587 VMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTK 666
|
....
gi 768017794 561 VFFK 564
Cdd:cd14916 667 VFFK 670
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
1-564 |
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: 824.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMN 80
Cdd:cd14923 130 LEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTN 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAY 160
Cdd:cd14923 210 PFDFPFVSQGEVTVASIDDSEELLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGY 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 161 LMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFE 240
Cdd:cd14923 290 LMGLNSAEMLKGLCCPRVKVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 241 IFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKvrrlrlsdvggphsysfcsq 320
Cdd:cd14923 370 IFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEK-------------------- 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 321 PLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETV 400
Cdd:cd14923 430 PMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKP-AKGKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETV 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 401 VPIFQKSQNRLLATLYENYAGscsTEPPKSGVKEK--RKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKT 478
Cdd:cd14923 509 VGLYQKSSLKLLSFLFSNYAG---AEAGDSGGSKKggKKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKT 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 479 PGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTFMDSRKATEKLLGSLDLDHTQYQFGH 558
Cdd:cd14923 586 PGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQFIDSKNASEKLLNSIDVDREQYRFGH 665
|
....*.
gi 768017794 559 TKVFFK 564
Cdd:cd14923 666 TKVFFK 671
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
1-564 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 820.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmN 80
Cdd:pfam00063 135 LEAFGNAKTVRNNNSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLT-N 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQ-GVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAA 159
Cdd:pfam00063 214 PKDYHYLSQsGCYTIDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAA 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 160 YLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAG 238
Cdd:pfam00063 294 SLLGIDSTELEKALCKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDvKTIEKASFIGVLDIYG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 239 FEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIEKvrrlrlsdvggphsysfc 318
Cdd:pfam00063 374 FEIFEKNSFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEK------------------ 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 319 sQPLGILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQPRPdkkrKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNE 398
Cdd:pfam00063 435 -KPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHFQKPRL----QGETHFIIKHYAGDVEYNVEGFLEKNKDPLND 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 399 TVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVK-EKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENK 477
Cdd:pfam00063 509 DLVSLLKSSSDPLLAELFPDYETAESAAANESGKStPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKK 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 478 TPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDtFMDSRKATEKLLGSLDLDHTQYQFG 557
Cdd:pfam00063 589 RAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFG 667
|
....*..
gi 768017794 558 HTKVFFK 564
Cdd:pfam00063 668 KTKIFFR 674
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
1-564 |
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: 812.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMN 80
Cdd:cd14918 129 LEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTN 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAY 160
Cdd:cd14918 209 PYDYAFVSQGEITVPSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAY 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 161 LMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFE 240
Cdd:cd14918 289 LQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFE 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 241 IFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKvrrlrlsdvggphsysfcsq 320
Cdd:cd14918 369 IFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEK-------------------- 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 321 PLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETV 400
Cdd:cd14918 429 PLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKV-VKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTV 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 401 VPIFQKSQNRLLATLYENYAgscSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPG 480
Cdd:cd14918 508 VGLYQKSAMKTLASLFSTYA---SAEADSGAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPG 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 481 VMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTFMDSRKATEKLLGSLDLDHTQYQFGHTK 560
Cdd:cd14918 585 AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTK 664
|
....
gi 768017794 561 VFFK 564
Cdd:cd14918 665 VFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
1-564 |
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: 811.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMN 80
Cdd:cd14909 127 LEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDN 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAY 160
Cdd:cd14909 207 IYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 161 LMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFE 240
Cdd:cd14909 287 LFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 241 IFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKvrrlrlsdvggphsysfcsq 320
Cdd:cd14909 367 IFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEK-------------------- 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 321 PLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETV 400
Cdd:cd14909 427 PMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTV 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 401 VPIFQKSQNRLLATLYENYAGscSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPG 480
Cdd:cd14909 507 VDQFKKSQNKLLIEIFADHAG--QSGGGEQAKGGRGKKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPG 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 481 VMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTfmDSRKATEKLLGSLDLDHTQYQFGHTK 560
Cdd:cd14909 585 VVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE--DPKKAAEIILESIALDPDQYRLGHTK 662
|
....
gi 768017794 561 VFFK 564
Cdd:cd14909 663 VFFR 666
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
1-564 |
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: 810.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMN 80
Cdd:cd14910 131 LEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTN 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAY 160
Cdd:cd14910 211 PYDYAFVSQGEITVPSIDDQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAY 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 161 LMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFE 240
Cdd:cd14910 291 LQNLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFE 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 241 IFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKvrrlrlsdvggphsysfcsq 320
Cdd:cd14910 371 IFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEK-------------------- 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 321 PLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETV 400
Cdd:cd14910 431 PMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKP-AKGKVEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETV 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 401 VPIFQKSQNRLLATLyenYAGSCSTEPPKSGVKE-KRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTP 479
Cdd:cd14910 510 VGLYQKSSMKTLALL---FSGAAAAEAEEGGGKKgGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTP 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 480 GVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTFMDSRKATEKLLGSLDLDHTQYQFGHT 559
Cdd:cd14910 587 GAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHT 666
|
....*
gi 768017794 560 KVFFK 564
Cdd:cd14910 667 KVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
1-564 |
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: 810.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMN 80
Cdd:cd14915 131 LEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTN 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAY 160
Cdd:cd14915 211 PYDFAFVSQGEITVPSIDDQEELMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAY 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 161 LMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFE 240
Cdd:cd14915 291 LTSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFE 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 241 IFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKvrrlrlsdvggphsysfcsq 320
Cdd:cd14915 371 IFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEK-------------------- 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 321 PLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETV 400
Cdd:cd14915 431 PMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKP-AKGKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETV 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 401 VPIFQKSQNRLLATLYEnyAGSCSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPG 480
Cdd:cd14915 510 VGLYQKSGMKTLAFLFS--GGQTAEAEGGGGKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPG 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 481 VMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTFMDSRKATEKLLGSLDLDHTQYQFGHTK 560
Cdd:cd14915 588 AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTK 667
|
....
gi 768017794 561 VFFK 564
Cdd:cd14915 668 VFFK 671
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
1-564 |
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: 808.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMN 80
Cdd:cd14934 125 LEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPN 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAY 160
Cdd:cd14934 205 PKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAH 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 161 LMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFE 240
Cdd:cd14934 285 LMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 241 IFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKvrrlrlsdvggphsysfcsq 320
Cdd:cd14934 365 IFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEK-------------------- 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 321 PLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETV 400
Cdd:cd14934 425 PMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKGPEAHFELVHYAGTVGYNITGWLEKNKDPLNETV 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 401 VPIFQKSQNRLLATLYENyagscstEPPKSGVKeKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPG 480
Cdd:cd14934 505 VGLFQKSSLGLLALLFKE-------EEAPAGSK-KQKRGSSFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSG 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 481 VMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDtFMDSRKATEKLLGSLDLDHTQYQFGHTK 560
Cdd:cd14934 577 VVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-FVDNKKASELLLGSIDLDVNEYKIGHTK 655
|
....
gi 768017794 561 VFFK 564
Cdd:cd14934 656 VFFR 659
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
1-564 |
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: 802.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMN 80
Cdd:cd14912 131 LEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTN 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAY 160
Cdd:cd14912 211 PYDYPFVSQGEISVASIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAY 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 161 LMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFE 240
Cdd:cd14912 291 LQSLNSADLLKALCYPRVKVGNEYVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFE 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 241 IFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKvrrlrlsdvggphsysfcsq 320
Cdd:cd14912 371 IFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEK-------------------- 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 321 PLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETV 400
Cdd:cd14912 431 PMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKV-VKGKAEAHFSLIHYAGVVDYNITGWLDKNKDPLNETV 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 401 VPIFQKSQNRLLATLYENyAGSCSTEPPKSGVKE-KRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTP 479
Cdd:cd14912 510 VGLYQKSAMKTLAYLFSG-AQTAEGASAGGGAKKgGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTP 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 480 GVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTFMDSRKATEKLLGSLDLDHTQYQFGHT 559
Cdd:cd14912 589 GAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHT 668
|
....*
gi 768017794 560 KVFFK 564
Cdd:cd14912 669 KVFFK 673
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
1-576 |
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: 782.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMn 80
Cdd:smart00242 140 LEAFGNAKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQG-VITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEA-DGTESADKA 158
Cdd:smart00242 219 PEDYRYLNQGgCLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTvKDKEELSNA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 159 AYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAG 238
Cdd:smart00242 299 AELLGVDPEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYG 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 239 FEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIEKvrrlrlsdvggphsysfc 318
Cdd:smart00242 379 FEIFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEK------------------ 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 319 sQPLGILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQPRpdkkRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNE 398
Cdd:smart00242 440 -KPPGILSLLDEECRFPKGTDQTFLEKLNQHH-KKHPHFSKPK----KKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSD 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 399 TVVPIFQKSQNRLLATLYENYAGScsteppksgvKEKRKKaasFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKT 478
Cdd:smart00242 514 DLIELLQSSKNPLIASLFPSGVSN----------AGSKKR---FQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKK 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 479 PGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTfMDSRKATEKLLGSLDLDHTQYQFGH 558
Cdd:smart00242 581 PGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWG-GDAKKACEALLQSLGLDEDEYQLGK 659
|
570
....*....|....*...
gi 768017794 559 TKVFFKAGLLGVLEELRD 576
Cdd:smart00242 660 TKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1-897 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 674.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmN 80
Cdd:COG5022 201 LEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQ-N 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQG-VITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKqKQREEQAEADGTESADKAA 159
Cdd:COG5022 280 PKDYIYLSQGgCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKAC 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 160 YLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGF 239
Cdd:COG5022 359 YLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGF 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 240 EIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEKvrrlrlsdvggphsysfcS 319
Cdd:COG5022 439 EIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY-FDNQPCIDLIEK------------------K 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 320 QPLGILSILEEECMFPKASDASFRAKLYDN-HAGKSPNFQqprpdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNE 398
Cdd:COG5022 500 NPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFK-----KSRFRDNKFVVKHYAGDVEYDVEGFLDKNKDPLND 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 399 TVVPIFQKSQNRLLATLYENYagscsteppksgvkEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKT 478
Cdd:COG5022 575 DLLELLKASTNEFVSTLFDDE--------------ENIESKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKS 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 479 PGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTFM---DSRKATEKLLGSLDLDHTQYQ 555
Cdd:COG5022 641 PWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTwkeDTKNAVKSILEELVIDSSKYQ 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 556 FGHTKVFFKAGLLGVLEELRDQRLAKVLTLLQARSRGRLMRLEYQRLLGGRDALFTIQWNIRAFNAVKNWSWMKLFFKMK 635
Cdd:COG5022 721 IGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQ 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 636 PLLRSAQAEEELAALRAELRGLRGALaAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEG 715
Cdd:COG5022 801 PLLSLLGSRKEYRSYLACIIKLQKTI-KREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVEL 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 716 KVKELSERLEDEEEVNAdLAARRRKLEDECTELKKDID-----DLELTLAKAEKEKQATEN-KVKNLTEEMAALDESVAR 789
Cdd:COG5022 880 AERQLQELKIDVKSISS-LKLVNLELESEIIELKKSLSsdlieNLEFKTELIARLKKLLNNiDLEEGPSIEYVKLPELNK 958
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 790 LTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQE----SVA 865
Cdd:COG5022 959 LHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSAskiiSSE 1038
|
890 900 910
....*....|....*....|....*....|...
gi 768017794 866 DAAQDKQQLEEKLKKK-DSELSQLSLRVEDEQL 897
Cdd:COG5022 1039 STELSILKPLQKLKGLlLLENNQLQARYKALKL 1071
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
1-564 |
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: 653.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMN 80
Cdd:cd00124 127 LEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHF----CSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREE--QAEADGTES 154
Cdd:cd00124 207 LSYYYLndylNSSGCDRIDGVDDAEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDES 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 155 ADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQF--FIG 232
Cdd:cd00124 287 LKAAAKLLGVDAEDLEEALTTRTIKVGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEStsFIG 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 233 VLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEKvrrlrlsdvggp 312
Cdd:cd00124 367 ILDIFGFENFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEG------------ 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 313 hsysfcsQPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFqqprpDKKRKYQAHFEVVHYAGVVPYSIVGWLEKN 392
Cdd:cd00124 434 -------KPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFF-----SKKRKAKLEFGIKHYAGDVTYDADGFLEKN 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 393 KDPLNETVVPIFQKSqnrllatlyenyagscsteppksgvkekrkkaASFqtvsqlhKENLNKLMTNLRATQPHFVRCIV 472
Cdd:cd00124 502 KDTLPPDLVDLLRSG--------------------------------SQF-------RSQLDALMDTLNSTQPHFVRCIK 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 473 PNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDtFMDSRKATEKLLGSLDLDHT 552
Cdd:cd00124 543 PNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEKA-SDSKKAAVLALLLLLKLDSS 621
|
570
....*....|..
gi 768017794 553 QYQFGHTKVFFK 564
Cdd:cd00124 622 GYQLGKTKVFLR 633
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
1-564 |
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: 623.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmN 80
Cdd:cd14911 136 LEAFGNAKTVKNDNSSRFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-D 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAY 160
Cdd:cd14911 215 VKSYAFLSNGSLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAH 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 161 LMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAGF 239
Cdd:cd14911 295 LLGLSVTDMTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGF 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 240 EIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKvrrlrlsdvggphsysfcs 319
Cdd:cd14911 375 EIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDK------------------- 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 320 qPLGILSILEEECMFPKASDASFRAKLYDNHAgKSPNFqqprpdKKRKYQ--AHFEVVHYAGVVPYSIVGWLEKNKDPLN 397
Cdd:cd14911 436 -PGGIMALLDEECWFPKATDKTFVDKLVSAHS-MHPKF------MKTDFRgvADFAIVHYAGRVDYSAAKWLMKNMDPLN 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 398 ETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVK-EKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNEN 476
Cdd:cd14911 508 ENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQfGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHE 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 477 KTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDtFMDSRKATEKLLGSLDLDHTQYQF 556
Cdd:cd14911 588 KRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKG-FMDGKKACEKMIQALELDSNLYRV 666
|
....*...
gi 768017794 557 GHTKVFFK 564
Cdd:cd14911 667 GQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
1-564 |
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: 610.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQ-DMLLLSM 79
Cdd:cd14920 127 LESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKsDLLLEGF 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 80 NpyDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAA 159
Cdd:cd14920 207 N--NYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLC 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 160 YLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAG 238
Cdd:cd14920 285 HLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 239 FEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKVrrlrlsdvggphsysfc 318
Cdd:cd14920 365 FEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERP----------------- 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 319 SQPLGILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQPRpdkKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNE 398
Cdd:cd14920 428 ANPPGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPR---QLKDKADFCIIHYAGKVDYKADEWLMKNMDPLND 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 399 TVVPIFQKSQNRLLATLYENY-----AGSCSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVP 473
Cdd:cd14920 504 NVATLLHQSSDRFVAELWKDVdrivgLDQVTGMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIP 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 474 NENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPdDTFMDSRKATEKLLGSLDLDHTQ 553
Cdd:cd14920 584 NHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIP-KGFMDGKQACERMIRALELDPNL 662
|
570
....*....|.
gi 768017794 554 YQFGHTKVFFK 564
Cdd:cd14920 663 YRIGQSKIFFR 673
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
1-564 |
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: 567.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGR-KPELQDmLLLSM 79
Cdd:cd01380 122 MEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAAsLPELKE-LHLGS 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 80 NPYDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAA 159
Cdd:cd01380 201 AEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIAC 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 160 YLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQF--FIGVLDIA 237
Cdd:cd01380 281 ELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhsFIGVLDIY 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 238 GFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEKvrrlrlsdvggphsysf 317
Cdd:cd01380 361 GFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEG----------------- 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 318 csqPLGILSILEEECMFPKASDASFRAKLYDNHAGK-SPNFQQPRPDKKRkyqahFEVVHYAGVVPYSIVGWLEKNKDPL 396
Cdd:cd01380 423 ---KLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTA-----FIVKHFADDVEYQVEGFLEKNRDTV 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 397 NETVVPIFQKSQNRllatlyenyagscsteppksgvkekrKKaasfqTVSQLHKENLNKLMTNLRATQPHFVRCIVPNEN 476
Cdd:cd01380 495 SEEHLNVLKASKNR--------------------------KK-----TVGSQFRDSLILLMETLNSTTPHYVRCIKPNDE 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 477 KTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAipDDTFMDSRKATEKLLGSLDLDHTQYQF 556
Cdd:cd01380 544 KLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSK--EWLRDDKKKTCENILENLILDPDKYQF 621
|
....*...
gi 768017794 557 GHTKVFFK 564
Cdd:cd01380 622 GKTKIFFR 629
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
1-564 |
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: 560.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmN 80
Cdd:cd14932 131 LEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLE-D 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAY 160
Cdd:cd14932 210 YSKYRFLSNGNVTIPGQQDKELFAETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCH 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 161 LMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAGF 239
Cdd:cd14932 290 LLGMNVTDFTRAILSPRIKVGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGF 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 240 EIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKVrrlrlsdvggphsysfcS 319
Cdd:cd14932 370 EIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKP-----------------N 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 320 QPLGILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQPrpdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNET 399
Cdd:cd14932 433 GPPGILALLDEECWFPKATDKSFVEKVVQEQ-GNNPKFQKP---KKLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNEN 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 400 VVPIFQKSQNRLLATLYENY---------AGSCSTEppkSGVKEKRKkaASFQTVSQLHKENLNKLMTNLRATQPHFVRC 470
Cdd:cd14932 509 VATLLNQSTDKFVSELWKDVdrivgldkvAGMGESL---HGAFKTRK--GMFRTVGQLYKEQLMNLMTTLRNTNPNFVRC 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 471 IVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDtFMDSRKATEKLLGSLDLD 550
Cdd:cd14932 584 IIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACVLMVKALELD 662
|
570
....*....|....
gi 768017794 551 HTQYQFGHTKVFFK 564
Cdd:cd14932 663 PNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
1-564 |
1.74e-174 |
|
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: 543.07 E-value: 1.74e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQ-DMLLLSM 79
Cdd:cd14921 127 LEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRsDLLLEGF 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 80 NpyDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAA 159
Cdd:cd14921 207 N--NYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVC 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 160 YLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAG 238
Cdd:cd14921 285 HLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 239 FEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKVrrlrlsdvggphsysfc 318
Cdd:cd14921 365 FEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERP----------------- 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 319 SQPLGILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQPrpdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNE 398
Cdd:cd14921 428 NNPPGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKP---KQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLND 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 399 TVVPIFQKSQNRLLATLYEN---------YAGSCSTEPPKSgvkeKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVR 469
Cdd:cd14921 504 NVTSLLNASSDKFVADLWKDvdrivgldqMAKMTESSLPSA----SKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVR 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 470 CIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDtFMDSRKATEKLLGSLDL 549
Cdd:cd14921 580 CIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKG-FMDGKQACILMIKALEL 658
|
570
....*....|....*
gi 768017794 550 DHTQYQFGHTKVFFK 564
Cdd:cd14921 659 DPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
1-564 |
3.67e-172 |
|
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: 536.96 E-value: 3.67e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmN 80
Cdd:cd15896 131 LEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLE-N 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAY 160
Cdd:cd15896 210 YNNYRFLSNGNVTIPGQQDKDLFTETMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCH 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 161 LMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAGF 239
Cdd:cd15896 290 LMGMNVTDFTRAILSPRIKVGRDYVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGF 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 240 EIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKvrrlrlsdvggPHSysfcs 319
Cdd:cd15896 370 EIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEK-----------PAS----- 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 320 qPLGILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQPrpdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNET 399
Cdd:cd15896 434 -PPGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKP---KKLKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDN 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 400 VVPIFQKSQNRLLATLYENYAGSCSTEpPKSGVKEK----RKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNE 475
Cdd:cd15896 509 VATLLNQSTDKFVSELWKDVDRIVGLD-KVSGMSEMpgafKTRKGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNH 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 476 NKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDtFMDSRKATEKLLGSLDLDHTQYQ 555
Cdd:cd15896 588 EKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACVLMIKSLELDPNLYR 666
|
....*....
gi 768017794 556 FGHTKVFFK 564
Cdd:cd15896 667 IGQSKVFFR 675
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
1-564 |
2.62e-171 |
|
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: 534.29 E-value: 2.62e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmn 80
Cdd:cd14919 124 LEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLE-- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYD-YHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAA 159
Cdd:cd14919 202 PYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVS 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 160 YLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAG 238
Cdd:cd14919 282 HLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAG 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 239 FEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKVrrlrlsdvggphsysfc 318
Cdd:cd14919 362 FEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKP----------------- 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 319 SQPLGILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQPrpdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNE 398
Cdd:cd14919 425 AGPPGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKP---KQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLND 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 399 TVVPIFQKSQNRLLATLYEN---------YAGSCSTEPPksGVKEKRKkaASFQTVSQLHKENLNKLMTNLRATQPHFVR 469
Cdd:cd14919 501 NIATLLHQSSDKFVSELWKDvdriigldqVAGMSETALP--GAFKTRK--GMFRTVGQLYKEQLAKLMATLRNTNPNFVR 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 470 CIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDtFMDSRKATEKLLGSLDL 549
Cdd:cd14919 577 CIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKG-FMDGKQACVLMIKALEL 655
|
570
....*....|....*
gi 768017794 550 DHTQYQFGHTKVFFK 564
Cdd:cd14919 656 DSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
1-564 |
7.35e-167 |
|
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: 522.35 E-value: 7.35e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMN 80
Cdd:cd14930 127 LEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPC 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYdYHFCSQGVITVDNmNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAY 160
Cdd:cd14930 207 SH-YRFLTNGPSSSPG-QERELFQETLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCR 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 161 LMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDtKLPRQ--FFIGVLDIAG 238
Cdd:cd14930 285 LLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAG 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 239 FEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKVrrlrlsdvggphsysfc 318
Cdd:cd14930 364 FEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERP----------------- 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 319 SQPLGILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQPRpdkKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNE 398
Cdd:cd14930 427 ANPPGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPR---HLRDQADFSVLHYAGKVDYKANEWLMKNMDPLND 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 399 TVVPIFQKSQNRLLATLYENYAGSCSTEPPKS---GVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNE 475
Cdd:cd14930 503 NVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSlgdGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNH 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 476 NKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDtFMDSRKATEKLLGSLDLDHTQYQ 555
Cdd:cd14930 583 EKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYR 661
|
....*....
gi 768017794 556 FGHTKVFFK 564
Cdd:cd14930 662 VGQSKIFFR 670
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
1-564 |
1.43e-165 |
|
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: 518.25 E-value: 1.43e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMN 80
Cdd:cd01378 122 LEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRP 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADgTESADKAAY 160
Cdd:cd01378 202 EQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAY 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 161 LMGVSSGDLLKGLLHPRVRVGNEY---VTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQ-FFIGVLDI 236
Cdd:cd01378 281 LLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDI 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 237 AGFEIFEFNSFEQLCINFTNEKLQQFFNQhmFVL--EQEEYKREGIDWVFIDFgLDLQPCIDLIEKvrrlrlsdvggphs 314
Cdd:cd01378 361 YGFEIFEKNSFEQFCINYVNEKLQQIFIE--LTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEE-------------- 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 315 ysfcsQPLGILSILEEECMFP-KASDASFRAKLydNHAGKSPNFQQPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNK 393
Cdd:cd01378 424 -----KPPGIFAILDDACLTAgDATDQTFLQKL--NQLFSNHPHFECPSGHFELRRGEFRIKHYAGDVTYNVEGFLDKNK 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 394 DPLNETVVPIFQKSQNRLLATLYEnyagscstEPPKSGVKeKRKKAASFQTvsqlhKENLNKLMTNLRATQPHFVRCIVP 473
Cdd:cd01378 497 DLLFKDLKELMQSSSNPFLRSLFP--------EGVDLDSK-KRPPTAGTKF-----KNSANALVETLMKKQPSYIRCIKP 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 474 NENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTfMDSRKATEKLLGSLDLDHTQ 553
Cdd:cd01378 563 NDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWD-GTWQGGVESILKDLNIPPEE 641
|
570
....*....|.
gi 768017794 554 YQFGHTKVFFK 564
Cdd:cd01378 642 YQMGKTKIFIR 652
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
1-564 |
6.40e-165 |
|
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: 516.42 E-value: 6.40e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMn 80
Cdd:cd01381 118 LEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGD- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQG-VITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQRE--EQAEADGTESADK 157
Cdd:cd01381 197 ASDYYYLTQGnCLTCEGRDDAAEFADIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLER 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 158 AAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFF---IGVL 234
Cdd:cd01381 277 AAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 235 DIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIekvrrlrlsdvggphs 314
Cdd:cd01381 357 DIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLI---------------- 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 315 ysfCSQPLGILSILEEECMFPKASDASFRAKLYDNHAGKSpNFQQPrpdkKRKYQAHFEVVHYAGVVPYSIVGWLEKNKD 394
Cdd:cd01381 420 ---ALKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNK-NYLKP----KSDLNTSFGINHFAGVVFYDTRGFLEKNRD 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 395 PLNETVVPIFQKSQNRLLATLYENYAGSCSteppksgvkEKRKKAasfQTVSQLHKENLNKLMTNLRATQPHFVRCIVPN 474
Cdd:cd01381 492 TFSADLLQLVQSSKNKFLKQLFNEDISMGS---------ETRKKS---PTLSSQFRKSLDQLMKTLSACQPFFVRCIKPN 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 475 ENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSaIPDDTFMDSRKATEKLLGSLDLDHTQY 554
Cdd:cd01381 560 EYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPG-IPPAHKTDCRAATRKICCAVLGGDADY 638
|
570
....*....|
gi 768017794 555 QFGHTKVFFK 564
Cdd:cd01381 639 QLGKTKIFLK 648
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
1-564 |
6.84e-160 |
|
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: 503.39 E-value: 6.84e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRK--PELQDMLLLS 78
Cdd:cd14883 118 LEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKEKLKLG 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 79 mNPYDYHFCSQ-GVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAE-ADGTESAD 156
Cdd:cd14883 198 -EPEDYHYLNQsGCIRIDNINDKKDFDHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILK 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 157 KAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDI 236
Cdd:cd14883 277 IVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDI 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 237 AGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIEKvrrlrlsdvggphsys 316
Cdd:cd14883 357 FGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEK---------------- 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 317 fcsQPLGILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQPrpdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPL 396
Cdd:cd14883 420 ---PPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKP---DRRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQ 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 397 NETVVPIFQKSQNRLLATL--YENYAGSCSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPN 474
Cdd:cd14883 493 QDDLFDLMSRSKNKFVKELftYPDLLALTGLSISLGGDTTSRGTSKGKPTVGDTFKHQLQSLVDVLSATQPWYVRCIKPN 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 475 ENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTfMDSRKATEKLLGSLDLDHTQY 554
Cdd:cd14883 573 SLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSADH-KETCGAVRALMGLGGLPEDEW 651
|
570
....*....|
gi 768017794 555 QFGHTKVFFK 564
Cdd:cd14883 652 QVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
1-564 |
2.00e-157 |
|
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: 496.07 E-value: 2.00e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMn 80
Cdd:cd01383 116 LEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQ-GVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAA 159
Cdd:cd01383 195 ASEYKYLNQsNCLTIDGVDDAKKFHELKEALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAA 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 160 YLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDT-KLPRQFFIGVLDIAG 238
Cdd:cd01383 275 SLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYG 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 239 FEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEKvrrlrlsdvggphsysfc 318
Cdd:cd01383 355 FESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEK------------------ 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 319 sQPLGILSILEEECMFPKASDASFRAKLyDNHAGKSPNFqqprpdKKRKYQAhFEVVHYAGVVPYSIVGWLEKNKDPLNE 398
Cdd:cd01383 416 -KPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCF------KGERGGA-FTIRHYAGEVTYDTSGFLEKNRDLLHS 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 399 TVVPIFQKSQNRLLATLYENYAGSCSTEPPKSgvkeKRKKAASF-QTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENK 477
Cdd:cd01383 487 DLIQLLSSCSCQLPQLFASKMLDASRKALPLT----KASGSDSQkQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQ 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 478 TPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTfmDSRKATEKLLGSLDLDHTQYQFG 557
Cdd:cd01383 563 LPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQ--DPLSTSVAILQQFNILPEMYQVG 640
|
....*..
gi 768017794 558 HTKVFFK 564
Cdd:cd01383 641 YTKLFFR 647
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
1-564 |
1.39e-145 |
|
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: 464.07 E-value: 1.39e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmN 80
Cdd:cd01384 123 LEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLK-D 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQ-GVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKqkqreEQAEADGTESADK-- 157
Cdd:cd01384 202 PKQFHYLNQsKCFELDGVDDAEEYRATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFS-----KGEEDDSSVPKDEks 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 158 ------AAYLMGVSSGDLLKGLLHpRVRVG-NEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFF 230
Cdd:cd01384 277 efhlkaAAELLMCDEKALEDALCK-RVIVTpDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRL 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 231 IGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEKvrrlrlsdvg 310
Cdd:cd01384 356 IGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK---------- 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 311 gphsysfcsQPLGILSILEEECMFPKASDASFRAKLYDNHAGKspnfqqPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLE 390
Cdd:cd01384 425 ---------KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDH------KRFSKPKLSRTDFTIDHYAGDVTYQTDLFLD 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 391 KNKDplneTVVP----IFQKSQNRLLATLYenyagscstePPKSGvkEKRKKAASFQTVSQLHKENLNKLMTNLRATQPH 466
Cdd:cd01384 490 KNKD----YVVAehqaLLNASKCPFVAGLF----------PPLPR--EGTSSSSKFSSIGSRFKQQLQELMETLNTTEPH 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 467 FVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAipDDTFMDSRKATEKLLGS 546
Cdd:cd01384 554 YIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEV--LKGSDDEKAACKKILEK 631
|
570
....*....|....*...
gi 768017794 547 LDLDhtQYQFGHTKVFFK 564
Cdd:cd01384 632 AGLK--GYQIGKTKVFLR 647
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
1-564 |
2.95e-134 |
|
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: 433.73 E-value: 2.95e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHF---------GPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSG----- 66
Cdd:cd14888 122 LEAFGNARTLRNDNSSRFGKFIELQFsklkskrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAareak 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 67 ------------------RKPELQDMLL-LSMNPYDYHFCSqGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIV 127
Cdd:cd14888 202 ntglsyeendeklakgadAKPISIDMSSfEPHLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIV 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 128 GALLHFGNMKFKQKQREEQA---EADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKA 204
Cdd:cd14888 281 AAILYLGNILFENNEACSEGavvSASCTDDLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARA 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 205 TYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWV 283
Cdd:cd14888 361 LYSCLFDKVVERTNESIGySKDNSLLFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWN 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 284 FIDFGlDLQPCIDLIEkvrrlrlsdvggphsysfcSQPLGILSILEEECMFPKASDASFRAKLYDNHAGKSpnfqqpRPD 363
Cdd:cd14888 441 PLDFP-DNQDCVDLLQ-------------------EKPLGIFCMLDEECFVPGGKDQGLCNKLCQKHKGHK------RFD 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 364 KKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPksgvkEKRKkaasFQ 443
Cdd:cd14888 495 VVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSAYLRRGTDGNT-----KKKK----FV 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 444 TVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRIL 523
Cdd:cd14888 566 TVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRIL 645
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 768017794 524 NPsaipddtfmdsrkatekllGSLDLDHTQYQFGHTKVFFK 564
Cdd:cd14888 646 LN-------------------GEGKKQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
1-564 |
1.33e-133 |
|
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: 431.12 E-value: 1.33e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMn 80
Cdd:cd14872 118 LEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSA- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 pyDYHFCSQ-GVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESAD--- 156
Cdd:cd14872 197 --AYGYLSLsGCIEVEGVDDVADFEEVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDvlk 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 157 KAAYLMGVSSGDLLKGLLHPRVRVgneyvtKGQ-------SVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQ 228
Cdd:cd14872 275 EVATLLGVDAATLEEALTSRLMEI------KGCdptriplTPAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKT 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 229 FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEKvrrlrlsd 308
Cdd:cd14872 349 TFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEK-------- 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 309 vggphsysfcsQPLGILSILEEECMFPKASDASFRAKLYDNHAGKSpNFQqprPDKKRKYQAHFEVVHYAGVVPYSIVGW 388
Cdd:cd14872 420 -----------KQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS-TFV---YAEVRTSRTEFIVKHYAGDVTYDITGF 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 389 LEKNKDPLNETVVPIFQKSQNRLLATLYenyagscstePPKSGvKEKRKKAasfqTVSQLHKENLNKLMTNLRATQPHFV 468
Cdd:cd14872 485 LEKNKDTLQKDLYVLLSSSKNKLIAVLF----------PPSEG-DQKTSKV----TLGGQFRKQLSALMTALNATEPHYI 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 469 RCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILnPSAIPDDTFMDSRKATEKLLGSLD 548
Cdd:cd14872 550 RCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-VKTIAKRVGPDDRQRCDLLLKSLK 628
|
570
....*....|....*.
gi 768017794 549 LDHTQYQFGHTKVFFK 564
Cdd:cd14872 629 QDFSKVQVGKTRVLYR 644
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
644-1721 |
1.53e-133 |
|
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: 444.62 E-value: 1.53e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 644 EEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSER 723
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 724 LEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQ 803
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 804 ALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKKDS 883
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 884 ELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGCR 963
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 964 KREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASA 1043
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1044 EKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLSRGKALAAQSLEELRRQLEEESKA 1123
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1124 KSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAiQRTEELEEAKKKLALRLQEAEEGVE 1203
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1204 AANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLR 1283
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1284 HGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQLEL 1363
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1364 SQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRL 1443
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1444 MQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLN 1523
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1524 QKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAAL 1603
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1604 RGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEA 1683
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 768017794 1684 EQQANTNLAKYRKAQHELDDAEERADMAETQANKLRAR 1721
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
1-564 |
5.02e-133 |
|
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: 429.75 E-value: 5.02e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLsmn 80
Cdd:cd01382 120 LEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLK--- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 pydyhfcsqgVITVDNMNDgeeLIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREE----QAEADGTESAD 156
Cdd:cd01382 197 ----------DPLLDDVGD---FIRMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSgggcNVKPKSEQSLE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 157 KAAYLMGVSSGDLLKGLLHpRVRVGNEYVTKGQS------VEQVVFAVGALAKATYDRLFRWLVSRINQTldtkLPRQ-- 228
Cdd:cd01382 264 YAAELLGLDQDELRVSLTT-RVMQTTRGGAKGTVikvplkVEEANNARDALAKAIYSKLFDHIVNRINQC----IPFEts 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 229 -FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEkvrrlrls 307
Cdd:cd01382 339 sYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIE-------- 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 308 dvggphsysfcSQPLGILSILEEECMFPKASDASFRAKLYDNHAgKSPNFQQPRPDKKRKYQA-----HFEVVHYAGVVP 382
Cdd:cd01382 410 -----------AKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK-NHFRLSIPRKSKLKIHRNlrddeGFLIRHFAGAVC 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 383 YSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYEnyagscSTEPPKSGVKEKRKKaASFQTVSQLHKENLNKLMTNLRA 462
Cdd:cd01382 478 YETAQFIEKNNDALHASLESLICESKDKFIRSLFE------SSTNNNKDSKQKAGK-LSFISVGNKFKTQLNLLMDKLRS 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 463 TQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDdtfMDSRKATEK 542
Cdd:cd01382 551 TGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR---LDPRLFCKA 627
|
570 580
....*....|....*....|..
gi 768017794 543 LLGSLDLDHTQYQFGHTKVFFK 564
Cdd:cd01382 628 LFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
1-564 |
3.44e-132 |
|
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: 427.65 E-value: 3.44e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmN 80
Cdd:cd14890 142 LESFGNAKTLRNDNSSRFGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQ-T 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGT-ESADKAA 159
Cdd:cd14890 221 PVEYFYLRGECSSIPSCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 160 YLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGF 239
Cdd:cd14890 301 ELLGVNEDALEKALLTRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 240 EIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIEkvrrlrlSDVGGphsysfcs 319
Cdd:cd14890 381 EKFEWNTFEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIE-------GKVNG-------- 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 320 qPLGILSILeEECMFPKASDAS--FRAKLYDNHAGKS------------PNFQQPRPDKKRkyqaHFEVVHYAGVVPYSI 385
Cdd:cd14890 445 -KPGIFITL-DDCWRFKGEEANkkFVSQLHASFGRKSgsggtrrgssqhPHFVHPKFDADK----QFGIKHYAGDVIYDA 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 386 VGWLEKNKDPLNETVVPIFQKSQNRLlatlyenyagscsteppksgvkekRKKAASFQTVSQLHkenlnKLMTNLRATQP 465
Cdd:cd14890 519 SGFNEKNNETLNAEMKELIKQSRRSI------------------------REVSVGAQFRTQLQ-----ELMAKISLTNP 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 466 HFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTFMdsrkatEKLLG 545
Cdd:cd14890 570 RYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTAENIEQLV------AVLSK 643
|
570
....*....|....*....
gi 768017794 546 SLDLDHTQYQFGHTKVFFK 564
Cdd:cd14890 644 MLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
1-562 |
4.73e-128 |
|
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: 416.11 E-value: 4.73e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKP-ELQDMLLLSM 79
Cdd:cd14901 137 LEAFGNARTNRNNNSSRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSdELHALGLTHV 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 80 NPYDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAA 159
Cdd:cd14901 217 EEYKYLNSSQCYDRRDGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRAA 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 160 Y-LMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLP--RQFFIGVLDI 236
Cdd:cd14901 297 CdLLGLDMDVLEKTLCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDI 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 237 AGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIEKVrrlrlsdvggphsys 316
Cdd:cd14901 377 FGFEIFATNSLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFEAR--------------- 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 317 fcsqPLGILSILEEECMFPKASDASFRAKLYDNHAGKSP----NFQQPRpdkkrkyqAHFEVVHYAGVVPYSIVGWLEKN 392
Cdd:cd14901 441 ----PTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKHASfsvsKLQQGK--------RQFVIHHYAGAVCYATDGFCDKN 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 393 KDPLNETVVPIFQKSQNRLLATlyenyagscsteppksgvkekrkkaasfqTVSQLHKENLNKLMTNLRATQPHFVRCIV 472
Cdd:cd14901 509 KDHVHSEALALLRTSSNAFLSS-----------------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIK 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 473 PNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSaIPDDTFMdSRKATEKLLGSLDL--- 549
Cdd:cd14901 560 PNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPD-GASDTWK-VNELAERLMSQLQHsel 637
|
570
....*....|....*.
gi 768017794 550 ---DHTQYQFGHTKVF 562
Cdd:cd14901 638 nieHLPPFQVGKTKVF 653
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
1-564 |
6.57e-128 |
|
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: 414.75 E-value: 6.57e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQ-DMLLLSM 79
Cdd:cd01379 119 MEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 80 NPYDYHFCSQGVITVDNMNDG---EELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQ----AEADGT 152
Cdd:cd01379 199 NKPPRYLQNDGLTVQDIVNNSgnrEKFEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNP 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 153 ESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL--DTKLP-RQF 229
Cdd:cd01379 279 EALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASdEPL 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 230 FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLiekvrrlrlsdv 309
Cdd:cd01379 359 SIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDM------------ 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 310 ggphsysFCSQPLGILSILEEECMFPKASDASFRAKLYDNHagKSPNFQQPRPDkkrkyQAHFEVVHYAGVVPYSIVGWL 389
Cdd:cd01379 426 -------FLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI--KSKYYWRPKSN-----ALSFGIHHYAGKVLYDASGFL 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 390 EKNKDPLNETVVPIFQKSQNRLLAtlyenyagscsteppksgvkekrkkaasfQTVSQLHKENLNKLMTNLRATQPHFVR 469
Cdd:cd01379 492 EKNRDTLPPDVVQLLRSSENPLVR-----------------------------QTVATYFRYSLMDLLSKMVVGQPHFVR 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 470 CIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAipDDTFMDSRKATEKLLGSLDL 549
Cdd:cd01379 543 CIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAFKW--NEEVVANRENCRLILERLKL 620
|
570
....*....|....*
gi 768017794 550 DHtqYQFGHTKVFFK 564
Cdd:cd01379 621 DN--WALGKTKVFLK 633
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
1-564 |
1.92e-127 |
|
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: 414.54 E-value: 1.92e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFgPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLsMN 80
Cdd:cd01387 119 LEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGL-QE 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQG-VITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQRE---EQAEADGTESAD 156
Cdd:cd01387 197 AEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQ 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 157 KAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDI 236
Cdd:cd01387 277 WVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDI 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 237 AGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIEKvrrlrlsdvggphsys 316
Cdd:cd01387 357 FGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYIREQIDWTEIAFA-DNQPVINLISK---------------- 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 317 fcsQPLGILSILEEECMFPKASDASFRAKLYDNHAgKSPNFQQPRPDkkrkyQAHFEVVHYAGVVPYSIVGWLEKNKDPL 396
Cdd:cd01387 420 ---KPVGILHILDDECNFPQATDHSFLEKCHYHHA-LNELYSKPRMP-----LPEFTIKHYAGQVWYQVHGFLDKNRDQL 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 397 NETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNEN 476
Cdd:cd01387 491 RQDVLELLVSSRTRVVAHLFSSHRAQTDKAPPRLGKGRFVTMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHK 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 477 KTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTFMDSRKAT-EKLLGSLDLDhtQYQ 555
Cdd:cd01387 571 KEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPRPAPGDMCVSLlSRLCTVTPKD--MYR 648
|
....*....
gi 768017794 556 FGHTKVFFK 564
Cdd:cd01387 649 LGATKVFLR 657
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
1-564 |
2.40e-127 |
|
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: 414.17 E-value: 2.40e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmN 80
Cdd:cd14903 120 LESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSA-N 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFcSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAE--ADGTESADKA 158
Cdd:cd14903 199 ECAYTG-ANKTIKIEGMSDRKHFARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 159 AYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAG 238
Cdd:cd14903 278 TKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFG 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 239 FEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEkvrrlrlsdvggphsysfc 318
Cdd:cd14903 358 FEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE------------------- 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 319 sQPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPDKkrkyqAHFEVVHYAGVVPYSIVGWLEKNKDPLNE 398
Cdd:cd14903 418 -DRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR-----TQFTIKHYAGPVTYESLGFLEKHKDALLP 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 399 TVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRK--KAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNEN 476
Cdd:cd14903 492 DLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRrgGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSI 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 477 KTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAipDDTFMDSRKATEKLLGSLDLDH-TQYQ 555
Cdd:cd14903 572 KSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEG--RNTDVPVAERCEALMKKLKLESpEQYQ 649
|
....*....
gi 768017794 556 FGHTKVFFK 564
Cdd:cd14903 650 MGLTRIYFQ 658
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
1-564 |
1.53e-126 |
|
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: 411.85 E-value: 1.53e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKpELQDMLLLSMN 80
Cdd:cd14892 138 LEAFGNAKTIRNDNSSRFGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLD-ANENAALELTP 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQG-VITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQ--KQREEQAEADGTESADK 157
Cdd:cd14892 217 AESFLFLNQGnCVEVDGVDDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnaDDEDVFAQSADGVNVAK 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 158 AAYLMGVSSGDLLKGLLhPRVRVGneyvTKGQSVE------QVVFAVGALAKATYDRLFRWLVSRIN-----QTL----- 221
Cdd:cd14892 297 AAGLLGVDAAELMFKLV-TQTTST----ARGSVLEikltarEAKNALDALCKYLYGELFDWLISRINachkqQTSgvtgg 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 222 DTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIEKv 301
Cdd:cd14892 372 AASPTFSPFIGILDIFGFEIMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQK- 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 302 rrlrlsdvggphsysfcsQPLGILSILEEECMFP-KASDASFRAKLYDNHAGKSPNFQQPRPDKKrkyqaHFEVVHYAGV 380
Cdd:cd14892 450 ------------------KPLGLLPLLEEQMLLKrKTTDKQLLTIYHQTHLDKHPHYAKPRFECD-----EFVLRHYAGD 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 381 VPYSIVGWLEKNKDPLnetvvpifqksQNRLLATLyenyagscsteppksgvkEKRKKaasFQTvsqlhkeNLNKLMTNL 460
Cdd:cd14892 507 VTYDVHGFLAKNNDNL-----------HDDLRDLL------------------RSSSK---FRT-------QLAELMEVL 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 461 RATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRIL-------NPSAIPDDTF 533
Cdd:cd14892 548 WSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLarnkagvAASPDACDAT 627
|
570 580 590
....*....|....*....|....*....|.
gi 768017794 534 MDSRKATEKLLGSLDLDhtQYQFGHTKVFFK 564
Cdd:cd14892 628 TARKKCEEIVARALERE--NFQLGRTKVFLR 656
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
1-564 |
1.19e-125 |
|
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: 409.18 E-value: 1.19e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmN 80
Cdd:cd14873 128 MEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-T 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQ-GVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFkqkqreeqAEADGTESADK-- 157
Cdd:cd14873 207 PENYHYLNQsGCVEDKTISDQESFREVITAMEVMQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKta 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 158 ---AAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKlpRQF-FIGV 233
Cdd:cd14873 279 lgrSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGK--EDFkSIGI 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 234 LDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEKvrrlrlsdvggph 313
Cdd:cd14873 357 LDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEK------------- 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 314 sysfcsqPLGILSILEEECMFPKASDASFRAKLYDNHAgkspnfQQPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNK 393
Cdd:cd14873 423 -------KLGLLALINEESHFPQATDSTLLEKLHSQHA------NNHFYVKPRVAVNNFGVKHYAGEVQYDVRGILEKNR 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 394 DPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKkaasfqTVSQLHKENLNKLMTNLRATQPHFVRCIVP 473
Cdd:cd14873 490 DTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRP------TVSSQFKDSLHSLMATLSSSNPFFVRCIKP 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 474 NENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDtfmDSRKATEKLLGSLDLDHTQ 553
Cdd:cd14873 564 NMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPE---DVRGKCTSLLQLYDASNSE 640
|
570
....*....|.
gi 768017794 554 YQFGHTKVFFK 564
Cdd:cd14873 641 WQLGKTKVFLR 651
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
1-564 |
4.44e-120 |
|
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: 395.21 E-value: 4.44e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGrKPELQDMLLLSMN 80
Cdd:cd01385 120 LEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAG-ASEEERKELHLKQ 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQ-GVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQK--QREEQAEADGTESADK 157
Cdd:cd01385 199 PEDYHYLNQsDCYTLEGEDEKYEFERLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDI 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 158 AAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL----DTKLPRQFFIGV 233
Cdd:cd01385 279 ISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGV 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 234 LDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEKvrrlrlsdvggph 313
Cdd:cd01385 359 LDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK------------- 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 314 sysfcsQPLGILSILEEECMFPKASDASFRAKlYDNHAGKSPNFQQPrpdkKRKYQAhFEVVHYAGVVPYSIVGWLEKNK 393
Cdd:cd01385 425 ------KPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKP----QVMEPA-FIIAHYAGKVKYQIKDFREKNL 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 394 DPLNETVVPIFQKSQNRLLATL--------------------YENYAGSCS-----TEPP---------KSGVKEKRKKA 439
Cdd:cd01385 493 DLMRPDIVAVLRSSSSAFVRELigidpvavfrwavlraffraMAAFREAGRrraqrTAGHsltlhdrttKSLLHLHKKKK 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 440 ASfqTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQR 519
Cdd:cd01385 573 PP--SVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQ 650
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 768017794 520 YRILNPSAIpddtfmDSRKATEK-LLGSLDLDHTQYQFGHTKVFFK 564
Cdd:cd01385 651 FQVLLPKGL------ISSKEDIKdFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
1-564 |
1.95e-118 |
|
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: 389.02 E-value: 1.95e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSG-KLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSm 79
Cdd:cd14891 139 LESFGNAKTLRNHNSSRFGKFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLL- 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 80 NPYDYHFCSQ-GVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKA 158
Cdd:cd14891 218 SPEDFIYLNQsGCVSDDNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAEIASESDKEA 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 159 ----AYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTK---LPrqfFI 231
Cdd:cd14891 298 lataAELLGVDEEALEKVITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDpdpLP---YI 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 232 GVLDIAGFEIFE-FNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIekvrrlrlsdvg 310
Cdd:cd14891 375 GVLDIFGFESFEtKNDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLI------------ 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 311 gphsysfCSQPLGILSILEEECMFPKASDASFRAKLYDNHAgKSPNFQQPRPDKKRKyqaHFEVVHYAGVVPYSIVGWLE 390
Cdd:cd14891 442 -------ASKPNGILPLLDNEARNPNPSDAKLNETLHKTHK-RHPCFPRPHPKDMRE---MFIVKHYAGTVSYTIGSFID 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 391 KNKDplnetvvpIFQKSQNRLLATlyenyagscsteppksgvkekrkkAASFQTVSQlhkenlnKLMTNLRATQPHFVRC 470
Cdd:cd14891 511 KNND--------IIPEDFEDLLAS------------------------SAKFSDQMQ-------ELVDTLEATRCNFIRC 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 471 IVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAI------PDDTFmdsrkaTEKLL 544
Cdd:cd14891 552 IKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLPPSVtrlfaeNDRTL------TQAIL 625
|
570 580
....*....|....*....|
gi 768017794 545 GSLDLDHTQYQFGHTKVFFK 564
Cdd:cd14891 626 WAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
1-564 |
2.52e-116 |
|
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: 382.50 E-value: 2.52e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmN 80
Cdd:cd14897 120 LEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLE-D 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQGVITVDNMNDGEELiatDH----------AMDILGFSVDEKCACYKIVGALLHFGNMKFkqkqrEEQAEAD 150
Cdd:cd14897 199 PDCHRILRDDNRNRPVFNDSEEL---EYyrqmfhdltnIMKLIGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTD 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 151 GTESADK-----AAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDtkl 225
Cdd:cd14897 271 GVTVADEyplhaVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLW--- 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 226 PRQFF--------IGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDL 297
Cdd:cd14897 348 PDKDFqimtrgpsIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLEL 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 298 IEKvrrlrlsdvggphsysfcsQPLGILSILEEECMFPKASDASFRAKLyDNHAGKSPNFQQPRPDKkrkyqAHFEVVHY 377
Cdd:cd14897 427 FFK-------------------KPLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESPRYVASPGNR-----VAFGIRHY 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 378 AGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYagscsteppksgvkekrkkaasfqtvsqlHKENLNKLM 457
Cdd:cd14897 482 AEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSY-----------------------------FKRSLSDLM 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 458 TNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSaiPDDTFMDSR 537
Cdd:cd14897 533 TKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDF--SNKVRSDDL 610
|
570 580
....*....|....*....|....*..
gi 768017794 538 KATEKLLGSLDLDhtQYQFGHTKVFFK 564
Cdd:cd14897 611 GKCQKILKTAGIK--GYQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
1-523 |
2.10e-112 |
|
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: 371.18 E-value: 2.10e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMlllsmn 80
Cdd:cd14900 145 LESFGNARTLRNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKR------ 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 pydyhfcsqgvitvDNMNDgeeliaTDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTE------- 153
Cdd:cd14900 219 --------------DMYRR------VMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDlapssiw 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 154 SADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL-----DTKLPRQ 228
Cdd:cd14900 279 SRDAAATLLSVDATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGL 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 229 FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIEKvrrlrlsd 308
Cdd:cd14900 359 HFIGILDIFGFEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLISQ-------- 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 309 vggphsysfcsQPLGILSILEEECMFPKASDASFRAKLYdNHAGKSPNFQQPRPDKKRkyqAHFEVVHYAGVVPYSIVGW 388
Cdd:cd14900 430 -----------RPTGILSLIDEECVMPKGSDTTLASKLY-RACGSHPRFSASRIQRAR---GLFTIVHYAGHVEYSTDGF 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 389 LEKNKDPLNETVVPIFQksqnrllatlyenYAGScsteppksgvkekrkkaasfqtvsqlHKENLNKLMTNLRATQPHFV 468
Cdd:cd14900 495 LEKNKDVLHQEAVDLFV-------------YGLQ--------------------------FKEQLTTLLETLQQTNPHYV 535
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 768017794 469 RCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRIL 523
Cdd:cd14900 536 RCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
1-564 |
3.97e-111 |
|
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: 368.97 E-value: 3.97e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFG-PSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSM 79
Cdd:cd14907 147 LEAFGNAKTVRNDNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKN 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 80 NPYDYHFCS---QGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQ--REEQAEADGTES 154
Cdd:cd14907 227 QLSGDRYDYlkkSNCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKET 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 155 ADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL------DTKLPRQ 228
Cdd:cd14907 307 LQIIAKLLGIDEEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekDQQLFQN 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 229 FF--IGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVF--IDFgLDLQPCIDLIEKvrrl 304
Cdd:cd14907 387 KYlsIGLLDIFGFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDK---- 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 305 rlsdvggphsysfcsQPLGILSILEEECMFPKASDASFRAKLYDNHAGKSpNFQQPRPDKKRKyqahFEVVHYAGVVPYS 384
Cdd:cd14907 462 ---------------PPIGIFNLLDDSCKLATGTDEKLLNKIKKQHKNNS-KLIFPNKINKDT----FTIRHTAKEVEYN 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 385 IVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKKaasfqTVSQLHKENLNKLMTNLRATQ 464
Cdd:cd14907 522 IEGFREKNKDEISQSIINCIQNSKNRIISSIFSGEDGSQQQNQSKQKKSQKKDK-----FLGSKFRNQMKQLMNELMQCD 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 465 PHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNpsaipddtfmdsrkatekll 544
Cdd:cd14907 597 VHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLK-------------------- 656
|
570 580
....*....|....*....|
gi 768017794 545 gsldldhTQYQFGHTKVFFK 564
Cdd:cd14907 657 -------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
1-564 |
3.49e-107 |
|
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: 357.68 E-value: 3.49e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFgPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLsMN 80
Cdd:cd14889 122 LEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGL-LD 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQGVITVDNMND-GEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREE-QAEADGTESADKA 158
Cdd:cd14889 200 PGKYRYLNNGAGCKREVQYwKKKYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAA 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 159 AYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLdtkLPRQFF------IG 232
Cdd:cd14889 280 AGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL---APKDDSsvelreIG 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 233 VLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLiekvrrlrlsdvggp 312
Cdd:cd14889 357 ILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDL--------------- 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 313 hsysFCSQPLGILSILEEECMFPKASDASFRAKLyDNHAGKSPNFQqprpdKKRKYQAHFEVVHYAGVVPYSIVGWLEKN 392
Cdd:cd14889 421 ----FLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYYG-----KSRSKSPKFTVNHYAGKVTYNASGFLEKN 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 393 KDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSG---VKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVR 469
Cdd:cd14889 491 RDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKlpqAGSDNFNSTRKQSVGAQFKHSLGVLMEKMFAASPHFVR 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 470 CIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRIL-NPSAIPDDtfmdsRKATEKLLGSLD 548
Cdd:cd14889 571 CIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILlCEPALPGT-----KQSCLRILKATK 645
|
570
....*....|....*.
gi 768017794 549 LdhTQYQFGHTKVFFK 564
Cdd:cd14889 646 L--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
1-564 |
2.13e-100 |
|
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: 338.07 E-value: 2.13e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSG-RKPELQDMLLLSM 79
Cdd:cd14904 120 LESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPN 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 80 NPYDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGtESADKAA 159
Cdd:cd14904 200 CQYQYLGDSLAQMQIPGLDDAKLFASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNG-SQLSQVA 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 160 YLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQF-FIGVLDIAG 238
Cdd:cd14904 279 KMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFG 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 239 FEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIEKvrrlrlsdvggphsysfc 318
Cdd:cd14904 359 FEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVIDG------------------ 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 319 sqPLGILSILEEECMFPKASDASFRAKLYDNHA--GKSPNFQQPRPDKkrkyqAHFEVVHYAGVVPYSIVGWLEKNKDPL 396
Cdd:cd14904 420 --KMGIIALMNDHLRQPRGTEEALVNKIRTNHQtkKDNESIDFPKVKR-----TQFIINHYAGPVTYETVGFMEKHRDTL 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 397 NETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKKAASFQtvsqlHKENLNKLMTNLRATQPHFVRCIVPNEN 476
Cdd:cd14904 493 QNDLLDLVLLSSLDLLTELFGSSEAPSETKEGKSGKGTKAPKSLGSQ-----FKTSLSQLMDNIKTTNTHYVRCIKPNAN 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 477 KTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDtfmDSRKATEKLLGSLDLDHT-QYQ 555
Cdd:cd14904 568 KSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSK---DVRRTCSVFMTAIGRKSPlEYQ 644
|
....*....
gi 768017794 556 FGHTKVFFK 564
Cdd:cd14904 645 IGKSLIYFK 653
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
1-564 |
1.01e-99 |
|
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: 337.70 E-value: 1.01e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGP-----SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDML 75
Cdd:cd14895 135 LESFGNARTLRNDNSSRFGKFVRMFFEGheldtSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLEL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 76 LL-SMNPYDYHFCSQGVITV--DNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGT 152
Cdd:cd14895 215 QLeLLSAQEFQYISGGQCYQrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 153 ESA------------------DKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLV 214
Cdd:cd14895 295 ASApcrlasaspssltvqqhlDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLV 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 215 SRINQTLDTklpRQF--------------FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGI 280
Cdd:cd14895 375 SKVNSASPQ---RQFalnpnkaankdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGI 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 281 DWVFIDFGLDlQPCIDLIEKvrrlrlsdvggphsysfcsQPLGILSILEEECMFPKASDASFRAKLYDNHAGKSpNFQQP 360
Cdd:cd14895 452 KWNAVDYEDN-SVCLEMLEQ-------------------RPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHS-NFSAS 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 361 RPDKKrkyQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKKA- 439
Cdd:cd14895 511 RTDQA---DVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSv 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 440 -ASFQTVSQLhKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQ 518
Cdd:cd14895 588 lSSVGIGSQF-KQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVK 666
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 768017794 519 RYRILNPSAIPDDTfmdsrkATEKLLGSLDLDHTqyQFGHTKVFFK 564
Cdd:cd14895 667 QYRLLVAAKNASDA------TASALIETLKVDHA--ELGKTRVFLR 704
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
1-564 |
2.34e-99 |
|
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: 336.11 E-value: 2.34e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSG------RKPELQDM 74
Cdd:cd14908 140 LEAFGNARTLRNDNSSRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGgdeeehEKYEFHDG 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 75 LLLSMN-PYDYHFCSQG-VITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGT 152
Cdd:cd14908 220 ITGGLQlPNEFHYTGQGgAPDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEE 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 153 ESADKAAY---LMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQF 229
Cdd:cd14908 300 GNEKCLARvakLLGVDVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDI 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 230 --FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIEkvrrlrls 307
Cdd:cd14908 380 rsSVGVLDIFGFECFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ-------- 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 308 dvggphsysfcSQPLGILSILEEECMFP-KASDASFRAKLYDNHAgksPNFQQPRPDKKR-------KYQAHFEVVHYAG 379
Cdd:cd14908 451 -----------AKKKGILTMLDDECRLGiRGSDANYASRLYETYL---PEKNQTHSENTRfeatsiqKTKLIFAVRHFAG 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 380 VVPYSI-VGWLEKNKDPLNETVVPIFQKSQNrllatlyenyagscsteppksgvkekrkkaasfqtvsqlHKENLNKLMT 458
Cdd:cd14908 517 QVQYTVeTTFCEKNKDEIPLTADSLFESGQQ---------------------------------------FKAQLHSLIE 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 459 NLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSaIPDDT---FMD 535
Cdd:cd14908 558 MIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLPL-IPEVVlswSME 636
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 768017794 536 SRKATEKLLGSLDLD-----------------HTQYQFGHTKVFFK 564
Cdd:cd14908 637 RLDPQKLCVKKMCKDlvkgvlspamvsmknipEDTMQLGKSKVFMR 682
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
1-617 |
1.68e-98 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 337.77 E-value: 1.68e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDML-LLSM 79
Cdd:PTZ00014 230 LEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYkLKSL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 80 NpyDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEA-----DGTES 154
Cdd:PTZ00014 310 E--EYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDAaaisdESLEV 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 155 ADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVL 234
Cdd:PTZ00014 388 FNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGML 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 235 DIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIekvrrlrlsdvggphs 314
Cdd:PTZ00014 468 DIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLL---------------- 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 315 ysfCSQPLGILSILEEECMFPKASDASFRAKLYDNHAgKSPNFQQPRPDKKRKyqahFEVVHYAGVVPYSIVGWLEKNKD 394
Cdd:PTZ00014 531 ---CGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNLK-NNPKYKPAKVDSNKN----FVIKHTIGDIQYCASGFLFKNKD 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 395 PLNETVVPIFQKSQNRLLATLYEnyagscsteppksGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPN 474
Cdd:PTZ00014 603 VLRPELVEVVKASPNPLVRDLFE-------------GVEVEKGKLAKGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKPN 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 475 ENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTfMDSRKATEKLLGSLDLDHTQY 554
Cdd:PTZ00014 670 ENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSS-LDPKEKAEKLLERSGLPKDSY 748
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768017794 555 QFGHTKVFFKAGLLGVLEELRDQRLAKVLTLLQARSrGRLMRLEYQRLLGGR-DALFTIQWNIR 617
Cdd:PTZ00014 749 AIGKTMVFLKKDAAKELTQIQREKLAAWEPLVSVLE-ALILKIKKKRKVRKNiKSLVRIQAHLR 811
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
1-526 |
1.69e-97 |
|
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: 331.47 E-value: 1.69e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLS-M 79
Cdd:cd14902 138 LESFGNAQTIRNDNSSRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQkG 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 80 NPYDYH---FCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESA- 155
Cdd:cd14902 218 GKYELLnsyGPSFARKRAVADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRf 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 156 --DKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFF--- 230
Cdd:cd14902 298 hlAKCAELMGVDVDKLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSIsde 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 231 ------IGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIEkvrrl 304
Cdd:cd14902 378 deelatIGILDIFGFESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFD----- 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 305 rlsdvggphsysfcSQPLGILSILEEECMFPKASDASFRAKLYDNHAGkspnfqqprpdkkrkyQAHFEVVHYAGVVPYS 384
Cdd:cd14902 452 --------------DKSNGLFSLLDQECLMPKGSNQALSTKFYRYHGG----------------LGQFVVHHFAGRVCYN 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 385 IVGWLEKNKDPLNETVVPIFQKSQNRLLATL--YENYAGSCSTEPPKSGVKEKRKKAASfqtVSQLHKENLNKLMTNLRA 462
Cdd:cd14902 502 VEQFVEKNTDALPADASDILSSSSNEVVVAIgaDENRDSPGADNGAAGRRRYSMLRAPS---VSAQFKSQLDRLIVQIGR 578
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768017794 463 TQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPS 526
Cdd:cd14902 579 TEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFKCF 642
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
1-564 |
4.11e-95 |
|
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: 322.71 E-value: 4.11e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDML-LLSM 79
Cdd:cd14876 121 LEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYhLLGL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 80 NPYDY--HFCSQgVITVDNMNDGEELIATDHAMdilGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADK 157
Cdd:cd14876 201 KEYKFlnPKCLD-VPGIDDVADFEEVLESLKSM---GLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVDDAAAISNESL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 158 -----AAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIG 232
Cdd:cd14876 277 evfkeACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMG 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 233 VLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIekvrrlrlsdvggp 312
Cdd:cd14876 357 MLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVL-------------- 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 313 hsysfCSQPLGILSILEEECMFPKASDASFRAKLYDNHAGkSPNFQQPRPDKKRKyqahFEVVHYAGVVPYSIVGWLEKN 392
Cdd:cd14876 422 -----CGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKS-NGKFKPAKVDSNIN----FIVVHTIGDIQYNAEGFLFKN 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 393 KDPLNETVVPIFQKSQNRLLATLYEnyagscsteppksGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIV 472
Cdd:cd14876 492 KDVLRAELVEVVQASTNPVVKALFE-------------GVVVEKGKIAKGSLIGSQFLKQLESLMGLINSTEPHFIRCIK 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 473 PNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTfMDSRKATEKLLGSLDLDHT 552
Cdd:cd14876 559 PNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLGIANDKS-LDPKVAALKLLESSGLSED 637
|
570
....*....|..
gi 768017794 553 QYQFGHTKVFFK 564
Cdd:cd14876 638 EYAIGKTMVFLK 649
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
1-564 |
1.06e-94 |
|
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: 321.34 E-value: 1.06e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFgPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmN 80
Cdd:cd14896 119 LESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQ-G 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQG-VITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESAD--K 157
Cdd:cd14896 197 PETYYYLNQGgACRLQGKEDAQDFEGLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEihT 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 158 AAYLMGVSSgDLLKGLLHPRVRVGN-EYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFF--IGVL 234
Cdd:cd14896 277 AARLLQVPP-ERLEGAVTHRVTETPyGRVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVV 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 235 DIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDfGLDLQPCIDLIekvrrlrlsdvggphs 314
Cdd:cd14896 356 DAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLL---------------- 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 315 ysfCSQPLGILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQPR---PDkkrkyqahFEVVHYAGVVPYSIVGWLEK 391
Cdd:cd14896 419 ---VDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQlplPV--------FTVRHYAGTVTYQVHKFLNR 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 392 NKDPLNETVVPIFQKSQNRLLATLYENyagscstEPPKSGVKEKRKKAAS-FQtvsqlhkENLNKLMTNLRATQPHFVRC 470
Cdd:cd14896 487 NRDQLDPAVVEMLAQSQLQLVGSLFQE-------AEPQYGLGQGKPTLASrFQ-------QSLGDLTARLGRSHVYFIHC 552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 471 IVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDdtFMDSRKATEKLLGSLDLD 550
Cdd:cd14896 553 LNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEA--LSDRERCGAILSQVLGAE 630
|
570
....*....|....
gi 768017794 551 HTQYQFGHTKVFFK 564
Cdd:cd14896 631 SPLYHLGATKVLLK 644
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
1-562 |
7.76e-87 |
|
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: 298.69 E-value: 7.76e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSG---------RKPEL 71
Cdd:cd14880 131 MEAFGNACTLRNNNSSRFGKFIQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGasaderlqwHLPEG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 72 QDMLLLSmNPydyhfcsqgvitvDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQA---E 148
Cdd:cd14880 211 AAFSWLP-NP-------------ERNLEEDCFEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpM 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 149 ADGTESADKAAYLMGVSSGDLLKGLlhpRVRVgneyVTKGQsvEQVVFAV-----------GALAKATYDRLFRWLVSRI 217
Cdd:cd14880 277 DDTKESVRTSALLLKLPEDHLLETL---QIRT----IRAGK--QQQVFKKpcsraecdtrrDCLAKLIYARLFDWLVSVI 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 218 NQTLDTKLPR-QFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCID 296
Cdd:cd14880 348 NSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLD 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 297 LIEkvrrlrlsdvggphsysfcSQPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPDKKrkyqAHFEVVH 376
Cdd:cd14880 427 LIE-------------------GSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKLSRE----PSFIVVH 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 377 YAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSgvkekRKKAASFQTVSQLhKENLNKL 456
Cdd:cd14880 484 YAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSG-----QSRAPVLTVVSKF-KASLEQL 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 457 MTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTFMDS 536
Cdd:cd14880 558 LQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLRRLRPHTSSGPHS 637
|
570 580
....*....|....*....|....*.
gi 768017794 537 RKATEKLLGSLdldhtqyQFGHTKVF 562
Cdd:cd14880 638 PYPAKGLSEPV-------HCGRTKVF 656
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
1-564 |
9.43e-86 |
|
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: 295.95 E-value: 9.43e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGP-SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSM 79
Cdd:cd14875 131 MESFGNARTVRNDNSSRFGKYIKLYFDPtSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLK 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 80 NPYDYHfCSQGVIT-----VDN--MNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGT 152
Cdd:cd14875 211 TAQDYK-CLNGGNTfvrrgVDGktLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADET 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 153 ESAdKAAYLMGVSSGDLLKGLLhprVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKL--PRQFF 230
Cdd:cd14875 290 PFL-TACRLLQLDPAKLRECFL---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGdcSGCKY 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 231 IGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIEKVRrlrlsdvg 310
Cdd:cd14875 366 IGLLDIFGFENFTRNSFEQLCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDQKR-------- 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 311 gphsysfcsqpLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPrpdkKRKYQAHFEVVHYAGVVPYSIVGWLE 390
Cdd:cd14875 437 -----------TGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPYFVLP----KSTIPNQFGVNHYAAFVNYNTDEWLE 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 391 KNKDPLNETVVPIFQKSQNRLLATLYenyagscSTEPpksgVKEKRKkaasfQTVSQLHKENLNKLMTNLRATQPHFVRC 470
Cdd:cd14875 502 KNTDALKEDMYECVSNSTDEFIRTLL-------STEK----GLARRK-----QTVAIRFQRQLTDLRTELESTETQFIRC 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 471 IVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDF-RQRYRILNPSAIPDDTFMDSRKATEKLLGS--- 546
Cdd:cd14875 566 IKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFcRYFYLIMPRSTASLFKQEKYSEAAKDFLAYyqr 645
|
570
....*....|....*....
gi 768017794 547 -LDLDHTQYQFGHTKVFFK 564
Cdd:cd14875 646 lYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
1-521 |
1.51e-85 |
|
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: 297.01 E-value: 1.51e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHF-GPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGR----KPELQDML 75
Cdd:cd14899 147 LEAFGNARTVRNDNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 76 LLSMNPYDYHFCSQGVITV--DNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQ--KQREEQAEADG 151
Cdd:cd14899 227 ALSGGPQSFRLLNQSLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 152 TESA----------DKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL 221
Cdd:cd14899 307 ARVMssttgafdhfTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 222 ---------------DTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFID 286
Cdd:cd14899 387 qrqasapwgadesdvDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVD 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 287 FGlDLQPCIDLIEKvrrlrlsdvggphsysfcsQPLGILSILEEECMFPKASDASFRAKLYDNHAGKS--PNFQQPrPDK 364
Cdd:cd14899 467 FP-NNRACLELFEH-------------------RPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNshPHFRSA-PLI 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 365 KRKYQahFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATL-----YENYAGSCSTEPPKSGVKEKRKKA 439
Cdd:cd14899 526 QRTTQ--FVVAHYAGCVTYTIDGFLAKNKDSFCESAAQLLAGSSNPLIQALaagsnDEDANGDSELDGFGGRTRRRAKSA 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 440 ASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQR 519
Cdd:cd14899 604 IAAVSVGTQFKIQLNELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGR 683
|
..
gi 768017794 520 YR 521
Cdd:cd14899 684 YR 685
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
1-526 |
7.24e-80 |
|
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: 279.94 E-value: 7.24e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHF-GPSGKLASADIDSYLLEKSRvIFQLPGER--SYHVYYQILSGRKPELQDMLLL 77
Cdd:cd14906 131 LEAFGNSRTTKNHNSSRFGKFLKIEFrSSDGKIDGASIETYLLEKSR-ISHRPDNInlSYHIFYYLVYGASKDERSKWGL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 78 SMNPYDYHF--CSQGVITV---------DNMNDGEELIAT----DHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQ 142
Cdd:cd14906 210 NNDPSKYRYldARDDVISSfksqssnknSNHNNKTESIESfqllKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDS 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 143 ---REEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNE--YVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRI 217
Cdd:cd14906 290 dfsKYAYQKDKVTASLESVSKLLGYIESVFKQALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKI 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 218 NQTLDTKLPRQ-----------FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFID 286
Cdd:cd14906 370 NRKFNQNTQSNdlaggsnkknnLFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSN 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 287 FgLDLQPCIDLIEKvrrlrlsdvggphsysfcsQPLGILSILEEECMFPKASDASFRAKlYDNHAGKSPNFQQPRPDKkr 366
Cdd:cd14906 450 F-IDNKECIELIEK-------------------KSDGILSLLDDECIMPKGSEQSLLEK-YNKQYHNTNQYYQRTLAK-- 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 367 kyqAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYagscSTEPPKSgvkekRKKAASFQTVS 446
Cdd:cd14906 507 ---GTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQ----ITSTTNT-----TKKQTQSNTVS 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 447 QLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPS 526
Cdd:cd14906 575 GQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
1-564 |
1.20e-79 |
|
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: 277.54 E-value: 1.20e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDML-LLSM 79
Cdd:cd14886 125 LESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLgFKSL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 80 NPYDYHFCSQgVITVDNMNDGEELIATDHAMDILgFSVDEKCACYKIVGALLHFGNMKFKQKQR---EEQAEADGTESAD 156
Cdd:cd14886 205 ESYNFLNASK-CYDAPGIDDQKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFG 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 157 KAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDI 236
Cdd:cd14886 283 KMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDI 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 237 AGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIEKvrrlrlsdvggPHsys 316
Cdd:cd14886 363 YGFEFFERNTYEQLLINYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDK-----------PN--- 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 317 fcsqpLGILSILEEECMFPKASDASFRAKLydNHAGKSPNFQqprPDKKRkyQAHFEVVHYAGVVPYSIVGWLEKNKDPL 396
Cdd:cd14886 428 -----LSIFSFLEEQCLIQTGSSEKFTSSC--KSKIKNNSFI---PGKGS--QCNFTIVHTAATVTYNTEEFVDKNKHKL 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 397 NETVVPIFQKSQNRLLATLYENYagscstePPKSGVKEKRKKAASFQTvsqlhkeNLNKLMTNLRATQPHFVRCIVPNEN 476
Cdd:cd14886 496 SVDILELLMGSTNPIVNKAFSDI-------PNEDGNMKGKFLGSTFQL-------SIDQLMKTLSATKSHFIRCIKTNQD 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 477 KTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNP-SAIPDDTFMDSRKATEKLLGSLDLDHTQYQ 555
Cdd:cd14886 562 KVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILIShNSSSQNAGEDLVEAVKSILENLGIPCSDYR 641
|
....*....
gi 768017794 556 FGHTKVFFK 564
Cdd:cd14886 642 IGKTKVFLR 650
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
1-564 |
2.57e-72 |
|
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: 257.24 E-value: 2.57e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSMN 80
Cdd:cd01386 120 LEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFcsqGVITVDNMNDGEELIA----TDHAMDILGFSVDEKCACYKIVGALLHFGN---MKFKQKQREEQAEadgTE 153
Cdd:cd01386 200 AESNSF---GIVPLQKPEDKQKAAAafskLQAAMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFAR---PE 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 154 SADKAAYLMGVSSGDLLK---------GLLHPRVRVGNEYVTKGQSVEQVVFAVGAL---AKATYDRLFRWLVSRINQTL 221
Cdd:cd01386 274 WAQRAAYLLGCTLEELSSaifkhhlsgGPQQSTTSSGQESPARSSSGGPKLTGVEALegfAAGLYSELFAAVVSLINRSL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 222 DTKLPRQFFIGVLDIAGFEIFEFN------SFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDwvfIDFGLD---LQ 292
Cdd:cd01386 354 SSSHHSTSSITIVDTPGFQNPAHSgsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVE---VDFDLPelsPG 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 293 PCIDLIEKVRRLRLSDVGGPHsysfcSQPLGILSILEEECMFPKASDASFRAKLYdNHAGKSPNFQQPRPDKKRKYQAHF 372
Cdd:cd01386 431 ALVALIDQAPQQALVRSDLRD-----EDRRGLLWLLDEEALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLRRSEGPLQF 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 373 EVVHYAGV--VPYSIVGWLEKNK-DPLNETVVPIFQKSQNRLlatlyenyagscsteppkSGVKekrKKAASFQTvsqlh 449
Cdd:cd01386 505 VLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQESQKET------------------AAVK---RKSPCLQI----- 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 450 KENLNKLMTNLRATQPHFVRCIVPNENKTPGV------------MDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFR 517
Cdd:cd01386 559 KFQVDALIDTLRRTGLHFVHCLLPQHNAGKDErstsspaagdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFR 638
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 768017794 518 QRYRILNPS----AIPDDTFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 564
Cdd:cd01386 639 RRFQVLAPPltkkLGLNSEVADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
1-564 |
2.58e-72 |
|
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: 256.28 E-value: 2.58e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGK-LASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSm 79
Cdd:cd14878 122 LEAFGHAKTTLNDLSSCFIKYFELQFCERKKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLN- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 80 NPYDYHFCSQG----VITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESA 155
Cdd:cd14878 201 NLCAHRYLNQTmredVSTAERSLNREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 156 DKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL----DTKLPRQFFI 231
Cdd:cd14878 281 EQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdEQKSMQTLDI 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 232 GVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDwvfidfgldlqpcidlIEKVRRLrlsdvgG 311
Cdd:cd14878 361 GILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQEQTECVQEGVT----------------METAYSP------G 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 312 PHSYS---FCSQPLGILSILEEECMFPKASDASFRAKLY------DNHAGKSPNFQQPRPDKKRKYQAHFEVVHYAGVVP 382
Cdd:cd14878 419 NQTGVldfFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQsllessNTNAVYSPMKDGNGNVALKDQGTAFTVMHYAGRVM 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 383 YSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENyagscsteppksgvkekrkKAASfqTVSQLHKeNLNKLMTNLRA 462
Cdd:cd14878 499 YEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQS-------------------KLVT--IASQLRK-SLADIIGKLQK 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 463 TQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIpddtfMDSRKATEK 542
Cdd:cd14878 557 CTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLL-----GEKKKQSAE 631
|
570 580
....*....|....*....|....*
gi 768017794 543 LLGSLDLDHTQ---YQFGHTKVFFK 564
Cdd:cd14878 632 ERCRLVLQQCKlqgWQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
1-564 |
9.37e-71 |
|
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: 251.09 E-value: 9.37e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDML-LLSM 79
Cdd:cd14937 114 LEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYkIRSE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 80 NPYDYHFCSQGVI-TVDNMNDGEELIATDHAMDIlgfsVDEKCACYKIVGALLHFGNMKFKQ-----KQREEQAEADGTE 153
Cdd:cd14937 194 NEYKYIVNKNVVIpEIDDAKDFGNLMISFDKMNM----HDMKDDLFLTLSGLLLLGNVEYQEiekggKTNCSELDKNNLE 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 154 SADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGV 233
Cdd:cd14937 270 LVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGI 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 234 LDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIdwvfidfgldlqpcidLIEKVRRLRLSDVggph 313
Cdd:cd14937 350 LDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETELYKAEDI----------------LIESVKYTTNESI---- 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 314 sYSFCSQPLGILSILEEECMFPKASDASFrAKLYDNHAGKSPNFQQprpdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNK 393
Cdd:cd14937 410 -IDLLRGKTSIISILEDSCLGPVKNDESI-VSVYTNKFSKHEKYAS----TKKDINKNFVIKHTVSDVTYTITNFISKNK 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 394 DPLNETVVPIFQKSQNRLLATLYENYAGSCSTeppksgvkeKRKKAASFQtvsqlHKENLNKLMTNLRATQPHFVRCIVP 473
Cdd:cd14937 484 DILPSNIVRLLKVSNNKLVRSLYEDVEVSESL---------GRKNLITFK-----YLKNLNNIISYLKSTNIYFIKCIKP 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 474 NENKTPGVMDAFLVLHQLRCNGVLEGIRIcRQGFPNRLLYTDFRQRYRILNPSAIPDDTFMDSRKATEKLLGSLDLDhtQ 553
Cdd:cd14937 550 NENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSSLTDKEKVSMILQNTVDPD--L 626
|
570
....*....|.
gi 768017794 554 YQFGHTKVFFK 564
Cdd:cd14937 627 YKVGKTMVFLK 637
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
5-563 |
1.37e-67 |
|
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: 241.56 E-value: 1.37e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 5 GNAKTLRNDNSSRFGKFIRIHFgPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLS-MNPYD 83
Cdd:cd14881 119 GSAKTATNSESSRIGHFIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgYSPAN 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 84 YHFCSQGVITVDNMNDGEELIATDHAMDILGFS-VDekcaCYKIVGALLHFGNMKFKQKQREEQAEADGTEsADKAAYLM 162
Cdd:cd14881 198 LRYLSHGDTRQNEAEDAARFQAWKACLGILGIPfLD----VVRVLAAVLLLGNVQFIDGGGLEVDVKGETE-LKSVAALL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 163 GVSSGDLLKGLlhpRVRVGNeyvTKGQSVEQVV------FAVGALAKATYDRLFRWLVSRINQ------TLDTKlPRQFF 230
Cdd:cd14881 273 GVSGAALFRGL---TTRTHN---ARGQLVKSVCdanmsnMTRDALAKALYCRTVATIVRRANSlkrlgsTLGTH-ATDGF 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 231 IGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDW-VFIDFgLDLQPCIDLIEkvrrlrlsdv 309
Cdd:cd14881 346 IGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCeVEVDY-VDNVPCIDLIS---------- 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 310 ggphsysfcSQPLGILSILEEECMfPKASDASFRAKLYDNHAGkSPNFQQPRPDKKRKyqahFEVVHYAGVVPYSIVGWL 389
Cdd:cd14881 415 ---------SLRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQ-NPRLFEAKPQDDRM----FGIRHFAGRVVYDASDFL 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 390 EKNKDPLNETVVPIFQKSqnrllatlyenyagSCSTeppksgvkekrkkaaSFQTVSQLHKENLNKLMTNLRATQPHFVR 469
Cdd:cd14881 480 DTNRDVVPDDLVAVFYKQ--------------NCNF---------------GFATHTQDFHTRLDNLLRTLVHARPHFVR 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 470 CIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIP---DDTFMDSRKATEKLLGS 546
Cdd:cd14881 531 CIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLrrvEEKALEDCALILQFLEA 610
|
570 580
....*....|....*....|..
gi 768017794 547 LDLDH-----TQYQFGHTKVFF 563
Cdd:cd14881 611 QPPSKlssvsTSWALGKRHIFL 632
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
1-527 |
1.18e-66 |
|
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: 237.49 E-value: 1.18e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFgpSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLlsmn 80
Cdd:cd14898 114 LEAFGNAKTQLNDNSSRFGKRIKLKF--DGKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI---- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 pyDYHFCSQGVITVDNMNdgEELIATDHAMDILG---FSVDEKCACykivgALLHFGNMKFKQkqrEEQAEADGTESADK 157
Cdd:cd14898 188 --DTSSTAGNKESIVQLS--EKYKMTCSAMKSLGianFKSIEDCLL-----GILYLGSIQFVN---DGILKLQRNESFTE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 158 AAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQffIGVLDIA 237
Cdd:cd14898 256 FCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIF 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 238 GFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEKvrrlrlsdvggphsysf 317
Cdd:cd14898 334 GFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEK----------------- 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 318 csqPLGILSILEEECMFPKASDASFRAKL--YDNHAGKSpnfqqprpdkkrKYQAHFEVVHYAGVVPYSIVGWLEKNKDP 395
Cdd:cd14898 396 ---PCGLMDLISEESFNAWGNVKNLLVKIkkYLNGFINT------------KARDKIKVSHYAGDVEYDLRDFLDKNREK 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 396 LNetVVPIfqksQNRLLATlyenyagscsteppksgvKEKRKKAASFqtvsqlHKENLNKLMTNLRATQPHFVRCIVPNE 475
Cdd:cd14898 461 GQ--LLIF----KNLLIND------------------EGSKEDLVKY------FKDSMNKLLNSINETQAKYIKCIRPNE 510
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 768017794 476 NKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSA 527
Cdd:cd14898 511 ECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
2-563 |
3.88e-61 |
|
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: 222.81 E-value: 3.88e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 2 EAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIfQLP-GERSYHVYYQILSGRKPELQDMLLLSmN 80
Cdd:cd14879 133 DSFGNAKTLTNPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVA-SVPtGERNFHVFYYLLAGASPEERQHLGLD-D 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDY-----HFCSQGVITVDNmNDGEELiatDH---AMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQ--REEQAEAD 150
Cdd:cd14879 211 PSDYallasYGCHPLPLGPGS-DDAEGF---QElktALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 151 GTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTkgqsveqvVF--AVGA------LAKATYDRLFRWLVSRINQTL- 221
Cdd:cd14879 287 NTDVLDIVAAFLGVSPEDLETSLTYKTKLVRKELCT--------VFldPEGAaaqrdeLARTLYSLLFAWVVETINQKLc 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 222 DTKLPRQFFIGVLDIAGFEIF---EFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDwvfidfgLDLQPCIDLI 298
Cdd:cd14879 359 APEDDFATFISLLDFPGFQNRsstGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVS-------VPATSYFDNS 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 299 EKVRRLRlsdvgGPhsysfcsqPLGILSILEEEC-MFPKASDASFRAKLYDNHAGKSPnFQQPRPDKKRKYQAHFEVVHY 377
Cdd:cd14879 432 DCVRLLR-----GK--------PGGLLGILDDQTrRMPKKTDEQMLEALRKRFGNHSS-FIAVGNFATRSGSASFTVNHY 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 378 AGVVPYSIVGWLEKNKDPLNETVVpifqksqnrllaTLyenyagscsteppksgvkekrkkaasFQTVSQLhKENLNKLM 457
Cdd:cd14879 498 AGEVTYSVEGFLERNGDVLSPDFV------------NL--------------------------LRGATQL-NAALSELL 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 458 TNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYrilnpsaIPDDTFMDSR 537
Cdd:cd14879 539 DTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERY-------KSTLRGSAAE 611
|
570 580
....*....|....*....|....*.
gi 768017794 538 KATEKLLGSLDLDHTQYQFGHTKVFF 563
Cdd:cd14879 612 RIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
2-528 |
3.26e-59 |
|
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: 216.66 E-value: 3.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 2 EAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmNP 81
Cdd:cd14874 109 KSFGCAKTLKNDEATRFGCSIDLLYKRNVLTGLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIK-GL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 82 YDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQR---EEQAEADGTESADK- 157
Cdd:cd14874 188 QKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNpnvEQDVVEIGNMSEVKw 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 158 AAYLMGVSSGDLLKGLLhPRVRVGNEYvtkgqSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLpRQFFIGVLDIA 237
Cdd:cd14874 268 VAFLLEVDFDQLVNFLL-PKSEDGTTI-----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPL-HTGVISILDHY 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 238 GFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDwvfIDFGLDLQpcidlIEKVRRLRLsdvggphsysF 317
Cdd:cd14874 341 GFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQLVDYAKDGIS---VDYKVPNS-----IENGKTVEL----------L 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 318 CSQPLGILSILEEECMFPKASDASFRAKLYDNHAGKSpNFQQPRpdkkRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLN 397
Cdd:cd14874 403 FKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRS-SYGKAR----NKERLEFGVRHCIGTTWYNVTDFFSRNKRIIS 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 398 ETVVPIFQKSQNRLLATLYENYAGSCSTEppksgvkekrkkaasFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENK 477
Cdd:cd14874 478 LSAVQLLRSSKNPIIGLLFESYSSNTSDM---------------IVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNER 542
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 768017794 478 TPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAI 528
Cdd:cd14874 543 QPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLPGDI 593
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
1-564 |
2.54e-56 |
|
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: 210.28 E-value: 2.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRK-PELQDMLLLSM 79
Cdd:cd14887 131 LEAFGNAHTVLNANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVaAATQKSSAGEG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 80 NPYDYhfcsqgvitvdnmnDGEELIAtdhAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADG-------- 151
Cdd:cd14887 211 DPEST--------------DLRRITA---AMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKltsvsvgc 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 152 ----------------------TESADK----AAYLMGVSSGD-----LLKGLLHPRVRVGNEYVTkgqsVEQVVFAVGA 200
Cdd:cd14887 274 eetaadrshssevkclssglkvTEASRKhlktVARLLGLPPGVegeemLRLALVSRSVRETRSFFD----LDGAAAARDA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 201 LAKATYDRLFRWLVSRINQTL-------------DTKLPRQF-FIGVLDIAGFEIFE---FNSFEQLCINFTNEKLQQFF 263
Cdd:cd14887 350 ACKNLYSRAFDAVVARINAGLqrsakpsesdsdeDTPSTTGTqTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFL 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 264 NQHMFVLEQEEYKREGI----DWVFIDFGLDLQPCIDLIEKVRRLRLSDVGGPHSYSFCSQP--LGILSILEEE-CMFPK 336
Cdd:cd14887 430 LEQLILNEHMLYTQEGVfqnqDCSAFPFSFPLASTLTSSPSSTSPFSPTPSFRSSSAFATSPslPSSLSSLSSSlSSSPP 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 337 ASDASFRAKLYDNHAGK----SPNFQQPRPDKKRKyQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVvpifqksqnrll 412
Cdd:cd14887 510 VWEGRDNSDLFYEKLNKniinSAKYKNITPALSRE-NLEFTVSHFACDVTYDARDFCRANREATSDEL------------ 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 413 atlyENYAGSCSTEPPKSGVKEKRKKAA---SFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLH 489
Cdd:cd14887 577 ----ERLFLACSTYTRLVGSKKNSGVRAissRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHR 652
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768017794 490 QLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDdtFMDSRKATEKLLGSLDLDHTQYQFGHTKVFFK 564
Cdd:cd14887 653 QLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALRE--ALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
1-512 |
1.40e-54 |
|
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: 203.98 E-value: 1.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHF---------GPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPEL 71
Cdd:cd14884 128 LESMSNATTIKNNNSSRCGRINLLIFeeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDED 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 72 QDMLLLSMNPYDYHFCSQGV------------ITVDNMNDGEELIATD--------HAMDILGFSVDEKCACYKIVGALL 131
Cdd:cd14884 208 LARRNLVRNCGVYGLLNPDEshqkrsvkgtlrLGSDSLDPSEEEKAKDeknfvallHGLHYIKYDERQINEFFDIIAGIL 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 132 HFGNMKFKQkqreeqaeadgtesadkAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFR 211
Cdd:cd14884 288 HLGNRAYKA-----------------AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFN 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 212 WLVSRINQT----------LDTKLPR--QFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREG 279
Cdd:cd14884 351 KIIEDINRNvlkckekdesDNEDIYSinEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYAREN 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 280 IDWVFIDFGlDLQPCIDLIEKVRRlRLSDVGGPHSysfCSQplgilsileeecmfpKASDASFRAKLYDNH--------- 350
Cdd:cd14884 431 IICCSDVAP-SYSDTLIFIAKIFR-RLDDITKLKN---QGQ---------------KKTDDHFFRYLLNNErqqqlegkv 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 351 -AGKSPNFQQPRPDKKRKYQAH-FEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRllaTLYENYAGscstepp 428
Cdd:cd14884 491 sYGFVLNHDADGTAKKQNIKKNiFFIRHYAGLVTYRINNWIDKNSDKIETSIETLISCSSNR---FLREANNG------- 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 429 ksgvkekrKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFP 508
Cdd:cd14884 561 --------GNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLS 632
|
....
gi 768017794 509 NRLL 512
Cdd:cd14884 633 HKIP 636
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
1-563 |
3.49e-43 |
|
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: 170.54 E-value: 3.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSG--RKPELQDMLLLS 78
Cdd:cd14893 141 LEAFGNAATRQNRNSSRFAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGvqHDPTLRDSLEMN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 79 MNPYDYHFCSQGVITVDNMNdgeeLIATDHAMDILGFSV-----DEKCACYKIVGALLHFGNMKF--KQKQREEQAEADG 151
Cdd:cd14893 221 KCVNEFVMLKQADPLATNFA----LDARDYRDLMSSFSAlrirkNQRVEIVRIVAALLHLGNVDFvpDPEGGKSVGGANS 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 152 TESADKAAYLMGVSSGDLLKGLL---HPRV------------RVGNEYVT--KGQSVEQVVFAVGALAKATYDRLFRWLV 214
Cdd:cd14893 297 TTVSDAQSCALKDPAQILLAAKLlevEPVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 215 SRINQTLDTKLPR---------QFFIGVLDIAGFEIFE--FNSFEQLCINFTNEKLQQFFNQHMFV-----LEQEEYKRE 278
Cdd:cd14893 377 ETLNGILGGIFDRyeksnivinSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 279 G--IDWVFIDFGLDLQPCIDLIEkvrrlrlsdvggphsysfcSQPLGILSILEEECMFPKASDASFRAKLY---DNHAGK 353
Cdd:cd14893 457 NrlTVNSNVDITSEQEKCLQLFE-------------------DKPFGIFDLLTENCKVRLPNDEDFVNKLFsgnEAVGGL 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 354 S-PN----FQQPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPP 428
Cdd:cd14893 518 SrPNmgadTTNEYLAPSKDWRLLFIVQHHCGKVTYNGKGLSSKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKA 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 429 KSGVKEKRKKAASFQTVSQLHKENLN--------------KLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCN 494
Cdd:cd14893 598 AKQTEERGSTSSKFRKSASSARESKNitdsaatdvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMN 677
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768017794 495 GVLEGIRICRQGFPNRLLYTDFRQRYRilnpsaipddTFMDSRKATEKLLGSLD----LDHTQYQFGHTKVFF 563
Cdd:cd14893 678 HLVELMQASRSIFTVHLTYGHFFRRYK----------NVCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
1-564 |
2.37e-37 |
|
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: 151.05 E-value: 2.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPE--LQDMLLLS 78
Cdd:cd14882 118 ILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQnrLKEYNLKA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 79 MNPYDYHFCSQGV-------ITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREeqAEADG 151
Cdd:cd14882 198 GRNYRYLRIPPEVppsklkyRRDDPEGNVERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELEN 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 152 TESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLdtKLPRQFF- 230
Cdd:cd14882 276 TEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKM--SFPRAVFg 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 231 ----IGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDliekvrrlrl 306
Cdd:cd14882 354 dkysISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRF-YDNKTAVD---------- 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 307 sdvggphsySFCSQPLGILSILEEecmfpkASDASFRAKLYDN--HAGKSPNFqqprpdkKRKYQAHFEVVHYAGVVPYS 384
Cdd:cd14882 423 ---------QLMTKPDGLFYIIDD------ASRSCQDQNYIMDriKEKHSQFV-------KKHSAHEFSVAHYTGRIIYD 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 385 IVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENyagscsteppkSGVKEKRKKAASFQTVSQlhkENLNKLMTNLRATQ 464
Cdd:cd14882 481 AREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-----------SQVRNMRTLAATFRATSL---ELLKMLSIGANSGG 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 465 PHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILnpsAIPDDTFMDSRKATEKLL 544
Cdd:cd14882 547 THFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFL---AFDFDETVEMTKDNCRLL 623
|
570 580
....*....|....*....|
gi 768017794 545 gSLDLDHTQYQFGHTKVFFK 564
Cdd:cd14882 624 -LIRLKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
1-516 |
2.31e-36 |
|
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: 148.32 E-value: 2.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmN 80
Cdd:cd14905 118 LESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLG-D 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQ-GVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQreEQAEADGTESADKAA 159
Cdd:cd14905 197 INSYHYLNQgGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKN--GKTEVKDRTLIESLS 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 160 YLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSveqvvfavgaLAKATYDRLFRWLVSRINQTLDtklPRQF--FIGVLDIA 237
Cdd:cd14905 275 HNITFDSTKLENILISDRSMPVNEAVENRDS----------LARSLYSALFHWIIDFLNSKLK---PTQYshTLGILDLF 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 238 GFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKvrrlrlsdvggphsysf 317
Cdd:cd14905 342 GQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQTERIPWMTPISFKDNEESVEMMEK----------------- 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 318 csqplgILSILEEECMFPKASDASFRAKLYD----NHA-GKSPNfqqprpdkkrkyqaHFEVVHYAGVVPYSIVGWLEKN 392
Cdd:cd14905 405 ------IINLLDQESKNINSSDQIFLEKLQNflsrHHLfGKKPN--------------KFGIEHYFGQFYYDVRGFIIKN 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 393 KDPLNETVVPIFQKSQNRLL----------ATLYE--------NYAG-----------SCSTEPPKSGVKEKRKK----- 438
Cdd:cd14905 465 RDEILQRTNVLHKNSITKYLfsrdgvfninATVAElnqmfdakNTAKksplsivkvllSCGSNNPNNVNNPNNNSggggg 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 439 -----------AASFQTVSqlhkeNLNKLMTNlRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGF 507
Cdd:cd14905 545 ggnsgggsgsgGSTYTTYS-----STNKAINN-SNCDFHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGY 618
|
570
....*....|...
gi 768017794 508 P----NRLLYTDF 516
Cdd:cd14905 619 TihynNKIFFDRF 631
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
1-562 |
1.74e-32 |
|
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: 136.50 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRIHFgPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGRKPELQDMLLLSmN 80
Cdd:cd14938 143 MEAFGNAKTVKNNNSSRFSKFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLK-N 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 81 PYDYHFCSQGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGN-------------MKFKQKQRE--- 144
Cdd:cd14938 221 IENYSMLNNEKGFEKFSDYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNiny 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 145 -------EQAEADGTESADKAAYLmgvsSGDLLKGLLHPRVR------VGNEYV-TKGQSVEQVVFAVGALAKATYDRLF 210
Cdd:cd14938 301 etilselENSEDIGLDENVKNLLL----ACKLLSFDIETFVKyfttnyIFNDSIlIKVHNETKIQKKLENFIKTCYEELF 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 211 RWLVSRINQTL-DTKLPRQF--FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDF 287
Cdd:cd14938 377 NWIIYKINEKCtQLQNININtnYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 288 GLDLQPCIDLIekvrrlrlsdVGGPHSYSFcsqplgilSILEEECMfPKASDASFRAKLYDNHAGKSPNFqqPRPDKKRK 367
Cdd:cd14938 457 NIDNEPLYNLL----------VGPTEGSLF--------SLLENVST-KTIFDKSNLHSSIIRKFSRNSKY--IKKDDITG 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 368 YQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENY----AGSCSTEPPKSGVKE-----KRKK 438
Cdd:cd14938 516 NKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSENEYMRQFCMFYnydnSGNIVEEKRRYSIQSalklfKRRY 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 439 AASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTP-GVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFR 517
Cdd:cd14938 596 DTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFL 675
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 768017794 518 QRYRILNPsaipddtfmDSRKATEKLLGSLDLDHTQYQFGHTKVF 562
Cdd:cd14938 676 SIFDIKNE---------DLKEKVEALIKSYQISNYEWMIGNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
977-1728 |
7.73e-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: 113.23 E-value: 7.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 977 EEAALRHEATVAALRRKQAEgAAELGEQVDSLQRVRQKLEK---EKSELR--------MEVDDLAANVETLTRAKASAEK 1045
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDI-LNELERQLKSLERQAEKAERykeLKAELRelelallvLRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1046 LCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKEcliSQLSRGKALAAQSLEELRRQLEEESKAKS 1125
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE---QQKQILRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1126 ALAHAVQALrhdcDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEAdaiqRTEELEEAKKKLALRLQEAE---EGV 1202
Cdd:TIGR02168 331 KLDELAEEL----AELEEKLEELKEELESLEAELEELEAELEELESRLEE----LEEQLETLRSKVAQLELQIAslnNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1203 EAANAKCSSLEKAKLRLQTESEDVTLELERATSAA-----AALDKKQRHLERALEERRRQEEEMQRELEAAQRESRGLGT 1277
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaelEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1278 ELFRLR---HGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALE-----------GEKSEIQAALE 1343
Cdd:TIGR02168 483 ELAQLQarlDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEaalggrlqavvVENLNAAKKAI 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1344 EAEGALELEETKTLRIQLELSQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLD--------AETRArnEALRLKKK 1415
Cdd:TIGR02168 563 AFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvVDDLD--NALELAKK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1416 MEGDLN------DLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAA 1489
Cdd:TIGR02168 641 LRPGYRivtldgDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1490 LEQGERSRRLAEQELLEA-------TERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAM 1562
Cdd:TIGR02168 721 LEELSRQISALRKDLARLeaeveqlEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1563 MAEELKKEQD--------------TSAHLERMKKTLEQTVRELQARLEEAEQAALRGgKKQVQKLEAKVRELEAELDAEQ 1628
Cdd:TIGR02168 801 LREALDELRAeltllneeaanlreRLESLERRIAATERRLEDLEEQIEELSEDIESL-AAEIEELEELIEELESELEALL 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1629 KKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYR-KAQHELDDAEER 1707
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEAL 959
|
810 820
....*....|....*....|....*..
gi 768017794 1708 ADMAETQANKLRARTR------DALGP 1728
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKrlenkiKELGP 986
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
637-1192 |
3.04e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.18 E-value: 3.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 637 LLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGK 716
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 717 VKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKA 796
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 797 LQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLEE 876
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 877 KLKKKDSELSQLSLRVEDEqllgAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASA 956
Cdd:COG1196 471 EAALLEAALAELLEELAEA----AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAA 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 957 GQREGCRKREAELGRLRRELEEAALRhEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETL 1036
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKAAKAG-RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1037 TRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLSRGKALAAQSLEELRRQ 1116
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768017794 1117 LEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQwrSKYEADAIQRteELEEAKKKLA 1192
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELP--EPPDLEELER--ELERLEREIE 777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
728-1693 |
2.16e-23 |
|
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: 108.61 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 728 EEVNADLAarrrKLEDECTELKKDIDDLELTLAKAEK--EKQATENKVKN--LTEEMAALDESVARLTKEKKALQEAHQQ 803
Cdd:TIGR02168 182 ERTRENLD----RLEDILNELERQLKSLERQAEKAERykELKAELRELELalLVLRLEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 804 ALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLrmdteraKRKLEGDLKLTQESVADAAQDKQQLEEKLKKKDS 883
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE-------ISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 884 ELSQLSLRVedeqllgAQMQKKIKELQARAEELEEELEAEraararvEKQRAEAARELEELSERLEEAGGASAGQREGCR 963
Cdd:TIGR02168 331 KLDELAEEL-------AELEEKLEELKEELESLEAELEEL-------EAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 964 KREAELGRLRRELEEAALRHEatvaalrrKQAEGAAELGEQVDSLQRvrQKLEKEKSELRMEVDDLAANVETLTRAKASA 1043
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRE--------RLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERLEEALEEL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1044 EKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKecliSQLSRGKALAAQSLEELRRQLEEESKA 1123
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ----SGLSGILGVLSELISVDEGYEAAIEAA 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1124 KSALAHAV-----QALRHDCDLLREQHEEEAE---AQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKKKLALRL 1195
Cdd:TIGR02168 543 LGGRLQAVvvenlNAAKKAIAFLKQNELGRVTflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLL 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1196 QeaeeGVEAANAKCSSLEKAKlRLQTESEDVTLELERATSaaaaldkkqrhleraleerrrqeeemqreleaaqresRGL 1275
Cdd:TIGR02168 623 G----GVLVVDDLDNALELAK-KLRPGYRIVTLDGDLVRP-------------------------------------GGV 660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1276 GTElfrlrhGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQaaleeaegaleleeTK 1355
Cdd:TIGR02168 661 ITG------GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLR--------------KE 720
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1356 TLRIQLELSQVKAEVDRkLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLElqlghatRQAT 1435
Cdd:TIGR02168 721 LEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE-------AQIE 792
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1436 EAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLH 1515
Cdd:TIGR02168 793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1516 SQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARL 1595
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT 952
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1596 EEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKS 1675
Cdd:TIGR02168 953 LEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
970
....*....|....*...
gi 768017794 1676 ykrQFEEAEQQANTNLAK 1693
Cdd:TIGR02168 1033 ---RFKDTFDQVNENFQR 1047
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1167-1728 |
2.42e-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: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1167 AQWRSKYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRH 1246
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1247 LERALEERRRQEEEMQRELEAAQRESRGLGTELfrlrhghEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEK 1326
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEEL-------EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1327 TKKALEGEKSEIQAALEEAEGALELEETKTLRIQLELSQVKAEVDRKLAEKDEECANLRRNHQRAVEslQASLDAETRAR 1406
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE--AAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1407 NEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDeEQRLAAELHEQAQALERRASLLAAELEEL 1486
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL-EGVKAALLLAGLRGLAGAVAVLIGVEAAY 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1487 RAALEQ--GERSRRLAEQELLEATERLNLLHSQNTG------LLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAIT 1558
Cdd:COG1196 537 EAALEAalAAALQNIVVEDDEVAAAAIEYLKAAKAGratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYY 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1559 DAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKgV 1638
Cdd:COG1196 617 VLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE-L 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1639 RKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAkyrKAQHELDDAEERADMAETQANKL 1718
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE---EEALEELPEPPDLEELERELERL 772
|
570
....*....|
gi 768017794 1719 RARtRDALGP 1728
Cdd:COG1196 773 ERE-IEALGP 781
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
645-1205 |
3.43e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.72 E-value: 3.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 645 EELAALRAELRGLRgaLAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERL 724
Cdd:COG1196 220 EELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 725 EDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQA 804
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 805 LGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKKDSE 884
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 885 LSQLSLRVEDEQLLGAQMQKKIKELQAraeeleeeleaeraararvekQRAEAARELEELSERLEEAGGASAGQREgcRK 964
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLE---------------------ELAEAAARLLLLLEAEADYEGFLEGVKA--AL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 965 REAELGRLRRELEEAALRHEATVAALRrkQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASAE 1044
Cdd:COG1196 515 LLAGLRGLAGAVAVLIGVEAAYEAALE--AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1045 KLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLSRGKALAAQSLEELRRQLEEESKAK 1124
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1125 SALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKKKLALRLQEAEEGVEA 1204
Cdd:COG1196 673 ALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA 752
|
.
gi 768017794 1205 A 1205
Cdd:COG1196 753 L 753
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
716-1310 |
5.31e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.86 E-value: 5.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 716 KVKELSERLEdEEEVNAdLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKK 795
Cdd:COG1196 214 RYRELKEELK-ELEAEL-LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 796 ALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLE 875
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 876 EKLKKKDSELSQLSLRVEDEQllgaqmqKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAggas 955
Cdd:COG1196 372 AELAEAEEELEELAEELLEAL-------RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE---- 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 956 agqregcRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEkekSELRMEVDDLAANVET 1035
Cdd:COG1196 441 -------EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL---LLLEAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1036 LTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESgelsrllEEKECLISQLSRGKALAAQSLEELRR 1115
Cdd:COG1196 511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE-------VAAAAIEYLKAAKAGRATFLPLDKIR 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1116 QLEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSK-YEADAIQRTEELEEAKKKLALR 1194
Cdd:COG1196 584 ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVtLAGRLREVTLEGEGGSAGGSLT 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1195 LQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQRESRG 1274
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
570 580 590
....*....|....*....|....*....|....*.
gi 768017794 1275 LGTELFRLRHGHEEALEALETLKRENKNLQEEISDL 1310
Cdd:COG1196 744 EEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
633-1541 |
6.63e-22 |
|
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: 103.60 E-value: 6.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 633 KMKPLLRSAQAEEELAALRAELRGLRGALAAA--EAKRQELEEThvsiTQEKNDLALQLQAEQDNLADAEERChlliksk 710
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELKAELRELELALLVLrlEELREELEEL----QEELKEAEEELEELTAELQELEEKL------- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 711 VQLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARL 790
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 791 TKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLEcslEQEKKLRMDTERAKRKLEgdlkltqesvadaaqd 870
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE---LQIASLNNEIERLEARLE---------------- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 871 kqQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQkkIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEE 950
Cdd:TIGR02168 411 --RLEDRRERLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 951 AGGasagqregcrkREAELGRLRRELEEAAlrheATVAALRRKQAEGAAELGeQVDSLQRVRQKLEKEKSE-LRMEVDDL 1029
Cdd:TIGR02168 487 LQA-----------RLDSLERLQENLEGFS----EGVKALLKNQSGLSGILG-VLSELISVDEGYEAAIEAaLGGRLQAV 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1030 AanVETLTRAKASAEKLcrtYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEekecLISQLSRGKALAAqs 1109
Cdd:TIGR02168 551 V--VENLNAAKKAIAFL---KQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKD----LVKFDPKLRKALS-- 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1110 leelrrqleeeskAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKanAEVAQWRSKYEADAIQRTEELEEAKK 1189
Cdd:TIGR02168 620 -------------YLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPG--GVITGGSAKTNSSILERRREIEELEE 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1190 KLAlrlqEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQ 1269
Cdd:TIGR02168 685 KIE----ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1270 RESRGLGTELfrlrhghEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGAL 1349
Cdd:TIGR02168 761 AEIEELEERL-------EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1350 ELEETKTLRIQLELSQVKAEVDrKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGH 1429
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIE-SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1430 ATRQATEAQAATRLMQAQLKEEQAGRDE-EQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRR-------LAE 1501
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlAAI 992
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 768017794 1502 QELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEE 1541
Cdd:TIGR02168 993 EEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1014-1626 |
1.41e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.32 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1014 KLEKEKSELRME--------VDD----LAANVETLTRAKASAEKLcRTYEDQLSEAKI-----KVEELQRQLADASTQRG 1076
Cdd:COG1196 171 KERKEEAERKLEateenlerLEDilgeLERQLEPLERQAEKAERY-RELKEELKELEAellllKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1077 RLQTESGELSRLLEEKECLISQLsrgkalaaqsleelRRQLEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQ 1156
Cdd:COG1196 250 ELEAELEELEAELAELEAELEEL--------------RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1157 RLLSKANAEVAQWRSKyEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSA 1236
Cdd:COG1196 316 ERLEELEEELAELEEE-LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1237 AAALDKKQRHLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSL 1316
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1317 SGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQLELSQVKAEVDRKLAEKDEECANLRrnhqRAVESLQ 1396
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA----LAAALQN 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1397 ASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRA 1476
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1477 SLLAAelEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKA 1556
Cdd:COG1196 631 RLEAA--LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE 708
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1557 ITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDA 1626
Cdd:COG1196 709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1423-1731 |
1.10e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 99.63 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1423 LELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQ 1502
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1503 ELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKK 1582
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1583 TLEQTVRELQARLEEAEQAALRgGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARM 1662
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAE-LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768017794 1663 QDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDALGPKLS 1731
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1164-1709 |
1.79e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 99.45 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1164 AEVAQWRSKYEADAIQRTEELEEAK-KKLALRLQEAEEGVEAANAKCSSLEKAKlrlqteSEDVTLELERATSAAAALDK 1242
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKKAEeKKKADEAKKAEEKKKADEAKKKAEEAKK------ADEAKKKAEEAKKKADAAKK 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1243 KQRHLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKR--ENKNLQEEISDLTDQVSLSGKS 1320
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKadEAKKKAEEDKKKADELKKAAAA 1416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1321 IQELEKTKKALEgeksEIQAALEEAEGALELEETKTLRIQLELSQvKAEVDRKLAEKDEECANLRRNHQRAVESLQASLD 1400
Cdd:PTZ00121 1417 KKKADEAKKKAE----EKKKADEAKKKAEEAKKADEAKKKAEEAK-KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1401 AEtRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAAtrlmQAQLKEEQAGRDEEQRLAAELheqaqaleRRAslla 1480
Cdd:PTZ00121 1492 AE-EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA----EEAKKADEAKKAEEKKKADEL--------KKA---- 1554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1481 aelEELRAALEqgersRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAitda 1560
Cdd:PTZ00121 1555 ---EELKKAEE-----KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA---- 1622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1561 ammaEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGG--KKQVQKLEAKVRELEAElDAEQKKHAEALKGV 1638
Cdd:PTZ00121 1623 ----EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAeeAKKAEEDKKKAEEAKKA-EEDEKKAAEALKKE 1697
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768017794 1639 RKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQAN---TNLAKYRKAQHELDDAEERAD 1709
Cdd:PTZ00121 1698 AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEeakKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1229-1726 |
3.00e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.00 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1229 ELERATSAAAALDKKQRHLERALEERRRQEEEMQreLEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEIS 1308
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAE--LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1309 DLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQLELSQVKAEVDRKLAEKDEECANLRRNH 1388
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1389 QRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQ 1468
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1469 AQALERRASLLA-AELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLE------ADLAQLSGEVEE 1541
Cdd:COG1196 459 EALLELLAELLEeAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglagavAVLIGVEAAYEA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1542 AAQERREAEEKAK--KAITDAAMMAEELKKEQD--------TSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQ 1611
Cdd:COG1196 539 ALEAALAAALQNIvvEDDEVAAAAIEYLKAAKAgratflplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1612 KLEAKVRELEAELDAEQKKHAEALKGVRK---------------HERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSY 1676
Cdd:COG1196 619 GDTLLGRTLVAARLEAALRRAVTLAGRLRevtlegeggsaggslTGGSRRELLAALLEAEAELEELAERLAEEELELEEA 698
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 768017794 1677 KRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDAL 1726
Cdd:COG1196 699 LLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
891-1705 |
1.79e-17 |
|
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: 89.08 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 891 RVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEaarelEELSERLEEAGGASAGQREGCRKREAE-- 968
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQE-----QLQAETELCAEAEEMRARLAARKQELEei 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 969 LGRLRRELEEAALRHEAtVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLtrakasaeklcr 1048
Cdd:pfam01576 77 LHELESRLEEEEERSQQ-LQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLL------------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1049 tyEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLsrgkalaaqsleelRRQLEEESKAKSALA 1128
Cdd:pfam01576 144 --EDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDL--------------EERLKKEEKGRQELE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1129 HAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELeEAKKKLALRLQEAEEGVEAANAK 1208
Cdd:pfam01576 208 KAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNAL-KKIRELEAQISELQEDLESERAA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1209 CSSLEKAKLRLQTESEDVTLELERATSAAAAldkkqrhlerALEERRRQEEEMQRELEAAQRESRGLGTELFRLRHGHEE 1288
Cdd:pfam01576 287 RNKAEKQRRDLGEELEALKTELEDTLDTTAA----------QQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQ 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1289 AL----EALETLKRENKN-------LQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEETKTL 1357
Cdd:pfam01576 357 ALeeltEQLEQAKRNKANlekakqaLESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLS 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1358 RIQLELSQVKA---EVDRKLAEKDEECANLRRNHQRAVESLQasldAETRARNEALRLKKKMEGDLNDLELQLGHATRQA 1434
Cdd:pfam01576 437 KLQSELESVSSllnEAEGKNIKLSKDVSSLESQLQDTQELLQ----EETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAK 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1435 TEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLL 1514
Cdd:pfam01576 513 RNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQ 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1515 HSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDT--------------------- 1573
Cdd:pfam01576 593 RQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAkeelertnkqlraemedlvss 672
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1574 ------SAH-LERMKKTLEQTVRELQARLEE-------AEQAALR---------------------GGKKQVQKLEAKVR 1618
Cdd:pfam01576 673 kddvgkNVHeLERSKRALEQQVEEMKTQLEEledelqaTEDAKLRlevnmqalkaqferdlqardeQGEEKRRQLVKQVR 752
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1619 ELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQ 1698
Cdd:pfam01576 753 ELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESE 832
|
....*..
gi 768017794 1699 HELDDAE 1705
Cdd:pfam01576 833 KKLKNLE 839
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1406-1737 |
2.54e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.46 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1406 RNEALRLKKKMEGDLN-------DLELQLGHATRQATEAQAATRLmqaqlkeeqagRDEEQRLAAELheqaQALERRASL 1478
Cdd:COG1196 174 KEEAERKLEATEENLErledilgELERQLEPLERQAEKAERYREL-----------KEELKELEAEL----LLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1479 LAAELEELRAALEQGERSRRLAEQELLEAT-ERLNLLHSQNTGLLNQKKK----LEADLAQLSGEVEEAAQERREAEEKA 1553
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAElEELRLELEELELELEEAQAeeyeLLAELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1554 KKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRggkkqvqkLEAKVRELEAELDAEQKKHAE 1633
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE--------AEAELAEAEEELEELAEELLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1634 ALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAET 1713
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
330 340
....*....|....*....|....
gi 768017794 1714 QANKLRARTRDALGPKLSLSPQHK 1737
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLL 494
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
715-1600 |
8.00e-16 |
|
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: 83.96 E-value: 8.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 715 GKVKELSERLEDEEEVNADLAARRRKLEDECTELKKdIDDLELTLAKAE-----KEKQATENKVKNLTEEMAALDESVAR 789
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 790 LTKEKKALQEAHQQALGDLQAEEDRVSALTKAK-LRLEQQVEDLECSLEQekklrmdterakrkLEGDLKLTQESVADAA 868
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqLRVKEKIGELEAEIAS--------------LERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 869 QDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAeeleeeleaeraararvEKQRAEAARELEelserl 948
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL-----------------EDLRAELEEVDK------ 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 949 eeaggASAGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAaELGEQVDSLQRVRQKLEKEKSELRMEVDD 1028
Cdd:TIGR02169 379 -----EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA-DLNAAIAGIEAKINELEEEKEDKALEIKK 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1029 LAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKEC-------LISQLSR 1101
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGS 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1102 GKALAAQSLeelrrqleeeskaKSALAHAVQALRHDCDLLreqheeeaeaQAELQRLLSKANAEVAQWRSKYEADAIQRT 1181
Cdd:TIGR02169 533 VGERYATAI-------------EVAAGNRLNNVVVEDDAV----------AKEAIELLKRRKAGRATFLPLNKMRDERRD 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1182 EEL--EEAKKKLALRLQEAEEGVEAANAKC-------SSLEKAKlRLQTESEDVTLE---LERATS------AAAALDKK 1243
Cdd:TIGR02169 590 LSIlsEDGVIGFAVDLVEFDPKYEPAFKYVfgdtlvvEDIEAAR-RLMGKYRMVTLEgelFEKSGAmtggsrAPRGGILF 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1244 QRHLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQE 1323
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1324 LEktkKALEGEKSEIQaaleeaegaleleetktlriqlELSQVKAEVDRKLAEKDEECANLRR--NHQRaVESLQASLDA 1401
Cdd:TIGR02169 749 LE---QEIENVKSELK----------------------ELEARIEELEEDLHKLEEALNDLEArlSHSR-IPEIQAELSK 802
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1402 --ETRARNEAlrLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQA-------L 1472
Cdd:TIGR02169 803 leEEVSRIEA--RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEleaalrdL 880
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1473 ERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAA-----QERR 1547
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELsledvQAEL 960
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....
gi 768017794 1548 EAEEKAKKAITDAAMMA-EELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQ 1600
Cdd:TIGR02169 961 QRVEEEIRALEPVNMLAiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1170-1725 |
1.22e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.27 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1170 RSKYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANaKCSSLEKAKLRLQTESEDVTLELERATSA-----AAALDKKQ 1244
Cdd:PTZ00121 1170 RKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAAR-KAEEERKAEEARKAEDAKKAEAVKKAEEAkkdaeEAKKAEEE 1248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1245 RHLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLrhghEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQEL 1324
Cdd:PTZ00121 1249 RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA----EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKA 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1325 EKTKKALEGEKSEIQAALEEAEGALELEETKtlRIQLELSQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETR 1404
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAA--ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1405 ARNEALRLKKKMEGDLNDLELQL-GHATRQATEAQAATRlmQAQLKEEQAGRDEEQRLAAELHEQAQAlERRASLLAAEL 1483
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKkAEEKKKADEAKKKAE--EAKKADEAKKKAEEAKKAEEAKKKAEE-AKKADEAKKKA 1479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1484 EELRAAleqgERSRRLAEQELLEATERlnllhsqntgllnQKKKLEADLAQLSGEVEEA--AQERREAEEKAKkaiTDAA 1561
Cdd:PTZ00121 1480 EEAKKA----DEAKKKAEEAKKKADEA-------------KKAAEAKKKADEAKKAEEAkkADEAKKAEEAKK---ADEA 1539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1562 MMAEELKKEQDTSaHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKgvRKH 1641
Cdd:PTZ00121 1540 KKAEEKKKADELK-KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK--KAE 1616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1642 ERRVK-ELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEE----AEQQANTNLAKYRKAQhELDDAEERADMAETQAN 1716
Cdd:PTZ00121 1617 EAKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkikAAEEAKKAEEDKKKAE-EAKKAEEDEKKAAEALK 1695
|
....*....
gi 768017794 1717 KLRARTRDA 1725
Cdd:PTZ00121 1696 KEAEEAKKA 1704
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
1-504 |
7.44e-15 |
|
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: 80.56 E-value: 7.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKF--IRIHFGPSG---KLASADIDSYLLEKSRVIFQL------PGERSYHVYYQILSGRKP 69
Cdd:cd14894 256 LEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYAMVAGVNA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 70 ELQDMLLLSMNPYDYHFCSQ------------GVITVDNM--NDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGN 135
Cdd:cd14894 336 FPFMRLLAKELHLDGIDCSAltylgrsdhklaGFVSKEDTwkKDVERWQQVIDGLDELNVSPDEQKTIFKVLSAVLWLGN 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 136 MKFKQKQREEQAEADGT---ESADKAAYLMGVSSGDLLKGLLHPR-VRVGNEYVTKGQSVE--QVVFAVGALAKATYDRL 209
Cdd:cd14894 416 IELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsVSLQSTSETFEVTLEkgQVNHVRDTLARLLYQLA 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 210 FRWLVSRINQTL----------------DTKLPRQF-FIGVLDIAGFEIFEFNSFEQLCINFTNEKLqqffnqhmfvleq 272
Cdd:cd14894 496 FNYVVFVMNEATkmsalstdgnkhqmdsNASAPEAVsLLKIVDVFGFEDLTHNSLDQLCINYLSEKL------------- 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 273 eeYKREgidwvfidfgldlQPCIDLIEKVRRLRLSDVGGPHSYSFCSQPLGILSILEEECMFPKASDAS----------F 342
Cdd:cd14894 563 --YARE-------------EQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENMNaqqeekrnklF 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 343 RAKLYDNHAGKSPNFQQPRPDKKRKYQAHFEVV-----HYAGVVPYSIVGWLEKNKDPL-NETVVPIFQKSQNRLLATLY 416
Cdd:cd14894 628 VRNIYDRNSSRLPEPPRVLSNAKRHTPVLLNVLpfvipHTRGNVIYDANDFVKKNSDFVyANLLVGLKTSNSSHFCRMLN 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 417 ENYAGSCSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGV 496
Cdd:cd14894 708 ESSQLGWSPNTNRSMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRL 787
|
....*...
gi 768017794 497 LEGIRICR 504
Cdd:cd14894 788 IRQMEICR 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
966-1721 |
7.79e-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: 80.50 E-value: 7.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 966 EAELGRLRRELEEAALRHEATVAALRrkqaegaaELGEQVDSLQRVRQKLEKEKsELRMEVDDLAANVetLTRAKASAEK 1045
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIID--------EKRQQLERLRREREKAERYQ-ALLKEKREYEGYE--LLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1046 LCRTYEDQLSEAKIKVEELQRQLADastqrgrLQTESGELSRLLEEKECLISQLSRGKALAAQSLeelrrqleeeskaks 1125
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISE-------LEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEK--------------- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1126 alahavqalrhdcdllreqheeeaeaqaelqrlLSKANAEVAQWRSKyEADAIQRTEELEEAKKKLALRLQEAEEGVEAA 1205
Cdd:TIGR02169 296 ---------------------------------IGELEAEIASLERS-IAEKERELEDAEERLAKLEAEIDKLLAEIEEL 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1206 NAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLRHG 1285
Cdd:TIGR02169 342 EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEE 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1286 HEEALEALETLKRENKNLQEEISDLTDQVSlsgKSIQELEKTKKALEGEKSEIqaaleeaegalELEETKTLRIQLELSQ 1365
Cdd:TIGR02169 422 LADLNAAIAGIEAKINELEEEKEDKALEIK---KQEWKLEQLAADLSKYEQEL-----------YDLKEEYDRVEKELSK 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1366 VKAEVDRKLAEKDE---------------------------ECANLRRNHQRAVES-----LQASLDAETRARNEALRLK 1413
Cdd:TIGR02169 488 LQRELAEAEAQARAseervrggraveevlkasiqgvhgtvaQLGSVGERYATAIEVaagnrLNNVVVEDDAVAKEAIELL 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1414 KKMEG-------------------------------DLNDLELQLGHATRQA-------TEAQAATRLM--------QAQ 1447
Cdd:TIGR02169 568 KRRKAgratflplnkmrderrdlsilsedgvigfavDLVEFDPKYEPAFKYVfgdtlvvEDIEAARRLMgkyrmvtlEGE 647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1448 LKEEQ----AGRDEEQRL---AAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTG 1520
Cdd:TIGR02169 648 LFEKSgamtGGSRAPRGGilfSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1521 LLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMkkTLEQTVRELQARLEEAEq 1600
Cdd:TIGR02169 728 LEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR--LSHSRIPEIQAELSKLE- 804
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1601 aalrggkKQVQKLEAKVRELEAELDAE-------QKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKV 1673
Cdd:TIGR02169 805 -------EEVSRIEARLREIEQKLNRLtlekeylEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 768017794 1674 KSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRAR 1721
Cdd:TIGR02169 878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
854-1583 |
1.48e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.80 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 854 EGDLKLTQESVADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQ 933
Cdd:PTZ00121 1078 DFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIA 1157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 934 RAEAARELEELSERLEEAGGASAGQR-------EGCRK----REAELGRLRRELE--EAALRHEATVAALRRKQAEGAAE 1000
Cdd:PTZ00121 1158 RKAEDARKAEEARKAEDAKKAEAARKaeevrkaEELRKaedaRKAEAARKAEEERkaEEARKAEDAKKAEAVKKAEEAKK 1237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1001 LGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRqlADASTQRGRLQT 1080
Cdd:PTZ00121 1238 DAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK--ADEAKKKAEEAK 1315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1081 ESGELSRLLEEKEclisqlSRGKALAAQSLEELRRQLEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLS 1160
Cdd:PTZ00121 1316 KADEAKKKAEEAK------KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1161 KANAEVAQWRSKYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKlrlqteSEDVTLELERATSAAAAL 1240
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK------ADEAKKKAEEAKKAEEAK 1463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1241 DKKQRHLERALEERRRQEEEMQRELEAAQRESRGLGTElfrLRHGHEEALEALETLKRENKNLQEEISDLTDqvSLSGKS 1320
Cdd:PTZ00121 1464 KKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE---AKKAAEAKKKADEAKKAEEAKKADEAKKAEE--AKKADE 1538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1321 IQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRiqlELSQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLD 1400
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK---NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1401 AETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLA 1480
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1481 AELEELRAALE---QGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEaDLAQLSGEVEEAAQERREAEEKAKKAI 1557
Cdd:PTZ00121 1696 KEAEEAKKAEElkkKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE-EAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
730 740
....*....|....*....|....*.
gi 768017794 1558 TDAAMMAEELKKEQDTSAHLERMKKT 1583
Cdd:PTZ00121 1775 KEKEAVIEEELDEEDEKRRMEVDKKI 1800
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
920-1707 |
5.63e-14 |
|
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: 77.80 E-value: 5.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 920 LEAERAARARVEKQRAEAARELEELSERLEEAggasAGQREGCRKREAELGRLR-RELEEAALRHEATVAALRRKQAEgA 998
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERL----RREREKAERYQALLKEKReYEGYELLKEKEALERQKEAIERQ-L 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 999 AELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLT-----RAKASAEKL---CRTYEDQLSEAKIKVEELQRQLAD 1070
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGeeeqlRVKEKIGELeaeIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1071 ASTQRGRLQTESGELSRLLEEKECLISQLSRGKALAAQSLEELRRQLEEESKAKSALAHAVQALRHDCDLLREQHEEEAE 1150
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1151 AQAELQRLLSKANAEVAQWRSKYeADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLEL 1230
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAI-AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1231 ERATSAAAALDKKQRhlerALEERRRQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEA-----LETLKRENKNLQE 1305
Cdd:TIGR02169 486 SKLQRELAEAEAQAR----ASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVaagnrLNNVVVEDDAVAK 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1306 EISDLTDQVSLSGKSIQELEKTKKALegekseiqaaleeaegaleleetKTLRIQLELSQVKAEVDrkLAEKDEECANLR 1385
Cdd:TIGR02169 562 EAIELLKRRKAGRATFLPLNKMRDER-----------------------RDLSILSEDGVIGFAVD--LVEFDPKYEPAF 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1386 RNHQR---AVESLQA-----------SLDAE-----------TRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAA 1440
Cdd:TIGR02169 617 KYVFGdtlVVEDIEAarrlmgkyrmvTLEGElfeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSE 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1441 TRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTG 1520
Cdd:TIGR02169 697 LRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1521 LLNQKKKLEADLAQlsGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEE--A 1598
Cdd:TIGR02169 777 LEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSieK 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1599 EQAALRGGKK----QVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVK 1674
Cdd:TIGR02169 855 EIENLNGKKEeleeELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
|
810 820 830
....*....|....*....|....*....|...
gi 768017794 1675 SYKRQFEEaEQQANTNLAKYRKAQHELDDAEER 1707
Cdd:TIGR02169 935 EIEDPKGE-DEEIPEEELSLEDVQAELQRVEEE 966
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
708-1597 |
8.32e-14 |
|
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: 77.32 E-value: 8.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 708 KSKVQLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESV 787
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 788 ARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLeQQVEDLECSLEQEKKlrmdtERAKRKLEGDLKLTQESvada 867
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKL-QEEELKLLAKEEEEL-----KSELLKLERRKVDDEEK---- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 868 aqdKQQLEEKLKKKDSELSQLSlrvedEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSER 947
Cdd:pfam02463 316 ---LKESEKEKKKAEKELKKEK-----EEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLS 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 948 LEEAGGASAGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVD 1027
Cdd:pfam02463 388 SAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1028 DLAANVETLTRAKASAEKLcrtyEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLSRGKALAA 1107
Cdd:pfam02463 468 KKSEDLLKETQLVKLQEQL----ELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKV 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1108 QSLEELRRQLEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEA 1187
Cdd:pfam02463 544 AISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAK 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1188 KKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLeleratSAAAALDKKQRHLERALEERRRQEEEMQRELEA 1267
Cdd:pfam02463 624 VVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEV------KASLSELTKELLEIQELQEKAESELAKEEILRR 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1268 AQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSgKSIQELEKTKKALEGEKSEIQAALEEAEG 1347
Cdd:pfam02463 698 QLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDE-EEEEEEKSRLKKEEKEEEKSELSLKEKEL 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1348 ALELEETKTLRIQLELSQVKAEVDRKLAEKDEEC-ANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQ 1426
Cdd:pfam02463 777 AEEREKTEKLKVEEEKEEKLKAQEEELRALEEELkEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEEL 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1427 LGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALErrasllaaelEELRAALEQGERSRRLAEQELLE 1506
Cdd:pfam02463 857 ERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELE----------EESQKLNLLEEKENEIEERIKEE 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1507 ATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERM----KK 1582
Cdd:pfam02463 927 AEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLeeekKK 1006
|
890
....*....|....*
gi 768017794 1583 TLEQTVRELQARLEE 1597
Cdd:pfam02463 1007 LIRAIIEETCQRLKE 1021
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1367-1729 |
2.27e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.95 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1367 KAEVDRKLAEKDEECANLRRNHQ-RAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQ 1445
Cdd:PTZ00121 1116 KAEEAKKKAEDARKAEEARKAEDaRKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRK 1195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1446 AQ--LKEEQAGRDEEQRLAAEL--HEQAQALE--RRASLLAAELEELRAALEQ--GERSRRLAEQELLEATERLNLLHSQ 1517
Cdd:PTZ00121 1196 AEdaRKAEAARKAEEERKAEEArkAEDAKKAEavKKAEEAKKDAEEAKKAEEErnNEEIRKFEEARMAHFARRQAAIKAE 1275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1518 NTGLLNQKKKLE----ADLAQLSGEVEEAAQERREAEEK-----AKKAITDAAMMAEELKKEQdtsahlERMKKTLEQTV 1588
Cdd:PTZ00121 1276 EARKADELKKAEekkkADEAKKAEEKKKADEAKKKAEEAkkadeAKKKAEEAKKKADAAKKKA------EEAKKAAEAAK 1349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1589 RELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDK 1668
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEE 1429
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768017794 1669 LQsKVKSYKRQFEEAEQ--QANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDALGPK 1729
Cdd:PTZ00121 1430 KK-KADEAKKKAEEAKKadEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
712-1075 |
2.53e-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: 75.48 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 712 QLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLT 791
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 792 KEKKALqeahqqalgdlqaeEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDK 871
Cdd:TIGR02168 761 AEIEEL--------------EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 872 QQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEA 951
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 952 GGASAGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAA 1031
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGP 986
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 768017794 1032 -NVETLTRAKASAEK---LCRTYEDqLSEAKIKVEELQRQLADASTQR 1075
Cdd:TIGR02168 987 vNLAAIEEYEELKERydfLTAQKED-LTEAKETLEEAIEEIDREARER 1033
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1244-1726 |
1.41e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.03 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1244 QRHLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQV-SLSGKSIQ 1322
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1323 ELEKTKKALEGEKSEIQaaleeaegaleleetktlRIQLELSQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAE 1402
Cdd:COG4913 342 QLEREIERLERELEERE------------------RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEAL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1403 TRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAEL------HEQAQ-ALER- 1474
Cdd:COG4913 404 EEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGELievrpeEERWRgAIERv 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1475 ----RASLL--AAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNqkkKLEADLAQLSGEVEEAAQERR- 1547
Cdd:COG4913 484 lggfALTLLvpPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAG---KLDFKPHPFRAWLEAELGRRFd 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1548 -------EAEEKAKKAITDAAMM-----AEELKKEQDTSAHL------ERMKKTLEQTVRELQARLEEAEQaalrggkkQ 1609
Cdd:COG4913 561 yvcvdspEELRRHPRAITRAGQVkgngtRHEKDDRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEE--------R 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1610 VQKLEAKVRELEAELDAEQK--KHAEALKGVRKHERRVKELayqaEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQA 1687
Cdd:COG4913 633 LEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAEL----EAELERLDASSDDLAALEEQLEELEAELEELEEEL 708
|
490 500 510
....*....|....*....|....*....|....*....
gi 768017794 1688 NTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDAL 1726
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
643-1334 |
7.53e-12 |
|
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: 70.87 E-value: 7.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 643 AEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKV-QLEGKVKELS 721
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIaSLERSIAEKE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 722 ERLEDeeevnadLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAH 801
Cdd:TIGR02169 315 RELED-------AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 802 QQalgdlqaeedRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGdlklTQESVADAAQDKQQLEEKLKKK 881
Cdd:TIGR02169 388 KD----------YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG----IEAKINELEEEKEDKALEIKKQ 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 882 DSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLE------------ 949
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsv 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 950 ---------EAGGASAG------------------QREGCRKREAELGRLRRELEEAALRHEATVAAL--------RRKQ 994
Cdd:TIGR02169 534 geryataieVAAGNRLNnvvveddavakeaiellkRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFavdlvefdPKYE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 995 AEGAAELGEQ--VDSLQRVRQKLEK-----------EKS------------------ELRMEVDDLAANVETLTRAKASA 1043
Cdd:TIGR02169 614 PAFKYVFGDTlvVEDIEAARRLMGKyrmvtlegelfEKSgamtggsraprggilfsrSEPAELQRLRERLEGLKRELSSL 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1044 EKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLSRGKALAAQSLEELRRQLEEESKA 1123
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1124 KSALAHAVQALRHDcdllreqheEEAEAQAELQRLLSKANAEVAQWRSkyeadaiqRTEELEEAKKKLALRLQEAEEGVE 1203
Cdd:TIGR02169 774 LHKLEEALNDLEAR---------LSHSRIPEIQAELSKLEEEVSRIEA--------RLREIEQKLNRLTLEKEYLEKEIQ 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1204 AANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLR 1283
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 768017794 1284 HGHEEALEALETLKRENKNLQEEISDLTdQVSLSGKSIQELEKTKKALEGE 1334
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGEDE-EIPEEELSLEDVQAELQRVEEE 966
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1368-1724 |
7.66e-12 |
|
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: 70.87 E-value: 7.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1368 AEVDRKLAEKDEECANLRRNHQRA---VESLQASLDAETRARNEALRLKkkmegdlndlELQLGHATRQATEAQAATRLM 1444
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLdliIDEKRQQLERLRREREKAERYQ----------ALLKEKREYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1445 QAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELraaleqGERSRRLAEQELLEATERLNLLHSQntgllnq 1524
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL------NKKIKDLGEEEQLRVKEKIGELEAE------- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1525 KKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAAlr 1604
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF-- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1605 ggkkqvQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAE 1684
Cdd:TIGR02169 381 ------AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE 454
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 768017794 1685 QQANTNLA--------------KYRKAQHELDDAEERADMAETQANKLRARTRD 1724
Cdd:TIGR02169 455 WKLEQLAAdlskyeqelydlkeEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1174-1721 |
9.90e-12 |
|
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: 70.47 E-value: 9.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1174 EADAIQRTEELEEA---------KKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESE------DVTLELERATSAAA 1238
Cdd:TIGR02168 151 EAKPEERRAIFEEAagiskykerRKETERKLERTRENLDRLEDILNELERQLKSLERQAEkaerykELKAELRELELALL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1239 ALDKKQRHLERALEERRRQEEEMQreLEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQvslsg 1318
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEE--LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ----- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1319 ksIQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQLELSQVKAEVDRkLAEKDEECANLRRNHQRAVESLQAS 1398
Cdd:TIGR02168 304 --KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES-LEAELEELEAELEELESRLEELEEQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1399 LDAETRARNEALRLKKKMEGDLNDLELQL----GHATRQATEAQAATRLMQAQLKEEQAGRDEEqrLAAELHEQAQALER 1474
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLerleDRRERLQQEIEELLKKLEEAELKELQAELEE--LEEELEELQEELER 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1475 raslLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHS---QNTGLLNQKKKLEADLAQLSG-------------- 1537
Cdd:TIGR02168 459 ----LEEALEELREELEEAEQALDAAERELAQLQARLDSLERlqeNLEGFSEGVKALLKNQSGLSGilgvlselisvdeg 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1538 ---EVEEAAQERREA-----EEKAKKAI--------TDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQA 1601
Cdd:TIGR02168 535 yeaAIEAALGGRLQAvvvenLNAAKKAIaflkqnelGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1602 ----------------------------------------ALRGG----------------KKQVQKLEAKV-------R 1618
Cdd:TIGR02168 615 rkalsyllggvlvvddldnalelakklrpgyrivtldgdlVRPGGvitggsaktnssilerRREIEELEEKIeeleekiA 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1619 ELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQ 1698
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
650 660
....*....|....*....|...
gi 768017794 1699 HELDDAEERADMAETQANKLRAR 1721
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 ... |
642-1093 |
1.21e-11 |
|
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: 70.20 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 642 QAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADaeerchllikskvqLEGKVKELS 721
Cdd:pfam01576 542 ALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSN--------------LEKKQKKFD 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 722 ERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAAL-------DESVARLTKEK 794
Cdd:pfam01576 608 QMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLvsskddvGKNVHELERSK 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 795 KALQEAHQQALGDLQAEEDRVSALTKAKLRLE-----------------------------QQVEDLECSLEQEKKLRMD 845
Cdd:pfam01576 688 RALEQQVEEMKTQLEELEDELQATEDAKLRLEvnmqalkaqferdlqardeqgeekrrqlvKQVRELEAELEDERKQRAQ 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 846 TERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERA 925
Cdd:pfam01576 768 AVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQE 847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 926 ARARVEKQRAEAARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEG---AAELG 1002
Cdd:pfam01576 848 DLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVeqlTTELA 927
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1003 EQVDSLQRV---RQKLEKEKSELRMEVDDLAANV----------------------ETLTRAKASAEKLCRTYEDQLSEA 1057
Cdd:pfam01576 928 AERSTSQKSesaRQQLERQNKELKAKLQEMEGTVkskfkssiaaleakiaqleeqlEQESRERQAANKLVRRTEKKLKEV 1007
|
490 500 510
....*....|....*....|....*....|....*.
gi 768017794 1058 KIKVEELQRQLADASTQRGRLQTESGELSRLLEEKE 1093
Cdd:pfam01576 1008 LLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAE 1043
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1180-1729 |
1.89e-11 |
|
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: 69.43 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1180 RTEELEEAKKKLALRLQEAEEgveaanaKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEE 1259
Cdd:pfam01576 69 RKQELEEILHELESRLEEEEE-------RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDIL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1260 EMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQ 1339
Cdd:pfam01576 142 LLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1340 AALEEAEGALELEETKTLRIQLELSQVKAEVDRKLAEKDEECANLRRnHQRAVESLQASLDAETRARNEALRLKKKMEGD 1419
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRE-LEAQISELQEDLESERAARNKAEKQRRDLGEE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1420 LNDLELQL-----GHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLA----------AELHEQ--------------AQ 1470
Cdd:pfam01576 301 LEALKTELedtldTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQemrqkhtqalEELTEQleqakrnkanlekaKQ 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1471 ALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEA-------- 1542
Cdd:pfam01576 381 ALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAegknikls 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1543 ------------AQERREAEEKAKKAIT--------DAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQA- 1601
Cdd:pfam01576 461 kdvsslesqlqdTQELLQEETRQKLNLStrlrqledERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTl 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1602 -ALRGGKKQVQkleakvRELEAELDAEQKKHAEALKGVRKHERRVKEL------AYQAEEDRKNLARMQDLVDKLQSKVK 1674
Cdd:pfam01576 541 eALEEGKKRLQ------RELEALTQQLEEKAAAYDKLEKTKNRLQQELddllvdLDHQRQLVSNLEKKQKKFDQMLAEEK 614
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 768017794 1675 SYKRQFEE----AEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDALGPK 1729
Cdd:pfam01576 615 AISARYAEerdrAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSK 673
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1281-1727 |
2.86e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.53 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1281 RLRHGHEEALEALETL--KRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGAleleetktlr 1358
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQieEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER---------- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1359 iQLELSQVKAEVDrKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLghATRQATEAQ 1438
Cdd:PRK02224 250 -REELETLEAEIE-DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARR--EELEDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1439 AATRLMQAQLKEEQAGRDEEQRL--AAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHS 1516
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLRedADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1517 QNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAitdAAMMAE----ELKKEQDTSAHLERMKKTLEQtVRELQ 1592
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEA---EALLEAgkcpECGQPVEGSPHVETIEEDRER-VEELE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1593 ARLEEAEQaalrggkkQVQKLEAKVRELEAELDAEqkKHAEALKGVRKH-ERRVKELAYQAEEDRKNLARMQDLVDKLQS 1671
Cdd:PRK02224 482 AELEDLEE--------EVEEVEERLERAEDLVEAE--DRIERLEERREDlEELIAERRETIEEKRERAEELRERAAELEA 551
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 768017794 1672 KVKSYKRQFEEAEQQANT---NLAKYRKAQHELDDAEERADMAETQANkLRARTRDALG 1727
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEareEVAELNSKLAELKERIESLERIRTLLA-AIADAEDEIE 609
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
638-910 |
7.37e-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: 67.40 E-value: 7.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 638 LRSAQAEEELAALRAELRGLRGALAAAEAKRQELEEthvsitqekndlalQLQAEQDNLADAEERCHLLIKSKVQLEGKV 717
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSSLQSELRRIEN--------------RLDELSQELSDASRKIGEIEKEIEQLEQEE 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 718 KELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATE-----NKVKNLTEEMAALDESVARLTK 792
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEarlshSRIPEIQAELSKLEEEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 793 EKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQ 872
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD 892
|
250 260 270
....*....|....*....|....*....|....*...
gi 768017794 873 QLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQ 910
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
641-841 |
3.26e-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: 64.01 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 641 AQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKEL 720
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 721 SERLED------------------EEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAA 782
Cdd:COG4942 103 KEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 768017794 783 LDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKK 841
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
663-1101 |
4.21e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.16 E-value: 4.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 663 AAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLEDEEEVNADLAARRRKLE 742
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 743 DECTELKKDIDDLEltlAKAEKEKQATENKVKnlTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAK 822
Cdd:PTZ00121 1391 KKADEAKKKAEEDK---KKADELKKAAAAKKK--ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK 1465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 823 LRLEQQVEDLECSLEQEKKlrmdTERAKRKLEgdlkltqESVADAAQDKQQLEEKlkKKDSELSQLSLRVEDEQLLGAQM 902
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKK----ADEAKKKAE-------EAKKKADEAKKAAEAK--KKADEAKKAEEAKKADEAKKAEE 1532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 903 QKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAALR 982
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 983 HEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRA----KASAEKLCRTYEDQ--LSE 1056
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKaeedKKKAEEAKKAEEDEkkAAE 1692
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 768017794 1057 AKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLSR 1101
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1382-1606 |
4.77e-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: 63.63 E-value: 4.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1382 ANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQL----KEEQAGRDE 1457
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeleKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1458 EQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSG 1537
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768017794 1538 EVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGG 1606
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
710-1092 |
4.91e-10 |
|
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: 64.15 E-value: 4.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 710 KVQLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVAR 789
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 790 LTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQ 869
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 870 DKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAAreleelserle 949
Cdd:pfam07888 193 EFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELS----------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 950 eaggASAGQREgcrKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSEL-RMEVdd 1028
Cdd:pfam07888 262 ----SMAAQRD---RTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELqRLEE-- 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768017794 1029 lAANVETLTRAKASAE----KLCRTYedQLSEAKIKVEELQRQLADASTQRGRLQTESGEL---SRLLEEK 1092
Cdd:pfam07888 333 -RLQEERMEREKLEVElgreKDCNRV--QLSESRRELQELKASLRVAQKEKEQLQAEKQELleyIRQLEQR 400
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1170-1721 |
7.24e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 7.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1170 RSKYEADAIQRTEELEEakkklalRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRhler 1249
Cdd:PRK03918 177 RIERLEKFIKRTENIEE-------LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEK---- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1250 aleerrrqeeemqrELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLqEEISDLTDQVSLSGKSIQELEKTKK 1329
Cdd:PRK03918 246 --------------ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1330 ALEGEKSEIQAALEEAEGALELEETKTLRIQlELSQVKAEVDRKLA--EKDEECANLRRNHQRAVESLQASLDAET---- 1403
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEelEERHELYEEAKAKKEELERLKKRLTGLTpekl 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1404 -RARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAA-TRLMQAQLKEEQAGR----DEEQRLAAELHEQAQALERRAS 1477
Cdd:PRK03918 390 eKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAiEELKKAKGKCPVCGRelteEHRKELLEEYTAELKRIEKELK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1478 LLAAELEELRAALEQGERsrrlaeqeLLEATERLNLLHSqntgLLNQKKKLEADLAQLSGE-VEEAAQERREAEEKAKKA 1556
Cdd:PRK03918 470 EIEEKERKLRKELRELEK--------VLKKESELIKLKE----LAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKL 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1557 ITDAAMMAEELKKEQDtsahLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEaELDAEQKKHAEALK 1636
Cdd:PRK03918 538 KGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAEK 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1637 GVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNL-----AKYRKAQHELDDAEERADMA 1711
Cdd:PRK03918 613 ELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEylelsRELAGLRAELEELEKRREEI 692
|
570
....*....|
gi 768017794 1712 ETQANKLRAR 1721
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 ... |
871-1721 |
8.56e-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: 63.84 E-value: 8.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 871 KQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEE 950
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 951 AGGASAGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLA 1030
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1031 ANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRL----QTESGELSRLLEEKECLISQLSRGKALA 1106
Cdd:pfam02463 328 KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELlakkKLESERLSSAAKLKEEELELKSEEEKEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1107 AQSLEELRRQLEEESKAKSALAHAVQALRHDCDLLR-----EQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRT 1181
Cdd:pfam02463 408 QLLLELARQLEDLLKEEKKEELEILEEEEESIELKQgklteEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1182 EELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEM 1261
Cdd:pfam02463 488 LLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLV 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1262 QRELEA---AQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEktKKALEGEKSEI 1338
Cdd:pfam02463 568 RALTELplgARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTEL--TKLKESAKAKE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1339 QAALEEAEGALELEETKTLRIQLELSQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALrLKKKMEG 1418
Cdd:pfam02463 646 SGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKL-EAEELLA 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1419 DLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRR 1498
Cdd:pfam02463 725 DRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELR 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1499 LAEQELLeatERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLE 1578
Cdd:pfam02463 805 ALEEELK---EEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEE 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1579 RMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKN 1658
Cdd:pfam02463 882 QKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEER 961
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768017794 1659 LARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQhELDDAEERADMAETQANKLRAR 1721
Cdd:pfam02463 962 NKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLE-EEKKKLIRAIIEETCQRLKEFL 1023
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1473-1707 |
1.24e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1473 ERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSqntglLNQKKKLEADLAQLSGEVEEAAQERREAeEK 1552
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR-----LAEYSWDEIDVASAEREIAELEAELERL-DA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1553 AKKAITDAAMMAEELKKEQDTsahLERMKKTLEQTVRELQARLEEAEQaalrggkkQVQKLEAKVRELEAELDAEQKKHA 1632
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEE---LEEELDELKGEIGRLEKELEQAEE--------ELDELQDRLEAAEDLARLELRALL 751
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768017794 1633 EALKGVRKHERRVKELAYQAEEDRKNL-ARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEER 1707
Cdd:COG4913 752 EERFAAALGDAVERELRENLEERIDALrARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEED 827
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
716-938 |
2.18e-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: 61.32 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 716 KVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKK 795
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 796 ALQEAHQQALGDLQaeedRVSALTKAKLRLEQQ-VEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQL 874
Cdd:COG4942 101 AQKEELAELLRALY----RLGRQPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768017794 875 EEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAA 938
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1003-1669 |
2.83e-09 |
|
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: 62.29 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1003 EQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASAEKLCRtYEDQLSEAKIKVEELQRQLADASTQRGRLQtES 1082
Cdd:TIGR00618 212 CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK-KQQLLKQLRARIEELRAQEAVLEETQERIN-RA 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1083 GELSRLLEEKECLIS---QLSRGKALAAQSLEELRRQLEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLL 1159
Cdd:TIGR00618 290 RKAAPLAAHIKAVTQieqQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1160 SKANAEVAQWRSKYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEdvtLELERATSAAAA 1239
Cdd:TIGR00618 370 ISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQE---LQQRYAELCAAA 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1240 LDKkqrhLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGK 1319
Cdd:TIGR00618 447 ITC----TAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDN 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1320 S------IQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQLELSQVKaevdRKLAEKDEECANLRRNHQRAVE 1393
Cdd:TIGR00618 523 PgpltrrMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILT----QCDNRSKEDIPNLQNITVRLQD 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1394 SLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLmqAQLKEEQAGRDEEQRLAAELHEQAQALE 1473
Cdd:TIGR00618 599 LTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTAL--HALQLTLTQERVREHALSIRVLPKELLA 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1474 RRASLLAA---ELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEAD---LAQLSGEVEEAAQERR 1547
Cdd:TIGR00618 677 SRQLALQKmqsEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARedaLNQSLKELMHQARTVL 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1548 EAEEKAKKAITDAAMMAEEL-KKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDA 1626
Cdd:TIGR00618 757 KARTEAHFNNNEEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSR 836
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 768017794 1627 EQKKHAeALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKL 1669
Cdd:TIGR00618 837 LEEKSA-TLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1407-1738 |
4.23e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.08 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1407 NEALRLKKKMEGDLNDLELQLGHATRQAT--EAQAATRLMQAQLKEEQAGRDEEQRLAAE---LHEQAQALERRASLLAA 1481
Cdd:PTZ00121 1079 FDFDAKEDNRADEATEEAFGKAEEAKKTEtgKAEEARKAEEAKKKAEDARKAEEARKAEDarkAEEARKAEDAKRVEIAR 1158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1482 ELEELRAAleqgERSRRLAEQELLEATERLnllhsqntglLNQKKKLEADLAQLSGEVEEA--AQERREAEEkAKKAitD 1559
Cdd:PTZ00121 1159 KAEDARKA----EEARKAEDAKKAEAARKA----------EEVRKAEELRKAEDARKAEAArkAEEERKAEE-ARKA--E 1221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1560 AAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAkvRELEAELDAEQKKHAEALKGVR 1639
Cdd:PTZ00121 1222 DAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA--RKADELKKAEEKKKADEAKKAE 1299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1640 KhERRVKELAYQAEEDRKnlarmqdlVDKLQSKVKSYKRQFEEAEqqantnlakyRKAQHELDDAEERADMAETQANKLR 1719
Cdd:PTZ00121 1300 E-KKKADEAKKKAEEAKK--------ADEAKKKAEEAKKKADAAK----------KKAEEAKKAAEAAKAEAEAAADEAE 1360
|
330
....*....|....*....
gi 768017794 1720 ARTRDALGPKLSLSPQHKE 1738
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKK 1379
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
637-1105 |
6.40e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.21 E-value: 6.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 637 LLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEEThvsiTQEKNDLALQLQAEQDNLADAEERchllikskvqlegk 716
Cdd:PRK02224 243 LEEHEERREELETLEAEIEDLRETIAETEREREELAEE----VRDLRERLEELEEERDDLLAEAGL-------------- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 717 vkelsERLEDEeevnaDLAARRRKLEDECTELKKDIDDLELTLakaekekQATENKVKNLTEEMAALDESVARLTKEKKA 796
Cdd:PRK02224 305 -----DDADAE-----AVEARREELEDRDEELRDRLEECRVAA-------QAHNEEAESLREDADDLEERAEELREEAAE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 797 LQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSL---EQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQ 873
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLgnaEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 874 L-------------------------EEKLKKKDSELSQLSL----------RVEDEQLLGAQMQKKIKELQARAEELEE 918
Cdd:PRK02224 448 LleagkcpecgqpvegsphvetieedRERVEELEAELEDLEEeveeveerleRAEDLVEAEDRIERLEERREDLEELIAE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 919 ELEAERAARARVEKQRAEAARELEELSERLEEAGGAsAGQREGCRKREAELGRLRRELEEA--ALRHEATVAALRRKQAE 996
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAEA-EEEAEEAREEVAELNSKLAELKERieSLERIRTLLAAIADAED 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 997 GAAELGEQVDSLQRV----RQKLEKE---KSELRMEVDDlaANVETLTRAKASAEklcrTYEDQLSEakiKVEELQRQLA 1069
Cdd:PRK02224 607 EIERLREKREALAELnderRERLAEKrerKRELEAEFDE--ARIEEAREDKERAE----EYLEQVEE---KLDELREERD 677
|
490 500 510
....*....|....*....|....*....|....*.
gi 768017794 1070 DASTQRGRLQTESGELSRLLEEKECLISQLSRGKAL 1105
Cdd:PRK02224 678 DLQAEIGAVENELEELEELRERREALENRVEALEAL 713
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
645-839 |
7.77e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 7.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 645 EELAALRAELRGLRGALAAAEAKR---QELEETHVSITQEKNDLA-LQLQAEQDNLADAEERCHLLIKSKVQLEGKVKEL 720
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIellEPIRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 721 SERLEDEEEVNADLAARRRKLEDECTELK-KDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQE 799
Cdd:COG4913 308 EAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 768017794 800 AHQQALGDLQAEEDRVS-ALTKAKLRLEQQVEDLEcSLEQE 839
Cdd:COG4913 388 EAAALLEALEEELEALEeALAEAEAALRDLRRELR-ELEAE 427
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
638-1071 |
8.11e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 8.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 638 LRSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQL-QAEQDNLADAEERCHLLIKSKVQLEGK 716
Cdd:COG4913 281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 717 VKELSERLED----EEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTK 792
Cdd:COG4913 361 RARLEALLAAlglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 793 EKKALQEAHQQALG-------------DLQAEEDR-----VSALTKAKLRL---EQQVEDLECSLEQEK-KLRMDTERAK 850
Cdd:COG4913 441 RLLALRDALAEALGldeaelpfvgeliEVRPEEERwrgaiERVLGGFALTLlvpPEHYAAALRWVNRLHlRGRLVYERVR 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 851 RklegdlklTQESVADAAQDKQQLEEKLKKKDSELS-----QLSLR-----VEDEQ------------------------ 896
Cdd:COG4913 521 T--------GLPDPERPRLDPDSLAGKLDFKPHPFRawleaELGRRfdyvcVDSPEelrrhpraitragqvkgngtrhek 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 897 ----------LLGAQMQKKIKELqaraeeleeeleaeraararvEKQRAEAARELEELSERLEEAggasAGQREGCRKRE 966
Cdd:COG4913 593 ddrrrirsryVLGFDNRAKLAAL---------------------EAELAELEEELAEAEERLEAL----EAELDALQERR 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 967 AELGRLrRELEEAALRHEATVAALRRKQAE-GAAELG-EQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASAE 1044
Cdd:COG4913 648 EALQRL-AEYSWDEIDVASAEREIAELEAElERLDASsDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726
|
490 500
....*....|....*....|....*..
gi 768017794 1045 KLCRTYEDQLSEAKIKVEELQRQLADA 1071
Cdd:COG4913 727 EELDELQDRLEAAEDLARLELRALLEE 753
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
641-894 |
8.44e-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: 60.85 E-value: 8.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 641 AQAEEELAALRAELRG-----LRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEG 715
Cdd:TIGR02169 775 HKLEEALNDLEARLSHsripeIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 716 KVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESvarltkekk 795
Cdd:TIGR02169 855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK--------- 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 796 alqeahqqalgdLQAEEDRVSALTKAKLRLEQQVEDlECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLE 875
Cdd:TIGR02169 926 ------------LEALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELK 992
|
250
....*....|....*....
gi 768017794 876 EKLKKKDSELSQLSLRVED 894
Cdd:TIGR02169 993 EKRAKLEEERKAILERIEE 1011
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1420-1604 |
8.46e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 8.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1420 LNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLlaAELEELRAALEQGERSRRL 1499
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREI--AELEAELERLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1500 AEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAammAEELKKEQDTSAHLER 1579
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL---LEERFAAALGDAVERE 766
|
170 180
....*....|....*....|....*
gi 768017794 1580 MKKTLEQTVRELQARLEEAEQAALR 1604
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEELER 791
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1445-1683 |
9.24e-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: 59.39 E-value: 9.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1445 QAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHsqntgllNQ 1524
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE-------KE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1525 KKKLEADLAQLSGEVEEAAqerREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEE--AEQAA 1602
Cdd:COG4942 92 IAELRAELEAQKEELAELL---RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAElaALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1603 LRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKgvrKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEE 1682
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
.
gi 768017794 1683 A 1683
Cdd:COG4942 246 A 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1461-1689 |
1.47e-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: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1461 LAAELHEQAQALERRAslLAAELEELR-------AALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLA 1533
Cdd:COG4942 9 LLLALAAAAQADAAAE--AEAELEQLQqeiaeleKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1534 QLSGEVEEAAQERREAEEKAKKAITDAAMMAE----ELKKEQDTSAHLERMKKTLEQTVRELQARLEEAeQAALRGGKKQ 1609
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL-RADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1610 VQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANT 1689
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
632-1078 |
1.48e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 632 FKMKPLLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEEthvsitqekndlalqlqaeqdnladaeerchlLIKSKV 711
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE--------------------------------LKKKLK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 712 QLEGKVKELSERLEDEEEVNAdLAARRRKLEDECTELkkDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLT 791
Cdd:PRK03918 349 ELEKRLEELEERHELYEEAKA-KKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 792 KEKKALQEAHQQ--ALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESvaDAAQ 869
Cdd:PRK03918 426 KAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLK--ELAE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 870 DKQQLEEKLKKKDSE-----------LSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAA 938
Cdd:PRK03918 504 QLKELEEKLKKYNLEelekkaeeyekLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELG 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 939 RELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEgAAELGEQVDSLQRV-----RQ 1013
Cdd:PRK03918 584 FESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKR-LEELRKELEELEKKyseeeYE 662
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768017794 1014 KLEKEKSELRMEVDDLAANVETLTRAKASAEKLCRTYEDQL---SEAKIKVEELQRQLADASTQRGRL 1078
Cdd:PRK03918 663 ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELeerEKAKKELEKLEKALERVEELREKV 730
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
643-832 |
1.69e-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: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 643 AEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLA--LQLQAEQDNLADAEERCHllikskvqlegkvkEL 720
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIA--------------EL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 721 SERLEDEEEVNADLAARRRKLEdectELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKA---- 796
Cdd:COG4913 674 EAELERLDASSDDLAALEEQLE----ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelra 749
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 768017794 797 -LQEAHQQALGDLQAE------EDRVSALTKAKLRLEQQVEDL 832
Cdd:COG4913 750 lLEERFAAALGDAVERelrenlEERIDALRARLNRAEEELERA 792
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
1-24 |
1.88e-08 |
|
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: 55.81 E-value: 1.88e-08
10 20
....*....|....*....|....
gi 768017794 1 MEAFGNAKTLRNDNSSRFGKFIRI 24
Cdd:cd01363 113 LEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1444-1724 |
2.06e-08 |
|
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: 59.42 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1444 MQAQLKEEQAGRDEEQRLAAELHE----QAQALERRASL---------LAAELEELRAALEQgeRSRRLaEQELLEATER 1510
Cdd:pfam01576 7 MQAKEEELQKVKERQQKAESELKElekkHQQLCEEKNALqeqlqaeteLCAEAEEMRARLAA--RKQEL-EEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1511 LNLLHSQNTGLLNQKKKLEADLAQLSG--EVEEAAQERREAEekakKAITDAAM--MAEELKKEQDTSAHLERMKKTLEQ 1586
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEqlDEEEAARQKLQLE----KVTTEAKIkkLEEDILLLEDQNSKLSKERKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1587 TVRELQARLEEAEQAAlRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLV 1666
Cdd:pfam01576 160 RISEFTSNLAEEEEKA-KSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 768017794 1667 DKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRD 1724
Cdd:pfam01576 239 AKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRD 296
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1265-1721 |
2.92e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1265 LEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEE 1344
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1345 AEGALELEETKTLRIQlELSQVKAEVDRKLAEKDEECANLRRNHQRaVESLQASLDAETRARnealRLKKKMEGDLNDLE 1424
Cdd:PRK03918 240 IEELEKELESLEGSKR-KLEEKIRELEERIEELKKEIEELEEKVKE-LKELKEKAEEYIKLS----EFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1425 LQLGHATRQATEAQAatRLMQAQLKEEQAG-----RDEEQRLAAELHEQAQALERRASLLaAELEELRAAL-----EQGE 1494
Cdd:PRK03918 314 KRLSRLEEEINGIEE--RIKELEEKEERLEelkkkLKELEKRLEELEERHELYEEAKAKK-EELERLKKRLtgltpEKLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1495 RSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSG--------------------------EVEEAAQERRE 1548
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkelleeytaELKRIEKELKE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1549 AEEKAKKAITDAAMMAEELKKEQDtsahLERMKKTLEQtVRELQARL-----EEAEQAA--LRGGKKQVQKLEAKVRELE 1621
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESE----LIKLKELAEQ-LKELEEKLkkynlEELEKKAeeYEKLKEKLIKLKGEIKSLK 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1622 AELDAEQ---KKHAEALKGVRKHERRVKELAYQAEEdrKNLARMQDLVDKLQSKVKSYKRQFE--EAEQQANTNLAKYRK 1696
Cdd:PRK03918 546 KELEKLEelkKKLAELEKKLDELEEELAELLKELEE--LGFESVEELEERLKELEPFYNEYLElkDAEKELEREEKELKK 623
|
490 500
....*....|....*....|....*
gi 768017794 1697 AQHELDDAEERADMAETQANKLRAR 1721
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKE 648
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1159-1589 |
3.32e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1159 LSKANAEVAQWRSKYE--ADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCS--SLEKAKLRLQTESEDVTLELERAT 1234
Cdd:COG4717 73 LKELEEELKEAEEKEEeyAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1235 SAAAALDKKQRHLERALEERRRQEEEMQRELE----AAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDL 1310
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEqlslATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1311 TDQVsLSGKSIQELEKTKK---------ALEGEKSEIQAALEEAEGALELEETKTLRIQLELSQVKAEVDRKLAEKDEEC 1381
Cdd:COG4717 233 ENEL-EAAALEERLKEARLllliaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1382 AnLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLmQAQLKEEQAGRDEEQRL 1461
Cdd:COG4717 312 A-LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI-AALLAEAGVEDEEELRA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1462 AAELHEQAQALERRASLLAAELEELRAALEQGERSRRLA--EQELLEATERLNLLHSQNTGLLNQKKKLEADLAQL--SG 1537
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELAELEAELEQLeeDG 469
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 768017794 1538 EVEEAAQERREAEEKAKKAITD--AAMMAEELKKEQDTSAHLERMKKTLEQTVR 1589
Cdd:COG4717 470 ELAELLQELEELKAELRELAEEwaALKLALELLEEAREEYREERLPPVLERASE 523
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
713-1232 |
3.37e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 713 LEGKVKELSERLEDEEEVNADLAARRRKLED----------ECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAA 782
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEvleeheerreELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 783 LDESVARLTKEkkalqeahqQALGDLQAE--EDRVSALTKAKLRLEQQVEDLECSLEQ-EKKLRMDTERAKRkLEGDLKL 859
Cdd:PRK02224 291 LEEERDDLLAE---------AGLDDADAEavEARREELEDRDEELRDRLEECRVAAQAhNEEAESLREDADD-LEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 860 TQESVADAAQDKQQLEEKLKKKDSELSQLSLRVEDeqllgaqmqkkikelqaraeeleeeleaeraararVEKQRAEAAR 939
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEIEELEEEIEE-----------------------------------LRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 940 ELEELSERLEEAggasAGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEkek 1019
Cdd:PRK02224 406 DLGNAEDFLEEL----REERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVE--- 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1020 sELRMEVDDLAANVETLTRAKASAEKLCRTyEDQLSEAKIKVEELQRQLADastQRGRLQTESGELSRLLEEKECLISQl 1099
Cdd:PRK02224 479 -ELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLEELIAE---RRETIEEKRERAEELRERAAELEAE- 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1100 SRGKALAAQSLEELRRQLEEESKA----KSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLlsKANAEVAQWRSKYEA 1175
Cdd:PRK02224 553 AEEKREAAAEAEEEAEEAREEVAElnskLAELKERIESLERIRTLLAAIADAEDEIERLREKR--EALAELNDERRERLA 630
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768017794 1176 DAIQRTEELEEAKKKLAL-----RLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELER 1232
Cdd:PRK02224 631 EKRERKRELEAEFDEARIeeareDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
712-910 |
4.26e-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: 57.47 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 712 QLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLT 791
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 792 KEKK----ALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADA 867
Cdd:COG4942 104 EELAellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 768017794 868 AQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQ 910
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1179-1683 |
4.31e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1179 QRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLqTESEDVTLELERATSAAAALDK---KQRHLERALEERR 1255
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI-EELEKELESLEGSKRKLEEKIReleERIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1256 RQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEK 1335
Cdd:PRK03918 279 EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1336 SEIQAALEEAEGALELEETKTLRIQLELSQVKAEVDrKLAEKDEECANLRRNhqraVESLQASLDAETRARNEALRLKKK 1415
Cdd:PRK03918 359 ERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE-ELEKAKEEIEEEISK----ITARIGELKKEIKELKKAIEELKK 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1416 MEGD----------------LNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLL 1479
Cdd:PRK03918 434 AKGKcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLK 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1480 AAELEELRAALEQGERSRRLAEQ------ELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGE--------VEEAAQE 1545
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKEKLIKlkgeikSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEleelgfesVEELEER 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1546 RREAEE------KAKKAITDAAMMAEELKKEQDT----SAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEA 1615
Cdd:PRK03918 594 LKELEPfyneylELKDAEKELEREEKELKKLEEEldkaFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSR 673
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768017794 1616 KVRELEAELDAEQKKHAEALKGVRKHERRVKELAyQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEA 1683
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTLEKLKEELEERE-KAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1159-1737 |
4.45e-08 |
|
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: 58.19 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1159 LSKANAEVAQWRSKYEADAIQRTEELEEAKKKLalrlqEAEEgveaanakcssleKAKLRLQTESEDVTLELERATSAAA 1238
Cdd:pfam05483 83 LYKEAEKIKKWKVSIEAELKQKENKLQENRKII-----EAQR-------------KAIQELQFENEKVSLKLEEEIQENK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1239 ALDKKQ---RHLERALEERRRQEEEMQRELEAAQRESRGLGTEL--------------------------FRLRHGHEEA 1289
Cdd:pfam05483 145 DLIKENnatRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLnnniekmilafeelrvqaenarlemhFKLKEDHEKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1290 LEALETLKRENKNLQEEISDLTDQVSLSGKSIQEL------EKTKKALEGEKSEIQAALEEAEGALELEETKTLR----- 1358
Cdd:pfam05483 225 QHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLtflleeSRDKANQLEEKTKLQDENLKELIEKKDHLTKELEdikms 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1359 IQLELSQVKA-EVDRKLAEK-------DEECANLRRNHQRAVESLQAS-LDAETRARNEALRL-KKKMEGDLNDLELQLG 1428
Cdd:pfam05483 305 LQRSMSTQKAlEEDLQIATKticqlteEKEAQMEELNKAKAAHSFVVTeFEATTCSLEELLRTeQQRLEKNEDQLKIITM 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1429 HATRQATEAQAATRL----------MQAQLKEEQAGRDEE---QRLAAELHEQAQALERRASLLAAELEELRAALEQGER 1495
Cdd:pfam05483 385 ELQKKSSELEEMTKFknnkeveleeLKKILAEDEKLLDEKkqfEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKT 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1496 SRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSA 1575
Cdd:pfam05483 465 SEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEM 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1576 HL----ERMKKTLEQTVRELQARLEEAEQAAlRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQ 1651
Cdd:pfam05483 545 NLrdelESVREEFIQKGDEVKCKLDKSEENA-RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1652 AEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRA----RTRDALG 1727
Cdd:pfam05483 624 GSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKeidkRCQHKIA 703
|
650
....*....|
gi 768017794 1728 PKLSLSPQHK 1737
Cdd:pfam05483 704 EMVALMEKHK 713
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1450-1703 |
4.53e-08 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 58.37 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1450 EEQAGRDEEQRLAAELHEQAQALERRAS---LLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKK 1526
Cdd:PLN02939 94 DDDHNRASMQRDEAIAAIDNEQQTNSKDgeqLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKIN 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1527 KLEADLAQLSGEVEEAAQERREAE------EKAKKAIT-----------------------------DAAMMAEELKKEQ 1571
Cdd:PLN02939 174 ILEMRLSETDARIKLAAQEKIHVEileeqlEKLRNELLirgateglcvhslskeldvlkeenmllkdDIQFLKAELIEVA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1572 DTS---AHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEA---LKGVRKHERRV 1645
Cdd:PLN02939 254 ETEervFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAalvLDQNQDLRDKV 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 768017794 1646 KELAYQAEEdrKNLARMQ-DLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDD 1703
Cdd:PLN02939 334 DKLEASLKE--ANVSKFSsYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQD 390
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1476-1717 |
4.91e-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: 57.08 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1476 ASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKK 1555
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1556 AITDAAMMAEELKKEQDTSAHLER-MKKTLEQTVRELQARLEEAEQAALRGG--KKQVQKLEAKVRELEAELDAEQKKHA 1632
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRaLYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1633 EALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAE 1712
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
....*
gi 768017794 1713 TQANK 1717
Cdd:COG4942 248 FAALK 252
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
635-1464 |
5.15e-08 |
|
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: 58.06 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 635 KPLLRSAQAEEELAALRAELRGLRGALAAA-----EAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKS 709
Cdd:pfam02463 200 LKLKEQAKKALEYYQLKEKLELEEEYLLYLdylklNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 710 KVQLEGKVKELSERLEDEEEVNADLAARRRKLEDEctELKKDIDDLELTLAKAEKEKQATENKVKnlteemaALDESVAR 789
Cdd:pfam02463 280 EKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE--KLKESEKEKKKAEKELKKEKEEIEELEK-------ELKELEIK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 790 LTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLEcsleqEKKLRMDTERAKRKLEGDLKLTQESVADAAQ 869
Cdd:pfam02463 351 REAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE-----EELELKSEEEKEAQLLLELARQLEDLLKEEK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 870 DKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLE 949
Cdd:pfam02463 426 KEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKA 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 950 EAGGAsagqREGCRKREAELGRLRRELEEAALRHEATVAalrrkqAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDL 1029
Cdd:pfam02463 506 RSGLK----VLLALIKDGVGGRIISAHGRLGDLGVAVEN------YKVAISTAVIVEVSATADEVEERQKLVRALTELPL 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1030 AAN-VETLTRAKASAEKLCRTYE--DQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLSRGKALA 1106
Cdd:pfam02463 576 GARkLRLLIPKLKLPLKSIAVLEidPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLE 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1107 AQSLEELRRQLEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEEL-E 1185
Cdd:pfam02463 656 EGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKiN 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1186 EAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQREL 1265
Cdd:pfam02463 736 EELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAE 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1266 EAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLtdqvslsgKSIQELEKTKKALEGEKSEIQAALEEA 1345
Cdd:pfam02463 816 LLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLE--------EEITKEELLQELLLKEEELEEQKLKDE 887
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1346 EGALELEETKTLRIQLELSQVKaEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLEL 1425
Cdd:pfam02463 888 LESKEEKEKEEKKELEEESQKL-NLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLL 966
|
810 820 830
....*....|....*....|....*....|....*....
gi 768017794 1426 QLghatRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAE 1464
Cdd:pfam02463 967 LA----KEELGKVNLMAIEEFEEKEERYNKDELEKERLE 1001
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
641-1098 |
5.28e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 641 AQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQekndLALQLQAEQDNLADAEERchlliksKVQLEGKVKEL 720
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE----LEKELESLEGSKRKLEEK-------IRELEERIEEL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 721 SERLEDEEEVNADLaARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEa 800
Cdd:PRK03918 272 KKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 801 hqqALGDLQAEEDRVSALTKAKL---RLEQQVEDLEC-SLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLE- 875
Cdd:PRK03918 350 ---LEKRLEELEERHELYEEAKAkkeELERLKKRLTGlTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKk 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 876 --EKLKKKDSE--LSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEA 951
Cdd:PRK03918 427 aiEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 952 GGASAGQREGCRKREAElGRLRRELEEAALRHEATVAALrRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLA- 1030
Cdd:PRK03918 507 ELEEKLKKYNLEELEKK-AEEYEKLKEKLIKLKGEIKSL-KKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGf 584
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768017794 1031 ANVETLTRAKASAEKLCRTY------EDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQ 1098
Cdd:PRK03918 585 ESVEELEERLKELEPFYNEYlelkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
699-1393 |
5.41e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 699 AEERCHLLIKSKVQlEGKVKELSERLEDEEEVNAdlaARRRKLEDECTELKKDIDDLELTLA-KAEKEKQATENKV---K 774
Cdd:PTZ00121 1148 AEDAKRVEIARKAE-DARKAEEARKAEDAKKAEA---ARKAEEVRKAEELRKAEDARKAEAArKAEEERKAEEARKaedA 1223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 775 NLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQ--QVEDLECSLEQEKKLRMDTERAKRK 852
Cdd:PTZ00121 1224 KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEarKADELKKAEEKKKADEAKKAEEKKK 1303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 853 LEgDLKLTQESVADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEEleaeraararvEK 932
Cdd:PTZ00121 1304 AD-EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA-----------EK 1371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 933 QRAEAARELEELSERLEEAGGASAGQREGCR-KREAElgRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRV 1011
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEdKKKAD--ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA 1449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1012 RQKLEKEKSelrmevddlAANVETLTRAKASAEKLCRTYED--QLSEAKIKVEELQRQlADASTQRGRLQTESGELSRLL 1089
Cdd:PTZ00121 1450 KKKAEEAKK---------AEEAKKKAEEAKKADEAKKKAEEakKADEAKKKAEEAKKK-ADEAKKAAEAKKKADEAKKAE 1519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1090 EEKECLISQLSRGKALAAQSLEELRRQLEEESKAKSALAHAVQalRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQW 1169
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEE--KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1170 RSKYEADAIQRTEEL---EEAKKKlALRLQEAEEgveaANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRH 1246
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAkkaEEAKIK-AEELKKAEE----EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE 1672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1247 LERALEERRRQEEEMQRELEAAQRESRGlGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEK 1326
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEE-AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768017794 1327 TkkalEGEKSEIQAALEEAEGALELEETKTLRIQLElsQVKAEVDRKLAEKDEECANLRRNHQRAVE 1393
Cdd:PTZ00121 1752 D----EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE--ELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1483-1727 |
8.86e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 8.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1483 LEELRAALEQGERSRRlAEQELLEATERLNLLhsqntgllnqkkkleADLAQLSGEVEEAAQERREAEE-----KAKKAI 1557
Cdd:COG4913 224 FEAADALVEHFDDLER-AHEALEDAREQIELL---------------EPIRELAERYAAARERLAELEYlraalRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1558 TDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQkleakvrELEAELDAEQKKHAEALKG 1637
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLE-------QLEREIERLERELEERERR 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1638 VRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELddAEERADMAETQAN- 1716
Cdd:COG4913 361 RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL--EAEIASLERRKSNi 438
|
250
....*....|....*.
gi 768017794 1717 -----KLRARTRDALG 1727
Cdd:COG4913 439 parllALRDALAEALG 454
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
637-1101 |
9.88e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 9.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 637 LLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLAlQLQAEQDNLADAEERCHLliksKVQLEGK 716
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE-KLEKLLQLLPLYQELEAL----EAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 717 VKELsERLEDEEEVNADLAARRRKLEDECTELKKDIDDLEltlakaEKEKQATENKVKNLTEEMAALDESVARLTKEKKA 796
Cdd:COG4717 145 PERL-EELEERLEELRELEEELEELEAELAELQEELEELL------EQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 797 LQEAHQQalgdlqaeedrvsaltkaklrLEQQVEDLECSLEQEKKlrmdtERAKRKLEGDLKLTQESVADAAQDKQQLEE 876
Cdd:COG4717 218 AQEELEE---------------------LEEELEQLENELEAAAL-----EERLKEARLLLLIAAALLALLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 877 KLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGAsa 956
Cdd:COG4717 272 ILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL-- 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 957 gqregcRKREAELGRLRRELEEAALRHEATvAALRRKQAEGAAELGEQVDSLQRvRQKLEKEKSELRMEVDDLAANVETL 1036
Cdd:COG4717 350 ------QELLREAEELEEELQLEELEQEIA-ALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEEL 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768017794 1037 TRAKASAEklcrtYEDQLSEAKIKVEELQRQLADASTQRGRLQTE------SGELSRLLEEKECLISQLSR 1101
Cdd:COG4717 422 LEALDEEE-----LEEELEELEEELEELEEELEELREELAELEAEleqleeDGELAELLQELEELKAELRE 487
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
972-1659 |
1.92e-07 |
|
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: 56.28 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 972 LRRELEEAALRHEAtVAALRRKQAEGAAELGEQvdsLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASAEKLC---- 1047
Cdd:pfam15921 115 LQTKLQEMQMERDA-MADIRRRESQSQEDLRNQ---LQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLqeir 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1048 ------------RTYE-DQLSEAKIK-----VEELQRQL-ADASTQRGRLQTESGELSRLLEEKECLISQL-----SRGK 1103
Cdd:pfam15921 191 silvdfeeasgkKIYEhDSMSTMHFRslgsaISKILRELdTEISYLKGRIFPVEDQLEALKSESQNKIELLlqqhqDRIE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1104 ALAAQSLEELRRQLEEESKAKSAlAHAVQALrhdcdlLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEE 1183
Cdd:pfam15921 271 QLISEHEVEITGLTEKASSARSQ-ANSIQSQ------LEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDK 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1184 LEEAKKKLALRLQEAEEG--------VEAANAKcSSLEKAKLRLQTESEDVTLELE-------RATSAAAALDkkqrHLE 1248
Cdd:pfam15921 344 IEELEKQLVLANSELTEArterdqfsQESGNLD-DQLQKLLADLHKREKELSLEKEqnkrlwdRDTGNSITID----HLR 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1249 RALEERRRQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTK 1328
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTV 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1329 KALEGEKSEIQAALEEAEGALELEETKT-LRIQlELSQVKAEVDR-------------KLAEKDEECANLRRNhqraVES 1394
Cdd:pfam15921 499 SDLTASLQEKERAIEATNAEITKLRSRVdLKLQ-ELQHLKNEGDHlrnvqtecealklQMAEKDKVIEILRQQ----IEN 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1395 LQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGR-------DEEQRLAAELHE 1467
Cdd:pfam15921 574 MTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKvklvnagSERLRAVKDIKQ 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1468 QAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERR 1547
Cdd:pfam15921 654 ERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQ 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1548 EaEEKAKKAITDAAMMAEELKKEQDTSAHLER--MKKTLEQTVRELQARLEEAEQAA--LRGGKKQVQKLEAKVRELEAE 1623
Cdd:pfam15921 734 K-QITAKRGQIDALQSKIQFLEEAMTNANKEKhfLKEEKNKLSQELSTVATEKNKMAgeLEVLRSQERRLKEKVANMEVA 812
|
730 740 750
....*....|....*....|....*....|....*.
gi 768017794 1624 LDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNL 1659
Cdd:pfam15921 813 LDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKEL 848
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1461-1698 |
2.48e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1461 LAAELHEQAQALERRASLLAAELEELRAALEQgersrrlAEQELLEATERLNLLHSQNtgllnQKKKLEADLAQLSGEVE 1540
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEE-------AEAALEEFRQKNGLVDLSE-----EAKLLLQQLSELESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1541 EAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAhlermKKTLEQTVRELQARLEEAEQaalRGGKK--QVQKLEAKVR 1618
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPDALPELLQSPV-----IQQLRAQLAELEAELAELSA---RYTPNhpDVIALRAQIA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1619 ELEAELDAEQKKHAEALKG-VRKHERRVKELAYQAEEDRKNLARMQdlvdKLQSKVKSYKRQFEEAEQQANTNLAKYRKA 1697
Cdd:COG3206 302 ALRAQLQQEAQRILASLEAeLEALQAREASLQAQLAQLEARLAELP----ELEAELRRLEREVEVARELYESLLQRLEEA 377
|
.
gi 768017794 1698 Q 1698
Cdd:COG3206 378 R 378
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1479-1719 |
4.48e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 53.76 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1479 LAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAIT 1558
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1559 DAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQAR---LEE--------AEQAALRGGKKQVQKLEAKVRELEAELDAE 1627
Cdd:COG1340 93 ELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEvlsPEEekelvekiKELEKELEKAKKALEKNEKLKELRAELKEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1628 QKKhaealkgVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEER 1707
Cdd:COG1340 173 RKE-------AEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKE 245
|
250
....*....|..
gi 768017794 1708 ADMAETQANKLR 1719
Cdd:COG1340 246 LKKLRKKQRALK 257
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
641-1227 |
5.66e-07 |
|
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: 54.80 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 641 AQAEEELAALRAELRGLRGALAAAEAKRQELeethvsiTQEKNDLALQLQAEQDNLADaEERCHLLIKSKV-QLEGKVKE 719
Cdd:pfam01576 429 AELAEKLSKLQSELESVSSLLNEAEGKNIKL-------SKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLrQLEDERNS 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 720 LSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQE 799
Cdd:pfam01576 501 LQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQ 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 800 AHQQALGDLQAEEDRVSALTKAKLRLEQQVED----------------------------LECSLEQEKKLRMDTERAKR 851
Cdd:pfam01576 581 ELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEekaisaryaeerdraeaeareketralsLARALEEALEAKEELERTNK 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 852 KLEGDLKLTQESVADAAQDKQQLEEKLKKKDSELSQLSLRVED-EQLLGAQMQKKI--------------KELQARAEEL 916
Cdd:pfam01576 661 QLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEElEDELQATEDAKLrlevnmqalkaqfeRDLQARDEQG 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 917 EEELEAERAARARVE-------KQRAEAARELEELSERLEEAGG----ASAGQREGC---RKREAELGRLRRELEEAALR 982
Cdd:pfam01576 741 EEKRRQLVKQVRELEaelederKQRAQAVAAKKKLELDLKELEAqidaANKGREEAVkqlKKLQAQMKDLQRELEEARAS 820
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 983 HEATVAALR---RKQAEGAAE---LGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASAEKLCRTYEDQLSE 1056
Cdd:pfam01576 821 RDEILAQSKeseKKLKNLEAEllqLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEE 900
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1057 AKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLSRgkalaaQSLEELRRQLEEESKAKSALAHAVQALRH 1136
Cdd:pfam01576 901 EQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLER------QNKELKAKLQEMEGTVKSKFKSSIAALEA 974
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1137 DCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEAD---AIQRTEELEEAK---KKLALRLQEAEEGVEAANAkcs 1210
Cdd:pfam01576 975 KIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDErrhADQYKDQAEKGNsrmKQLKRQLEEAEEEASRANA--- 1051
|
650
....*....|....*..
gi 768017794 1211 slekAKLRLQTESEDVT 1227
Cdd:pfam01576 1052 ----ARRKLQRELDDAT 1064
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
683-909 |
6.23e-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: 54.26 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 683 NDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKA 762
Cdd:TIGR04523 310 KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 763 EKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKL 842
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQ 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768017794 843 RMDTERAKRKLEGDLKLTQESVADAAQD-------KQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKEL 909
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKELKSKEKElkklneeKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1265-1708 |
1.03e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1265 LEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEE 1344
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1345 aegaleleetktlriqLELSQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLE 1424
Cdd:COG4717 128 ----------------LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1425 LQLGHATRQATEAQAATRLMQAQLK---------EEQAGRDEEQRLAAELHEQAQALERRASLLAA-------------- 1481
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEeaqeeleelEEELEQLENELEAAALEERLKEARLLLLIAAAllallglggsllsl 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1482 ---------------------------ELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQ 1534
Cdd:COG4717 272 iltiagvlflvlgllallflllarekaSLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1535 LSGEVEEAAQERR-EAEEKAKKAITDAAMMA--EELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQvq 1611
Cdd:COG4717 352 LLREAEELEEELQlEELEQEIAALLAEAGVEdeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE-- 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1612 kLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELayqaEEDrknlarmqDLVDKLQSKVKSYKRQFEEAEQQAntnl 1691
Cdd:COG4717 430 -LEEELEELEEELEELEEELEELREELAELEAELEQL----EED--------GELAELLQELEELKAELRELAEEW---- 492
|
490
....*....|....*..
gi 768017794 1692 AKYRKAQHELDDAEERA 1708
Cdd:COG4717 493 AALKLALELLEEAREEY 509
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
633-817 |
1.14e-06 |
|
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: 51.46 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 633 KMKPLLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERchllikskvq 712
Cdd:COG1579 5 DLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 713 lEGKVKELSERLEDEEEVNAdlaarrrkledecteLKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTK 792
Cdd:COG1579 75 -IKKYEEQLGNVRNNKEYEA---------------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138
|
170 180
....*....|....*....|....*
gi 768017794 793 EKKALQEAHQQALGDLQAEEDRVSA 817
Cdd:COG1579 139 ELEEKKAELDEELAELEAELEELEA 163
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1176-1624 |
1.28e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1176 DAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERR 1255
Cdd:PRK02224 283 DLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELR 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1256 RQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEK 1335
Cdd:PRK02224 363 EEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1336 SEIQAALEEAEGALELEETKTLRIQLELS---QVKAEVDRKLAEKDEECANLRRNHQRAVESlqasldAETRARNEALRL 1412
Cdd:PRK02224 443 EEAEALLEAGKCPECGQPVEGSPHVETIEedrERVEELEAELEDLEEEVEEVEERLERAEDL------VEAEDRIERLEE 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1413 KKKMEGDLndleLQLGHATRQATEAQAATRLMQAQLKEEQAgrDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQ 1492
Cdd:PRK02224 517 RREDLEEL----IAERRETIEEKRERAEELRERAAELEAEA--EEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1493 GERSRRL------AEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAA-QERREAEEKAKKAITDAAMMAE 1565
Cdd:PRK02224 591 LERIRTLlaaiadAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLD 670
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768017794 1566 ELKKEQDTSAHLERMKKTLEQTVRELQARLE--EAEQAALRGGKKQVQKLEAKVRELEAEL 1624
Cdd:PRK02224 671 ELREERDDLQAEIGAVENELEELEELRERREalENRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
641-1045 |
1.31e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 641 AQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKN--DLALQLQAEQDNLADAEERCHllikskvQLEGKVK 718
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLE-------ELEERLE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 719 ELSERLEDEEEVNADLAARRRKLEDECTEL----KKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEK 794
Cdd:COG4717 157 ELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 795 KALQEAHQQ-----------ALGDLQAEEDRVSA----------------------LTKAKLRLEQQVEDLECSLEQEKK 841
Cdd:COG4717 237 EAAALEERLkearlllliaaALLALLGLGGSLLSliltiagvlflvlgllallfllLAREKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 842 LRMDTERAKRKLEGDLKLTQESVADA---AQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELqaraeelee 918
Cdd:COG4717 317 EEEELEELLAALGLPPDLSPEELLELldrIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEEL--------- 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 919 eLEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEaalrheaTVAALRRKQAEGA 998
Cdd:COG4717 388 -RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEE-------ELEELREELAELE 459
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 768017794 999 AELG--EQVDSLQRVRQKLEKEKSELRMEVDDLAAN---VETLTRAKASAEK 1045
Cdd:COG4717 460 AELEqlEEDGELAELLQELEELKAELRELAEEWAALklaLELLEEAREEYRE 511
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
732-961 |
1.36e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 732 ADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAE 811
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 812 EDRVS---ALTKAK---------LRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLEEKLK 879
Cdd:COG3883 99 GGSVSyldVLLGSEsfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 880 KKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQR 959
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAA 258
|
..
gi 768017794 960 EG 961
Cdd:COG3883 259 AG 260
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
645-1039 |
1.77e-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: 53.03 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 645 EELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLAdaeerchlLIKSKVQLEGK-------V 717
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLN--------LVQTALRQQEKieryqedL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 718 KELSERLEDEEEVNADLAARRrkledectelkkdiddleltlAKAEKEKQATENKVKNLTEEMA----ALDESVARLTKE 793
Cdd:COG3096 357 EELTERLEEQEEVVEEAAEQL---------------------AEAEARLEAAEEEVDSLKSQLAdyqqALDVQQTRAIQY 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 794 KKALQ---EAHQQ-ALGDLQAE--EDRVSALtkaKLRLEQQVEDLecsLEQEKKLRmDTERAKRKLEGDLKLTQESV--- 864
Cdd:COG3096 416 QQAVQaleKARALcGLPDLTPEnaEDYLAAF---RAKEQQATEEV---LELEQKLS-VADAARRQFEKAYELVCKIAgev 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 865 --ADAAQDKQQL-------------EEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARAR 929
Cdd:COG3096 489 erSQAWQTARELlrryrsqqalaqrLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 930 VEKQRAEAAReleelserleeaggasagQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQ 1009
Cdd:COG3096 569 LEEQAAEAVE------------------QRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTA 630
|
410 420 430
....*....|....*....|....*....|
gi 768017794 1010 RVRQKLEKEKsELRMEVDDLAANVETLTRA 1039
Cdd:COG3096 631 AMQQLLERER-EATVERDELAARKQALESQ 659
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1367-1695 |
1.83e-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: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1367 KAEVDRKLAEKDEECANL--RRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDL-------ELQLGHATRQATEA 1437
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVerRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIrqeerkrELERIRQEEIAMEI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1438 QAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASL--LAAELEELRAALEQG-ERSRRLAEQELLEATERLNLL 1514
Cdd:pfam17380 375 SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIqqQKVEMEQIRAEQEEArQREVRRLEEERAREMERVRLE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1515 HSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKaitdaaMMAEELKKEQDTSAHLERMKKTLEQTVRELQAR 1594
Cdd:pfam17380 455 EQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRK------ILEKELEERKQAMIEEERKRKLLEKEMEERQKA 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1595 LEEAEQAalrggkkqvqkleakvRELEAELDAEQKKhaealkgvrKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVK 1674
Cdd:pfam17380 529 IYEEERR----------------REAEEERRKQQEM---------EERRRIQEQMRKATEERSRLEAMEREREMMRQIVE 583
|
330 340
....*....|....*....|..
gi 768017794 1675 SYKRQFE-EAEQQANTNLAKYR 1695
Cdd:pfam17380 584 SEKARAEyEATTPITTIKPIYR 605
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
446-473 |
1.89e-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: 1.89e-06
10 20
....*....|....*....|....*...
gi 768017794 446 SQLHKENLNKLMTNLRATQPHFVRCIVP 473
Cdd:cd01363 143 FEIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1455-1640 |
2.07e-06 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 52.38 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1455 RDEEQRLAaELHEQAQALERRASLLAAELEEL-RAALEQGE------RSRRLAE-QELLEATER-LNLLHSQNTGLLNQ- 1524
Cdd:COG0497 168 RALKKELE-ELRADEAERARELDLLRFQLEELeAAALQPGEeeeleeERRRLSNaEKLREALQEaLEALSGGEGGALDLl 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1525 ---KKKLEaDLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELkkEQDTS---------AHLERMKKTLEQTVRELQ 1592
Cdd:COG0497 247 gqaLRALE-RLAEYDPSLAELAERLESALIELEEAASELRRYLDSL--EFDPErleeveerlALLRRLARKYGVTVEELL 323
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 768017794 1593 ARLEEAEQ--AALRGGKKQVQKLEAKVRELEAELDAEqkkhAEALKGVRK 1640
Cdd:COG0497 324 AYAEELRAelAELENSDERLEELEAELAEAEAELLEA----AEKLSAARK 369
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1456-1627 |
2.37e-06 |
|
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: 50.69 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1456 DEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNllhsQNTGLLNQKKKLEaDLAQL 1535
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK----KYEEQLGNVRNNK-EYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1536 SGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQdtsAHLERMKKTLEQTVRELQARLEEAEqaalrggkKQVQKLEA 1615
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELE---AELAELEAELEEKKAELDEELAELE--------AELEELEA 163
|
170
....*....|..
gi 768017794 1616 KVRELEAELDAE 1627
Cdd:COG1579 164 EREELAAKIPPE 175
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1577-1698 |
2.39e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 51.51 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1577 LERMKK-TLEQTVRELQARLEEAE------QAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALkgvrkheRRVKELA 1649
Cdd:PRK09039 71 LERQGNqDLQDSVANLRASLSAAEaersrlQALLAELAGAGAAAEGRAGELAQELDSEKQVSARAL-------AQVELLN 143
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 768017794 1650 YQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAkyRKAQ 1698
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALA--QRVQ 190
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
717-1332 |
3.59e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 717 VKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNL---TEEMAALDESVARLTKE 793
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELeelKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 794 KKALQEahqqalgDLQAEEDRVSALTKAKLRLEQQVEDLEcSLEQE-------KKLRMDTERAKRKLEGDL-------KL 859
Cdd:PRK03918 254 KRKLEE-------KIRELEERIEELKKEIEELEEKVKELK-ELKEKaeeyiklSEFYEEYLDELREIEKRLsrleeeiNG 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 860 TQESVADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAAR 939
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 940 ELEELSerleeaggasaGQREGCRKREAELGRLRRELEEA-----ALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQK 1014
Cdd:PRK03918 406 EISKIT-----------ARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEK 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1015 LEKEKSELRmEVDDLAANVETLTRAKASAEKLcRTYEDQLSeaKIKVEELQRQLADASTQRGRLQTESGELSRLLEEkec 1094
Cdd:PRK03918 475 ERKLRKELR-ELEKVLKKESELIKLKELAEQL-KELEEKLK--KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE--- 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1095 lisqLSRGKALaaqsleelrrqleeeSKAKSALAHAVQALRhdcdllreqheeeaeaqaelqRLLSKANAEVAQWRSKYE 1174
Cdd:PRK03918 548 ----LEKLEEL---------------KKKLAELEKKLDELE---------------------EELAELLKELEELGFESV 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1175 ADAIQRTEELEEAKKKLaLRLQEAEEGVEaanakcsSLEKAKLRLQTESEDVTLELERATSAAAALDKKqrhleraleER 1254
Cdd:PRK03918 588 EELEERLKELEPFYNEY-LELKDAEKELE-------REEKELKKLEEELDKAFEELAETEKRLEELRKE---------LE 650
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768017794 1255 RRQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTdqvslsgKSIQELEKTKKALE 1332
Cdd:PRK03918 651 ELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE-------KAKKELEKLEKALE 721
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1461-1658 |
4.77e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1461 LAAELHEQAQALE----RRASLLAAELEELRAALEQGERSrrlaEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLs 1536
Cdd:COG4717 47 LLERLEKEADELFkpqgRKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEKL- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1537 gEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAK 1616
Cdd:COG4717 122 -EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 768017794 1617 VRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKN 1658
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
1538-1649 |
5.08e-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: 50.76 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1538 EVEEAAQERREAEEKAKKAITDAAMMAEELkkeqdtsahlERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEaKV 1617
Cdd:pfam07767 206 EAEKKRLKEEEKLERVLEKIAESAATAEAR----------EEKRKTKAQRNKEKRRKEEEREAKEEKALKKKLAQLE-RL 274
|
90 100 110
....*....|....*....|....*....|..
gi 768017794 1618 RELEAELDAEQKKHAEALKGVRKHERRVKELA 1649
Cdd:pfam07767 275 KEIAKEIAEKEKEREEKAEARKREKRKKKKEE 306
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1381-1687 |
5.11e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 51.72 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1381 CANLRRNHQRAvESLQASLDAETRARNEALRLKKKMEgdlndLELQLGHATRQATEAQAATRLMQAQLKEEQAG------ 1454
Cdd:PRK10246 585 CASLNITLQPQ-DDIQPWLDAQEEHERQLRLLSQRHE-----LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGyaltlp 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1455 -----------RDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLN 1523
Cdd:PRK10246 659 qedeeaswlatRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQ 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1524 QKKKLEADLAQlsgeveeaAQERREAEEKAKKAITDAAMMAEELKKEqdTSAHLERMKKTLEQTVRELQARLEEAEQAal 1603
Cdd:PRK10246 739 QDVLEAQRLQK--------AQAQFDTALQASVFDDQQAFLAALLDEE--TLTQLEQLKQNLENQRQQAQTLVTQTAQA-- 806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1604 rggkkQVQKLEAKVRELEAELDAEQKKHAEAL--KGVRKHERRVKELAYQAEEDRKNLARMQDLVdklqskvksykRQFE 1681
Cdd:PRK10246 807 -----LAQHQQHRPDGLDLTVTVEQIQQELAQlaQQLRENTTRQGEIRQQLKQDADNRQQQQALM-----------QQIA 870
|
....*.
gi 768017794 1682 EAEQQA 1687
Cdd:PRK10246 871 QATQQV 876
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
861-1087 |
8.08e-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: 50.15 E-value: 8.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 861 QESVADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAarE 940
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL--R 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 941 LEELSERLEEAGGASAGQREGCRKREAELgrLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKS 1020
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALL--LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768017794 1021 ELRMEVDDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSR 1087
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
767-1023 |
8.67e-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: 50.15 E-value: 8.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 767 QATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLEcslEQEKKLRMDT 846
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE---AELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 847 ERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQAraeeleeeleaeraA 926
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRA--------------D 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 927 RARVEKQRAEAAReleelserleeaggasagQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGA---AELGE 1003
Cdd:COG4942 159 LAELAALRAELEA------------------ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAaelAELQQ 220
|
250 260
....*....|....*....|
gi 768017794 1004 QVDSLQRVRQKLEKEKSELR 1023
Cdd:COG4942 221 EAEELEALIARLEAEAAAAA 240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1523-1724 |
9.05e-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: 50.15 E-value: 9.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1523 NQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQ-- 1600
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAel 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1601 AALRGG-KKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQ 1679
Cdd:COG4942 100 EAQKEElAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 768017794 1680 FEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRD 1724
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1539-1678 |
9.29e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 50.63 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1539 VEEAAQERREAE--EKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQaalrggkkQVQKLEAK 1616
Cdd:COG2433 378 IEEALEELIEKElpEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDE--------RIERLERE 449
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768017794 1617 VRELEAELDAEQKKHAEalkgVRKHERRVKELayqaeedRKNLARMQDLVDKLQSKVKSYKR 1678
Cdd:COG2433 450 LSEARSEERREIRKDRE----ISRLDREIERL-------ERELEEERERIEELKRKLERLKE 500
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
994-1238 |
9.29e-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: 50.15 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 994 QAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADAST 1073
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1074 QRGRLQTESGELSRLLEekecLISQLSRGKALAAQSLEELRRQLEEESKAKS-ALAHAVQALRHDCDLLREQHEEEAEAQ 1152
Cdd:COG4942 98 ELEAQKEELAELLRALY----RLGRQPPLALLLSPEDFLDAVRRLQYLKYLApARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1153 AELQRLLskanAEVAQWRSKYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANakcsSLEKAKLRLQTESEDVTLELER 1232
Cdd:COG4942 174 AELEALL----AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE----ELEALIARLEAEAAAAAERTPA 245
|
....*.
gi 768017794 1233 ATSAAA 1238
Cdd:COG4942 246 AGFAAL 251
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1289-1503 |
1.28e-05 |
|
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: 49.38 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1289 ALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQLELSQVKA 1368
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1369 EVDRKLAEKDEECANLRRNHQRAVESL----QASLDAETRAR-----NEALR-LKKKMEGDLNDLELQLGHATRQATEAQ 1438
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQylkylAPARReQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768017794 1439 AATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQE 1503
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1358-1566 |
1.39e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1358 RIQLELSQVKAEVDRkLAEKDEECANLRRNHQRA--VESLQASLDAETRARNEAL--RLKKKMEGDLNDLELQLGHATRQ 1433
Cdd:COG4913 239 RAHEALEDAREQIEL-LEPIRELAERYAAARERLaeLEYLRAALRLWFAQRRLELleAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1434 ATEAQAATRLMQAQLkeEQAGRDEEQRLAAELH---EQAQALERRASLLAAELEELRAALEQGERS----RRLAEQELLE 1506
Cdd:COG4913 318 LDALREELDELEAQI--RGNGGDRLEQLEREIErleRELEERERRRARLEALLAALGLPLPASAEEfaalRAEAAALLEA 395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768017794 1507 ATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERR---EAEEKAKKAITDAAMMAEE 1566
Cdd:COG4913 396 LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSnipARLLALRDALAEALGLDEA 458
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1012-1702 |
1.63e-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: 49.97 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1012 RQKLEKEKSELRMEVDDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLaDASTQRGRLQTESGELSRLLEE 1091
Cdd:TIGR00618 193 HGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR-EAQEEQLKKQQLLKQLRARIEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1092 KECLISQLSrgkalaaqsleeLRRQLEEESKAKSALAHAVQALRHdcdlLREQHEEEAEAQAELQRLLSKANAEvAQWRS 1171
Cdd:TIGR00618 272 LRAQEAVLE------------ETQERINRARKAAPLAAHIKAVTQ----IEQQAQRIHTELQSKMRSRAKLLMK-RAAHV 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1172 KYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKlRLQTESEDVTLELERATSAAAALDKKQRhLERAL 1251
Cdd:TIGR00618 335 KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKLQSLCKELDILQR-EQATI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1252 EERRRQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSlSGKSIQELEKTKKAL 1331
Cdd:TIGR00618 413 DTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ-TKEQIHLQETRKKAV 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1332 EGEKSEIQAALEEAEGALELEETKTLRIQLELsqvkaEVDRKLAEKDEecaNLRRNHQRAVESLQASLDAEtraRNEALR 1411
Cdd:TIGR00618 492 VLARLLELQEEPCPLCGSCIHPNPARQDIDNP-----GPLTRRMQRGE---QTYAQLETSEEDVYHQLTSE---RKQRAS 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1412 LKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERrasllaaELEELRAALE 1491
Cdd:TIGR00618 561 LKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQP-------EQDLQDVRLH 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1492 QGERSRRLAEQELLEATERLNLLhsqntgllnqKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQ 1571
Cdd:TIGR00618 634 LQQCSQELALKLTALHALQLTLT----------QERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQ 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1572 DTSAHLERMKKTLEQTVRELQARLEEAE---QAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKEL 1648
Cdd:TIGR00618 704 TLLRELETHIEEYDREFNEIENASSSLGsdlAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHL 783
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768017794 1649 AYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEA-----------EQQANTNLAKYRKAQHELD 1702
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIlnlqcetlvqeEEQFLSRLEEKSATLGEIT 848
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1281-1601 |
1.72e-05 |
|
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: 49.74 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1281 RLRHGHEEALEALE---TLKRENKNLQEEISD----LTDQVSLSGKSIQELEKTKkaLEGEKSEIQAALEEAEGALELEE 1353
Cdd:pfam17380 300 RLRQEKEEKAREVErrrKLEEAEKARQAEMDRqaaiYAEQERMAMERERELERIR--QEERKRELERIRQEEIAMEISRM 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1354 TKTLRIQLELSQ----VKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQlgh 1429
Cdd:pfam17380 378 RELERLQMERQQknerVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE--- 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1430 atrQATEAQAATRLMQaqlkEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELleaTE 1509
Cdd:pfam17380 455 ---EQERQQQVERLRQ----QEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEM---EE 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1510 RLNLLHSQntgllnqkkkleadlaqlsgeveeaaQERREAEEKAKKA--ITDAAMMAEELKKEQDTSAHLERMKKTleqt 1587
Cdd:pfam17380 525 RQKAIYEE--------------------------ERRREAEEERRKQqeMEERRRIQEQMRKATEERSRLEAMERE---- 574
|
330
....*....|....
gi 768017794 1588 vRELQARLEEAEQA 1601
Cdd:pfam17380 575 -REMMRQIVESEKA 587
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1547-1688 |
1.89e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1547 REAEEKAKKAITDAAMMAEELKKEQDTSA--HLERMKKTLEQTVRE-------LQARLEEAEQA---ALRGGKKQVQKLE 1614
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAkeEIHKLRNEFEKELRErrnelqkLEKRLLQKEENldrKLELLEKREEELE 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768017794 1615 AKVRELEAELDAEQKKHAEALKGVRKHERRVKELA-YQAEEDRKNLarMQDLVDKLQSKVKSYKRQFE-EAEQQAN 1688
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEELIEEQLQELERISgLTAEEAKEIL--LEKVEEEARHEAAVLIKEIEeEAKEEAD 187
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1470-1721 |
1.98e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1470 QALERRASLLAAE---------LEELRAALEQGERSRRLAEQELLEATERLNLLhsqNTGLLNQKK---------KLEAD 1531
Cdd:PRK04863 287 EALELRRELYTSRrqlaaeqyrLVEMARELAELNEAESDLEQDYQAASDHLNLV---QTALRQQEKieryqadleELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1532 LAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRelqaRLEEAEQA------ALRG 1605
Cdd:PRK04863 364 LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQ----ALERAKQLcglpdlTADN 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1606 GKKQVQKLEAKVREL-EAELDAEQK---------KHAEALKGVRK---------HERRVKELAYQAEEDRKNLARMQDLV 1666
Cdd:PRK04863 440 AEDWLEEFQAKEQEAtEELLSLEQKlsvaqaahsQFEQAYQLVRKiagevsrseAWDVARELLRRLREQRHLAEQLQQLR 519
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768017794 1667 DKLQ------SKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRAR 1721
Cdd:PRK04863 520 MRLSeleqrlRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARER 580
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
973-1704 |
2.16e-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: 49.57 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 973 RRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQrvrqKLEKEKSELRMEVDDLAANVETLTRAKASAEKLCRtYED 1052
Cdd:COG3096 280 RRELSERALELRRELFGARRQLAEEQYRLVEMARELE----ELSARESDLEQDYQAASDHLNLVQTALRQQEKIER-YQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1053 QLSEAKIKVEELQRQLADASTQRGRLQTEsgeLSRLLEEKECLISQLS-RGKALAAQSLEelrrqleeeskaksALAH-- 1129
Cdd:COG3096 355 DLEELTERLEEQEEVVEEAAEQLAEAEAR---LEAAEEEVDSLKSQLAdYQQALDVQQTR--------------AIQYqq 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1130 AVQALRHDCDLLREQHeeeaeaqaelqrlLSKANAEvaQWRSKYEADAIQRTEELEEAKKKLAL------RLQEAEEGVE 1203
Cdd:COG3096 418 AVQALEKARALCGLPD-------------LTPENAE--DYLAAFRAKEQQATEEVLELEQKLSVadaarrQFEKAYELVC 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1204 AANAKCS---SLEKAKLRLQTESEDVTLeLERATSAAAALDKKQRhleraleerrrqeeemqreLEAAQRESRGLGTELF 1280
Cdd:COG3096 483 KIAGEVErsqAWQTARELLRRYRSQQAL-AQRLQQLRAQLAELEQ-------------------RLRQQQNAERLLEEFC 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1281 RLRHGHEEALEALETLKREnknLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAA----------------LEE 1344
Cdd:COG3096 543 QRIGQQLDAAEELEELLAE---LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlaaqdalerlreQSG 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1345 AEGALELEETKTLRIQLE-LSQVKAEVDRKLAEKDEECANLRRNHQ----------RAVESLQASLDAETR--------- 1404
Cdd:COG3096 620 EALADSQEVTAAMQQLLErEREATVERDELAARKQALESQIERLSQpggaedprllALAERLGGVLLSEIYddvtledap 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1405 --------ARNE--------ALRLKKKMEGDLNDLELQLGHAT------RQATEAQAA--TRLMQAQL------KEEQAG 1454
Cdd:COG3096 700 yfsalygpARHAivvpdlsaVKEQLAGLEDCPEDLYLIEGDPDsfddsvFDAEELEDAvvVKLSDRQWrysrfpEVPLFG 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1455 RDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGER--SRRLA-------EQELLEATERLNllhsqntgllnqk 1525
Cdd:COG3096 780 RAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvGGHLAvafapdpEAELAALRQRRS------------- 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1526 kKLEADLAQLSGEVEEAAQERREAEEKA---KKAITDAAMMAEElkkeqdtsahlermkkTLEQTVRELQARLEEAEQAA 1602
Cdd:COG3096 847 -ELERELAQHRAQEQQLRQQLDQLKEQLqllNKLLPQANLLADE----------------TLADRLEELREELDAAQEAQ 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1603 -------------------LRGGKKQVQKLEAKVRELEAELDaEQKKHAEALKGVRKherRVKELAYQAEEDRknLARMQ 1663
Cdd:COG3096 910 afiqqhgkalaqleplvavLQSDPEQFEQLQADYLQAKEQQR-RLKQQIFALSEVVQ---RRPHFSYEDAVGL--LGENS 983
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 768017794 1664 DLVDKLqskvksyKRQFEEAEQQANTNLAKYRKAQHELDDA 1704
Cdd:COG3096 984 DLNEKL-------RARLEQAEEARREAREQLRQAQAQYSQY 1017
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1455-1721 |
2.31e-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: 49.57 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1455 RDEEQRLAAELhEQAQALERRASLLAAE-LEELRAALEQGERSRRLAEQELLEATERLNLLHsqnTGLLNQKK------- 1526
Cdd:COG3096 280 RRELSERALEL-RRELFGARRQLAEEQYrLVEMARELEELSARESDLEQDYQAASDHLNLVQ---TALRQQEKieryqed 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1527 --KLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELK------KEQDTSA--------HLERMKKTLEQTvrE 1590
Cdd:COG3096 356 leELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqqalDVQQTRAiqyqqavqALEKARALCGLP--D 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1591 LQARLEEAEQAALRGgkkQVQKLEAKVRELEAEL---DAEQKKHAEALKGVRKH----ER-----RVKELAYQAEEDRKN 1658
Cdd:COG3096 434 LTPENAEDYLAAFRA---KEQQATEEVLELEQKLsvaDAARRQFEKAYELVCKIagevERsqawqTARELLRRYRSQQAL 510
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768017794 1659 LARMQDLVDKLQ------SKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRAR 1721
Cdd:COG3096 511 AQRLQQLRAQLAeleqrlRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ 579
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
644-870 |
2.55e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 644 EEELAALRAELRglrgalaAAEAKRQELEETH--VSITQEKNDLALQLQAEQDNLADAEERchlliksKVQLEGKVKELS 721
Cdd:COG3206 181 EEQLPELRKELE-------EAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAE-------LAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 722 ERLEDEEEVNADLAArrrklEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAh 801
Cdd:COG3206 247 AQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEA- 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 802 qqalgDLQAEEDRVSALTKAKLRLEQQVEDLEcSLEQE-KKLRMDTERAKRKLEGDLKLTQESVADAAQD 870
Cdd:COG3206 321 -----ELEALQAREASLQAQLAQLEARLAELP-ELEAElRRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
686-1310 |
2.79e-05 |
|
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: 49.07 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 686 ALQLQAEQDNLADAEERCHLLIKSKVQLEgkvKELSERLEDEEEVNADLAARRRKLEDECTELKkdiddleltlAKAEKE 765
Cdd:pfam12128 243 FTKLQQEFNTLESAELRLSHLHFGYKSDE---TLIASRQEERQETSAELNQLLRTLDDQWKEKR----------DELNGE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 766 KQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQAL----GDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKK 841
Cdd:pfam12128 310 LSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLpswqSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNN 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 842 L---RMDTERAKRKLEGDLKLTQESvadaaQDKQQLEEKLKkkdSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEE 918
Cdd:pfam12128 390 RdiaGIKDKLAKIREARDRQLAVAE-----DDLQALESELR---EQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 919 ELEAERAARARVEKQRAE---AARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAALRHEA---TVAALRR 992
Cdd:pfam12128 462 LLLQLENFDERIERAREEqeaANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPqagTLLHFLR 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 993 KQAEGAAE-LGEQVDSLQRVRQKLEKEKSEL----------------RMEVDDLAANVETLTRAKASAEKLCRT------ 1049
Cdd:pfam12128 542 KEAPDWEQsIGKVISPELLHRTDLDPEVWDGsvggelnlygvkldlkRIDVPEWAASEEELRERLDKAEEALQSarekqa 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1050 -YEDQLSEAKIKVEELQRQLADASTQrgrLQTESGELSRLLEEKECLisQLSRGKALAAQSLEELRRQLEEESKAKSALA 1128
Cdd:pfam12128 622 aAEEQLVQANGELEKASREETFARTA---LKNARLDLRRLFDEKQSE--KDKKNKALAERKDSANERLNSLEAQLKQLDK 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1129 HAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKKKlalrlQEAEEGVEaanak 1208
Cdd:pfam12128 697 KHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKR-----DLASLGVD----- 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1209 csslEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQRESRGlgtELFRLRHGHEE 1288
Cdd:pfam12128 767 ----PDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQ---QLARLIADTKL 839
|
650 660
....*....|....*....|..
gi 768017794 1289 ALEALETLKRENKNLQEEISDL 1310
Cdd:pfam12128 840 RRAKLEMERKASEKQQVRLSEN 861
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1420-1694 |
3.01e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.14 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1420 LNDLELQLGHATRQATEAQAATRLMQAQLKE--EQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQgersr 1497
Cdd:PRK11281 17 FLLLCLSSAFARAASNGDLPTEADVQAQLDAlnKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQ----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1498 rlAEQELLEATERLNLLHSQNTGLLNQK------KKLEADLAQLSGEVEEAAQERREAE----------EKAKKAITDAA 1561
Cdd:PRK11281 92 --APAKLRQAQAELEALKDDNDEETRETlstlslRQLESRLAQTLDQLQNAQNDLAEYNsqlvslqtqpERAQAALYANS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1562 MMAEELKKEqdtsahLERMKKTLEQTVRELQARLeEAEQAALRGGKKQVQKLEAKVRELeaeLDAEQKKHAEALKGVRKH 1641
Cdd:PRK11281 170 QRLQQIRNL------LKGGKVGGKALRPSQRVLL-QAEQALLNAQNDLQRKSLEGNTQL---QDLLQKQRDYLTARIQRL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 768017794 1642 ERRVKELayQAEEDRKNLARMQDLVDKLQSKVKSYKRQ---FEEAEQQANTNLAKY 1694
Cdd:PRK11281 240 EHQLQLL--QEAINSKRLTLSEKTVQEAQSQDEAARIQanpLVAQELEINLQLSQR 293
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1454-1697 |
3.15e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1454 GRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGER--SRRLA-------EQELLEATERLNllhsqntgllnq 1524
Cdd:PRK04863 780 GRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRfiGSHLAvafeadpEAELRQLNRRRV------------ 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1525 kkKLEADLAQLsgevEEAAQERREAEEKAKKAITDaammaeeLKKEQDTSAHLERmkKTLEQTVRELQARLEEAEQAAL- 1603
Cdd:PRK04863 848 --ELERALADH----ESQEQQQRSQLEQAKEGLSA-------LNRLLPRLNLLAD--ETLADRVEEIREQLDEAEEAKRf 912
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1604 --RGGKK--QVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAY--------QAEEDRKNLARMQDLVDKLQS 1671
Cdd:PRK04863 913 vqQHGNAlaQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEvvqrrahfSYEDAAEMLAKNSDLNEKLRQ 992
|
250 260
....*....|....*....|....*.
gi 768017794 1672 KVKSYKRQFEEAEQQANTNLAKYRKA 1697
Cdd:PRK04863 993 RLEQAEQERTRAREQLRQAQAQLAQY 1018
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
633-897 |
4.73e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 633 KMKPLLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQ 712
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 713 LEGKVKELSERLEDEEEVNADlaaRRRKLEDECTELKKDIDDLELTLAKAEKEKQATE-NKVKnlTEEMAALDESVARLT 791
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAE---ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEeNKIK--AAEEAKKAEEDKKKA 1677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 792 KEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDK 871
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
250 260
....*....|....*....|....*...
gi 768017794 872 --QQLEEKLKKKDSELSQLSLRVEDEQL 897
Cdd:PTZ00121 1758 kiAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
637-894 |
4.78e-05 |
|
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: 48.25 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 637 LLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEethvsitQEKNDLalqlqaeQDNLADAEERCHLLIKSKVQLEGK 716
Cdd:pfam01576 825 LAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQ-------QERDEL-------ADEIASGASGKSALQDEKRRLEAR 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 717 VKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVArlTKEKKA 796
Cdd:pfam01576 891 IAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK--SKFKSS 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 797 LQEahqqalgdlqaeedrvsaltkaklrLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLEE 876
Cdd:pfam01576 969 IAA-------------------------LEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKD 1023
|
250
....*....|....*...
gi 768017794 877 KLKKKDSELSQLSLRVED 894
Cdd:pfam01576 1024 QAEKGNSRMKQLKRQLEE 1041
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
640-822 |
5.09e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 640 SAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERchlLIKSKVQLEGKVKE 719
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE---IAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 720 LSERL------------------------------------EDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAE 763
Cdd:COG3883 88 LGERAralyrsggsvsyldvllgsesfsdfldrlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 768017794 764 KEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAK 822
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1427-1654 |
5.55e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1427 LGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLA--AELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQEL 1504
Cdd:COG3883 2 LALALAAPTPAFADPQIQAKQKELSELQAELEAAQAelDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1505 LEATERLN------------------LLHSQNTG-LLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKaitdaammAE 1565
Cdd:COG3883 82 EERREELGeraralyrsggsvsyldvLLGSESFSdFLDRLSALSKIADADADLLEELKADKAELEAKKAE--------LE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1566 ELKKEqdtsahLERMKKTLEQTVRELQARLEEAeQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRV 1645
Cdd:COG3883 154 AKLAE------LEALKAELEAAKAELEAQQAEQ-EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
....*....
gi 768017794 1646 KELAYQAEE 1654
Cdd:COG3883 227 AAAAAAAAA 235
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1355-1715 |
6.31e-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: 48.02 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1355 KTLRIQLELSQVKAEVDRKLAEKDEECANLRRNHQRAVESLQasldaetRARNeALRLKKKME---GDLNDLELQLGHAT 1431
Cdd:COG3096 296 GARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLN-------LVQT-ALRQQEKIEryqEDLEELTERLEEQE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1432 RQATEAQ-----AATRLMQA---------QLKEEQAGRDEEQRLAAELHEQAQALERRASLLAA----------ELEELR 1487
Cdd:COG3096 368 EVVEEAAeqlaeAEARLEAAeeevdslksQLADYQQALDVQQTRAIQYQQAVQALEKARALCGLpdltpenaedYLAAFR 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1488 AALEQGERSRRLAEQELLEATERlnllHSQNtgllnqKKKLEAdLAQLSGEVEeaaqeRREAEEKAKKAITDAammaeel 1567
Cdd:COG3096 448 AKEQQATEEVLELEQKLSVADAA----RRQF------EKAYEL-VCKIAGEVE-----RSQAWQTARELLRRY------- 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1568 kkeqdtsahlermkktleqtvRELQARLEeaeqaalrggkkQVQKLEAKVRELEAELDAEQKKhaealkgvrkhERRVKE 1647
Cdd:COG3096 505 ---------------------RSQQALAQ------------RLQQLRAQLAELEQRLRQQQNA-----------ERLLEE 540
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768017794 1648 LAYQAEEDRKNlarmQDLVDKLQSKVKSykrQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQA 1715
Cdd:COG3096 541 FCQRIGQQLDA----AEELEELLAELEA---QLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARA 601
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1500-1716 |
6.96e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1500 AEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLER 1579
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1580 MK--KTLEQTVRELQA--RLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEED 1655
Cdd:COG3883 108 LLgsESFSDFLDRLSAlsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768017794 1656 RKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQAN 1716
Cdd:COG3883 188 SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
635-1339 |
7.62e-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: 47.73 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 635 KPLLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEkndlaLQLQAEQDNL---ADAEERCHLLIKSKV 711
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQS-----LATRLELDGFergPFSERQIKNFHTLVI 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 712 Q-LEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARL 790
Cdd:TIGR00606 401 ErQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQEL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 791 TKEKKALQEAHQQALGDLQAEEDRV-----SALTKAKLRLEQQVEDLECSLEQEKKL------RMDTERAKRKLEGDLKL 859
Cdd:TIGR00606 481 RKAERELSKAEKNSLTETLKKEVKSlqnekADLDRKLRKLDQEMEQLNHHTTTRTQMemltkdKMDKDEQIRKIKSRHSD 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 860 TQESVADAAQDKQQLEEKLKKKDSELSQLSLRVedeqllgAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAAr 939
Cdd:TIGR00606 561 ELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRL-------AKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVC- 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 940 eleelserleeaggasagqreGCRKREAELGRLRRELEEAAlRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEK 1019
Cdd:TIGR00606 633 ---------------------GSQDEESDLERLKEEIEKSS-KQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTE 690
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1020 SELRMEVDDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVE----ELQRQLADASTQRGRLQTESGELSRL---LEEK 1092
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPgrqsIIDLKEKEIPELRNKLQKVNRDIQRLkndIEEQ 770
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1093 ECLISQLSRGKALAA--------------QSLEELRRQLEEESKAKSA-LAHAVQALRHDCDLLREQHEEEAEAQAELQR 1157
Cdd:TIGR00606 771 ETLLGTIMPEEESAKvcltdvtimerfqmELKDVERKIAQQAAKLQGSdLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1158 LLSKANAEVAQWRSKYE---------ADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTL 1228
Cdd:TIGR00606 851 LIQDQQEQIQHLKSKTNelkseklqiGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1229 ELEraTSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEI- 1307
Cdd:TIGR00606 931 SKE--TSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDId 1008
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 768017794 1308 ------SDLTDQVSLSGKS--IQELEKTKKALEGEKSEIQ 1339
Cdd:TIGR00606 1009 tqkiqeRWLQDNLTLRKREneLKEVEEELKQHLKEMGQMQ 1048
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1361-1656 |
8.40e-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: 47.32 E-value: 8.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1361 LELSQVKAEVDRKLAE--------KDEECANLRRNHQRAVESLQASLDAETRaRNEALRLKKKMEGDLNDLELQLGHATR 1432
Cdd:NF033838 135 LEPGKKVAEATKKVEEaekkakdqKEEDRRNYPTNTYKTLELEIAESDVEVK-KAELELVKEEAKEPRDEEKIKQAKAKV 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1433 QATEAQAaTRLMQAQLKEEQAGRDEEQRLAAELHEQAqalerrasllaaelEELRAALEQGE---RSRRLAEQELLEATE 1509
Cdd:NF033838 214 ESKKAEA-TRLEKIKTDREKAEEEAKRRADAKLKEAV--------------EKNVATSEQDKpkrRAKRGVLGEPATPDK 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1510 RLNLLHSQNTGLlnQKKKLEADLAQLSGEVEEAAQERREAEEKAKKaitdaammaeelKKEQDTSAHLERMKKTLEQTVR 1589
Cdd:NF033838 279 KENDAKSSDSSV--GEETLPSPSLKPEKKVAEAEKKVEEAKKKAKD------------QKEEDRRNYPTNTYKTLELEIA 344
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768017794 1590 ELQARLEEAEQAALRGGKKQVQKlEAKVRELEAELDAEqKKHAEALKGVRKHERRVKELAYQ--AEEDR 1656
Cdd:NF033838 345 ESDVKVKEAELELVKEEAKEPRN-EEKIKQAKAKVESK-KAEATRLEKIKTDRKKAEEEAKRkaAEEDK 411
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
698-870 |
8.46e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 698 DAEERCHLLIKSKVQLEGKVKELSERLEDEEEVNADLAARRRKL----------------EDECTELKKDIDDLELT--- 758
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdeidvasaEREIAELEAELERLDASsdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 759 LAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKL--RLEQQVEDlecsl 836
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLeeRFAAALGD----- 761
|
170 180 190
....*....|....*....|....*....|....
gi 768017794 837 EQEKKLRMDTERAKRKLEGDLKLTQESVADAAQD 870
Cdd:COG4913 762 AVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1538-1700 |
1.41e-04 |
|
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: 46.48 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1538 EVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEE----AEQAALRGGKKQVQKL 1613
Cdd:pfam15709 349 EVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERkqrlQLQAAQERARQQQEEF 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1614 EAKVRELeaeldaEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQdlvdklQSKVKSYKRQFEEAEQQANTNLAK 1693
Cdd:pfam15709 429 RRKLQEL------QRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMA------EEERLEYQRQKQEAEEKARLEAEE 496
|
....*..
gi 768017794 1694 YRKAQHE 1700
Cdd:pfam15709 497 RRQKEEE 503
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1443-1653 |
1.52e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.11 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1443 LMQAQLKEEQAGRDEE-QRLAAELHEQAQ--ALERRASL-LAAELEELRAALEQGErsrrlAEQElleaterlnllhsqn 1518
Cdd:PRK09039 39 VAQFFLSREISGKDSAlDRLNSQIAELADllSLERQGNQdLQDSVANLRASLSAAE-----AERS--------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1519 tgllnqkkKLEADLAQLSGEVEEAAQerreaeekakkaitDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLeEA 1598
Cdd:PRK09039 99 --------RLQALLAELAGAGAAAEG--------------RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQL-AA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 768017794 1599 EQAALRGGKKQVQKLEAKVRELEAELDAeqkkhaeALKgvrkheRRVKELA-YQAE 1653
Cdd:PRK09039 156 LEAALDASEKRDRESQAKIADLGRRLNV-------ALA------QRVQELNrYRSE 198
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
653-909 |
1.54e-04 |
|
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: 46.64 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 653 ELRGLRGALAAAEA---KRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLEDEEE 729
Cdd:pfam05483 406 ELEELKKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKL 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 730 VNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQ 809
Cdd:pfam05483 486 KNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVK 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 810 AEEDRVsaltkaklrlEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKKDSELSQLS 889
Cdd:pfam05483 566 CKLDKS----------EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYE 635
|
250 260
....*....|....*....|
gi 768017794 890 LRVEDEQLLGAQMQKKIKEL 909
Cdd:pfam05483 636 IKVNKLELELASAKQKFEEI 655
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
966-1682 |
1.66e-04 |
|
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: 46.76 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 966 EAELGRLRRELEEaalrHEATVAALRRKQAEGAAELGEQVDSLQ-RVRQKLEKEKSELRMEVDDLAANVETLTRAKASAe 1044
Cdd:pfam12128 257 ELRLSHLHFGYKS----DETLIASRQEERQETSAELNQLLRTLDdQWKEKRDELNGELSAADAAVAKDRSELEALEDQH- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1045 klcRTYEDQ-LSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLS-RGKALAAQSLEELRRQLEEESK 1122
Cdd:pfam12128 332 ---GAFLDAdIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKeQNNRDIAGIKDKLAKIREARDR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1123 AKSALAHAVQALrhdCDLLREQHEEEAEAQAELQRLLSKANAEVaqwrsKYEADAIQRTEELEEAKKKLALRLQEAEEGV 1202
Cdd:pfam12128 409 QLAVAEDDLQAL---ESELREQLEAGKLEFNEEEYRLKSRLGEL-----KLRLNQATATPELLLQLENFDERIERAREEQ 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1203 EAANAKCSSLEKAKLRLQTESEDVTLELERATsaAAALDKKQRHLERALEERRRQEEEMQRELEAAQ--RESRG--LGTE 1278
Cdd:pfam12128 481 EAANAEVERLQSELRQARKRRDQASEALRQAS--RRLEERQSALDELELQLFPQAGTLLHFLRKEAPdwEQSIGkvISPE 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1279 LFRLRHGHEEALEAleTLKRENK----NLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQaaleeaegaleleet 1354
Cdd:pfam12128 559 LLHRTDLDPEVWDG--SVGGELNlygvKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQA--------------- 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1355 ktlRIQLELSQVKAEVDR-KLAEKDEECA--NLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHAT 1431
Cdd:pfam12128 622 ---AAEEQLVQANGELEKaSREETFARTAlkNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKH 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1432 RQATEAQAATRLmQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELraaleQGERSRRLAEQELLEATErl 1511
Cdd:pfam12128 699 QAWLEEQKEQKR-EARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKAL-----ETWYKRDLASLGVDPDVI-- 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1512 nllhsqntgllnqkKKLEADLAQLSGEVEEAAQERREAEEKAKkaitdaaMMAEELKKEQDtsaHLERMKKTLEQTVREL 1591
Cdd:pfam12128 771 --------------AKLKREIRTLERKIERIAVRRQEVLRYFD-------WYQETWLQRRP---RLATQLSNIERAISEL 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1592 QARLEEAEQAAlrggKKQVQKLEakvRELEAeLDAEQKKHAEALKGVRKHERRVKELA--YQAEEDRKNLARMQDLVDKL 1669
Cdd:pfam12128 827 QQQLARLIADT----KLRRAKLE---MERKA-SEKQQVRLSENLRGLRCEMSKLATLKedANSEQAQGSIGERLAQLEDL 898
|
730
....*....|...
gi 768017794 1670 QSKVKSYKRQFEE 1682
Cdd:pfam12128 899 KLKRDYLSESVKK 911
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
665-910 |
1.70e-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: 46.55 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 665 EAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLEDEEEVNADLAARRRKLEDE 744
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 745 CTELKKDIDDLELTLAKAEKEKQATE-------NKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSA 817
Cdd:TIGR04523 112 IKNDKEQKNKLEVELNKLEKQKKENKknidkflTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 818 LTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRK---LEGDLKLTQesvadaaQDKQQLEEKLKKKDSELSQLSLRVED 894
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQnnqLKDNIEKKQ-------QEINEKTTEISNTQTQLNQLKDEQNK 264
|
250
....*....|....*.
gi 768017794 895 EQllgAQMQKKIKELQ 910
Cdd:TIGR04523 265 IK---KQLSEKQKELE 277
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1392-1602 |
1.83e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1392 VESLQASLDAetrARNEALRLKKKMegDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQA 1471
Cdd:COG3206 184 LPELRKELEE---AEAALEEFRQKN--GLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1472 LERrasllAAELEELRAALEQgersrrlAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREA-- 1549
Cdd:COG3206 259 LLQ-----SPVIQQLRAQLAE-------LEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEAlq 326
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 768017794 1550 --EEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAA 1602
Cdd:COG3206 327 arEASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAE 381
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
667-1197 |
1.91e-04 |
|
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: 46.25 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 667 KRQELEETHVSITQEKN---DLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLEDEEEVNADLAARRRKLED 743
Cdd:pfam05483 238 KEKQVSLLLIQITEKENkmkDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 744 ECTELKKDIDDLeltlaKAEKEKQATE-NKVKN----LTEEMAALDESVARLTKEKKALQEAHQQALG----DLQAEEDR 814
Cdd:pfam05483 318 DLQIATKTICQL-----TEEKEAQMEElNKAKAahsfVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 815 VSALTKAKLRLEQQVEDLECSLEQEKKLrMDTERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKkkdselSQLSLRVED 894
Cdd:pfam05483 393 LEEMTKFKNNKEVELEELKKILAEDEKL-LDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLE------IQLTAIKTS 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 895 EQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGCRK----REAELg 970
Cdd:pfam05483 466 EEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQienlEEKEM- 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 971 RLRRELE---EAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASAEKLC 1047
Cdd:pfam05483 545 NLRDELEsvrEEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKG 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1048 RTYEDQLSEAKIKVEELQRQLADASTQRGRL-QTESGELSRLLEEKECLISQLSRGKALAAQSLEELRRQLEEESKAKSA 1126
Cdd:pfam05483 625 SAENKQLNAYEIKVNKLELELASAKQKFEEIiDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAE 704
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768017794 1127 LAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELE---EAKKKLALRLQE 1197
Cdd:pfam05483 705 MVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEiekEEKEKLKMEAKE 778
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1499-1723 |
2.31e-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: 46.16 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1499 LAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKaitdaammaeelKKEQDTSAHLE 1578
Cdd:NF033838 101 LYELNVLKEKSEAELTSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKD------------QKEEDRRNYPT 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1579 RMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKlEAKVRELEAELDAEQKKhAEALKGVRKHERRVKELAYQAEEDRKN 1658
Cdd:NF033838 169 NTYKTLELEIAESDVEVKKAELELVKEEAKEPRD-EEKIKQAKAKVESKKAE-ATRLEKIKTDREKAEEEAKRRADAKLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1659 LARMQDLVDKLQSKVKSYKRQF---EEAEQQANTNLAKYR--------------KAQHELDDAEERADMAETQANKLRAR 1721
Cdd:NF033838 247 EAVEKNVATSEQDKPKRRAKRGvlgEPATPDKKENDAKSSdssvgeetlpspslKPEKKVAEAEKKVEEAKKKAKDQKEE 326
|
..
gi 768017794 1722 TR 1723
Cdd:NF033838 327 DR 328
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
636-910 |
2.97e-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: 45.71 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 636 PLLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQ----------------EKNDLALQLQAEQDNLADA 699
Cdd:COG3096 776 PLFGRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvgghlavafapdpeaELAALRQRRSELERELAQH 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 700 EERCHLL------IKSKVQLEGKV---------KELSERLED-EEEVNADLAARR---------RKLEDECTELKKD--- 751
Cdd:COG3096 856 RAQEQQLrqqldqLKEQLQLLNKLlpqanlladETLADRLEElREELDAAQEAQAfiqqhgkalAQLEPLVAVLQSDpeq 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 752 IDDLELTLAKAEKEKQATENKVKNLTEEMA-----ALDESVARLTkEKKALQEAHQQALgdLQAEEDRvsalTKAKLRLE 826
Cdd:COG3096 936 FEQLQADYLQAKEQQRRLKQQIFALSEVVQrrphfSYEDAVGLLG-ENSDLNEKLRARL--EQAEEAR----REAREQLR 1008
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 827 QQVEDLECSLE--------QEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKKDSELSQLS---LRVEDE 895
Cdd:COG3096 1009 QAQAQYSQYNQvlaslkssRDAKQQTLQELEQELEELGVQADAEAEERARIRRDELHEELSQNRSRRSQLEkqlTRCEAE 1088
|
330
....*....|....*
gi 768017794 896 QllgAQMQKKIKELQ 910
Cdd:COG3096 1089 M---DSLQKRLRKAE 1100
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1363-1539 |
3.27e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1363 LSQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRlkKKMEGDLNDLELQLGHATRQATEAQAATR 1442
Cdd:COG3206 217 LLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVI--QQLRAQLAELEAELAELSARYTPNHPDVI 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1443 LMQAQLKE-EQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERsrrlAEQELLEATERLNLLHSQNTGL 1521
Cdd:COG3206 295 ALRAQIAAlRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE----LEAELRRLEREVEVARELYESL 370
|
170
....*....|....*...
gi 768017794 1522 LNQKKKLEADLAQLSGEV 1539
Cdd:COG3206 371 LQRLEEARLAEALTVGNV 388
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1389-1705 |
3.50e-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: 45.39 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1389 QRAVESLQASLDAETRARNEAL-----RLKKKMEGDLNDLELQLGHATRQATEAQ--AATRLMQAQLKEEQAGRDEEQRL 1461
Cdd:NF033838 68 EKILSEIQKSLDKRKHTQNVALnkklsDIKTEYLYELNVLKEKSEAELTSKTKKEldAAFEQFKKDTLEPGKKVAEATKK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1462 AAELHEQA--QALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERlnllHSQNTGLLNQ-KKKLEADLAQLSgE 1538
Cdd:NF033838 148 VEEAEKKAkdQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKEEAK----EPRDEEKIKQaKAKVESKKAEAT-R 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1539 VEEAAQERREAEEKAKKaiTDAAMMAEELKKEQDTSAHlERMKKTLEQTVRELQARLEEAEQAAlRGGKKQVQKLEAKVR 1618
Cdd:NF033838 223 LEKIKTDREKAEEEAKR--RADAKLKEAVEKNVATSEQ-DKPKRRAKRGVLGEPATPDKKENDA-KSSDSSVGEETLPSP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1619 ELEAEldaeqKKHAEALKGVRKHERRVKElayQAEEDRKNLA--RMQDL---VDKLQSKVKSYKRQF--EEAEQQANTNL 1691
Cdd:NF033838 299 SLKPE-----KKVAEAEKKVEEAKKKAKD---QKEEDRRNYPtnTYKTLeleIAESDVKVKEAELELvkEEAKEPRNEEK 370
|
330
....*....|....
gi 768017794 1692 AKYRKAQHELDDAE 1705
Cdd:NF033838 371 IKQAKAKVESKKAE 384
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
644-1074 |
3.56e-04 |
|
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: 45.49 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 644 EEELAALRAELRGLRGALAAAEAKR--QELEETHVSIT---QEKNDLALQLQAEQDNLADAEErchlliKSKVQLEGKVK 718
Cdd:pfam15921 244 EDQLEALKSESQNKIELLLQQHQDRieQLISEHEVEITgltEKASSARSQANSIQSQLEIIQE------QARNQNSMYMR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 719 ELSERLEDEEEVNADLAARRRKLEDECTELKKD--IDDLELTLAKAEKEKQATENkvKNLTEEMAALdesVARLTKEKKA 796
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQLQKL---LADLHKREKE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 797 LQEAHQQ--------------------ALGDLQAEEDRVSALTKA-----KLRLEQQVEDLEC---SLEQEKKLRMDTER 848
Cdd:pfam15921 393 LSLEKEQnkrlwdrdtgnsitidhlrrELDDRNMEVQRLEALLKAmksecQGQMERQMAAIQGkneSLEKVSSLTAQLES 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 849 AK---RKLEGDL---KLTQES----VADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEE 918
Cdd:pfam15921 473 TKemlRKVVEELtakKMTLESsertVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEA 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 919 ELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREgcrkREAELGRLRRELEEAALRHEATVAALRRKQAEGA 998
Cdd:pfam15921 553 LKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQ----LEKEINDRRLELQEFKILKDKKDAKIRELEARVS 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 999 AELGEQVDSLQRVRQKLEKEKsELRMEVDDLAANVET----LTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQ 1074
Cdd:pfam15921 629 DLELEKVKLVNAGSERLRAVK-DIKQERDQLLNEVKTsrneLNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSE 707
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
707-1045 |
3.59e-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: 45.50 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 707 IKSKVQLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLteemaaldes 786
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI---------- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 787 vaRLTKEKKALQEAHQQalgDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKltqESVAD 866
Cdd:pfam17380 354 --RQEERKRELERIRQE---EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKV---EMEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 867 AAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSE 946
Cdd:pfam17380 426 RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERK 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 947 RLEEaggasagqrEGCRKREAelgrLRRELEEaalRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKeKSELRMEV 1026
Cdd:pfam17380 506 QAMI---------EEERKRKL----LEKEMEE---RQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRK-ATEERSRL 568
|
330
....*....|....*....
gi 768017794 1027 DDLAANVETLTRAKASAEK 1045
Cdd:pfam17380 569 EAMEREREMMRQIVESEKA 587
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1275-1620 |
3.86e-04 |
|
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: 44.89 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1275 LGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALegekseiqaaleeaegaleleET 1354
Cdd:pfam07888 85 LKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTL---------------------TQ 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1355 KTLRIQLELSQVKAEVDRKLAEKDEEcanlrrnhQRAVESLQASLDAetrARNEALRLKKKMEGDLNDLELQLGHATR-Q 1433
Cdd:pfam07888 144 RVLERETELERMKERAKKAGAQRKEE--------EAERKQLQAKLQQ---TEEELRSLSKEFQELRNSLAQRDTQVLQlQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1434 ATEAQAATRLMQAQLKEEQAGRDEEQrlAAELHEQAQALERRASLLAAELEEL------------RAALEQGERSRRLAE 1501
Cdd:pfam07888 213 DTITTLTQKLTTAHRKEAENEALLEE--LRSLQERLNASERKVEGLGEELSSMaaqrdrtqaelhQARLQAAQLTLQLAD 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1502 QELLEATERLNlLHSQNTGLLNQKKKLEADLAQLSGEV---EEAAQERREAEEKAKKaitdaammaeELKKEQDTSahle 1578
Cdd:pfam07888 291 ASLALREGRAR-WAQERETLQQSAEADKDRIEKLSAELqrlEERLQEERMEREKLEV----------ELGREKDCN---- 355
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 768017794 1579 rmKKTLEQTVRELQARleeaeQAALRGGKKQVQKLEAKVREL 1620
Cdd:pfam07888 356 --RVQLSESRRELQEL-----KASLRVAQKEKEQLQAEKQEL 390
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1448-1717 |
3.89e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 45.31 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1448 LKEEQAGRDEEQRLAAELHE-QAQALERRASL--LAAELEELRAALEQGERSRRLAE-------------QELLEATERL 1511
Cdd:PLN03188 938 LEEELASLMHEHKLLKEKYEnHPEVLRTKIELkrVQDELEHYRNFYDMGEREVLLEEiqdlrsqlqyyidSSLPSARKRN 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1512 NLLHSQNTGLLNQKKKLEAdlaqLSGEVEEAAQERREAEE-KAKKAITDAAMMAEELKKEQDTSAHL-ERMKKTLEqTVR 1589
Cdd:PLN03188 1018 SLLKLTYSCEPSQAPPLNT----IPESTDESPEKKLEQERlRWTEAESKWISLAEELRTELDASRALaEKQKHELD-TEK 1092
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1590 ELQARLEEAEQAALRGGKK---QVQKLEAKVRELEAELDAEQK-----KHAEALKGVRKHERR--------VKELAYQAE 1653
Cdd:PLN03188 1093 RCAEELKEAMQMAMEGHARmleQYADLEEKHIQLLARHRRIQEgiddvKKAAARAGVRGAESKfinalaaeISALKVERE 1172
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768017794 1654 EDRKNLarmQDLVDKLQSKVksykRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANK 1717
Cdd:PLN03188 1173 KERRYL---RDENKSLQAQL----RDTAEAVQAAGELLVRLKEAEEALTVAQKRAMDAEQEAAE 1229
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1531-1727 |
4.01e-04 |
|
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: 44.84 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1531 DLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQdtSAHLERMKKTLEQTVRELQARleEAEQAALRGGKKQV 1610
Cdd:TIGR02794 44 DPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQR--AAEQARQKELEQRAAAEKAAK--QAEQAAKQAEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1611 QKLEAKVRELeaeldAEQKKHAEALKGVRKHErrvkELAYQAEEDRKN-----------LARMQDLVDKLQSKVKSYKRQ 1679
Cdd:TIGR02794 120 QAEEAKAKQA-----AEAKAKAEAEAERKAKE----EAAKQAEEEAKAkaaaeakkkaeEAKKKAEAEAKAKAEAEAKAK 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 768017794 1680 FEEAEQQANTNLAKYRKAQHELDDAE-ERADMAETQANKLRARTRDALG 1727
Cdd:TIGR02794 191 AEEAKAKAEAAKAKAAAEAAAKAEAEaAAAAAAEAERKADEAELGDIFG 239
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1288-1518 |
4.20e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.29 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1288 EALEA-LETLKRENKNLQEEISDLTDQV------SLSGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQ 1360
Cdd:PRK11281 83 EQLKQqLAQAPAKLRQAQAELEALKDDNdeetreTLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQ 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1361 LELS---QVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARnealrlKKKMEGD--LNDL-ELQLGHATRQA 1434
Cdd:PRK11281 163 AALYansQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQ------RKSLEGNtqLQDLlQKQRDYLTARI 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1435 TEAQAATRLMQAQLKEEQAGRDEEQrlAAELHEQAQALERRA-SLLAAELEelraaleqgeRSRRLAeQELLEATERLNL 1513
Cdd:PRK11281 237 QRLEHQLQLLQEAINSKRLTLSEKT--VQEAQSQDEAARIQAnPLVAQELE----------INLQLS-QRLLKATEKLNT 303
|
....*
gi 768017794 1514 LHSQN 1518
Cdd:PRK11281 304 LTQQN 308
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
646-838 |
4.32e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 646 ELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSkvQLEGKVKELSERlE 725
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--LLEERFAAALGD-A 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 726 DEEEVNADLAARRRKLEdecTELKKDIDDLELTLAKAekeKQATENKVKNLTEEMAALDESVARLT------------KE 793
Cdd:COG4913 763 VERELRENLEERIDALR---ARLNRAEEELERAMRAF---NREWPAETADLDADLESLPEYLALLDrleedglpeyeeRF 836
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 768017794 794 KKALQEAHQQALGDLQaeedrvSALTKAKLRLEQQVEDLECSLEQ 838
Cdd:COG4913 837 KELLNENSIEFVADLL------SKLRRAIREIKERIDPLNDSLKR 875
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1301-1726 |
5.04e-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: 45.04 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1301 KNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQLELSQVKAEVDRKLA--EKD 1378
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNdiEEQ 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1379 EECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNdlELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEE 1458
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAA--KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELN 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1459 QRLAAELHEQAQALERRASLLAAELEELRAALeqgERSRRLAEQELLEATErlnlLHSQNTGLLNQKKKLEADLAQLSGE 1538
Cdd:TIGR00606 849 RKLIQDQQEQIQHLKSKTNELKSEKLQIGTNL---QRRQQFEEQLVELSTE----VQSLIREIKDAKEQDSPLETFLEKD 921
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1539 VEEAAQERREAEEKAKKAITDAAMMAEELKK--------EQDTSAHLERMKKTLEQTVRELQARLEEAEQaalrggkkQV 1610
Cdd:TIGR00606 922 QQEKEELISSKETSNKKAQDKVNDIKEKVKNihgymkdiENKIQDGKDDYLKQKETELNTVNAQLEECEK--------HQ 993
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1611 QKLEAKVRELEAELDAeQKKHAEALKG---VRKHERRVKELAYQAEEDRKNLARMQdlvdKLQSKVKSYKRQFEEAEQQA 1687
Cdd:TIGR00606 994 EKINEDMRLMRQDIDT-QKIQERWLQDnltLRKRENELKEVEEELKQHLKEMGQMQ----VLQMKQEHQKLEENIDLIKR 1068
|
410 420 430
....*....|....*....|....*....|....*....
gi 768017794 1688 NTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDAL 1726
Cdd:TIGR00606 1069 NHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMM 1107
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
725-910 |
5.47e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 725 EDEEEVN---ADLAARRRKLEDEctelkkdiddleltLAKAEKEKQATENKVKNLTEEMAALDEsvaRLTKEKKALQEAH 801
Cdd:PRK00409 513 EDKEKLNeliASLEELERELEQK--------------AEEAEALLKEAEKLKEELEEKKEKLQE---EEDKLLEEAEKEA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 802 QQALGDLQAEEDRVsaltkakLRLEQQVEDLECSLEQEKKLrmdtERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKK 881
Cdd:PRK00409 576 QQAIKEAKKEADEI-------IKELRQLQKGGYASVKAHEL----IEARKRLNKANEKKEKKKKKQKEKQEELKVGDEVK 644
|
170 180 190
....*....|....*....|....*....|....*.
gi 768017794 882 DSELSQ----LSLRVEDE---QLLGAQMQKKIKELQ 910
Cdd:PRK00409 645 YLSLGQkgevLSIPDDKEaivQAGIMKMKVPLSDLE 680
|
|
| FUSC |
pfam04632 |
Fusaric acid resistance protein family; This family includes a conserved region found in two ... |
1427-1618 |
5.47e-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: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1427 LGHATRQATEA--QAATRLMQAQLKEEQAGRDEEQRLAAeLHEQAQALERRASLLAAELEELRAaleqgeRSRRLAE--Q 1502
Cdd:pfam04632 153 VGPALRARLRArlRDALRLAAAALAGAPGAEAFEAARLR-LAADILALEALRSHAAFESPRGRA------RARALRRllA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1503 ELLEATERLNLLHSQ----NTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAkkAITDAAMMAEELKKEQDTSAhle 1578
Cdd:pfam04632 226 RMLALLPRLRSLARLlarlRTEGAGTVPELAALLDELAAWEAALAAEALQAALAA--LRARLRALRPALPLDFDTAA--- 300
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 768017794 1579 rmkkTLEQTVRELQARLEEAEQ--AALRGGKKQVQKLEAKVR 1618
Cdd:pfam04632 301 ----ELLARLADLLAELAEALAscRALRHPIAQGARPARLAR 338
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1469-1624 |
5.57e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1469 AQALER-RASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERR 1547
Cdd:COG2433 379 EEALEElIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEER 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1548 EAEEKAKkaitdaammaeELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAA---LRGGKKQVQKLEA----KVREL 1620
Cdd:COG2433 459 REIRKDR-----------EISRLDREIERLERELEEERERIEELKRKLERLKELWkleHSGELVPVKVVEKftkeAIRRL 527
|
....
gi 768017794 1621 EAEL 1624
Cdd:COG2433 528 EEEY 531
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1369-1570 |
6.09e-04 |
|
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: 44.56 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1369 EVDRKLAEKdEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDlndlelqlghaTRQATEAQAATRLMQAQL 1448
Cdd:pfam15709 349 EVERKRREQ-EEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEE-----------ERQRQEEEERKQRLQLQA 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1449 KEEQAGRDEEqrlaaELHEQAQALERRAsllaaELEELRAALEQGERSRRLAEQeLLEATERLNLLHSQNTGLLNQKKKL 1528
Cdd:pfam15709 417 AQERARQQQE-----EFRRKLQELQRKK-----QQEEAERAEAEKQRQKELEMQ-LAEEQKRLMEMAEEERLEYQRQKQE 485
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 768017794 1529 EADLAQLsgeveEAAQERREAEEKAKKAITDAAMMAEELKKE 1570
Cdd:pfam15709 486 AEEKARL-----EAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
738-1450 |
6.26e-04 |
|
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: 44.57 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 738 RRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAH--QQALGDLQAEEDRV 815
Cdd:TIGR00618 193 HGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 816 SALTKaklRLEQQVEdlecsleqekklRMDTERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKKDSELSQLSLRVEDE 895
Cdd:TIGR00618 273 RAQEA---VLEETQE------------RINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 896 QLLGAQmQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELeelserleeaggASAGQREGCRKREAELGRLRRE 975
Cdd:TIGR00618 338 SSIEEQ-RRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIH------------TLQQQKTTLTQKLQSLCKELDI 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 976 LEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASAEKLCRTYEDQLS 1055
Cdd:TIGR00618 405 LQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQ 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1056 EAKIKVEELQRQLADASTQRGRLQTES-----GELSRLLEEKECLISQLSRGKALAAQSLEELRRQLEEESKAKSALAHA 1130
Cdd:TIGR00618 485 ETRKKAVVLARLLELQEEPCPLCGSCIhpnpaRQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQ 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1131 VQALRHDCDLLreqheeeaeaqaELQRLLSKANAEVAQwrsKYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKcs 1210
Cdd:TIGR00618 565 MQEIQQSFSIL------------TQCDNRSKEDIPNLQ---NITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDL-- 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1211 sLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERA-LEERRRQEEEMQRELEAAQRESRGLGTELFRLRHGHEEA 1289
Cdd:TIGR00618 628 -QDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSiRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLL 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1290 LEALETLKRENKNLQE-------EISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQLE 1362
Cdd:TIGR00618 707 RELETHIEEYDREFNEienasssLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAE 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1363 LS---QVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQA 1439
Cdd:TIGR00618 787 IQffnRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQ 866
|
730
....*....|.
gi 768017794 1440 ATRLMQAQLKE 1450
Cdd:TIGR00618 867 EQAKIIQLSDK 877
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
641-909 |
6.33e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 641 AQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLE------ 714
Cdd:PRK04863 275 MRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEkieryq 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 715 GKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDL--------------------------------------E 756
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELksqladyqqaldvqqtraiqyqqavqalerakqlcglpD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 757 LTLAKAEKEKQATENKVKNLTEEMAALDE--SVARLTKEK--KALQ------------EAHQQALGDL-QAEEDRVSALT 819
Cdd:PRK04863 435 LTADNAEDWLEEFQAKEQEATEELLSLEQklSVAQAAHSQfeQAYQlvrkiagevsrsEAWDVARELLrRLREQRHLAEQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 820 KAKLRleQQVEDLECSLEQEKKLrmdtERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLG 899
Cdd:PRK04863 515 LQQLR--MRLSELEQRLRQQQRA----ERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQL 588
|
330
....*....|
gi 768017794 900 AQMQKKIKEL 909
Cdd:PRK04863 589 EQLQARIQRL 598
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
737-888 |
6.54e-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: 44.63 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 737 RRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKE----KKALQEAhQQALGDLQAEE 812
Cdd:pfam05667 329 LQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQykvkKKTLDLL-PDAEENIAKLQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 813 DRVSALTKAKLRLEQQ-----VEDLEcSLEQEKKLRMDTE-RAKRKLEgDLKLTQESVadaaqdkQQLEEKLKKKDSELS 886
Cdd:pfam05667 408 ALVDASAQRLVELAGQwekhrVPLIE-EYRALKEAKSNKEdESQRKLE-EIKELREKI-------KEVAEEAKQKEELYK 478
|
..
gi 768017794 887 QL 888
Cdd:pfam05667 479 QL 480
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
645-1036 |
6.66e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 645 EELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKvQLEGKVKELSERL 724
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIE-RYQADLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 725 EDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDE-----SVARLTKEKkaLQE 799
Cdd:PRK04863 365 EEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERakqlcGLPDLTADN--AED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 800 AHQQalgdLQAEEDrvsALTKAKLRLEQQVEDLECSLEQEKKlrmdTERAKRKLEGDLkltqeSVADAAQDKQQLEEKLK 879
Cdd:PRK04863 443 WLEE----FQAKEQ---EATEELLSLEQKLSVAQAAHSQFEQ----AYQLVRKIAGEV-----SRSEAWDVARELLRRLR 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 880 kkdselsqlSLRVEDEQLlgAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAG-- 957
Cdd:PRK04863 507 ---------EQRHLAEQL--QQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESvs 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 958 ----QREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKsELRMEVDDLAANV 1033
Cdd:PRK04863 576 eareRRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERER-ELTVERDELAARK 654
|
...
gi 768017794 1034 ETL 1036
Cdd:PRK04863 655 QAL 657
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1433-1630 |
6.67e-04 |
|
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: 43.09 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1433 QATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQ----ALERRASLLA---AELEELRAALEQGERSRRLAEQELL 1505
Cdd:pfam00261 9 ELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQlleeELERTEERLAealEKLEEAEKAADESERGRKVLENRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1506 EATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLE------- 1578
Cdd:pfam00261 89 KDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEaseekas 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 768017794 1579 RMKKTLEQTVRELQARLEEAEQAAlRGGKKQVQKLEAKVRELEAELDAEQKK 1630
Cdd:pfam00261 169 EREDKYEEQIRFLTEKLKEAETRA-EFAERSVQKLEKEVDRLEDELEAEKEK 219
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
711-898 |
6.92e-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: 44.46 E-value: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 711 VQLEGKVKELSERLEDEEEVNADLAAR-------RRKLEDECTELKKDIDDLELTLAKA----EKEKQATENKVKNLTEE 779
Cdd:pfam09726 398 VRLEQDIKKLKAELQASRQTEQELRSQissltslERSLKSELGQLRQENDLLQTKLHNAvsakQKDKQTVQQLEKRLKAE 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 780 MAALDESVARLTKEKKALQEahqqalgdlqaEEDrvsalTKAKLRLEQQVEDLECSlEQEKKLRMDTERAKRKLEGDLKL 859
Cdd:pfam09726 478 QEARASAEKQLAEEKKRKKE-----------EEA-----TAARAVALAAASRGECT-ESLKQRKRELESEIKKLTHDIKL 540
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 768017794 860 TQESVADAAQDKQQLEE-KLKKKDSE--LSQLSLRVEDEQLL 898
Cdd:pfam09726 541 KEEQIRELEIKVQELRKyKESEKDTEvlMSALSAMQDKNQHL 582
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
758-959 |
7.22e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 758 TLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSAL----TKAKLRLEQQVEDLE 833
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLqaeiAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 834 CSLEQEKKLRMDTERAKRKLEGD---------------LKLTQESVADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLL 898
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSEsfsdfldrlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768017794 899 GAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQR 959
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1484-1721 |
7.27e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1484 EELRAALEQgersrrLAEQELLEATERLNLLHSQNT-GLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKaitdaam 1562
Cdd:PRK11281 39 ADVQAQLDA------LNKQKLLEAEDKLVQQDLEQTlALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEA------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1563 maeeLKKEQDTSAhlermKKTLE-QTVRELQARLEEAE------QAALRGGKKQVQKLEAKVRELEAELDAEQKKHAE-- 1633
Cdd:PRK11281 106 ----LKDDNDEET-----RETLStLSLRQLESRLAQTLdqlqnaQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQir 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1634 -ALKGVR------KHERRVK---ELAY---QAEEDRKNLA---RMQDLvDKLQSKVKSYKRQFEEAEQQANTNL--AKYR 1695
Cdd:PRK11281 177 nLLKGGKvggkalRPSQRVLlqaEQALlnaQNDLQRKSLEgntQLQDL-LQKQRDYLTARIQRLEHQLQLLQEAinSKRL 255
|
250 260
....*....|....*....|....*..
gi 768017794 1696 K-AQHELDDAEERADMAETQANKLRAR 1721
Cdd:PRK11281 256 TlSEKTVQEAQSQDEAARIQANPLVAQ 282
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1287-1724 |
7.52e-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: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1287 EEALEALETLKRENKNLQ----EEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQLE 1362
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIdkflTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1363 LSQVKA--EVDRKLAEKDEECANLRRNHQRAVESLQAsldaetrarnealrlkkkmegDLNDLELQLGHATRQATEAQAA 1440
Cdd:TIGR04523 203 LSNLKKkiQKNKSLESQISELKKQNNQLKDNIEKKQQ---------------------EINEKTTEISNTQTQLNQLKDE 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1441 TRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELE-----ELRAALEQGERSRRLAEQELLEATERLNLLH 1515
Cdd:TIGR04523 262 QNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLN 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1516 SQNTGLLNQKKKLEADLAQLsgeveeaaqeRREAEEKAKKAitdaammaEELKKEQDTsaHLERMKKtLEQTVRELQARL 1595
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEK----------QRELEEKQNEI--------EKLKKENQS--YKQEIKN-LESQINDLESKI 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1596 EEAEqaalrggkKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKS 1675
Cdd:TIGR04523 401 QNQE--------KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV 472
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 768017794 1676 YKRQfeeaeqqantnlakYRKAQHELDDAEERADMAETQANKLRARTRD 1724
Cdd:TIGR04523 473 LSRS--------------INKIKQNLEQKQKELKSKEKELKKLNEEKKE 507
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1396-1556 |
7.59e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1396 QASLDAETRARNEAL-RLKKKMeGDLNDLeLQLGHATRQATEAQAATrlMQAQLKEEQAGRDEEQRLAAELHEQAQALER 1474
Cdd:PRK09039 41 QFFLSREISGKDSALdRLNSQI-AELADL-LSLERQGNQDLQDSVAN--LRASLSAAEAERSRLQALLAELAGAGAAAEG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1475 RASLLAAELEELRAaleQGERSRRLAEqelleaterlnllhsqntgLLNQkkKLEADLAQLsGEVEEA--AQERREAEEK 1552
Cdd:PRK09039 117 RAGELAQELDSEKQ---VSARALAQVE-------------------LLNQ--QIAALRRQL-AALEAAldASEKRDRESQ 171
|
....
gi 768017794 1553 AKKA 1556
Cdd:PRK09039 172 AKIA 175
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
713-893 |
7.63e-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: 44.43 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 713 LEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTK 792
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 793 EKKALQE---AHQQALGDLQ---AEEDRV-SALTKAKLRLEQQVEDlecSLEQEKKLRMDTERAKRKLEGDLKLTQESVA 865
Cdd:pfam10174 423 RVKSLQTdssNTDTALTTLEealSEKERIiERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELTEKESSLI 499
|
170 180
....*....|....*....|....*...
gi 768017794 866 DAAQDKQQLEEKLKKKDSELSQLSLRVE 893
Cdd:pfam10174 500 DLKEHASSLASSGLKKDSKLKSLEIAVE 527
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1296-1683 |
8.33e-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: 8.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1296 LKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAAleeaegaleleetktlriqlelsqvKAEVDRKLA 1375
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESE-------------------------NSEKQRELE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1376 EKDEECANLRRNHQRAVESLQasldaetrarnealrlkkKMEGDLNDLELQLGHATRQATEAQAATRLMQA--QLKEEQA 1453
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEIK------------------NLESQINDLESKIQNQEKLNQQKDEQIKKLQQekELLEKEI 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1454 GRDEEQRLA------------AELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGL 1521
Cdd:TIGR04523 429 ERLKETIIKnnseikdltnqdSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1522 LNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQdtsahlermkktLEQTVRELQARLEEAEQA 1601
Cdd:TIGR04523 509 EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN------------LEKEIDEKNKEIEELKQT 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1602 ALRGGKKQVQKlEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFE 1681
Cdd:TIGR04523 577 QKSLKKKQEEK-QELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIK 655
|
..
gi 768017794 1682 EA 1683
Cdd:TIGR04523 656 EI 657
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1265-1477 |
8.42e-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: 43.60 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1265 LEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEE 1344
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1345 AEGALELEETKTlRIQLELSQ-------VKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAEtraRNEALRLKKKME 1417
Cdd:COG4942 109 LLRALYRLGRQP-PLALLLSPedfldavRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE---RAELEALLAELE 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768017794 1418 GDLNDLELQLghATRQATEAQAATRLM--QAQLKEEQAGRDEEQRLAAELHEQAQALERRAS 1477
Cdd:COG4942 185 EERAALEALK--AERQKLLARLEKELAelAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
727-910 |
8.47e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 727 EEEVNADL--AARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQA 804
Cdd:PRK11281 38 EADVQAQLdaLNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 805 LGDLQAEEdrvsaltkaklrLEQQVEDLECSLEQEKK-----------LRMDTERAkrklegdlkltQESVADAAQDKQQ 873
Cdd:PRK11281 118 LSTLSLRQ------------LESRLAQTLDQLQNAQNdlaeynsqlvsLQTQPERA-----------QAALYANSQRLQQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 768017794 874 LEEKLK-----KKDSELSQLSLRVEDEQLLGAQMQKKIKELQ 910
Cdd:PRK11281 175 IRNLLKggkvgGKALRPSQRVLLQAEQALLNAQNDLQRKSLE 216
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1524-1636 |
8.69e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.71 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1524 QKKKLEADLAQLSGEV--EEAAQERREAEEKAK----KAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEE 1597
Cdd:COG2268 224 EEAELEQEREIETARIaeAEAELAKKKAEERREaetaRAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREE 303
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 768017794 1598 AEQAALRGGKKQVQKLEAKVRElEAELDAEQ---KKHAEALK 1636
Cdd:COG2268 304 AELEADVRKPAEAEKQAAEAEA-EAEAEAIRakgLAEAEGKR 344
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1432-1625 |
9.17e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.64 E-value: 9.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1432 RQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATErl 1511
Cdd:PRK09510 81 RKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAA-- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1512 nllhsqntgllnQKKKLEADLAQLSgevEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVREL 1591
Cdd:PRK09510 159 ------------AAKKAAAEAKKKA---EAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....*..
gi 768017794 1592 QARLEEAE---QAALRGGKKQVQKLEAKVRELEAELD 1625
Cdd:PRK09510 224 KAAAAKAAaeaKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1531-1701 |
9.74e-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: 42.60 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1531 DLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAaLRGGKKQV 1610
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-LGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1611 QkleakVRELEAELDAEQKKHAEAlkgvrkhERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTN 1690
Cdd:COG1579 90 E-----YEALQKEIESLKRRISDL-------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170
....*....|.
gi 768017794 1691 LAKYRKAQHEL 1701
Cdd:COG1579 158 LEELEAEREEL 168
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1396-1672 |
1.03e-03 |
|
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: 43.26 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1396 QASLDAETRA----RNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQaqa 1471
Cdd:pfam15905 75 QKELEKEIRAlvqeRGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSEDGTQ--- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1472 leRRASLLAAELEELRAALEQGERSRRLAEQEL---LEATERlNLLHSQntgllnqkkkleADLAQLSG---EVEEAAQE 1545
Cdd:pfam15905 152 --KKMSSLSMELMKLRNKLEAKMKEVMAKQEGMegkLQVTQK-NLEHSK------------GKVAQLEEklvSTEKEKIE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1546 RREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAAlrggKKQVQKLEAKVRELEAELD 1625
Cdd:pfam15905 217 EKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQEL----SKQIKDLNEKCKLLESEKE 292
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 768017794 1626 AEQKKHAEalkgvrKHERRVKELayqaEEDRKNLARMQDLVDKLQSK 1672
Cdd:pfam15905 293 ELLREYEE------KEQTLNAEL----EELKEKLTLEEQEHQKLQQK 329
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
751-864 |
1.15e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.92 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 751 DIDDLELTLAKAEKEKQATENkvknltEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVE 830
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKK------EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG 485
|
90 100 110
....*....|....*....|....*....|....
gi 768017794 831 DLEcslEQEKKLrmdtERAKRKLEGDLKLTQESV 864
Cdd:COG0542 486 KIP---ELEKEL----AELEEELAELAPLLREEV 512
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1182-1630 |
1.16e-03 |
|
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: 43.86 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1182 EELEEAKKKLA---LRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQE 1258
Cdd:TIGR04523 314 SELKNQEKKLEeiqNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1259 EEMQRELEAAQRESRGLGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGE---- 1334
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQlkvl 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1335 KSEIQAALEEAEGALELEETKTLRIqLELSQVKAEVDRKLAEKDEECANLRRNhQRAVESLQASLDAETRARNEALrLKK 1414
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEKEL-KKLNEEKKELEEKVKDLTKKISSLKEK-IEKLESEKKEKESKISDLEDEL-NKD 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1415 KMEGDLNDLELQLGHATRQATeaqaatrlmqaQLKEEQAGRDEEQRlaaELHEQAQALERRASLLAAELEELRAALEQGE 1494
Cdd:TIGR04523 551 DFELKKENLEKEIDEKNKEIE-----------ELKQTQKSLKKKQE---EKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1495 RSRRLAEQElleaTERLNllhSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKK-EQDT 1573
Cdd:TIGR04523 617 KELEKAKKE----NEKLS---SIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDwLKEL 689
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 768017794 1574 SAHLErmKKTLEQTVRELQARLEEAEqaalrggkKQVQKLEAKVRELEAELDAEQKK 1630
Cdd:TIGR04523 690 SLHYK--KYITRMIRIKDLPKLEEKY--------KEIEKELKKLDEFSKELENIIKN 736
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
649-904 |
1.33e-03 |
|
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: 43.59 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 649 ALRAELRGLRGALAAAEAKRQELEETHVSITQE-----KNDLALQLQAEQDNLADAEERCHLLIKSKVQLE----GKVKE 719
Cdd:pfam07111 112 AGQAEAEGLRAALAGAEMVRKNLEEGSQRELEEiqrlhQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkraGEAKQ 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 720 LSERLEDEEEVNADLAARRRKLEDECT---ELKKDIDDL---ELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKE 793
Cdd:pfam07111 192 LAEAQKEAELLRKQLSKTQEELEAQVTlveSLRKYVGEQvppEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVR 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 794 KK------ALQEAHQ----QALGDLQAEEDRvsaltKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQES 863
Cdd:pfam07111 272 VQslthmlALQEEELtrkiQPSDSLEPEFPK-----KCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQ 346
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 768017794 864 VADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQK 904
Cdd:pfam07111 347 VTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQE 387
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
773-1246 |
1.59e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 773 VKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLEcslEQEKKLRMDTERAKRK 852
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELE---AELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 853 LEgdlkltqesVADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQaraEELEEELEAERAARARVEK 932
Cdd:COG4717 125 LQ---------LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA---ELQEELEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 933 QRAEAARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVR 1012
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1013 QKLEKeksELRMEVDDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEK 1092
Cdd:COG4717 273 LTIAG---VLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1093 ECLISQLSRgkalAAQSLEELRRQLEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSK 1172
Cdd:COG4717 350 QELLREAEE----LEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1173 YEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLE------KAKLRLQTESEDVTLELERATSAAAALDKKQRH 1246
Cdd:COG4717 426 DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEedgelaELLQELEELKAELRELAEEWAALKLALELLEEA 505
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1291-1616 |
1.61e-03 |
|
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: 43.02 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1291 EALETLKRENKNLQEEISDLTDQVSLSgKSIQELEKTKKALEGEKseiqaaleeaegaleleetktlriqlELSQVKAEV 1370
Cdd:COG5185 282 ENANNLIKQFENTKEKIAEYTKSIDIK-KATESLEEQLAAAEAEQ--------------------------ELEESKRET 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1371 DRKLAEKDEECANLRRNHQRAVESLQAslDAETRARNEALRLKKKMegdLNDLELQLgHATRQATEAQAATRLMQAQlke 1450
Cdd:COG5185 335 ETGIQNLTAEIEQGQESLTENLEAIKE--EIENIVGEVELSKSSEE---LDSFKDTI-ESTKESLDEIPQNQRGYAQ--- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1451 eqagrdeeqrlaaelhEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEA 1530
Cdd:COG5185 406 ----------------EILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAY 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1531 DLAQLSGEVEEAAQERREAEEKAKKaitdAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQV 1610
Cdd:COG5185 470 DEINRSVRSKKEDLNEELTQIESRV----STLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLI 545
|
....*.
gi 768017794 1611 QKLEAK 1616
Cdd:COG5185 546 PASELI 551
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
1397-1633 |
1.63e-03 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 43.44 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1397 ASLDAETRARNEALRLKKKME-GDLNDLELQLGHATRQATEAQAAT------RLMQAQLKEEQAGRDEEQRLAAELHEQA 1469
Cdd:PRK14900 779 AVADPALRDLLQAGELARVHRvAGVEGSRLVVAAATAPAPQSAVGVgpgfevRVPLAGVIDLAAETARVDKEIGKVDQDL 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1470 QALERR---ASLLAaeleelRAALEQGERSRRLAEQelleaterlnllhsqntgLLNQKKKLEADLAQLSGEVEEAAQER 1546
Cdd:PRK14900 859 AVLERKlqnPSFVQ------NAPPAVVEKDRARAEE------------------LREKRGKLEAHRAMLSGSEANSARRD 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1547 REAEEKAKKAITDAAmmAEELKKEQDTSAhLERMKKTLEqTVRELQARLEEAEQAALRGGKKQVQK-LEAKVRELEAELD 1625
Cdd:PRK14900 915 TMEIQNEQKPTQDGP--AAEAQPAQENTV-VESAEKAVA-AVSEAAQQAATAVASGIEKVAEAVRKtVRRSVKKAAATRA 990
|
....*...
gi 768017794 1626 AEQKKHAE 1633
Cdd:PRK14900 991 AMKKKVAK 998
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1465-1704 |
2.17e-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: 42.01 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1465 LHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQ 1544
Cdd:pfam06008 10 ALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1545 ERREAEEKAKKAITDAAMMAEELkkEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAEL 1624
Cdd:pfam06008 90 AIKNLIDNIKEINEKVATLGEND--FALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1625 DAEQKKHAEALKGV-RKHERRVKEL--------AYQAEEDRKNLARMQDLVDKLQSK--VKSYKRQFEEAEQQANTNLAK 1693
Cdd:pfam06008 168 QEENKALANALRDSlAEYEAKLSDLrellreaaAKTRDANRLNLANQANLREFQRKKeeVSEQKNQLEETLKTARDSLDA 247
|
250
....*....|.
gi 768017794 1694 YRKAQHELDDA 1704
Cdd:pfam06008 248 ANLLLQEIDDA 258
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1012-1245 |
2.22e-03 |
|
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: 42.44 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1012 RQKLEKEKSELRMEVDDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEE 1091
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1092 KECLISQLSRgkaLAAQSLEELRRQLEEESKAKSALAHAVQALRHdcdllreqheeeaeaqaelqrllskanaeVAQWRS 1171
Cdd:COG4942 102 QKEELAELLR---ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKY-----------------------------LAPARR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768017794 1172 KYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQR 1245
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1362-1666 |
2.34e-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: 43.02 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1362 ELSQVKAEVDRKLAEKDEEcanlRRNHQRAVESLQASLDAETRARNEALRLkkkmegDLNDLELQLGHATRQATEAQAAT 1441
Cdd:COG3096 840 ALRQRRSELERELAQHRAQ----EQQLRQQLDQLKEQLQLLNKLLPQANLL------ADETLADRLEELREELDAAQEAQ 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1442 RLMQAQlkeeqagrdeeQRLAAELHEQAQALERRAsllaAELEELRAALEQGERSRRLAEQELLEATE----RLNLLHSQ 1517
Cdd:COG3096 910 AFIQQH-----------GKALAQLEPLVAVLQSDP----EQFEQLQADYLQAKEQQRRLKQQIFALSEvvqrRPHFSYED 974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1518 NTGLLNQKKKLEADLAQlsgEVEEAAQERREAEEKAKKAItdaammaeelKKEQDTSAHLERMKKTLEQTVRELQARLEE 1597
Cdd:COG3096 975 AVGLLGENSDLNEKLRA---RLEQAEEARREAREQLRQAQ----------AQYSQYNQVLASLKSSRDAKQQTLQELEQE 1041
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768017794 1598 AEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLV 1666
Cdd:COG3096 1042 LEELGVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQV 1110
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
732-881 |
2.63e-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: 41.45 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 732 ADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEmaaLDESVARLTKEKKALQEAH-QQALGDLQA 810
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE---IEEVEARIKKYEEQLGNVRnNKEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768017794 811 EEDrvsALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKK 881
Cdd:COG1579 97 EIE---SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1295-1601 |
3.00e-03 |
|
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: 42.32 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1295 TLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQLELSQVKAEVDRKL 1374
Cdd:pfam05701 223 NWEKELKQAEEELQRLNQQLLSAKDLKSKLETASALLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIQAALASAKKEL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1375 AE--------KDEecANLRRNhqrAVESLQASLDAEtRARNEALRLKKKMEG-DLNDLELQLGHATRQATEAQAAtrlmq 1445
Cdd:pfam05701 303 EEvkaniekaKDE--VNCLRV---AAASLRSELEKE-KAELASLRQREGMASiAVSSLEAELNRTKSEIALVQAK----- 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1446 aqlkeEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLA------------EQELLEATERLNL 1513
Cdd:pfam05701 372 -----EKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAAstvesrleavlkEIEAAKASEKLAL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1514 LHSQntGLLNQKKKLEADLAQLSG--------EVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTS-AHLERMKKTL 1584
Cdd:pfam05701 447 AAIK--ALQESESSAESTNQEDSPrgvtlsleEYYELSKRAHEAEELANKRVAEAVSQIEEAKESELRSlEKLEEVNREM 524
|
330
....*....|....*..
gi 768017794 1585 EQTVRELQARLEEAEQA 1601
Cdd:pfam05701 525 EERKEALKIALEKAEKA 541
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
642-832 |
3.01e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 642 QAEEELAALRaELRGLRGALAAAEAKRQELEEthvsitqeknDLALQLQAEQdNLADAEERCHLLIKSKVQLEGKVKELS 721
Cdd:PRK04863 497 VARELLRRLR-EQRHLAEQLQQLRMRLSELEQ----------RLRQQQRAER-LLAEFCKRLGKNLDDEDELEQLQEELE 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 722 ERLEDEEEVNADLAARRRKLEDECTELKKDIDdlelTLAKAEKEKQATENKVKNLTEEMAALDESVARLTkekkALQEAH 801
Cdd:PRK04863 565 ARLESLSESVSEARERRMALRQQLEQLQARIQ----RLAARAPAWLAAQDALARLREQSGEEFEDSQDVT----EYMQQL 636
|
170 180 190
....*....|....*....|....*....|.
gi 768017794 802 QQALGDLQAEEDRVSAltkAKLRLEQQVEDL 832
Cdd:PRK04863 637 LERERELTVERDELAA---RKQALDEEIERL 664
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1524-1725 |
3.04e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.24 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1524 QKKKLEADLAQLSGEVEEAAQERREAE--EKAKKAitdaammAEELKKEQD--TSAHLERMK----KTLEQTVRELQARL 1595
Cdd:PRK05035 442 EQEKKKAEEAKARFEARQARLEREKAAreARHKKA-------AEARAAKDKdaVAAALARVKakkaAATQPIVIKAGARP 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1596 EEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGV--RKHERRVKELAYQAEEDRKNLARMQDLVDklqSKV 1673
Cdd:PRK05035 515 DNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAkaKKAAQQAANAEAEEEVDPKKAAVAAAIAR---AKA 591
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 768017794 1674 KSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDA 1725
Cdd:PRK05035 592 KKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDP 643
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1590-1727 |
3.18e-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: 41.06 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1590 ELQARLEEAEQAaLRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDL--VD 1667
Cdd:COG1579 14 ELDSELDRLEHR-LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeYE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1668 KLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDALG 1727
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1444-1624 |
3.24e-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: 42.36 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1444 MQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQgERSRRLAEQELLEATERLNllhsqntglln 1523
Cdd:pfam13166 298 AISSLLAQLPAVSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRALEA-KRKDPFKSIELDSVDAKIE----------- 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1524 QKKKLEADLAQLSGEVEEAAQERREAEEKAKKAItdAAMMAEELKKEQDTsahLERMKKTLEQTVRELQARLEEAEqaal 1603
Cdd:pfam13166 366 SINDLVASINELIAKHNEITDNFEEEKNKAKKKL--RLHLVEEFKSEIDE---YKDKYAGLEKAINSLEKEIKNLE---- 436
|
170 180
....*....|....*....|.
gi 768017794 1604 rggkKQVQKLEAKVRELEAEL 1624
Cdd:pfam13166 437 ----AEIKKLREEIKELEAQL 453
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
660-1101 |
3.27e-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: 42.42 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 660 ALAAAEAKRQELEETHvsitQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLEDEEEVNADLAARRR 739
Cdd:pfam05557 32 LEKKASALKRQLDRES----DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 740 KLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQ---------------- 803
Cdd:pfam05557 108 CLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRikelefeiqsqeqdse 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 804 ALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKlTQESVADAAQDKQQLEEKLK--KK 881
Cdd:pfam05557 188 IVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEK-YREEAATLELEKEKLEQELQswVK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 882 DSELSQLSLRVEDEqllgaqMQKKIKELQARAEELEEELEAERAARARVEKQRAEAAREleelserleeaggasagqreg 961
Cdd:pfam05557 267 LAQDTGLNLRSPED------LSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQE--------------------- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 962 CRKREAELGRLRRELEeaalRHEATVAALRR------KQAEGAAELGEQVDS---LQRVRQKLEKEKSELRMEVDDLAAN 1032
Cdd:pfam05557 320 LAQYLKKIEDLNKKLK----RHKALVRRLQRrvllltKERDGYRAILESYDKeltMSNYSPQLLERIEEAEDMTQKMQAH 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768017794 1033 VETLTRAKASAEKLCRTYEDQLS--EAKIKVEELQRQLADASTQ-------RGRLQTESGELSRLLEEKECLISQLSR 1101
Cdd:pfam05557 396 NEEMEAQLSVAEEELGGYKQQAQtlERELQALRQQESLADPSYSkeevdslRRKLETLELERQRLREQKNELEMELER 473
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1570-1652 |
3.52e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.25 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1570 EQDTSAHLERMKKTLEQTVRELQARLEEAEQAA--LRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKherRVKE 1647
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALAEAQQqeLVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQ---KRKE 220
|
....*
gi 768017794 1648 LAYQA 1652
Cdd:PRK11448 221 ITDQA 225
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
775-1002 |
3.55e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 775 NLTEEMAALDESVARLTKEKKALQEAHQQALGDLQA--EEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRK 852
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 853 LEGDLKLTQESVADAAQDK--QQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARV 930
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEA 324
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768017794 931 EKQRAEAARELEELSErleeaggasaGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELG 1002
Cdd:COG3206 325 LQAREASLQAQLAQLE----------ARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVG 386
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
744-879 |
4.00e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 41.25 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 744 ECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKL 823
Cdd:COG4026 129 EYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKRL 208
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768017794 824 ----RLEQQVEDL-ECSLEQEKKLRMDTERAKrklEGDLKLTQESVadAAQDKQQLEEKLK 879
Cdd:COG4026 209 levfSLEELWKELfPEELPEEDFIYFATENLK---PGKIIVGQGYI--AAESKEDAEEWLK 264
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1358-1616 |
4.22e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1358 RIQLELSQVKA-EVDRKLAEKDEECANLRRNHQRAVESLQASldaetrarNEALRLKKKME---GDLNDLELQLGHAT-- 1431
Cdd:PRK04863 299 RRQLAAEQYRLvEMARELAELNEAESDLEQDYQAASDHLNLV--------QTALRQQEKIEryqADLEELEERLEEQNev 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1432 ------------RQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAE----------LEELRAA 1489
Cdd:PRK04863 371 veeadeqqeeneARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQLCGLPdltadnaedwLEEFQAK 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1490 LEQGERSRRLAEQ------------------------------------ELLEATERLNLLHSQNTGLLNQKKKLEADLA 1533
Cdd:PRK04863 451 EQEATEELLSLEQklsvaqaahsqfeqayqlvrkiagevsrseawdvarELLRRLREQRHLAEQLQQLRMRLSELEQRLR 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1534 QlsgeveEAAQER--REAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQaalrggkkQVQ 1611
Cdd:PRK04863 531 Q------QQRAERllAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQA--------RIQ 596
|
....*
gi 768017794 1612 KLEAK 1616
Cdd:PRK04863 597 RLAAR 601
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1288-1721 |
4.76e-03 |
|
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: 41.55 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1288 EALEALETLKRENKNLQEEISDLTDQVSLSG----KSIQELEKTKKALEGEKSEIQAALEEAEGALELEETKTLRIQlEL 1363
Cdd:pfam05701 32 QTVERRKLVELELEKVQEEIPEYKKQSEAAEaakaQVLEELESTKRLIEELKLNLERAQTEEAQAKQDSELAKLRVE-EM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1364 SQVKAEVDRKLAEkdEECANLRRNHQRAVESLQAsldaetrARNEALRLKKKMEGDLNDLELqlghATRQATEAQAATRL 1443
Cdd:pfam05701 111 EQGIADEASVAAK--AQLEVAKARHAAAVAELKS-------VKEELESLRKEYASLVSERDI----AIKRAEEAVSASKE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1444 MQAQLKEeqagrdeeqrLAAELHEQAQALER-RASLLAAELEELRAALEQGERSRRLaEQELLEATERLNLLHSQNTGLL 1522
Cdd:pfam05701 178 IEKTVEE----------LTIELIATKESLESaHAAHLEAEEHRIGAALAREQDKLNW-EKELKQAEEELQRLNQQLLSAK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1523 NQKKKLEADL-------AQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKE-QDTSAHLERMK---KTLEQTVREL 1591
Cdd:pfam05701 247 DLKSKLETASallldlkAELAAYMESKLKEEADGEGNEKKTSTSIQAALASAKKElEEVKANIEKAKdevNCLRVAAASL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1592 QARLEEaEQAALRGGKKQVQKLEAKVRELEAELDaeqkkhaealkgvrkheRRVKELAYQAEEDRKNLARMQDLVDKLQs 1671
Cdd:pfam05701 327 RSELEK-EKAELASLRQREGMASIAVSSLEAELN-----------------RTKSEIALVQAKEKEAREKMVELPKQLQ- 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 768017794 1672 kvksykrqfeEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRAR 1721
Cdd:pfam05701 388 ----------QAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESR 427
|
|
| COG4646 |
COG4646 |
Adenine-specific DNA methylase, N12 class [Replication, recombination and repair]; |
963-1637 |
4.83e-03 |
|
Adenine-specific DNA methylase, N12 class [Replication, recombination and repair];
Pssm-ID: 443684 [Multi-domain] Cd Length: 1711 Bit Score: 41.77 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 963 RKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKAS 1042
Cdd:COG4646 1005 RQEEILEEQIAEILKAIKELKAVVRKRFTVKQLESTKKLGAGKLKQLDLLALKDLDVPWEPLDVDQLFGRGSRQGNNNFL 1084
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1043 AEKLCRTYEDQLSEAKIKVEELQRQLA-DASTQRGRLQTESGELSRLLEEKECLISQLSRGKALAAQSLEELRRQLEEES 1121
Cdd:COG4646 1085 VTKMRNVAGLAFSDAAKLSDYFGKQRYrDELTAGKGVVVATGTDESNLMYELYTAQAYLQLLLLGKQGLTNFDTWASTLE 1164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1122 KAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKKKLALRLQEAE-- 1199
Cdd:COG4646 1165 ELVTAAELAPERTAYRANTREAKAVNLPEEDVMIKEAEDAKTADELLLPTPEKISGGVATKPSEVQKELLEELEERAAiv 1244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1200 -----EGVEAANAKCSSLEKAKLRLQTesEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQRESRG 1274
Cdd:COG4646 1245 rkndgEPDRDNMLVITDDGRKAALDQR--LDIKTLPDDEGSLVALCVTNIDRIWEDNPESKLTQLVFCDLSTPKGDGTFN 1322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1275 LGTELFRLRHGHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKTKKALEGEKSEIQAALEEAEGALELEET 1354
Cdd:COG4646 1323 DLEDIREKLIEEEIAELEIAFIHLALDDQEKAELFARDRLGAVEKLRISTAKMGAGTNVRLLLEATHDLDVPWRPRDAEQ 1402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1355 KTLRIQLELSQVKAEV----------DRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLE 1424
Cdd:COG4646 1403 RAGRGRRQGNENEEVEeiryvtentfDAYLWQAAETKQKFIAQIMTSKSPVRSLEDVDEAALSYAERKALAAGRPKEKEK 1482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1425 LQLGHATRQATEAQAATR----LMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLA 1500
Cdd:COG4646 1483 MDLDIEVLKLKLLDAAALeqlyAEEDKLRKSYLDEEEALEERIEAATKDLRLARAASQEEADEQESASKEAAAGEKKAAA 1562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1501 EQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAkkaitdAAMMAEELKKEQDTSAHLERM 1580
Cdd:COG4646 1563 AELLAALQAAGLIVLDGGRTPRGEKGGGLLARALLEAATLLLPIEEAEGSEGA------DATGDRRTGAAAEIELAAEAL 1636
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 768017794 1581 KKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKG 1637
Cdd:COG4646 1637 ILNLAERLERALRDGAEEEEIAPRELEAALKEEAALLARAGELAELELDKADLEAEL 1693
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1479-1557 |
5.11e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.86 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1479 LAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQE----RREAEEKAK 1554
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQErkqkRKEITDQAA 226
|
...
gi 768017794 1555 KAI 1557
Cdd:PRK11448 227 KRL 229
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1482-1615 |
5.17e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1482 ELEELRAALEQgerSRRLAEQELLEATErlnllhsqntgLLNQKKKLEADLAQLSGEVEEA-AQERREAEEKAKKAITDA 1560
Cdd:PRK00409 517 KLNELIASLEE---LERELEQKAEEAEA-----------LLKEAEKLKEELEEKKEKLQEEeDKLLEEAEKEAQQAIKEA 582
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 768017794 1561 AMMAEELKKEQDTsahLERMKKTL--EQTVRELQARLEEAEQAALRGGKKQVQKLEA 1615
Cdd:PRK00409 583 KKEADEIIKELRQ---LQKGGYASvkAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
966-1128 |
5.46e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 966 EAELGRLRRELEEAALRHEATVAALRRKQAEgAAELGEQVDSLQrvrQKLEKEKSELRMEV------------------- 1026
Cdd:COG3883 36 QAELDALQAELEELNEEYNELQAELEALQAE-IDKLQAEIAEAE---AEIEERREELGERAralyrsggsvsyldvllgs 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1027 ---DDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLSRGK 1103
Cdd:COG3883 112 esfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191
|
170 180
....*....|....*....|....*
gi 768017794 1104 ALAAQSLEELRRQLEEESKAKSALA 1128
Cdd:COG3883 192 AAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1420-1561 |
5.51e-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: 40.29 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1420 LNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERR-----ASLLAA----ELEELRAAL 1490
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyeEQLGNVrnnkEYEALQKEI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768017794 1491 EQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAA 1561
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1526-1700 |
6.03e-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: 39.55 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1526 KKLEADLAQLSGEVEEAAQERREAEEKAKKAITdAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRG 1605
Cdd:pfam01442 7 DELSTYAEELQEQLGPVAQELVDRLEKETEALR-ERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEELRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1606 GKKQVQKLEAKVRELEAELDAEQKKHAEALKGVrkherrvkeLAYQAEEDRKNLA-RMQDLVDKLQSKVKSYKRQFEEAE 1684
Cdd:pfam01442 86 LNADAEELQEKLAPYGEELRERLEQNVDALRAR---------LAPYAEELRQKLAeRLEELKESLAPYAEEVQAQLSQRL 156
|
170
....*....|....*.
gi 768017794 1685 QQANTNLAKYRKAQHE 1700
Cdd:pfam01442 157 QELREKLEPQAEDLRE 172
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1295-1724 |
7.38e-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: 41.20 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1295 TLKRENKNLQEEISDLTdqvslsgKSIQELEKTKKALEGEKSeiqaaleeaegaleleetktlriqlelsqvKAEVDRKL 1374
Cdd:pfam13166 86 TLGEESIEIQEKIAKLK-------KEIKDHEEKLDAAEANLQ------------------------------KLDKEKEK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1375 AEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDlelqlghatrqateaqAATRLMQAQLKEEQAG 1454
Cdd:pfam13166 129 LEADFLDECWKKIKRKKNSALSEALNGFKYEANFKSRLLREIEKDNFN----------------AGVLLSDEDRKAALAT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1455 RDEEQR----------LAAELHEQAQALERRASLLAAELEELRaaleqgersRRLAEQELLEATERLNLLHSQNTGLLNQ 1524
Cdd:pfam13166 193 VFSDNKpeiapltfnvIDFDALEKAEILIQKVIGKSSAIEELI---------KNPDLADWVEQGLELHKAHLDTCPFCGQ 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1525 ------KKKLEadlAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEA 1598
Cdd:pfam13166 264 plpaerKAALE---AHFDDEFTEFQNRLQKLIEKVESAISSLLAQLPAVSDLASLLSAFELDVEDIESEAEVLNSQLDGL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1599 EQAALRGGKKQVQKLEAKVreLEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARmqDLVDKLQSKVKSYKR 1678
Cdd:pfam13166 341 RRALEAKRKDPFKSIELDS--VDAKIESINDLVASINELIAKHNEITDNFEEEKNKAKKKLRL--HLVEEFKSEIDEYKD 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 768017794 1679 QFEEAEQQANtnlakyrKAQHELDDAEERADMAETQANKLRARTRD 1724
Cdd:pfam13166 417 KYAGLEKAIN-------SLEKEIKNLEAEIKKLREEIKELEAQLRD 455
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
713-910 |
7.42e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 713 LEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDI----DDLELTLAKAEKEKQATENKVKNLTEEMAALDESVA 788
Cdd:PHA02562 193 IQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIkaeiEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 789 RLTKEKKALQEAHQ--QALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKlRMDterakrklegdlkltqeSVAD 866
Cdd:PHA02562 273 QFQKVIKMYEKGGVcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEE-IMD-----------------EFNE 334
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 768017794 867 AAQDKQQLEEKLKKKDSELSQLSLRVEDeqllgaqMQKKIKELQ 910
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLITLVDKAKK-------VKAAIEELQ 371
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
645-879 |
8.12e-03 |
|
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: 40.82 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 645 EELAALRAELRGLRGALAAAEA--------KRQELEETHVSITQEKNDLALQLQAE-QDN------LADAEERchlLIKS 709
Cdd:pfam15070 53 QELETSLAELKNQAAVPPAEEEqppagpseEEQRLQEEAEQLQKELEALAGQLQAQvQDNeqlsrlNQEQEQR---LLEL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 710 KVQLEGKVKELSERLEDEEEVNADLA------ARRRKLEDECTEL-----KKDIDDLELTLA-KAEKE-KQATENKVKNL 776
Cdd:pfam15070 130 ERAAERWGEQAEDRKQILEDMQSDRAtisralSQNRELKEQLAELqngfvKLTNENMELTSAlQSEQHvKKELAKKLGQL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 777 TEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVedlecsLEQEKKL-RMDTERAKRKLEG 855
Cdd:pfam15070 210 QEELGELKETLELKSQEAQSLQEQRDQYLAHLQQYVAAYQQLASEKEELHKQY------LLQTQLMdRLQHEEVQGKVAA 283
|
250 260
....*....|....*....|....*....
gi 768017794 856 D-----LKLTQESVADAAQDKQQLEEKLK 879
Cdd:pfam15070 284 EmarqeLQETQERLEALTQQNQQLQAQLS 312
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
669-1031 |
8.37e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 669 QELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLEDEEEVNADLAARRRKLEDECTEL 748
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 749 KKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQ 828
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 829 VEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADAAQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKE 908
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 909 LQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAALRHEATVA 988
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 768017794 989 ALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAA 1031
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
717-1103 |
8.43e-03 |
|
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: 40.77 E-value: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 717 VKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEK----------QATENKVKNLTEEMAALDES 786
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLlklelllsnlKKKIQKNKSLESQISELKKQ 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 787 VARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLK-LTQESVA 865
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdLNNQKEQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 866 DAAQD-KQQLEEKLKKKDSELSQLSLRVEDEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQRAEaareleel 944
Cdd:TIGR04523 307 DWNKElKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE-------- 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 945 serleeaggaSAGQREGCRKREAELGRLRRELEeaalrheatvaalrrKQAEGAAELGEQVDSLQRVRQKLEKEKSELRM 1024
Cdd:TIGR04523 379 ----------NQSYKQEIKNLESQINDLESKIQ---------------NQEKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768017794 1025 EVDDLAANVETLTRAKASAEKlcrtyedQLSEAKIKVEELQRQLADASTQRGRLQTESGELSRLLEEKECLISQLSRGK 1103
Cdd:TIGR04523 434 TIIKNNSEIKDLTNQDSVKEL-------IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1528-1621 |
8.52e-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: 40.25 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1528 LEADLAQLSGEVE-EAAQERREAEEKAKKAITDAAMMAEELKKEQDTS--AHLERMKKTLEQTVRELQARLEEA------ 1598
Cdd:cd16269 187 LQADQALTEKEKEiEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSyeEHLRQLKEKMEEERENLLKEQERAlesklk 266
|
90 100
....*....|....*....|....*
gi 768017794 1599 EQAAL--RGGKKQVQKLEAKVRELE 1621
Cdd:cd16269 267 EQEALleEGFKEQAELLQEEIRSLK 291
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1439-1725 |
8.59e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1439 AATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQN 1518
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1519 TGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEA 1598
Cdd:COG4372 104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1599 EQAALRggkkqvqkLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKR 1678
Cdd:COG4372 184 ALDELL--------KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 768017794 1679 QFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDA 1725
Cdd:COG4372 256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLL 302
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
856-1045 |
8.65e-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: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 856 DLKLTQESVADAAQDKQQLEEkLKKKDSELSQLSLRVE--DEQLLGAQMQKKIKELQARAEELEEELEAERAARARVEKQ 933
Cdd:COG4913 236 DLERAHEALEDAREQIELLEP-IRELAERYAAARERLAelEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 934 RAEAARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQ 1013
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE 394
|
170 180 190
....*....|....*....|....*....|..
gi 768017794 1014 KLEKEKSELRMEVDDLAANVETLTRAKASAEK 1045
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1445-1596 |
8.67e-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: 40.43 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1445 QAQLKEEQAgRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGErsrrlaeQELLEATERLNLLHSQNTGLLNQ 1524
Cdd:cd22656 107 TDDEELEEA-KKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQ-------TALETLEKALKDLLTDEGGAIAR 178
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768017794 1525 K--KKLEADLAQLSgevEEAAQERREAEEKAKKAITDAammAEELKKEQDTSAHLERMKKTLEQTVRELQARLE 1596
Cdd:cd22656 179 KeiKDLQKELEKLN---EEYAAKLKAKIDELKALIADD---EAKLAAALRLIADLTAADTDLDNLLALIGPAIP 246
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
644-803 |
9.08e-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: 40.65 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 644 EEELAALRAELRGLRGALAAAEAKRQELEETHVSITQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSER 723
Cdd:pfam07888 79 ESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKER 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 724 LEDeeevnadLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEkkaLQEAHQQ 803
Cdd:pfam07888 159 AKK-------AGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQK---LTTAHRK 228
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1523-1731 |
9.11e-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: 40.21 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1523 NQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAA 1602
Cdd:TIGR02794 61 PAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1603 LRggkKQVQKLEAKvreleAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEE 1682
Cdd:TIGR02794 141 ER---KAKEEAAKQ-----AEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAK 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 768017794 1683 AEQQANTNLAKYRKAQHELDDAEERADMA-ETQANKLRARTRDALGPKLS 1731
Cdd:TIGR02794 213 AEAEAAAAAAAEAERKADEAELGDIFGLAsGSNAEKQGGARGAAAGSEVD 262
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1358-1492 |
9.23e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 40.42 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1358 RIQLELSQVKAEVDRKLAEKDEECANLRRNHQRA-----VESLQASLDaetRARNEALRLKKKMEGDL---NDLElqlgH 1429
Cdd:COG1566 80 DLQAALAQAEAQLAAAEAQLARLEAELGAEAEIAaaeaqLAAAQAQLD---LAQRELERYQALYKKGAvsqQELD----E 152
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768017794 1430 ATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQAlerrasllAAELEELRAALEQ 1492
Cdd:COG1566 153 ARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQA--------EAALAQAELNLAR 207
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
664-869 |
9.55e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 664 AEAKRQELEETHVSITQEKNdlalqlqaeqdnlADAEErchllIKSKVQLEGKVKELSERLEDEEEVNAdlaaRRRKLED 743
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAK-------------KEAEA-----IKKEALLEAKEEIHKLRNEFEKELRE----RRNELQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 744 ECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDesvarltKEKKALQEAHQQALGDLQaeedRVSALTKAKL 823
Cdd:PRK12704 87 LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE-------KKEEELEELIEEQLQELE----RISGLTAEEA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 768017794 824 RlEQQVEDLECSLEQEKKLRMDTERAKRKLEGDlKLTQESVADAAQ 869
Cdd:PRK12704 156 K-EILLEKVEEEARHEAAVLIKEIEEEAKEEAD-KKAKEILAQAIQ 199
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1358-1685 |
9.69e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1358 RIQLELSQVKAEVDRKLAEKDEECANLRRNhQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEA 1437
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQA-RSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1438 QAATRLMQAQLKEEQAGRDEEQRLAAELHEQAQALERRASLLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQ 1517
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1518 NTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEE 1597
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017794 1598 AEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYK 1677
Cdd:COG4372 281 AALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLS 360
|
....*...
gi 768017794 1678 RQFEEAEQ 1685
Cdd:COG4372 361 KGAEAGVA 368
|
|
| |
