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Conserved domains on  [gi|568961011|ref|XP_006511002|]
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unconventional myosin-Vc isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
81-741 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: 1207.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFAESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01380     1 PAVLHNLKVRFCQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  161 GESGAGKTVSARYAMRYFATVSKSSSN-AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRT 239
Cdd:cd01380    81 GESGAGKTVSAKYAMRYFATVGGSSSGeTQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDF 319
Cdd:cd01380   161 YLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  320 QMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARD 399
Cdd:cd01380   241 QMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  400 ALAKKIYAHLFDFIVEQINQALHF--SGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMK 477
Cdd:cd01380   321 ALAKHIYAQLFDWIVDRINKALASpvKEKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVK 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  478 EDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNK-NSLFEKPRMSNSSFIIQHFADKVE 556
Cdd:cd01380   401 EEIEWSFIDFYDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTAFIVKHFADDVE 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  557 YQCEGFLEKNRDTVYDMLVEILRASKFHlcaaffqespvpsspfgamitvksakqviKPntkhfrtTVGNKFRSSLYLLM 636
Cdd:cd01380   481 YQVEGFLEKNRDTVSEEHLNVLKASKNR-----------------------------KK-------TVGSQFRDSLILLM 524
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  637 ETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSDKKEV 716
Cdd:cd01380   525 ETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLRDDKKKT 604
                         650       660
                  ....*....|....*....|....*
gi 568961011  717 CKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd01380   605 CENILENLILDPDKYQFGKTKIFFR 629
Smc super family cl34174
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
848-1155 6.34e-15

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 80.14  E-value: 6.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  848 RRYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNiQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAalrvgdlEKVQ 927
Cdd:COG1196   213 ERYQELKAELRELELALLLAKLKELRKELEELEEELS-RLEEELEELQEELEEAEKEIEELKSELEELR-------EELE 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  928 KLEAELEKAATHRHSYEEKGRRYRDTVEE---RLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTrqLFDDVQKE 1004
Cdd:COG1196   285 ELQEELLELKEEIEELEGEISLLRERLEElenELEELEERLEELKEKIEALKEELEERETLLEELEQLLA--ELEEAKEE 362
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1005 EQQRL-VLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQA 1083
Cdd:COG1196   363 LEEKLsALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELE 442
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568961011 1084 QKIDVEKHVQSQKREMRERMSEVTKQLLE-SYDIEDVRSRLSvEDLEHLNEDGELWFAYEGLKKATRVLESHF 1155
Cdd:COG1196   443 ELNEELEELEEQLEELRDRLKELERELAElQEELQRLEKELS-SLEARLDRLEAEQRASQGVRAVLEALESGL 514
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
831-851 3.54e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


:

Pssm-ID: 425778  Cd Length: 21  Bit Score: 35.76  E-value: 3.54e-03
                           10        20
                   ....*....|....*....|.
gi 568961011   831 RVATITIQAHTRGFLARRRYR 851
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21
 
Name Accession Description Interval E-value
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
81-741 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: 1207.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFAESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01380     1 PAVLHNLKVRFCQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  161 GESGAGKTVSARYAMRYFATVSKSSSN-AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRT 239
Cdd:cd01380    81 GESGAGKTVSAKYAMRYFATVGGSSSGeTQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDF 319
Cdd:cd01380   161 YLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  320 QMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARD 399
Cdd:cd01380   241 QMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  400 ALAKKIYAHLFDFIVEQINQALHF--SGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMK 477
Cdd:cd01380   321 ALAKHIYAQLFDWIVDRINKALASpvKEKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVK 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  478 EDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNK-NSLFEKPRMSNSSFIIQHFADKVE 556
Cdd:cd01380   401 EEIEWSFIDFYDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTAFIVKHFADDVE 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  557 YQCEGFLEKNRDTVYDMLVEILRASKFHlcaaffqespvpsspfgamitvksakqviKPntkhfrtTVGNKFRSSLYLLM 636
Cdd:cd01380   481 YQVEGFLEKNRDTVSEEHLNVLKASKNR-----------------------------KK-------TVGSQFRDSLILLM 524
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  637 ETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSDKKEV 716
Cdd:cd01380   525 ETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLRDDKKKT 604
                         650       660
                  ....*....|....*....|....*
gi 568961011  717 CKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd01380   605 CENILENLILDPDKYQFGKTKIFFR 629
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
62-752 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: 963.16  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011     62 NPDILVGENDLTALSYLHEPAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVA 141
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRY-LKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIA 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011    142 EEAYKQMARNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNA-HVEDKVLASNPITEAVGNAKTTRNDNSSRFGK 220
Cdd:smart00242   80 DNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVgSVEDQILESNPILEAFGNAKTLRNNNSSRFGK 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011    221 YTEISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDR 300
Cdd:smart00242  160 FIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDA 239
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011    301 ADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNE-RSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIV 379
Cdd:smart00242  240 EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDnAASTVKDKEELSNAAELLGVDPEELEKALTKRKIK 319
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011    380 TSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKL 459
Cdd:smart00242  320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEKL 399
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011    460 QQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNKNSLFEK 538
Cdd:smart00242  400 QQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKpPGILSLLDEECRFPKGTDQTFLEKLNQHH-KKHPHFSK 478
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011    539 P-RMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESpvpsspfgamitVKSAKQVIKPnt 617
Cdd:smart00242  479 PkKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG------------VSNAGSKKRF-- 544
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011    618 khfrTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYS 697
Cdd:smart00242  545 ----QTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQ 620
                           650       660       670       680       690
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 568961011    698 RYGILMTQQELSLS-DKKEVCKVVLHRLIQDSNQYQFGRTKIFFRAGQVAYLEKLR 752
Cdd:smart00242  621 RYRVLLPDTWPPWGgDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELR 676
Myosin_head pfam00063
Myosin head (motor domain);
70-741 0e+00

Myosin head (motor domain);


Pssm-ID: 395017  Cd Length: 674  Bit Score: 916.67  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011    70 NDLTALSYLHEPAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMA 149
Cdd:pfam00063    2 EDMVELSYLNEPSVLHNLKKRYK-SDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   150 RNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSSSN---AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISF 226
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAgnvGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   227 DERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVET 306
Cdd:pfam00063  161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKIT 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   307 QKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVV 386
Cdd:pfam00063  241 DKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETVS 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   387 KPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHF-SGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNL 465
Cdd:pfam00063  321 KPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVkTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFNH 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   466 HVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNKNSLFEKPR-MSN 543
Cdd:pfam00063  401 HMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKpLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHFQKPRlQGE 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   544 SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvKSAKQVIKPNTKHFRTT 623
Cdd:pfam00063  480 THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAAN----ESGKSTPKRTKKKRFIT 555
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   624 VGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM 703
Cdd:pfam00063  556 VGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILA 635
                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 568961011   704 TQ-QELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:pfam00063  636 PKtWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
COG5022 COG5022
Myosin heavy chain [General function prediction only];
12-1181 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 908.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   12 RVWIPDPEEVWKSAEIAK-DYRAGDRVLRLLLEDGmELEyPVDPGSLPPLR-NPDILVGENDLTALSYLHEPAVLHNLRI 89
Cdd:COG5022    11 GCWIPDEEKGWIWAEIIKeAFNKGKVTEEGKKEDG-ESV-SVKKKVLGNDRiKLPKFDGVDDLTELSYLNEPAVLHNLEK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   90 RFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGESGAGKTV 169
Cdd:COG5022    89 RY-NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  170 SARYAMRYFATVSKSSSN--AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLLEKSRV 247
Cdd:COG5022   168 NAKRIMQYLASVTSSSTVeiSSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRV 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  248 VFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKIL 327
Cdd:COG5022   248 VHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKIL 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  328 AAILHLGNVQVTTVGNERSSVSeDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYA 407
Cdd:COG5022   328 AAILHIGNIEFKEDRNGAAIFS-DNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYS 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  408 HLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDF 487
Cdd:COG5022   407 NLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY 486
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  488 YDNQPVIDLIEAK--MGILELLDEECLLPHGTDENWLQKLYNNF-VNKNSLFEKPRMSNSSFIIQHFADKVEYQCEGFLE 564
Cdd:COG5022   487 FDNQPCIDLIEKKnpLGILSLLDEECVMPHATDESFTSKLAQRLnKNSNPKFKKSRFRDNKFVVKHYAGDVEYDVEGFLD 566
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  565 KNRDTVYDMLVEILRASKFHLCAAFFQEspvpsspfgamiTVKSAKQVIKPntkhfrtTVGNKFRSSLYLLMETLNATTP 644
Cdd:COG5022   567 KNKDPLNDDLLELLKASTNEFVSTLFDD------------EENIESKGRFP-------TLGSRFKESLNSLMSTLNSTQP 627
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  645 HYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM-----TQQELSLSDKKEVCKV 719
Cdd:COG5022   628 HYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSpskswTGEYTWKEDTKNAVKS 707
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  720 VLHRLIQDSNQYQFGRTKIFFRAGQVAYLEKLRLDKLRQDCIMIQKHVRGWLQRRKFLRERQAALTIQRYFRGQQTVR-- 797
Cdd:COG5022   708 ILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRlv 787
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  798 ----KAITATALKEAWAAIILQKYCRGYLvrnlyQLIRVATITIqahTRGFLARRRYRKLLQEHKAVILQKYARAWLARR 873
Cdd:COG5022   788 dyelKWRLFIKLQPLLSLLGSRKEYRSYL-----ACIIKLQKTI---KREKKLRETEEVEFSLKAEVLIQKFGRSLKAKK 859
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  874 RFQNIRRFVLNIQLTYRVQRLQKKLEDQNREnhglVEKLTSLAALRVGD----LEKVQKLEAELEKAATHRH---SYEEK 946
Cdd:COG5022   860 RFSLLKKETIYLQSAQRVELAERQLQELKID----VKSISSLKLVNLELeseiIELKKSLSSDLIENLEFKTeliARLKK 935
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  947 GRRYRDTVEERLSKLQKHNAELELQRERAEqmLQEKSEELKEKMDKLTrQLFDDVQKEEQQRlvleKGFELKTQAYEKQI 1026
Cdd:COG5022   936 LLNNIDLEEGPSIEYVKLPELNKLHEVESK--LKETSEEYEDLLKKST-ILVREGNKANSEL----KNFKKELAELSKQY 1008
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1027 ESLREEIKALKDERSQL-HHQLEEGQVTSDRlkGEVARLSKQAKTISEFEKEIELLQAQKIDVekhvqSQKREMRERMSe 1105
Cdd:COG5022  1009 GALQESTKQLKELPVEVaELQSASKIISSES--TELSILKPLQKLKGLLLLENNQLQARYKAL-----KLRRENSLLDD- 1080
                        1130      1140      1150      1160      1170      1180      1190
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568961011 1106 vtkqlLESYDIEDVRSRLSVedlehLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEIN 1181
Cdd:COG5022  1081 -----KQLYQLESTENLLKT-----INVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVF 1146
PTZ00014 PTZ00014
myosin-A; Provisional
71-791 1.67e-146

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 464.12  E-value: 1.67e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   71 DLTALSYLHEPAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAY-SGQNMGDMDPHIFAVAEEAYKQMA 149
Cdd:PTZ00014  100 DIGLLPHTNIPCVLDFLKHRY-LKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYrDAKDSDKLPPHVFTTARRALENLH 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  150 RNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDER 229
Cdd:PTZ00014  179 GVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEE 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  230 NQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYtrMGGNTV-IEGVNDRADMVETQK 308
Cdd:PTZ00014  259 GGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKY--INPKCLdVPGIDDVKDFEEVME 336
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTtvGNERSSVSE----DDSHLKVF---CELLGLETSKVAQWLCNRKIVTS 381
Cdd:PTZ00014  337 SFDSMGLSESQIEDIFSILSGVLLLGNVEIE--GKEEGGLTDaaaiSDESLEVFneaCELLFLDYESLKKELTVKVTYAG 414
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  382 SETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQ 461
Cdd:PTZ00014  415 NQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQK 494
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  462 QFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR 540
Cdd:PTZ00014  495 NFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGkSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKV 574
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  541 MSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGamitvksAKQVIkpntkhf 620
Cdd:PTZ00014  575 DSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKGKLA-------KGQLI------- 640
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  621 rttvGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYG 700
Cdd:PTZ00014  641 ----GSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFK 716
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  701 ILmtqqELSLS-----DKKEVCKVVLHRLIQDSNQYQFGRTKIFFR---AGQVAYLEKLRLDKLRQDCIMIQKHVRGWLQ 772
Cdd:PTZ00014  717 YL----DLAVSndsslDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKK 792
                         730
                  ....*....|....*....
gi 568961011  773 RRKFLRERQAALTIQRYFR 791
Cdd:PTZ00014  793 KRKVRKNIKSLVRIQAHLR 811
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
848-1155 6.34e-15

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 80.14  E-value: 6.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  848 RRYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNiQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAalrvgdlEKVQ 927
Cdd:COG1196   213 ERYQELKAELRELELALLLAKLKELRKELEELEEELS-RLEEELEELQEELEEAEKEIEELKSELEELR-------EELE 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  928 KLEAELEKAATHRHSYEEKGRRYRDTVEE---RLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTrqLFDDVQKE 1004
Cdd:COG1196   285 ELQEELLELKEEIEELEGEISLLRERLEElenELEELEERLEELKEKIEALKEELEERETLLEELEQLLA--ELEEAKEE 362
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1005 EQQRL-VLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQA 1083
Cdd:COG1196   363 LEEKLsALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELE 442
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568961011 1084 QKIDVEKHVQSQKREMRERMSEVTKQLLE-SYDIEDVRSRLSvEDLEHLNEDGELWFAYEGLKKATRVLESHF 1155
Cdd:COG1196   443 ELNEELEELEEQLEELRDRLKELERELAElQEELQRLEKELS-SLEARLDRLEAEQRASQGVRAVLEALESGL 514
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
890-1207 2.23e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 71.63  E-value: 2.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  890 RVQRLQKKLEDQNRENHGLVEKLTSLAALR--VGDLEK---------VQKLEAELEKAATHRHSYEEKgrryRDTVEERL 958
Cdd:PRK03918  339 RLEELKKKLKELEKRLEELEERHELYEEAKakKEELERlkkrltgltPEKLEKELEELEKAKEEIEEE----ISKITARI 414
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  959 SKLQKHNAEL-------------------ELQRERAEQMLQEKSEELK------EKMDKLTRQLFDDVQKEEQQRLVLEK 1013
Cdd:PRK03918  415 GELKKEIKELkkaieelkkakgkcpvcgrELTEEHRKELLEEYTAELKriekelKEIEEKERKLRKELRELEKVLKKESE 494
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1014 GFELKTQAyeKQIESLREEIKALKDErsqlhhQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKhvq 1093
Cdd:PRK03918  495 LIKLKELA--EQLKELEEKLKKYNLE------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK--- 563
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1094 sQKREMRERMSEVTKQLLES--YDIEDVRSRLsvEDLEhlnedgELWFAYEGLKKATRVLESHFQSQKDCYE------KE 1165
Cdd:PRK03918  564 -KLDELEEELAELLKELEELgfESVEELEERL--KELE------PFYNEYLELKDAEKELEREEKELKKLEEeldkafEE 634
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 568961011 1166 IEGLNFKVVHLSQEINHLQKLFREETdiNESIRHEVTRLTSE 1207
Cdd:PRK03918  635 LAETEKRLEELRKELEELEKKYSEEE--YEELREEYLELSRE 674
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
893-1207 4.18e-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: 70.86  E-value: 4.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   893 RLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVE---ERLSKLQKHNAELE 969
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleERIAQLSKELTELE 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   970 LQRERAEQMLQEKSEELKEkmdkltrqlfDDVQKEEQQRLVlekgfelktQAYEKQIESLREEIKALKDERSQLHhqlEE 1049
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAE----------AEAEIEELEAQI---------EQLKEELKALREALDELRAELTLLN---EE 818
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1050 GQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEkHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVEDLE 1129
Cdd:TIGR02168  819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA-AEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1130 HLNEDGElwfAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEIN--------HLQKLFREETDINESIRHEV 1201
Cdd:TIGR02168  898 ELSEELR---ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeeysltleEAEALENKIEDDEEEARRRL 974

                   ....*.
gi 568961011  1202 TRLTSE 1207
Cdd:TIGR02168  975 KRLENK 980
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
849-1136 2.80e-11

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 435022 [Multi-domain]  Cd Length: 1112  Bit Score: 68.20  E-value: 2.80e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   849 RYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNIQLTYRVQR--LQKKLEDQNRENHGLVEKLTSLAALRVGDLEKV 926
Cdd:pfam15921  268 RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNsmYMRQLSDLESTVSQLRSELREAKRMYEDKIEEL 347
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   927 QK----LEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQmLQEKSEELKEKMDKLTRQLfDDVQ 1002
Cdd:pfam15921  348 EKqlvlANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKR-LWDRDTGNSITIDHLRREL-DDRN 425
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1003 KEEQQRLVLEKGFELKTQA-YEKQIESLREEIKALkDERSQLHHQLEEgqvTSDRLKGEVARLSKQAKTISEFEKEIEll 1081
Cdd:pfam15921  426 MEVQRLEALLKAMKSECQGqMERQMAAIQGKNESL-EKVSSLTAQLES---TKEMLRKVVEELTAKKMTLESSERTVS-- 499
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568961011  1082 qaqkiDVEKHVQSQKREMRERMSEVTKqllesydiedVRSR--LSVEDLEHLNEDGE 1136
Cdd:pfam15921  500 -----DLTASLQEKERAIEATNAEITK----------LRSRvdLKLQELQHLKNEGD 541
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
960-1131 1.00e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 45.78  E-value: 1.00e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011    960 KLQKHNAELELQRERAEQMLQEkSEELKEKMDKLtrqlfDDVQKEEQQRLVlekgfelktqAYEKQIESLREEIKALKDE 1039
Cdd:smart00787  120 QLVKTFARLEAKKMWYEWRMKL-LEGLKEGLDEN-----LEGLKEDYKLLM----------KELELLNSIKPKLRDRKDA 183
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   1040 RSQLHHQLEEG-----QVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQS---QKREMRERMSEVTKQLL 1111
Cdd:smart00787  184 LEEELRQLKQLedeleDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDltnKKSELNTEIAEAEKKLE 263
                           170       180
                    ....*....|....*....|...
gi 568961011   1112 ES--YDIEDVRS-RLSVEDLEHL 1131
Cdd:smart00787  264 QCrgFTFKEIEKlKEQLKLLQSL 286
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
929-1030 1.54e-04

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: 45.26  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  929 LEAELEKAATHRHSYEEKGRRyrdTVEERLSK-LQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLFDD-----VQ 1002
Cdd:cd16269   187 LQADQALTEKEKEIEAERAKA---EAAEQERKlLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEqeralES 263
                          90       100
                  ....*....|....*....|....*...
gi 568961011 1003 KEEQQRLVLEKGFELKTQAYEKQIESLR 1030
Cdd:cd16269   264 KLKEQEALLEEGFKEQAELLQEEIRSLK 291
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
831-851 3.54e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 425778  Cd Length: 21  Bit Score: 35.76  E-value: 3.54e-03
                           10        20
                   ....*....|....*....|.
gi 568961011   831 RVATITIQAHTRGFLARRRYR 851
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
830-851 3.99e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 35.76  E-value: 3.99e-03
                            10        20
                    ....*....|....*....|..
gi 568961011    830 IRVATITIQAHTRGFLARRRYR 851
Cdd:smart00015    2 LTRAAIIIQAAWRGYLARKRYK 23
 
Name Accession Description Interval E-value
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
81-741 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: 1207.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFAESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01380     1 PAVLHNLKVRFCQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  161 GESGAGKTVSARYAMRYFATVSKSSSN-AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRT 239
Cdd:cd01380    81 GESGAGKTVSAKYAMRYFATVGGSSSGeTQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDF 319
Cdd:cd01380   161 YLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  320 QMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARD 399
Cdd:cd01380   241 QMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  400 ALAKKIYAHLFDFIVEQINQALHF--SGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMK 477
Cdd:cd01380   321 ALAKHIYAQLFDWIVDRINKALASpvKEKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVK 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  478 EDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNK-NSLFEKPRMSNSSFIIQHFADKVE 556
Cdd:cd01380   401 EEIEWSFIDFYDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTAFIVKHFADDVE 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  557 YQCEGFLEKNRDTVYDMLVEILRASKFHlcaaffqespvpsspfgamitvksakqviKPntkhfrtTVGNKFRSSLYLLM 636
Cdd:cd01380   481 YQVEGFLEKNRDTVSEEHLNVLKASKNR-----------------------------KK-------TVGSQFRDSLILLM 524
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  637 ETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSDKKEV 716
Cdd:cd01380   525 ETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLRDDKKKT 604
                         650       660
                  ....*....|....*....|....*
gi 568961011  717 CKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd01380   605 CENILENLILDPDKYQFGKTKIFFR 629
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
62-752 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: 963.16  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011     62 NPDILVGENDLTALSYLHEPAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVA 141
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRY-LKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIA 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011    142 EEAYKQMARNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNA-HVEDKVLASNPITEAVGNAKTTRNDNSSRFGK 220
Cdd:smart00242   80 DNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVgSVEDQILESNPILEAFGNAKTLRNNNSSRFGK 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011    221 YTEISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDR 300
Cdd:smart00242  160 FIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDA 239
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011    301 ADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNE-RSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIV 379
Cdd:smart00242  240 EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDnAASTVKDKEELSNAAELLGVDPEELEKALTKRKIK 319
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011    380 TSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKL 459
Cdd:smart00242  320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEKL 399
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011    460 QQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNKNSLFEK 538
Cdd:smart00242  400 QQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKpPGILSLLDEECRFPKGTDQTFLEKLNQHH-KKHPHFSK 478
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011    539 P-RMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESpvpsspfgamitVKSAKQVIKPnt 617
Cdd:smart00242  479 PkKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG------------VSNAGSKKRF-- 544
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011    618 khfrTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYS 697
Cdd:smart00242  545 ----QTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQ 620
                           650       660       670       680       690
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 568961011    698 RYGILMTQQELSLS-DKKEVCKVVLHRLIQDSNQYQFGRTKIFFRAGQVAYLEKLR 752
Cdd:smart00242  621 RYRVLLPDTWPPWGgDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELR 676
Myosin_head pfam00063
Myosin head (motor domain);
70-741 0e+00

Myosin head (motor domain);


Pssm-ID: 395017  Cd Length: 674  Bit Score: 916.67  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011    70 NDLTALSYLHEPAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMA 149
Cdd:pfam00063    2 EDMVELSYLNEPSVLHNLKKRYK-SDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   150 RNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSSSN---AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISF 226
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAgnvGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   227 DERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVET 306
Cdd:pfam00063  161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKIT 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   307 QKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVV 386
Cdd:pfam00063  241 DKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETVS 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   387 KPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHF-SGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNL 465
Cdd:pfam00063  321 KPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVkTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFNH 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   466 HVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNKNSLFEKPR-MSN 543
Cdd:pfam00063  401 HMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKpLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHFQKPRlQGE 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   544 SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvKSAKQVIKPNTKHFRTT 623
Cdd:pfam00063  480 THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAAN----ESGKSTPKRTKKKRFIT 555
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   624 VGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM 703
Cdd:pfam00063  556 VGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILA 635
                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 568961011   704 TQ-QELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:pfam00063  636 PKtWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
COG5022 COG5022
Myosin heavy chain [General function prediction only];
12-1181 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 908.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   12 RVWIPDPEEVWKSAEIAK-DYRAGDRVLRLLLEDGmELEyPVDPGSLPPLR-NPDILVGENDLTALSYLHEPAVLHNLRI 89
Cdd:COG5022    11 GCWIPDEEKGWIWAEIIKeAFNKGKVTEEGKKEDG-ESV-SVKKKVLGNDRiKLPKFDGVDDLTELSYLNEPAVLHNLEK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   90 RFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGESGAGKTV 169
Cdd:COG5022    89 RY-NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  170 SARYAMRYFATVSKSSSN--AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLLEKSRV 247
Cdd:COG5022   168 NAKRIMQYLASVTSSSTVeiSSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRV 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  248 VFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKIL 327
Cdd:COG5022   248 VHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKIL 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  328 AAILHLGNVQVTTVGNERSSVSeDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYA 407
Cdd:COG5022   328 AAILHIGNIEFKEDRNGAAIFS-DNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYS 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  408 HLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDF 487
Cdd:COG5022   407 NLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY 486
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  488 YDNQPVIDLIEAK--MGILELLDEECLLPHGTDENWLQKLYNNF-VNKNSLFEKPRMSNSSFIIQHFADKVEYQCEGFLE 564
Cdd:COG5022   487 FDNQPCIDLIEKKnpLGILSLLDEECVMPHATDESFTSKLAQRLnKNSNPKFKKSRFRDNKFVVKHYAGDVEYDVEGFLD 566
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  565 KNRDTVYDMLVEILRASKFHLCAAFFQEspvpsspfgamiTVKSAKQVIKPntkhfrtTVGNKFRSSLYLLMETLNATTP 644
Cdd:COG5022   567 KNKDPLNDDLLELLKASTNEFVSTLFDD------------EENIESKGRFP-------TLGSRFKESLNSLMSTLNSTQP 627
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  645 HYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM-----TQQELSLSDKKEVCKV 719
Cdd:COG5022   628 HYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSpskswTGEYTWKEDTKNAVKS 707
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  720 VLHRLIQDSNQYQFGRTKIFFRAGQVAYLEKLRLDKLRQDCIMIQKHVRGWLQRRKFLRERQAALTIQRYFRGQQTVR-- 797
Cdd:COG5022   708 ILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRlv 787
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  798 ----KAITATALKEAWAAIILQKYCRGYLvrnlyQLIRVATITIqahTRGFLARRRYRKLLQEHKAVILQKYARAWLARR 873
Cdd:COG5022   788 dyelKWRLFIKLQPLLSLLGSRKEYRSYL-----ACIIKLQKTI---KREKKLRETEEVEFSLKAEVLIQKFGRSLKAKK 859
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  874 RFQNIRRFVLNIQLTYRVQRLQKKLEDQNREnhglVEKLTSLAALRVGD----LEKVQKLEAELEKAATHRH---SYEEK 946
Cdd:COG5022   860 RFSLLKKETIYLQSAQRVELAERQLQELKID----VKSISSLKLVNLELeseiIELKKSLSSDLIENLEFKTeliARLKK 935
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  947 GRRYRDTVEERLSKLQKHNAELELQRERAEqmLQEKSEELKEKMDKLTrQLFDDVQKEEQQRlvleKGFELKTQAYEKQI 1026
Cdd:COG5022   936 LLNNIDLEEGPSIEYVKLPELNKLHEVESK--LKETSEEYEDLLKKST-ILVREGNKANSEL----KNFKKELAELSKQY 1008
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1027 ESLREEIKALKDERSQL-HHQLEEGQVTSDRlkGEVARLSKQAKTISEFEKEIELLQAQKIDVekhvqSQKREMRERMSe 1105
Cdd:COG5022  1009 GALQESTKQLKELPVEVaELQSASKIISSES--TELSILKPLQKLKGLLLLENNQLQARYKAL-----KLRRENSLLDD- 1080
                        1130      1140      1150      1160      1170      1180      1190
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568961011 1106 vtkqlLESYDIEDVRSRLSVedlehLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEIN 1181
Cdd:COG5022  1081 -----KQLYQLESTENLLKT-----INVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVF 1146
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
81-741 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  Cd Length: 633  Bit Score: 821.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMG-DMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd00124     1 AAILHNLRERYARDL-IYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  160 SGESGAGKTVSARYAMRYFATVSKSSSNAH------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQII 233
Cdd:cd00124    80 SGESGAGKTETTKLVLKYLAALSGSGSSKSsssassIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  234 GANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEE----FNYTRMGGNTVIEGVNDRADMVETQKT 309
Cdd:cd00124   160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSyyylNDYLNSSGCDRIDGVDDAEEFQELLDA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  310 FTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNE--RSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVK 387
Cdd:cd00124   240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  388 PMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQH--TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNL 465
Cdd:cd00124   320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEstSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  466 HVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSNS 544
Cdd:cd00124   400 HVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKpLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKAKL 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  545 SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKfhlcaaffqespvpsspfgamitvksakqvikpntkhfrttv 624
Cdd:cd00124   480 EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS------------------------------------------ 517
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  625 gnKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMT 704
Cdd:cd00124   518 --QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAP 595
                         650       660       670
                  ....*....|....*....|....*....|....*...
gi 568961011  705 Q-QELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd00124   596 GaTEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
81-741 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: 743.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01377     1 ASVLHNLRERY-YSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILIT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  161 GESGAGKTVSARYAMRYFATVSKSSSNAH--------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQI 232
Cdd:cd01377    80 GESGAGKTENTKKVIQYLASVAASSKKKKesgkkkgtLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  233 IGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTL 312
Cdd:cd01377   160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  313 LGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd01377   240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  393 QAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQ 472
Cdd:cd01377   320 QVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  473 EEYMKEDIPWTLIDF-YDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMS--NSSFII 548
Cdd:cd01377   400 EEYKKEGIEWTFIDFgLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKPKksEAHFIL 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  549 QHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAMITVKSAkqvikpntkhFRtTVGNKF 628
Cdd:cd01377   480 KHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGGGKKKKKGGS----------FR-TVSQLH 548
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  629 RSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQEL 708
Cdd:cd01377   549 KEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIP 628
                         650       660       670
                  ....*....|....*....|....*....|....
gi 568961011  709 -SLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd01377   629 kGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
81-741 0e+00

class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.


Pssm-ID: 276835  Cd Length: 647  Bit Score: 701.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd01384     1 PGVLHNLKVRY-ELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  160 SGESGAGKTVSARYAMRYFATVSK--SSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANM 237
Cdd:cd01384    80 SGESGAGKTETTKMLMQYLAYMGGraVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  238 RTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKK 317
Cdd:cd01384   160 RTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  318 DFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDS---HLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd01384   240 EEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKsefHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAA 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  395 INARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEE 474
Cdd:cd01384   320 TLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  475 YMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPRMSNSSFIIQHFAD 553
Cdd:cd01384   400 YTKEEIDWSYIEFVDNQDVLDLIEKKPgGIIALLDEACMFPRSTHETFAQKLYQTLKD-HKRFSKPKLSRTDFTIDHYAG 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  554 KVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSspfgamiTVKSAKqvikpntkhFrTTVGNKFRSSLY 633
Cdd:cd01384   479 DVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREG-------TSSSSK---------F-SSIGSRFKQQLQ 541
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  634 LLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSDK 713
Cdd:cd01384   542 ELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVLKGSDDE 621
                         650       660
                  ....*....|....*....|....*...
gi 568961011  714 KEVCKVVLHRLiqDSNQYQFGRTKIFFR 741
Cdd:cd01384   622 KAACKKILEKA--GLKGYQIGKTKVFLR 647
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
81-741 0e+00

class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276834  Cd Length: 647  Bit Score: 685.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDmdPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01383     1 PSVLHNLEYRY-SQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKLLDS--PHVYAVADTAYREMMRDEINQSIIIS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  161 GESGAGKTVSARYAMRYFATVSKSSSNahVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTY 240
Cdd:cd01383    78 GESGAGKTETAKIAMQYLAALGGGSSG--IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  241 LLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQ 320
Cdd:cd01383   156 LLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKEDQ 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  321 MDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDA 400
Cdd:cd01383   236 EHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  401 LAKKIYAHLFDFIVEQINQALHFSGKQH-TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKED 479
Cdd:cd01383   316 LAKAIYASLFDWLVEQINKSLEVGKRRTgRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDG 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  480 IPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLyNNFVNKNSLFEKPRmsNSSFIIQHFADKVEYQ 558
Cdd:cd01383   396 IDWTKVDFEDNQECLDLIEKKpLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCFKGER--GGAFTIRHYAGEVTYD 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  559 CEGFLEKNRDTVYDMLVEILRASKFHLCAAF------FQESPVPSSPFGamitvKSAKQvikpntkhfRTTVGNKFRSSL 632
Cdd:cd01383   473 TSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFaskmldASRKALPLTKAS-----GSDSQ---------KQSVATKFKGQL 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  633 YLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSD 712
Cdd:cd01383   539 FKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQD 618
                         650       660
                  ....*....|....*....|....*....
gi 568961011  713 KKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd01383   619 PLSTSVAILQQFNILPEMYQVGYTKLFFR 647
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
82-741 0e+00

class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276832  Cd Length: 648  Bit Score: 677.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   82 AVLHNLRIRFAEsKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd01381     2 GILRNLLIRYRE-KLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  162 ESGAGKTVSARYAMRYFATVSKSSSnaHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYL 241
Cdd:cd01381    81 ESGAGKTESTKLILQYLAAISGQHS--WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  242 LEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQM 321
Cdd:cd01381   159 LEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIW 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  322 DVFKILAAILHLGNVQ--VTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARD 399
Cdd:cd01381   239 DIFKLLAAILHLGNIKfeATVVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVRD 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  400 ALAKKIYAHLFDFIVEQINQALHF-SGKQH--TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYM 476
Cdd:cd01381   319 AFVKGIYGRLFIWIVNKINSAIYKpRGTDSsrTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEYD 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  477 KEDIPWTLIDFYDNQPVIDLI-EAKMGILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPRM-SNSSFIIQHFADK 554
Cdd:cd01381   399 KEGINWQHIEFVDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGN-NKNYLKPKSdLNTSFGINHFAGV 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  555 VEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSpfgamitvKSAKQVIkpntkhfrtTVGNKFRSSLYL 634
Cdd:cd01381   478 VFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGS--------ETRKKSP---------TLSSQFRKSLDQ 540
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  635 LMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL------MTQQEL 708
Cdd:cd01381   541 LMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLvpgippAHKTDC 620
                         650       660       670
                  ....*....|....*....|....*....|...
gi 568961011  709 SLSDKKEVCKVVLHrliqDSNqYQFGRTKIFFR 741
Cdd:cd01381   621 RAATRKICCAVLGG----DAD-YQLGKTKIFLK 648
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
82-741 0e+00

class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276829  Cd Length: 652  Bit Score: 676.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd01378     2 AINENLKKRF-ENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  162 ESGAGKTVSARYAMRYFATVSKSSSN--AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRT 239
Cdd:cd01378    81 ESGAGKTEASKRIMQYIAAVSGGSESevERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDF 319
Cdd:cd01378   161 YLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  320 QMDVFKILAAILHLGNVQVTTVGNERSSVSeDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSE---TVVKPMTRPQAIN 396
Cdd:cd01378   241 QDSIFRILAAILHLGNIQFAEDEEGNAAIS-DTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGgrsVYEVPLNVEQAAY 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  397 ARDALAKKIYAHLFDFIVEQINQALHFSGKQH-TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEY 475
Cdd:cd01378   320 ARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQEEY 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  476 MKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPH-GTDENWLQKLyNNFVNKNSLFEKP----RMSNSSFIIQ 549
Cdd:cd01378   400 VREGIEWTPIKYFNNKIICDLIEEKpPGIFAILDDACLTAGdATDQTFLQKL-NQLFSNHPHFECPsghfELRRGEFRIK 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  550 HFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQEspvpsspfgamitvksakQVIKPNTKhfR-TTVGNKF 628
Cdd:cd01378   479 HYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPE------------------GVDLDSKK--RpPTAGTKF 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  629 RSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGilmtqqel 708
Cdd:cd01378   539 KNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYK-------- 610
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 568961011  709 SLSDK---------KEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd01378   611 LLSPKtwpawdgtwQGGVESILKDLNIPPEEYQMGKTKIFIR 652
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
82-741 0e+00

class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276849 [Multi-domain]  Cd Length: 661  Bit Score: 659.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14883     2 GINTNLKVRYK-KDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  162 ESGAGKTVSARYAMRYFATVSKSSSnaHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYL 241
Cdd:cd14883    81 ESGAGKTETTKLILQYLCAVTNNHS--WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  242 LEKSRVVFQSENERNYHIFYQLCASAQQS-EFKH-LKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDF 319
Cdd:cd14883   159 LEQSRITFQAPGERNYHVFYQLLAGAKHSkELKEkLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPEEM 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  320 QMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSH-LKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINAR 398
Cdd:cd14883   239 QEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKEiLKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDNR 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  399 DALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKE 478
Cdd:cd14883   319 DAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKE 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  479 DIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNKNSLFEKP--RMSNSSFIIQHFADKV 555
Cdd:cd14883   399 GINWSHIVFTDNQECLDLIEKPpLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPdrRRWKTEFGVKHYAGEV 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  556 EYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFF----QESPVPSSPFGAMITVKSAkqvikpnTKHFRTTVGNKFRSS 631
Cdd:cd14883   478 TYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtypdLLALTGLSISLGGDTTSRG-------TSKGKPTVGDTFKHQ 550
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  632 LYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQ-QELSL 710
Cdd:cd14883   551 LQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRaRSADH 630
                         650       660       670
                  ....*....|....*....|....*....|.
gi 568961011  711 SDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14883   631 KETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
81-741 0e+00

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: 611.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14872     1 AMIVHNLRKRFKNDQ-IYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  161 GESGAGKTVSARYAMRYFATVSKSSSNahVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTY 240
Cdd:cd14872    80 GESGAGKTEATKQCLSFFAEVAGSTNG--VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  241 LLEKSRVVFQSENERNYHIFYQLCASAQQSefKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQ 320
Cdd:cd14872   158 LLEKSRVVYQIKGERNFHIFYQLLASPDPA--SRGGWGSSAAYGYLSLSGCIEVEGVDDVADFEEVVLAMEQLGFDDADI 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  321 MDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCE---LLGLETSKVAQWLCNRKI-VTSSETVVKPMTRPQAIN 396
Cdd:cd14872   236 NNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTSRLMeIKGCDPTRIPLTPAQATD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  397 ARDALAKKIYAHLFDFIVEQINQALH-FSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEY 475
Cdd:cd14872   316 ACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEALY 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  476 MKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNF-VNKNSLFEKPRMSNSSFIIQHFAD 553
Cdd:cd14872   396 QSEGVKFEHIDFIDNQPVLDLIEKKQpGLMLALDDQVKIPKGSDATFMIAANQTHaAKSTFVYAEVRTSRTEFIVKHYAG 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  554 KVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvpsspfgamitvksakQVIKPNTKHFRTTVGNKFRSSLY 633
Cdd:cd14872   476 DVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF--------------------PPSEGDQKTSKVTLGGQFRKQLS 535
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  634 LLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSL-SD 712
Cdd:cd14872   536 ALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVKTIAKRVgPD 615
                         650       660
                  ....*....|....*....|....*....
gi 568961011  713 KKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14872   616 DRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
81-741 0e+00

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: 602.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14903     1 AAILYNVKKRFL-RKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  160 SGESGAGKTVSARYAMRYFATVSKSSSNAHVEdKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRT 239
Cdd:cd14903    80 SGESGAGKTETTKILMNHLATIAGGLNDSTIK-KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEfkHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDF 319
Cdd:cd14903   159 YLLEKTRVISHERPERNYHIFYQLLASPDVEE--RLFLDSANECAYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEEK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  320 QMDVFKILAAILHLGNVQVTTVGN--ERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINA 397
Cdd:cd14903   237 QEVLFEVLAGILHLGQLQIQSKPNddEKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDC 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  398 RDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMK 477
Cdd:cd14903   317 RDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEE 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  478 EDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSNSSFIIQHFADKVEY 557
Cdd:cd14903   397 EGIRWAHIDFADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSRTQFTIKHYAGPVTY 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  558 QCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAMITVKSAKQVIKPNTKhfrTTVGNKFRSSLYLLME 637
Cdd:cd14903   477 ESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRGGALTT---TTVGTQFKDSLNELMT 553
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  638 TLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSDKKEVC 717
Cdd:cd14903   554 TIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEGRNTDVPVAERC 633
                         650       660
                  ....*....|....*....|....*
gi 568961011  718 KVVLHRL-IQDSNQYQFGRTKIFFR 741
Cdd:cd14903   634 EALMKKLkLESPEQYQMGLTRIYFQ 658
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
84-741 0e+00

class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276833  Cd Length: 649  Bit Score: 595.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   84 LHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd01382     4 LNNIRVRYSKDK-IYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  163 SGAGKTVSARYAMRYFaTVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLL 242
Cdd:cd01382    83 SGAGKTESTKYILRYL-TESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  243 EKSRVVFQSENERNYHIFYQLCASAQQSEFKHLklgsaeefnytrmggnTVIEGVNDRADMVETQKTFTLLGFKKDFQMD 322
Cdd:cd01382   162 EKSRICVQSKEERNYHIFYRLCAGAPEDLREKL----------------LKDPLLDDVGDFIRMDKAMKKIGLSDEEKLD 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  323 VFKILAAILHLGNVQVTTVGNER---SSVSEDDSH-LKVFCELLGLETSKVAQWLCNRKIVTSSE----TVVK-PMTRPQ 393
Cdd:cd01382   226 IFRVVAAVLHLGNIEFEENGSDSgggCNVKPKSEQsLEYAAELLGLDQDELRVSLTTRVMQTTRGgakgTVIKvPLKVEE 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  394 AINARDALAKKIYAHLFDFIVEQINQALHFSGKQHtFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQE 473
Cdd:cd01382   306 ANNARDALAKAIYSKLFDHIVNRINQCIPFETSSY-FIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILKEEQE 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  474 EYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFvNKNSLFEKPRMSNSS------- 545
Cdd:cd01382   385 LYEKEGLGVKEVEYVDNQDCIDLIEAKLvGILDLLDEESKLPKPSDQHFTSAVHQKH-KNHFRLSIPRKSKLKihrnlrd 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  546 ---FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSpfgamitvKSAKQVIKPNTKhfrt 622
Cdd:cd01382   464 degFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNK--------DSKQKAGKLSFI---- 531
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  623 TVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL 702
Cdd:cd01382   532 SVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKY 611
                         650       660       670
                  ....*....|....*....|....*....|....*....
gi 568961011  703 MTqQELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd01382   612 LP-PKLARLDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
84-741 0e+00

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: 588.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   84 LHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGES 163
Cdd:cd01385     4 LENLRARFKHGK-IYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  164 GAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLLE 243
Cdd:cd01385    83 GSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYLLE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  244 KSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQMDV 323
Cdd:cd01385   163 KSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQRQI 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  324 FKILAAILHLGNVQV---TTVGNERSSVSEDDShLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDA 400
Cdd:cd01385   243 FSVLSAVLHLGNIEYkkkAYHRDESVTVGNPEV-LDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRDA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  401 LAKKIYAHLFDFIVEQINQAL----HFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYM 476
Cdd:cd01385   322 MAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYK 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  477 KEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKlYNNFVNKNSLFEKPRMSNSSFIIQHFADKV 555
Cdd:cd01385   402 KEGISWHNIEYTDNTGCLQLISKKpTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQVMEPAFIIAHYAGKV 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  556 EYQCEGFLEKNRDTVYDMLVEILRASK-----------------------FHLCAAFFQESPVPSS----PFGAMITVKS 608
Cdd:cd01385   481 KYQIKDFREKNLDLMRPDIVAVLRSSSsafvreligidpvavfrwavlraFFRAMAAFREAGRRRAqrtaGHSLTLHDRT 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  609 AKQVIKPNTKHFRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPS 688
Cdd:cd01385   561 TKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSV 640
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568961011  689 RWTYLEFYSRYGILMTQQELSlsdKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd01385   641 RYTFQEFITQFQVLLPKGLIS---SKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
82-741 0e+00

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: 572.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14873     2 SIMYNLFQRYKRNQ-IYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  161 GESGAGKTVSARYAMRYFATVSKSSSNA-------HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQII 233
Cdd:cd14873    81 GESGAGKTESTKLILKFLSVISQQSLELslkektsCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  234 GANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLL 313
Cdd:cd14873   161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEVM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  314 GFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSvseDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14873   241 QFSKEEVREVSRLLAGILHLGNIEFITAGGAQVS---FKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQ 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  394 AINARDALAKKIYAHLFDFIVEQINQALHfsGKQH-TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQ 472
Cdd:cd14873   318 AVDSRDSLAMALYARCFEWVIKKINSRIK--GKEDfKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQ 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  473 EEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPRMSNSSFIIQHFA 552
Cdd:cd14873   396 LEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHAN-NHFYVKPRVAVNNFGVKHYA 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  553 DKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQEspvpsspfgamITVKSAKQVIKPNTKHFRTTVGNKFRSSL 632
Cdd:cd14873   475 GEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEH-----------VSSRNNQDTLKCGSKHRRPTVSSQFKDSL 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  633 YLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLsD 712
Cdd:cd14873   544 HSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPE-D 622
                         650       660
                  ....*....|....*....|....*....
gi 568961011  713 KKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14873   623 VRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
82-741 0e+00

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: 571.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMAR----NNRNQS 156
Cdd:cd14890     2 SLLHTLRLRY-ERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  157 IIVSGESGAGKTVSARYAMRYFATVSKSSSN-----------------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFG 219
Cdd:cd14890    81 IIISGESGAGKTEATKIIMQYLARITSGFAQgasgegeaaseaieqtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  220 KYTEISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVND 299
Cdd:cd14890   161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLR-GECSSIPSCDD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  300 RADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVgnERSSVSEDDS---HLKVFCELLGLETSKVAQWLCNR 376
Cdd:cd14890   240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESE--NDTTVLEDATtlqSLKLAAELLGVNEDALEKALLTR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  377 KIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYAN 456
Cdd:cd14890   318 QLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  457 EKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM----GILELLDEECLLpHGTDEN--WLQKLYNNF- 529
Cdd:cd14890   398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVngkpGIFITLDDCWRF-KGEEANkkFVSQLHASFg 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  530 -----------VNKNSLFEKPRMSNS-SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASkfhlcaaffqespvps 597
Cdd:cd14890   477 rksgsggtrrgSSQHPHFVHPKFDADkQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQS---------------- 540
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  598 spfgamitvksakqvikpnTKHFR-TTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVL 676
Cdd:cd14890   541 -------------------RRSIReVSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMM 601
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961011  677 ETIRISAQSYPSRWTYLEFYSRYGILMTQQElslsDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14890   602 EAIQIRQQGFALREEHDSFFYDFQVLLPTAE----NIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
82-741 0e+00

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: 569.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd01387     2 TVLWNLKTRY-ERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  162 ESGAGKTVSARYAMRYFATVSKSSSNAhVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFdERNQIIGANMRTYL 241
Cdd:cd01387    81 ESGSGKTEATKLIMQYLAAVNQRRNNL-VTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAITSQYL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  242 LEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQM 321
Cdd:cd01387   159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQD 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  322 DVFKILAAILHLGNV----QVTTVGNERSSVSEDdSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINA 397
Cdd:cd01387   239 SIFRILASVLHLGNVyfhkRQLRHGQEGVSVGSD-AEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDA 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  398 RDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMK 477
Cdd:cd01387   318 RDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYIR 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  478 EDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKL-YNNFVNKnsLFEKPRMSNSSFIIQHFADKV 555
Cdd:cd01387   398 EQIDWTEIAFADNQPVINLISKKpVGILHILDDECNFPQATDHSFLEKChYHHALNE--LYSKPRMPLPEFTIKHYAGQV 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  556 EYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQ------ESPVPSSPFGAMITvksakqvIKPNTKhfrtTVGNKFR 629
Cdd:cd01387   476 WYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSshraqtDKAPPRLGKGRFVT-------MKPRTP----TVAARFQ 544
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  630 SSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQeLS 709
Cdd:cd01387   545 DSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALK-LP 623
                         650       660       670
                  ....*....|....*....|....*....|....
gi 568961011  710 LSDKKEVCKVVLHRL--IQDSNQYQFGRTKIFFR 741
Cdd:cd01387   624 RPAPGDMCVSLLSRLctVTPKDMYRLGATKVFLR 657
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
81-741 0e+00

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: 562.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFAESkLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01379     1 DTIVSQLQKRYSRD-QIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  161 GESGAGKTVSARYAMRYFATVSKSSsNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTY 240
Cdd:cd01379    80 GESGAGKTESANLLVQQLTVLGKAN-NRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  241 LLEKSRVVFQSENERNYHIFYQLCAS-AQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMV---ETQKTFTLLGFK 316
Cdd:cd01379   159 LLEKSRVVHQAIGERNFHIFYYIYAGlAEDKKLAKYKLPENKPPRYLQNDGLTVQDIVNNSGNREkfeEIEQCFKVIGFT 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  317 KDFQMDVFKILAAILHLGNVQVTTVGNE----RSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd01379   239 KEEVDSVYSILAAILHIGDIEFTEVESNhqtdKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVE 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  393 QAINARDALAKKIYAHLFDFIVEQINQAL----HFSGKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVF 468
Cdd:cd01379   319 EATDARDAMAKALYGRLFSWIVNRINSLLkpdrSASDEPLS-IGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIF 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  469 KLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvnKNSLFEKPRMSNSSFI 547
Cdd:cd01379   398 AWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKpMGLLALLDEESRFPKATDQTLVEKFHNNI--KSKYYWRPKSNALSFG 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  548 IQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLcaaffqespvpsspfgamitvksakqvikpntkhFRTTVGNK 627
Cdd:cd01379   476 IHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPL----------------------------------VRQTVATY 521
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  628 FRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQE 707
Cdd:cd01379   522 FRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAFKWN 601
                         650       660       670
                  ....*....|....*....|....*....|....
gi 568961011  708 LSLSDKKEVCKVVLHRLIQDSnqYQFGRTKIFFR 741
Cdd:cd01379   602 EEVVANRENCRLILERLKLDN--WALGKTKVFLK 633
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
81-741 0e+00

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: 562.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14904     1 PSILFNLKKRFAASK-PYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  160 SGESGAGKTVSARYAMRYFATVSKSSSNAHVeDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRT 239
Cdd:cd14904    80 SGESGAGKTETTKIVMNHLASVAGGRKDKTI-AKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCET 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYtrMGGN---TVIEGVNDRADMVETQKTFTLLGFK 316
Cdd:cd14904   159 YLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQY--LGDSlaqMQIPGLDDAKLFASTQKSLSLIGLD 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  317 KDFQMDVFKILAAILHLGNVQVTTVGnERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAIN 396
Cdd:cd14904   237 NDAQRTLFKILSGVLHLGEVMFDKSD-ENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEE 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  397 ARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEY 475
Cdd:cd14904   316 NRDALAKAIYSKLFDWMVVKINAAISTDDDRiKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEEY 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  476 MKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNK--NSLFEKPRMSNSSFIIQHFAD 553
Cdd:cd14904   396 IREGLQWDHIEYQDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQTKkdNESIDFPKVKRTQFIINHYAG 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  554 KVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvKSAKQVIKPNtkhfrtTVGNKFRSSLY 633
Cdd:cd14904   476 PVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAPSETKEG----KSGKGTKAPK------SLGSQFKTSLS 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  634 LLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIlMTQQELSLSDK 713
Cdd:cd14904   546 QLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAI-MFPPSMHSKDV 624
                         650       660
                  ....*....|....*....|....*....
gi 568961011  714 KEVCKVVLHRLIQDSN-QYQFGRTKIFFR 741
Cdd:cd14904   625 RRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
81-739 0e+00

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: 550.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAY---SGQNMGD---MDPHIFAVAEEAYKQMARNNR- 153
Cdd:cd14901     1 PSILHVLRRRF-AHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehGERRAAGerkLPPHVYAVADKAFRAMLFASRg 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  154 ---NQSIIVSGESGAGKTVSARYAMRYFATVS-KSSSNAH------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTE 223
Cdd:cd14901    80 qkcDQSILVSGESGAGKTETTKIIMNYLASVSsATTHGQNaterenVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  224 ISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTV-IEGVNDRAD 302
Cdd:cd14901   160 LGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDrRDGVDDSVQ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  303 MVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQ-VTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTS 381
Cdd:cd14901   240 YAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCfVKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAG 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  382 SETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHF--SGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKL 459
Cdd:cd14901   320 GEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYseSTGASRFIGIVDIFGFEIFATNSLEQLCINFANEKL 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  460 QQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNKNSL-FE 537
Cdd:cd14901   400 QQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARpTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKHASFsVS 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  538 KPRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLcaaffqespVPSspfgamitvksakqvikpnt 617
Cdd:cd14901   480 KLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAF---------LSS-------------------- 530
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  618 khfrtTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYS 697
Cdd:cd14901   531 -----TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVH 605
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568961011  698 RYGILMTQQElslSDKKEVCKVVLHR---------LIQDSNQYQFGRTKIF 739
Cdd:cd14901   606 TYSCLAPDGA---SDTWKVNELAERLmsqlqhselNIEHLPPFQVGKTKVF 653
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
87-741 4.97e-179

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: 544.35  E-value: 4.97e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   87 LRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMD---PHIFAVAEEAYKQM----ARNNRNQSIIV 159
Cdd:cd14892     7 LRRRY-ERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATASsppPHVFSIAERAYRAMkgvgKGQGTPQSIVV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  160 SGESGAGKTVSARYAMRYFATVSKSSS---------NAH--VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDE 228
Cdd:cd14892    86 SGESGAGKTEASKYIMKYLATASKLAKgastskgaaNAHesIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  229 RNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQK 308
Cdd:cd14892   166 DGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVDGVDDATEFKQLRD 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKV--FCELLGLETSKVAQWLCNRKIVTSSETVV 386
Cdd:cd14892   246 AMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNVakAAGLLGVDAAELMFKLVTQTTSTARGSVL 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  387 K-PMTRPQAINARDALAKKIYAHLFDFIVEQINqALH-----------FSGKQHTFIGVLDIYGFETFDVNSFEQFCINY 454
Cdd:cd14892   326 EiKLTAREAKNALDALCKYLYGELFDWLISRIN-ACHkqqtsgvtggaASPTFSPFIGILDIFGFEIMPTNSFEQLCINF 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  455 ANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPH-GTDENWLQKLYNNFVNK 532
Cdd:cd14892   405 TNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKpLGLLPLLEEQMLLKRkTTDKQLLTIYHQTHLDK 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  533 NSLFEKPRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKfhlcaaffqespvpsspfgamitvksakqv 612
Cdd:cd14892   485 HPHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS------------------------------ 534
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  613 ikpntkhfrttvgnKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTY 692
Cdd:cd14892   535 --------------KFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQF 600
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568961011  693 LEFYSRYGIL--------MTQQELSLSD-KKEVCKVVLHRLiqDSNQYQFGRTKIFFR 741
Cdd:cd14892   601 EEFYEKFWPLarnkagvaASPDACDATTaRKKCEEIVARAL--ERENFQLGRTKVFLR 656
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
81-741 2.09e-177

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: 540.43  E-value: 2.09e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSgQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14888     1 ASILHSLNLRFDIDE-IYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  160 SGESGAGKTVSARYAMRYFATVSKSS--SNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERN------- 230
Cdd:cd14888    79 SGESGAGKTESTKYVMKFLACAGSEDikKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLKskrmsgd 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  231 --QIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQS-------EFKHLKLG----------------SAEEFNY 285
Cdd:cd14888   159 rgRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAkntglsyEENDEKLAkgadakpisidmssfePHLKFRY 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  286 TRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQ-VTTVGNERSSV--SEDDSHLKVFCELL 362
Cdd:cd14888   239 LTKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILfENNEACSEGAVvsASCTDDLEKVASLL 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  363 GLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHT-FIGVLDIYGFET 441
Cdd:cd14888   319 GVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLlFCGVLDIFGFEC 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  442 FDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDEN 520
Cdd:cd14888   399 FQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKpLGIFCMLDEECFVPGGKDQG 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  521 WLQKLYNNFVNkNSLFEKPRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKfhlcaaffqeSPVPSSPF 600
Cdd:cd14888   479 LCNKLCQKHKG-HKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSK----------NPFISNLF 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  601 GAMItvkSAKQVIKPNTKHFRtTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIR 680
Cdd:cd14888   548 SAYL---RRGTDGNTKKKKFV-TVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQ 623
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568961011  681 ISAQSYPSRWTYLEFYSRYGILMTQQElslsdKKEVckvvlhrliqdsNQYQFGRTKIFFR 741
Cdd:cd14888   624 VSRAGYPVRLSHAEFYNDYRILLNGEG-----KKQL------------SIWAVGKTLCFFK 667
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
82-741 1.06e-168

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: 518.03  E-value: 1.06e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14920     2 SVLHNLKDRYY-SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  162 ESGAGKTVSARYAMRYFATVSKSSSN-------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIG 234
Cdd:cd14920    81 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  235 ANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVNDRADMVETQKTFTLLG 314
Cdd:cd14920   161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIMG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  315 FKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14920   240 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQA 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  395 INARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQE 473
Cdd:cd14920   320 DFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  474 EYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNfVNKNSLFEKPRM--SNSSFI 547
Cdd:cd14920   400 EYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQE-QGSHSKFQKPRQlkDKADFC 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  548 IQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQE--SPVPSSPFGAMiTVKSAKQVIKPNTKHFRtTVG 625
Cdd:cd14920   479 IIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdRIVGLDQVTGM-TETAFGSAYKTKKGMFR-TVG 556
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  626 NKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQ 705
Cdd:cd14920   557 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 636
                         650       660       670
                  ....*....|....*....|....*....|....*..
gi 568961011  706 Q-ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14920   637 AiPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
MYSc_Myh3 cd14913
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...
81-741 2.27e-166

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: 511.52  E-value: 2.27e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14913     1 PAVLYNLKDRYT-SWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  161 GESGAGKTVSARYAMRYFATVS---------KSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQ 231
Cdd:cd14913    80 GESGAGKTVNTKRVIQYFATIAatgdlakkkDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  232 IIGANMRTYLLEKSRVVFQSENERNYHIFYQLCaSAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQKTF 310
Cdd:cd14913   160 LASADIETYLLEKSRVTFQLKAERSYHIFYQIL-SNKKPELIELLLITTNPYDYPFISqGEILVASIDDAEELLATDSAI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  311 TLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMT 390
Cdd:cd14913   239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  391 RPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKL 470
Cdd:cd14913   319 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  471 EQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRM----SNSS 545
Cdd:cd14913   399 EQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVvkgrAEAH 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  546 FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvpsSPFGAMITVKSAKQVIKPNTKHFRtTVG 625
Cdd:cd14913   479 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY-------ATFATADADSGKKKVAKKKGSSFQ-TVS 550
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  626 NKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQ 705
Cdd:cd14913   551 ALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNAS 630
                         650       660       670
                  ....*....|....*....|....*....|....*...
gi 568961011  706 Q--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14913   631 AipEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myh7b cd14927
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...
82-741 1.04e-165

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: 510.27  E-value: 1.04e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14927     2 SVLHNLRRRYS-RWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  162 ESGAGKTVSARYAMRYFATVS-------------KSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDE 228
Cdd:cd14927    81 ESGAGKTVNTKRVIQYFAIVAalgdgpgkkaqflATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  229 RNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQ 307
Cdd:cd14927   161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQI-LSGKKPELQDMLLVSMNPYDYHFCSqGVTTVDNMDDGEELMATD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  308 KTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVK 387
Cdd:cd14927   240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  388 PMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHV 467
Cdd:cd14927   320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHM 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  468 FKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSN--- 543
Cdd:cd14927   400 FILEQEEYKREGIEWVFIDFgLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKkrk 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  544 --SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqESPVPSSpfgamiTVKSAKQVIKPNTKHFR 621
Cdd:cd14927   480 yeAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY-ENYVGSD------STEDPKSGVKEKRKKAA 552
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  622 T--TVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRY 699
Cdd:cd14927   553 SfqTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRY 632
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....
gi 568961011  700 GILMTQQ--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14927   633 RILNPSAipDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
MYSc_Myh15_mammals cd14929
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...
81-741 1.40e-165

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: 509.13  E-value: 1.40e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14929     1 ASVLHTLRRRY-DHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  161 GESGAGKTVSARYAMRYFATVSKSSSN----AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGAN 236
Cdd:cd14929    80 GESGAGKTVNTKHIIQYFATIAAMIESkkklGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSAD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  237 MRTYLLEKSRVVFQSENERNYHIFYQLCASAQqsEFKHLKLGSA--EEFNYTRMGGNTViEGVNDRADMVETQKTFTLLG 314
Cdd:cd14929   160 IDIYLLEKSRVIFQQPGERNYHIFYQILSGKK--ELRDLLLVSAnpSDFHFCSCGAVAV-ESLDDAEELLATEQAMDILG 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  315 FKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14929   237 FLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQV 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  395 INARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEE 474
Cdd:cd14929   317 TYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEE 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  475 YMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSNSSFIIQ---- 549
Cdd:cd14929   397 YRKEGIDWVSIDFgLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHfelv 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  550 HFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQE--SPVPSSPFGAMITVKSAKqvikpntkhFRtTVGNK 627
Cdd:cd14929   477 HYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENyiSTDSAIQFGEKKRKKGAS---------FQ-TVASL 546
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  628 FRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL--MTQ 705
Cdd:cd14929   547 HKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILnpRTF 626
                         650       660       670
                  ....*....|....*....|....*....|....*.
gi 568961011  706 QELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14929   627 PKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
MYSc_Myh1_insects_crustaceans cd14909
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
81-741 2.06e-165

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: 509.00  E-value: 2.06e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14909     1 ASVLHNLRQRY-YAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  161 GESGAGKTVSARYAMRYFATVSKSS-------SNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQII 233
Cdd:cd14909    80 GESGAGKTENTKKVIAYFATVGASKktdeaakSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  234 GANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQKTFTL 312
Cdd:cd14909   160 GADIETYLLEKARVISQQSLERSYHIFYQI-MSGSVPGVKEMCLLSDNIYDYYIVSqGKVTVPNVDDGEEFSLTDQAFDI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  313 LGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd14909   239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQ 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  393 QAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQ 472
Cdd:cd14909   319 QVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  473 EEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSN-----SSF 546
Cdd:cd14909   399 EEYKREGIDWAFIDFgMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpgqqaAHF 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  547 IIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvksAKQVIKPNTKHFrTTVGN 626
Cdd:cd14909   479 AIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQ------AKGGRGKKGGGF-ATVSS 551
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  627 KFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQ 706
Cdd:cd14909   552 AYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAG 631
                         650       660       670
                  ....*....|....*....|....*....|....*
gi 568961011  707 ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14909   632 IQGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
83-741 1.17e-163

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: 504.56  E-value: 1.17e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP---------IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14907     3 LLINLKKRYQQDK-IFTYVGPTLIVMNPYKQIDnlfseevmqMYKEQIIQNGEYFDIKKEPPHIYAIAALAFKQLFENNK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  154 NQSIIVSGESGAGKTVSARYAMRYFATVS------------------KSSSNAHVEDKVLASNPITEAVGNAKTTRNDNS 215
Cdd:cd14907    82 KQAIVISGESGAGKTENAKYAMKFLTQLSqqeqnseevltltssiraTSKSTKSIEQKILSCNPILEAFGNAKTVRNDNS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  216 SRFGKYTEISFDERNQ-IIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKL---GSAEEFNYTRMGGN 291
Cdd:cd14907   162 SRFGKYVSILVDKKKRkILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLknqLSGDRYDYLKKSNC 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  292 TVIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQ---VTTVGNERSSVSeDDSHLKVFCELLGLETSK 368
Cdd:cd14907   242 YEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQfddSTLDDNSPCCVK-NKETLQIIAKLLGIDEEE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  369 VAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSG--KQHTF------IGVLDIYGFE 440
Cdd:cd14907   321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMPKDekDQQLFqnkylsIGLLDIFGFE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  441 TFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTL--IDFYDNQPVIDLIE-AKMGILELLDEECLLPHGT 517
Cdd:cd14907   401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSYTDNQDVIDLLDkPPIGIFNLLDDSCKLATGT 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  518 DENWLQKLYNNFvNKNSLFEKPRMSNS-SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESpvp 596
Cdd:cd14907   481 DEKLLNKIKKQH-KNNSKLIFPNKINKdTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGE--- 556
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  597 sspfGAMITVKSAKQVIKPNTKHFrttVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVL 676
Cdd:cd14907   557 ----DGSQQQNQSKQKKSQKKDKF---LGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVL 629
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961011  677 ETIRISAQSYPSRWTYLEFYSRYGILmtqqelslsdkkevckvvlhrliqdSNQYQFGRTKIFFR 741
Cdd:cd14907   630 ESIRVRKQGYPYRKSYEDFYKQYSLL-------------------------KKNVLFGKTKIFMK 669
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
83-741 7.52e-159

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: 490.36  E-value: 7.52e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDM-DPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14897     3 IVQTLKSRYNKDK-FYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVRSQrPPHLFWIADQAYRRLLETGRNQCILVSG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  162 ESGAGKTVSARYAMRYFATVSkSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYL 241
Cdd:cd14897    82 ESGAGKTESTKYMIKHLMKLS-PSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  242 LEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVNDRADMVETQKTFT-------LLG 314
Cdd:cd14897   161 LEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILR-DDNRNRPVFNDSEELEYYRQMFHdltnimkLIG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  315 F-KKDFQMdVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14897   240 FsEEDISV-IFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQ 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  394 AINARDALAKKIYAHLFDFIVEQINQALH----FSGK-QHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVF 468
Cdd:cd14897   319 ANDSRDALAKDLYSRLFGWIVGQINRNLWpdkdFQIMtRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVF 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  469 KLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLyNNFVNKNSLFEKPRMSNSSFI 547
Cdd:cd14897   399 PRERSEYEIEGIEWRDIEYHDNDDVLELFFKKpLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESPRYVASPGNRVAFG 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  548 IQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvpsspfgamitvksakqvikpnTKHfrttvgnk 627
Cdd:cd14897   478 IRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF--------------------------TSY-------- 523
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  628 FRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQE 707
Cdd:cd14897   524 FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFSN 603
                         650       660       670
                  ....*....|....*....|....*....|....
gi 568961011  708 LSLSDKKEVCKVVLHrlIQDSNQYQFGRTKIFFR 741
Cdd:cd14897   604 KVRSDDLGKCQKILK--TAGIKGYQFGKTKVFLK 635
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
82-741 3.97e-157

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: 487.57  E-value: 3.97e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14911     2 SVLHNIKDRYY-SGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  162 ESGAGKTVSARYAMRYFATVS----KSSSNAH------------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEIS 225
Cdd:cd14911    81 ESGAGKTENTKKVIQFLAYVAaskpKGSGAVPhpavnpavligeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  226 FDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVNDRADMVE 305
Cdd:cd14911   161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLS-NGSLPVPGVDDYAEFQA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  306 TQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETV 385
Cdd:cd14911   240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  386 VKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFN 464
Cdd:cd14911   320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQgASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  465 LHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSN 543
Cdd:cd14911   400 HTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDFRGV 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  544 SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAMITVKSAKQVIKpntKHFRtT 623
Cdd:cd14911   480 ADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQFGARTRK---GMFR-T 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  624 VGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM 703
Cdd:cd14911   556 VSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLT 635
                         650       660       670
                  ....*....|....*....|....*....|....*....
gi 568961011  704 TQQ-ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14911   636 PNViPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
MYSc_Myh7 cd14917
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...
81-741 1.35e-155

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: 483.07  E-value: 1.35e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14917     1 PAVLYNLKERYA-SWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  161 GESGAGKTVSARYAMRYFATVS---------KSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQ 231
Cdd:cd14917    80 GESGAGKTVNTKRVIQYFAVIAaigdrskkdQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  232 IIGANMRTYLLEKSRVVFQSENERNYHIFYQLCaSAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQKTF 310
Cdd:cd14917   160 LASADIETYLLEKSRVIFQLKAERDYHIFYQIL-SNKKPELLDMLLITNNPYDYAFISqGETTVASIDDAEELMATDNAF 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  311 TLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMT 390
Cdd:cd14917   239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  391 RPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKL 470
Cdd:cd14917   319 VQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  471 EQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR----MSNSS 545
Cdd:cd14917   399 EQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRnikgKPEAH 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  546 FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPfgamitVKSAKQVIKPNTKHfrTTVG 625
Cdd:cd14917   479 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAP------IEKGKGKAKKGSSF--QTVS 550
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  626 NKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQ 705
Cdd:cd14917   551 ALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 630
                         650       660       670
                  ....*....|....*....|....*....|....*...
gi 568961011  706 Q--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14917   631 AipEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
81-741 1.62e-153

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: 478.25  E-value: 1.62e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAY------SGQNM---GDMDPHIFAVAEEAYKQMARN 151
Cdd:cd14908     1 PAILHSLSRRFFRGI-IYTWTGPVLIAVNPFQRLPLYGKEILESYrqegllRSQGIespQALGPHVFAIADRSYRQMMSE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  152 NR-NQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAHVE----------DKVLASNPITEAVGNAKTTRNDNSSRFGK 220
Cdd:cd14908    80 IRaSQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEgeelgklsimDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  221 YTEISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGS--------AEEFNYTRMGGNT 292
Cdd:cd14908   160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDgitgglqlPNEFHYTGQGGAP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  293 VIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVS---EDDSHLKVFCELLGLETSKV 369
Cdd:cd14908   240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIaeeGNEKCLARVAKLLGVDVDKL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  370 AQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQ--HTFIGVLDIYGFETFDVNSF 447
Cdd:cd14908   320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKdiRSSVGVLDIFGFECFAHNSF 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  448 EQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEA-KMGILELLDEECLLP-HGTDENWLQKL 525
Cdd:cd14908   400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAkKKGILTMLDDECRLGiRGSDANYASRL 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  526 YNNF-------VNKNSLFEKPRM--SNSSFIIQHFADKVEYQCE-GFLEKNRDTVydmlveilraskfhlcaaffqespv 595
Cdd:cd14908   480 YETYlpeknqtHSENTRFEATSIqkTKLIFAVRHFAGQVQYTVEtTFCEKNKDEI------------------------- 534
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  596 psspfgamitvksakqvikPNTKHFRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGV 675
Cdd:cd14908   535 -------------------PLTADSLFESGQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGV 595
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  676 LETIRISAQSYPSRWTYLEFYSRYGILM-TQQELSLSDK-----------KEVCKV-VLHRLIQD--------SNQYQFG 734
Cdd:cd14908   596 LEAVRVARSGYPVRLPHKDFFKRYRMLLpLIPEVVLSWSmerldpqklcvKKMCKDlVKGVLSPAmvsmknipEDTMQLG 675

                  ....*..
gi 568961011  735 RTKIFFR 741
Cdd:cd14908   676 KSKVFMR 682
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
83-741 3.97e-153

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: 476.32  E-value: 3.97e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   83 VLHNLRIRFAESkLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQM----ARNNRNQSII 158
Cdd:cd14889     3 LLEVLKVRFMQS-NIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMlgrlARGPKNQCIV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  159 VSGESGAGKTVSARYAMRYFATVSKSssNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFdERNQIIGANMR 238
Cdd:cd14889    82 ISGESGAGKTESTKLLLRQIMELCRG--NSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  239 TYLLEKSRVVFQSENERNYHIFYQLCA--SAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADmvETQKTFTLLGFK 316
Cdd:cd14889   159 EYLLEKSRVVHQDGGEENFHIFYYMFAgiSAEDRENYGLLDPGKYRYLNNGAGCKREVQYWKKKYD--EVCNAMDMVGFT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  317 KDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSH-LKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAI 395
Cdd:cd14889   237 EQEEVDMFTILAGILSLGNITFEMDDDEALKVENDSNGwLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQAE 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  396 NARDALAKKIYAHLFDFIVEQINQAL----HFSGKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLE 471
Cdd:cd14889   317 DARDSIAKVAYGRVFGWIVSKINQLLapkdDSSVELRE-IGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLME 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  472 QEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNKNSLFEKPRMSNSSFIIQH 550
Cdd:cd14889   396 QKEYKKEGIDWKEITYKDNKPILDLFLNKpIGILSLLDEQSHFPQATDESFVDKLNIHF-KGNSYYGKSRSKSPKFTVNH 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  551 FADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESpvpSSPFGAMITVKSAKQVIKPNTKHFR-TTVGNKFR 629
Cdd:cd14889   475 YAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTAT---RSRTGTLMPRAKLPQAGSDNFNSTRkQSVGAQFK 551
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  630 SSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELS 709
Cdd:cd14889   552 HSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILLCEPALP 631
                         650       660       670
                  ....*....|....*....|....*....|..
gi 568961011  710 LSdkKEVCKVVLHRliQDSNQYQFGRTKIFFR 741
Cdd:cd14889   632 GT--KQSCLRILKA--TKLVGWKCGKTRLFFK 659
MYSc_Myh16 cd14934
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...
82-741 8.62e-152

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: 472.98  E-value: 8.62e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14934     2 SVLDNLRQRYTNMR-IYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  162 ESGAGKTVSARYAMRYFATVSKSSSNA-----HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGAN 236
Cdd:cd14934    81 ESGAGKTENTKKVIQYFANIGGTGKQSsdgkgSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  237 MRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKL-GSAEEFNYTRMGgNTVIEGVNDRADMVETQKTFTLLGF 315
Cdd:cd14934   161 IESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvPNPKEYHWVSQG-VTVVDNMDDGEELQITDVAFDVLGF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  316 KKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAI 395
Cdd:cd14934   240 SAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCN 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  396 NARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEY 475
Cdd:cd14934   320 NSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEY 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  476 MKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKP-----RMSNSSFIIQ 549
Cdd:cd14934   400 KREGIEWVFIDFgLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPkggkgKGPEAHFELV 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  550 HFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSpfgamitvkSAKQviKPNTKHFrtTVGNKFR 629
Cdd:cd14934   480 HYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAG---------SKKQ--KRGSSFM--TVSNFYR 546
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  630 SSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQ-EL 708
Cdd:cd14934   547 EQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNViPQ 626
                         650       660       670
                  ....*....|....*....|....*....|...
gi 568961011  709 SLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14934   627 GFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
MYSc_Myh8 cd14918
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...
81-741 1.73e-151

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: 472.30  E-value: 1.73e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14918     1 PGVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  161 GESGAGKTVSARYAMRYFATVSKSSS---------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQ 231
Cdd:cd14918    80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  232 IIGANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQKTF 310
Cdd:cd14918   160 LASADIETYLLEKSRVTFQLKAERSYHIFYQI-TSNKKPDLIEMLLITTNPYDYAFVSqGEITVPSIDDQEELMATDSAI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  311 TLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMT 390
Cdd:cd14918   239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  391 RPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKL 470
Cdd:cd14918   319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  471 EQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRM----SNSS 545
Cdd:cd14918   399 EQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVvkgkAEAH 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  546 FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvpsSPFGAMITVKSAKQVIKPNTKHFRtTVG 625
Cdd:cd14918   479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLF-------STYASAEADSGAKKGAKKKGSSFQ-TVS 550
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  626 NKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQ 705
Cdd:cd14918   551 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS 630
                         650       660       670
                  ....*....|....*....|....*....|....*...
gi 568961011  706 Q--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14918   631 AipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myh6 cd14916
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...
81-741 6.16e-151

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: 471.08  E-value: 6.16e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14916     1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  161 GESGAGKTVSARYAMRYFATVSK----------SSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERN 230
Cdd:cd14916    80 GESGAGKTVNTKRVIQYFASIAAigdrskkenpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  231 QIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCaSAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQKT 309
Cdd:cd14916   160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQIL-SNKKPELLDMLLVTNNPYDYAFVSqGEVSVASIDDSEELLATDSA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  310 FTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPM 389
Cdd:cd14916   239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  390 TRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFK 469
Cdd:cd14916   319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  470 LEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR----MSNS 544
Cdd:cd14916   399 LEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRnvkgKQEA 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  545 SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvpSSPFGAMITVKSAKQVIKPNTKHFRtTV 624
Cdd:cd14916   479 HFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLF------STYASADTGDSGKGKGGKKKGSSFQ-TV 551
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  625 GNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL-- 702
Cdd:cd14916   552 SALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILnp 631
                         650       660       670
                  ....*....|....*....|....*....|....*....
gi 568961011  703 MTQQELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14916   632 AAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
82-741 8.95e-151

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: 470.66  E-value: 8.95e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14932     2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  162 ESGAGKTVSARYAMRYFATVSKSS-----------SNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERN 230
Cdd:cd14932    81 ESGAGKTENTKKVIQYLAYVASSFktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  231 QIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLgsaEEFNYTRM--GGNTVIEGVNDRADMVETQK 308
Cdd:cd14932   161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCL---EDYSKYRFlsNGNVTIPGQQDKELFAETME 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14932   238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKA 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  389 MTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHV 467
Cdd:cd14932   318 QTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  468 FKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNfVNKNSLFEKPR--M 541
Cdd:cd14932   398 FILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQE-QGNNPKFQKPKklK 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  542 SNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESP--VPSSPFGAMitVKSAKQVIKPNTKH 619
Cdd:cd14932   477 DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDriVGLDKVAGM--GESLHGAFKTRKGM 554
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  620 FRtTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRY 699
Cdd:cd14932   555 FR-TVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 633
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|...
gi 568961011  700 GILM-TQQELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14932   634 EILTpNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
MYSc_Myh2_mammals cd14912
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
81-741 1.34e-150

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: 470.37  E-value: 1.34e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14912     1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  161 GESGAGKTVSARYAMRYFATVSKSSS-----------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDER 229
Cdd:cd14912    80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  230 NQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQK 308
Cdd:cd14912   160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI-TSNKKPELIEMLLITTNPYDYPFVSqGEISVASIDDQEELMATDS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14912   239 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  389 MTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVF 468
Cdd:cd14912   319 QTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  469 KLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRM----SN 543
Cdd:cd14912   399 VLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVvkgkAE 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  544 SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvKSAKQVIKPNTKHFRtT 623
Cdd:cd14912   479 AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAG----GGAKKGGKKKGSSFQ-T 553
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  624 VGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM 703
Cdd:cd14912   554 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 633
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|
gi 568961011  704 TQQ--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14912   634 ASAipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
MYSc_Myh1_mammals cd14910
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
81-741 2.05e-149

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: 466.90  E-value: 2.05e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14910     1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  161 GESGAGKTVSARYAMRYFATVSKSSS-----------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDER 229
Cdd:cd14910    80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  230 NQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQK 308
Cdd:cd14910   160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI-MSNKKPDLIEMLLITTNPYDYAFVSqGEITVPSIDDQEELMATDS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14910   239 AIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKG 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  389 MTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVF 468
Cdd:cd14910   319 QTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  469 KLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSN---- 543
Cdd:cd14910   399 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKgkve 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  544 SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvksAKQVIKPNTKHFRtT 623
Cdd:cd14910   479 AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEGG------GKKGGKKKGSSFQ-T 551
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  624 VGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM 703
Cdd:cd14910   552 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 631
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|
gi 568961011  704 TQQ--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14910   632 ASAipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
81-741 6.28e-149

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: 464.90  E-value: 6.28e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFA-ESKLIYTYSGIILVAMNPYKQLPiygDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNN---RNQS 156
Cdd:cd14891     1 AGILHNLEERSKlDNQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSgrmQNQS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  157 IIVSGESGAGKTVSARYAMRY------------FATVSKSSSNAH-----VEDKVLASNPITEAVGNAKTTRNDNSSRFG 219
Cdd:cd14891    78 IVISGESGAGKTETSKIILRFlttravggkkasGQDIEQSSKKRKlsvtsLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  220 KYTEISF-DERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVN 298
Cdd:cd14891   158 KFMKLQFtKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNID 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  299 DRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQV----TTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLC 374
Cdd:cd14891   238 DAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFdeedTSEGEAEIASESDKEALATAAELLGVDEEALEKVIT 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  375 NRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFD-VNSFEQFCIN 453
Cdd:cd14891   318 QREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLIN 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  454 YANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFvNK 532
Cdd:cd14891   398 YANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPnGILPLLDNEARNPNPSDAKLNETLHKTH-KR 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  533 NSLF--EKPRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASkfhlcaaffqespvpsspfgamitvksak 610
Cdd:cd14891   477 HPCFprPHPKDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS----------------------------- 527
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  611 qvikpntkhfrttvgNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRW 690
Cdd:cd14891   528 ---------------AKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRV 592
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568961011  691 TYLEFYSRYGILMTQQELSL--SDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14891   593 TYAELVDVYKPVLPPSVTRLfaENDRTLTQAILWAFRVPSDAYRLGRTRVFFR 645
MYSc_Myh13 cd14923
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...
81-741 8.30e-148

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: 462.62  E-value: 8.30e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14923     1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  161 GESGAGKTVSARYAMRYFATVS----------KSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERN 230
Cdd:cd14923    80 GESGAGKTVNTKRVIQYFATIAvtgdkkkeqqPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  231 QIIGANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQKT 309
Cdd:cd14923   160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQI-MSNKKPELIDLLLISTNPFDFPFVSqGEVTVASIDDSEELLATDNA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  310 FTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPM 389
Cdd:cd14923   239 IDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQ 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  390 TRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFK 469
Cdd:cd14923   319 NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  470 LEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR----MSNS 544
Cdd:cd14923   399 LEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKpakgKAEA 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  545 SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvkSAKQVIKPNTKHFRtTV 624
Cdd:cd14923   479 HFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSG-----GSKKGGKKKGSSFQ-TV 552
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  625 GNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMT 704
Cdd:cd14923   553 SAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNA 632
                         650       660       670
                  ....*....|....*....|....*....|....*....
gi 568961011  705 QQ--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14923   633 SAipEGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
MYSc_Myh4 cd14915
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...
81-741 1.22e-147

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: 462.28  E-value: 1.22e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14915     1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  161 GESGAGKTVSARYAMRYFATVSKSSS-----------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDER 229
Cdd:cd14915    80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeaasgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  230 NQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQK 308
Cdd:cd14915   160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI-MSNKKPELIEMLLITTNPYDFAFVSqGEITVPSIDDQEELMATDS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14915   239 AVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKG 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  389 MTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVF 468
Cdd:cd14915   319 QTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  469 KLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR----MSN 543
Cdd:cd14915   399 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKpakgKAE 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  544 SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvksAKQVIKPNTKHFRtT 623
Cdd:cd14915   479 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGG------GKKGGKKKGSSFQ-T 551
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  624 VGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM 703
Cdd:cd14915   552 VSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 631
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|
gi 568961011  704 TQQ--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14915   632 ASAipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
82-741 5.85e-147

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: 460.64  E-value: 5.85e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14921     2 SVLHNLRERYF-SGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  162 ESGAGKTVSARYAMRYFATVSKS-------SSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIG 234
Cdd:cd14921    81 ESGAGKTENTKKVIQYLAVVASShkgkkdtSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  235 ANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLgsaEEF-NYTRMGGNTVIEGVNDRADMV-ETQKTFTL 312
Cdd:cd14921   161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLL---EGFnNYTFLSNGFVPIPAAQDDEMFqETLEAMSI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  313 LGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd14921   238 MGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKE 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  393 QAINARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLE 471
Cdd:cd14921   318 QADFAIEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  472 QEEYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPRM--SNSS 545
Cdd:cd14921   398 QEEYQREGIEWNFIDFgLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQGN-HPKFQKPKQlkDKTE 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  546 FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQE-SPVPSSPFGAMITVKSAKQVIKPNTKHFRtTV 624
Cdd:cd14921   477 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDvDRIVGLDQMAKMTESSLPSASKTKKGMFR-TV 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  625 GNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMT 704
Cdd:cd14921   556 GQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 635
                         650       660       670
                  ....*....|....*....|....*....|....*...
gi 568961011  705 QQ-ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14921   636 NAiPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
PTZ00014 PTZ00014
myosin-A; Provisional
71-791 1.67e-146

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 464.12  E-value: 1.67e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   71 DLTALSYLHEPAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAY-SGQNMGDMDPHIFAVAEEAYKQMA 149
Cdd:PTZ00014  100 DIGLLPHTNIPCVLDFLKHRY-LKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYrDAKDSDKLPPHVFTTARRALENLH 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  150 RNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDER 229
Cdd:PTZ00014  179 GVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEE 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  230 NQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYtrMGGNTV-IEGVNDRADMVETQK 308
Cdd:PTZ00014  259 GGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKY--INPKCLdVPGIDDVKDFEEVME 336
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTtvGNERSSVSE----DDSHLKVF---CELLGLETSKVAQWLCNRKIVTS 381
Cdd:PTZ00014  337 SFDSMGLSESQIEDIFSILSGVLLLGNVEIE--GKEEGGLTDaaaiSDESLEVFneaCELLFLDYESLKKELTVKVTYAG 414
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  382 SETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQ 461
Cdd:PTZ00014  415 NQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQK 494
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  462 QFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR 540
Cdd:PTZ00014  495 NFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGkSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKV 574
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  541 MSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGamitvksAKQVIkpntkhf 620
Cdd:PTZ00014  575 DSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKGKLA-------KGQLI------- 640
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  621 rttvGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYG 700
Cdd:PTZ00014  641 ----GSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFK 716
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  701 ILmtqqELSLS-----DKKEVCKVVLHRLIQDSNQYQFGRTKIFFR---AGQVAYLEKLRLDKLRQDCIMIQKHVRGWLQ 772
Cdd:PTZ00014  717 YL----DLAVSndsslDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKK 792
                         730
                  ....*....|....*....
gi 568961011  773 RRKFLRERQAALTIQRYFR 791
Cdd:PTZ00014  793 KRKVRKNIKSLVRIQAHLR 811
MYSc_Myh14_mammals cd14930
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...
82-741 5.14e-143

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: 449.93  E-value: 5.14e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14930     2 SVLHNLRERYY-SGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  162 ESGAGKTVSARYAMRYFATVSKSSSN-------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIG 234
Cdd:cd14930    81 ESGAGKTENTKKVIQYLAHVASSPKGrkepgvpGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  235 ANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTviEGVNDRADMVETQKTFTLLG 314
Cdd:cd14930   161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSS--SPGQERELFQETLESLRVLG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  315 FKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14930   239 FSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  395 INARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQE 473
Cdd:cd14930   319 DFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  474 EYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNfVNKNSLFEKPR--MSNSSFI 547
Cdd:cd14930   399 EYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQE-QGGHPKFQRPRhlRDQADFS 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  548 IQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFF----------QESPVPSSPFGAmitvksakqviKPNT 617
Cdd:cd14930   478 VLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvegivgleQVSSLGDGPPGG-----------RPRR 546
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  618 KHFRtTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYS 697
Cdd:cd14930   547 GMFR-TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQ 625
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*
gi 568961011  698 RYGILMTQQ-ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14930   626 RYEILTPNAiPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
83-739 1.29e-141

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: 445.83  E-value: 1.29e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   83 VLHNLRIRFAESkLIYTYSGIILVAMNPYKQLP-IYGDAIIHAY-SGQNMGDMDPHIFAVAEEAYK--QMARNNRNQSII 158
Cdd:cd14880     3 VLRCLQARYTAD-TFYTNAGCTLVALNPFKPVPqLYSPELMREYhAAPQPQKLKPHIFTVGEQTYRnvKSLIEPVNQSIV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  159 VSGESGAGKTVSARYAMRYFATVSKSSSN-------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQ 231
Cdd:cd14880    82 VSGESGAGKTWTSRCLMKFYAVVAASPTSweshkiaERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQ 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  232 IIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEgvndraDMVE-TQKTF 310
Cdd:cd14880   162 MTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNLEE------DCFEvTREAM 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  311 TLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSS---VSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVV- 386
Cdd:cd14880   236 LHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQQVf 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  387 -KPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHT-FIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFN 464
Cdd:cd14880   316 kKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTtFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFV 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  465 LHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSN 543
Cdd:cd14880   396 AHYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSpISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKLSR 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  544 S-SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvPSSPfgamitVKSAKQVIKPNTKHFRT 622
Cdd:cd14880   476 EpSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLF-----PANP------EEKTQEEPSGQSRAPVL 544
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  623 TVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL 702
Cdd:cd14880   545 TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLL 624
                         650       660       670
                  ....*....|....*....|....*....|....*..
gi 568961011  703 MTQQELSLSDKKEVCKVVLHrliqdSNQYQFGRTKIF 739
Cdd:cd14880   625 RRLRPHTSSGPHSPYPAKGL-----SEPVHCGRTKVF 656
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
81-741 1.52e-141

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: 447.48  E-value: 1.52e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDaiIHAYSGQNMGDMD--PHIFAVAEEAYKQMARNN------ 152
Cdd:cd14895     1 PAFVDYLAQRYGVDQ-VYCRSGAVLIAVNPFKHIPGLYD--LHKYREEMPGWTAlpPHVFSIAEGAYRSLRRRLhepgas 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  153 -RNQSIIVSGESGAGKTVSARYAMRYFATVSK--------SSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTE 223
Cdd:cd14895    78 kKNQTILVSGESGAGKTETTKFIMNYLAESSKhttatsssKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFVR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  224 ISF-----DERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFK--HLKLGSAEEFNYTRMGGNTVI-E 295
Cdd:cd14895   158 MFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLelQLELLSAQEFQYISGGQCYQRnD 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  296 GVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVqvtTVGNERSSVSEDDS---------------------H 354
Cdd:cd14895   238 GVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNV---LFVASSEDEGEEDNgaasapcrlasaspssltvqqH 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  355 LKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALhfSGKQHT----- 429
Cdd:cd14895   315 LDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSAS--PQRQFAlnpnk 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  430 --------FIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK- 500
Cdd:cd14895   393 aankdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRp 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  501 MGILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPRMSNS--SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEIL 578
Cdd:cd14895   473 SGIFSLLDEECVVPKGSDAGFARKLYQRLQE-HSNFSASRTDQAdvAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVL 551
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  579 -RASKFHLCAAFfqespvpsSPFGAmiTVKSAKQVIKPNTKHFRTT-----VGNKFRSSLYLLMETLNATTPHYVRCIKP 652
Cdd:cd14895   552 gKTSDAHLRELF--------EFFKA--SESAELSLGQPKLRRRSSVlssvgIGSQFKQQLASLLDVVQQTQTHYIRCIKP 621
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  653 NDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQ---ELSLSDKKEVCKVvlhrliqdsN 729
Cdd:cd14895   622 NDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKnasDATASALIETLKV---------D 692
                         730
                  ....*....|..
gi 568961011  730 QYQFGRTKIFFR 741
Cdd:cd14895   693 HAELGKTRVFLR 704
MYSc_Myh9 cd14919
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...
82-741 1.76e-141

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: 446.08  E-value: 1.76e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14919     2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  162 ESGAGKTVSARYAMRYFATVSKS----SSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANM 237
Cdd:cd14919    81 ESGAGKTENTKKVIQYLAHVASShkskKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  238 RTYLLEKSRVVFQSENERNYHIFYQLCASAQQsefkHLKLG-SAEEFNYTRM--GGNTVIEGVNDRADMVETQKTFTLLG 314
Cdd:cd14919   161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGE----HLKTDlLLEPYNKYRFlsNGHVTIPGQQDKDMFQETMEAMRIMG 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  315 FKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14919   237 IPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQA 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  395 INARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQE 473
Cdd:cd14919   317 DFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQE 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  474 EYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNfVNKNSLFEKPRM--SNSSFI 547
Cdd:cd14919   397 EYQREGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQE-QGTHPKFQKPKQlkDKADFC 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  548 IQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQE-SPVPSSPFGAMITVKSAKQVIKPNTKHFRtTVGN 626
Cdd:cd14919   476 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvDRIIGLDQVAGMSETALPGAFKTRKGMFR-TVGQ 554
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  627 KFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQ 706
Cdd:cd14919   555 LYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS 634
                         650       660       670
                  ....*....|....*....|....*....|....*.
gi 568961011  707 -ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14919   635 iPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
MYSc_Myh19 cd15896
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...
82-741 5.80e-140

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: 442.20  E-value: 5.80e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd15896     2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  162 ESGAGKTVSARYAMRYFATVSKS-----------SSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERN 230
Cdd:cd15896    81 ESGAGKTENTKKVIQYLAHVASShktkkdqnslaLSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  231 QIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLgsaEEFNYTRM--GGNTVIEGVNDRADMVETQK 308
Cdd:cd15896   161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLL---ENYNNYRFlsNGNVTIPGQQDKDLFTETME 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKP 388
Cdd:cd15896   238 AFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKA 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  389 MTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHV 467
Cdd:cd15896   318 QTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  468 FKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIE---AKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSN 543
Cdd:cd15896   398 FILEQEEYQREGIEWSFIDFgLDLQPCIDLIEkpaSPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKD 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  544 SS-FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQ--ESPVPSSPFGAMITVKSAkqvIKPNTKHF 620
Cdd:cd15896   478 EAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKdvDRIVGLDKVSGMSEMPGA---FKTRKGMF 554
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  621 RtTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYG 700
Cdd:cd15896   555 R-TVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 633
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 568961011  701 ILMTQQ-ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd15896   634 ILTPNAiPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
MYSc_Myo14 cd14876
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...
81-739 2.32e-139

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: 439.42  E-value: 2.32e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSG-QNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14876     1 PCVLDFLKHRYLKNQ-IYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  160 SGESGAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRT 239
Cdd:cd14876    80 SGESGAGKTEATKQIMRYFASAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYtrMGGNTV-IEGVNDRADMVETQKTFTLLGFKKD 318
Cdd:cd14876   160 FLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKF--LNPKCLdVPGIDDVADFEEVLESLKSMGLTEE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  319 FQMDVFKILAAILHLGNVQVTT-----VGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14876   238 QIDTVFSIVSGVLLLGNVKITGkteqgVDDAAAISNESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDD 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  394 AINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQE 473
Cdd:cd14876   318 AEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERESK 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  474 EYMKEDIPWTLIDFYDNQPVID-LIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSNSSFIIQHFA 552
Cdd:cd14876   398 LYKDEGIPTAELEYTSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKVDSNINFIVVHTI 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  553 DKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSpfgamitvKSAK-QVIkpntkhfrttvGNKFRSS 631
Cdd:cd14876   478 GDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKG--------KIAKgSLI-----------GSQFLKQ 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  632 LYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILmtqqELSLS 711
Cdd:cd14876   539 LESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFL----DLGIA 614
                         650       660       670
                  ....*....|....*....|....*....|...
gi 568961011  712 -DKKEVCKVVLHRLIQDSN----QYQFGRTKIF 739
Cdd:cd14876   615 nDKSLDPKVAALKLLESSGlsedEYAIGKTMVF 647
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
81-741 2.48e-139

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: 441.64  E-value: 2.48e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAY--------SGQNMGDMDPHIFAVAEEAYKQMARN 151
Cdd:cd14902     1 AALLQALSERF-EHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYkasmtstsPVSQLSELPPHVFAIGGKAFGGLLKP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  152 NR-NQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAHVED--------KVLASNPITEAVGNAKTTRNDNSSRFGKYT 222
Cdd:cd14902    80 ERrNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGsdaveigkRILQTNPILESFGNAQTIRNDNSSRFGKFI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  223 EISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEF----NYTRMGGNTVIEGVN 298
Cdd:cd14902   160 KIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYellnSYGPSFARKRAVADK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  299 DRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVS---EDDSHLKVFCELLGLETSKVAQWLCN 375
Cdd:cd14902   240 YAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAvtaASRFHLAKCAELMGVDVDKLETLLSS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  376 RKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQAL-HFSGKQH--------TFIGVLDIYGFETFDVNS 446
Cdd:cd14902   320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEInYFDSAVSisdedeelATIGILDIFGFESLNRNG 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  447 FEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKL 525
Cdd:cd14902   400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSnGLFSLLDQECLMPKGSNQALSTKF 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  526 YNNFVNKNslfekprmsnsSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSpfgamiT 605
Cdd:cd14902   480 YRYHGGLG-----------QFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRDSP------G 542
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  606 VKSAKQVIKPNTKHFRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQS 685
Cdd:cd14902   543 ADNGAAGRRRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHG 622
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  686 YPSRWTYLEFYSRYGILMTQQELSLSDKK-------------EVCKVVLHRLIQDSNQ---------------------- 730
Cdd:cd14902   623 YSVRLAHASFIELFSGFKCFLSTRDRAAKmnnhdlaqalvtvLMDRVLLEDGVEREEKnpgaltavtgdgsgtafendcr 702
                         730
                  ....*....|....
gi 568961011  731 ---YQFGRTKIFFR 741
Cdd:cd14902   703 rkdVQVGRTLVFCK 716
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
83-734 1.29e-135

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: 431.71  E-value: 1.29e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   83 VLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQN-MGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14906     3 ILNNLGKRY-KSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINqNKSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  161 GESGAGKTVSARYAMRYFATVSKSSS---------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQ 231
Cdd:cd14906    82 GESGSGKTEASKTILQYLINTSSSNQqqnnnnnnnNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSDG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  232 II-GANMRTYLLEKSRVVFQSENER-NYHIFYQLCASAQQSEFKHLKLGS-AEEFNY-------------TRMGGNTVIE 295
Cdd:cd14906   162 KIdGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLNNdPSKYRYldarddvissfksQSSNKNSNHN 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  296 GVNDRADMVETQKTFTL-LGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVF---CELLGLETSKVAQ 371
Cdd:cd14906   242 NKTESIESFQLLKQSMEsMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLesvSKLLGYIESVFKQ 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  372 WLCNRKIVTSSETVV--KPMTRPQAINARDALAKKIYAHLFDFIVEQINQ-----------ALHFSGKQHTFIGVLDIYG 438
Cdd:cd14906   322 ALLNRNLKAGGRGSVycRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRkfnqntqsndlAGGSNKKNNLFIGVLDIFG 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  439 FETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGT 517
Cdd:cd14906   402 FENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKsDGILSLLDDECIMPKGS 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  518 DENWLQKLYNNFVNKNSLFEKPrMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQEspvps 597
Cdd:cd14906   482 EQSLLEKYNKQYHNTNQYYQRT-LAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQ----- 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  598 spfgamitvksaKQVIKPNTKHFRT---TVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACG 674
Cdd:cd14906   556 ------------QITSTTNTTKKQTqsnTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVG 623
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  675 VLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSlSDKKEVCKVVLHRLIQDSNQYQFG 734
Cdd:cd14906   624 VLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRK-NNNNPKLASQLILQNIQSKLKTMG 682
MYSc_Myo25 cd14886
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...
83-741 5.66e-135

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: 427.77  E-value: 5.66e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMG-----DMDPHIFAVAEEAYKQMARNNRNQS 156
Cdd:cd14886     3 VIDILRDRFAKDK-IYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  157 IIVSGESGAGKTVSARYAMRYFATVSKSSSNAhVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGAN 236
Cdd:cd14886    82 CIVSGESGAGKTETAKQLMNFFAYGHSTSSTD-VQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  237 MRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFK 316
Cdd:cd14886   161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKLFSK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  317 KDFQmDVFKILAAILHLGNVQ---VTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14886   241 NEID-SFYKCISGILLAGNIEfseEGDMGVINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQ 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  394 AINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQE 473
Cdd:cd14886   320 AEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEIQ 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  474 EYMKEDIPWTLIDFYDNQPVIDLIEA-KMGILELLDEECLLPHGTDENWLQKLYNNFvnKNSLFEKPRMSNSSFIIQHFA 552
Cdd:cd14886   400 EYEIEGIDHSMITFTDNSNVLAVFDKpNLSIFSFLEEQCLIQTGSSEKFTSSCKSKI--KNNSFIPGKGSQCNFTIVHTA 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  553 DKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSspfgamitvksakqvikPNTKHfrTTVGNKFRSSL 632
Cdd:cd14886   478 ATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNED-----------------GNMKG--KFLGSTFQLSI 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  633 YLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSL-- 710
Cdd:cd14886   539 DQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILISHNSSSQna 618
                         650       660       670
                  ....*....|....*....|....*....|..
gi 568961011  711 -SDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14886   619 gEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
83-702 1.88e-131

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: 417.79  E-value: 1.88e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAY---------SGQNMGD--MDPHIFAVAEEAYKQMAR 150
Cdd:cd14900     3 ILSALETRFYAQK-IYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssSTRNKGSdpMPPHIYQVAGEAYKAMML 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  151 --NNR--NQSIIVSGESGAGKTVSARYAMRYFA---------TVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSR 217
Cdd:cd14900    82 glNGVmsDQSILVSGESGSGKTESTKFLMEYLAqagdnnlaaSVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  218 FGKYTEISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKhlklgsaeEFNYTRMggntviegv 297
Cdd:cd14900   162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK--------RDMYRRV--------- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  298 NDRADMVetqktftllGFKKDFQMDVFKILAAILHLGNV--QVTTVGNERSSvseDDSHLKVFCE--------LLGLETS 367
Cdd:cd14900   225 MDAMDII---------GFTPHERAGIFDLLAALLHIGNLtfEHDENSDRLGQ---LKSDLAPSSIwsrdaaatLLSVDAT 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  368 KVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHF--SGKQHT---FIGVLDIYGFETF 442
Cdd:cd14900   293 KLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMddSSKSHGglhFIGILDIFGFEVF 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  443 DVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENW 521
Cdd:cd14900   373 PKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRpTGILSLIDEECVMPKGSDTTL 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  522 LQKLYNNFVNkNSLFEKPRMSNSS--FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRAskfhlcaaffqespvpssp 599
Cdd:cd14900   453 ASKLYRACGS-HPRFSASRIQRARglFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVY------------------- 512
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  600 fgamitvksakqvikpntkhfrttvGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETI 679
Cdd:cd14900   513 -------------------------GLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAV 567
                         650       660
                  ....*....|....*....|...
gi 568961011  680 RISAQSYPSRWTYLEFYSRYGIL 702
Cdd:cd14900   568 RVARAGFPIRLLHDEFVARYFSL 590
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
81-741 5.67e-130

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: 414.56  E-value: 5.67e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14896     1 SSVLLCLKKRF-HLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  161 GESGAGKTVSARYAMRYFATVSKSSSNAHVE--DKVLasnPITEAVGNAKTTRNDNSSRFGKYTEISFdERNQIIGANMR 238
Cdd:cd14896    80 GHSGSGKTEAAKKIVQFLSSLYQDQTEDRLRqpEDVL---PILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  239 TYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKD 318
Cdd:cd14896   156 HYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  319 FQMDVFKILAAILHLGNVQVTTVGNERSSVSE--DDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAIN 396
Cdd:cd14896   236 ELTAIWAVLAAILQLGNICFSSSERESQEVAAvsSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAID 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  397 ARDALAKKIYAHLFDFIVEQINQALHFSGKQHTF--IGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEE 474
Cdd:cd14896   316 ARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEEE 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  475 YMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPRMSNSSFIIQHFAD 553
Cdd:cd14896   396 CQRELLPWVPIPQPPRESCLDLLVDQpHSLLSILDDQTWLSQATDHTFLQKCHYHHGD-HPSYAKPQLPLPVFTVRHYAG 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  554 KVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESpvpsspfgamitvkSAKQVIKPNtkhfRTTVGNKFRSSLY 633
Cdd:cd14896   475 TVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEA--------------EPQYGLGQG----KPTLASRFQQSLG 536
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  634 LLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSDK 713
Cdd:cd14896   537 DLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEALSDR 616
                         650       660
                  ....*....|....*....|....*...
gi 568961011  714 KEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14896   617 ERCGAILSQVLGAESPLYHLGATKVLLK 644
MYSc_Myo38 cd14899
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...
82-699 8.80e-117

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: 381.37  E-value: 8.80e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYS---GQNMGDM-------DPHIFAVAEEAYKQMAR 150
Cdd:cd14899     2 SILNALRLRY-ERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhNSQFGDRvtstdprEPHLFAVARAAYIDIVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  151 NNRNQSIIVSGESGAGKTVSARYAMRYFATVS----------------KSSSNAHVEDKVLASNPITEAVGNAKTTRNDN 214
Cdd:cd14899    81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCgtgnnnltnsesisppASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  215 SSRFGKYTEISF-DERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQL------CASAQQSEFKHLKLGSAEEFNYTR 287
Cdd:cd14899   161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELlsadnnCVSKEQKQVLALSGGPQSFRLLNQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  288 MGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNER------------SSVSEDDSHL 355
Cdd:cd14899   241 SLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKGddtvfadearvmSSTTGAFDHF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  356 KVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGK--------- 426
Cdd:cd14899   321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASapwgadesd 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  427 ------QHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK 500
Cdd:cd14899   401 vddeedATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELFEHR 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  501 -MGILELLDEECLLPHGTDENWLQKLYNNFVNKNslfEKPRMSNSS-------FIIQHFADKVEYQCEGFLEKNRDTVYD 572
Cdd:cd14899   481 pIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKN---SHPHFRSAPliqrttqFVVAHYAGCVTYTIDGFLAKNKDSFCE 557
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  573 MLVEILRASKFHLCAAFFQESPVPSSPFGAMITVKSAKQVIKPNTKHFRTTVGNKFRSSLYLLMETLNATTPHYVRCIKP 652
Cdd:cd14899   558 SAAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIKP 637
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*..
gi 568961011  653 NDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRY 699
Cdd:cd14899   638 NDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
83-741 7.18e-113

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: 369.14  E-value: 7.18e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   83 VLHNLRIRFAESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAY-SGQNMGDMDPHIFAVAEEAYKQM-ARNNRNQSIIVS 160
Cdd:cd14875     3 LLHCIKERFEKLHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVVIS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  161 GESGAGKTVSARYAMRYFATVS----KSSSNAHVEDKVLA----SNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQI 232
Cdd:cd14875    83 GESGSGKTENAKMLIAYLGQLSymhsSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPTSGV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  233 -IGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHL-KLGSAEEFNYTRmGGNTVI------EGVNDRADMV 304
Cdd:cd14875   163 mVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLN-GGNTFVrrgvdgKTLDDAHEFQ 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  305 ETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVsEDDSHLKVFCELLGLETSKVAQWLcnrkIVTSSET 384
Cdd:cd14875   242 NVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQI-ADETPFLTACRLLQLDPAKLRECF----LVKSKTS 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  385 VVKPMTRPQ-AINARDALAKKIYAHLFDFIVEQINQALHFSG--KQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQ 461
Cdd:cd14875   317 LVTILANKTeAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGdcSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  462 QFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR 540
Cdd:cd14875   397 HYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKrTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPYFVLPK 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  541 MS-NSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASkfhlcAAFFQESPVPSSPFGAmitvksakqvikpntkH 619
Cdd:cd14875   477 STiPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNS-----TDEFIRTLLSTEKGLA----------------R 535
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  620 FRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRY 699
Cdd:cd14875   536 RKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYF 615
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*....
gi 568961011  700 GILMTQQELSL---SDKKEVCKVVL---HRLIQ-DSNQYQFGRTKIFFR 741
Cdd:cd14875   616 YLIMPRSTASLfkqEKYSEAAKDFLayyQRLYGwAKPNYAVGKTKVFLR 664
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
82-740 4.93e-112

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: 366.10  E-value: 4.93e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   82 AVLHNLRIRFAESkLIYTY-SGIILVAMNPYKQLPIYGDAIIHAY-------SGQNMGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14879     5 AITSHLASRFRSD-LPYTRlGSSALVAVNPYKYLSSNSDASLGEYgseyydtTSGSKEPLPPHAYDLAARAYLRMRRRSE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  154 NQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAH-VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQI 232
Cdd:cd14879    84 DQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKKGTkLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNERGRL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  233 IGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYT-RMGGNTVIEGV--NDRADMVETQKT 309
Cdd:cd14879   164 IGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLaSYGCHPLPLGPgsDDAEGFQELKTA 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  310 FTLLGFKKDFQMDVFKILAAILHLGNVQVTT--VGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNR-KIVtSSEtVV 386
Cdd:cd14879   244 LKTLGFKRKHVAQICQLLAAILHLGNLEFTYdhEGGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTYKtKLV-RKE-LC 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  387 KPMTRP-QAINARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFD---VNSFEQFCINYANEKLQQ 461
Cdd:cd14879   322 TVFLDPeGAAAQRDELARTLYSLLFAWVVETINQKLCAPEDDfATFISLLDFPGFQNRSstgGNSLDQFCVNFANERLHN 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  462 QFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMG--ILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKP 539
Cdd:cd14879   402 YVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKPGglLGILDDQTRRMPKKTDEQMLEALRKRFGNHSSFIAVG 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  540 RMS----NSSFIIQHFADKVEYQCEGFLEKNRDtvydmlveilraskfHLCAAFfqespvpsspfgaMITVKSAKQvikp 615
Cdd:cd14879   482 NFAtrsgSASFTVNHYAGEVTYSVEGFLERNGD---------------VLSPDF-------------VNLLRGATQ---- 529
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  616 ntkhfrttvgnkFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEF 695
Cdd:cd14879   530 ------------LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEF 597
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*
gi 568961011  696 YSRYGILMTQQELSLSDKKevckvVLHRLIQDSNQYQFGRTKIFF 740
Cdd:cd14879   598 CERYKSTLRGSAAERIRQC-----ARANGWWEGRDYVLGNTKVFL 637
MYSc_Myo37 cd14898
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...
82-702 9.59e-109

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: 354.97  E-value: 9.59e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQlpIYGDAIIHAYSgQNMGDMDPHIFAVAEEAYKQMARNNrNQSIIVSG 161
Cdd:cd14898     2 ATLEILEKRYASGK-IYTKSGLVFLALNPYET--IYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVHG-NQTIVISG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  162 ESGAGKTVSARYAMRYFatVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDerNQIIGANMRTYL 241
Cdd:cd14898    77 ESGSGKTENAKLVIKYL--VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETYL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  242 LEKSRVVFQSENERNYHIFYQLCASAqqsefkhlKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKdFQm 321
Cdd:cd14898   153 LEKSRVTHHEKGERNFHIFYQFCASK--------RLNIKNDFIDTSSTAGNKESIVQLSEKYKMTCSAMKSLGIAN-FK- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  322 DVFKILAAILHLGNVQVTtvgNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDAL 401
Cdd:cd14898   223 SIEDCLLGILYLGSIQFV---NDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIRNSM 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  402 AKKIYAHLFDFIVEQINQALHFSGKQHtfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIP 481
Cdd:cd14898   300 ARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEEGIE 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  482 WTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKL--YNN-FVNKNslfekprmSNSSFIIQHFADKVEYQ 558
Cdd:cd14898   378 WPDVEFFDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIkkYLNgFINTK--------ARDKIKVSHYAGDVEYD 449
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  559 CEGFLEKNRDtvydmlveilrasKFHLcaaffqespvpsSPFGAMITvksakqvikpNTKHFRTTVGNKFRSSLYLLMET 638
Cdd:cd14898   450 LRDFLDKNRE-------------KGQL------------LIFKNLLI----------NDEGSKEDLVKYFKDSMNKLLNS 494
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961011  639 LNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL 702
Cdd:cd14898   495 INETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRIL 558
MYSc_Myo26 cd14887
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...
81-741 5.17e-102

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: 341.24  E-value: 5.17e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFAES-------KLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14887     1 PNLLENLYQRYNKAyinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  154 NQSIIVSGESGAGKTVSARYAMRYFATVS---KSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERN 230
Cdd:cd14887    81 SQSILISGESGAGKTETSKHVLTYLAAVSdrrHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  231 QIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSefKHLKLGSAEEFNYTrmggntviegvndrADMVETQKTF 310
Cdd:cd14887   161 KLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAA--ATQKSSAGEGDPES--------------TDLRRITAAM 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  311 TLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLC---NRKIVTSSETVVK 387
Cdd:cd14887   225 KTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSVSVGCEETAADRSHSSEVKClssGLKVTEASRKHLK 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  388 PMTRP--------------------------------QAINARDALAKKIYAHLFDFIVEQINQALHFSGK--------- 426
Cdd:cd14887   305 TVARLlglppgvegeemlrlalvsrsvretrsffdldGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsded 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  427 -----QHTFIGVLDIYGFETF---DVNSFEQFCINYANEKlqqqfnLHVFKLEQ----EE--YMKEDIPWTLIDFYDNQP 492
Cdd:cd14887   385 tpsttGTQTIGILDLFGFEDLrnhSKNRLEQLCINYANER------LHCFLLEQlilnEHmlYTQEGVFQNQDCSAFPFS 458
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  493 -------------VIDLI-EAKMGILELLDEECLLPH----------GTDENW------------LQKLYNNFVNKNSLF 536
Cdd:cd14887   459 fplastltsspssTSPFSpTPSFRSSSAFATSPSLPSslsslssslsSSPPVWegrdnsdlfyekLNKNIINSAKYKNIT 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  537 EKPRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRAskfhlCAAFFQESPVPSSPFGAMITVKsakqvikpn 616
Cdd:cd14887   539 PALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLA-----CSTYTRLVGSKKNSGVRAISSR--------- 604
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  617 tkhfRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFY 696
Cdd:cd14887   605 ----RSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELW 680
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....*
gi 568961011  697 SRYGILMTQQELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14887   681 RRYETKLPMALREALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
MYSc_Myo24A cd14937
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
83-741 4.32e-98

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: 327.74  E-value: 4.32e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   83 VLHNLRIRFaESKLIYTYSGIILVAMNPYKQLpiygDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd14937     3 VLNMLALRY-KKNYIYTIAEPMLISINPYQVI----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  163 SGAGKTVSARYAMRYFatVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLL 242
Cdd:cd14937    78 SGSGKTEASKLVIKYY--LSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  243 EKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTrMGGNTVIEGVNDRADMVETQKTFTLLGFKkDFQMD 322
Cdd:cd14937   156 ENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYI-VNKNVVIPEIDDAKDFGNLMISFDKMNMH-DMKDD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  323 VFKILAAILHLGNVQVTTV-GNERSSVSE-DDSHLKVFCE---LLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINA 397
Cdd:cd14937   234 LFLTLSGLLLLGNVEYQEIeKGGKTNCSElDKNNLELVNEisnLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESVSI 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  398 RDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMK 477
Cdd:cd14937   314 CKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETELYKA 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  478 EDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENwLQKLYNNFVNKNSLFEKPRMS-NSSFIIQHFADKVE 556
Cdd:cd14937   394 EDILIESVKYTTNESIIDLLRGKTSIISILEDSCLGPVKNDES-IVSVYTNKFSKHEKYASTKKDiNKNFVIKHTVSDVT 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  557 YQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSpfgamitvksakqVIKPNTKHFrttvgnKFRSSLYLLM 636
Cdd:cd14937   473 YTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSES-------------LGRKNLITF------KYLKNLNNII 533
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  637 ETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAqSYPSRWTYLEFYSRYGIL--MTQQELSLSDKK 714
Cdd:cd14937   534 SYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNISF-FFQYKYTFDVFLSYFEYLdySTSKDSSLTDKE 612
                         650       660
                  ....*....|....*....|....*..
gi 568961011  715 EVCKVVLHRLiqDSNQYQFGRTKIFFR 741
Cdd:cd14937   613 KVSMILQNTV--DPDLYKVGKTMVFLK 637
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
82-741 4.90e-95

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: 319.84  E-value: 4.90e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAY---SGQNMGDMDPHIFAVAEEAYKQMARNNRNQSII 158
Cdd:cd14878     2 SLLYEIQKRFGNNQ-IYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  159 VSGESGAGKTVSARYAMRYFATVSKSSSNAhVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISF-DERNQIIGANM 237
Cdd:cd14878    81 LSGERGSGKTEASKQIMKHLTCRASSSRTT-FDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  238 RTYLLEKSRVVFQSENERNYHIFYQLC--ASAQQSEFKHLKLGSAEEF-NYTRMGGNTVIEGVNDRADMVETQKTFTLLG 314
Cdd:cd14878   160 YTYMLEKSRLVSQPPGQSNFLIFYLLMdgLSAEEKYGLHLNNLCAHRYlNQTMREDVSTAERSLNREKLAVLKQALNVVG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  315 FKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14878   240 FSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIA 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  395 INARDALAKKIYAHLFDFIVEQINQALH----FSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKL 470
Cdd:cd14878   320 EFYRDLLAKSLYSRLFSFLVNTVNCCLQsqdeQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQ 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  471 EQEEYMKEDIPWTLIDFYDNQP-VIDLIEAK-MGILELLDEECLLPHGTDENWLQKL--YNNFVNKNSLFEK-------- 538
Cdd:cd14878   400 EQTECVQEGVTMETAYSPGNQTgVLDFFFQKpSGFLSLLDEESQMIWSVEPNLPKKLqsLLESSNTNAVYSPmkdgngnv 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  539 -PRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESpvpsspfgamitvksakqvikpnt 617
Cdd:cd14878   480 aLKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSK------------------------ 535
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  618 khfRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYS 697
Cdd:cd14878   536 ---LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLS 612
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*....
gi 568961011  698 RYGILMtqqELSLSDKK-----EVCKVVLHRLIQDSnqYQFGRTKIFFR 741
Cdd:cd14878   613 RYKPLA---DTLLGEKKkqsaeERCRLVLQQCKLQG--WQMGVRKVFLK 656
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
82-740 1.15e-91

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: 309.74  E-value: 1.15e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   82 AVLHNLRIRFAESKLiYTYSGIILVAMNPYKQLPiygdAIIHAYSGQNMGDMdPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14881     2 AVMKCLQARFYAKEF-FTNVGPILLSVNPYRDVG----NPLTLTSTRSSPLA-PQLLKVVQEAVRQQSETGYPQAIILSG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  162 ESGAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDErnqiiGANMRT-- 239
Cdd:cd14881    76 TSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-----GALYRTki 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  240 --YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKT-FTLLGFK 316
Cdd:cd14881   151 hcYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKAcLGILGIP 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  317 kdFqMDVFKILAAILHLGNVQVTTvGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAIN 396
Cdd:cd14881   231 --F-LDVVRVLAAVLLLGNVQFID-GGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKSVCDANMSNM 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  397 ARDALAKKIYAHLFDFIVEQIN--QALHFSGKQHT---FIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLE 471
Cdd:cd14881   307 TRDALAKALYCRTVATIVRRANslKRLGSTLGTHAtdgFIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNTHIFKSS 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  472 QEEYMKEDIPWTL-IDFYDNQPVIDLIEA-KMGILELLDEECLlPHGTDENWLQKLYNNFVNKNSLFEKPRMSNSSFIIQ 549
Cdd:cd14881   387 IESCRDEGIQCEVeVDYVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLFEAKPQDDRMFGIR 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  550 HFADKVEYQCEGFLEKNRDTVYDMLVEILRAskfHLCAaffqespvpsspFGamitvksakqvIKPNTKHFRTTVGNkfr 629
Cdd:cd14881   466 HFAGRVVYDASDFLDTNRDVVPDDLVAVFYK---QNCN------------FG-----------FATHTQDFHTRLDN--- 516
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  630 sslylLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELS 709
Cdd:cd14881   517 -----LLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLR 591
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|.
gi 568961011  710 LSDKKEV--CKVVL-----HRLIQDSN---QYQFGRTKIFF 740
Cdd:cd14881   592 RVEEKALedCALILqfleaQPPSKLSSvstSWALGKRHIFL 632
MYSc_Myo23 cd14884
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ...
81-732 1.50e-89

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: 305.29  E-value: 1.50e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYS-------GQNMGDMDPHIFAVAEEAYKQMARNN 152
Cdd:cd14884     1 PNVLQNLKNRYLKNK-IYTFHASLLLALNPYKPLKeLYDQDVMNVYLhkksnsaASAAPFPKAHIYDIANMAYKNMRGKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  153 RNQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQI 232
Cdd:cd14884    80 KRQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEVENT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  233 I---------GANMRTYLLEKSRVVFQSENERNYHIFYQL---CASAQQSE------FKHLKLGSAEEFNYTR-MGGNTV 293
Cdd:cd14884   160 QknmfngcfrNIKIKILLLEINRCIAHNFGERNFHVFYQVlrgLSDEDLARrnlvrnCGVYGLLNPDESHQKRsVKGTLR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  294 IEGVNDRADMVETQK---TFTLL-------GFKKDFQMDVFKILAAILHLGNvqvttvgnerssvseddSHLKVFCELLG 363
Cdd:cd14884   240 LGSDSLDPSEEEKAKdekNFVALlhglhyiKYDERQINEFFDIIAGILHLGN-----------------RAYKAAAECLQ 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  364 LETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQAlHFSGKQ-------------HTF 430
Cdd:cd14884   303 IEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRN-VLKCKEkdesdnediysinEAI 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  431 IGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEE 510
Cdd:cd14884   382 ISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAKIFRRLDDITKL 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  511 CLLPHG-TDENWLQKLYNNfVNKNSLFEK-------PRMSNSS----------FIIQHFADKVEYQCEGFLEKNRDTVYD 572
Cdd:cd14884   462 KNQGQKkTDDHFFRYLLNN-ERQQQLEGKvsygfvlNHDADGTakkqnikkniFFIRHYAGLVTYRINNWIDKNSDKIET 540
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  573 MLVEILRASKfhlcaaffqespvpsspfgaMITVKSAkqVIKPNTKHFrTTVGNKFRSSLYLLMETLNATTPHYVRCIKP 652
Cdd:cd14884   541 SIETLISCSS--------------------NRFLREA--NNGGNKGNF-LSVSKKYIKELDNLFTQLQSTDMYYIRCFLP 597
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  653 NDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRwtylefysrygilMTQQELSLSDKKEVCKVVLHRLIQDSNQYQ 732
Cdd:cd14884   598 NAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHK-------------IPKKETAAALKEQIAKELEKCNSNTDIEYQ 664
MYSc_Myo18 cd01386
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...
83-741 4.64e-87

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: 298.45  E-value: 4.64e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   83 VLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd01386     3 VLHTLRQRYG-ANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  163 SGAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLL 242
Cdd:cd01386    82 SGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  243 EKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRA-DMVETQKTFTLLGFKKDFQM 321
Cdd:cd01386   162 ERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKQKAAaAFSKLQAAMKTLGISEEEQR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  322 DVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRK---IVTSSETVVKPMTRPQ----- 393
Cdd:cd01386   242 AIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHHlsgGPQQSTTSSGQESPARsssgg 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  394 ----AINARDALAKKIYAHLFDFIVEQINQALhfSGKQHTF--IGVLDIYGFEtfdvN----------SFEQFCINYANE 457
Cdd:cd01386   322 pkltGVEALEGFAAGLYSELFAAVVSLINRSL--SSSHHSTssITIVDTPGFQ----NpahsgsqrgaTFEDLCHNYAQE 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  458 KLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDN-QPVIDLI---------------EAKMGILELLDEECLLPHGTDENW 521
Cdd:cd01386   396 RLQLLFHERTFVAPLERYKQENVEVDFDLPELSpGALVALIdqapqqalvrsdlrdEDRRGLLWLLDEEALYPGSSDDTF 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  522 LQKLYNNF----VNKNSLFEKPRMSNSSFIIQHF--ADKVEYQCEGFLeknrdtvydmlveilRASKFHLCA----AFFQ 591
Cdd:cd01386   476 LERLFSHYgdkeGGKGHSLLRRSEGPLQFVLGHLlgTNPVEYDVSGWL---------------KAAKENPSAqnatQLLQ 540
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  592 ESpvpSSPFGAmitVKsakqvikpntkhfRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPN------DEKMPFEFDSKR 665
Cdd:cd01386   541 ES---QKETAA---VK-------------RKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagkdERSTSSPAAGDE 601
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  666 IVQ------QLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSDKKEVC--KVVLHRLIQ----DSNQYQF 733
Cdd:cd01386   602 LLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGLNSEVAdeRKAVEELLEeldlEKSSYRI 681

                  ....*...
gi 568961011  734 GRTKIFFR 741
Cdd:cd01386   682 GLSQVFFR 689
MYSc_Myo44 cd14905
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...
93-741 3.91e-81

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: 281.21  E-value: 3.91e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   93 ESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSgQNMGdMDPHIFAVAEEAYKQMARNNRNQSIIVSGESGAGKTVSA 171
Cdd:cd14905    12 KKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN-QRRG-LPPHLFALAAKAISDMQDFRRDQLIFIGGESGSGKSENT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  172 RYAMRYFATVSKSSSNaHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLLEKSRVVFQS 251
Cdd:cd14905    90 KIIIQYLLTTDLSRSK-YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQN 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  252 ENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAIL 331
Cdd:cd14905   169 KGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFII 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  332 HLGNVQVTTvGNERSSVsEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSEtvvkpmtrpqAINARDALAKKIYAHLFD 411
Cdd:cd14905   249 ILGNVTFFQ-KNGKTEV-KDRTLIESLSHNITFDSTKLENILISDRSMPVNE----------AVENRDSLARSLYSALFH 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  412 FIVEQINQALHFSGKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPW-TLIDFYDN 490
Cdd:cd14905   317 WIIDFLNSKLKPTQYSHT-LGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQTERIPWmTPISFKDN 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  491 QPVIDLIEAKMGILELLDEECllpHGTDENWLQKLyNNFVNKNSLF-EKPrmsnSSFIIQHFADKVEYQCEGFLEKNRDT 569
Cdd:cd14905   396 EESVEMMEKIINLLDQESKNI---NSSDQIFLEKL-QNFLSRHHLFgKKP----NKFGIEHYFGQFYYDVRGFIIKNRDE 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  570 VYDML-----------------VEILRASKFHLCAAFFQESPVPSSPFGAMITVKSA-----KQVIKPNTKH------FR 621
Cdd:cd14905   468 ILQRTnvlhknsitkylfsrdgVFNINATVAELNQMFDAKNTAKKSPLSIVKVLLSCgsnnpNNVNNPNNNSggggggGN 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  622 TTVGNKFRSSLYLLMETLNATTP------HYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEF 695
Cdd:cd14905   548 SGGGSGSGGSTYTTYSSTNKAINnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIF 627
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*...
gi 568961011  696 YSRYGILMTQQE--LSLSDKKEVCKVVLHRLIQDSnqYQFGRTKIFFR 741
Cdd:cd14905   628 FDRFSFFFQNQRnfQNLFEKLKENDINIDSILPPP--IQVGNTKIFLR 673
MYSc_Myo12 cd14874
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...
82-741 9.37e-79

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: 272.90  E-value: 9.37e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYsgqnmgdmdpHIFAVAEEAYKQMARNNRN-QSIIVS 160
Cdd:cd14874     2 GIAQNLHERF-KKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  161 GESGAGKTVSARYAMRYFATVSKSS-SNAHVEdkvlASNPITEAVGNAKTTRNDNSSRFGKYTEISFdERNQIIGANMR- 238
Cdd:cd14874    71 GESGSGKSYNAFQVFKYLTSQPKSKvTTKHSS----AIESVFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLTGLNLKy 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  239 TYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNT--VIEGVNDRADMVETQKTftlLGFK 316
Cdd:cd14874   146 TVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTenIQSDVNHFKHLEDALHV---LGFS 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  317 KDFQMDVFKILAAILHLGNVQVTTVGNerSSVSED------DSHLKVFCELLGLEtskVAQWLcnrKIVTSSETVVKPMT 390
Cdd:cd14874   223 DDHCISIYKIISTILHIGNIYFRTKRN--PNVEQDvveignMSEVKWVAFLLEVD---FDQLV---NFLLPKSEDGTTID 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  391 RPQAINARDALAKKIYAHLFDFIVEQInqALHFSGKQHT-FIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFK 469
Cdd:cd14874   295 LNAALDNRDSFAMLIYEELFKWVLNRI--GLHLKCPLHTgVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFH 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  470 LEQEEYMKEDIPwtlIDF-----YDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNKnSLFEKPRMSN 543
Cdd:cd14874   373 DQLVDYAKDGIS---VDYkvpnsIENGKTVELLFKKpYGLLPLLTDECKFPKGSHESYLEHCNLNHTDR-SSYGKARNKE 448
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  544 S-SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQespvpSSPFGAMITVKSAKQVIKPNTKHfrt 622
Cdd:cd14874   449 RlEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE-----SYSSNTSDMIVSQAQFILRGAQE--- 520
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  623 tvgnkfrsslylLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL 702
Cdd:cd14874   521 ------------IADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|
gi 568961011  703 MTQQELSLSDKKEVCKVVLH-RLIQDSNQYQFGRTKIFFR 741
Cdd:cd14874   589 LPGDIAMCQNEKEIIQDILQgQGVKYENDFKIGTEYVFLR 628
MYSc_Myo21 cd14882
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...
83-741 1.37e-77

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: 270.07  E-value: 1.37e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   83 VLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd14882     3 ILEELRHRY-LMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  163 SGAGKTVSARYAMRYFATVSKSSSNahVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLL 242
Cdd:cd14882    82 SYSGKTTNARLLIKHLCYLGDGNRG--ATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  243 EKSRVVFQSENERNYHIFYQLCASAQQSE-FKHLKLGSAEEFNYTRMGGNTVIEGV----NDRADMVETQKTFTLLGFKK 317
Cdd:cd14882   160 EKLRVSTTDGNQSNFHIFYYFYDFIEAQNrLKEYNLKAGRNYRYLRIPPEVPPSKLkyrrDDPEGNVERYKEFEEILKDL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  318 DFQMD----VFKILAAILHLGNVQVttVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14882   240 DFNEEqletVRKVLAAILNLGEIRF--RQNGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRKHTTEE 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  394 AINARDALAKKIYAHLFDFIVEQINQALHFS----GKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFK 469
Cdd:cd14882   318 ARDARDVLASTLYSRLVDWIINRINMKMSFPravfGDKYS-ISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHYNQRIFI 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  470 LEQEEYMKEDIPWTLIDFYDNQPVID-LIEAKMGILELLDEECLLPHGTdenwlQKLYNNFVNKNSLFEKPrMSNSSFII 548
Cdd:cd14882   397 SEMLEMEEEDIPTINLRFYDNKTAVDqLMTKPDGLFYIIDDASRSCQDQ-----NYIMDRIKEKHSQFVKK-HSAHEFSV 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  549 QHFADKVEYQCEGFLEKNRDTVYDMLVEILRASkfhlcaaffqespvpsspfgamiTVKSAKQVIKPNTKHFRTTVGNKF 628
Cdd:cd14882   471 AHYTGRIIYDAREFADKNRDFVPPEMIETMRSS-----------------------LDESVKLMFTNSQVRNMRTLAATF 527
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  629 RSSLYLLMETL----NATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMT 704
Cdd:cd14882   528 RATSLELLKMLsigaNSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLAF 607
                         650       660       670
                  ....*....|....*....|....*....|....*..
gi 568961011  705 QQELSLSDKKEVCKVVLHRLIQDSnqYQFGRTKIFFR 741
Cdd:cd14882   608 DFDETVEMTKDNCRLLLIRLKMEG--WAIGKTKVFLK 642
MYSc_Myo32 cd14893
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...
84-699 3.43e-66

class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276858  Cd Length: 741  Bit Score: 239.49  E-value: 3.43e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   84 LHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQN----------MGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14893     4 LYTLRARYRMEQ-VYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSReqtplyekdtVNDAPPHVFALAQNALRCMQDAGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  154 NQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAH-----------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYT 222
Cdd:cd14893    83 DQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPdsegasgvlhpIGQQILHAFTILEAFGNAATRQNRNSSRFAKMI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  223 EISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQ--SEFKHLKLG-SAEEFNYTRMGGNTVIEGVND 299
Cdd:cd14893   163 SVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdpTLRDSLEMNkCVNEFVMLKQADPLATNFALD 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  300 RADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQV---------------TTVGNERSSVSEDDSHLKVFCELLGL 364
Cdd:cd14893   243 ARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggksvggansTTVSDAQSCALKDPAQILLAAKLLEV 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  365 ETSKVAQWLCNRKIVT--SSETV--VKPMTRPQAINARDALAKKIYAHLFDFIVEQINQAL-----HFSGK----QHTFI 431
Cdd:cd14893   323 EPVVLDNYFRTRQFFSkdGNKTVssLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdRYEKSniviNSQGV 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  432 GVLDIYGFETFD--VNSFEQFCINYANEK-----LQQQFNLHVFKLEQEEYMKED--IPWTLIDF-YDNQPVIDLIEAK- 500
Cdd:cd14893   403 HVLDMVGFENLTpsQNSFDQLCFNYWSEKvhhfyVQNTLAINFSFLEDESQQVENrlTVNSNVDItSEQEKCLQLFEDKp 482
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  501 MGILELLDEECLLPHGTDENWLQKLY--NNFV------NKNSLFEKPRMSNSS-----FIIQHFADKVEYQCEGFLEKNR 567
Cdd:cd14893   483 FGIFDLLTENCKVRLPNDEDFVNKLFsgNEAVgglsrpNMGADTTNEYLAPSKdwrllFIVQHHCGKVTYNGKGLSSKNM 562
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  568 DTVYDMLVEILRASKFHLCAAffqespVPSSPFGAMITVKSAKQVIKpntkhfRTTVGNKFRSSLY-------------- 633
Cdd:cd14893   563 LSISSTCAAIMQSSKNAVLHA------VGAAQMAAASSEKAAKQTEE------RGSTSSKFRKSASsaresknitdsaat 630
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568961011  634 -------LLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRY 699
Cdd:cd14893   631 dvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY 703
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
104-227 1.33e-44

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: 159.05  E-value: 1.33e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  104 ILVAMNPYKQLPIYGDA-IIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGESGAGKTVSARYAMRYFATVS 182
Cdd:cd01363     1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568961011  183 KSSSNA--------------HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFD 227
Cdd:cd01363    81 FNGINKgetegwvylteitvTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLD 139
MYSc_Myo24B cd14938
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
81-739 5.17e-43

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: 168.86  E-value: 5.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQN-MGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14938     1 PSVLYHLKERF-KNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDcIEDLSLNEYHVVHNALKNLNELKRNQSIII 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  160 SGESGAGKTVSARYAMRYFATVSKSS------SNAHVEDKVLAS----------------NPITEAVGNAKTTRNDNSSR 217
Cdd:cd14938    80 SGESGSGKSEIAKNIINFIAYQVKGSrrlptnLNDQEEDNIHNEentdyqfnmsemlkhvNVVMEAFGNAKTVKNNNSSR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  218 FGKYTEISFDERnQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEefNYTRMGGNTVIEGV 297
Cdd:cd14938   160 FSKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIE--NYSMLNNEKGFEKF 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  298 NDRAD-MVETQKTFTLLgFKKDFQMD-VFKILAAILHLGNVQVTTV---------------------------GNERSSV 348
Cdd:cd14938   237 SDYSGkILELLKSLNYI-FDDDKEIDfIFSVLSALLLLGNTEIVKAfrkksllmgknqcgqninyetilseleNSEDIGL 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  349 SEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSeTVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQH 428
Cdd:cd14938   316 DENVKNLLLACKLLSFDIETFVKYFTTNYIFNDS-ILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNIN 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  429 TF---IGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTL-IDFYDNQPVID-LIEAKMGI 503
Cdd:cd14938   395 INtnyINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYnSENIDNEPLYNlLVGPTEGS 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  504 LELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR---MSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRA 580
Cdd:cd14938   475 LFSLLENVSTKTIFDKSNLHSSIIRKFSRNSKYIKKDditGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQ 554
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  581 SKFHLCAAFFQESPVPSSpfgAMITVKSAKQVIKPNTKHFRTTVGNK-------FRSSLYLLMETLNATTPHYVRCIKPN 653
Cdd:cd14938   555 SENEYMRQFCMFYNYDNS---GNIVEEKRRYSIQSALKLFKRRYDTKnqmavslLRNNLTELEKLQETTFCHFIVCMKPN 631
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  654 DEK-MPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSrygILMTQQElslsDKKEVCKVVLHRLIQDSNQYQ 732
Cdd:cd14938   632 ESKrELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLS---IFDIKNE----DLKEKVEALIKSYQISNYEWM 704

                  ....*..
gi 568961011  733 FGRTKIF 739
Cdd:cd14938   705 IGNNMIF 711
MYSc_Myo33 cd14894
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...
187-705 1.29e-35

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: 146.81  E-value: 1.29e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  187 NAHVEDK---VLASNPITEAVGNAKTTRNDNSSRFGKYT--EISFDERN---QIIGANMRTYLLEKSRVVFQ------SE 252
Cdd:cd14894   239 NPHAAKKlsiVLDSNIVLEAFGHATTSMNLNSSRFGKMTtlQVAFGLHPwefQICGCHISPFLLEKSRVTSErgresgDQ 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  253 NERNYHIFYQLCASAQQSEF-----KHLKLGSAEEFNYTRMG-GNTVIEGVNDRADM----VETQKT----FTLLGFKKD 318
Cdd:cd14894   319 NELNFHILYAMVAGVNAFPFmrllaKELHLDGIDCSALTYLGrSDHKLAGFVSKEDTwkkdVERWQQvidgLDELNVSPD 398
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  319 FQMDVFKILAAILHLGNVQVT--TVGNE--RSSVSEDDSHLKVfCELLGL-ETSKVAQWLCNRKIV--TSSETVVKPMTR 391
Cdd:cd14894   399 EQKTIFKVLSAVLWLGNIELDyrEVSGKlvMSSTGALNAPQKV-VELLELgSVEKLERMLMTKSVSlqSTSETFEVTLEK 477
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  392 PQAINARDALAKKIYAHLFDFIVEQINQALHFS-----GKQH------------TFIGVLDIYGFETFDVNSFEQFCINY 454
Cdd:cd14894   478 GQVNHVRDTLARLLYQLAFNYVVFVMNEATKMSalstdGNKHqmdsnasapeavSLLKIVDVFGFEDLTHNSLDQLCINY 557
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  455 ANEKLQQqfnlhvfKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQ-----KLY-NN 528
Cdd:cd14894   558 LSEKLYA-------REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENMNAQQeekrnKLFvRN 630
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  529 FVNKNS--LFEKPR-MSNSS-----------FIIQHFADKVEYQCEGFLEKNRDTVY-DMLVEILRASKFHLCAAFFQES 593
Cdd:cd14894   631 IYDRNSsrLPEPPRvLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYaNLLVGLKTSNSSHFCRMLNESS 710
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  594 PVPSSPFGAMITVKSAKQVIKpNTKHFrttVGnKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRAC 673
Cdd:cd14894   711 QLGWSPNTNRSMLGSAESRLS-GTKSF---VG-QFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQ 785
                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 568961011  674 GV---LETIRISAQSYP----SRWTYLefySRYGILMTQ 705
Cdd:cd14894   786 RLirqMEICRNSSSSYSaidiSKSTLL---TRYGSLLRE 821
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
848-1155 6.34e-15

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 80.14  E-value: 6.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  848 RRYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNiQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAalrvgdlEKVQ 927
Cdd:COG1196   213 ERYQELKAELRELELALLLAKLKELRKELEELEEELS-RLEEELEELQEELEEAEKEIEELKSELEELR-------EELE 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  928 KLEAELEKAATHRHSYEEKGRRYRDTVEE---RLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTrqLFDDVQKE 1004
Cdd:COG1196   285 ELQEELLELKEEIEELEGEISLLRERLEElenELEELEERLEELKEKIEALKEELEERETLLEELEQLLA--ELEEAKEE 362
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1005 EQQRL-VLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQA 1083
Cdd:COG1196   363 LEEKLsALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELE 442
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568961011 1084 QKIDVEKHVQSQKREMRERMSEVTKQLLE-SYDIEDVRSRLSvEDLEHLNEDGELWFAYEGLKKATRVLESHF 1155
Cdd:COG1196   443 ELNEELEELEEQLEELRDRLKELERELAElQEELQRLEKELS-SLEARLDRLEAEQRASQGVRAVLEALESGL 514
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
891-1207 6.20e-14

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 77.06  E-value: 6.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  891 VQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELEL 970
Cdd:COG1196   167 VSKYKERKEEAERKLERTEENLERLEDLLEELEKQLEKLERQAEKAERYQELKAELRELELALLLAKLKELRKELEELEE 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  971 QRERAEQMLQEKSEELKEKMDKLT--RQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLE 1048
Cdd:COG1196   247 ELSRLEEELEELQEELEEAEKEIEelKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLE 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1049 EGQVTSDRLKGEVARLSKQ----AKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLE-SYDIEDVRSRL 1123
Cdd:COG1196   327 ELKEKIEALKEELEERETLleelEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEiRNELEELKREI 406
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1124 svEDLEhlnedgelwfayEGLKKATRVLESHFQSQKDcYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTR 1203
Cdd:COG1196   407 --ESLE------------ERLERLSERLEDLKEELKE-LEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAE 471

                  ....
gi 568961011 1204 LTSE 1207
Cdd:COG1196   472 LQEE 475
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
893-1200 2.01e-13

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 75.52  E-value: 2.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  893 RLQKKLEDQNRENHGLVEKLTSLAalrvgdlEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERlsKLQKHNAELELQR 972
Cdd:COG1196   657 RNKRSSLAQKRELKELEEELAELE-------AQLEKLEEELKSLKNELRSLEDLLEELRRQLEEL--ERQLEELKRELAA 727
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  973 -ERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTqAYEKQIESLREEIKALKDERSQLHHQLEEGQ 1051
Cdd:COG1196   728 lEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALA-KLKEEIEELEEKRQALQEELEELEEELEEAE 806
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1052 VTSDRLKGEVARLSKQaktISEFEKEIELLQAQKIDVEkhvqSQKREMRERMSEVTKQlLESYDIEDVRSRLSVEDLEHl 1131
Cdd:COG1196   807 RRLDALERELESLEQR---RERLEQEIEELEEEIEELE----EKLDELEEELEELEKE-LEELKEELEELEAEKEELED- 877
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961011 1132 nEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHE 1200
Cdd:COG1196   878 -ELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLET 945
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
837-1199 1.03e-12

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 72.87  E-value: 1.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  837 IQAHTRGFLARRRYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNIQLTY-----RVQRLQKKLEDQNRENHGLVEK 911
Cdd:COG0419   234 IEALEERLAELEEEKERLEELKARLLEIESLELEALKIREEELRELERLLEELeekieRLEELEREIEELEEELEGLRAL 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  912 LTSLAALR---VGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKE 988
Cdd:COG0419   314 LEELEELLeklKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQE 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  989 KMDKLT--RQLFDDVQ--KEEQQRLVLEKGFELKTqaYEKQIESLREEIKALKdERSQLHHQLEEGQVTSDRLKGEVARL 1064
Cdd:COG0419   394 LKEELAelSAALEEIQeeLEELEKELEELERELEE--LEEEIKKLEEQINQLE-SKELMIAELAGAGEKCPVCGQELPEE 470
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1065 SKQaKTISEFEKEIELLQaQKIDVEKHvqsqKREMRERMSEVTKQL---LESYDIEDVRSRLSVEDLEHLNEDGElwfay 1141
Cdd:COG0419   471 HEK-ELLELYELELEELE-EELSREKE----EAELREEIEELEKELrelEEELIELLELEEALKEELEEKLEKLE----- 539
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568961011 1142 EGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRH 1199
Cdd:COG0419   540 NLLEELEELKEKLQLQQLKEELRQLEDRLQELKELLEELRLLRTRKEELEELRERLKE 597
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
890-1207 2.23e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 71.63  E-value: 2.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  890 RVQRLQKKLEDQNRENHGLVEKLTSLAALR--VGDLEK---------VQKLEAELEKAATHRHSYEEKgrryRDTVEERL 958
Cdd:PRK03918  339 RLEELKKKLKELEKRLEELEERHELYEEAKakKEELERlkkrltgltPEKLEKELEELEKAKEEIEEE----ISKITARI 414
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  959 SKLQKHNAEL-------------------ELQRERAEQMLQEKSEELK------EKMDKLTRQLFDDVQKEEQQRLVLEK 1013
Cdd:PRK03918  415 GELKKEIKELkkaieelkkakgkcpvcgrELTEEHRKELLEEYTAELKriekelKEIEEKERKLRKELRELEKVLKKESE 494
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1014 GFELKTQAyeKQIESLREEIKALKDErsqlhhQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKhvq 1093
Cdd:PRK03918  495 LIKLKELA--EQLKELEEKLKKYNLE------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK--- 563
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1094 sQKREMRERMSEVTKQLLES--YDIEDVRSRLsvEDLEhlnedgELWFAYEGLKKATRVLESHFQSQKDCYE------KE 1165
Cdd:PRK03918  564 -KLDELEEELAELLKELEELgfESVEELEERL--KELE------PFYNEYLELKDAEKELEREEKELKKLEEeldkafEE 634
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 568961011 1166 IEGLNFKVVHLSQEINHLQKLFREETdiNESIRHEVTRLTSE 1207
Cdd:PRK03918  635 LAETEKRLEELRKELEELEKKYSEEE--YEELREEYLELSRE 674
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
893-1207 4.18e-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: 70.86  E-value: 4.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   893 RLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVE---ERLSKLQKHNAELE 969
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleERIAQLSKELTELE 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   970 LQRERAEQMLQEKSEELKEkmdkltrqlfDDVQKEEQQRLVlekgfelktQAYEKQIESLREEIKALKDERSQLHhqlEE 1049
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAE----------AEAEIEELEAQI---------EQLKEELKALREALDELRAELTLLN---EE 818
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1050 GQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEkHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVEDLE 1129
Cdd:TIGR02168  819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA-AEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1130 HLNEDGElwfAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEIN--------HLQKLFREETDINESIRHEV 1201
Cdd:TIGR02168  898 ELSEELR---ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeeysltleEAEALENKIEDDEEEARRRL 974

                   ....*.
gi 568961011  1202 TRLTSE 1207
Cdd:TIGR02168  975 KRLENK 980
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
850-1079 7.31e-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: 70.09  E-value: 7.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   850 YRKLLQEHKAVILQKYARAWLARRRFQNIRRfvLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKL 929
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQILRERLANLER--QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   930 EAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQ---MLQEKSEELKEKMDKLTRQLFDDVQ---- 1002
Cdd:TIGR02168  364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERledRRERLQQEIEELLKKLEEAELKELQaele 443
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1003 KEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHH----------QLEEGQVTSD----------RLKGEVA 1062
Cdd:TIGR02168  444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQlqarldslerLQENLEGFSEgvkallknqsGLSGILG 523
                          250
                   ....*....|....*..
gi 568961011  1063 RLSKQAKTISEFEKEIE 1079
Cdd:TIGR02168  524 VLSELISVDEGYEAAIE 540
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
847-1134 8.23e-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: 70.09  E-value: 8.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   847 RRRYRKL-LQEHKAVILQKYarawlaRRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENH-------GLVEKLTSLAAL 918
Cdd:TIGR02168  199 ERQLKSLeRQAEKAERYKEL------KAELRELELALLVLRLEELREELEELQEELKEAEEeleeltaELQELEEKLEEL 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   919 RVGDLE---KVQKLEAELEKAATHRHSYEEKGRRYRdtveERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLT- 994
Cdd:TIGR02168  273 RLEVSEleeEIEELQKELYALANEISRLEQQKQILR----ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEe 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   995 -RQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLR-------EEIKALKDERSQLHHQLEEGQVTSDRLKGEV----- 1061
Cdd:TIGR02168  349 lKEELESLEAELEELEAELEELESRLEELEEQLETLRskvaqleLQIASLNNEIERLEARLERLEDRRERLQQEIeellk 428
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568961011  1062 ----ARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKqllESYDIEDVRSRL-SVEDLEHLNED 1134
Cdd:TIGR02168  429 kleeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA---AERELAQLQARLdSLERLQENLEG 503
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
922-1198 1.59e-11

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: 69.32  E-value: 1.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   922 DLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEE-----------RLSKLQKHNAELELQRERAEQMLQEKSEELKEKM 990
Cdd:TIGR02168  187 NLDRLEDILNELERQLKSLERQAEKAERYKELKAElrelelallvlRLEELREELEELQEELKEAEEELEELTAELQELE 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   991 DKLT----RQLFDDVQKEEQQRLVLEKGFELktQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSK 1066
Cdd:TIGR02168  267 EKLEelrlEVSELEEEIEELQKELYALANEI--SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE 344
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1067 Q-----------AKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTK-----QLLESY--DIEDVRSRLSVEDL 1128
Cdd:TIGR02168  345 KleelkeeleslEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASlnneiERLEARleRLEDRRERLQQEIE 424
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1129 EHL-----NEDGELWFAYEGLKKATRVLESHF----------QSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDI 1193
Cdd:TIGR02168  425 ELLkkleeAELKELQAELEELEEELEELQEELerleealeelREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF 504

                   ....*
gi 568961011  1194 NESIR 1198
Cdd:TIGR02168  505 SEGVK 509
HEC1 COG5185
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, ...
943-1207 2.75e-11

Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227512 [Multi-domain]  Cd Length: 622  Bit Score: 67.70  E-value: 2.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  943 YEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEkSEELKEKMdKLTRQLFDDVQKEEQQRLVLEKGFELKTQAY 1022
Cdd:COG5185   251 YEPSEQELKLGFEKFVHIINTDIANLKTQNDNLYEKIQE-AMKISQKI-KTLREKWRALKSDSNKYENYVNAMKQKSQEW 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1023 -------EKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKgevarlsKQAKTISEFEKEIELLQAQKIDVEKHVQSQ 1095
Cdd:COG5185   329 pgkleklKSEIELKEEEIKALQSNIDELHKQLRKQGISTEQFE-------LMNQEREKLTRELDKINIQSDKLTKSVKSR 401
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1096 KREMRERMSEVTKqLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYE-------GLKKATRVLESHFQSQKDCYEKEIEG 1168
Cdd:COG5185   402 KLEAQGIFKSLEK-TLRQYDSLIQNITRSRSQIGHNVNDSSLKINIEqlfpkgsGINESIKKSILELNDEIQERIKTEEN 480
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 568961011 1169 LNFKvvhLSQEINHLQKLFREETDINESIRHEVTRLTSE 1207
Cdd:COG5185   481 KSIT---LEEDIKNLKHDINELTQILEKLELELSEANSK 516
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
849-1136 2.80e-11

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 435022 [Multi-domain]  Cd Length: 1112  Bit Score: 68.20  E-value: 2.80e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   849 RYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNIQLTYRVQR--LQKKLEDQNRENHGLVEKLTSLAALRVGDLEKV 926
Cdd:pfam15921  268 RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNsmYMRQLSDLESTVSQLRSELREAKRMYEDKIEEL 347
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   927 QK----LEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQmLQEKSEELKEKMDKLTRQLfDDVQ 1002
Cdd:pfam15921  348 EKqlvlANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKR-LWDRDTGNSITIDHLRREL-DDRN 425
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1003 KEEQQRLVLEKGFELKTQA-YEKQIESLREEIKALkDERSQLHHQLEEgqvTSDRLKGEVARLSKQAKTISEFEKEIEll 1081
Cdd:pfam15921  426 MEVQRLEALLKAMKSECQGqMERQMAAIQGKNESL-EKVSSLTAQLES---TKEMLRKVVEELTAKKMTLESSERTVS-- 499
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568961011  1082 qaqkiDVEKHVQSQKREMRERMSEVTKqllesydiedVRSR--LSVEDLEHLNEDGE 1136
Cdd:pfam15921  500 -----DLTASLQEKERAIEATNAEITK----------LRSRvdLKLQELQHLKNEGD 541
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
886-1204 4.63e-11

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 67.43  E-value: 4.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  886 QLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAathrhsyeekgrryrdtvEERLSKLQKHN 965
Cdd:COG1196   720 ELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESL------------------EEALAKLKEEI 781
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  966 AELELQRERAEQMLQEKSEELKEkMDKLTRQLFDDVQKEEQQRlvlekgfelktQAYEKQIESLREEIKALKDERSQLHH 1045
Cdd:COG1196   782 EELEEKRQALQEELEELEEELEE-AERRLDALERELESLEQRR-----------ERLEQEIEELEEEIEELEEKLDELEE 849
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1046 QLEEGQvtsDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSV 1125
Cdd:COG1196   850 ELEELE---KELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEV 926
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1126 E--DLEHLNEDGELWFAYEGLKKATRVLeshfqsqkdcyEKEIEGL---NFKVVhlsQEINHLQKLFREETDINESIRHE 1200
Cdd:COG1196   927 ElpELEEELEEEYEDTLETELEREIERL-----------EEEIEALgpvNLRAI---EEYEEVEERYEELKSQREDLEEA 992

                  ....
gi 568961011 1201 VTRL 1204
Cdd:COG1196   993 KEKL 996
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
848-1079 6.28e-11

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 67.05  E-value: 6.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  848 RRYRKLLQEHKAVILQKYARAwlaRRRFQNIRRFVLNiqLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQ 927
Cdd:COG1196   785 EEKRQALQEELEELEEELEEA---ERRLDALERELES--LEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELE 859
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  928 KLEAELEKAATHRHSYEEKGRRYRDTVEE---RLSKLQKHNAELELQRERAEQMLqeksEELKEKMDKLtrqlfdDVQKE 1004
Cdd:COG1196   860 ELKEELEELEAEKEELEDELKELEEEKEEleeELRELESELAELKEEIEKLRERL----EELEAKLERL------EVELP 929
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961011 1005 EQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIE 1079
Cdd:COG1196   930 ELEEELEEEYEDTLETELEREIERLEEEIEALGPVNLRAIEEYEEVEERYEELKSQREDLEEAKEKLLEVIEELD 1004
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
849-1185 2.90e-10

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: 65.09  E-value: 2.90e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   849 RYRKLLQEhkaviLQKYaRAWLARRRFQNIRRfvlniqltyRVQRLQKKLEDQNREnhglVEKLTslaalrvgdlEKVQK 928
Cdd:TIGR02169  212 RYQALLKE-----KREY-EGYELLKEKEALER---------QKEAIERQLASLEEE----LEKLT----------EEISE 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   929 LEAELEKAATHRhsyEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELkEKMDKLTRQLFDDVQKEEQQR 1008
Cdd:TIGR02169  263 LEKRLEEIEQLL---EELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKEREL-EDAEERLAKLEAEIDKLLAEI 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1009 LVLEKgfelKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVarlskqaktiSEFEKEIELLQaQKIDV 1088
Cdd:TIGR02169  339 EELER----EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL----------KDYREKLEKLK-REINE 403
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1089 EKHVQSQKREMRERMSEvtkqllesyDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLEShFQSQKDCYEKEIEG 1168
Cdd:TIGR02169  404 LKRELDRLQEELQRLSE---------ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ-LAADLSKYEQELYD 473
                          330
                   ....*....|....*..
gi 568961011  1169 LNFKVVHLSQEINHLQK 1185
Cdd:TIGR02169  474 LKEEYDRVEKELSKLQR 490
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
896-1133 3.68e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 64.68  E-value: 3.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  896 KKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERA 975
Cdd:PRK02224  272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  976 EQmLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEkgfelktqAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSD 1055
Cdd:PRK02224  352 DD-LEERAEELREEAAELESELEEAREAVEDRREEIE--------ELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1056 RLKGEVARLSKQAKTISE-FEKEIELLQA-------QKIDVEKHVQSQKrEMRERMSEVTKQLLesyDIEDVRSRLS--V 1125
Cdd:PRK02224  423 ELREREAELEATLRTARErVEEAEALLEAgkcpecgQPVEGSPHVETIE-EDRERVEELEAELE---DLEEEVEEVEerL 498

                  ....*...
gi 568961011 1126 EDLEHLNE 1133
Cdd:PRK02224  499 ERAEDLVE 506
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
890-1129 3.70e-10

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: 64.70  E-value: 3.70e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   890 RVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEK-GRRYRDTVEERLSKLQKHNAEL 968
Cdd:TIGR02169  724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlNDLEARLSHSRIPEIQAELSKL 803
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   969 ELQRERAEQMLQEKSEELKEKmDKLTRQLFDDVQKEEQQRLVLE---KGFELKTQAYEKQIESLREEIKALKDERSQLHH 1045
Cdd:TIGR02169  804 EEEVSRIEARLREIEQKLNRL-TLEKEYLEKEIQELQEQRIDLKeqiKSIEKEIENLNGKKEELEEELEELEAALRDLES 882
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1046 QLEEgqvtsdrLKGEVARLSKQaktISEFEKEIELLQAQkIDVEKHVQSQKREMRERMSEVTKQLLESY--DIEDVRSRL 1123
Cdd:TIGR02169  883 RLGD-------LKKERDELEAQ---LRELERKIEELEAQ-IEKKRKRLSELKAKLEALEEELSEIEDPKgeDEEIPEEEL 951

                   ....*.
gi 568961011  1124 SVEDLE 1129
Cdd:TIGR02169  952 SLEDVQ 957
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
851-1123 7.09e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.54  E-value: 7.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  851 RKLLQEHKAVILQKYarawlaRRRFQNIRRFVLNI-----QLTYRVQRLQKKLEDQNR--ENHGLVEKLTSL-AALRVGD 922
Cdd:PRK03918  443 RELTEEHRKELLEEY------TAELKRIEKELKEIeekerKLRKELRELEKVLKKESEliKLKELAEQLKELeEKLKKYN 516
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  923 LEKVQKLEAELEKaaTHRHSYEEKGRryRDTVEERLSKLQkhnaELELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQ 1002
Cdd:PRK03918  517 LEELEKKAEEYEK--LKEKLIKLKGE--IKSLKKELEKLE----ELKKKLAELEKKLDELEEELAELLKELEELGFESVE 588
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1003 KEEQQRLVLEKGFE--LKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQ---------AKTI 1071
Cdd:PRK03918  589 ELEERLKELEPFYNeyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeyeelREEY 668
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568961011 1072 SEFEKEIELLQAQKIDVEKHVQSQKR---EMRERMSEVTKQLLESYDIEDVRSRL 1123
Cdd:PRK03918  669 LELSRELAGLRAELEELEKRREEIKKtleKLKEELEEREKAKKELEKLEKALERV 723
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
872-1113 1.00e-09

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: 62.83  E-value: 1.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   872 RRRFQNIRRFVLNIQLTyRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEE-KGRRY 950
Cdd:pfam17380  359 KRELERIRQEEIAMEIS-RMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEaRQREV 437
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   951 RDTVEERLSKLQKHNAElELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYekqiesLR 1030
Cdd:pfam17380  438 RRLEEERAREMERVRLE-EQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAM------IE 510
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1031 EEIKalkdeRSQLHHQLEEGQVTsdrlkgeVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKR---EMRERMSEVT 1107
Cdd:pfam17380  511 EERK-----RKLLEKEMEERQKA-------IYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERsrlEAMEREREMM 578

                   ....*.
gi 568961011  1108 KQLLES 1113
Cdd:pfam17380  579 RQIVES 584
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
925-1213 1.19e-09

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: 63.15  E-value: 1.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   925 KVQKLEAELEKAAThrhsyEEKGRRYRDTVEERLSKLQKhnaeLELQRERAEQmLQEKSEELKEKMDKLTRQLFDDVQKE 1004
Cdd:TIGR02168  171 KERRKETERKLERT-----RENLDRLEDILNELERQLKS----LERQAEKAER-YKELKAELRELELALLVLRLEELREE 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1005 EQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQ 1084
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1085 KIDVEKHVQSQKREMRERMSEVTKQLLE-SYDIEDVRSRLSVedlehlnedgelwfayegLKKATRVLESHFQSQkdcyE 1163
Cdd:TIGR02168  321 LEAQLEELESKLDELAEELAELEEKLEElKEELESLEAELEE------------------LEAELEELESRLEEL----E 378
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 568961011  1164 KEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLTSENMPLLS 1213
Cdd:TIGR02168  379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
892-1208 2.28e-09

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 62.09  E-value: 2.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  892 QRLQKKLEDQNRENHGLVEKLTSLAALRVGDLE--------KVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQK 963
Cdd:COG0419   192 GQLSELLEDIEDLLEALEEELKELKKLEEIQEEqeeeeleqEIEALEERLAELEEEKERLEELKARLLEIESLELEALKI 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  964 HNAELElQRERAEQMLQEKSEELKEKMDKLTRQlfddvQKEEQQRLVLEKgfelKTQAYEKQIESLREEIKALKDERSQL 1043
Cdd:COG0419   272 REEELR-ELERLLEELEEKIERLEELEREIEEL-----EEELEGLRALLE----ELEELLEKLKSLEERLEKLEEKLEKL 341
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1044 HHQLEEGQVTSDRLKGEVARLSKQAKT-ISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKqLLESYDiEDVRSR 1122
Cdd:COG0419   342 ESELEELAEEKNELAKLLEERLKELEErLEELEKELEKALERLKQLEEAIQELKEELAELSAALEE-IQEELE-ELEKEL 419
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1123 LSVE-DLEHLNED-GELWFAYEGLKKATRVLESHFQSQKDCY--EKEIEGLNFKVV--HLSQEINHLQKLFREETDINEs 1196
Cdd:COG0419   420 EELErELEELEEEiKKLEEQINQLESKELMIAELAGAGEKCPvcGQELPEEHEKELleLYELELEELEEELSREKEEAE- 498
                         330
                  ....*....|..
gi 568961011 1197 IRHEVTRLTSEN 1208
Cdd:COG0419   499 LREEIEELEKEL 510
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
945-1207 3.83e-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: 61.24  E-value: 3.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   945 EKGRRYRDTVEERLSKLQKHNAELELQRERaeqmLQEKSEElKEKMDKLTRQLfddvQKEEQQRLVLEK-GFELKTQAYE 1023
Cdd:TIGR02169  173 EKALEELEEVEENIERLDLIIDEKRQQLER----LRREREK-AERYQALLKEK----REYEGYELLKEKeALERQKEAIE 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1024 KQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQA-----KTISEFEKEIELLQAQKIDVEKHVQSQKRE 1098
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqlrvkEKIGELEAEIASLERSIAEKERELEDAEER 323
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1099 MRERMSEVTKQLLESYDIEdvrsrlsvEDLEHLNEDGELWFA-YEGLKKATRVLESH-----------FQSQKDcYEKEI 1166
Cdd:TIGR02169  324 LAKLEAEIDKLLAEIEELE--------REIEEERKRRDKLTEeYAELKEELEDLRAEleevdkefaetRDELKD-YREKL 394
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 568961011  1167 EGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLTSE 1207
Cdd:TIGR02169  395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
893-1128 7.10e-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: 60.47  E-value: 7.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   893 RLQKKLEDQNRENHGLVEKLtSLAALRVGDLE-KVQKLEAELEKAATHRHSYEEKGRRY---RDTVEERLSKLQkhnAEL 968
Cdd:TIGR02169  291 RVKEKIGELEAEIASLERSI-AEKERELEDAEeRLAKLEAEIDKLLAEIEELEREIEEErkrRDKLTEEYAELK---EEL 366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   969 ELQRERAEQM------LQEKSEELKEKMDKLTRQLFDdvQKEEQQRLVLEKgfelktQAYEKQIESLREEIKALKDERSQ 1042
Cdd:TIGR02169  367 EDLRAELEEVdkefaeTRDELKDYREKLEKLKREINE--LKRELDRLQEEL------QRLSEELADLNAAIAGIEAKINE 438
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1043 LHHQLEEGQvtsDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRErmSEVTKQLLESYdiedVRSR 1122
Cdd:TIGR02169  439 LEEEKEDKA---LEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE--AEAQARASEER----VRGG 509

                   ....*.
gi 568961011  1123 LSVEDL 1128
Cdd:TIGR02169  510 RAVEEV 515
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
846-1115 7.75e-09

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: 60.46  E-value: 7.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   846 ARRRYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNI-----QLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRV 920
Cdd:TIGR02168  699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   921 GDLEKVQKLEAELEKA----ATHRHSYEEKGRRYRDT------VEERLSKLQKHNAELELQRERAEQMLQEKSE------ 984
Cdd:TIGR02168  779 EAEAEIEELEAQIEQLkeelKALREALDELRAELTLLneeaanLRERLESLERRIAATERRLEDLEEQIEELSEdiesla 858
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   985 ----ELKEKMDKLTRQL---FDDVQKEEQQRLVLEKGFELKT---QAYEKQIESLREEIKALKDERSQLHHQLEEGQVTS 1054
Cdd:TIGR02168  859 aeieELEELIEELESELealLNERASLEEALALLRSELEELSeelRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1055 DRLKG-----------------------------EVARLSKQAK--------TISEFEKEIE---LLQAQKIDVEKHVQS 1094
Cdd:TIGR02168  939 DNLQErlseeysltleeaealenkieddeeearrRLKRLENKIKelgpvnlaAIEEYEELKErydFLTAQKEDLTEAKET 1018
                          330       340
                   ....*....|....*....|.
gi 568961011  1095 QKREMRERMSEVTKQLLESYD 1115
Cdd:TIGR02168 1019 LEEAIEEIDREARERFKDTFD 1039
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
862-1189 1.13e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 59.69  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  862 LQKYARAW--------LARRRFQNIRRFvlnIQLTYRVQRL----QKKLEDQNRENHGLVEKLTSLAalrvgdlEKVQKL 929
Cdd:PRK03918  157 LDDYENAYknlgevikEIKRRIERLEKF---IKRTENIEELikekEKELEEVLREINEISSELPELR-------EELEKL 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  930 EAELEKAATHRHSYEEKgrryrdtvEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRqlFDDVQKEEQQRL 1009
Cdd:PRK03918  227 EKEVKELEELKEEIEEL--------EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE--LKELKEKAEEYI 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1010 VLEK---GFELKTQAYEKQIESLREEIKALKDersqlhhQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKI 1086
Cdd:PRK03918  297 KLSEfyeEYLDELREIEKRLSRLEEEINGIEE-------RIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKA 369
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1087 DVEKHVQSQKREMRERMSEVTKQLLE----SYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVL--------ESH 1154
Cdd:PRK03918  370 KKEELERLKKRLTGLTPEKLEKELEElekaKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgreltEEH 449
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 568961011 1155 FQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFRE 1189
Cdd:PRK03918  450 RKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
890-1150 1.18e-08

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 224259 [Multi-domain]  Cd Length: 294  Bit Score: 57.77  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  890 RVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLeaeLEKAATHRHSYEEKGRRYRDTVEERLsklqKHNAELE 969
Cdd:COG1340    14 KRKQLKEEIEELKEKRDELRKEASELAEKRDELNAKVREL---REKAQELREERDEINEEVQELKEKRD----EINAKLQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  970 LQRERAEQMLQEKSE---------ELKEKMDKL-----TRQLFDDVQKEEQQRLV-LEKGFELKTQAYE--KQIESLREE 1032
Cdd:COG1340    87 ELRKEYRELKEKRNEfnlggrsikSLEREIERLekkqqTSVLTPEEERELVQKIKeLRKELEDAKKALEenEKLKELKAE 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1033 IKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAktiSEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTK--QL 1110
Cdd:COG1340   167 IDELKKKAREIHEKIQELANEAQEYHEEMIKLFEEA---DELRKEADELHEEFVELSKKIDELHEEFRNLQNELREleKK 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 568961011 1111 LESYDIEDVRSRLSVEDLEhLNEDGELwfAYEGLKKATRV 1150
Cdd:COG1340   244 IKALRAKEKAAKRREKREE-LKERAEE--IYEKFKRGEKL 280
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
896-1112 1.22e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 59.69  E-value: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  896 KKLEDQNRENHGLVEKLTSLAALRVG---DLEKVQKLEAEL-----------EKAATHRHSYEEKGRRYRDTVEERLSKL 961
Cdd:PRK03918  518 EELEKKAEEYEKLKEKLIKLKGEIKSlkkELEKLEELKKKLaelekkldeleEELAELLKELEELGFESVEELEERLKEL 597
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  962 QK-HNAELELQRerAEQMLQEKSEELKEKMDKLTrQLFDDVQKEEQQRLVLEKGFELKTQAY--------EKQIESLREE 1032
Cdd:PRK03918  598 EPfYNEYLELKD--AEKELEREEKELKKLEEELD-KAFEELAETEKRLEELRKELEELEKKYseeeyeelREEYLELSRE 674
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1033 IKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLE 1112
Cdd:PRK03918  675 LAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEIASEIFE 754
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
890-1137 1.88e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 58.90  E-value: 1.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  890 RVQRLQKKLEDqnrenhgLVEKLTSLAAlRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKL-------Q 962
Cdd:PRK02224  476 RVEELEAELED-------LEEEVEEVEE-RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAeelreraA 547
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  963 KHNAELELQRERAeQMLQEKSEELKEKMDKLTRQLfdDVQKEEQQRL-VLEKGFELKTqAYEKQIESLREEIKALKD--- 1038
Cdd:PRK02224  548 ELEAEAEEKREAA-AEAEEEAEEAREEVAELNSKL--AELKERIESLeRIRTLLAAIA-DAEDEIERLREKREALAElnd 623
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1039 -------ERSQLHHQLEEgQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKRE------MRERMSE 1105
Cdd:PRK02224  624 errerlaEKRERKRELEA-EFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEleeleeLRERREA 702
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 568961011 1106 V--TKQLLESYDIE---------DVRSRL---SVEDLEH-LNEDGEL 1137
Cdd:PRK02224  703 LenRVEALEALYDEaeelesmygDLRAELrqrNVETLERmLNETFDL 749
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
886-1107 1.89e-08

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 59.00  E-value: 1.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  886 QLTYRVQRLQKKLEDQNRENH--GLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKgrRYRDTVEERL-SKLQ 962
Cdd:COG0419   563 QLEDRLQELKELLEELRLLRTrkEELEELRERLKELKKKLKELEERLSQLEELLQSLELSEAE--NELEEAEEELeSELE 640
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  963 KHNAELELQR--ERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKtqAYEKQIESLREEIKALKDER 1040
Cdd:COG0419   641 KLNLQAELEEllQAALEELEEKVEELEAEIRRELQRIENEEQLEEKLEELEQLEEELE--QLREELEELLKKLGEIEQLI 718
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568961011 1041 SQLHHQLEEgqvtSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVT 1107
Cdd:COG0419   719 EELESRKAE----LEELKKELEKLEKALELLEELREKLGKAGLRADILRNLLAQIEAEANEILSKLS 781
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ...
874-1129 1.94e-08

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 225638 [Multi-domain]  Cd Length: 1480  Bit Score: 59.13  E-value: 1.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  874 RFQNIRRFVLNIQLTYRvQRLQKKLEDQNRENHGLVEKLTSLAALrvgdLEKVQKLEAELEKAATH--------RHsyEE 945
Cdd:COG3096   276 RHANERRVHLDQALEFR-RELYTSRQQLAAEQYRHVDMSRELAEL----NGAEGDLEADYQAASDHlnlvqtalRQ--QE 348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  946 KGRRYRDTVEERLSKLQKHNAELELQRERAEQMlQEKSEELKEKMDKLTRQLFD-----DVQK----EEQQRL-VLEKGF 1015
Cdd:COG3096   349 KIERYQADLEELTIRLEEQNEVVEEANERQEEN-EARAEAAELEVDELKSQLADyqqalDVQQtraiQYQQAIaALERAK 427
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1016 EL--KTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSD--------------RLKGEVAR---------LSKQAKT 1070
Cdd:COG3096   428 ELchLPDLTADSAEEWLETFQAKEEEATEKLLSLEQKMSMAQaahsqfeqayqlvvAIAGELARseawdvareLLREGPD 507
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961011 1071 ISEFEKEIELLQAQKIDVEKHVQSQkREMRERMSEVTKQLLESYDI---EDVRSRLS--VEDLE 1129
Cdd:COG3096   508 QRHLAEQVQPLRMRLSELEQRLRQQ-QSAERLLADFCKRQGKNLDAeelEALHQELEalIESLS 570
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
894-1185 2.81e-08

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: 435008 [Multi-domain]  Cd Length: 329  Bit Score: 57.13  E-value: 2.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   894 LQKKLEDQNRenHGLVEKLTSLAALRVGDLEK-VQKLEAELEKAathrhsyEEKgrrYRDTVEERLSkLQKHNAELELQR 972
Cdd:pfam15905   65 SQKDLKESKD--QKELEKEIRALVQERGEQDKrLQALEEELEKV-------EAK---LNAAVREKTS-LSASVASLEKQL 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   973 ---ERAEQMLQEKSEE--LKEKMDKLTRQLF---DDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLH 1044
Cdd:pfam15905  132 lelTRVNELLKAKFSEdgTQKKMSSLSMELMklrNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTE 211
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1045 HQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQllesydIEDVRSRLS 1124
Cdd:pfam15905  212 KEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQ------IKDLNEKCK 285
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568961011  1125 VedLEHLNEDgelwfayeglkkatrvLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQK 1185
Cdd:pfam15905  286 L--LESEKEE----------------LLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
894-1185 5.60e-08

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: 57.34  E-value: 5.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   894 LQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRdTVEERLSKLQKHNAELELQRE 973
Cdd:TIGR04523  157 LNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK-SLESQISELKKQNNQLKDNIE 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   974 RAEQMLQEKSEELKEKMDKLTrQLFDDVQKEEQQrlVLEKGFELKTQayEKQIESLREEIKALKDERSQLHHQLEegQVT 1053
Cdd:TIGR04523  236 KKQQEINEKTTEISNTQTQLN-QLKDEQNKIKKQ--LSEKQKELEQN--NKKIKELEKQLNQLKSEISDLNNQKE--QDW 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1054 SDRLKGEVA-----------RLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLE--SYdiedvr 1120
Cdd:TIGR04523  309 NKELKSELKnqekkleeiqnQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEnqSY------ 382
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568961011  1121 sRLSVEDLEHLNEDGELWFayEGLKKATRVLESH---FQSQKDCYEKEIEGLNFKVVHLSQEINHLQK 1185
Cdd:TIGR04523  383 -KQEIKNLESQINDLESKI--QNQEKLNQQKDEQikkLQQEKELLEKEIERLKETIIKNNSEIKDLTN 447
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
892-1133 5.92e-08

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: 57.06  E-value: 5.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   892 QRLQKKLEDQNREnhglVE---KLTSLAALRVGDLEKVQKLEAELEKAATHRH------SYEEKGRRYRDTVEERLSKLQ 962
Cdd:pfam17380  299 ERLRQEKEEKARE----VErrrKLEEAEKARQAEMDRQAAIYAEQERMAMEREreleriRQEERKRELERIRQEEIAMEI 374
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   963 KHNAELE-LQRERaeqmlQEKSEELKEKMDKLTRQlfdDVQKEEQQRLVLEKGFELKtQAYEKQIESLREEIKALKDERS 1041
Cdd:pfam17380  375 SRMRELErLQMER-----QQKNERVRQELEAARKV---KILEEERQRKIQQQKVEME-QIRAEQEEARQREVRRLEEERA 445
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1042 -----------QLHHQLE---EGQVTSDRLKGEVARLSKQAKTISE-----FEKEIELLQAQKIDVEKHVQSQKREMRER 1102
Cdd:pfam17380  446 remervrleeqERQQQVErlrQQEEERKRKKLELEKEKRDRKRAEEqrrkiLEKELEERKQAMIEEERKRKLLEKEMEER 525
                          250       260       270
                   ....*....|....*....|....*....|.
gi 568961011  1103 MSEVTKQLLESYDIEDVRSRLSVEDLEHLNE 1133
Cdd:pfam17380  526 QKAIYEEERRREAEEERRKQQEMEERRRIQE 556
COG1579 COG1579
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ...
952-1115 6.43e-08

Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only];


Pssm-ID: 224495 [Multi-domain]  Cd Length: 239  Bit Score: 55.06  E-value: 6.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  952 DTVEERLSKLQKHNAELELQRERAEQMLQEKSEELkEKMDKLTRQLFDDVQKEEQQRLVLEKGF-ELKTQ----AYEKQI 1026
Cdd:COG1579    20 DRLEPRIKEIRKALKKAKAELEALNKALEALEIEL-EDLENQVSQLESEIQEIRERIKRAEEKLsAVKDErelrALNIEI 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1027 ESLREEIKALKDERSQLHHQLEEGQvtsDRLKGEVARLSKQAKTISEFEKEIELlQAQKIDVEKH-VQSQKREMRERMSE 1105
Cdd:COG1579    99 QIAKERINSLEDELAELMEEIEKLE---KEIEDLKERLERLEKNLAEAEARLEE-EVAEIREEGQeLSSKREELKEKLDP 174
                         170
                  ....*....|
gi 568961011 1106 vtkQLLESYD 1115
Cdd:COG1579   175 ---ELLSEYE 181
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
845-1090 6.93e-08

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227278 [Multi-domain]  Cd Length: 420  Bit Score: 56.27  E-value: 6.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  845 LARRRYRKLLQEHKAvILQKYARAWLARRRFQNiRRFVLNIQLTYRVQRLQKkLEDQNRENHGLVEKLtsLAAL-RVGDL 923
Cdd:COG4942    56 EQQDQRAKLEKQLKS-LETEIASLEAQLIETAD-DLKKLRKQIADLNARLNA-LEVQEREQRRRLAEQ--LAALqRSGRN 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  924 EKVQKL----EAELEKAATHRHSYEEKGRRYR-DTVEERLSKLQKHNAELELQRERAEQMLQEKSEElKEKMDKLtrqlf 998
Cdd:COG4942   131 PPPALLvspeDAQRSVRLAIYYGALNPARAERiDALKATLKQLAAVRAEIAAEQAELTTLLSEQRAQ-QAKLAQL----- 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  999 ddvqKEEQQRLvlEKGFELKTQAYEKQIESLREEIKALKDERSQLhhqleEGQVTSDRLKGEVARLSKQAKTISEFEKEI 1078
Cdd:COG4942   205 ----LEERKKT--LAQLNSELSADQKKLEELRANESRLKNEIASA-----EAAAAKAREAAAAAEAAAARARAAEAKRTG 273
                         250
                  ....*....|..
gi 568961011 1079 ELLQAQKIDVEK 1090
Cdd:COG4942   274 ETYKPTAPEKML 285
mukB PRK04863
chromosome partition protein MukB;
866-1133 7.12e-08

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 57.27  E-value: 7.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  866 ARAWLarrRFQNIRRFVLNIQLTYRvQRLQKKLEDQNRENHGLVEKLTSLAALRvgdlEKVQKLEAELEKAATHRHS--- 942
Cdd:PRK04863  271 AADYM---RHANERRVHLEEALELR-RELYTSRRQLAAEQYRLVEMARELAELN----EAESDLEQDYQAASDHLNLvqt 342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  943 ---YEEKGRRYRDTVEERLSKLQKHNAELELQRERAEqMLQEKSEELKEKMDKLTRQLFDDVQK-EEQQRLVLEkgFELK 1018
Cdd:PRK04863  343 alrQQEKIERYQADLEELEERLEEQNEVVEEADEQQE-ENEARAEAAEEEVDELKSQLADYQQAlDVQQTRAIQ--YQQA 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1019 TQAYEKQ-----------------IESLREEIKALKDERSQLHHQLEEGQVTSD----------RLKGEVARL--SKQAK 1069
Cdd:PRK04863  420 VQALERAkqlcglpdltadnaedwLEEFQAKEQEATEELLSLEQKLSVAQAAHSqfeqayqlvrKIAGEVSRSeaWDVAR 499
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961011 1070 -TISEFEKEIEL------LQAQKIDVEKHVQSQKREMReRMSEVTKQLLESYDIEDVRSRLSVE---DLEHLNE 1133
Cdd:PRK04863  500 eLLRRLREQRHLaeqlqqLRMRLSELEQRLRQQQRAER-LLAEFCKRLGKNLDDEDELEQLQEEleaRLESLSE 572
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
884-1185 9.87e-08

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: 428520 [Multi-domain]  Cd Length: 660  Bit Score: 56.28  E-value: 9.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   884 NIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLaalrvgdlekvQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQK 963
Cdd:pfam05557   50 NQELQKRIRLLEKREAEAEEALREQAELNRLK-----------KKNLEALNKKLNEKESQLADAREVISCLKNELSELRR 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   964 --HNAELELQRERAE-QMLQEKSEELKEKMDKLTrQLFDDVQKeeQQRLVLEKgfELKTQAYEKQIESLREEIKALKDER 1040
Cdd:pfam05557  119 qiQRQELELSSTNSElEELQERLDLQKAKAQEAE-QLRQNLEA--QQSSLAEA--EQRIKELEFEIQSQEQDSEIVKNSK 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1041 SQLhHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQ----------AQKIDVEKHVQSQKREMRERMSEVTKQL 1110
Cdd:pfam05557  194 SEL-ARIPELERELERLREHNKHLNENIENKLLLKEEVEDLKrklereegyrEELATLELEKEKLEQELKSWEKLAQDTG 272
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568961011  1111 LESYDIEDVRSR---LSVEDLEHLNEDGELWFAYEGLKKATRVLeshfQSQKDCYEKEIEGLNFKVVHLSQEINHLQK 1185
Cdd:pfam05557  273 LNLRSPEDLSRRieqLQQREITLKEENSSLTSSARQLEKAQREL----EQELAQYLKNIEDLNKKLKRHKALVRRLQR 346
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
988-1193 1.02e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 56.61  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  988 EKMDKLTRQL--FDDVQKEEQQRLVLEKGFELKTQAYEKQI---ESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVA 1062
Cdd:PRK03918  145 ESREKVVRQIlgLDDYENAYKNLGEVIKEIKRRIERLEKFIkrtENIEELIKEKEKELEEVLREINEISSELPELREELE 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1063 RLSKQAKTISEFEKEIELLQAQKIDVEKHVQS---QKREMRERMSEVTKQllesydIEDVRSRlsVEDLEHLNEDGELWF 1139
Cdd:PRK03918  225 KLEKEVKELEELKEEIEELEKELESLEGSKRKleeKIRELEERIEELKKE------IEELEEK--VKELKELKEKAEEYI 296
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568961011 1140 AYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDI 1193
Cdd:PRK03918  297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKEL 350
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
846-1090 1.13e-07

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 56.31  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  846 ARRRYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNIQLtyRVQRLQKKLEDQNRENhgLVEKLTSLAalrvgdlEK 925
Cdd:COG0419   499 LREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLEN--LLEELEELKEKLQLQQ--LKEELRQLE-------DR 567
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  926 VQKLEAELEKAATHRHSYE--EKGRRYRDTVEERLSKLQKHNAELE-----LQRERAEQMLQEKSEELKEKMDKL----- 993
Cdd:COG0419   568 LQELKELLEELRLLRTRKEelEELRERLKELKKKLKELEERLSQLEellqsLELSEAENELEEAEEELESELEKLnlqae 647
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  994 -TRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESL--REEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKT 1070
Cdd:COG0419   648 lEELLQAALEELEEKVEELEAEIRRELQRIENEEQLEekLEELEQLEEELEQLREELEELLKKLGEIEQLIEELESRKAE 727
                         250       260
                  ....*....|....*....|
gi 568961011 1071 ISEFEKEIELLQAQKIDVEK 1090
Cdd:COG0419   728 LEELKKELEKLEKALELLEE 747
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
851-1137 1.45e-07

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 224259 [Multi-domain]  Cd Length: 294  Bit Score: 54.69  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  851 RKLLQEH--KAVILQKYARAWLARRRFQN--IRRFVLNIQ--------LTYRVQRLQKKLEDQNRENHGL---VEKLTSL 915
Cdd:COG1340    19 KEEIEELkeKRDELRKEASELAEKRDELNakVRELREKAQelreerdeINEEVQELKEKRDEINAKLQELrkeYRELKEK 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  916 AALRVGDLEKVQKLEAELEKaathrhsyEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSE--ELKEKMDKL 993
Cdd:COG1340    99 RNEFNLGGRSIKSLEREIER--------LEKKQQTSVLTPEEERELVQKIKELRKELEDAKKALEENEKlkELKAEIDEL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  994 TRQLFDdvQKEEQQRLVLEkgfelkTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQaktISE 1073
Cdd:COG1340   171 KKKARE--IHEKIQELANE------AQEYHEEMIKLFEEADELRKEADELHEEFVELSKKIDELHEEFRNLQNE---LRE 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961011 1074 FEKEIELLQAQKIDVEKhvQSQKREMRERMSEVTKQLLESydiedvrSRLSVEDLEHLNEDGEL 1137
Cdd:COG1340   240 LEKKIKALRAKEKAAKR--REKREELKERAEEIYEKFKRG-------EKLTTEELLLLQKAGLV 294
PTZ00121 PTZ00121
MAEBL; Provisional
890-1192 1.96e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.92  E-value: 1.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  890 RVQRLQKKLEDQNRenhglVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRryrdtvEERLSKLQKHNAELE 969
Cdd:PTZ00121 1379 KADAAKKKAEEKKK-----ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK------ADEAKKKAEEAKKAD 1447
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  970 LQRERAEQmlQEKSEELKEKMDKLTRQlfDDVQKEEQQRlvlEKGFELKTQAYE--KQIESLR--EEIKALKDE--RSQL 1043
Cdd:PTZ00121 1448 EAKKKAEE--AKKAEEAKKKAEEAKKA--DEAKKKAEEA---KKADEAKKKAEEakKKADEAKkaAEAKKKADEakKAEE 1520
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1044 HHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDV--EKHVQSQKREMRERMSEVTKQlLESYDIEDVRS 1121
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKaeEAKKAEEDKNMALRKAEEAKK-AEEARIEEVMK 1599
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961011 1122 RLSVEDL---EHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETD 1192
Cdd:PTZ00121 1600 LYEEEKKmkaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
864-1126 2.27e-07

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 55.13  E-value: 2.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   864 KYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKKLE--DQNRENHGLVEKLTSLAALRvgDLEKVQKL-EAELEKAAThr 940
Cdd:pfam17380  259 RYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEkmEQERLRQEKEEKAREVERRR--KLEEAEKArQAEMDRQAA-- 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   941 hSYEEKGRRYRDTvEERLSKLQKHNAELELQRERAEQMLQEKSeelkeKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQ 1020
Cdd:pfam17380  335 -IYAEQERMAMER-ERELERIRQEERKRELERIRQEEIAMEIS-----RMRELERLQMERQQKNERVRQELEAARKVKIL 407
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1021 AYEKQieslrEEIKALKDERSQLHHQLEEG-QVTSDRLKGEVAR-LSKQAKTISEFEKEIELLQAQ-------KIDVEKH 1091
Cdd:pfam17380  408 EEERQ-----RKIQQQKVEMEQIRAEQEEArQREVRRLEEERAReMERVRLEEQERQQQVERLRQQeeerkrkKLELEKE 482
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 568961011  1092 VQSQKREMRERMSEVTKQLLESYD--IEDVRSRLSVE 1126
Cdd:pfam17380  483 KRDRKRAEEQRRKILEKELEERKQamIEEERKRKLLE 519
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
896-1213 2.58e-07

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 54.86  E-value: 2.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   896 KKLEDQNRENHGLVEKLtslaalrvgdLEKVQKLEAELekaATHRHSYEEkgrrYRDTVEERLSKLQKHNAELE------ 969
Cdd:pfam06160  110 DELLESEEKNREEVEEL----------KDKYRELRKTL---LANRFSYGP----AIDELEKQLAEIEEEFSQFEeltesg 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   970 --LQRERAEQMLQEKSEELKEKMDKLTrQLFDDVQKEEQQRL---------VLEKGFELKTQAYEKQIESLREEIKALKd 1038
Cdd:pfam06160  173 dyLEAREVLEKLEEETDALEELMEDIP-PLYEELKTELPDQLeelkegyreMEEEGYALEHLNVDKEIQQLEEQLEENL- 250
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1039 ersqlhHQLEEGQVtsDRLKGEVARLSKQAKTISE-FEKEIEllqAQKiDVEKHvQSQKREMRERMSEVTKQLLESYDIE 1117
Cdd:pfam06160  251 ------ALLENLEL--DEAEEALEEIEERIDQLYDlLEKEVD---AKK-YVEKN-LPEIEDYLEHAEEQNKELKEELERV 317
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1118 DVRSRLSVEDLEHLNE-DGELwfayEGLKKATRVLESHFQSQKDCY----------EKEIEGLNFKVVHLSqeiNHLQKL 1186
Cdd:pfam06160  318 QQSYTLNENELERVRGlEKQL----EELEKRYDEIVERLEEKEVAYselqeeleeiLEQLEEIEEEQEEFK---ESLQSL 390
                          330       340       350
                   ....*....|....*....|....*....|....
gi 568961011  1187 FREETDINESIR------HEVTRLTS-ENMPLLS 1213
Cdd:pfam06160  391 RKDELEAREKLDefklelREIKRLVEkSNLPGLP 424
PTZ00121 PTZ00121
MAEBL; Provisional
890-1115 2.70e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.53  E-value: 2.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  890 RVQRLQKKLEDQNRENHGLVEKLTSLAAlrvgdlEKVQKLEAELEKAATHRHSYEEKGR--RYRDTVEERLSKLQKHNAE 967
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKA------EEAKKAEEAKIKAEELKKAEEEKKKveQLKKKEAEEKKKAEELKKA 1655
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  968 LELQRERAEQmLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLE---KGFELKTQAYE--KQIESLREEIKALKDERSQ 1042
Cdd:PTZ00121 1656 EEENKIKAAE-EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEeakKAEELKKKEAEekKKAEELKKAEEENKIKAEE 1734
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568961011 1043 LHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKhvQSQKREMRERMSEVTKQLLESYD 1115
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE--EELDEEDEKRRMEVDKKIKDIFD 1805
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
890-1112 2.95e-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: 55.03  E-value: 2.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   890 RVQRLQKKLEDQNRENHGLVEKLTSLAaLRVGDLE--------KVQKLEAELEKAathRHSYEEKGRRYRDTVEErLSKL 961
Cdd:TIGR04523  427 EIERLKETIIKNNSEIKDLTNQDSVKE-LIIKNLDntresletQLKVLSRSINKI---KQNLEQKQKELKSKEKE-LKKL 501
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   962 QKHNAELELQreraEQMLQEKSEELKEKMDKLTRQLfddVQKEEQ----QRLVLEKGFELKTQAYEKQIESLREEIKALK 1037
Cdd:TIGR04523  502 NEEKKELEEK----VKDLTKKISSLKEKIEKLESEK---KEKESKisdlEDELNKDDFELKKENLEKEIDEKNKEIEELK 574
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1038 DERSQLHHQLEEGQVTSDRLKGEVARLSKQ----AKTISEFEKEIELLQAQKIDVE---KHVQSQKREMRERMSEVTKQL 1110
Cdd:TIGR04523  575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEieekEKKISSLEKELEKAKKENEKLSsiiKNIKSKKNKLKQEVKQIKETI 654

                   ..
gi 568961011  1111 LE 1112
Cdd:TIGR04523  655 KE 656
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
898-1207 4.32e-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: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 54.40  E-value: 4.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   898 LEDQN----RENHGLVEKLTSLAALRVGDLEKV---QKLEAELEKAATH---RHSYEEKGR----RYRDTVEERLSKLQK 963
Cdd:pfam01576  143 LEDQNnklqKERKLLEERISEFTSNLAEEEEKSkslNKLKNKHEAMISDledRLKKEEKGRqeleKAKRKLEGESSDLQE 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   964 HNAELELQRERAEQMLQEKSEELKEKMDKLTR------QLFDDVQKEEQQRLVLEKGFELKTQA---YEKQIESLREEIK 1034
Cdd:pfam01576  223 QIAELQAQIAELRAQLAKKEEELQAALARLEEetaqknAALKKLRELEAQLSELQEDLESERAArakAEKQRRDLGEELE 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1035 ALKDE--------------RSQ-------LHHQLE------EGQVTSDRLKG-----------EVARLSKQA-------- 1068
Cdd:pfam01576  303 ALKTEledtldttaaqqelRSKreqevteLKKALEeetrshEAQLQEMRQKHtqaleelteqlEQAKRNKASlekakqal 382
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1069 -KTISEFEKEIELLQAQKIDVE---KHVQSQKREMRERMSEVTKQLLEsydIEDVRSRLSVEdLEHLNED-GELWFAYEG 1143
Cdd:pfam01576  383 eSENAELQAELRSLQQAKQDSEhkrKKLEGQLQELQSRLSESERQRAE---LAEKLSKLQSE-LESVSSLlNEAEGKNIK 458
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568961011  1144 LKKATRVLESHFQSQKDCYEKEI-EGLNF--KVVHLSQEINHLQKLFREETDINESIRHEVTRLTSE 1207
Cdd:pfam01576  459 LSKDVSSLESQLQDTQELLQEETrQKLNLssRLRQLEDEKNSLQEQLEEEEEAKRNVERQLQTLQAQ 525
EzrA COG4477
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ...
896-1210 7.11e-07

Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 226883 [Multi-domain]  Cd Length: 570  Bit Score: 53.53  E-value: 7.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  896 KKLEDQNRENHG----LVEKLTSLAALRVGDL-EKVQKLEAELEKAATHRHSYE---EKGrryrDTVEER--LSKLQKHN 965
Cdd:COG4477   131 VESEEKNSEEIDhvleLYEELRRDVLANRHQYgEAAPELEKKLENIEEELSQFVeltSSG----DYIEARevLEEAEEHM 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  966 AELELQRERAEQMLQEKSEELKEKMDKLtrqlfddvqkEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLhh 1045
Cdd:COG4477   207 IALRSIMERIPSLLAELQTELPGQLQDL----------KAGYRDMKEEGYHLEHVNIDSRLERLKEQLVENSELLTQL-- 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1046 QLEEGQVTSDRLKGEVARLSKQaktiseFEKEIEllqAQKIDVEKHvqSQKREMRERMSEVTKQLLEsyDIEDVRS--RL 1123
Cdd:COG4477   275 ELDEAEEELGLIQEKIESLYDL------LEREVE---AKNVVEENL--PILPDYLEKAKENNEHLKE--EIERVKEsyRL 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1124 SVEDL-------EHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINES 1196
Cdd:COG4477   342 AETELgsvrkfeKELKELESVLDEILENIEAQEVAYSELQDNLEEIEKALTDIEDEQEKVQEHLTSLRKDELEARENLER 421
                         330
                  ....*....|....*...
gi 568961011 1197 IR---HEVTR-LTSENMP 1210
Cdd:COG4477   422 LKsklHEIKRyMEKSNLP 439
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
894-1213 8.83e-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: 53.49  E-value: 8.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   894 LQKKLEDQNRENHGLVEKLTSLAalrvgdlEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELElQRE 973
Cdd:TIGR04523  216 LESQISELKKQNNQLKDNIEKKQ-------QEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIK-ELE 287
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   974 RAEQMLQEKSEELK-EKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEK---QIESLREEIKALKDERSQLHHQLEE 1049
Cdd:TIGR04523  288 KQLNQLKSEISDLNnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQlneQISQLKKELTNSESENSEKQRELEE 367
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1050 GQVTSDRLKGEvarlskqaktISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEV-----TKQLLESyDIEDVRSRLS 1124
Cdd:TIGR04523  368 KQNEIEKLKKE----------NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIkklqqEKELLEK-EIERLKETII 436
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1125 -----VEDLEhlNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINEsirh 1199
Cdd:TIGR04523  437 knnseIKDLT--NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEE---- 510
                          330
                   ....*....|....
gi 568961011  1200 EVTRLTSENMPLLS 1213
Cdd:TIGR04523  511 KVKDLTKKISSLKE 524
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
1013-1207 1.62e-06

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 52.79  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1013 KGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHV 1092
Cdd:COG1196   670 KELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEEL 749
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1093 QSQKREMRERMSEVTKQLLEsydIEDVRSRLSvEDLEHLNEDGElwfAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFK 1172
Cdd:COG1196   750 EEELEELQERLEELEEELES---LEEALAKLK-EEIEELEEKRQ---ALQEELEELEEELEEAERRLDALERELESLEQR 822
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 568961011 1173 VVHLSQEINHLQKLFREETDINESIRHEVTRLTSE 1207
Cdd:COG1196   823 RERLEQEIEELEEEIEELEEKLDELEEELEELEKE 857
DUF812 pfam05667
Protein of unknown function (DUF812); This family consists of several eukaryotic proteins of ...
892-1115 1.78e-06

Protein of unknown function (DUF812); This family consists of several eukaryotic proteins of unknown function.


Pssm-ID: 428574 [Multi-domain]  Cd Length: 601  Bit Score: 52.32  E-value: 1.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   892 QRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKV-----QKLEAELEKAATHRHSYEEKGRRYRDTVE-ERLSKLQKHN 965
Cdd:pfam05667  246 TKLLKRIAEQLRSAALASTEATSGASRSKQDLAELlssfgGSSTTDTNLTKGSRFTHTEKLQFTNEEAPaATSSPPTKAE 325
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   966 AELELQRERAEQM--LQEKSEELKEKMDKL----------TRQLFDDVQKEEQQRLVLEKGFELKTQAY------EKQIE 1027
Cdd:pfam05667  326 TEEELQQQREEELeeLQEQLEELESSIEELekeikklessIKQVEEELEELKEQNEELEKQYKVKKKTLdllpdaEENIA 405
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1028 SLREEIKALKDERSQLHHQLEEGQVTsdrLKGEVARLsKQAKTISEFEKEielLQAQKIdvekhvqsqkREMRERMSEVT 1107
Cdd:pfam05667  406 KLQALVEASAQRLVELAGQWEKHRVP---LIEEYRAL-KEAKSNKESESQ---RKLEEI----------KELREKIKEVA 468
                          250
                   ....*....|....*...
gi 568961011  1108 ----------KQLLESYD 1115
Cdd:pfam05667  469 eearskeelyKQLVAEYE 486
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
886-1200 2.35e-06

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: 52.28  E-value: 2.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   886 QLTYRVQRLQKKLEDQNRENHGLVEKLTSLAalrvgdlEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKhn 965
Cdd:TIGR00618  532 RGEQTYAQLETSEEDVYHQLTSERKQRASLK-------EQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK-- 602
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   966 aELELQRERAEQmLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLR--EEIKALKDERSQL 1043
Cdd:TIGR00618  603 -LSEAEDMLACE-QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALsiRVLPKELLASRQL 680
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1044 HHQLEEG---QVTSDR--LKGEVARLSKQAKTISEFEKEIELLQ----AQKIDVEK----HVQSQKREMRERmSEVTKQL 1110
Cdd:TIGR00618  681 ALQKMQSekeQLTYWKemLAQCQTLLRELETHIEEYDREFNEIEnassSLGSDLAAredaLNQSLKELMHQA-RTVLKAR 759
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1111 LESYDIEDVRSRLSV---EDLEHLNEDGELWF-AYEGLKKATRVLESHFQSQKDCYEKEiegLNFKVVHLSQEINHLQKL 1186
Cdd:TIGR00618  760 TEAHFNNNEEVTAALqtgAELSHLAAEIQFFNrLREEDTHLLKTLEAEIGQEIPSDEDI---LNLQCETLVQEEEQFLSR 836
                          330
                   ....*....|....
gi 568961011  1187 FREETDINESIRHE 1200
Cdd:TIGR00618  837 LEEKSATLGEITHQ 850
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
883-1213 2.41e-06

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: 51.94  E-value: 2.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   883 LNIQLTYRVQRLQKKLEDQNRE-NHGLVEKLTSlaalrvgDLEKVQKLEAELEKAATHRhsyeekgrryrdtvEERLSKL 961
Cdd:TIGR04523  282 KIKELEKQLNQLKSEISDLNNQkEQDWNKELKS-------ELKNQEKKLEEIQNQISQN--------------NKIISQL 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   962 QKHNAELELQRERAEQMLQEKSEELKEKMDKLtRQLFDDVQ--KEEQQRLVLEKG-FELKTQAYEKQIESLREEIKALKD 1038
Cdd:TIGR04523  341 NEQISQLKKELTNSESENSEKQRELEEKQNEI-EKLKKENQsyKQEIKNLESQINdLESKIQNQEKLNQQKDEQIKKLQQ 419
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1039 ERSQLHHQLEEGQVTSDRLKGEVARLSKQ-----------AKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVT 1107
Cdd:TIGR04523  420 EKELLEKEIERLKETIIKNNSEIKDLTNQdsvkeliiknlDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK 499
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1108 KQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQS-----QKDCYEKEIEGLNFKVVHLSQEINH 1182
Cdd:TIGR04523  500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKddfelKKENLEKEIDEKNKEIEELKQTQKS 579
                          330       340       350
                   ....*....|....*....|....*....|....
gi 568961011  1183 L---QKLFREETDINESIRHEVTRLTSENMPLLS 1213
Cdd:TIGR04523  580 LkkkQEEKQELIDQKEKEKKDLIKEIEEKEKKIS 613
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
853-1113 2.73e-06

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: 429718 [Multi-domain]  Cd Length: 488  Bit Score: 51.43  E-value: 2.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   853 LLQEHKAVILQK---YARAWLARRRFQNIRRfvlniQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRvgdlekvQKL 929
Cdd:pfam07888   46 LLQAQEAANRQRekeKERYKRDREQWERQRR-----ELESRVAELKEELRQSREKVEELEEKYKELSRSG-------EEL 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   930 EAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKmdkltRQLFDDVQKEEQQRL 1009
Cdd:pfam07888  114 AEEKDALLAQRAESEARIRELEEDIKTLTQRVLERETELERMKERVKKAGAQRKEEEAER-----KQLQAKLQQTEEELR 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1010 VLEKGF-ELKTQAYEK--QIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKi 1086
Cdd:pfam07888  189 SLSKEFqELRNSLAQRdtQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQR- 267
                          250       260
                   ....*....|....*....|....*..
gi 568961011  1087 dveKHVQSQKREMRERMSEVTKQLLES 1113
Cdd:pfam07888  268 ---DRTQAELHQARLQAAQLTLQLADA 291
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ...
932-1208 3.12e-06

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: 51.90  E-value: 3.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   932 ELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEK-----SEELKEKMDKLTRQLFDDVQKEEQ 1006
Cdd:pfam02463  157 EIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKkaleyYQLKEKLELEEEYLLYLDYLKLNE 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1007 QRLVL------------EKGFELKTQAYEKQIESLREEIKALKDERSQ----LHHQLEEGQVTSDRLKGEVARLSKqakt 1070
Cdd:pfam02463  237 ERIDLlqellrdeqeeiESSKQEIEKEEEKLAQVLKENKEEEKEKKLQeeelKLLAKEEEELKSELLKLERRKVDD---- 312
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1071 isefEKEIELLQAQKIDVEKHVQSQKREMRERmsevtKQLLESYDIEDVRSRLSVEDLEHLNEDGELwfAYEGLKKATRV 1150
Cdd:pfam02463  313 ----EEKLKESEKEKKKAEKELKKEKEEIEEL-----EKELKELEIKREAEEEEEEELEKLQEKLEQ--LEEELLAKKKL 381
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568961011  1151 LESHFQSQKDCYEKEIEGLNFKVvhlsQEINHLQKLFREETDINESIRHEVTRLTSEN 1208
Cdd:pfam02463  382 ESERLSSAAKLKEEELELKSEEE----KEAQLLLELARQLEDLLKEEKKEELEILEEE 435
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
924-1084 4.23e-06

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: 426264 [Multi-domain]  Cd Length: 170  Bit Score: 48.42  E-value: 4.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   924 EKVQKLEAELEKAAthrhsyeekgRRYRDTVEERLSKLQKH-NAELELQRERAE-------QMLQEKSEELKEKMDKLTR 995
Cdd:pfam01442    6 TYAEELQEQLGPVA----------QELVDRLEKETEALRERlQKDLEEVRAKLEpyleelqAKLQQNVEELRQRLEPYTE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   996 QLFDDVQK--EEQQRLVLEKGFELKTQAyEKQIESLREEIKALKDE-RSQLHHQLEEGQVTSDRLKGEV-ARLSKQAKTI 1071
Cdd:pfam01442   76 ELRKRLNAdaEELQEKLAPYGEELRERL-EQNVDALRARLAPYAEElRQKLAERLEELKESLAPYAEEVqAQLSQRLQEL 154
                          170
                   ....*....|....
gi 568961011  1072 SE-FEKEIELLQAQ 1084
Cdd:pfam01442  155 REkLEPQAEDLREK 168
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
897-1118 4.39e-06

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: 49.72  E-value: 4.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   897 KLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAE 976
Cdd:pfam06008   41 QIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDL 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   977 QMLQEKSEELKEKMDklTRQLFDDVQKEEQQrlvLEKGFELKTQAyEKQIESLREEIKALKDersQLHHQLEEgqvTSDR 1056
Cdd:pfam06008  121 SRMLAEAQRMLGEIR--SRDFGTQLQNAEAE---LKAAQDLLSRI-QTWFQSPQEENKALAN---ALRDSLAE---YEAK 188
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568961011  1057 LKGEVARLSK-QAKTisefeKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIED 1118
Cdd:pfam06008  189 LSDLRELLREaAAKT-----RDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKTARDSLD 246
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
891-1118 4.54e-06

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 51.31  E-value: 4.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   891 VQRLQKKLEDQNRENHGlveKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQkhNAELEL 970
Cdd:pfam01576  403 SEHKRKKLEGQLQELQS---RLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQ--DTQELL 477
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   971 QRE---------RAEQM------LQEKSEELKEKMDKLTR-------QLFDDVQKEEQQRLVLEKGFELKTQaYEKQIES 1028
Cdd:pfam01576  478 QEEtrqklnlssRLRQLedeknsLQEQLEEEEEAKRNVERqlqtlqaQLSDLKKKLEEDAGAVEALEEGRKR-LQRELEA 556
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1029 L--REEIKA-----LKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRE 1101
Cdd:pfam01576  557 LtqRLEEKAaaydkLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKET 636
                          250
                   ....*....|....*..
gi 568961011  1102 RMSEVTKQLLESYDIED 1118
Cdd:pfam01576  637 KALSLARALEEALDAKE 653
CCDC73 pfam15818
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ...
944-1213 4.89e-06

Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.


Pssm-ID: 434960 [Multi-domain]  Cd Length: 1050  Bit Score: 51.04  E-value: 4.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   944 EEKGRRYRDT-VEERLSKLQKHNAELELQREraeqMLQEKSEEL----KEKMDKLTRQLFDDVQKEEQqrlvlEKG-FEL 1017
Cdd:pfam15818   15 ELRMRREAETqYEEQIGKIIVETQELKWQKE----TLQNQKETLakqhKEAMAVFKKQLQMKMCALEE-----EKGkYQL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1018 KTQAYEKQIESLREEIKALkdersqlhhqleegqvtsdrlkgEVARLSKQaKTISEFEKEIELLQAQKIDVEKhvqsQKR 1097
Cdd:pfam15818   86 ATEIKEKEIEGLKETLKAL-----------------------QVSKYSLQ-KKVSEMEQKVQLHLLAKEDHHK----QLN 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1098 EMRERMSEVTKQL---------LESYDIEDVR--SRLSVedlehLNE--DGELWFAYEGLKKATRVL-ESHFQSQkdcYE 1163
Cdd:pfam15818  138 EIEKYYATITGQFglvkenhekLEQNVQEAIQlnKRLSA-----LNKkqESEICSLKKELKKVTSDLiKSKVTCQ---YK 209
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 568961011  1164 KEIEGLNFKVVHlsQEINHLQKLFREETDINESIRHEVTRLTSENMPLLS 1213
Cdd:pfam15818  210 MGEENINLTIKE--QKFQELQERLNMELELNKKINEEITHIQEEKQDIII 257
ERM pfam00769
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ...
934-1127 6.86e-06

Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.


Pssm-ID: 425860 [Multi-domain]  Cd Length: 247  Bit Score: 48.78  E-value: 6.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   934 EKAATHRHSYEEKGRRYRDT---VEERLSKLQKHNAELELQRERAEQ---MLQEKSEELKEKMDKLTRQLFDdvQKEEQQ 1007
Cdd:pfam00769    2 EEAEREKQELEERLKQYEEEtrkAQEELEESEETAELLEEKLRVAEEeaeLLEQKAQEAEEEKERLEESAEM--EAEEKE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1008 RLvlekgfELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKgevarlskqaktisefEKEIELLQAQKID 1087
Cdd:pfam00769   80 QL------ERELREAQEEVARLEEESERKEEEAERLQEELEEAREEEEEAK----------------EKLLAASTSPSHH 137
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 568961011  1088 VEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVED 1127
Cdd:pfam00769  138 HSEESENEDDEEEEESYEGGSAELSNDGDMDQLSDRIEEE 177
PTZ00121 PTZ00121
MAEBL; Provisional
924-1209 7.06e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 7.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  924 EKVQKLEAELEKAATHRHSYEE--KGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKltRQLFDDV 1001
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEakKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEK--KKAEEAK 1570
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1002 QKEEQQRLVLEKGFELKtQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGE----------VARLSKQAKTI 1071
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAK-KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAeeekkkveqlKKKEAEEKKKA 1649
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1072 SEFEKEIELLQAQKIDVEKHVQSQKREMRE-RMSEVTKQLLESYDIEDVRSRLSVEDLEHLNEDgELWFAyEGLKKATRV 1150
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE-EKKKA-EELKKAEEE 1727
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1151 LESHF-QSQKDCYEKEIEGLNFKVVHlsQEINHLQKLFREETDINESIRHEVTRLTSENM 1209
Cdd:PTZ00121 1728 NKIKAeEAKKEAEEDKKKAEEAKKDE--EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
893-1120 7.11e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 435022 [Multi-domain]  Cd Length: 1112  Bit Score: 50.49  E-value: 7.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   893 RLQKKLEDQNREnhglvekLTSLAALRVGDLEKVQKLEA-----ELEKAAThRHSYEEKGRRYRDTVEER---LSKLQKH 964
Cdd:pfam15921  594 QLEKEINDRRLE-------LQEFKILKDKKDAKIRELEArvsdlELEKVKL-VNAGSERLRAVKDIKQERdqlLNEVKTS 665
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   965 NAELELQRERAEQM---LQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEK-------------GFELKTQAYEKQIES 1028
Cdd:pfam15921  666 RNELNSLSEDYEVLkrnFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSmegsdghamkvamGMQKQITAKRGQIDA 745
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1029 LREEIKAL--------------KDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISE----FEKEIELLQAQKIDVEK 1090
Cdd:pfam15921  746 LQSKIQFLeeamtnankekhflKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEkvanMEVALDKASLQFAECQD 825
                          250       260       270
                   ....*....|....*....|....*....|
gi 568961011  1091 HVQSQKREmrermsEVTKQLLESYDIEDVR 1120
Cdd:pfam15921  826 IIQRQEQE------SVRLKLQHTLDVKELQ 849
mukB PRK04863
chromosome partition protein MukB;
923-1124 9.78e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 50.34  E-value: 9.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  923 LEKVQKLEAELEKAATHRhSYEEKGRRYRD--TVEERLSKLQKHNAELElQRERAEQMLQekseelkekmdkltrQLFDD 1000
Cdd:PRK04863  479 YQLVRKIAGEVSRSEAWD-VARELLRRLREqrHLAEQLQQLRMRLSELE-QRLRQQQRAE---------------RLLAE 541
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1001 VQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEgqvtsdrLKGEVARLSKQAKTISEFEKEIEL 1080
Cdd:PRK04863  542 FCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ-------LQARIQRLAARAPAWLAAQDALAR 614
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568961011 1081 LQAQ-------KIDVEKHVQSQKRemRERMSEVTKQLLES--YDIEDVRSRLS 1124
Cdd:PRK04863  615 LREQsgeefedSQDVTEYMQQLLE--RERELTVERDELAArkQALDEEIERLS 665
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
892-1167 1.06e-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: 1.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   892 QRLQKKLEDQNRENHGLVEKLTslaalrvgDLEKVQKLEAELEKAathrhsyeeKGRRYRDTVEERLSKLQKHNAELELQ 971
Cdd:TIGR00618  246 TQKREAQEEQLKKQQLLKQLRA--------RIEELRAQEAVLEET---------QERINRARKAAPLAAHIKAVTQIEQQ 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   972 RERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLV--LEKGFELKTQAYEKQIeSLREEIKALKDERSQLHHQLEE 1049
Cdd:TIGR00618  309 AQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLqtLHSQEIHIRDAHEVAT-SIREISCQQHTLTQHIHTLQQQ 387
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1050 GQVTSDRLKGEVARLSK---QAKTISEFEKEIELLQAQKIDVEKHVQSQKR--EMRERMSEVTKQLLESYDIEDVRSRLS 1124
Cdd:TIGR00618  388 KTTLTQKLQSLCKELDIlqrEQATIDTRTSAFRDLQGQLAHAKKQQELQQRyaELCAAAITCTAQCEKLEKIHLQESAQS 467
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 568961011  1125 VEDLEHLNEDGELWFAYEGLKKATR--VLESHFQSQKDCYEKEIE 1167
Cdd:TIGR00618  468 LKEREQQLQTKEQIHLQETRKKAVVlaRLLELQEEPCPLCGSCIH 512
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
890-1079 1.13e-05

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 50.10  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  890 RVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLE-KVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAEL 968
Cdd:COG1196   341 ERETLLEELEQLLAELEEAKEELEEKLSALLEELEeLFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERL 420
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  969 ELQRERAEQMLQEKSE------ELKEKMDKLTRQLFDDVQKEEQQRLVLEKgFELKTQAYEKQIESLREEIKALKDERSQ 1042
Cdd:COG1196   421 EDLKEELKELEAELEElqteleELNEELEELEEQLEELRDRLKELERELAE-LQEELQRLEKELSSLEARLDRLEAEQRA 499
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 568961011 1043 LHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIE 1079
Cdd:COG1196   500 SQGVRAVLEALESGLPGVYGPVAELIKVKEKYETALE 536
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
886-1180 1.27e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 435022 [Multi-domain]  Cd Length: 1112  Bit Score: 49.71  E-value: 1.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   886 QLTYRVQRLQKKLEDQNRenhgLVEKLTSLAALRVGDLE-KVQKLEAELEKAATHRhsyeekgRRYRDTVEERLSKLQKH 964
Cdd:pfam15921   82 EYSHQVKDLQRRLNESNE----LHEKQKFYLRQSVIDLQtKLQEMQMERDAMADIR-------RRESQSQEDLRNQLQNT 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   965 NAELELQRERAEQMLQEKSEELkekmDKLTRQLF--DDVQKEEQQRLVlekGFElktQAYEKQIESlreeikalKDERSQ 1042
Cdd:pfam15921  151 VHELEAAKCLKEDMLNDSNTQI----EQLRKMMLshEGVLQEIRSILV---DFE---EASGKKIYE--------HDSMST 212
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1043 LHHQ---------LEEGQVTSDRLKGEVARLSKQAKTI-SEFEKEIELLQAQKID-VEKHVQSQKRE---MRERMSEVTK 1108
Cdd:pfam15921  213 IHFRslgsaiskiLRELDTEISYLKGRIFPVEDQLEALkSESQNKIELLLQQHQDrIEQLISEHEVEitgLTEKASSARS 292
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568961011  1109 QllesydIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEI 1180
Cdd:pfam15921  293 Q------ANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEL 358
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
955-1106 1.33e-05

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: 49.44  E-value: 1.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   955 EERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMD-KLT-----RQLFDDVQKEEQQRLVLEKGFE-LKTQAY--EKQ 1025
Cdd:pfam10174  337 EQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEeKSTlageiRDLKDMLDVKERKINVLQKKIEnLQEQLRdkDKQ 416
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1026 IESLREEIKALKDERSQ-------LHHQLEEGQVTSDRLKGEVARLSKqaktisEFEKEIELLQAQKIDVEKHVQSQKRE 1098
Cdd:pfam10174  417 LAGLKERVKSLQTDSSNtdtalttLEEALSEKERIIERLKEQREREDR------ERLEELESLKKENKDLKEKVSALQPE 490

                   ....*...
gi 568961011  1099 MRERMSEV 1106
Cdd:pfam10174  491 LTEKESSL 498
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ...
845-1137 1.53e-05

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: 49.58  E-value: 1.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   845 LARRRYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLaalrvgdLE 924
Cdd:pfam02463  185 LAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIES-------SK 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   925 KVQKLEAELEKaatHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKE 1004
Cdd:pfam02463  258 QEIEKEEEKLA---QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEK 334
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1005 EQ--QRLVLEKGFELKTQAYEKQIESLREEIKAL---KDERSQLHHQLEEGQVTSDRLKGEVarLSKQAKTISEFEKEIE 1079
Cdd:pfam02463  335 EEieELEKELKELEIKREAEEEEEEELEKLQEKLeqlEEELLAKKKLESERLSSAAKLKEEE--LELKSEEEKEAQLLLE 412
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568961011  1080 LLQAQKIDVEKHVQSQKREmrermSEVTKQLLESYDIEDVRSRLSVEDLEHLNEDGEL 1137
Cdd:pfam02463  413 LARQLEDLLKEEKKEELEI-----LEEEEESIELKQGKLTEEKEELEKQELKLLKDEL 465
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
941-1117 1.78e-05

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 225288 [Multi-domain]  Cd Length: 652  Bit Score: 48.93  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  941 HSYEEKGRRyrdtVEERLSKLQKhnaelELQRERAEQM------LQEKSEELKEKmdkltRQLFDDVQKEEQQRlVLEKG 1014
Cdd:COG2433   355 LAYKPKLEK----VERKLPELGI-----WKDVERIKALvirgypLAEALSKVKEE-----ERPREKEGTEEEER-REITV 419
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1015 FELKTQAYEKQIESLREEIKALKDErsqlhhqLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQs 1094
Cdd:COG2433   420 YEKRIKKLEETVERLEEENSELKRE-------LEELKREIEKLESELERFRREVRDKVRKDREIRARDRRIERLEKELE- 491
                         170       180
                  ....*....|....*....|...
gi 568961011 1095 QKREMRERMSEVTKQLLESYDIE 1117
Cdd:COG2433   492 EKKKRVEELERKLAELRKMRKLE 514
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
627-652 3.41e-05

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: 45.80  E-value: 3.41e-05
                          10        20
                  ....*....|....*....|....*.
gi 568961011  627 KFRSSLYLLMETLNATTPHYVRCIKP 652
Cdd:cd01363   145 IINESLNTLMNVLRATRPHFVRCISP 170
PTZ00121 PTZ00121
MAEBL; Provisional
924-1167 3.56e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 3.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  924 EKVQKLEaELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAEL-----------ELQRERAEQMlqEKSEELKEKMDK 992
Cdd:PTZ00121 1561 EEKKKAE-EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEkkmkaeeakkaEEAKIKAEEL--KKAEEEKKKVEQ 1637
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  993 LTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLR--EEIKALKDERSQLHHQLEEgqvtsdrlKGEVARLSKQAKT 1070
Cdd:PTZ00121 1638 LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKkaEEAKKAEEDEKKAAEALKK--------EAEEAKKAEELKK 1709
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1071 ISEFEKEiellQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRlsveDLEHLNEDGELWfAYEGLKKATRV 1150
Cdd:PTZ00121 1710 KEAEEKK----KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK----KIAHLKKEEEKK-AEEIRKEKEAV 1780
                         250
                  ....*....|....*..
gi 568961011 1151 LESHFQSQKDCYEKEIE 1167
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEVD 1797
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organisation of microtubules varies with the cell type and is ...
890-1009 3.74e-05

MAP7 (E-MAP-115) family; The organisation of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilizing protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 428577 [Multi-domain]  Cd Length: 153  Bit Score: 45.01  E-value: 3.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   890 RVQRLQKKLEDQNR-----ENHGLVEKLTSLAAlrvgdlEKVQKLEAELEKAATHRH-SYEEKGRRYRDTVEERLSKLQK 963
Cdd:pfam05672   21 RQAREQREREEQERlekeeEERLRREELRRRAE------EERARREEEARRLEEERKrEEEERQRKAEEEAEEKEQREKE 94
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 568961011   964 HNAELELQRERAEQMLQEKSEELKEKMDKLTrqlfddvQKEEQQRL 1009
Cdd:pfam05672   95 EQERLQKQKEEAEAKAREEAERQRQEREKIM-------QQEEQERL 133
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
922-1129 3.93e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 433539 [Multi-domain]  Cd Length: 341  Bit Score: 47.22  E-value: 3.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   922 DLEKVQKLEAELEKAATHRHSY----EEKGRRYRDTVEERlsklqKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQL 997
Cdd:pfam13868    4 NSDELRELNSKLLAAKCNKERDaqieEKKRIKAEEKEEER-----RLDEMMEEERERALEEEEEKEEERKEERKQYRQEL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   998 FDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREE----IKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQA-KTIS 1072
Cdd:pfam13868   79 EEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEdqaeAEEKLEKQRQLREEIDEFNEEQAKWKELEKEEEKEEdLRIL 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568961011  1073 EFEKEIELLQAQKidvEKHVQSQKREMRERMSEVTKQLLESYD----IEDVRSRLSVEDLE 1129
Cdd:pfam13868  159 EYLKEKAEREEER---EAERREIKEEKEREIARLRAQQEKAQDekaeRDELRAKLYQEEQE 216
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
896-1204 3.96e-05

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 47.91  E-value: 3.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  896 KKLEDQNRENHGLVEKLtslaalrvgdLEKVQKLEAELekaATHRHSYeekGRRYrDTVEERLSKLQKHNAELE------ 969
Cdd:PRK04778  129 QELLESEEKNREEVEQL----------KDLYRELRKSL---LANRFSF---GPAL-DELEKQLENLEEEFSQFVeltesg 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  970 --LQRERAEQMLQEKSEELKEKMDKLTrQLFDDVQKEEQQRL---------VLEKGFELKTQAYEKQIESLREEIKALKD 1038
Cdd:PRK04778  192 dyVEAREILDQLEEELAALEQIMEEIP-ELLKELQTELPDQLqelkagyreLVEEGYHLDHLDIEKEIQDLKEQIDENLA 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1039 ERSQLhhqleegqvtsdrlkgEVARLSKQAKTISE--------FEKEIEllqAQKiDVEKHvQSQKREMRERMSEVTKQL 1110
Cdd:PRK04778  271 LLEEL----------------DLDEAEEKNEEIQEridqlydiLEREVK---ARK-YVEKN-SDTLPDFLEHAKEQNKEL 329
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1111 L-------ESY-----DIEDVRSRLsvEDLEHLNEDgelwfayegLKKATRVLESH---FQSQKDCYEKEIEGLnfKVVH 1175
Cdd:PRK04778  330 KeeidrvkQSYtlnesELESVRQLE--KQLESLEKQ---------YDEITERIAEQeiaYSELQEELEEILKQL--EEIE 396
                         330       340       350
                  ....*....|....*....|....*....|.
gi 568961011 1176 LSQE--INHLQKLFREETDINESIRHEVTRL 1204
Cdd:PRK04778  397 KEQEklSEMLQGLRKDELEAREKLERYRNKL 427
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
924-1086 4.04e-05

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 47.83  E-value: 4.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   924 EKVQKLEAELE--KAATHRHSYE--EKGRRYRDTVEERLSKLQKHNAELELQRERAEQmlQEKSEELKEKMDKLTRQLFD 999
Cdd:pfam09731  294 REIDQLSKKLAelKKREEKHIERalEKQKEELDKLAEELSARLEEVRAADEAQLRLEF--EREREEIRESYEEKLRTELE 371
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1000 DVQKEEQQRLvlekGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEgqvtsdrLKGEVARLSKQAKTISEFEKEIe 1079
Cdd:pfam09731  372 RQAEAHEEHL----KDVLVEQEIELQREFLQDIKEKVEEERAGRLLKLNE-------LLANLKGLEKATSSHSEVEDEN- 439

                   ....*..
gi 568961011  1080 lLQAQKI 1086
Cdd:pfam09731  440 -RKAQQL 445
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
913-1106 4.07e-05

Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 47.71  E-value: 4.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  913 TSLAALRVGD------LEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEEL 986
Cdd:COG4372    57 ATLAILFLLNrnlrsgVFQLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQ 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  987 KEkMDKLTRQlfddvQKEEQQRLvlekgfelKTQAYEKQieSLREEIKALKDERSQLhhqleegQVTSDRLKGEVARLSK 1066
Cdd:COG4372   137 QE-LARLTKQ-----AQDLQTRL--------KTLAEQRR--QLEAQAQSLQASQKQL-------QASATQLKSQVLDLKL 193
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 568961011 1067 QAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEV 1106
Cdd:COG4372   194 RSAQIEQEAQNLATRANAAQARTEELARRAAAAQQTAQAI 233
Lipoprotein_7 pfam01540
Adhesin lipoprotein; This family consists of the p50 and variable adherence-associated antigen ...
926-1139 4.46e-05

Adhesin lipoprotein; This family consists of the p50 and variable adherence-associated antigen (Vaa) adhesins from Mycoplasma hominis. M. hominis is a mycoplasma associated with human urogenital diseases, pneumonia, and septic arthritis. An adhesin is a cell surface molecule that mediates adhesion to other cells or to the surrounding surface or substrate. The Vaa antigen is a 50-kDa surface lipoprotein that has four tandem repetitive DNA sequences encoding a periodic peptide structure, and is highly immunogenic in the human host. p50 is also a 50-kDa lipoprotein, having three repeats A,B and C, that may be a tetramer of 191-kDa in its native environment.


Pssm-ID: 110537 [Multi-domain]  Cd Length: 353  Bit Score: 47.39  E-value: 4.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   926 VQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAEL-ELQRERAE--QMLQEKSEELKEKM---DKLTRQL-- 997
Cdd:pfam01540   92 ISKLSAAVENAKNEKKAIDDKNAQIAKELAERNAKIQSNIEELkKINNEAFElsKTVNKTIAEVEKKFkipKDFKEQLen 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   998 -FDDVQKEEQQRLVLEKGFELKTQAYEKQIESLRE-------EIK--------ALKDERSQLHhQLEEGQVTSDRLKGEV 1061
Cdd:pfam01540  172 fADDLLDKSRQIDEFTTVTSTQEGFTLAELESFKEitttwfnGMKsewarvldAWKNELTEIN-SIIKGVEELKKLSHEI 250
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961011  1062 ARLSKQA-KTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVEDLEHLNEDGELWF 1139
Cdd:pfam01540  251 SEFSNSVkKTISELEKKFKIDDKTNKEEAKKFKNELENFADQLLNKSHEIDKFVTVTSARGDFSLSELESFKSFNTTWF 329
COG5281 COG5281
Phage-related minor tail protein [Mobilome: prophages, transposons];
894-1136 6.01e-05

Phage-related minor tail protein [Mobilome: prophages, transposons];


Pssm-ID: 227606 [Multi-domain]  Cd Length: 833  Bit Score: 47.33  E-value: 6.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  894 LQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSY--EEKGRRYRDTVEERLSKLQKHNAELELQ 971
Cdd:COG5281   357 LAAKLAAEKLARVTAQGALNARLKLAQDDLTQAELNYAAADQAANQEGALnaREDEAEVLSTQEERRDILKNLLADAEKR 436
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  972 RERAEQMLQEKSEELKEKMDKLTRQLFDDV-QKEEQQRLvlekgfelKTQAYEKQIESLREEIKALKDERSQLhHQLEEG 1050
Cdd:COG5281   437 TARQEELNKALAKAKILQADKAAKAYQEDIlQREAQSRG--------KTAAAERSQEQMTAALKALLAFQQQI-ADLSGA 507
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1051 QVTSDRLKGEVARLSKQAKTISEfEKEIELLQAQKIDvekhvQSQKREmrerMSEVTKQLLESYDIEDVRSRLSVEDLEH 1130
Cdd:COG5281   508 KEKASDQKSLLWKAEEQYALLKE-EAKQRQLQEQKAL-----LEHKKE----TLEYTSQLAELLDQQADRFELSAQAAGS 577

                  ....*.
gi 568961011 1131 LNEDGE 1136
Cdd:COG5281   578 QKERGS 583
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
881-1043 6.80e-05

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 435008 [Multi-domain]  Cd Length: 329  Bit Score: 46.35  E-value: 6.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   881 FVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAathrHSYEEKGRRYR---DTVEER 957
Cdd:pfam15905  176 MAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITEL----SCVSEQVEKYKldiAQLEEL 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   958 LSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLtrqlfddvqKEEQQRLVLEkgFELKTQAYEKQIESLREEIKALK 1037
Cdd:pfam15905  252 LKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLL---------ESEKEELLRE--YEEKEQTLNAELEELKEKLTLEE 320

                   ....*.
gi 568961011  1038 DERSQL 1043
Cdd:pfam15905  321 QEHQKL 326
JMY pfam15871
Junction-mediating and -regulatory protein; JMY, Junction-mediating and -regulatory protein is ...
890-1051 7.26e-05

Junction-mediating and -regulatory protein; JMY, Junction-mediating and -regulatory protein is also a WASP homolog-associated protein with actin, membranes and microtubules. This middle region is the coiled-coil region that putatively binds microtubules to the scaffold. This ability to interact with microtubules plays a role in membrane tubulation.


Pssm-ID: 434985  Cd Length: 298  Bit Score: 46.18  E-value: 7.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   890 RVQRLQKKLEDQNRENHglvEKLTSLAALRVGDLEKVQKLEAELEKaathrhSYEEKGRRYRDTV----EERLSKLQKHN 965
Cdd:pfam15871  129 RVEALQKEAEEWQRRAE---EAVDSIQDITVNYFKETVKALKAMQK------QMEQDQKRFGKAAwasaAPRLEKLKYML 199
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   966 AELELQRERAEQM-LQEKSEELKEKMDKLTrqlfddvQKEEQQRLV--LE-KGFELKTQAYEKQIESLREEIKALKDERS 1041
Cdd:pfam15871  200 AKETLQLMRAKELcLNQKRAEIKKEMESLD-------EGEGAVAVVdeLEiQYYELQLELYEVQLEILKNEELLLTAQLD 272
                          170
                   ....*....|
gi 568961011  1042 QLHHQLEEGQ 1051
Cdd:pfam15871  273 SLRRQIKEKQ 282
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
895-1206 8.60e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 47.02  E-value: 8.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   895 QKKLEDQNRENHGLVEKLTSLAALRVGDLE----KVQKLEAELEKAATHRHSYEEKGRRYRDTVE-ERL--SKLQKHNAE 967
Cdd:pfam05483  417 DEKLLDEKKQFEKIAEELKGKEQELIFLLQarekEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEkEKLknIELTAHCDK 496
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   968 LELQRERAEQMLQEKSEELKEKMDKLtrqlfDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDErsqLHHQL 1047
Cdd:pfam05483  497 LLLENKELTQEASDMTLELKKHQEDI-----INCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDE---VKCKL 568
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1048 EEGQVTSDRLKGEVARLSKQAKTI----SEFEKEIEllqaQKIDVEKHVQSQKREMRERMSEVTKQlLESYDIEDVRSRL 1123
Cdd:pfam05483  569 DKSEENARSIEYEVLKKEKQMKILenkcNNLKKQIE----NKNKNIEELHQENKALKKKGSAENKQ-LNAYEIKVNKLEL 643
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1124 SVEDLEHlnedgelwfayeglkkatrvlesHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFRE----ETDINESIRH 1199
Cdd:pfam05483  644 ELASAKQ-----------------------KFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEavklQKEIDKRCQH 700

                   ....*..
gi 568961011  1200 EVTRLTS 1206
Cdd:pfam05483  701 KIAEMVA 707
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
884-1110 8.81e-05

SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.


Pssm-ID: 293683 [Multi-domain]  Cd Length: 228  Bit Score: 45.50  E-value: 8.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   884 NIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLaalrvgdlekvqKLEAELEKAATHRhsyeeKGRRYRDtVEERLSKLQK 963
Cdd:pfam17078   19 NLQLTVQSQNLLSKLEIAQQKESKFLENLASL------------KHENDNLSSMLNR-----KERRLKD-LEDQLSELKN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   964 HNAELELQ----RERAEQmLQEKSEELKEKMDKLTRQLfdDVQKEEQQRLvlekgfelkTQAYEKQIESLREEIKALKDE 1039
Cdd:pfam17078   81 SYEELTESnkqlKKRLEN-SSASETTLEAELERLQIQY--DALVDSQNEY---------KDHYQQEINTLQESLEDLKLE 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1040 rsqLHHQLEE-GQVTSDRLKGEVARLS------KQAKTISEfEKEIELLQ-----AQKIDVEKHVQSQKrEMRERMSEVT 1107
Cdd:pfam17078  149 ---NEKQLENyQQRISSNDKDIDTKLDsynnkfKNLDNIYV-NKNNKLLTkldslAQLLDLPSWLNLYP-ESRNKILEYA 223

                   ...
gi 568961011  1108 KQL 1110
Cdd:pfam17078  224 EKM 226
CCDC154 pfam15450
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ...
911-1160 8.91e-05

Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.


Pssm-ID: 434726 [Multi-domain]  Cd Length: 520  Bit Score: 46.77  E-value: 8.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   911 KLTSLAALRVGDLEKVQKL--EAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKhnaelelQRERAEQMLQEKSEELKE 988
Cdd:pfam15450  187 KLCSFLQKSFLALEKRMKAseSTRLKAESSLREELEGKWQKLQELTEERLRALTG-------QLEQEEGHLLEQCRGLDE 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   989 KMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESL----REEIKALKDE----RSQLHHQLEEGQVTSDRLKGE 1060
Cdd:pfam15450  260 AVVQLTKFVRQNQVSLNRVLLAEQKARDAKGQLEESRAGELasymQESLEAMQLAgdlaRRETQAALELLQEKSQVLEHS 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1061 VARLSKQAKTISEF--------------------EKEIELLQAQKIDVEKHVQSQK------REMRERMSEVTKQllesy 1114
Cdd:pfam15450  340 VAELVTQLKDLSDHflalswrldlqeqtlglklsEAQEEWEGAERRSLEKLAQWQKevpahlREVQEKVDSLPRQ----- 414
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 568961011  1115 dIEDVRSRL----SVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKD 1160
Cdd:pfam15450  415 -IEAVSDKCvlhkSDSDLKISAEGKAREFEVKALRQELATLLSSVQLLKE 463
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
870-1100 9.80e-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: 46.76  E-value: 9.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   870 LARRRFQNIRrfvLN-IQLTYRVQRLQKKLEDQ-NRENHGLVEKLTSLAA-LRVGDLEKVQKLEAELEKAATHRhsyEEK 946
Cdd:pfam12128  643 FARTALKNAR---LDlRRLFDEKQSEKDKKNKAlAERKDSANERLNSLEAqLKQLDKKHQAWLEEQKEQKREAR---TEK 716
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   947 GRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLtrqlfdDVqkEEQQRLVLEKGFELKTQAYEkQI 1026
Cdd:pfam12128  717 QAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASL------GV--DPDVIAKLKREIRTLERKIE-RI 787
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1027 ESLREEIKALKD--------ERSQLHHQLEEGQVTSDRLKGEVARLSKQAKT-ISEFEKEIELLQAQKIDVEKHVQSQKR 1097
Cdd:pfam12128  788 AVRRQEVLRYFDwyqetwlqRRPRLATQLSNIERAISELQQQLARLIADTKLrRAKLEMERKASEKQQVRLSENLRGLRC 867

                   ...
gi 568961011  1098 EMR 1100
Cdd:pfam12128  868 EMS 870
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
960-1131 1.00e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 45.78  E-value: 1.00e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011    960 KLQKHNAELELQRERAEQMLQEkSEELKEKMDKLtrqlfDDVQKEEQQRLVlekgfelktqAYEKQIESLREEIKALKDE 1039
Cdd:smart00787  120 QLVKTFARLEAKKMWYEWRMKL-LEGLKEGLDEN-----LEGLKEDYKLLM----------KELELLNSIKPKLRDRKDA 183
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   1040 RSQLHHQLEEG-----QVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQS---QKREMRERMSEVTKQLL 1111
Cdd:smart00787  184 LEEELRQLKQLedeleDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDltnKKSELNTEIAEAEKKLE 263
                           170       180
                    ....*....|....*....|...
gi 568961011   1112 ES--YDIEDVRS-RLSVEDLEHL 1131
Cdd:smart00787  264 QCrgFTFKEIEKlKEQLKLLQSL 286
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
924-1082 1.07e-04

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 430106 [Multi-domain]  Cd Length: 176  Bit Score: 44.15  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   924 EKVQKLEAELEKAATHRHSYE-EKGRRYRDTVEERLSKLQKHNAEL-ELQRERAE--QMLQEKSEELKEKMDKLTRQlfd 999
Cdd:pfam08614   21 AENAALQSEPESVPPSTSSSTaSASPVQSASIQSLEQLLAQLREELaELYRSRGElaQQLVDLNEELQELEKKLRED--- 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1000 dvqkeeqqrlvlekgfelktqayEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVA----RLSKQAKTISEFE 1075
Cdd:pfam08614   98 -----------------------ERRLAELEAERAQLEEKLRDREEELREKRKLNQDLQDELValqlQLNMAEEKLRKLE 154

                   ....*...
gi 568961011  1076 KE-IELLQ 1082
Cdd:pfam08614  155 KEnRELVE 162
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1015-1205 1.08e-04

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: 46.59  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1015 FELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVA-----------RLSKQAKTISEFEKEIELLQA 1083
Cdd:TIGR02168  668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEqlrkeleelsrQISALRKDLARLEAEVEQLEE 747
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1084 QKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSvEDLEHLNEDGELW-FAYEGLKKATRVLESHFQSQkdcy 1162
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE-AQIEQLKEELKALrEALDELRAELTLLNEEAANL---- 822
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 568961011  1163 EKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLT 1205
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
924-1100 1.11e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 46.74  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  924 EKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELelqRERAEQMLQEKSEELKEKMDKLTRQLfddvqk 1003
Cdd:PRK00409  523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL---LEEAEKEAQQAIKEAKKEADEIIKEL------ 593
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1004 eeqQRLVLEKGFELKTQAYE---KQIESLREEIKALKDERSQLHHQLEEGQ---VTSDRLKGEVARLSKQAKTISEF--- 1074
Cdd:PRK00409  594 ---RQLQKGGYASVKAHELIearKRLNKANEKKEKKKKKQKEKQEELKVGDevkYLSLGQKGEVLSIPDDKEAIVQAgim 670
                         170       180       190
                  ....*....|....*....|....*....|.
gi 568961011 1075 -----EKEIELLQAQKIDVEKHVQSQKREMR 1100
Cdd:PRK00409  671 kmkvpLSDLEKIQKPKKKKKKKPKTVKPKPR 701
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
957-1085 1.13e-04

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 224755 [Multi-domain]  Cd Length: 225  Bit Score: 45.00  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  957 RLSKLQKHNA-ELELQRERAEQMLQEKSEELKEKMDKLT----------RQLFDDVQKEEQQRLVLEKGFEL-KTQAYEK 1024
Cdd:COG1842     6 RLKDLVKANInELLDKAEDPEKMLEQAIRDMESELAKARqalaqaiarqKQLERKLEEAQARAEKLEEKAELaLQAGNED 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568961011 1025 QIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQaktISEFEKEIELLQAQK 1085
Cdd:COG1842    86 LAREALEEKQSLEDLAKALEAELQQAEEQVEKLKKQLAALEQK---IAELRAKKEALKARK 143
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
890-1104 1.16e-04

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: 46.60  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   890 RVQRLQKKLEDQNRENHGLVEKLTSLAAlrvgDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELE 969
Cdd:TIGR02169  792 RIPEIQAELSKLEEEVSRIEARLREIEQ----KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE 867
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   970 LQRERAEQMLQEKSEELKEkmdkltrqlfddvqkeeqqrlvlekgfelktqaYEKQIESLREEIKALKDERSQLHHQLEE 1049
Cdd:TIGR02169  868 EELEELEAALRDLESRLGD---------------------------------LKKERDELEAQLRELERKIEELEAQIEK 914
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568961011  1050 GQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKhVQSQKREMRERMS 1104
Cdd:TIGR02169  915 KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED-VQAELQRVEEEIR 968
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
875-1208 1.51e-04

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 46.58  E-value: 1.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   875 FQNIRRFVLNIQLTYR-VQRLQKKLED--QNRENHGLVEKLTSLAALRvGDLEKVQKLEAELEKAATHRHSYEEKGRRYR 951
Cdd:TIGR01612 1442 FKNADENNENVLLLFKnIEMADNKSQHilKIKKDNATNDHDFNINELK-EHIDKSKGCKDEADKNAKAIEKNKELFEQYK 1520
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   952 DTVEERLSKLqkhnAELELQ------RERAEQMLQE----------KSEELKEKMDKLTRQLF---DDVQKEEQQ----- 1007
Cdd:TIGR01612 1521 KDVTELLNKY----SALAIKnkfaktKKDSEIIIKEikdahkkfilEAEKSEQKIKEIKKEKFrieDDAAKNDKSnkaai 1596
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1008 --RLVLEKgFE---LKTQAYEKQIESLREEIKALKDERSQL-----HHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKE 1077
Cdd:TIGR01612 1597 diQLSLEN-FEnkfLKISDIKKKINDCLKETESIEKKISSFsidsqDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKE 1675
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1078 IELLQAQ----KIDVEKHVQSQKREMRERMSEV----------TKQLLESyDIEDVRSRLSVEDLEHLNEDGElwfayeg 1143
Cdd:TIGR01612 1676 LDELDSEiekiEIDVDQHKKNYEIGIIEKIKEIaiankeeiesIKELIEP-TIENLISSFNTNDLEGIDPNEK------- 1747
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961011  1144 lkkatrvLESHFQSQKDCYEKEIEGLNFKVvhlsqeiNHLQKLFREETDINEsIRHevTRLTSEN 1208
Cdd:TIGR01612 1748 -------LEEYNTEIGDIYEEFIELYNIIA-------GCLETVSKEPITYDE-IKN--TRINAQN 1795
YhaN COG4717
Uncharacterized protein YhaN, contains AAA domain [Function unknown];
741-1184 1.54e-04

Uncharacterized protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 227061 [Multi-domain]  Cd Length: 984  Bit Score: 46.38  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  741 RAGQVAYLEKLRLDKLRQDCIMIQK---HVRGWLQRRKFLRERQAAltiqryFRGQQTVRKAITAtalkeAWAAIILqky 817
Cdd:COG4717   418 RAGDEAREEKIAANSQVIDKEEVCNlydRRDTAWQKQRFLREKQTA------FERQKTEHTKIIA-----LRLAGML--- 483
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  818 cRGYLVRNLYQLIrvATITIQAHTRGFLarrryrkllqehKAVILQKYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKK 897
Cdd:COG4717   484 -LVALSRLLTSLI--FQIIFAVAQIVFL------------SAEIKSSSRAVREEKAAVTDIPEELARLLITDELPELAVD 548
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  898 LEDQNRENHGLVEKLTSLAALRvgdlEKVQKLEAELEKAATHRHSYEEKGRRYRDT-----------VEERLS------K 960
Cdd:COG4717   549 LLVQSRIRQHWQQLRKALDQLE----AAYEALEGRFAAAEAAMAEWQSEWEEALDElglsrelspeqQLDILStmkdlkK 624
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  961 LQKHNAELELQRERaeqmLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELktqayEKQIESLREEIKALKDER 1040
Cdd:COG4717   625 LMQKKAELTHQVAR----LREEQAAFEERVEGLLAVLEAQFIDLSTLFCVQRLRVAA-----ELQKEEARLALEGNIERT 695
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1041 SQLHHQLEEgqvtsdrlkgevarlskqakTISEFEKEIE-LLQAQKIDVE-------KHVQsQKREMRERMSEVTKQLLE 1112
Cdd:COG4717   696 KELNDELRA--------------------ELELHRKEILdLFDCGTADTEdafreaaREEQ-QLTQRESRLESLEAQLEG 754
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568961011 1113 SYDiedvrSRLSVEDLEHLNEDGELWFAYEglkkatrvleshfQSQKDCYEKEIEGLNFKVVHLSQEINHLQ 1184
Cdd:COG4717   755 VAA-----EAYELSASLDQRELKEEELALL-------------EEAIDALDEEVEELHAQVAALSRQIAQLE 808
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
929-1030 1.54e-04

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: 45.26  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  929 LEAELEKAATHRHSYEEKGRRyrdTVEERLSK-LQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLFDD-----VQ 1002
Cdd:cd16269   187 LQADQALTEKEKEIEAERAKA---EAAEQERKlLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEqeralES 263
                          90       100
                  ....*....|....*....|....*...
gi 568961011 1003 KEEQQRLVLEKGFELKTQAYEKQIESLR 1030
Cdd:cd16269   264 KLKEQEALLEEGFKEQAELLQEEIRSLK 291
COG4026 COG4026
Uncharacterized protein, contains TOPRIM domain, potential nuclease [General function ...
861-1042 1.72e-04

Uncharacterized protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 226513 [Multi-domain]  Cd Length: 290  Bit Score: 44.90  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  861 ILQKYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAAlrvgdleKVQKLEAELEKAATHR 940
Cdd:COG4026   107 LVRKELKNALVRAGLKTLQRVPEYMDLKEDYEELKEKLEELQKEKEELLKELEELEA-------EYEEVQERLKRLEVEN 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  941 HSYEEKgrryRDTVEERLSKLQKHNAELELQRERAEQMLQEK--SEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGF--- 1015
Cdd:COG4026   180 SRLEEM----LKKLPGEVYDLKKRWDELEPGVELPEEELISDlvKETLNLAPKDIEGQGYIYAEDEKEVEILLGTVYiaa 255
                         170       180
                  ....*....|....*....|....*....
gi 568961011 1016 ELKTQAYE--KQIESLREEIKALKDERSQ 1042
Cdd:COG4026   256 PSREDAVEelEIIKEAIEEVIPEIDEEGE 284
COG4026 COG4026
Uncharacterized protein, contains TOPRIM domain, potential nuclease [General function ...
970-1086 1.97e-04

Uncharacterized protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 226513 [Multi-domain]  Cd Length: 290  Bit Score: 44.90  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  970 LQRERAEQMLQEKSEELKEKmdkltrqlFDDVQKEEQQrlVLEKGFELktqayEKQIESLREEIKALKDERSQLHHQLee 1049
Cdd:COG4026   124 LQRVPEYMDLKEDYEELKEK--------LEELQKEKEE--LLKELEEL-----EAEYEEVQERLKRLEVENSRLEEML-- 186
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 568961011 1050 gqvtsDRLKGEVARLSKQaktISEFEKEIELLQAQKI 1086
Cdd:COG4026   187 -----KKLPGEVYDLKKR---WDELEPGVELPEEELI 215
PRK01156 PRK01156
chromosome segregation protein; Provisional
890-1204 1.99e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 45.66  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  890 RVQRLQKKLEDQNRENHGLVEKLTSLAALrvgdLEKVQKLEAELEKAATHRHSYEEKGRRYRDtVEERLSKLQkhNAELE 969
Cdd:PRK01156  219 EIERLSIEYNNAMDDYNNLKSALNELSSL----EDMKNRYESEIKTAESDLSMELEKNNYYKE-LEERHMKII--NDPVY 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  970 LQRERAEQMLQEKSEelKEKMDKLTRQLFDDVQKEEQQRLVLEkgfelktqayekQIESLREEIKALKDERSQLHHQLEE 1049
Cdd:PRK01156  292 KNRNYINDYFKYKND--IENKKQILSNIDAEINKYHAIIKKLS------------VLQKDYNDYIKKKSRYDDLNNQILE 357
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1050 GQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLE-SYDIE--DVRSRLSVE 1126
Cdd:PRK01156  358 LEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDiSSKVSslNQRIRALRE 437
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568961011 1127 DLEHLNEDGELwfaYEGLKKATrVLESHFQSQKDcyEKEIEGLNFKVVHLSQEINHLQklfREETDINESIRHEVTRL 1204
Cdd:PRK01156  438 NLDELSRNMEM---LNGQSVCP-VCGTTLGEEKS--NHIINHYNEKKSRLEEKIREIE---IEVKDIDEKIVDLKKRK 506
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
894-1185 2.01e-04

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: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 45.92  E-value: 2.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   894 LQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAathrHSYEEKGRRYRDTVEERLSKLQkhnAELELQRE 973
Cdd:pfam01576  375 LEKAKQALESENAELQAELRSLQQAKQDSEHKRKKLEGQLQEL----QSRLSESERQRAELAEKLSKLQ---SELESVSS 447
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   974 RAEQmLQEKSEELKEKMDKLTRQLFDD---VQKEEQQRLvlekgfelktqayekqieSLREEIKALKDERSQLHHQLEEg 1050
Cdd:pfam01576  448 LLNE-AEGKNIKLSKDVSSLESQLQDTqelLQEETRQKL------------------NLSSRLRQLEDEKNSLQEQLEE- 507
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1051 qvtsdrlkGEVARlskqaktiSEFEKEIELLQAQKIDVEKHVQsQKREMRERMSEVTKQLLEsyDIEDVRSRLSvedleh 1130
Cdd:pfam01576  508 --------EEEAK--------RNVERQLQTLQAQLSDLKKKLE-EDAGAVEALEEGRKRLQR--ELEALTQRLE------ 562
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568961011  1131 lnedgELWFAYEGLKKATRVLeshfqsqkdcyEKEIEGLNFKVVHLSQEINHLQK 1185
Cdd:pfam01576  563 -----EKAAAYDKLEKTKNRL-----------QQELDDLLVDLDHQRQLVSNLEK 601
K-box pfam01486
K-box region; The K-box region is commonly found associated with SRF-type transcription ...
973-1048 2.03e-04

K-box region; The K-box region is commonly found associated with SRF-type transcription factors see pfam00319. The K-box is a possible coiled-coil structure. Possible role in multimer formation.


Pssm-ID: 426286 [Multi-domain]  Cd Length: 91  Bit Score: 41.29  E-value: 2.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   973 ERAEQMLQEKSEELKEKMDKLTRQL------------FDDVQKEEQQrlvLEKGF----ELKTQAYEKQIESLREEIKAL 1036
Cdd:pfam01486    3 ENEQENWQQEAAKLKKEIENLQRSQrhllgedlsslsLKELQQLEQQ---LEKSLkrirSRKNQLLLEQIEELKKKERIL 79
                           90
                   ....*....|..
gi 568961011  1037 KDERSQLHHQLE 1048
Cdd:pfam01486   80 QEENKELRKKLE 91
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
852-1166 2.09e-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: 45.81  E-value: 2.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   852 KLLQEHKAVILQKYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEA 931
Cdd:TIGR00606  785 KVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKS 864
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   932 ELEKAATHRHSYEEKGRR---YRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRqlfddvqKEEQQR 1008
Cdd:TIGR00606  865 KTNELKSEKLQIGTNLQRrqqFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISS-------KETSNK 937
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1009 LVlekgfelktqayEKQIESLREEIKALKDERSQLHHQLEEGQvtSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDV 1088
Cdd:TIGR00606  938 KA------------QDKVNDIKEKVKNIHGYMKDIENKIQDGK--DDYLKQKETELNTVNAQLEECEKHQEKINEDMRLM 1003
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1089 EKHVQSQKREMRERMSEVTKQLLESyDIEDVRSRLSVEDLEhLNEDG--ELWFAYEGLKKATRVL---ESHFQSQKDCYE 1163
Cdd:TIGR00606 1004 RQDIDTQKIQERWLQDNLTLRKREN-ELKEVEEELKQHLKE-MGQMQvlQMKQEHQKLEENIDLIkrnHVLALGRQKGYE 1081

                   ...
gi 568961011  1164 KEI 1166
Cdd:TIGR00606 1082 KEI 1084
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
890-1129 2.21e-04

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: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 45.54  E-value: 2.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   890 RVQRLQKKLEDQNRENHGLVEKLTSLAalrvgdlekvQKLEAELEKAAthrhSYEEKGRRYRDTVEERLSKLQKHNAELE 969
Cdd:pfam01576   20 KQQKAESELKELEKKHQQLCEEKNILA----------EQLQAETELFA----EAEEMRARLAARKQELEEILHELEARLE 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   970 LQRERAEQMLQEKsEELKEKMDKLTRQLfdDVQKEEQQRLVLEKgfelktQAYEKQIESLREEIKALKDERSQLH---HQ 1046
Cdd:pfam01576   86 EEEERSQQLQNEK-KKMQQHIQDLEEQL--EEEEAARQKLQLEK------VTTEAKIKKMEEDILLLEDQNNKLQkerKL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1047 LEE--GQVTSDRLKGE--VARLS----KQAKTISEFEKEIELLQAQKIDVEKhvqsQKREMRERMSEVTKQLLE-SYDIE 1117
Cdd:pfam01576  157 LEEriSEFTSNLAEEEekSKSLNklknKHEAMISDLEDRLKKEEKGRQELEK----AKRKLEGESSDLQEQIAElQAQIA 232
                          250
                   ....*....|..
gi 568961011  1118 DVRSRLSVEDLE 1129
Cdd:pfam01576  233 ELRAQLAKKEEE 244
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
921-1112 2.72e-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: 434873 [Multi-domain]  Cd Length: 521  Bit Score: 44.94  E-value: 2.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   921 GDLEKVQKLEAELEKAATHRHSYEEKGRRYR---DTVEERLSKLQKHNAELELQR-------ERAEQMLQEKSEELKEKM 990
Cdd:pfam15709  306 GNMESEEERSEEDPSKALLEKREQEKASRDRlraERAEMRRLEVERKRREQEEQRrlqqeqlERAEKMREELELEQQRRF 385
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   991 D--KLTRQLFDDvqkEEQQRLVLEKGFELKTQAYE----KQIESLREEIKALKDERSQlhHQLEEGQVTSDRLKGEVARL 1064
Cdd:pfam15709  386 EeiRLRKQRLEE---ERQRQEEEERKQRLQLQAAQerarQQQEEFRRKLQELQRKKQQ--EEAERAEAEKQRQKELEMQL 460
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 568961011  1065 SKQAKTISEFEKEIEL-LQAQKIDVEKHVQSQKREMRERMSEVTKQLLE 1112
Cdd:pfam15709  461 AEEQKRLMEMAEEERLeYQRQKQEAEEKARLEAEERRQKEEEAARLALE 509
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
887-1060 2.75e-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: 45.48  E-value: 2.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   887 LTYRVQRLQKKLEDQNRENHGLVEKLTSLAA-LRVGDLeKVQKLEAELEKAathRHSYEEKGRRYRDTVEER-------L 958
Cdd:pfam05483  599 LKKQIENKNKNIEELHQENKALKKKGSAENKqLNAYEI-KVNKLELELASA---KQKFEEIIDNYQKEIEDKkiseeklL 674
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   959 SKLQKHNA----ELELQRErAEQMLQEKSEELKEKMDKLTRQlFDDVQKEEQQRLVLEKGfelKTQAYEKQIESLREEIK 1034
Cdd:pfam05483  675 EEVEKAKAiadeAVKLQKE-IDKRCQHKIAEMVALMEKHKHQ-YDKIIEERDSELGLYKN---KEQEQSSAKAALEIELS 749
                          170       180
                   ....*....|....*....|....*.
gi 568961011  1035 ALKDERSQLHHQLEEGQVTSDRLKGE 1060
Cdd:pfam05483  750 NIKAELLSLKKQLEIEKEEKEKLKME 775
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
890-1130 2.80e-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: 45.21  E-value: 2.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   890 RVQRLQKKLEDQNRENHGLVEklTSLAALRvGDL----EKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQkhn 965
Cdd:pfam12128  280 ERQETSAELNQLLRTLDDQWK--EKRDELN-GELsaadAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQ--- 353
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   966 AELELQRER------AEQMLQEKSEELKEKMD-KLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKA--- 1035
Cdd:pfam12128  354 SELENLEERlkaltgKHQDVTAKYNRRRSKIKeQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAgkl 433
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1036 -LKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKhVQSQKREMRERMSEVTKQL-LES 1113
Cdd:pfam12128  434 eFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVER-LQSELRQARKRRDQASEALrQAS 512
                          250
                   ....*....|....*..
gi 568961011  1114 YDIEDVRSRLsvEDLEH 1130
Cdd:pfam12128  513 RRLEERQSAL--DELEL 527
PRK12704 PRK12704
phosphodiesterase; Provisional
954-1109 2.96e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.77  E-value: 2.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  954 VEERLSKLQKHNAE------LELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIE 1027
Cdd:PRK12704   24 VRKKIAEAKIKEAEeeakriLEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1028 SLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEiellQAQKIDVEKhvqsQKREMRERMSEVT 1107
Cdd:PRK12704  104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE----EAKEILLEK----VEEEARHEAAVLI 175

                  ..
gi 568961011 1108 KQ 1109
Cdd:PRK12704  176 KE 177
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
924-1112 2.99e-04

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: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 45.15  E-value: 2.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   924 EKVQKLEAELEkaathrhsyeEKGRRYRDTVEERLSKLQKHNAELELQRErAEQM---LQEKSEELKEKMDKLTRQLfdD 1000
Cdd:pfam01576   19 EKQQKAESELK----------ELEKKHQQLCEEKNILAEQLQAETELFAE-AEEMrarLAARKQELEEILHELEARL--E 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1001 VQKEEQQRLVLEKgfelktQAYEKQIESLREEIKALKDERSQLhhQLEegQVTSDrlkgevarlskqAKtISEFEKEIEL 1080
Cdd:pfam01576   86 EEEERSQQLQNEK------KKMQQHIQDLEEQLEEEEAARQKL--QLE--KVTTE------------AK-IKKMEEDILL 142
                          170       180       190
                   ....*....|....*....|....*....|..
gi 568961011  1081 LQAQKIDVEKhvqsQKREMRERMSEVTKQLLE 1112
Cdd:pfam01576  143 LEDQNNKLQK----ERKLLEERISEFTSNLAE 170
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
979-1185 3.41e-04

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.


Pssm-ID: 405647 [Multi-domain]  Cd Length: 206  Bit Score: 43.22  E-value: 3.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   979 LQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEkgfelktQAYEKQIESLREEIKALKDERSQLHHQLEEGQvtsdrlk 1058
Cdd:pfam14988    9 LAKKTEEKQKKIEKLWNQYVQECEEIERRRQELA-------SRYTQQTAELQTQLLQKEKEQASLKKELQALR------- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1059 gEVARLSKQAktisefEKEIELLQAQKIDVEKHVQSQKREMRERMSEvTKQLLESyDIEDVRSRLSVEDLEHlnedgELW 1138
Cdd:pfam14988   75 -PFAKLKESQ------EREIQDLEEEKEKVRAETAEKDREAHLQFLK-EKALLEK-QLQELRILELGERATR-----ELK 140
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 568961011  1139 FAYEGLK-KATRVLESHFQSQKdcyeKEIEGLNFKVVHLSQEINHLQK 1185
Cdd:pfam14988  141 RKAQALKlAAKQALSEFCRSIK----RENRQLQKELLQLIQETQALEA 184
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ...
747-1079 4.95e-04

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: 44.58  E-value: 4.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   747 YLEKLRLDKLRQDCIMIQKHVRGWLQRRKFLRERQAALTIQRYFRGQQTVRKAITATALKEAWAAIILQKYCRGYLVRNL 826
Cdd:pfam02463  695 LRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEK 774
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   827 yQLIRVATITIQAHTRGFLARRRYRKLLQEHKAVILQKYARAWLarRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENH 906
Cdd:pfam02463  775 -ELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL--EEEQLLIEQEEKIKEEELEELALELKEEQKLEKL 851
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   907 GLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQE----- 981
Cdd:pfam02463  852 AEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEaeill 931
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   982 ----KSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKtqayEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRL 1057
Cdd:pfam02463  932 kyeeEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEEL----GKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKL 1007
                          330       340
                   ....*....|....*....|..
gi 568961011  1058 KGEVARLsKQAKTISEFEKEIE 1079
Cdd:pfam02463 1008 IRAIIEE-TCQRLKEFLELFVS 1028
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
885-1104 4.98e-04

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: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 44.38  E-value: 4.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   885 IQLTYRVQRLQKKLEDQNRENHGLVEKLTSLaalrVGDLEKVQKLEAELEKAathRHSYEEKGRRYRDTVEERLSKLQK- 963
Cdd:pfam01576  639 LSLARALEEALDAKEELERQNKQLRAEMEDL----VSSKDDVGKNVHELERS---KRALEQQVEEMKTQLEELEDELQAt 711
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   964 HNAELEL---------QRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQR---LVLEKGFELKTQAYEKQIESL-- 1029
Cdd:pfam01576  712 EDAKLRLevnmqalkaQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRaqaVAAKKKLELDLKELEAQIEAAnk 791
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1030 -REE-IKALKDERSQ---LHHQLEEGQVTSDRLKGEVARLSKQAKTIsefekEIELLQAQKI-----DVEKHVQSQKREM 1099
Cdd:pfam01576  792 gRDEaVKQLKKLQAQmkdLQRELDEARASRDEIFAQSKESEKKLKSL-----EAELLQLQEDlaaaeRARRQAQQERDEL 866

                   ....*
gi 568961011  1100 RERMS 1104
Cdd:pfam01576  867 AEEIA 871
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
890-1128 5.36e-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: 5.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   890 RVQRLQKKLEDQNREnhgLVEKLTSLAALRvgdlEKVQKLEAELEKAATHRhsyeekgrryrDTVEERLSKLQKHNAELE 969
Cdd:pfam10174  395 KINVLQKKIENLQEQ---LRDKDKQLAGLK----ERVKSLQTDSSNTDTAL-----------TTLEEALSEKERIIERLK 456
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   970 LQRERAEQMLQEKSE-------ELKEKMDKLTRQLFDdvqKEEQQRLVLEKGFELKTQAYEK--QIESLREEIKALKDER 1040
Cdd:pfam10174  457 EQREREDRERLEELEslkkenkDLKEKVSALQPELTE---KESSLIDLKEHASSLASSGLKKdsKLKSLEIAVEQKKEEC 533
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1041 SQLHHQLEEGQVT----------SDRLK-----------------GEVARL-----------SKQAKTISEFEKEIELL- 1081
Cdd:pfam10174  534 SKLENQLKKAHNAeeavrtnpeiNDRIRlleqevarykeesgkaqAEVERLlgilrevenekNDKDKKIAELESLTLRQm 613
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 568961011  1082 --QAQKIDVEKHVQSQKRemRERMSEVTKQLLESYDIEDVRSRLSVEDL 1128
Cdd:pfam10174  614 keQNKKVANIKHGQQEMK--KKGAQLLEEARRREDNLADNSQQLQLEEL 660
PTZ00121 PTZ00121
MAEBL; Provisional
924-1200 5.75e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 5.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  924 EKVQKLEaELEKAATHRHSYE-EKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLtrqlfddvQ 1002
Cdd:PTZ00121 1543 EEKKKAD-ELKKAEELKKAEEkKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA--------K 1613
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1003 KEEQQRLvleKGFELKTQAYE-KQIESLREEIKALKDERSQLHHQLEEGQVtsdrlkgevaRLSKQAKTISEFEKEIELL 1081
Cdd:PTZ00121 1614 KAEEAKI---KAEELKKAEEEkKKVEQLKKKEAEEKKKAEELKKAEEENKI----------KAAEEAKKAEEDKKKAEEA 1680
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1082 QAQKIDVEKHVQSQKREMRE-RMSEVTKQLLEsydiEDVRSRLSVEDLEHLNEdgelwFAYEGLKKatrvlESHFQSQKD 1160
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEaKKAEELKKKEA----EEKKKAEELKKAEEENK-----IKAEEAKK-----EAEEDKKKA 1746
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 568961011 1161 CYEKEIEGLNFKVVHLSQEINHLQKLFREETD--INESIRHE 1200
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEavIEEELDEE 1788
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
887-1201 7.29e-04

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: 43.90  E-value: 7.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   887 LTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDT---VEERLSKLQK 963
Cdd:TIGR02169  411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEydrVEKELSKLQR 490
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   964 HNAELELQRE---------RAEQMLQEKS---------------------------------------------EELKE- 988
Cdd:TIGR02169  491 ELAEAEAQARaseervrggRAVEEVLKASiqgvhgtvaqlgsvgeryataievaagnrlnnvvveddavakeaiELLKRr 570
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   989 -----------KMDKLTRQL-----------------FDD---------------VQKEE-------QQRLV------LE 1012
Cdd:TIGR02169  571 kagratflplnKMRDERRDLsilsedgvigfavdlveFDPkyepafkyvfgdtlvVEDIEaarrlmgKYRMVtlegelFE 650
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1013 K------------GFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQaktISEFEKEIEL 1080
Cdd:TIGR02169  651 KsgamtggsraprGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK---IGEIEKEIEQ 727
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1081 LQAQkidvEKHVQSQKREMRERMSEvTKQLLESYD--IEDVRSRLS------------VEDLE-HLNEDG--ELWFAYEG 1143
Cdd:TIGR02169  728 LEQE----EEKLKERLEELEEDLSS-LEQEIENVKseLKELEARIEeleedlhkleeaLNDLEaRLSHSRipEIQAELSK 802
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568961011  1144 LKKATRVLESHFQSqkdcYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEV 1201
Cdd:TIGR02169  803 LEEEVSRIEARLRE----IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
954-1208 7.47e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 43.98  E-value: 7.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  954 VEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDkltrqlfddvQKEEQQRLVLEKgfelKTQAYEKQIESLREEI 1033
Cdd:COG0419   183 AKAKIEELEGQLSELLEDIEDLLEALEEELKELKKLEE----------IQEEQEEEELEQ----EIEALEERLAELEEEK 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1034 KALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQaktISEFEKEIELLQAQKIDVEkhvqsQKREMRERMSEVTKQLLES 1113
Cdd:COG0419   249 ERLEELKARLLEIESLELEALKIREEELRELERL---LEELEEKIERLEELEREIE-----ELEEELEGLRALLEELEEL 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1114 YD-IEDVRSRLS--VEDLEHLNEDGELWFAYEG-LKKATRVLESHFQSQKDCYEKEIEGLNFKV----VHLSQEINHLQK 1185
Cdd:COG0419   321 LEkLKSLEERLEklEEKLEKLESELEELAEEKNeLAKLLEERLKELEERLEELEKELEKALERLkqleEAIQELKEELAE 400
                         250       260
                  ....*....|....*....|...
gi 568961011 1186 LFREETDINESIRHEVTRLTSEN 1208
Cdd:COG0419   401 LSAALEEIQEELEELEKELEELE 423
PRK12704 PRK12704
phosphodiesterase; Provisional
924-1085 7.74e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.61  E-value: 7.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  924 EKVQKLEAELEKaathrhsyeekgrryrdTVEERLSKLQKhnaeLELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQK 1003
Cdd:PRK12704   64 EEIHKLRNEFEK-----------------ELRERRNELQK----LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1004 EEQqrlVLEKGFELKtQAYEKQIESLrEEIKAL-KDE-RSQLHHQLEEgqvtsdRLKGEVARLskqaktISEFEKEIElL 1081
Cdd:PRK12704  123 QQE---LEKKEEELE-ELIEEQLQEL-ERISGLtAEEaKEILLEKVEE------EARHEAAVL------IKEIEEEAK-E 184

                  ....
gi 568961011 1082 QAQK 1085
Cdd:PRK12704  185 EADK 188
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
884-1058 8.26e-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: 43.66  E-value: 8.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   884 NIQLTYRVQRLQKKL---EDQNRENHGLVEKLtsLAALRVGDLEKVQKLE--AELEKAATHRHSYEEKGRRYRDTVEERL 958
Cdd:pfam10174  553 NPEINDRIRLLEQEVaryKEESGKAQAEVERL--LGILREVENEKNDKDKkiAELESLTLRQMKEQNKKVANIKHGQQEM 630
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   959 SKlqKHNAELELQRERAEQM----LQEKSEELKEKMDKlTRQLFDDVQKE---EQQRLV----------------LEKGF 1015
Cdd:pfam10174  631 KK--KGAQLLEEARRREDNLadnsQQLQLEELMGALEK-TRQELDATKARlssTQQSLAekdghltnlraerrkqLEEIL 707
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1016 ELKTQAYEKQI-----------------ESLREEIKALKDERSQLHHQLEegQVTSDRLK 1058
Cdd:pfam10174  708 EMKQEALLAAIsekdaniallelssskkKKTQEEVMALKREKDRLVHQLK--QQTQNRMK 765
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
943-1122 8.33e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227278 [Multi-domain]  Cd Length: 420  Bit Score: 43.17  E-value: 8.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  943 YEEKGRRYRDTvEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLFD----DVQKEEQQRLVLE------ 1012
Cdd:COG4942    47 IAALEKKIREQ-QDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARlnalEVQEREQRRRLAEqlaalq 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1013 -----------------KGFELKTQAYEKQIESLREEIKALKDERSQLHHQ---LEEGQVTSDRLKGE-VARLSKQAKTI 1071
Cdd:COG4942   126 rsgrnpppallvspedaQRSVRLAIYYGALNPARAERIDALKATLKQLAAVraeIAAEQAELTTLLSEqRAQQAKLAQLL 205
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568961011 1072 SEFEKEIELLQAQKidvEKHvQSQKREMRERMSEVtKQLLESYDIEDVRSR 1122
Cdd:COG4942   206 EERKKTLAQLNSEL---SAD-QKKLEELRANESRL-KNEIASAEAAAAKAR 251
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
852-1127 8.84e-04

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 43.88  E-value: 8.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  852 KLLQEHKAVILQKYA--RAWL------ARRRFQNIRRFVLNIqltyrvqrLQKKLEDQNRENHGLVEKLTSLAALRVGDL 923
Cdd:PTZ00108  980 DILKEFYLVRLDLYKkrKEYLlgklerELARLSNKVRFIKHV--------INGELVITNAKKKDLVKELKKLGYVRFKDI 1051
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  924 EKVQK---LEAELEKAATHRHSYEEKGRRYRDTVEE------------RLSKLQKHNAELELQRERAEQMLQEKSEEL-K 987
Cdd:PTZ00108 1052 IKKKSekiTAEEEEGAEEDDEADDEDDEEELGAAVSydyllsmpiwslTKEKVEKLNAELEKKEKELEKLKNTTPKDMwL 1131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  988 EKMDKLTRQLFDDVQKEEQQRLVLEKgFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRlKGEVARLSKQ 1067
Cdd:PTZ00108 1132 EDLDKFEEALEEQEEVEEKEIAKEQR-LKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSK-RVDSDEKRKL 1209
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1068 AKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVED 1127
Cdd:PTZ00108 1210 DDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEG 1269
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
999-1207 8.99e-04

Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 43.47  E-value: 8.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  999 DDVQKE-EQQRLVLEKGFELKTQAyEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKE 1077
Cdd:COG4372    77 DDIRPQlRALRTELGTAQGEKRAA-ETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTKQAQDLQTRLKT 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1078 IELLQAQKIDVEKHVQSQKREMRERMSEVTKQllesydiedvRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHfQS 1157
Cdd:COG4372   156 LAEQRRQLEAQAQSLQASQKQLQASATQLKSQ----------VLDLKLRSAQIEQEAQNLATRANAAQARTEELARR-AA 224
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 568961011 1158 QKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLTSE 1207
Cdd:COG4372   225 AAQQTAQAIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAQARLEQE 274
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
886-1206 9.07e-04

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: 426331 [Multi-domain]  Cd Length: 1081  Bit Score: 43.61  E-value: 9.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   886 QLTYRVQRLQKKLEDQNRENhglvekltSLAALRVGDLE-KVQKLEAELEKAathrhsyeEKGRryrdtvEERLSKLQKH 964
Cdd:pfam01576  746 QLVKQVRELEAELEDERKQR--------AQAVAAKKKLElDLKELEAQIEAA--------NKGR------DEAVKQLKKL 803
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   965 NAEL-ELQRE-------RAEQMLQEKSEELKEK-MDKLTRQLFDDVQKEEQQRLVLEK-----GFELKTQAYEKQieSLR 1030
Cdd:pfam01576  804 QAQMkDLQREldearasRDEIFAQSKESEKKLKsLEAELLQLQEDLAAAERARRQAQQerdelAEEIASGNSGKS--ALL 881
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1031 EEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTIS-EFEKEIELLQAQKiDVEKHVQSQKREMRERMSEVTKQ 1109
Cdd:pfam01576  882 DEKRRLEARIAQLEEELEEEQSNTELLNDRLRKLTLQVEQLTtELAAERSTSQKSE-SARQQLERQNKELKAKLQEMEGT 960
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1110 L----------LESyDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHfQSQKDCYEKEIEGLNFKVVHL--- 1176
Cdd:pfam01576  961 VkskykssiaaLEA-KIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDE-RRNADQYKDQAEKGNSRLKQLkrq 1038
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 568961011  1177 -------SQEIN----HLQKLFREETDINESIRHEVTRLTS 1206
Cdd:pfam01576 1039 leeaeeeASRANaarrKLQRELDDATESAEAMNREVTTLRS 1079
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
887-1110 9.53e-04

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteristic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 43.13  E-value: 9.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   887 LTYRVQRLQKKLEDQNRENHGLVEKLTSLAALrvgdlekVQKLEAELEKAATHRHSYEEKGRRYR---DTVEERLSKLQK 963
Cdd:pfam19220   88 LVARLAKLEAALREAEAAKEELRIELRDKTAQ-------AEALERQLAAETEQNRALEEENKALReeaQAAEKALQRAEG 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   964 HNAELELQRERAEQ---MLQEKSEELKEKMDKLTRQLFDDVQK--EEQQRL-VLEKGFELKTQAYEKQIESLREEIKALK 1037
Cdd:pfam19220  161 ELATARERLALLEQenrRLQALSEEQAAELAELTRRLAELETQldATRARLrALEGQLAAEQAERERAEAQLEEAVEAHR 240
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1038 DERSQLHHQLEEGQ---VTSDRLKGEVA---------------RLSKQAKTISEFEKEIELLQAQKIDVE---KHVQSQK 1096
Cdd:pfam19220  241 AERASLRMKLEALTaraAATEQLLAEARnqlrdrdeairaaerRLKEASIERDTLERRLAGLEADLERRTqqfQEMQRAR 320
                          250
                   ....*....|....
gi 568961011  1097 REMRERMSEVTKQL 1110
Cdd:pfam19220  321 AELEERAEMLTKAL 334
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
855-1068 1.02e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 224755 [Multi-domain]  Cd Length: 225  Bit Score: 41.92  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  855 QEHKAVILQKYARAwlARRRFQNIRRFVlnIQLTYRVQRLQKKLEDQNRENHGLVEKltSLAALRVGD-------LEKVQ 927
Cdd:COG1842    22 AEDPEKMLEQAIRD--MESELAKARQAL--AQAIARQKQLERKLEEAQARAEKLEEK--AELALQAGNedlareaLEEKQ 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  928 KLEaelEKAATHRHSYEEKgRRYRDTVEERLSKLQKHNAELELQRERAeqMLQEKSEELKEKMDKLTR--------QLFD 999
Cdd:COG1842    96 SLE---DLAKALEAELQQA-EEQVEKLKKQLAALEQKIAELRAKKEAL--KARKAAAKAQEKVNRSLGggssssamAAFE 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961011 1000 DVqkeEQQRLVLEKGFELKTQAYEKQIESLREEIKalkdersqlhhQLEEGQVTSDRLKGEVARLSKQA 1068
Cdd:COG1842   170 RM---EEKIEEREARAEAAAELAEGSGDDLDKEFA-----------QAGAQSAVDSRLAALKARMKGPA 224
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
952-1189 1.06e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 224259 [Multi-domain]  Cd Length: 294  Bit Score: 42.75  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  952 DTVEERLSKLQKHNAELELQRERAEQmLQEKSEELKEKMDKLTRQLfddvqkeeqqRLVLEKGFELKTQAYEkqiesLRE 1031
Cdd:COG1340     6 DKLDELELKRKQLKEEIEELKEKRDE-LRKEASELAEKRDELNAKV----------RELREKAQELREERDE-----INE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1032 EIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQK------IDVEKHVQSQKREMRERMSE 1105
Cdd:COG1340    70 EVQELKEKRDEINAKLQELRKEYRELKEKRNEFNLGGRSIKSLEREIERLEKKQqtsvltPEEERELVQKIKELRKELED 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1106 VTKQLLESYDIEDVRSR---LSVEDLEHLNEDGELwfAYEGLKKATRVLESHfqSQKDCYEKEIEGLNFKVVHLSQEINH 1182
Cdd:COG1340   150 AKKALEENEKLKELKAEideLKKKAREIHEKIQEL--ANEAQEYHEEMIKLF--EEADELRKEADELHEEFVELSKKIDE 225

                  ....*..
gi 568961011 1183 LQKLFRE 1189
Cdd:COG1340   226 LHEEFRN 232
DUF4618 pfam15397
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ...
895-1052 1.18e-03

Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.


Pssm-ID: 434695 [Multi-domain]  Cd Length: 258  Bit Score: 42.24  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   895 QKKLEDQNREnhglVEKLTSLAALRVGDLEK-VQKLEAELEKAATHRHSYeekgRRYRD--------TVEERLSKLQKHN 965
Cdd:pfam15397   62 KKQLQQAKAE----LQEWEEKEESKLNKLEQqLEQLNAKIQKTQEELNFL----STYKDkeypvkavQIANLVRQLQQLK 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   966 AELELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQ---QRLVLEKgfELKTQAYEKQIESLREEIKALKDERSQ 1042
Cdd:pfam15397  134 DSQQDELDELEEMRREVLESLSRKIQKKKEKILSSLAEKTQspyQESLLQK--TRDNQVMLKEIEQFREFIDELEEEIPK 211
                          170
                   ....*....|
gi 568961011  1043 LHHQLEEGQV 1052
Cdd:pfam15397  212 LKAEVQQLQA 221
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
878-1069 1.26e-03

Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 43.09  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  878 IRRFVLNIQLTyRVQRLQKKLEDQNRE-NHGLVEKLTSLAALRvgdlEKVQKLEAELEKAATHRHSYEEKgrryRDTVEE 956
Cdd:COG4372   102 TEREAARSELQ-KARQEREAVRQELAAaRQNLAKAQQELARLT----KQAQDLQTRLKTLAEQRRQLEAQ----AQSLQA 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  957 RLSKLQKHNAELELQRE----RAEQMLQEKSE--ELKEKMDKLTRQLfddvQKEEQQRLVLEKgfelKTQAYEKQIESLR 1030
Cdd:COG4372   173 SQKQLQASATQLKSQVLdlklRSAQIEQEAQNlaTRANAAQARTEEL----ARRAAAAQQTAQ----AIQQRDAQISQKA 244
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 568961011 1031 EEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAK 1069
Cdd:COG4372   245 QQIAARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQ 283
DUF4618 pfam15397
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ...
891-1101 1.32e-03

Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.


Pssm-ID: 434695 [Multi-domain]  Cd Length: 258  Bit Score: 41.86  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   891 VQRLQKKLEDQNRENHGLVEKLTSL---AALRVGDL----EKVQKLEAELEKaathrhSYEEKGRRYRDTVEERLSKLQK 963
Cdd:pfam15397    8 LEELKKHEDFLTKLNLELIKAIQDTedsTALKVRKLlqqyEKFGTIISILEY------SNKKQLQQAKAELQEWEEKEES 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   964 HNAELELQRERAEQMLQEKSEE---LKEKMDK-----------LTRQLfDDVQKEEQ-QRLVLEKGFELKTQAYEKQIES 1028
Cdd:pfam15397   82 KLNKLEQQLEQLNAKIQKTQEElnfLSTYKDKeypvkavqianLVRQL-QQLKDSQQdELDELEEMRREVLESLSRKIQK 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961011  1029 LREEIKALKDERSQLHHQ--LEEGQVTSDRLKGEVARlskQAKTISEFEKEIELLQAQkidVEKhVQSQKREMRE 1101
Cdd:pfam15397  161 KKEKILSSLAEKTQSPYQesLLQKTRDNQVMLKEIEQ---FREFIDELEEEIPKLKAE---VQQ-LQAQRQEPRE 228
GumC COG3206
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane ...
859-1043 1.39e-03

Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225747 [Multi-domain]  Cd Length: 458  Bit Score: 42.82  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  859 AVILQKYARAWLAR------RRFQNIRRFvLNIQLTYRVQRLQ--KKLEDQNRENHGLVE--KLTSLAALRVGDL-EKVQ 927
Cdd:COG3206   171 AKLANALAQAYLADqleaqlEAFRRASDS-LDERLEELRARLQeaEAQVEDFRAQHGLTDaaRGQLLSEQQLSALnTQLQ 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  928 KLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLT---RQLfDDVQKE 1004
Cdd:COG3206   250 SARARLAQAEARLASLLQLLPLGREAAALREVLESPTIQDLRQQYAQVRQQIADLSTELGAKHPQLValeAQL-AELRQQ 328
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 568961011 1005 EQQRLV-LEKGFELKTQAYEKQIESLREEIKALKDERSQL 1043
Cdd:COG3206   329 IAAELRqILASLPNELALLEQQEAALEKELAQLKGRLSKL 368
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
886-1130 1.39e-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: 42.82  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   886 QLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKgrryRDTVEERL------- 958
Cdd:pfam07111  335 QLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQ----TASAEEQLkfvvnam 410
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   959 ----SKLQKHNAELE--------------------------LQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQR 1008
Cdd:pfam07111  411 sstqIWLETTMTRVEqavaripslsnrlsyavrkvhtikglMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREER 490
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1009 LVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLE-EGQVTSDRLKG-----EVARLSKQAKTISEFEKEIELLQ 1082
Cdd:pfam07111  491 NRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEqELQRAQESLASvgqqlEVARQGQQESTEEAASLRQELTQ 570
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568961011  1083 AQKI---DVEKHVQSQKREMRERMSEVTKQLLESYDiEDVRSRLSVEDLEH 1130
Cdd:pfam07111  571 QQEIygqALQEKVAEVETRLREQLSDTKRRLNEARR-EQAKAVVSLRQIQH 620
PTZ00121 PTZ00121
MAEBL; Provisional
852-1261 1.44e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  852 KLLQEHKAVILQKYARAWLARRRFQNIRRfvlNIQLTYRVQRLQKKLEDQNRENHGlVEKLTSLAALRVGDLEKvqKLEA 931
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKK---AEEEKKKVEQLKKKEAEEKKKAEE-LKKAEEENKIKAAEEAK--KAEE 1672
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  932 ELEKAATHRHSYEEKGRRYRDTV--EERLSKLQKHNAELELQRERAEQMLQE------KSEELKEKMDkltrqlfDDVQK 1003
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKkeAEEAKKAEELKKKEAEEKKKAEELKKAeeenkiKAEEAKKEAE-------EDKKK 1745
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1004 EEQQRlvLEKGFELKTQAYEKQIESLREEIKALKDErsqlhhQLEEGQVTSD-RLKGEVARLSKQAKtiSEFEKEIELLQ 1082
Cdd:PTZ00121 1746 AEEAK--KDEEEKKKIAHLKKEEEKKAEEIRKEKEA------VIEEELDEEDeKRRMEVDKKIKDIF--DNFANIIEGGK 1815
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1083 AQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVEDLEHLNEDGElwFAYEGLKKA---TRVLESHFQSQ- 1158
Cdd:PTZ00121 1816 EGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEAD--FNKEKDLKEddeEEIEEADEIEKi 1893
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1159 -KDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESiRHEVTRLTSENMpllsvmcfsatCGNAGYSPASEIAEDHT 1237
Cdd:PTZ00121 1894 dKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEET-REEIIKISKKDM-----------CINDFSSKFCDYMKDNI 1961
                         410       420
                  ....*....|....*....|....*..
gi 568961011 1238 ---RCGYFFRLTICCGFASFLLLWPNH 1261
Cdd:PTZ00121 1962 ssgNCSDEERKELCCSISDFCLKYFDH 1988
RmuC COG1322
DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and ...
890-1069 1.62e-03

DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and repair];


Pssm-ID: 224241 [Multi-domain]  Cd Length: 448  Bit Score: 42.38  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  890 RVQRLQKKLEDQNRENH--GLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEErlsKLQKHNAE 967
Cdd:COG1322    16 NLAFIRQLLLRLGRLEQmlGELAAVLEQLLLLLAFRAEAEQLRTFARSLQALNLELIQELNELKARLQQ---QLLQSREQ 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  968 LELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQrlvLEKGFELKTQAYEKQiesLREEIKALKDERSQLHHQL 1047
Cdd:COG1322    93 LQLLIESLAQLSSEFQELANEIFEELNRRLAELNQQNLKQ---LLKPLREVLEKFREQ---LEQRIHESAEERSTLLEEI 166
                         170       180
                  ....*....|....*....|..
gi 568961011 1048 EEGQvtsdrlkGEVARLSKQAK 1069
Cdd:COG1322   167 DRLL-------GEIQQLAQEAG 181
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
838-1054 1.64e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 434789 [Multi-domain]  Cd Length: 374  Bit Score: 42.34  E-value: 1.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   838 QAHTRGFLARRRYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVlniqlTYRVQRLQKKLEDQNRENhglVEKLTSLA- 916
Cdd:pfam15558  108 QEKLERAAQEAEQRKQCQEQNLKEKEEELQALREQNGLQLQERLE-----QACHKRQLKELEEQKKVQ---ENNLSELLn 179
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   917 --ALRVgDLEKVQKLEAELEKAAT---HRHSYEekgrRYRDTVEERLSKL----QKHNAELELQRERAEQMLQEKSEELK 987
Cdd:pfam15558  180 hqARKV-LVDCQAKAEELLRRLSLeqsLQRSQE----NYEQLVEERHRELrekaQKEEEQFQRAKLRAEEKEEEQQEHKE 254
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   988 ---EKMDKLTRQ--------LFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKAL---KDERSQLHHQ-----LE 1048
Cdd:pfam15558  255 alaELADQKIQQarsvahktVQDKAQRARELNLEREKNHHLLKLKVEKEEECHREGIKEAikkKEQRSEQISRekeatLE 334

                   ....*.
gi 568961011  1049 EGQVTS 1054
Cdd:pfam15558  335 EARKTA 340
UPF0242 pfam06785
Uncharacterized protein family (UPF0242);
904-1036 1.73e-03

Uncharacterized protein family (UPF0242);


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 40.96  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   904 ENHGLVEKLTSLAALrvgDLEKVQKLEAELEKaathRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKS 983
Cdd:pfam06785   66 EKSFLEEKEAKLTEL---DAEGFKILEETLEE----LQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFR 138
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568961011   984 EELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFElKTQAYEKQIESLREEIKAL 1036
Cdd:pfam06785  139 LESEEQLAEKQLLINEYQQTIEEQRSVLEKRQD-QIENLESKVRDLNYEIKTL 190
Filament pfam00038
Intermediate filament protein;
923-1189 1.74e-03

Intermediate filament protein;


Pssm-ID: 425436 [Multi-domain]  Cd Length: 313  Bit Score: 41.82  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   923 LEKVQKLEAE---LEKAATHRhsYEEKGRR-------YRDTVEE---RLSKLQKHNAELELQRERaeqmLQEKSEELKEK 989
Cdd:pfam00038   17 IDKVRFLEQQnkdLETKISEL--RQKKGAEpsrlyslYEREIRElrrQLDTLTVERARLQLELDN----LRLAAEDFRQK 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   990 MDK---LTRQLFDDVQkeeQQRLVLEKGFELKTQAyEKQIESLREEIKALK----DERSQLHHQLEEGQVTsdrLKGEVA 1062
Cdd:pfam00038   91 YEDelnLRQSAEADIV---GLRKDLDEATLARVDL-EMKIESLKEELAFLKknheEEVRELQSQVSDTQVN---VEMDAA 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1063 RLSKQAKTISEFEKEIELLQAQ-KIDVEKHVQSQKREMRERmSEVTKQLLESYDIEDVRSRLSVEDLEHlnedgELwfay 1141
Cdd:pfam00038  164 RKLDLTSALAEIRAQYEEIAEKnREEAEEWYQSKLEELQQA-AARNGDALRSAKEEITELRRQIQSLEI-----EL---- 233
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568961011  1142 EGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINH----LQKLFRE 1189
Cdd:pfam00038  234 QSLKKQKASLERQLAETEERYELQLADYQELISELEAELQQirqeMARQLRE 285
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
886-1199 1.79e-03

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: 42.73  E-value: 1.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   886 QLTYRVQRLQKKLEDQNRENHGLVEKLTSLA-----ALRVGDLE-KVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLS 959
Cdd:TIGR00606  595 KLNKELASLEQNKNHINNELESKEEQLSSYEdklfdVCGSQDEEsDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTD 674
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   960 KLQ----------KHNAELELQRERAEQMLQEKSEELKEkmdklTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESL 1029
Cdd:TIGR00606  675 ENQsccpvcqrvfQTEAELQEFISDLQSKLRLAPDKLKS-----TESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPEL 749
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1030 REEIKALKDERSQLHHQLEEgqvtSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQ 1109
Cdd:TIGR00606  750 RNKLQKVNRDIQRLKNDIEE----QETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQ 825
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1110 LLESyDIEDVRSRL-----SVEDLEHLNEDGELWFAYegLKKATRVLESH-------------FQSQKDCYEKEIEGLNF 1171
Cdd:TIGR00606  826 QVNQ-EKQEKQHELdtvvsKIELNRKLIQDQQEQIQH--LKSKTNELKSEklqigtnlqrrqqFEEQLVELSTEVQSLIR 902
                          330       340
                   ....*....|....*....|....*...
gi 568961011  1172 KVVHLSQEINHLQKLFREETDINESIRH 1199
Cdd:TIGR00606  903 EIKDAKEQDSPLETFLEKDQQEKEELIS 930
mukB PRK04863
chromosome partition protein MukB;
896-1202 1.88e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.64  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  896 KKLEDQNRENHGLVEKLTSLAAlrvgDLEKVQKL--------------------EAELEKAATHR-------HSYEEKGR 948
Cdd:PRK04863  786 KRIEQLRAEREELAERYATLSF----DVQKLQRLhqafsrfigshlavafeadpEAELRQLNRRRveleralADHESQEQ 861
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  949 RYR---DTVEERLSKLQKHNAELELQrerAEQMLQEKSEELKEKMDKLtrqlfddvqkEEQQRLVLEKGFELktQAYEKQ 1025
Cdd:PRK04863  862 QQRsqlEQAKEGLSALNRLLPRLNLL---ADETLADRVEEIREQLDEA----------EEAKRFVQQHGNAL--AQLEPI 926
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1026 IESLR---EEIKALKDERSQLHHQLEEGQVTSDRLKGEVARL-----SKQAKTISEFEKEIELLQAQkidvEKHVQSQKR 1097
Cdd:PRK04863  927 VSVLQsdpEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRahfsyEDAAEMLAKNSDLNEKLRQR----LEQAEQERT 1002
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1098 EMRERMSEVTKQLLEsYD--IEDVRSRLSV-EDL--EHLNEDGELWFAY-EGLKKATRVLE-------SHFQSQKDCYEK 1164
Cdd:PRK04863 1003 RAREQLRQAQAQLAQ-YNqvLASLKSSYDAkRQMlqELKQELQDLGVPAdSGAEERARARRdelharlSANRSRRNQLEK 1081
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 568961011 1165 EIeglnfkvVHLSQEINHLQKLFREETDINESIRHEVT 1202
Cdd:PRK04863 1082 QL-------TFCEAEMDNLTKKLRKLERDYHEMREQVV 1112
PRK09039 PRK09039
peptidoglycan -binding protein;
983-1084 1.89e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.88  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  983 SEEL--KEK-MDKLTRQLfddvqKEEQQRLVLEKgfeLKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKG 1059
Cdd:PRK09039   45 SREIsgKDSaLDRLNSQI-----AELADLLSLER---QGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEG 116
                          90       100
                  ....*....|....*....|....*....
gi 568961011 1060 EVARLSKQ---AKTIS-EFEKEIELLQAQ 1084
Cdd:PRK09039  117 RAGELAQEldsEKQVSaRALAQVELLNQQ 145
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
886-1123 2.21e-03

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 434815 [Multi-domain]  Cd Length: 193  Bit Score: 40.65  E-value: 2.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   886 QLTYRVQRLQKKLEDQNRENHglvekltslaalrvgDLEKVQKLEaelEKAAthrhsyeekgRRYRDTVEERLSKLQKHN 965
Cdd:pfam15619   15 ELQNELAELQRKLEELRKENK---------------LLKRLQRRQ---EKAL----------GKYEDTESELPQLIARHN 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   966 AELELQRERaeqmlqekseeLKEKMDKLTRQlfddvqkeeqqrlvlekgfELKTQAYEKQIESLREEIKALKD------- 1038
Cdd:pfam15619   67 EEVRVLRER-----------LRRSQEKERDL-------------------ERKLKEKEAELLRLRDELKKLKKlsedknl 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1039 -ERSQLHHQLEEGQvtsdrlkgevARLSKQAKTISEFEKEIELLQAQkidVEKHVQSQKREMRERMSEVTKQLLEsydIE 1117
Cdd:pfam15619  117 aEREELQKKLAQLE----------AKLEEKEEKIQELERKLELEEKN---FRRQLAAEKKKHKEAQEEVKILQEE---IE 180

                   ....*.
gi 568961011  1118 DVRSRL 1123
Cdd:pfam15619  181 RLQQKL 186
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
923-1049 2.29e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 225288 [Multi-domain]  Cd Length: 652  Bit Score: 42.38  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  923 LEKVQKLEAELEKAATHRHSYEEKGrryrdTVEERLSKLQKHNAELElqRERAEqmLQEKSEELKEKMDKLTRQLfDDVQ 1002
Cdd:COG2433   394 LSKVKEEERPREKEGTEEEERREIT-----VYEKRIKKLEETVERLE--EENSE--LKRELEELKREIEKLESEL-ERFR 463
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568961011 1003 KEEQQrlvlEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEE 1049
Cdd:COG2433   464 REVRD----KVRKDREIRARDRRIERLEKELEEKKKRVEELERKLAE 506
fliH PRK06669
flagellar assembly protein H; Validated
949-1133 2.55e-03

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 41.16  E-value: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  949 RYRDTVEERLSKL-----QKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQrlvlekgFELKTQAYE 1023
Cdd:PRK06669   37 RLREEEEEQVEQLreeanDEAKEIIEEAEEDAFEIVEAAEEEAKEELLKKTDEASSIIEKLQMQ-------IEREQEEWE 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1024 KQIESLREEIKALKdersqlhhqLEEG-QVTSDRLKGEVARLSKQA-----KTISEFEKEIELLQAQKIDV-----EKHV 1092
Cdd:PRK06669  110 EELERLIEEAKAEG---------YEEGyEKGREEGLEEVRELIEQLnkiieKLIKKREEILESSEEEIVELaldiaKKVI 180
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568961011 1093 QSQKREMRERMSEVTKQLLESY-DIEDVRSRLSVEDLEHLNE 1133
Cdd:PRK06669  181 KEISENSKEIALALVKELLKEVkDATDITIRVNPEDYEYVKE 222
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
892-1109 2.75e-03

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


Pssm-ID: 430780 [Multi-domain]  Cd Length: 302  Bit Score: 41.47  E-value: 2.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   892 QRLQKKLEDQNRENHGLVEKLTSLAALRvgdlEKVQKLEAELEKaatHRHSYEEKGRRYRDTVEERLSKLQKH------- 964
Cdd:pfam09728   42 KKLKKKQDQLQKEKDQLQSELSKAILAK----SKLEKLCRELQK---QNKKLKEESKKLAKEEEEKRKELSEKfqatlkd 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   965 -NAELELQRERAEQMLQEkSEELKEKMDKLTRQL------FDDV--QKEEQQRLVLEK----GFELKTQAYEKQIESLRE 1031
Cdd:pfam09728  115 iQDKMEEKSEPNNKLREE-NEELREKLKSLIEQYelreehFEKLlkTKELEVQLAEAKlqqaTEEEEKKAQEKEVAKARE 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1032 ---EIKALKDERSQLHHQLEE-----GQVTS---------DRLKGEVARLSKQAKTiseFEKEIELLQAQKIDVEKHVQS 1094
Cdd:pfam09728  194 lkaQVQTLSETEKELREQLNLyvekfEEFQDtlnksnevfTTFKKEMEKMSKKIKK---LEKENLTWKRKWEKSNKALLE 270
                          250
                   ....*....|....*
gi 568961011  1095 QKREMRERMSEVTKQ 1109
Cdd:pfam09728  271 MAEERQKLKEELEKL 285
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
890-1037 2.79e-03

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 39.60  E-value: 2.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   890 RVQRLQKKLEDQNRENHGLVEKLTSLAAlrvgdleKVQKLEAELEKAathrhsyEEKGRRYRDTVEERlSKLQKHNAELE 969
Cdd:pfam12718   15 RAEELEEKVKELEQENLEKEQEIKSLTH-------KNQQLEEEVEKL-------EEQLKEAKEKAEES-EKLKTNNENLT 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568961011   970 LQRERAEQMLQEKSEELKEKMDKLtRQLfdDVQKEEQQRLVleKGFELKTQAYEKQIESLREEIKALK 1037
Cdd:pfam12718   80 RKIQLLEEELEESDKRLKETTEKL-RET--DVKAEHLERKV--QALEQERDEWEKKYEELEEKYKEAK 142
DHR10 pfam18595
Designed helical repeat protein 10 domain; Repeat proteins composed of multiple tandem copies ...
926-995 2.91e-03

Designed helical repeat protein 10 domain; Repeat proteins composed of multiple tandem copies of a modular structure unit1 are widespread in nature and have critical roles in molecular recognition, signaling, and other essential biological processes. This entry describes a MazG related domain also designated as Designed helical repeat protein 10 (DHR10). This domain is also found at the N-terminal region of Nuf2 proteins pfam03800.


Pssm-ID: 436606 [Multi-domain]  Cd Length: 117  Bit Score: 38.73  E-value: 2.91e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568961011   926 VQKLEAELEKAATHRHSYEEKGRRYRDTV--EERLSK-LQKHNAELElqreRAEQMLQEKSEELKEKMDKLTR 995
Cdd:pfam18595   49 LAKLEEAKKKLKELRDALEEKEIELRELErrEERLQRqLENAQEKLE----RLREQAEEKREAAQARLEELRE 117
Ax_dynein_light pfam10211
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ...
970-1048 3.34e-03

Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organisms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.


Pssm-ID: 431138 [Multi-domain]  Cd Length: 187  Bit Score: 39.87  E-value: 3.34e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961011   970 LQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQqrlvLEKGFELKTQAYEKQIEslrEEIKALKDERSQLHHQLE 1048
Cdd:pfam10211  115 LQAEQGKSELEKKIADLEEEKEELEKQVAELKAKCEA----IEKREEERRQAEEKKHA---EEIAFLKKTNQQLKAQLE 186
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
831-851 3.54e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 425778  Cd Length: 21  Bit Score: 35.76  E-value: 3.54e-03
                           10        20
                   ....*....|....*....|.
gi 568961011   831 RVATITIQAHTRGFLARRRYR 851
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
954-1109 3.58e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227278 [Multi-domain]  Cd Length: 420  Bit Score: 41.25  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  954 VEERLSKLQKH----NAELELQRERAEQmLQEKSEELKEKMDKLTRQLF---DDVQKEEQQRLVLEKGFELKTQAYEKQI 1026
Cdd:COG4942    36 DDKQLKQIQKEiaalEKKIREQQDQRAK-LEKQLKSLETEIASLEAQLIetaDDLKKLRKQIADLNARLNALEVQEREQR 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1027 ESLREEIKALKdeRSQLHHQLEEGQVTSDRLKGEvaRLSKQ--------AKTISEFEKEIELLQAQKIDVEkhvqSQKRE 1098
Cdd:COG4942   115 RRLAEQLAALQ--RSGRNPPPALLVSPEDAQRSV--RLAIYygalnparAERIDALKATLKQLAAVRAEIA----AEQAE 186
                         170
                  ....*....|.
gi 568961011 1099 MRERMSEVTKQ 1109
Cdd:COG4942   187 LTTLLSEQRAQ 197
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
968-1129 3.67e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  968 LELQRERA-------EQMLQEKSEELkekmDKLTRQLFDDVQKEEQQRLvlekgfelktQAYEKQIESLREEIKALKDER 1040
Cdd:PRK02224  164 LEEYRERAsdarlgvERVLSDQRGSL----DQLKAQIEEKEEKDLHERL----------NGLESELAELDEEIERYEEQR 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1041 SQLHHQLEEGQVTsdrlkgeVARLSKQAKTISEFEKEIELLQAQKIDVEKhvqsQKREMRERMSEVTKQLLE-SYDIEDV 1119
Cdd:PRK02224  230 EQARETRDEADEV-------LEEHEERREELETLEAEIEDLRETIAETER----EREELAEEVRDLRERLEElEEERDDL 298
                         170
                  ....*....|
gi 568961011 1120 RSRLSVEDLE 1129
Cdd:PRK02224  299 LAEAGLDDAD 308
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
830-851 3.99e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 35.76  E-value: 3.99e-03
                            10        20
                    ....*....|....*....|..
gi 568961011    830 IRVATITIQAHTRGFLARRRYR 851
Cdd:smart00015    2 LTRAAIIIQAAWRGYLARKRYK 23
DUF874 pfam05917
Helicobacter pylori protein of unknown function (DUF874); This family consists of several ...
886-1038 4.06e-03

Helicobacter pylori protein of unknown function (DUF874); This family consists of several hypothetical proteins specific to Helicobacter pylori. The function of this family is unknown.


Pssm-ID: 283549 [Multi-domain]  Cd Length: 398  Bit Score: 40.99  E-value: 4.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   886 QLTYRVQRLQKKLEDQNRENHGLVEKLTS-----LAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRyrdtVEERLSK 960
Cdd:pfam05917   81 ELDDKVQDKSKQAEKENQINWWKYSGLTIaasllLAACSAGDTDEQIELEQEKKEAENAEDRANKNGIE----LEQEKQK 156
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568961011   961 LQKHNAELELQRERAEQMLQeKSEELKEKMDKltrqlfdDVQKEEQQRlvlekgfelktqayEKQIESLREEIKALKD 1038
Cdd:pfam05917  157 TNKSGIELANNQIKAEQEQQ-KTEQEKQKAEK-------EAIELEQEK--------------QKTIKTQRDLIKEQKD 212
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ...
910-1135 4.09e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 225638 [Multi-domain]  Cd Length: 1480  Bit Score: 41.80  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  910 EKLTSLAALRVGDLEKVQKLEAELEKAAThRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQ-EKSEELKE 988
Cdd:COG3096   442 EWLETFQAKEEEATEKLLSLEQKMSMAQA-AHSQFEQAYQLVVAIAGELARSEAWDVARELLREGPDQRHLaEQVQPLRM 520
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  989 KMDKLTRQLFDDVQKEE-------QQRLVLE-KGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEgqvtsdrLKGE 1060
Cdd:COG3096   521 RLSELEQRLRQQQSAERlladfckRQGKNLDaEELEALHQELEALIESLSDSVSNAREQRMALRQEQEQ-------LQSR 593
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961011 1061 VARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSvEDLEHLNEDG 1135
Cdd:COG3096   594 IQSLMQRAPVWLAAQNALEQLSEQSGEEFTDSQDVTEYMQQLLEREREATVERDELGARKNALD-EEIERLSQPG 667
PTZ00121 PTZ00121
MAEBL; Provisional
924-1198 4.13e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  924 EKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMlQEKSEELKEKMDKLTRQLFDDVQK 1003
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA-EKKKEEAKKKADAAKKKAEEKKKA 1393
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1004 EEQQRLVLE---KGFELKTQAYEKQIEslrEEIKALKDER---SQLHHQLEEGQVTSD-RLKGEVARLSKQAKTISEFEK 1076
Cdd:PTZ00121 1394 DEAKKKAEEdkkKADELKKAAAAKKKA---DEAKKKAEEKkkaDEAKKKAEEAKKADEaKKKAEEAKKAEEAKKKAEEAK 1470
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1077 EIELLQAQKIDVEKHVQSQKR--EMRERMSEVTKQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEgLKKATRVlesh 1154
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKaeEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE-AKKAEEK---- 1545
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 568961011 1155 fqsqkdcyEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIR 1198
Cdd:PTZ00121 1546 --------KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALR 1581
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
961-1030 4.14e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 397124 [Multi-domain]  Cd Length: 297  Bit Score: 40.73  E-value: 4.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   961 LQKHNAELELQRERAEQML--QEKSEE-----LKEKMDKLTRQLFDDVQ-----KEEQQRLVLEKGFELKTQAYEKQIES 1028
Cdd:pfam02841  216 AEAEQELLREKQKEEEQMMeaQERSYQehvkqLIEKMEAEREQLLAEQErmlehKLQEQEELLKEGFKTEAESLQKEIQD 295

                   ..
gi 568961011  1029 LR 1030
Cdd:pfam02841  296 LK 297
COG4487 COG4487
Uncharacterized protein, contains DUF2130 domain [Function unknown];
892-1085 4.67e-03

Uncharacterized protein, contains DUF2130 domain [Function unknown];


Pssm-ID: 226889 [Multi-domain]  Cd Length: 438  Bit Score: 40.96  E-value: 4.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  892 QRLQKKLEDQNRENHGLV-EKLTSLAALRVGDLEKVQKLEAELEKAATHRHSyEEKGRRYRDTVEERlsklQKHNAELEL 970
Cdd:COG4487    34 QEDQSRILNTLEEFEKEAnEKRAQYRSAKKKELSQLEEQLINQKKEQKNLFN-EQIKQFELALQDEI----AKLEALELL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  971 QRERaEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAyEKQIESlreeikALKDERSQLHHQLEEG 1050
Cdd:COG4487   109 NLEK-DKELELLEKELDELSKELQKQLQNTAEIIEKKRENNKNEERLKFEN-EKKLEE------SLELEREKFEEQLHEA 180
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 568961011 1051 QVTSDRLKGEVARLSKQAktISEFEKEIELLQAQK 1085
Cdd:COG4487   181 NLDLEFKENEEQRESKWA--ILKKLKRRAELGSQQ 213
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
923-1169 4.98e-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: 4.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  923 LEKVQKLEAELEKAAT---HRHSYEEKGRRYR----DTVEERLSKLQKHNAELELQRERAEqmLQEKSEELKEKMDKLT- 994
Cdd:cd16269    61 LQELLDLHAACEKEALevfMKRSFKDEDQKFQkklmEQLEEKKEEFCKQNEEASSKRCQAL--LQELSAPLEEKISQGSy 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  995 -----RQLF-DDVQK-EEQQRLVLEKGFELK--TQAYEKQIESLREEIkaLKDERSQLHHQLEEgqvtsdrlkgEVARLS 1065
Cdd:cd16269   139 svpggYQLYlEDREKlVEKYRQVPRKGVKAEevLQEFLQSKEAEAEAI--LQADQALTEKEKEI----------EAERAK 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1066 KQAKtisefEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLEsyDIEDVRSRLSvEDLEHLnedgelwfayegLK 1145
Cdd:cd16269   207 AEAA-----EQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEE--ERENLLKEQE-RALESK------------LK 266
                         250       260
                  ....*....|....*....|....
gi 568961011 1146 KATRVLESHFQSQKDCYEKEIEGL 1169
Cdd:cd16269   267 EQEALLEEGFKEQAELLQEEIRSL 290
YhaN COG4717
Uncharacterized protein YhaN, contains AAA domain [Function unknown];
894-1130 5.52e-03

Uncharacterized protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 227061 [Multi-domain]  Cd Length: 984  Bit Score: 40.98  E-value: 5.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  894 LQKKLEDQNRENHGLVEKLTSLAALRV--GDLEKVQKLEAEL-EKAATHRH---SYEEKGRRYRDTV---EERLSKLQKH 964
Cdd:COG4717   207 YHKLLESRRAEHARLAELRSELRADRDhiRALRDAVELWPRLqEWKQLEQEltrRREELATFPRDGVlrlEKREAHLQKT 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  965 NAELELQRERAEQM--LQEKSEELKEKMdkltrqLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIK---ALKDE 1039
Cdd:COG4717   287 EAEIDALLVRLAELkdLASQLIPAKEAV------LQALVRLHQQLSEIKASAFELTETLAGIEADLRDKEEAagnGFEAE 360
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1040 RSQLHHQLEEGQVTSDR---LKGEVARLSKQAKTISEFEKEIELLQAQKI-DVEKHVQSQKrEMRERMSEVTKQLLESYD 1115
Cdd:COG4717   361 RVHDLRSLECMLRYQSSqreLKQTEAAYCKRLDEKRLFEDEAEEEARQRLaDDEEEVRAGD-EAREEKIAANSQVIDKEE 439
                         250
                  ....*....|....*
gi 568961011 1116 IEDVRSRLSVEDLEH 1130
Cdd:COG4717   440 VCNLYDRRDTAWQKQ 454
GimC COG1382
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
923-1046 5.71e-03

Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 224300 [Multi-domain]  Cd Length: 119  Bit Score: 38.06  E-value: 5.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  923 LEKVQKLEAELEKAATHRhsyeekgrryrDTVEERLSKLQKHNAELELQRERAEqmLQEKSEELKEKMDKltrqlfDDVQ 1002
Cdd:COG1382    12 LAQLQQLQQQLQKVILQK-----------QQLEAQLKEIEKALEELEKLDEDAP--VYKKVGNLLVKVSK------EEAV 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568961011 1003 KEEQQRLVLekgFELKTQAYEKQIESLREEIKALKDERSQLHHQ 1046
Cdd:COG1382    73 DELEERKET---LELRIKTLEKQEEKLQERLEELQSEIQKALGD 113
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
891-1049 5.89e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 39.74  E-value: 5.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  891 VQRLQKKLEDQNRE---NHGLVEKLTSLA-ALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNA 966
Cdd:cd00176    35 VEALLKKHEALEAElaaHEERVEALNELGeQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  967 ELELQRERAEQMLQEKSEELKEKMDKLTRQL--FDDVQKE------------EQQRLVLEKGFELKTQAYEKQIESLREE 1032
Cdd:cd00176   115 ADDLEQWLEEKEAALASEDLGKDLESVEELLkkHKELEEEleaheprlkslnELAEELLEEGHPDADEEIEEKLEELNER 194
                         170
                  ....*....|....*..
gi 568961011 1033 IKALKDERSQLHHQLEE 1049
Cdd:cd00176   195 WEELLELAEERQKKLEE 211
COG1579 COG1579
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ...
1003-1183 6.02e-03

Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only];


Pssm-ID: 224495 [Multi-domain]  Cd Length: 239  Bit Score: 40.04  E-value: 6.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1003 KEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQ 1082
Cdd:COG1579     3 NNNLKSLLAIQKLDLEKDRLEPRIKEIRKALKKAKAELEALNKALEALEIELEDLENQVSQLESEIQEIRERIKRAEEKL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1083 A------QKIDVEKHVQSQKREMRERMSEVTkqllesyDIEDVRSRLSVEdlehlnedgelwfaYEGLKKATRVLESHFQ 1156
Cdd:COG1579    83 SavkderELRALNIEIQIAKERINSLEDELA-------ELMEEIEKLEKE--------------IEDLKERLERLEKNLA 141
                         170       180
                  ....*....|....*....|....*..
gi 568961011 1157 SQKDCYEKEIEGLNFKVVHLSQEINHL 1183
Cdd:COG1579   142 EAEARLEEEVAEIREEGQELSSKREEL 168
46 PHA02562
endonuclease subunit; Provisional
896-1107 6.32e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.77  E-value: 6.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  896 KKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSyeekgrRYRDTVEERLSKLQKHNAELELQRERA 975
Cdd:PHA02562  170 KLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIA------RKQNKYDELVEEAKTIKAEIEELTDEL 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  976 EQmLQEKSEELKEKMDKLTRQLFDDVQKEEQ-QRLV--LEKGFELKTQAyeKQIESLREEIKALKDERSQLHHQLEEGQV 1052
Cdd:PHA02562  244 LN-LVMDIEDPSAALNKLNTAAAKIKSKIEQfQKVIkmYEKGGVCPTCT--QQISEGPDRITKIKDKLKELQHSLEKLDT 320
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568961011 1053 TSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVT 1107
Cdd:PHA02562  321 AIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFV 375
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
983-1208 7.29e-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: 7.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   983 SEELKEK-MDKLTRQLFDDVQKEEQQRLVLEKGFELKtqayEKQIESLREEIKALKDERSQLhhqleegqvtSDRLKGEV 1061
Cdd:TIGR04523   30 KQDTEEKqLEKKLKTIKNELKNKEKELKNLDKNLNKD----EEKINNSNNKIKILEQQIKDL----------NDKLKKNK 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1062 ARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDvrsrlsveDLEHLNEDgelwfaY 1141
Cdd:TIGR04523   96 DKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEK--------ELEKLNNK------Y 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  1142 EGLKKATRVLEshfqSQKDCYEKEIEGLNFKVVHLSQEINHLQ-KLFREETDI--NESIRHEVTRLTSEN 1208
Cdd:TIGR04523  162 NDLKKQKEELE----NELNLLEKEKLNIQKNIDKIKNKLLKLElLLSNLKKKIqkNKSLESQISELKKQN 227
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
948-1050 7.71e-03

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 223571 [Multi-domain]  Cd Length: 557  Bit Score: 40.28  E-value: 7.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  948 RRYRDTVEERLSKLQKHNAELEL--QRERAEQMLQEKSEELKEKMDKLTRQLfddvqkeEQQRLVLEKGFElktqayekq 1025
Cdd:COG0497   314 RKYGVTIEDLLEYLDKIKEELAQldNSEESLEALEKEVKKLKAELLEAAEAL-------SAIRKKAAKELE--------- 377
                          90       100
                  ....*....|....*....|....*
gi 568961011 1026 iESLREEIKALKDERSQLHHQLEEG 1050
Cdd:COG0497   378 -KEVTAELKALAMEKARFTVELKPL 401
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
899-1037 8.21e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 225288 [Multi-domain]  Cd Length: 652  Bit Score: 40.46  E-value: 8.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011  899 EDQNRENHGLVEKltslAALRVGDLEKV-QKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQ--KHNAELELQRERA 975
Cdd:COG2433   400 EERPREKEGTEEE----ERREITVYEKRiKKLEETVERLEEENSELKRELEELKREIEKLESELErfRREVRDKVRKDRE 475
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961011  976 EQMLQEKSEEL-KEKMDKLTR--QLFDDVQKEEQQRLVLEKGFELKTQAYEK----QIESLREEIKALK 1037
Cdd:COG2433   476 IRARDRRIERLeKELEEKKKRveELERKLAELRKMRKLELSGKGTPVKVVEKltleAIEEAEEEYGIKE 544
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
980-1113 8.82e-03

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 38.05  E-value: 8.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011   980 QEKSEELKEKMdkltRQLFDDVQKEEQQRLVLEKgfelKTQAYEKQIESLREEIKALKDERSQLHH------------QL 1047
Cdd:pfam12718   13 QERAEELEEKV----KELEQENLEKEQEIKSLTH----KNQQLEEEVEKLEEQLKEAKEKAEESEKlktnnenltrkiQL 84
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568961011  1048 --EEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKhvqsqkremreRMSEVTKQLLES 1113
Cdd:pfam12718   85 leEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEK-----------KYEELEEKYKEA 141
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
1023-1109 9.19e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 40.32  E-value: 9.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1023 EKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKtisEFEKEIELLQAQKIDVEKHVQSQKREMRER 1102
Cdd:PRK11448  141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAA---ELEEKQQELEAQLEQLQEKAAETSQERKQK 217

                  ....*..
gi 568961011 1103 MSEVTKQ 1109
Cdd:PRK11448  218 RKEITDQ 224
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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