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Conserved domains on  [gi|78706810|ref|NP_001027208|]
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myosin 95E, isoform E [Drosophila melanogaster]

Protein Classification

class I myosin( domain architecture ID 11715022)

class I myosin is an unconventional myosin; it contains a a head/motor domain that has ATPase activity and functions as a molecular motor, utilizing ATP hydrolysis to generate directed movement toward the plus end along actin filaments

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Motor_domain super family cl22853
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
403-937 2.25e-158

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.


The actual alignment was detected with superfamily member smart00242:

Pssm-ID: 473979 [Multi-domain]  Cd Length: 677  Bit Score: 490.52  E-value: 2.25e-158
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810     403 LEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLKLYRn 482
Cdd:smart00242  140 LEAFGNAKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS- 218
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810     483 VEKYELLRNTTAMEEDRMN----FHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNIDGTEGcqVSNVYEVQ 558
Cdd:smart00242  219 PEDYRYLNQGGCLTVDGIDdaeeFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAST--VKDKEELS 296
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810     559 ETAQLLNMEAQILINCLTRaNSTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQREKN-LALLD 637
Cdd:smart00242  297 NAAELLGVDPEELEKALTK-RKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYfIGVLD 375
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810     638 FYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPSYGILSLINE----P 713
Cdd:smart00242  376 IYGFEIFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEecrfP 455
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810     714 hlNSNDA-LLLRVQQCCAGHPNFMTTGSNS-MCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLSLVQSLFPE 791
Cdd:smart00242  456 --KGTDQtFLEKLNQHHKKHPHFSKPKKKGrTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS 533
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810     792 GNPRRQVTKKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLVHLCRTGHCYHL 871
Cdd:smart00242  534 GVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRL 613
                           490       500       510       520       530       540
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78706810     872 LHVKFFHRYKLLNSLTWPHFhGGSQVEGIALIIRNLPLPSAEFTIGTKNVFVRsPRTVYELEQFRR 937
Cdd:smart00242  614 PFDEFLQRYRVLLPDTWPPW-GGDAKKACEALLQSLGLDEDEYQLGKTKVFLR-PGQLAELEELRE 677
Motor_domain super family cl22853
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
3-123 6.72e-35

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.


The actual alignment was detected with superfamily member smart00242:

Pssm-ID: 473979 [Multi-domain]  Cd Length: 677  Bit Score: 143.45  E-value: 6.72e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810       3 QEIGTWDSVLLENLSEDSFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAY 82
Cdd:smart00242    4 KFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIADNAY 83
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 78706810      83 QSLKDQSEDQCVLLTGESGAGKTETFKMIVNFLTHIQDRSH 123
Cdd:smart00242   84 RNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNT 124
Myosin_TH1 pfam06017
Unconventional myosin tail, actin- and lipid-binding; Unconventional myosins, ie those that ...
1092-1288 7.17e-32

Unconventional myosin tail, actin- and lipid-binding; Unconventional myosins, ie those that are not found in muscle, have the common, classical-type head domain, sometimes a neck with the IQ calmodulin-binding motifs, and then non-standard tails. These tails determine the subcellular localization of the unconventional myosins and also help determine their individual functions. The family carries several different unconventional myosins, eg. Myo1f is expressed mainly in immune cells as well as in the inner ear where it can be associated with deafness, Myo1d has a lipid-binding module in their tail and is implicated in endosome vesicle recycling in epithelial cells. Myo1a, b, c and g from various eukaryotes are also found in this family.


:

Pssm-ID: 461801  Cd Length: 196  Bit Score: 123.48  E-value: 7.17e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   1092 KVTASIIFKDRKASYGRSVGHPFVGDYVRLRHN-----QQWKKICAETNDQYVVFADIINKIARSSgKFVP--------- 1157
Cdd:pfam06017    1 KDYASDLLKGRKERRRFSLLRRFMGDYLGLENNfsgpgPKLRKAVGIGGDEKVLFSDRVSKFNRSS-KPSPrililtdka 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   1158 ---ILLVLSTssllllDQRTLQIKYRVPASEIYRMSLSPYLDDIAVFHVKASEfgrkKGDFVFQTGHVIEIVTKMFLVIQ 1234
Cdd:pfam06017   80 vylIDQKKLK------NGLQYVLKRRIPLSDITGVSVSPLQDDWVVLHLGSPQ----KGDLLLECDFKTELVTHLSKAYK 149
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 78706810   1235 NATGKPPEIHISTEFEANFG---QQTVIFSfkyggmsdlaQGPPKVTRKANRMEIIV 1288
Cdd:pfam06017  150 KKTNRKLNVKIGDTIEYRKKkgkIRTVKFV----------KDEPKGKDSYKSGTVSV 196
 
Name Accession Description Interval E-value
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
403-937 2.25e-158

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: 490.52  E-value: 2.25e-158
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810     403 LEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLKLYRn 482
Cdd:smart00242  140 LEAFGNAKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS- 218
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810     483 VEKYELLRNTTAMEEDRMN----FHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNIDGTEGcqVSNVYEVQ 558
Cdd:smart00242  219 PEDYRYLNQGGCLTVDGIDdaeeFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAST--VKDKEELS 296
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810     559 ETAQLLNMEAQILINCLTRaNSTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQREKN-LALLD 637
Cdd:smart00242  297 NAAELLGVDPEELEKALTK-RKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYfIGVLD 375
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810     638 FYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPSYGILSLINE----P 713
Cdd:smart00242  376 IYGFEIFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEecrfP 455
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810     714 hlNSNDA-LLLRVQQCCAGHPNFMTTGSNS-MCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLSLVQSLFPE 791
Cdd:smart00242  456 --KGTDQtFLEKLNQHHKKHPHFSKPKKKGrTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS 533
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810     792 GNPRRQVTKKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLVHLCRTGHCYHL 871
Cdd:smart00242  534 GVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRL 613
                           490       500       510       520       530       540
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78706810     872 LHVKFFHRYKLLNSLTWPHFhGGSQVEGIALIIRNLPLPSAEFTIGTKNVFVRsPRTVYELEQFRR 937
Cdd:smart00242  614 PFDEFLQRYRVLLPDTWPPW-GGDAKKACEALLQSLGLDEDEYQLGKTKVFLR-PGQLAELEELRE 677
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
403-924 2.29e-151

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: 471.26  E-value: 2.29e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLKLYRN 482
Cdd:cd01378  122 LEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRP 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  483 VEKYELLRNTTAMEE---DRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPitniDGTEGCQVSNVYEVQE 559
Cdd:cd01378  202 EQYYYYSKSGCFDVDgidDAADFKEVLNAMKVIGFTEEEQDSIFRILAAILHLGNIQFAE----DEEGNAAISDTSVLDF 277
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  560 TAQLLNMEAQILINCLT-RANSTNSAQEDV-GCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESL--KSTQREKNLAL 635
Cdd:cd01378  278 VAYLLGVDPDQLEKALThRTIETGGGGRSVyEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLaaKSGGKKKVIGV 357
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  636 LDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPSYGILSLINE--- 712
Cdd:cd01378  358 LDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQEEYVREGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDacl 437
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  713 -PHLNSNDALLLRVQQCCAGHPNFMTTGSN----SMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLSLVQS 787
Cdd:cd01378  438 tAGDATDQTFLQKLNQLFSNHPHFECPSGHfelrRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRS 517
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  788 LFPEGNPRRqVTKKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLVHLCRTGH 867
Cdd:cd01378  518 LFPEGVDLD-SKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGF 596
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 78706810  868 CYHLLHVKFFHRYKLLNSLTWPHFHGGSQvEGIALIIRNLPLPSAEFTIGTKNVFVR 924
Cdd:cd01378  597 AYRQTYEKFLERYKLLSPKTWPAWDGTWQ-GGVESILKDLNIPPEEYQMGKTKIFIR 652
Myosin_head pfam00063
Myosin head (motor domain);
403-924 3.64e-137

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 434.40  E-value: 3.64e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810    403 LEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLKLyRN 482
Cdd:pfam00063  135 LEAFGNAKTVRNNNSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRL-TN 213
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810    483 VEKYELLRN----TTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVpitNIDGTEGCQVSNVYEVQ 558
Cdd:pfam00063  214 PKDYHYLSQsgcyTIDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFK---KERNDEQAVPDDTENLQ 290
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810    559 ETAQLLNMEAQILINCLTRaNSTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQREKN--LALL 636
Cdd:pfam00063  291 KAASLLGIDSTELEKALCK-RRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKAsfIGVL 369
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810    637 DFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPSYGILSLINE---- 712
Cdd:pfam00063  370 DIYGFEIFEKNSFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEeclf 449
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810    713 PHlNSNDALLLRVQQCCAGHPNFM--TTGSNSmCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLSLVQSLFP 790
Cdd:pfam00063  450 PK-ATDQTFLDKLYSTFSKHPHFQkpRLQGET-HFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFP 527
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810    791 EGN--------------PRRQVTKKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSL 856
Cdd:pfam00063  528 DYEtaesaaanesgkstPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGV 607
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78706810    857 MPLVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPHFHGGSQvEGIALIIRNLPLPSAEFTIGTKNVFVR 924
Cdd:pfam00063  608 LEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKGDAK-KGCEAILQSLNLDKEEYQFGKTKIFFR 674
COG5022 COG5022
Myosin heavy chain [General function prediction only];
403-1019 7.67e-116

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 395.60  E-value: 7.67e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLlKSLKLYRN 482
Cdd:COG5022  201 LEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEEL-KKLLLLQN 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  483 VEKYELLRNTTAMEE----DRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNidgtEGCQVSNVYEVQ 558
Cdd:COG5022  280 PKDYIYLSQGGCDKIdgidDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRN----GAAIFSDNSVLD 355
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  559 ETAQLLNMEAQILINCLTRANS-TNSaqEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQREKN-LALL 636
Cdd:COG5022  356 KACYLLGIDPSLFVKWLVKRQIkTGG--EWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNfIGVL 433
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  637 DFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPS-YGILSLINE--- 712
Cdd:COG5022  434 DIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKKNpLGILSLLDEecv 513
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  713 -PHLNSNDAL-----LLRVQQccagHPNFMTTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLSLVQ 786
Cdd:COG5022  514 mPHATDESFTsklaqRLNKNS----NPKFKKSRFRDNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVS 589
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  787 SLFP---EGNPRRqvtkKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLVHLC 863
Cdd:COG5022  590 TLFDdeeNIESKG----RFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRIS 665
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  864 RTGHCYHLLHVKFFHRYKLL---NSLTWPHFHGGSQVEGIALIIRNLPLPSAEFTIGTKNVFVRSPrTVYELEQFRRLRI 940
Cdd:COG5022  666 RAGFPSRWTFDEFVQRYRILspsKSWTGEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAG-VLAALEDMRDAKL 744
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  941 SELAVLIQTMFRMYHARKRFQRMRHSQMIISSAWRTWR-ECRFgipftgRRHLW-SLYRVAREEYRSLKYKRQVRWAIDI 1018
Cdd:COG5022  745 DNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRlRRLV------DYELKwRLFIKLQPLLSLLGSRKEYRSYLAC 818

                 .
gi 78706810 1019 I 1019
Cdd:COG5022  819 I 819
PTZ00014 PTZ00014
myosin-A; Provisional
389-962 1.22e-68

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 248.02  E-value: 1.22e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   389 TQRMRECVTCADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLG 468
Cdd:PTZ00014  216 DLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKG 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   469 ADLQLLKSLKLyRNVEKYELLRN--TTAME-EDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNIDG 545
Cdd:PTZ00014  296 ANDEMKEKYKL-KSLEEYKYINPkcLDVPGiDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGL 374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   546 TEGCQVSNVYE--VQETAQLLNMEAQILINCLTRANSTNSAQEDVGcEMDARQAATNRNTLCRTLYSRLFTWLVNKINES 623
Cdd:PTZ00014  375 TDAAAISDESLevFNEACELLFLDYESLKKELTVKVTYAGNQKIEG-PWSKDESEMLKDSLSKAVYEKLFLWIIRNLNAT 453
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   624 LKSTQREKN-LALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKP 702
Cdd:PTZ00014  454 IEPPGGFKVfIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGK 533
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   703 SYGILSLINEPHL--NSNDALLLRV-QQCCAGHPNFMTTGSNS-MCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFY 778
Cdd:PTZ00014  534 GKSVLSILEDQCLapGGTDEKFVSScNTNLKNNPKYKPAKVDSnKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVK 613
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   779 QSKLSLVQSLFpEGNprrQVTK----KPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYM 854
Cdd:PTZ00014  614 ASPNPLVRDLF-EGV---EVEKgklaKGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSL 689
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   855 SLMPLVHLCRTGHCYHLLHVKFFHRYKLLNsLTWPHFHGGSQVEGIALIIRNLPLPSAEFTIGTKNVFVrSPRTVYELEQ 934
Cdd:PTZ00014  690 SILEALQLRQLGFSYRRTFAEFLSQFKYLD-LAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFL-KKDAAKELTQ 767
                         570       580
                  ....*....|....*....|....*...
gi 78706810   935 FRRLRISELAVLIQtMFRMYHARKRFQR 962
Cdd:PTZ00014  768 IQREKLAAWEPLVS-VLEALILKIKKKR 794
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
3-123 6.72e-35

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: 143.45  E-value: 6.72e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810       3 QEIGTWDSVLLENLSEDSFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAY 82
Cdd:smart00242    4 KFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIADNAY 83
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 78706810      83 QSLKDQSEDQCVLLTGESGAGKTETFKMIVNFLTHIQDRSH 123
Cdd:smart00242   84 RNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNT 124
Myosin_TH1 pfam06017
Unconventional myosin tail, actin- and lipid-binding; Unconventional myosins, ie those that ...
1092-1288 7.17e-32

Unconventional myosin tail, actin- and lipid-binding; Unconventional myosins, ie those that are not found in muscle, have the common, classical-type head domain, sometimes a neck with the IQ calmodulin-binding motifs, and then non-standard tails. These tails determine the subcellular localization of the unconventional myosins and also help determine their individual functions. The family carries several different unconventional myosins, eg. Myo1f is expressed mainly in immune cells as well as in the inner ear where it can be associated with deafness, Myo1d has a lipid-binding module in their tail and is implicated in endosome vesicle recycling in epithelial cells. Myo1a, b, c and g from various eukaryotes are also found in this family.


Pssm-ID: 461801  Cd Length: 196  Bit Score: 123.48  E-value: 7.17e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   1092 KVTASIIFKDRKASYGRSVGHPFVGDYVRLRHN-----QQWKKICAETNDQYVVFADIINKIARSSgKFVP--------- 1157
Cdd:pfam06017    1 KDYASDLLKGRKERRRFSLLRRFMGDYLGLENNfsgpgPKLRKAVGIGGDEKVLFSDRVSKFNRSS-KPSPrililtdka 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   1158 ---ILLVLSTssllllDQRTLQIKYRVPASEIYRMSLSPYLDDIAVFHVKASEfgrkKGDFVFQTGHVIEIVTKMFLVIQ 1234
Cdd:pfam06017   80 vylIDQKKLK------NGLQYVLKRRIPLSDITGVSVSPLQDDWVVLHLGSPQ----KGDLLLECDFKTELVTHLSKAYK 149
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 78706810   1235 NATGKPPEIHISTEFEANFG---QQTVIFSfkyggmsdlaQGPPKVTRKANRMEIIV 1288
Cdd:pfam06017  150 KKTNRKLNVKIGDTIEYRKKkgkIRTVKFV----------KDEPKGKDSYKSGTVSV 196
Myosin_head pfam00063
Myosin head (motor domain);
9-122 2.14e-31

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 132.40  E-value: 2.14e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810      9 DSVLLENLSEDSFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQ 88
Cdd:pfam00063    3 DMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQD 82
                           90       100       110
                   ....*....|....*....|....*....|....
gi 78706810     89 SEDQCVLLTGESGAGKTETFKMIVNFLTHIQDRS 122
Cdd:pfam00063   83 KENQSILISGESGAGKTENTKKIMQYLASVSGSG 116
COG5022 COG5022
Myosin heavy chain [General function prediction only];
3-123 7.21e-30

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 129.43  E-value: 7.21e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810    3 QEIGTWDSVLLENLSEDSFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAY 82
Cdd:COG5022   64 KFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAY 143
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 78706810   83 QSLKDQSEDQCVLLTGESGAGKTETFKMIVNFLTHIQDRSH 123
Cdd:COG5022  144 RNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSST 184
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
19-118 6.40e-29

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: 124.19  E-value: 6.40e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   19 DSFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTG 98
Cdd:cd01378    1 EAINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
                         90       100
                 ....*....|....*....|
gi 78706810   99 ESGAGKTETFKMIVNFLTHI 118
Cdd:cd01378   81 ESGAGKTEASKRIMQYIAAV 100
PTZ00014 PTZ00014
myosin-A; Provisional
27-115 2.83e-12

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 71.21  E-value: 2.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810    27 QRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGD-KGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGESGAGKT 105
Cdd:PTZ00014  118 HRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDaKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKT 197
                          90
                  ....*....|
gi 78706810   106 ETFKMIVNFL 115
Cdd:PTZ00014  198 EATKQIMRYF 207
 
Name Accession Description Interval E-value
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
403-937 2.25e-158

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: 490.52  E-value: 2.25e-158
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810     403 LEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLKLYRn 482
Cdd:smart00242  140 LEAFGNAKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS- 218
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810     483 VEKYELLRNTTAMEEDRMN----FHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNIDGTEGcqVSNVYEVQ 558
Cdd:smart00242  219 PEDYRYLNQGGCLTVDGIDdaeeFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAST--VKDKEELS 296
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810     559 ETAQLLNMEAQILINCLTRaNSTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQREKN-LALLD 637
Cdd:smart00242  297 NAAELLGVDPEELEKALTK-RKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYfIGVLD 375
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810     638 FYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPSYGILSLINE----P 713
Cdd:smart00242  376 IYGFEIFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEecrfP 455
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810     714 hlNSNDA-LLLRVQQCCAGHPNFMTTGSNS-MCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLSLVQSLFPE 791
Cdd:smart00242  456 --KGTDQtFLEKLNQHHKKHPHFSKPKKKGrTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS 533
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810     792 GNPRRQVTKKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLVHLCRTGHCYHL 871
Cdd:smart00242  534 GVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRL 613
                           490       500       510       520       530       540
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78706810     872 LHVKFFHRYKLLNSLTWPHFhGGSQVEGIALIIRNLPLPSAEFTIGTKNVFVRsPRTVYELEQFRR 937
Cdd:smart00242  614 PFDEFLQRYRVLLPDTWPPW-GGDAKKACEALLQSLGLDEDEYQLGKTKVFLR-PGQLAELEELRE 677
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
403-924 2.29e-151

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: 471.26  E-value: 2.29e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLKLYRN 482
Cdd:cd01378  122 LEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRP 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  483 VEKYELLRNTTAMEE---DRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPitniDGTEGCQVSNVYEVQE 559
Cdd:cd01378  202 EQYYYYSKSGCFDVDgidDAADFKEVLNAMKVIGFTEEEQDSIFRILAAILHLGNIQFAE----DEEGNAAISDTSVLDF 277
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  560 TAQLLNMEAQILINCLT-RANSTNSAQEDV-GCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESL--KSTQREKNLAL 635
Cdd:cd01378  278 VAYLLGVDPDQLEKALThRTIETGGGGRSVyEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLaaKSGGKKKVIGV 357
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  636 LDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPSYGILSLINE--- 712
Cdd:cd01378  358 LDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQEEYVREGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDacl 437
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  713 -PHLNSNDALLLRVQQCCAGHPNFMTTGSN----SMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLSLVQS 787
Cdd:cd01378  438 tAGDATDQTFLQKLNQLFSNHPHFECPSGHfelrRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRS 517
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  788 LFPEGNPRRqVTKKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLVHLCRTGH 867
Cdd:cd01378  518 LFPEGVDLD-SKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGF 596
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 78706810  868 CYHLLHVKFFHRYKLLNSLTWPHFHGGSQvEGIALIIRNLPLPSAEFTIGTKNVFVR 924
Cdd:cd01378  597 AYRQTYEKFLERYKLLSPKTWPAWDGTWQ-GGVESILKDLNIPPEEYQMGKTKIFIR 652
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
403-924 1.98e-137

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


Pssm-ID: 276950 [Multi-domain]  Cd Length: 633  Bit Score: 433.56  E-value: 1.98e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLKLYRN 482
Cdd:cd00124  127 LEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELL 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  483 VEKYELLRNTTA-------MEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNiDGTEGCQVSNVY 555
Cdd:cd00124  207 LSYYYLNDYLNSsgcdridGVDDAEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEE-DEDSSAEVADDE 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  556 EVQETAQLLNMEAQILINCLTraNSTNSAQEDVGC-EMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQREKN-- 632
Cdd:cd00124  286 SLKAAAKLLGVDAEDLEEALT--TRTIKVGGETITkPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAESts 363
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  633 -LALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPSYGILSLIN 711
Cdd:cd00124  364 fIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKPLGILSLLD 443
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  712 E----PhlNSNDALLLR-VQQCCAGHPNFMT-TGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPkyisaafyQSKLSLV 785
Cdd:cd00124  444 EeclfP--KGTDATFLEkLYSAHGSHPRFFSkKRKAKLEFGIKHYAGDVTYDADGFLEKNKDTLP--------PDLVDLL 513
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  786 QSlfpegnprrqvtkkpstlSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLVHLCRT 865
Cdd:cd00124  514 RS------------------GSQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRA 575
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 78706810  866 GHCYHLLHVKFFHRYKLLNSLTWPHFHGGSQVEGIALIIrNLPLPSAEFTIGTKNVFVR 924
Cdd:cd00124  576 GYPVRLPFDEFLKRYRILAPGATEKASDSKKAAVLALLL-LLKLDSSGYQLGKTKVFLR 633
Myosin_head pfam00063
Myosin head (motor domain);
403-924 3.64e-137

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 434.40  E-value: 3.64e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810    403 LEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLKLyRN 482
Cdd:pfam00063  135 LEAFGNAKTVRNNNSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRL-TN 213
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810    483 VEKYELLRN----TTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVpitNIDGTEGCQVSNVYEVQ 558
Cdd:pfam00063  214 PKDYHYLSQsgcyTIDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFK---KERNDEQAVPDDTENLQ 290
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810    559 ETAQLLNMEAQILINCLTRaNSTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQREKN--LALL 636
Cdd:pfam00063  291 KAASLLGIDSTELEKALCK-RRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKAsfIGVL 369
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810    637 DFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPSYGILSLINE---- 712
Cdd:pfam00063  370 DIYGFEIFEKNSFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEeclf 449
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810    713 PHlNSNDALLLRVQQCCAGHPNFM--TTGSNSmCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLSLVQSLFP 790
Cdd:pfam00063  450 PK-ATDQTFLDKLYSTFSKHPHFQkpRLQGET-HFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFP 527
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810    791 EGN--------------PRRQVTKKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSL 856
Cdd:pfam00063  528 DYEtaesaaanesgkstPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGV 607
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78706810    857 MPLVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPHFHGGSQvEGIALIIRNLPLPSAEFTIGTKNVFVR 924
Cdd:pfam00063  608 LEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKGDAK-KGCEAILQSLNLDKEEYQFGKTKIFFR 674
COG5022 COG5022
Myosin heavy chain [General function prediction only];
403-1019 7.67e-116

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 395.60  E-value: 7.67e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLlKSLKLYRN 482
Cdd:COG5022  201 LEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEEL-KKLLLLQN 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  483 VEKYELLRNTTAMEE----DRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNidgtEGCQVSNVYEVQ 558
Cdd:COG5022  280 PKDYIYLSQGGCDKIdgidDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRN----GAAIFSDNSVLD 355
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  559 ETAQLLNMEAQILINCLTRANS-TNSaqEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQREKN-LALL 636
Cdd:COG5022  356 KACYLLGIDPSLFVKWLVKRQIkTGG--EWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNfIGVL 433
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  637 DFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPS-YGILSLINE--- 712
Cdd:COG5022  434 DIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKKNpLGILSLLDEecv 513
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  713 -PHLNSNDAL-----LLRVQQccagHPNFMTTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLSLVQ 786
Cdd:COG5022  514 mPHATDESFTsklaqRLNKNS----NPKFKKSRFRDNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVS 589
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  787 SLFP---EGNPRRqvtkKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLVHLC 863
Cdd:COG5022  590 TLFDdeeNIESKG----RFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRIS 665
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  864 RTGHCYHLLHVKFFHRYKLL---NSLTWPHFHGGSQVEGIALIIRNLPLPSAEFTIGTKNVFVRSPrTVYELEQFRRLRI 940
Cdd:COG5022  666 RAGFPSRWTFDEFVQRYRILspsKSWTGEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAG-VLAALEDMRDAKL 744
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  941 SELAVLIQTMFRMYHARKRFQRMRHSQMIISSAWRTWR-ECRFgipftgRRHLW-SLYRVAREEYRSLKYKRQVRWAIDI 1018
Cdd:COG5022  745 DNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRlRRLV------DYELKwRLFIKLQPLLSLLGSRKEYRSYLAC 818

                 .
gi 78706810 1019 I 1019
Cdd:COG5022  819 I 819
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
399-924 1.21e-100

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: 335.45  E-value: 1.21e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  399 ADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLK 478
Cdd:cd14883  114 ANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHSKELKEK 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  479 LY-RNVEKYELLRNTTAMEEDRMN----FHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVpitNIDGTEGCQVSN 553
Cdd:cd14883  194 LKlGEPEDYHYLNQSGCIRIDNINdkkdFDHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFE---DIDGETGALTVE 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  554 VYEVQET-AQLLNMEAQILINCLT------RANSTnsaqedvgcEMDAR--QAATNRNTLCRTLYSRLFTWLVNKINESL 624
Cdd:cd14883  271 DKEILKIvAKLLGVDPDKLKKALTirqinvRGNVT---------EIPLKvqEARDNRDAMAKALYSRTFAWLVNHINSCT 341
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  625 KSTQREKN-LALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPS 703
Cdd:cd14883  342 NPGQKNSRfIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKEGINWSHIVFTDNQECLDLIEKPP 421
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  704 YGILSLINE----PHlNSNDALLLRVQQCCAGHPNFMtTGSNSMC---FQIRHYASVVNYSIHRFLEKNSDMLPKYISAA 776
Cdd:cd14883  422 LGILKLLDEecrfPK-GTDLTYLEKLHAAHEKHPYYE-KPDRRRWkteFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDL 499
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  777 FYQSKLSLVQSLF---------------PEGNPRRQVTKKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQ 841
Cdd:cd14883  500 MSRSKNKFVKELFtypdllaltglsislGGDTTSRGTSKGKPTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNV 579
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  842 FDMALVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLnsLTWPHFHGGSQVEGIALII-RNLPLPSAEFTIGTKN 920
Cdd:cd14883  580 FDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCL--DPRARSADHKETCGAVRALmGLGGLPEDEWQVGKTK 657

                 ....
gi 78706810  921 VFVR 924
Cdd:cd14883  658 VFLR 661
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
399-924 1.75e-100

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: 334.44  E-value: 1.75e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  399 ADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLK 478
Cdd:cd14872  114 ANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWG 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  479 LyrnVEKYELLRNTTAME----EDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNIDGTEGCQVSNV 554
Cdd:cd14872  194 S---SAAYGYLSLSGCIEvegvDDVADFEEVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANR 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  555 YEVQETAQLLNMEAQILINCLTRANSTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQREKN-- 632
Cdd:cd14872  271 DVLKEVATLLGVDAATLEEALTSRLMEIKGCDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTtf 350
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  633 LALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPSYGILSLINE 712
Cdd:cd14872  351 IGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEALYQSEGVKFEHIDFIDNQPVLDLIEKKQPGLMLALDD 430
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  713 ----PhlNSNDA-LLLRVQQCCAGHPNFM--TTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLSLV 785
Cdd:cd14872  431 qvkiP--KGSDAtFMIAANQTHAAKSTFVyaEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLI 508
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  786 QSLFPEGNPrRQVTKKPsTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLVHLCRT 865
Cdd:cd14872  509 AVLFPPSEG-DQKTSKV-TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKT 586
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 78706810  866 GHCYHLLHVKFFHRYKLLNSlTWPHFHGGSQVEGIALIIRNLPLPSAEFTIGTKNVFVR 924
Cdd:cd14872  587 GYPFRYSHERFLKRYRFLVK-TIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
403-883 1.63e-99

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: 331.56  E-value: 1.63e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTR---ITDPiigERNFHIFYQLLLGADLQLLKSLKL 479
Cdd:cd01384  123 LEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRTYLLERSRvvqVSDP---ERNYHCFYQLCAGAPPEDREKYKL 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  480 yRNVEKYELLRNTTAMEEDRMN----FHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNIDGTEGCQVSNVY 555
Cdd:cd01384  200 -KDPKQFHYLNQSKCFELDGVDdaeeYRATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEF 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  556 EVQETAQLLNMEAQILINCLTRANSTNSAQEDVGCeMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQREKNL-A 634
Cdd:cd01384  279 HLKAAAELLMCDEKALEDALCKRVIVTPDGIITKP-LDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLiG 357
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  635 LLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPSYGILSLINE-- 712
Cdd:cd01384  358 VLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEFVDNQDVLDLIEKKPGGIIALLDEac 437
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  713 --PHlNSNDALLLRVQQCCAGHPNFMTTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLSLVQSLFP 790
Cdd:cd01384  438 mfPR-STHETFAQKLYQTLKDHKRFSKPKLSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFP 516
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  791 EGNPRRqvTKKPSTLSS---NIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLVHLCRTGH 867
Cdd:cd01384  517 PLPREG--TSSSSKFSSigsRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGY 594
                        490
                 ....*....|....*.
gi 78706810  868 CYHLLHVKFFHRYKLL 883
Cdd:cd01384  595 PTRKPFEEFLDRFGLL 610
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
403-924 1.61e-97

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: 326.73  E-value: 1.61e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLKLYRN 482
Cdd:cd01377  128 LEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGD 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  483 VEKYELLRN---TTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVP-----ITNIDGTEgcqvsnv 554
Cdd:cd01377  208 PSYYFFLSQgelTIDGVDDAEEFKLTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQrrreeQAELDGTE------- 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  555 yEVQETAQLLNMEAQILINCLTRANSTnsaqedVGCEM-----DARQAATNRNTLCRTLYSRLFTWLVNKINESL-KSTQ 628
Cdd:cd01377  281 -EADKAAHLLGVNSSDLLKALLKPRIK------VGREWvtkgqNKEQVVFSVGALAKALYERLFLWLVKRINKTLdTKSK 353
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  629 REKNLALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFH--VLrsEQELYIREGLEWSRIDY-FDNESICELIDKPSYG 705
Cdd:cd01377  354 RQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHmfVL--EQEEYKKEGIEWTFIDFgLDLQPTIDLIEKPNMG 431
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  706 ILSLINE----PhlNSNDALLLR--VQQCCAGHPNFM--TTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAF 777
Cdd:cd01377  432 ILSILDEecvfP--KATDKTFVEklYSNHLGKSKNFKkpKPKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALL 509
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  778 YQSKLSLVQSLFPE-----GNPRRQVTKKPS--TLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQ 850
Cdd:cd01377  510 KKSSDPLVASLFKDyeesgGGGGKKKKKGGSfrTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQ 589
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78706810  851 VRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNsltwPHFHGGSQVEGIA---LIIRNLPLPSAEFTIGTKNVFVR 924
Cdd:cd01377  590 LRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILA----PNAIPKGFDDGKAaceKILKALQLDPELYRIGNTKVFFK 662
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
403-924 1.53e-96

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: 323.44  E-value: 1.53e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLKLyRN 482
Cdd:cd01381  118 LEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLEL-GD 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  483 VEKYELL--RNTTAME--EDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITnIDGTEGCQVSNVYEVQ 558
Cdd:cd01381  197 ASDYYYLtqGNCLTCEgrDDAAEFADIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEATV-VDNLDASEVRDPPNLE 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  559 ETAQLLNMEAQILINCLTRaNSTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINES----LKSTQREKNLA 634
Cdd:cd01381  276 RAAKLLEVPKQDLVDALTT-RTIFTRGETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAiykpRGTDSSRTSIG 354
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  635 LLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPSYGILSLINE-- 712
Cdd:cd01381  355 VLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEYDKEGINWQHIEFVDNQDVLDLIALKPMNIMSLIDEes 434
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  713 --PHlNSNDALLLRVQQCCAGHPNFMTTGSNS-MCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLSLVQSLF 789
Cdd:cd01381  435 kfPK-GTDQTMLEKLHSTHGNNKNYLKPKSDLnTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLF 513
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  790 PEGNPRRQVT-KKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLVHLCRTGHC 868
Cdd:cd01381  514 NEDISMGSETrKKSPTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYP 593
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 78706810  869 YHLLHVKFFHRYKLLNSLTWPHfHGGSQVEGIALIIRNLPLPSAEFTIGTKNVFVR 924
Cdd:cd01381  594 IRHTFEEFVERYRVLVPGIPPA-HKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
403-883 8.82e-95

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: 318.49  E-value: 8.82e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLKLyRN 482
Cdd:cd01383  116 LEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNL-KS 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  483 VEKYELLRNTTAME----EDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFvpiTNIDGTEGCQVSNVYEVQ 558
Cdd:cd01383  195 ASEYKYLNQSNCLTidgvDDAKKFHELKEALDTVGISKEDQEHIFQMLAAVLWLGNISF---QVIDNENHVEVVADEAVS 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  559 ETAQLLNMEAQILIncltRANSTNSAQ---EDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQRE--KNL 633
Cdd:cd01383  272 TAASLLGCNANDLM----LALSTRKIQaggDKIVKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRtgRSI 347
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  634 ALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPSYGILSLINEP 713
Cdd:cd01383  348 SILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDGIDWTKVDFEDNQECLDLIEKKPLGLISLLDEE 427
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  714 ---HLNSNDALLLRVQQCCAGHPNFmtTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLSLVQsLFP 790
Cdd:cd01383  428 snfPKATDLTFANKLKQHLKSNSCF--KGERGGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQ-LFA 504
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  791 EG-----------NPRRQVTKKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPL 859
Cdd:cd01383  505 SKmldasrkalplTKASGSDSQKQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEV 584
                        490       500
                 ....*....|....*....|....
gi 78706810  860 VHLCRTGHCYHLLHVKFFHRYKLL 883
Cdd:cd01383  585 VRISRSGYPTRMTHQEFARRYGFL 608
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
385-924 3.58e-94

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: 317.49  E-value: 3.58e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  385 HKSPTQRMRECVTCADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQ 464
Cdd:cd14890  124 IEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQ 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  465 LLLGADLQLLKSLKLYRNVEKYELLRNTTAM--EEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITN 542
Cdd:cd14890  204 LLAGADEALRERLKLQTPVEYFYLRGECSSIpsCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESEND 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  543 IDGTEGcqVSNVYEVQETAQLLNMEAQILINC-LTRANSTNSA----QEDVGcemdarQAATNRNTLCRTLYSRLFTWLV 617
Cdd:cd14890  284 TTVLED--ATTLQSLKLAAELLGVNEDALEKAlLTRQLFVGGKtivqPQNVE------QARDKRDALAKALYSSLFLWLV 355
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  618 NKINESLKSTQREKN-LALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESIC 696
Cdd:cd14890  356 SELNRTISSPDDKWGfIGVLDIYGFEKFEWNTFEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACL 435
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  697 ELID-KPS--YGILSLINE--------------PHLNSN---DALLLRVQQCCAGHPNFMTTG-SNSMCFQIRHYASVVN 755
Cdd:cd14890  436 ELIEgKVNgkPGIFITLDDcwrfkgeeankkfvSQLHASfgrKSGSGGTRRGSSQHPHFVHPKfDADKQFGIKHYAGDVI 515
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  756 YSIHRFLEKNSDMLPKYISAAFYQSKLSLvqslfpegnprRQVtkkpsTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNE 835
Cdd:cd14890  516 YDASGFNEKNNETLNAEMKELIKQSRRSI-----------REV-----SVGAQFRTQLQELMAKISLTNPRYVRCIKPNE 579
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  836 GKQPHQFDMALVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNsltwPHFHGGSQVegIALIIRNLPLPSAEFT 915
Cdd:cd14890  580 TKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLL----PTAENIEQL--VAVLSKMLGLGKADWQ 653

                 ....*....
gi 78706810  916 IGTKNVFVR 924
Cdd:cd14890  654 IGSSKIFLK 662
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
391-924 8.72e-91

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: 307.84  E-value: 8.72e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  391 RMRECVTCADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGAD 470
Cdd:cd14892  126 SIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLD 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  471 LQLLKSLKLyRNVEKYELLRNTTAMEEDRMN----FHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNiDGT 546
Cdd:cd14892  206 ANENAALEL-TPAESFLFLNQGNCVEVDGVDdateFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENAD-DED 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  547 EGCQVSNVYEVQETAQLLNMEAQILINCL-TRANST---NSAQEDVGCemdaRQAATNRNTLCRTLYSRLFTWLVNKINE 622
Cdd:cd14892  284 VFAQSADGVNVAKAAGLLGVDAAELMFKLvTQTTSTargSVLEIKLTA----REAKNALDALCKYLYGELFDWLISRINA 359
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  623 SLK-----------STQREKNLALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFD 691
Cdd:cd14892  360 CHKqqtsgvtggaaSPTFSPFIGILDIFGFEIMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQD 439
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  692 NESICELIDKPSYGILSLINEPHL---NSNDALLLRV--QQCCAGHPNFMTTGSNSMCFQIRHYASVVNYSIHRFLEKNS 766
Cdd:cd14892  440 NQDCLDLIQKKPLGLLPLLEEQMLlkrKTTDKQLLTIyhQTHLDKHPHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNN 519
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  767 DMLpkyisaafYQSKLSLVQSlfpegnprrqvtkkpstlSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMAL 846
Cdd:cd14892  520 DNL--------HDDLRDLLRS------------------SSKFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCEL 573
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  847 VQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLL------NSLTWPHFHGGSQVEGIALIIRNLPLPSAeFTIGTKN 920
Cdd:cd14892  574 VRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLarnkagVAASPDACDATTARKKCEEIVARALEREN-FQLGRTK 652

                 ....
gi 78706810  921 VFVR 924
Cdd:cd14892  653 VFLR 656
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
386-924 8.75e-90

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: 305.14  E-value: 8.75e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  386 KSPTQRMRECVTCADVFLEAMGNACTLKNNNSSRYGKLfdIEIDFK-GDPMGVHITHYMLEKTRITDPIIGERNFHIFYQ 464
Cdd:cd01387  102 QRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKY--LEVFFEgGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYE 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  465 LLLGADLQLLKSLKLyRNVEKYELLRN----TTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPI 540
Cdd:cd01387  180 LLAGLPAQLRQKYGL-QEAEKYFYLNQggncEIAGKSDADDFRRLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKR 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  541 TNIDGTEGCQVSNVYEVQETAQLLNMEAQILINCLTrANSTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKI 620
Cdd:cd01387  259 QLRHGQEGVSVGSDAEIQWVAHLLQISPEGLQKALT-FKVTETRRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRV 337
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  621 NESLKS-TQREKNLALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELI 699
Cdd:cd01387  338 NAIVYSgTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYIREQIDWTEIAFADNQPVINLI 417
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  700 DKPSYGILSLI----NEPHLNSNDALllrvQQCCAGH---PNFMTTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKY 772
Cdd:cd01387  418 SKKPVGILHILddecNFPQATDHSFL----EKCHYHHalnELYSKPRMPLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQD 493
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  773 ISAAFYQSKLSLVQSLF-----------PEGNPRRQVTKKPS--TLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQP 839
Cdd:cd01387  494 VLELLVSSRTRVVAHLFsshraqtdkapPRLGKGRFVTMKPRtpTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEP 573
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  840 HQFDMALVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPHfhgGSQVEGIALIIRNLP--LPSAEFTIG 917
Cdd:cd01387  574 MLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPR---PAPGDMCVSLLSRLCtvTPKDMYRLG 650

                 ....*..
gi 78706810  918 TKNVFVR 924
Cdd:cd01387  651 ATKVFLR 657
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
403-884 1.51e-89

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: 304.65  E-value: 1.51e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLFDIEIDFK-GDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLKLYR 481
Cdd:cd14907  147 LEAFGNAKTVRNDNSSRFGKYVSILVDKKkRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKN 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  482 NV--EKYELLRNTTAMEEDRMN----FHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITnIDGTEGCQVSNVY 555
Cdd:cd14907  227 QLsgDRYDYLKKSNCYEVDTINdeklFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDST-LDDNSPCCVKNKE 305
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  556 EVQETAQLLNMEAQILINCLT-RANSTNSAQEDvgCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESL---------K 625
Cdd:cd14907  306 TLQIIAKLLGIDEEELKEALTtKIRKVGNQVIT--SPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqqL 383
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  626 STQREKNLALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLE--WSRIDYFDNESICELIDKPS 703
Cdd:cd14907  384 FQNKYLSIGLLDIFGFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSYTDNQDVIDLLDKPP 463
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  704 YGILSLINEPHL--NSNDALLLrvQQCCAGHPNF----MTTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAF 777
Cdd:cd14907  464 IGIFNLLDDSCKlaTGTDEKLL--NKIKKQHKNNskliFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCI 541
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  778 YQSKLSLVQSLF--------PEGNPRRQVTKKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQH 849
Cdd:cd14907  542 QNSKNRIISSIFsgedgsqqQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLN 621
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 78706810  850 QVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLN 884
Cdd:cd14907  622 QIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLK 656
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
403-883 2.44e-89

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: 303.92  E-value: 2.44e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLfdIEIDF-----------KGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADL 471
Cdd:cd14888  122 LEAFGNARTLRNDNSSRFGKF--IELQFsklkskrmsgdRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAARE 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  472 QLLKSLKLYRNVEKYELLRNTTAME------EDRMNFHY-TKRS-------------------LDVLGLSCEESNSIFRV 525
Cdd:cd14888  200 AKNTGLSYEENDEKLAKGADAKPISidmssfEPHLKFRYlTKSSchelpdvddleefestlyaMQTVGISPEEQNQIFSI 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  526 IAVVLKLGNFIFVpiTNIDGTEGCQVSNVYE--VQETAQLLNMEAQILINCLTrANSTNSAQEDVGCEMDARQAATNRNT 603
Cdd:cd14888  280 VAAILYLGNILFE--NNEACSEGAVVSASCTddLEKVASLLGVDAEDLLNALC-YRTIKTAHEFYTKPLRVDEAEDVRDA 356
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  604 LCRTLYSRLFTWLVNKINESLKSTQREKNL--ALLDFYGFEALDHNSFEQFAINYSAEKIHQ---NFVFhvlRSEQELYI 678
Cdd:cd14888  357 LARALYSCLFDKVVERTNESIGYSKDNSLLfcGVLDIFGFECFQLNSFEQLCINFTNERLQQffnNFVF---KCEEKLYI 433
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  679 REGLEWSRIDYFDNESICELIDKPSYGILSLINE----PHlNSNDALLLRVQQCCAGHPNFMTTGSNSMCFQIRHYASVV 754
Cdd:cd14888  434 EEGISWNPLDFPDNQDCVDLLQEKPLGIFCMLDEecfvPG-GKDQGLCNKLCQKHKGHKRFDVVKTDPNSFVIVHFAGPV 512
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  755 NYSIHRFLEKNSDMLPKYISAAFYQSKLSLVQSLFP----EGNPRRQVTKKPSTLSSNIRTQLQTLLAIVKHRRSHYVFC 830
Cdd:cd14888  513 KYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSaylrRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRC 592
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 78706810  831 IKPNEGKQPHQFDMALVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLL 883
Cdd:cd14888  593 IKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRIL 645
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
389-860 4.34e-89

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: 302.63  E-value: 4.34e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  389 TQRMREcvtcADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLG 468
Cdd:cd01382  110 EQRILE----ANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAG 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  469 AdlqllkSLKLYRnvekyELLRNTtaMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNiDGTEG 548
Cdd:cd01382  186 A------PEDLRE-----KLLKDP--LLDDVGDFIRMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGS-DSGGG 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  549 CQVSNVYE--VQETAQLLNMEAQILINCLTRANSTNSAQEDVGCEM----DARQAATNRNTLCRTLYSRLFTWLVNKINE 622
Cdd:cd01382  252 CNVKPKSEqsLEYAAELLGLDQDELRVSLTTRVMQTTRGGAKGTVIkvplKVEEANNARDALAKAIYSKLFDHIVNRINQ 331
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  623 SLKSTQREKNLALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKP 702
Cdd:cd01382  332 CIPFETSSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEYVDNQDCIDLIEAK 411
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  703 SYGILSLINEPHL---NSNDALLLRVQQCCAGHPNFMTTGSNSM----------CFQIRHYASVVNYSIHRFLEKNSDML 769
Cdd:cd01382  412 LVGILDLLDEESKlpkPSDQHFTSAVHQKHKNHFRLSIPRKSKLkihrnlrddeGFLIRHFAGAVCYETAQFIEKNNDAL 491
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  770 PKYISAAFYQSKLSLVQSLFPEGNPRRQVTKKPS------TLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFD 843
Cdd:cd01382  492 HASLESLICESKDKFIRSLFESSTNNNKDSKQKAgklsfiSVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFE 571
                        490
                 ....*....|....*..
gi 78706810  844 MALVQHQVRYmSLMPLV 860
Cdd:cd01382  572 GAQILSQLQC-SGMVSV 587
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
403-924 8.53e-88

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: 298.68  E-value: 8.53e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLfdIEIDF--KGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLKLy 480
Cdd:cd01380  122 MEAFGNAKTTRNDNSSRFGKY--IEILFdkNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHL- 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  481 RNVEKYELLRNTTAMEEDRMN----FHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPitniDGTEGCQVSNVYE 556
Cdd:cd01380  199 GSAEDFFYTNQGGSPVIDGVDdaaeFEETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKA----TRNDSASISPDDE 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  557 -VQETAQLLNMEAQILINCLTRaNSTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQREKN--- 632
Cdd:cd01380  275 hLQIACELLGIDESQLAKWLCK-RKIVTRSEVIVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhsf 353
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  633 LALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPSyGILSLINE 712
Cdd:cd01380  354 IGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVKEEIEWSFIDFYDNQPCIDLIEGKL-GILDLLDE 432
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  713 ----PHlNSNDALLLRVQQCCAGHPN------FMTTGSnsmcFQIRHYASVVNYSIHRFLEKNSDMLPkyisaafyQSKL 782
Cdd:cd01380  433 ecrlPK-GSDENWAQKLYNQHLKKPNkhfkkpRFSNTA----FIVKHFADDVEYQVEGFLEKNRDTVS--------EEHL 499
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  783 SLVQSlfpegnprRQVTKKpsTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLVHL 862
Cdd:cd01380  500 NVLKA--------SKNRKK--TVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRI 569
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78706810  863 CRTGHCYHLLHVKFFHRYKLLnsLTWPHFHGGSQVEGIALIIRNLPLPSAEFTIGTKNVFVR 924
Cdd:cd01380  570 SAAGFPSRWTYEEFFSRYRVL--LPSKEWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
403-883 1.15e-84

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: 290.05  E-value: 1.15e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYqlllGADLQLLKSLKLYRN 482
Cdd:cd14897  120 LEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFY----ALFAGMSRDRLLYYF 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  483 VEK---YELLRN----------TTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNidgTEGC 549
Cdd:cd14897  196 LEDpdcHRILRDdnrnrpvfndSEELEYYRQMFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDED---TDGV 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  550 QVSNVYEVQETAQLLNMEAQILINCLTrANSTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQR 629
Cdd:cd14897  273 TVADEYPLHAVAKLLGIDEVELTEALI-SNVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKD 351
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  630 EKN------LALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPS 703
Cdd:cd14897  352 FQImtrgpsIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYHDNDDVLELFFKKP 431
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  704 YGILSLINE-PHL-NSNDA-LLLRVQQCCAGHPNFMTTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQS 780
Cdd:cd14897  432 LGILPLLDEeSTFpQSTDSsLVQKLNKYCGESPRYVASPGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNS 511
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  781 KLSLVQSLFpegnprrqvtkkpstlSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLV 860
Cdd:cd14897  512 NNEFISDLF----------------TSYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIA 575
                        490       500
                 ....*....|....*....|...
gi 78706810  861 HLCRTGHCYHLLHVKFFHRYKLL 883
Cdd:cd14897  576 KIRRDGYPIRIKYEDFVKRYKEI 598
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
402-883 4.06e-84

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: 289.15  E-value: 4.06e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  402 FLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLKLYR 481
Cdd:cd14904  119 LLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDP 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  482 NVEkYELLRNTTAME-----EDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPitniDGTEGCQVSNVYE 556
Cdd:cd14904  199 NCQ-YQYLGDSLAQMqipglDDAKLFASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDK----SDENGSRISNGSQ 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  557 VQETAQLLNMEAQILINCL-TRanSTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKS--TQREKNL 633
Cdd:cd14904  274 LSQVAKMLGLPTTRIEEALcNR--SVVTRNESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTddDRIKGQI 351
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  634 ALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKpSYGILSLINEp 713
Cdd:cd14904  352 GVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEEYIREGLQWDHIEYQDNQGIVEVIDG-KMGIIALMND- 429
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  714 HL----NSNDALLLRVQ---QCCAGHPNFMTTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLSLVQ 786
Cdd:cd14904  430 HLrqprGTEEALVNKIRtnhQTKKDNESIDFPKVKRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLT 509
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  787 SLF--------PEGNPRRQVTKKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMP 858
Cdd:cd14904  510 ELFgsseapseTKEGKSGKGTKAPKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIE 589
                        490       500
                 ....*....|....*....|....*
gi 78706810  859 LVHLCRTGHCYHLLHVKFFHRYKLL 883
Cdd:cd14904  590 AIRITRSGYPSRLTPKELATRYAIM 614
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
382-883 2.83e-83

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: 286.68  E-value: 2.83e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  382 HRRHKSPTQRMRECVTCADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHI 461
Cdd:cd14901  116 HGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHI 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  462 FYQLLLGADLQLLKSLKLYrNVEKYELLRNTTAME-----EDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFI 536
Cdd:cd14901  196 FYELLRGASSDELHALGLT-HVEEYKYLNSSQCYDrrdgvDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLC 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  537 FVPITNIDGTegCQVSNVYEVQETAQLLNMEAQILINCLT----RANStnsaqEDVGCEMDARQAATNRNTLCRTLYSRL 612
Cdd:cd14901  275 FVKKDGEGGT--FSMSSLANVRAACDLLGLDMDVLEKTLCtreiRAGG-----EYITMPLSVEQALLTRDVVAKTLYAQL 347
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  613 FTWLVNKINESLK---STQREKNLALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDY 689
Cdd:cd14901  348 FDWLVDRINESIAyseSTGASRFIGIVDIFGFEIFATNSLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY 427
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  690 FDNESICELIDKPSYGILSLINEPHL--NSNDA-LLLRVQQCCAGHPNFMTT----GSNsmCFQIRHYASVVNYSIHRFL 762
Cdd:cd14901  428 PNNDACVAMFEARPTGLFSLLDEQCLlpRGNDEkLANKYYDLLAKHASFSVSklqqGKR--QFVIHHYAGAVCYATDGFC 505
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  763 EKNSDMLPKYISAAFYQSKLSLVqslfpegnprrqvtkkPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQF 842
Cdd:cd14901  506 DKNKDHVHSEALALLRTSSNAFL----------------SSTVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEF 569
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 78706810  843 DMALVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLL 883
Cdd:cd14901  570 DAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCL 610
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
386-886 5.34e-80

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: 277.06  E-value: 5.34e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  386 KSPTQRMRECVTCADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQL 465
Cdd:cd14873  111 KEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYAL 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  466 LLGADLQLLKSLKLyRNVEKYELLRNTTAMEEDRMN----FHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPit 541
Cdd:cd14873  191 LAGLEHEEREEFYL-STPENYHYLNQSGCVEDKTISdqesFREVITAMEVMQFSKEEVREVSRLLAGILHLGNIEFIT-- 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  542 nidgTEGCQVSNVYEVQETAQLLNMEAQILINCLTRaNSTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKIN 621
Cdd:cd14873  268 ----AGGAQVSFKTALGRSAELLGLDPTQLTDALTQ-RSMFLRGEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKIN 342
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  622 ESLKSTQREKNLALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDK 701
Cdd:cd14873  343 SRIKGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDWIDNGECLDLIEK 422
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  702 pSYGILSLINE----PHlNSNDALLLRVQQCCAGHPNFMTTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAF 777
Cdd:cd14873  423 -KLGLLALINEeshfPQ-ATDSTLLEKLHSQHANNHFYVKPRVAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLL 500
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  778 YQSKLSLVQSLFPEGNPR-RQVT-------KKPsTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQH 849
Cdd:cd14873  501 RESRFDFIYDLFEHVSSRnNQDTlkcgskhRRP-TVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLN 579
                        490       500       510
                 ....*....|....*....|....*....|....*..
gi 78706810  850 QVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNSL 886
Cdd:cd14873  580 QLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRN 616
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
386-883 6.83e-79

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: 273.38  E-value: 6.83e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  386 KSPTQRMRECVTCADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYql 465
Cdd:cd01379  102 KANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFY-- 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  466 LLGADLQLLKSLKLYR--NVEKYELLRNTTAMEEDRMN-------FHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFI 536
Cdd:cd01379  180 YIYAGLAEDKKLAKYKlpENKPPRYLQNDGLTVQDIVNnsgnrekFEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIE 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  537 FVPI-TNIDGTEGCQVSNVYEVQETAQLLNMEAQILINCLTRaNSTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTW 615
Cdd:cd01379  260 FTEVeSNHQTDKSSRISNPEALNNVAKLLGIEADELQEALTS-HSVVTRGETIIRNNTVEEATDARDAMAKALYGRLFSW 338
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  616 LVNKINESLK----STQREKNLALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFD 691
Cdd:cd01379  339 IVNRINSLLKpdrsASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYED 418
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  692 NESICE-LIDKPsYGILSLINE----PhlNSNDALLLRVQQCCAGHPNFMTTGSNSMCFQIRHYASVVNYSIHRFLEKNS 766
Cdd:cd01379  419 NRPLLDmFLQKP-MGLLALLDEesrfP--KATDQTLVEKFHNNIKSKYYWRPKSNALSFGIHHYAGKVLYDASGFLEKNR 495
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  767 DMLPKYISAAFYQSKLSLVQslfpegnprrqvtkkpSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMAL 846
Cdd:cd01379  496 DTLPPDVVQLLRSSENPLVR----------------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREK 559
                        490       500       510
                 ....*....|....*....|....*....|....*..
gi 78706810  847 VQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLL 883
Cdd:cd01379  560 VLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFL 596
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
403-901 1.58e-78

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: 273.26  E-value: 1.58e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLKLYRN 482
Cdd:cd14880  131 MEAFGNACTLRNNNSSRFGKFIQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEG 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  483 VEKYELLRNTTAMEEDrmNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVpiTNIDGTEGCQVSNVYE--VQET 560
Cdd:cd14880  211 AAFSWLPNPERNLEED--CFEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFA--DSEDEAQPCQPMDDTKesVRTS 286
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  561 AQLLNMEAQILINCLTRANSTNSAQEDVGCEMDAR-QAATNRNTLCRTLYSRLFTWLVNKINESLKSTQREKN--LALLD 637
Cdd:cd14880  287 ALLLKLPEDHLLETLQIRTIRAGKQQQVFKKPCSRaECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTtfIGLLD 366
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  638 FYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPSYGILSLINEP-HLN 716
Cdd:cd14880  367 VYGFESFPENSLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSPISICSLINEEcRLN 446
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  717 --SNDALL-LRVQQCCAGHPNFmttGSNSMC----FQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLSLVQSLF 789
Cdd:cd14880  447 rpSSAAQLqTRIESALAGNPCL---GHNKLSrepsFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLF 523
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  790 PEgNPRRQVTKKPSTLS--------SNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLVH 861
Cdd:cd14880  524 PA-NPEEKTQEEPSGQSrapvltvvSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIH 602
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 78706810  862 LCRTGHCYHLLHVKFFHRYKLLNSL---TWPHFHGGSQVEGIA 901
Cdd:cd14880  603 ISAAGFPIRVSHQNFVERYKLLRRLrphTSSGPHSPYPAKGLS 645
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
399-890 1.30e-74

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: 261.01  E-value: 1.30e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  399 ADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYqlllgadlqllkslk 478
Cdd:cd14900  141 TNILLESFGNARTLRNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFY--------------- 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  479 lyrnvekyELLRNTTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFV--PITNIDGTEGCQV--SNV 554
Cdd:cd14900  206 --------EMAIGASEAARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEhdENSDRLGQLKSDLapSSI 277
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  555 YEVQETAQLLNMEAQILINCLTrANSTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQREKN-- 632
Cdd:cd14900  278 WSRDAAATLLSVDATKLEKALS-VRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKShg 356
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  633 ----LALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPSYGILS 708
Cdd:cd14900  357 glhfIGILDIFGFEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRPTGILS 436
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  709 LINEPHL--NSNDALLL-RVQQCCAGHPNFMTTGSNSM--CFQIRHYASVVNYSIHRFLEKNSDMLpkyisaafYQSKLS 783
Cdd:cd14900  437 LIDEECVmpKGSDTTLAsKLYRACGSHPRFSASRIQRArgLFTIVHYAGHVEYSTDGFLEKNKDVL--------HQEAVD 508
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  784 LVQSlfpegnprrqvtkkpstlSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLVHLC 863
Cdd:cd14900  509 LFVY------------------GLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVA 570
                        490       500
                 ....*....|....*....|....*..
gi 78706810  864 RTGHCYHLLHVKFFHRYKLLNSLTWPH 890
Cdd:cd14900  571 RAGFPIRLLHDEFVARYFSLARAKNRL 597
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
393-924 2.73e-74

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: 260.48  E-value: 2.73e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  393 RECVTCaDVF--LEAMGNACTLKNNNSSRYGKLFDIEIDfKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGAD 470
Cdd:cd14896  108 RLRQPE-DVLpiLESFGHAKTILNANASRFGQVLRLHLQ-HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLD 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  471 LQLLKSLKLyRNVEKYELLRNTTAME----EDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNiDGT 546
Cdd:cd14896  186 PEEREQLSL-QGPETYYYLNQGGACRlqgkEDAQDFEGLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSER-ESQ 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  547 EGCQVSNVYEVQETAQLLNMEAQILINCLTRaNSTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKS 626
Cdd:cd14896  264 EVAAVSSWAEIHTAARLLQVPPERLEGAVTH-RVTETPYGRVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAP 342
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  627 TQREKN---LALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPS 703
Cdd:cd14896  343 PGEAESdatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEEECQRELLPWVPIPQPPRESCLDLLVDQP 422
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  704 YGILSLINEPHLNSNDALLLRVQQCC---AGHPNFMTTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQS 780
Cdd:cd14896  423 HSLLSILDDQTWLSQATDHTFLQKCHyhhGDHPSYAKPQLPLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQS 502
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  781 KLSLVQSLFPEGNPRRQVTKKPSTLSSNIRTQLQTLLAivKHRRSHYVF--CIKPNEGKQPHQFDMALVQHQVRYMSLMP 858
Cdd:cd14896  503 QLQLVGSLFQEAEPQYGLGQGKPTLASRFQQSLGDLTA--RLGRSHVYFihCLNPNPGKLPGLFDVGHVTEQLRQAGILE 580
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78706810  859 LVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPHFhggSQVEGIALIIRN-LPLPSAEFTIGTKNVFVR 924
Cdd:cd14896  581 AIGTRSEGFPVRVPFQAFLARFGALGSERQEAL---SDRERCGAILSQvLGAESPLYHLGATKVLLK 644
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
403-924 7.93e-74

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: 260.39  E-value: 7.93e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLfdIEIDFKGDPM--GVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLKL- 479
Cdd:cd01385  120 LEAFGNAKTAHNNNSSRFGKF--IQVNYRENGMvrGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLk 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  480 ------YRNVEKYELLRNttamEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNiDGTEGCQVSN 553
Cdd:cd01385  198 qpedyhYLNQSDCYTLEG----EDEKYEFERLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAY-HRDESVTVGN 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  554 VYEVQETAQLLNMEAQILINCLTRANSTNSAqEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESL---KSTQRE 630
Cdd:cd01385  273 PEVLDIISELLRVKEETLLEALTTKKTVTVG-ETLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkKDLEEA 351
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  631 KNLAL--LDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPSYGILS 708
Cdd:cd01385  352 KGLSIgvLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYKKEGISWHNIEYTDNTGCLQLISKKPTGLLC 431
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  709 LINE----PHlNSNDALLLRVQQCCAGHPNFMTTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLSL 784
Cdd:cd01385  432 LLDEesnfPG-ATNQTLLAKFKQQHKDNKYYEKPQVMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAF 510
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  785 VQSL-----------------------FPEGNPRRQ----------------------VTKKPSTLSSNIRTQLQTLLAI 819
Cdd:cd01385  511 VRELigidpvavfrwavlrafframaaFREAGRRRAqrtaghsltlhdrttksllhlhKKKKPPSVSAQFQTSLSKLMET 590
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  820 VKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLL--NSLtwphfhgGSQV 897
Cdd:cd01385  591 LGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLlpKGL-------ISSK 663
                        570       580
                 ....*....|....*....|....*..
gi 78706810  898 EGIALIIRNLPLPSAEFTIGTKNVFVR 924
Cdd:cd01385  664 EDIKDFLEKLNLDRDNYQIGKTKVFLK 690
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
403-886 2.28e-73

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: 259.07  E-value: 2.28e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLkslklyrn 482
Cdd:cd14908  140 LEAFGNARTLRNDNSSRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEH-------- 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  483 vEKYELLRNTTAME--------------------EDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITN 542
Cdd:cd14908  212 -EKYEFHDGITGGLqlpnefhytgqggapdlrefTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE 290
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  543 IDGTEGCQVSNVYEVQETAQLLNMEAQILINCLTrANSTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINE 622
Cdd:cd14908  291 DGAAEIAEEGNEKCLARVAKLLGVDVDKLLRALT-SKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNS 369
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  623 SLKSTQREK---NLALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELI 699
Cdd:cd14908  370 SINWENDKDirsSVGVLDIFGFECFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTI 449
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  700 DKPSYGILSLINE----PHLNS--------NDALLLRVQQCCAGHPNFMTTGS--NSMCFQIRHYASVVNYSIHR-FLEK 764
Cdd:cd14908  450 QAKKKGILTMLDDecrlGIRGSdanyasrlYETYLPEKNQTHSENTRFEATSIqkTKLIFAVRHFAGQVQYTVETtFCEK 529
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  765 NSDMLPKYisaafyqsklslVQSLFPEGnprrqvtkkpstlsSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDM 844
Cdd:cd14908  530 NKDEIPLT------------ADSLFESG--------------QQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTR 583
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 78706810  845 ALVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNSL 886
Cdd:cd14908  584 KRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLPL 625
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
399-883 4.38e-73

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: 258.73  E-value: 4.38e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  399 ADVFLEAMGNACTLKNNNSSRYGKLFDI-----EIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQL 473
Cdd:cd14895  131 ANPILESFGNARTLRNDNSSRFGKFVRMffeghELDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDM 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  474 LKSLKLY--RNVEKYEL------LRNTTAMEEDRmnFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVP------ 539
Cdd:cd14895  211 KLELQLEllSAQEFQYIsggqcyQRNDGVRDDKQ--FQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVAssedeg 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  540 -ITNIDGTEGCQVSNVYEVQETAQ--------LLNMEAQILINCLTRaNSTNSAQEDVGCEMDARQAATNRNTLCRTLYS 610
Cdd:cd14895  289 eEDNGAASAPCRLASASPSSLTVQqhldivskLFAVDQDELVSALTT-RKISVGGETFHANLSLAQCGDARDAMARSLYA 367
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  611 RLFTWLVNKINESLKSTQREKN------------LALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYI 678
Cdd:cd14895  368 FLFQFLVSKVNSASPQRQFALNpnkaankdttpcIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHI 447
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  679 REGLEWSRIDYFDNESICELIDKPSYGILSLINEPHL--NSNDALLLR-VQQCCAGHPNFMTTGSNS--MCFQIRHYASV 753
Cdd:cd14895  448 EEGIKWNAVDYEDNSVCLEMLEQRPSGIFSLLDEECVvpKGSDAGFARkLYQRLQEHSNFSASRTDQadVAFQIHHYAGA 527
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  754 VNYSIHRFLEKNSDMLPKYISAAFYQSKLSLVQSLF-----------PEGNP---RRQVTKKPSTLSSNIRTQLQTLLAI 819
Cdd:cd14895  528 VRYQAEGFCEKNKDQPNAELFSVLGKTSDAHLRELFeffkasesaelSLGQPklrRRSSVLSSVGIGSQFKQQLASLLDV 607
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78706810  820 VKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLL 883
Cdd:cd14895  608 VQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLL 671
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
402-883 6.93e-73

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: 257.14  E-value: 6.93e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  402 FLEAMGNACTLKNNNSSRYGKLfdIEIDFK-GDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLKLY 480
Cdd:cd14889  121 LLEAFGNAQTVMNDNSSRFGKY--IQLRFRnGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLL 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  481 rNVEKYELLRNTTAMEED----RMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPitniDGTEGCQVSNVYE 556
Cdd:cd14889  199 -DPGKYRYLNNGAGCKREvqywKKKYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITFEM----DDDEALKVENDSN 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  557 --VQETAQLLNMEAQILINCLTRANSTNSAqEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESL----KSTQRE 630
Cdd:cd14889  274 gwLKAAAGQFGVSEEDLLKTLTCTVTFTRG-EQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLapkdDSSVEL 352
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  631 KNLALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPSYGILSLI 710
Cdd:cd14889  353 REIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLL 432
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  711 NE----PHlNSNDALLLRVQQCCAGHPNFMTTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLSLVQ 786
Cdd:cd14889  433 DEqshfPQ-ATDESFVDKLNIHFKGNSYYGKSRSKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLS 511
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  787 SLF-------PEGNPRRqvtKKPSTLSSNI-RTQLQTLLAIVKHRRS-----------HYVFCIKPNEGKQPHQFDMALV 847
Cdd:cd14889  512 VLFtatrsrtGTLMPRA---KLPQAGSDNFnSTRKQSVGAQFKHSLGvlmekmfaaspHFVRCIKPNHVKVPGQLDSKYI 588
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 78706810  848 QHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLL 883
Cdd:cd14889  589 QDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKIL 624
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
403-883 3.77e-72

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: 254.70  E-value: 3.77e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQllKSLKLYRN 482
Cdd:cd14903  120 LESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVE--ERLFLDSA 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  483 VEKYELLRNTTAMEE---DRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNIDGTEGCQVSNVyEVQE 559
Cdd:cd14903  198 NECAYTGANKTIKIEgmsDRKHFARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAIAPGDQ-GAVY 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  560 TAQLLNMEAQILINCLTrANSTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQREKN-LALLDF 638
Cdd:cd14903  277 ATKLLGLSPEALEKALC-SRTMRAAGDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANhIGVLDI 355
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  639 YGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKpSYGILSLINEPHL--N 716
Cdd:cd14903  356 FGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEEEGIRWAHIDFADNQDVLAVIED-RLGIISLLNDEVMrpK 434
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  717 SNDALLlrVQQCCAGHPNFMTT----GSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLSLVQSLFPE- 791
Cdd:cd14903  435 GNEESF--VSKLSSIHKDEQDViefpRTSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEk 512
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  792 --------------GNPRRQVTKKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLM 857
Cdd:cd14903  513 vespaaastslargARRRRGGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVI 592
                        490       500
                 ....*....|....*....|....*.
gi 78706810  858 PLVHLCRTGHCYHLLHVKFFHRYKLL 883
Cdd:cd14903  593 EAIRISRAAYPNRLLHEEFLDKFWLF 618
MYSc_Myh3 cd14913
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...
396-924 7.85e-72

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: 254.21  E-value: 7.85e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  396 VTCADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLK 475
Cdd:cd14913  122 IISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIE 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  476 SLKLYRNVEKYELLRN---TTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFV-----PITNIDGTE 547
Cdd:cd14913  202 LLLITTNPYDYPFISQgeiLVASIDDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKqkqreEQAEPDGTE 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  548 gcqvsnvyEVQETAQLLNMEAQILIN--CLTRANSTNsaqEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLK 625
Cdd:cd14913  282 --------VADKTAYLMGLNSSDLLKalCFPRVKVGN---EYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD 350
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  626 ST-QREKNLALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESIC-ELIDKPs 703
Cdd:cd14913  351 TKlPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACiELIEKP- 429
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  704 YGILSLINE----PHLNSNDALLLRVQQCCAGHPNF----MTTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISA 775
Cdd:cd14913  430 MGIFSILEEecmfPKATDTSFKNKLYDQHLGKSNNFqkpkVVKGRAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVG 509
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  776 AFYQSKLSLVQSLFP-------EGNPRRQVTKKPS---TLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMA 845
Cdd:cd14913  510 LYQKSSNRLLAHLYAtfatadaDSGKKKVAKKKGSsfqTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHS 589
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78706810  846 LVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPHFHGGSQVEGIALIIRNLPLPSAEFTIGTKNVFVR 924
Cdd:cd14913  590 LVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
399-924 4.06e-71

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: 252.24  E-value: 4.06e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  399 ADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLk 478
Cdd:cd14920  123 ANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDL- 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  479 LYRNVEKYELLRNTT---AMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNIDgtEGCQVSNVy 555
Cdd:cd14920  202 LLEGFNNYRFLSNGYipiPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTD--QASMPENT- 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  556 EVQETAQLLNMEaqilINCLTRANST---NSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQREKN 632
Cdd:cd14920  279 VAQKLCHLLGMN----VMEFTRAILTpriKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA 354
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  633 --LALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDY-FDNESICELIDKPSY--GIL 707
Cdd:cd14920  355 sfIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVL 434
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  708 SLINE----PHLnSNDALLLRVQQCCAGHPNFMTTGS--NSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSK 781
Cdd:cd14920  435 ALLDEecwfPKA-TDKTFVEKLVQEQGSHSKFQKPRQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSS 513
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  782 LSLVQSLFPEGN---PRRQVTKKPSTL-SSNIRTQ--------------LQTLLAIVKHRRSHYVFCIKPNEGKQPHQFD 843
Cdd:cd14920  514 DRFVAELWKDVDrivGLDQVTGMTETAfGSAYKTKkgmfrtvgqlykesLTKLMATLRNTNPNFVRCIIPNHEKRAGKLD 593
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  844 MALVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPH-FHGGSQveGIALIIRNLPLPSAEFTIGTKNVF 922
Cdd:cd14920  594 PHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgFMDGKQ--ACERMIRALELDPNLYRIGQSKIF 671

                 ..
gi 78706810  923 VR 924
Cdd:cd14920  672 FR 673
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
403-883 6.01e-71

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: 252.89  E-value: 6.01e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLKLyRN 482
Cdd:cd14902  138 LESFGNAQTIRNDNSSRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGL-QK 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  483 VEKYELL--------RNTTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNIDGTEGCQVSNV 554
Cdd:cd14902  217 GGKYELLnsygpsfaRKRAVADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASR 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  555 YEVQETAQLLNMEAQILINCLTrANSTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKIN------ESLKSTQ 628
Cdd:cd14902  297 FHLAKCAELMGVDVDKLETLLS-SREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSdeinyfDSAVSIS 375
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  629 REKN----LALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPSY 704
Cdd:cd14902  376 DEDEelatIGILDIFGFESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSN 455
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  705 GILSLINEPHL---NSNDALLLRVQQCCAGHPNFMttgsnsmcfqIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSK 781
Cdd:cd14902  456 GLFSLLDQECLmpkGSNQALSTKFYRYHGGLGQFV----------VHHFAGRVCYNVEQFVEKNTDALPADASDILSSSS 525
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  782 LSLVQSLFPEGNP------------RRQVTKKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQH 849
Cdd:cd14902  526 NEVVVAIGADENRdspgadngaagrRRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVE 605
                        490       500       510
                 ....*....|....*....|....*....|....
gi 78706810  850 QVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLL 883
Cdd:cd14902  606 QMRSVGVLEAVRIARHGYSVRLAHASFIELFSGF 639
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
403-884 1.59e-70

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: 251.44  E-value: 1.59e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLFDIEI---DFKGDpmGVHITHYMLEKTRITD-PIIGERNFHIFYQLLLGADLQLLKSLK 478
Cdd:cd14906  131 LEAFGNSRTTKNHNSSRFGKFLKIEFrssDGKID--GASIETYLLEKSRISHrPDNINLSYHIFYYLVYGASKDERSKWG 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  479 LYRNVEKYELL------------------RNTTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPI 540
Cdd:cd14906  209 LNNDPSKYRYLdarddvissfksqssnknSNHNNKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEED 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  541 TNIDGTEGCQVSNVYEVQETAQLLNMEAQILINCLTRANSTNSAQEDVGCE-MDARQAATNRNTLCRTLYSRLFTWLVNK 619
Cdd:cd14906  289 SDFSKYAYQKDKVTASLESVSKLLGYIESVFKQALLNRNLKAGGRGSVYCRpMEVAQSEQTRDALSKSLYVRLFKYIVEK 368
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  620 INESLKSTQREKNLA------------LLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRI 687
Cdd:cd14906  369 INRKFNQNTQSNDLAggsnkknnlfigVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNS 448
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  688 DYFDNESICELIDKPSYGILSLINEPHL---NSNDALLLRVQQCCAGHPNFMTTGSNSMCFQIRHYASVVNYSIHRFLEK 764
Cdd:cd14906  449 NFIDNKECIELIEKKSDGILSLLDDECImpkGSEQSLLEKYNKQYHNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEK 528
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  765 NSDMLPKYISAAFYQSKLSLVQSLF-PEGNPRRQVTKKPS---TLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPH 840
Cdd:cd14906  529 NRDSLYSDVEDLLLASSNFLKKSLFqQQITSTTNTTKKQTqsnTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCN 608
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....
gi 78706810  841 QFDMALVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLN 884
Cdd:cd14906  609 NFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIV 652
MYSc_Myo25 cd14886
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...
385-924 1.86e-70

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: 249.80  E-value: 1.86e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  385 HKSPTQRMRECVTCADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQ 464
Cdd:cd14886  107 HSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQ 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  465 LLLGADLQLLKSLKLyRNVEKYELLRNTTAME----EDRMNFHYTKRSLDVLgLSCEESNSIFRVIAVVLKLGNFIFVPI 540
Cdd:cd14886  187 CIKGLSPEEKKSLGF-KSLESYNFLNASKCYDapgiDDQKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEE 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  541 TNIDGTEGCQVSNVYEVQETAQLLNMEAQILINCL-TRANSTNSaqEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNK 619
Cdd:cd14886  265 GDMGVINAAKISNDEDFGKMCELLGIESSKAAQAIiTKVVVINN--ETIISPVTQAQAEVNIRAVAKDLYGALFELCVDT 342
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  620 INESLKSTQREKN-LALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICEL 698
Cdd:cd14886  343 LNEIIQFDADARPwIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFTDNSNVLAV 422
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  699 IDKPSYGILSLINEPHL----NSNdalllRVQQCCAGH---PNFMTTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPK 771
Cdd:cd14886  423 FDKPNLSIFSFLEEQCLiqtgSSE-----KFTSSCKSKiknNSFIPGKGSQCNFTIVHTAATVTYNTEEFVDKNKHKLSV 497
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  772 YISAAFYQSKLSLVQSLFpEGNPRRQVTKKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQV 851
Cdd:cd14886  498 DILELLMGSTNPIVNKAF-SDIPNEDGNMKGKFLGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQL 576
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78706810  852 RYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPHFHGGSQ-VEGIALIIRNLPLPSAEFTIGTKNVFVR 924
Cdd:cd14886  577 ISLSIFESIQTIHRGFAYNDTFEEFFHRNKILISHNSSSQNAGEDlVEAVKSILENLGIPCSDYRIGKTKVFLR 650
MYSc_Myh7 cd14917
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...
383-924 4.75e-70

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: 248.86  E-value: 4.75e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  383 RRHKSPTQ-RMRECVTCADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHI 461
Cdd:cd14917  108 KKDQTPGKgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHI 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  462 FYQLLLGADLQLLKSLKLYRNVEKYELL---RNTTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFV 538
Cdd:cd14917  188 FYQILSNKKPELLDMLLITNNPYDYAFIsqgETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFK 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  539 -----PITNIDGTEgcqvsnvyEVQETAQLLNMEAQILIN--CLTRANSTNsaqEDVGCEMDARQAATNRNTLCRTLYSR 611
Cdd:cd14917  268 qkqreEQAEPDGTE--------EADKSAYLMGLNSADLLKglCHPRVKVGN---EYVTKGQNVQQVIYATGALAKAVYEK 336
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  612 LFTWLVNKINESLKSTQ-REKNLALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDY- 689
Cdd:cd14917  337 MFNWMVTRINATLETKQpRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFg 416
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  690 FDNESICELIDKPsYGILSLINEPHLNSNDALLLRVQQCCAGH----PNFMT----TGSNSMCFQIRHYASVVNYSIHRF 761
Cdd:cd14917  417 MDLQACIDLIEKP-MGIMSILEEECMFPKATDMTFKAKLFDNHlgksNNFQKprniKGKPEAHFSLIHYAGTVDYNIIGW 495
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  762 LEKNSDMLPKYISAAFYQSKLSLVQSLFP----------EGNPRRQVTKKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCI 831
Cdd:cd14917  496 LQKNKDPLNETVVGLYQKSSLKLLSNLFAnyagadapieKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCI 575
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  832 KPNEGKQPHQFDMALVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPHFHGGSQVEGIALIIRNLPLPS 911
Cdd:cd14917  576 IPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSRKGAEKLLSSLDIDH 655
                        570
                 ....*....|...
gi 78706810  912 AEFTIGTKNVFVR 924
Cdd:cd14917  656 NQYKFGHTKVFFK 668
MYSc_Myh1_insects_crustaceans cd14909
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
403-924 5.40e-69

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: 245.90  E-value: 5.40e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLKLYRN 482
Cdd:cd14909  127 LEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDN 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  483 VEKYELL---RNTTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFV-----PITNIDGTEgcqvsnv 554
Cdd:cd14909  207 IYDYYIVsqgKVTVPNVDDGEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKqrgreEQAEQDGEE------- 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  555 yEVQETAQLLNMEAQILINCLTRANsTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQ-REKNL 633
Cdd:cd14909  280 -EGGRVSKLFGCDTAELYKNLLKPR-IKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQkRQHFI 357
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  634 ALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDY-FDNESICELIDKPsYGILSLINE 712
Cdd:cd14909  358 GVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIDWAFIDFgMDLLACIDLIEKP-MGILSILEE 436
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  713 PHLNSNDALLLRVQQCCAGH----PNFM-----TTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLS 783
Cdd:cd14909  437 ESMFPKATDQTFSEKLTNTHlgksAPFQkpkppKPGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNK 516
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  784 LVQSLFPE-----GNP------RRQVTKKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVR 852
Cdd:cd14909  517 LLIEIFADhagqsGGGeqakggRGKKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLT 596
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78706810  853 YMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPHFHGGSQVEGIalIIRNLPLPSAEFTIGTKNVFVR 924
Cdd:cd14909  597 CNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEEDPKKAAEI--ILESIALDPDQYRLGHTKVFFR 666
MYSc_Myh16 cd14934
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...
399-924 1.05e-68

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: 244.94  E-value: 1.05e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  399 ADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLK 478
Cdd:cd14934  121 ANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLL 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  479 LYRNVEKYELL-RNTTAME--EDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFvpiTNIDGTEGCQVSNVY 555
Cdd:cd14934  201 LVPNPKEYHWVsQGVTVVDnmDDGEELQITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKF---KQKPREEQAEVDTTE 277
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  556 EVQETAQLLNMEAQILINCLTRANsTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKS-TQREKNLA 634
Cdd:cd14934  278 VADKVAHLMGLNSGELQKGITRPR-VKVGNEFVQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTkMQRQFFIG 356
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  635 LLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDY-FDNESICELIDKPsYGILSLINEP 713
Cdd:cd14934  357 VLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWVFIDFgLDLQACIDLLEKP-MGIFSILEEQ 435
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  714 HL--NSNDALLLRV--QQCCAGHPNFMT------TGSNSMcFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLS 783
Cdd:cd14934  436 CVfpKATDATFKAAlyDNHLGKSSNFLKpkggkgKGPEAH-FELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLG 514
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  784 LVQSLFPE-----GNPRRQVTKKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMP 858
Cdd:cd14934  515 LLALLFKEeeapaGSKKQKRGSSFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLE 594
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78706810  859 LVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPHFHGGSQvEGIALIIRNLPLPSAEFTIGTKNVFVR 924
Cdd:cd14934  595 GIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQGFVDNK-KASELLLGSIDLDVNEYKIGHTKVFFR 659
PTZ00014 PTZ00014
myosin-A; Provisional
389-962 1.22e-68

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 248.02  E-value: 1.22e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   389 TQRMRECVTCADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLG 468
Cdd:PTZ00014  216 DLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKG 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   469 ADLQLLKSLKLyRNVEKYELLRN--TTAME-EDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNIDG 545
Cdd:PTZ00014  296 ANDEMKEKYKL-KSLEEYKYINPkcLDVPGiDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGL 374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   546 TEGCQVSNVYE--VQETAQLLNMEAQILINCLTRANSTNSAQEDVGcEMDARQAATNRNTLCRTLYSRLFTWLVNKINES 623
Cdd:PTZ00014  375 TDAAAISDESLevFNEACELLFLDYESLKKELTVKVTYAGNQKIEG-PWSKDESEMLKDSLSKAVYEKLFLWIIRNLNAT 453
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   624 LKSTQREKN-LALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKP 702
Cdd:PTZ00014  454 IEPPGGFKVfIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGK 533
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   703 SYGILSLINEPHL--NSNDALLLRV-QQCCAGHPNFMTTGSNS-MCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFY 778
Cdd:PTZ00014  534 GKSVLSILEDQCLapGGTDEKFVSScNTNLKNNPKYKPAKVDSnKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVK 613
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   779 QSKLSLVQSLFpEGNprrQVTK----KPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYM 854
Cdd:PTZ00014  614 ASPNPLVRDLF-EGV---EVEKgklaKGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSL 689
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   855 SLMPLVHLCRTGHCYHLLHVKFFHRYKLLNsLTWPHFHGGSQVEGIALIIRNLPLPSAEFTIGTKNVFVrSPRTVYELEQ 934
Cdd:PTZ00014  690 SILEALQLRQLGFSYRRTFAEFLSQFKYLD-LAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFL-KKDAAKELTQ 767
                         570       580
                  ....*....|....*....|....*...
gi 78706810   935 FRRLRISELAVLIQtMFRMYHARKRFQR 962
Cdd:PTZ00014  768 IQREKLAAWEPLVS-VLEALILKIKKKR 794
MYSc_Myh15_mammals cd14929
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...
399-924 8.40e-68

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: 242.19  E-value: 8.40e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  399 ADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLk 478
Cdd:cd14929  120 ANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLL- 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  479 LYRNVEKYELLR-NTTAME--EDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFV-----PITNIDGTEgcq 550
Cdd:cd14929  199 VSANPSDFHFCScGAVAVEslDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKqkpreEQLEADGTE--- 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  551 vsnvyEVQETAQLLNMEAQILINCLTRANsTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKST-QR 629
Cdd:cd14929  276 -----NADKAAFLMGINSSELVKGLIHPR-IKVGNEYVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLDAKlSR 349
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  630 EKNLALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDY-FDNESICELIDKPsYGILS 708
Cdd:cd14929  350 QFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEEYRKEGIDWVSIDFgLDLQACIDLIEKP-MGIFS 428
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  709 LINEPHLNSNDALLLRVQQCCAGH----PNFMTTGSN----SMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQS 780
Cdd:cd14929  429 ILEEECMFPKATDLTFKTKLFDNHfgksVHFQKPKPDkkkfEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKS 508
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  781 KLSLVQSLF----------PEGNPRRQVTKKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQ 850
Cdd:cd14929  509 SNRLLASLFenyistdsaiQFGEKKRKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQ 588
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78706810  851 VRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPHFHGGSQVEGIALIIRNLPLPSAEFTIGTKNVFVR 924
Cdd:cd14929  589 LRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
399-923 3.26e-67

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: 240.14  E-value: 3.26e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  399 ADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLK 478
Cdd:cd14879  128 AEFVLDSFGNAKTLTNPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLG 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  479 L-----YRNVEKYELLR-NTTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVpITNIDGTEGCQVS 552
Cdd:cd14879  208 LddpsdYALLASYGCHPlPLGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFT-YDHEGGEESAVVK 286
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  553 NVYEVQETAQLLNMEAQILINCLTraNSTNSAQEDVgCE--MDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQRE 630
Cdd:cd14879  287 NTDVLDIVAAFLGVSPEDLETSLT--YKTKLVRKEL-CTvfLDPEGAAAQRDELARTLYSLLFAWVVETINQKLCAPEDD 363
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  631 KN--LALLDFYGFE---ALDHNSFEQFAINYSAEKIHQnfvfHVLRS----EQELYIREGLEWSRIDYFDNESICELIDK 701
Cdd:cd14879  364 FAtfISLLDFPGFQnrsSTGGNSLDQFCVNFANERLHN----YVLRSfferKAEELEAEGVSVPATSYFDNSDCVRLLRG 439
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  702 PSYGILSLINE----PHLNSNDALLLRVQQCCAGHPNF-----MTTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMlpky 772
Cdd:cd14879  440 KPGGLLGILDDqtrrMPKKTDEQMLEALRKRFGNHSSFiavgnFATRSGSASFTVNHYAGEVTYSVEGFLERNGDV---- 515
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  773 ISAAFyqskLSLVQSlfpegnprrqvtkkpstlSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVR 852
Cdd:cd14879  516 LSPDF----VNLLRG------------------ATQLNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIR 573
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78706810  853 YMSLMPLVHLCRTGHCYHLLHVKFFHRYKllnsltwPHFHGGSQVEGIALIIRNLPLPSAEFTIGTKNVFV 923
Cdd:cd14879  574 SLGLPELAARLRVEYVVSLEHAEFCERYK-------STLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
399-924 8.77e-67

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: 239.50  E-value: 8.77e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  399 ADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLK 478
Cdd:cd14911  132 ANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFI 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  479 LyRNVEKYELLRN---TTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNIDGTegcQVSNVY 555
Cdd:cd14911  212 L-DDVKSYAFLSNgslPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQA---TLPDNT 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  556 EVQETAQLLNMEAQILINCLTRANsTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQREKN--L 633
Cdd:cd14911  288 VAQKIAHLLGLSVTDMTRAFLTPR-IKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGAsfI 366
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  634 ALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDY-FDNESICELIDKPsYGILSLINE 712
Cdd:cd14911  367 GILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKP-GGIMALLDE 445
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  713 PHL---NSNDALLLRVQQCCAGHPNFMTTGSNSMC-FQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLSLVQSL 788
Cdd:cd14911  446 ECWfpkATDKTFVDKLVSAHSMHPKFMKTDFRGVAdFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNI 525
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  789 FPE----GNPRRQVTKKP----------STLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYM 854
Cdd:cd14911  526 WKDaeivGMAQQALTDTQfgartrkgmfRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCN 605
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78706810  855 SLMPLVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPH-FHGGSQveGIALIIRNLPLPSAEFTIGTKNVFVR 924
Cdd:cd14911  606 GVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKgFMDGKK--ACEKMIQALELDSNLYRVGQSKIFFR 674
MYSc_Myh2_mammals cd14912
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
392-924 2.01e-66

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: 238.48  E-value: 2.01e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  392 MRECVTCADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADL 471
Cdd:cd14912  120 LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKP 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  472 QLLKSLKLYRNVEKYELLRN---TTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFV-----PITNI 543
Cdd:cd14912  200 ELIEMLLITTNPYDYPFVSQgeiSVASIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKqkqreEQAEP 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  544 DGTEGCQVSNVYEVQETAQLLNMEaqilinCLTRANSTNsaqEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINES 623
Cdd:cd14912  280 DGTEVADKAAYLQSLNSADLLKAL------CYPRVKVGN---EYVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQ 350
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  624 LKSTQ-REKNLALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESIC-ELIDK 701
Cdd:cd14912  351 LDTKQpRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACiELIEK 430
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  702 PsYGILSLINE----PHLNSNDALLLRVQQCCAGHPNF----MTTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYI 773
Cdd:cd14912  431 P-MGIFSILEEecmfPKATDTSFKNKLYEQHLGKSANFqkpkVVKGKAEAHFSLIHYAGVVDYNITGWLDKNKDPLNETV 509
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  774 SAAFYQSKLSLVQSLFP----------EGNPRRQVTKKPS---TLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPH 840
Cdd:cd14912  510 VGLYQKSAMKTLAYLFSgaqtaegasaGGGAKKGGKKKGSsfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPG 589
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  841 QFDMALVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPHFHGGSQVEGIALIIRNLPLPSAEFTIGTKN 920
Cdd:cd14912  590 AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTK 669

                 ....
gi 78706810  921 VFVR 924
Cdd:cd14912  670 VFFK 673
MYSc_Myh8 cd14918
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...
392-924 2.38e-66

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: 238.09  E-value: 2.38e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  392 MRECVTCADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADL 471
Cdd:cd14918  118 LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKP 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  472 QLLKSLKLYRNVEKYELLRN---TTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFV-----PITNI 543
Cdd:cd14918  198 DLIEMLLITTNPYDYAFVSQgeiTVPSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKqkqreEQAEP 277
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  544 DGTEGCQVSNVYEVQETAQLLNMEaqilinCLTRANSTNsaqEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINES 623
Cdd:cd14918  278 DGTEVADKAAYLQSLNSADLLKAL------CYPRVKVGN---EYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQ 348
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  624 LKSTQ-REKNLALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESIC-ELIDK 701
Cdd:cd14918  349 LDTKQpRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACiELIEK 428
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  702 PsYGILSLINE----PHLNSNDALLLRVQQCCAGHPNF----MTTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYI 773
Cdd:cd14918  429 P-LGIFSILEEecmfPKATDTSFKNKLYDQHLGKSANFqkpkVVKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTV 507
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  774 SAAFYQSKLSLVQSLFP-------EGNPRRQVTKKPS---TLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFD 843
Cdd:cd14918  508 VGLYQKSAMKTLASLFStyasaeaDSGAKKGAKKKGSsfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAME 587
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  844 MALVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPHFHGGSQVEGIALIIRNLPLPSAEFTIGTKNVFV 923
Cdd:cd14918  588 HELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFF 667

                 .
gi 78706810  924 R 924
Cdd:cd14918  668 K 668
MYSc_Myh6 cd14916
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...
399-924 3.90e-66

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: 237.65  E-value: 3.90e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  399 ADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLK 478
Cdd:cd14916  126 ANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLL 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  479 LYRNVEKYELLRN---TTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFV-----PITNIDGTEGCQ 550
Cdd:cd14916  206 VTNNPYDYAFVSQgevSVASIDDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKqkqreEQAEPDGTEDAD 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  551 vsnvyevqETAQLLNMEAQILIN--CLTRANSTNsaqEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQ 628
Cdd:cd14916  286 --------KSAYLMGLNSADLLKglCHPRVKVGN---EYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQ 354
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  629 -REKNLALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDY-FDNESICELIDKPsYGI 706
Cdd:cd14916  355 pRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEKP-MGI 433
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  707 LSLINEPHLNSNDALLLRVQQCCAGH----PNFM----TTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFY 778
Cdd:cd14916  434 MSILEEECMFPKASDMTFKAKLYDNHlgksNNFQkprnVKGKQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQ 513
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  779 QSKLSLVQSLFP--------EGNPRRQVTKKPS---TLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALV 847
Cdd:cd14916  514 KSSLKLMATLFStyasadtgDSGKGKGGKKKGSsfqTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLV 593
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78706810  848 QHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPHFHGGSQVEGIALIIRNLPLPSAEFTIGTKNVFVR 924
Cdd:cd14916  594 MHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
MYSc_Myh9 cd14919
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...
382-924 3.45e-65

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: 234.60  E-value: 3.45e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  382 HRRHKSPTQRMRECVTcADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHI 461
Cdd:cd14919  104 HKSKKDQGELERQLLQ-ANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHI 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  462 FYQLLLGADLQLLKSLkLYRNVEKYELLRN---TTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFV 538
Cdd:cd14919  183 FYYLLSGAGEHLKTDL-LLEPYNKYRFLSNghvTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFK 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  539 PITNidgTEGCQVSNVYEVQETAQLLNMEaqilINCLTRANST---NSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTW 615
Cdd:cd14919  262 KERN---TDQASMPDNTAAQKVSHLLGIN----VTDFTRGILTpriKVGRDYVQKAQTKEQADFAIEALAKATYERMFRW 334
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  616 LVNKINESLKSTQREKN--LALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDY-FDN 692
Cdd:cd14919  335 LVLRINKALDKTKRQGAsfIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDL 414
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  693 ESICELIDKPS--YGILSLINE----PHLnSNDALLLRVQQCCAGHPNFMTTGS--NSMCFQIRHYASVVNYSIHRFLEK 764
Cdd:cd14919  415 QPCIDLIEKPAgpPGILALLDEecwfPKA-TDKSFVEKVVQEQGTHPKFQKPKQlkDKADFCIIHYAGKVDYKADEWLMK 493
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  765 NSDMLPKYISAAFYQSKLSLVQSLFPEGN----------------PRRQVTKKP--STLSSNIRTQLQTLLAIVKHRRSH 826
Cdd:cd14919  494 NMDPLNDNIATLLHQSSDKFVSELWKDVDriigldqvagmsetalPGAFKTRKGmfRTVGQLYKEQLAKLMATLRNTNPN 573
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  827 YVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPH-FHGGSQveGIALIIR 905
Cdd:cd14919  574 FVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKgFMDGKQ--ACVLMIK 651
                        570
                 ....*....|....*....
gi 78706810  906 NLPLPSAEFTIGTKNVFVR 924
Cdd:cd14919  652 ALELDSNLYRIGQSKVFFR 670
MYSc_Myh7b cd14927
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...
399-924 7.67e-65

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: 233.69  E-value: 7.67e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  399 ADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLK 478
Cdd:cd14927  129 ANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLL 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  479 LYRNVEKYELL-RNTTAME--EDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPI-----TNIDGTEgcq 550
Cdd:cd14927  209 VSMNPYDYHFCsQGVTTVDnmDDGEELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKqreeqAEADGTE--- 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  551 vsnvyEVQETAQLLNMEAQILINCLTRANsTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKST-QR 629
Cdd:cd14927  286 -----SADKAAYLMGVSSADLLKGLLHPR-VKVGNEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKlPR 359
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  630 EKNLALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDY-FDNESICELIDKPsYGILS 708
Cdd:cd14927  360 QFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFIDFgLDLQACIDLIEKP-LGILS 438
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  709 LINEPHL---NSNDALLLRVQQCCAGH-PNFMTTGSN-----SMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQ 779
Cdd:cd14927  439 ILEEECMfpkASDASFKAKLYDNHLGKsPNFQKPRPDkkrkyEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQK 518
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  780 SKLSLVQSLF-------PEGNPRRQVTKKP------STLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMAL 846
Cdd:cd14927  519 SQNKLLATLYenyvgsdSTEDPKSGVKEKRkkaasfQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFL 598
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78706810  847 VQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPHFHGGSQVEGIALIIRNLPLPSAEFTIGTKNVFVR 924
Cdd:cd14927  599 VLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIPDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
MYSc_Myh1_mammals cd14910
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
392-924 8.76e-65

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: 233.47  E-value: 8.76e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  392 MRECVTCADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADL 471
Cdd:cd14910  120 LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKP 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  472 QLLKSLKLYRNVEKYELLRN---TTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFV-----PITNI 543
Cdd:cd14910  200 DLIEMLLITTNPYDYAFVSQgeiTVPSIDDQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKqkqreEQAEP 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  544 DGTEGCQVSNVYEVQETAQLLNMEaqilinCLTRANSTNsaqEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINES 623
Cdd:cd14910  280 DGTEVADKAAYLQNLNSADLLKAL------CYPRVKVGN---EYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQ 350
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  624 LKSTQ-REKNLALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESIC-ELIDK 701
Cdd:cd14910  351 LDTKQpRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACiELIEK 430
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  702 PsYGILSLINE----PHLNSNDALLLRVQQCCAGHPNFM----TTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYI 773
Cdd:cd14910  431 P-MGIFSILEEecmfPKATDTSFKNKLYEQHLGKSNNFQkpkpAKGKVEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETV 509
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  774 SAAFYQSKLSLVQSLFP--------EGNPRRQVTKKPS---TLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQF 842
Cdd:cd14910  510 VGLYQKSSMKTLALLFSgaaaaeaeEGGGKKGGKKKGSsfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAM 589
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  843 DMALVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPHFHGGSQVEGIALIIRNLPLPSAEFTIGTKNVF 922
Cdd:cd14910  590 EHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVF 669

                 ..
gi 78706810  923 VR 924
Cdd:cd14910  670 FK 671
MYSc_Myh4 cd14915
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...
392-924 1.40e-64

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: 233.08  E-value: 1.40e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  392 MRECVTCADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADL 471
Cdd:cd14915  120 LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKP 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  472 QLLKSLKLYRNVEKYELLRN---TTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNIDGTE- 547
Cdd:cd14915  200 ELIEMLLITTNPYDFAFVSQgeiTVPSIDDQEELMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEp 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  548 -GCQVSNvyevqETAQLLNMEAQILIN--CLTRANSTNsaqEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESL 624
Cdd:cd14915  280 dGTEVAD-----KAAYLTSLNSADLLKalCYPRVKVGN---EYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQL 351
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  625 KSTQ-REKNLALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESIC-ELIDKP 702
Cdd:cd14915  352 DTKQpRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACiELIEKP 431
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  703 sYGILSLINE----PHLNSNDALLLRVQQCCAGHPNFM----TTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYIS 774
Cdd:cd14915  432 -MGIFSILEEecmfPKATDTSFKNKLYEQHLGKSNNFQkpkpAKGKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVV 510
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  775 AAFYQSKLSLVQSLFP-------EGNPRRQVTKKP----STLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFD 843
Cdd:cd14915  511 GLYQKSGMKTLAFLFSggqtaeaEGGGGKKGGKKKgssfQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAME 590
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  844 MALVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPHFHGGSQVEGIALIIRNLPLPSAEFTIGTKNVFV 923
Cdd:cd14915  591 HELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFF 670

                 .
gi 78706810  924 R 924
Cdd:cd14915  671 K 671
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
403-852 1.84e-64

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: 231.86  E-value: 1.84e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLFDIEidFKGDP---MGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLKL 479
Cdd:cd14891  139 LESFGNAKTLRNHNSSRFGKFMKLQ--FTKDKfklAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLL 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  480 YRNVEKYELLRN--TTAME-EDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVpitNIDGTEGCQVSNVYE 556
Cdd:cd14891  217 LSPEDFIYLNQSgcVSDDNiDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFD---EEDTSEGEAEIASES 293
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  557 VQET----AQLLNMEAQILINCLT-RANSTNSaqEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQRE- 630
Cdd:cd14891  294 DKEAlataAELLGVDEEALEKVITqREIVTRG--ETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPl 371
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  631 KNLALLDFYGFEALD-HNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELI-DKPSyGILS 708
Cdd:cd14891  372 PYIGVLDIFGFESFEtKNDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIaSKPN-GILP 450
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  709 LINEPHLN---SNDALLLRVQQCCAGHPNFMTTGSNSM--CFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLS 783
Cdd:cd14891  451 LLDNEARNpnpSDAKLNETLHKTHKRHPCFPRPHPKDMreMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASSAKF 530
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78706810  784 LvqslfpegnprrqvtkkpstlssnirTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVR 852
Cdd:cd14891  531 S--------------------------DQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLR 573
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
399-924 4.14e-64

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: 231.84  E-value: 4.14e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  399 ADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLK 478
Cdd:cd14932  127 ANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELC 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  479 LyRNVEKYELLRN---TTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNIDGTegcQVSNVY 555
Cdd:cd14932  207 L-EDYSKYRFLSNgnvTIPGQQDKELFAETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQA---SMPDDT 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  556 EVQETAQLLNMEaqilINCLTRA---NSTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQREKN 632
Cdd:cd14932  283 AAQKVCHLLGMN----VTDFTRAilsPRIKVGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGA 358
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  633 --LALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDY-FDNESICELIDKPS--YGIL 707
Cdd:cd14932  359 sfIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPNgpPGIL 438
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  708 SLINE----PHLnSNDALLLRVQQCCAGHPNFMTTG--SNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSK 781
Cdd:cd14932  439 ALLDEecwfPKA-TDKSFVEKVVQEQGNNPKFQKPKklKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQST 517
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  782 LSLVQSLFPEGN---PRRQVTKKPSTLSSNIRT--------------QLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDM 844
Cdd:cd14932  518 DKFVSELWKDVDrivGLDKVAGMGESLHGAFKTrkgmfrtvgqlykeQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAH 597
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  845 ALVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPH-FHGGSQveGIALIIRNLPLPSAEFTIGTKNVFV 923
Cdd:cd14932  598 HLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgFMDGKQ--ACVLMVKALELDPNLYRIGQSKVFF 675

                 .
gi 78706810  924 R 924
Cdd:cd14932  676 R 676
MYSc_Myh13 cd14923
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...
399-889 8.14e-64

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: 230.73  E-value: 8.14e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  399 ADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLK 478
Cdd:cd14923  126 ANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLL 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  479 LYRNVEKYELLRN---TTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNIDGTE--GCQVSN 553
Cdd:cd14923  206 ISTNPFDFPFVSQgevTVASIDDSEELLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEpdGTEVAD 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  554 vyevqETAQLLNMEAQILIN--CLTRANSTNsaqEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQ-RE 630
Cdd:cd14923  286 -----KAGYLMGLNSAEMLKglCCPRVKVGN---EYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQpRQ 357
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  631 KNLALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESIC-ELIDKPsYGILSL 709
Cdd:cd14923  358 YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACiELIEKP-MGIFSI 436
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  710 INE----PHLNSNDALLLRVQQCCAGHPNFM----TTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSK 781
Cdd:cd14923  437 LEEecmfPKATDTSFKNKLYDQHLGKSNNFQkpkpAKGKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSS 516
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  782 LSLVQSLFPE---------GNPRRQVTKKPS---TLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQH 849
Cdd:cd14923  517 LKLLSFLFSNyagaeagdsGGSKKGGKKKGSsfqTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMH 596
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 78706810  850 QVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNSLTWP 889
Cdd:cd14923  597 QLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIP 636
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
383-924 6.10e-63

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: 228.36  E-value: 6.10e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  383 RRHKSPTQRMRECVTCADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIF 462
Cdd:cd14921  107 KKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIF 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  463 YQLLLGADLQLLKSLkLYRNVEKYELLRN----TTAMEEDRMnFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFV 538
Cdd:cd14921  187 YYLIAGAKEKMRSDL-LLEGFNNYTFLSNgfvpIPAAQDDEM-FQETLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFK 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  539 PITNidgTEGCQVSNVYEVQETAQLLNMEAQILINCLTRANsTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVN 618
Cdd:cd14921  265 KERN---TDQASMPDNTAAQKVCHLMGINVTDFTRSILTPR-IKVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILT 340
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  619 KINESLKSTQREKN--LALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDY-FDNESI 695
Cdd:cd14921  341 RVNKALDKTHRQGAsfLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPC 420
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  696 CELIDKPSY--GILSLINE----PHLnSNDALLLRVQQCCAGHPNFMTTGS--NSMCFQIRHYASVVNYSIHRFLEKNSD 767
Cdd:cd14921  421 IELIERPNNppGVLALLDEecwfPKA-TDKSFVEKLCTEQGNHPKFQKPKQlkDKTEFSIIHYAGKVDYNASAWLTKNMD 499
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  768 MLPKYISAAFYQSKLSLVQSLFPEGN----------------PRRQVTKKP--STLSSNIRTQLQTLLAIVKHRRSHYVF 829
Cdd:cd14921  500 PLNDNVTSLLNASSDKFVADLWKDVDrivgldqmakmtesslPSASKTKKGmfRTVGQLYKEQLGKLMTTLRNTTPNFVR 579
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  830 CIKPNEGKQPHQFDMALVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPH-FHGGSQveGIALIIRNLP 908
Cdd:cd14921  580 CIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKgFMDGKQ--ACILMIKALE 657
                        570
                 ....*....|....*.
gi 78706810  909 LPSAEFTIGTKNVFVR 924
Cdd:cd14921  658 LDPNLYRIGQSKIFFR 673
MYSc_Myh19 cd15896
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...
399-924 3.95e-61

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: 223.02  E-value: 3.95e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  399 ADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLk 478
Cdd:cd15896  127 ANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSEL- 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  479 LYRNVEKYELLRN---TTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNidgTEGCQVSNVY 555
Cdd:cd15896  206 LLENYNNYRFLSNgnvTIPGQQDKDLFTETMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERH---TDQASMPDNT 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  556 EVQETAQLLNMEaqilINCLTRA---NSTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQREKN 632
Cdd:cd15896  283 AAQKVCHLMGMN----VTDFTRAilsPRIKVGRDYVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGA 358
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  633 --LALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDY-FDNESICELIDKPSY--GIL 707
Cdd:cd15896  359 sfIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIEKPASppGIL 438
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  708 SLINE----PHLnSNDALLLRVQQCCAGHPNFMTTG--SNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSK 781
Cdd:cd15896  439 ALLDEecwfPKA-TDKSFVEKVLQEQGTHPKFFKPKklKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQST 517
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  782 LSLVQSLFPEGN--------------PRRQVTKKP--STLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMA 845
Cdd:cd15896  518 DKFVSELWKDVDrivgldkvsgmsemPGAFKTRKGmfRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPH 597
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  846 LVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPH-FHGGSQveGIALIIRNLPLPSAEFTIGTKNVFVR 924
Cdd:cd15896  598 LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgFMDGKQ--ACVLMIKSLELDPNLYRIGQSKVFFR 675
MYSc_Myh14_mammals cd14930
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...
399-924 1.32e-59

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: 218.04  E-value: 1.32e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  399 ADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLk 478
Cdd:cd14930  123 ANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADL- 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  479 LYRNVEKYELLRN--TTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNidgTEGCQVSNVYE 556
Cdd:cd14930  202 LLEPCSHYRFLTNgpSSSPGQERELFQETLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERN---TDQATMPDNTA 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  557 VQETAQLLNMEaqilINCLTRANST---NSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQREKN- 632
Cdd:cd14930  279 AQKLCRLLGLG----VTDFSRALLTpriKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAs 354
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  633 -LALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDY-FDNESICELIDKPSY--GILS 708
Cdd:cd14930  355 fLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLA 434
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  709 LINE----PHLnSNDALLLRVQQCCAGHPNFMTTGS--NSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKL 782
Cdd:cd14930  435 LLDEecwfPKA-TDKSFVEKVAQEQGGHPKFQRPRHlrDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTD 513
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  783 SLVQSLF-------------------PEGNPRRQVTKkpsTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFD 843
Cdd:cd14930  514 RLTAEIWkdvegivgleqvsslgdgpPGGRPRRGMFR---TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLE 590
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  844 MALVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPH-FHGGSQveGIALIIRNLPLPSAEFTIGTKNVF 922
Cdd:cd14930  591 PRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKgFMDGKQ--ACEKMIQALELDPNLYRVGQSKIF 668

                 ..
gi 78706810  923 VR 924
Cdd:cd14930  669 FR 670
MYSc_Myo37 cd14898
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...
389-885 3.78e-59

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: 214.76  E-value: 3.78e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  389 TQRMRECVTCADVFLEAMGNACTLKNNNSSRYGKLfdIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLG 468
Cdd:cd14898  100 TTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKR--IKLKFDGKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCAS 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  469 adlqllKSLKLYRN-VEKYELLRNTTAMEEDRMNFHYTKRSLDVLGLSceESNSIFRVIAVVLKLGNFIFVpitnidgTE 547
Cdd:cd14898  178 ------KRLNIKNDfIDTSSTAGNKESIVQLSEKYKMTCSAMKSLGIA--NFKSIEDCLLGILYLGSIQFV-------ND 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  548 GCQV--SNVYeVQETAQLLNMEAQILINCLTRAnSTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLk 625
Cdd:cd14898  243 GILKlqRNES-FTEFCKLHNIQEEDFEESLVKF-SIQVKGETIEVFNTLKQARTIRNSMARLLYSNVFNYITASINNCL- 319
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  626 STQREKNLALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPSyG 705
Cdd:cd14898  320 EGSGERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEEGIEWPDVEFFDNNQCIRDFEKPC-G 398
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  706 ILSLINEPHLN---SNDALLLRVQQCCAGHPNfmTTGSNSMcfQIRHYASVVNYSIHRFLEKNSDMlpkyisaafyqskl 782
Cdd:cd14898  399 LMDLISEESFNawgNVKNLLVKIKKYLNGFIN--TKARDKI--KVSHYAGDVEYDLRDFLDKNREK-------------- 460
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  783 slvQSLFPEGNPRRQVTKKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLVHL 862
Cdd:cd14898  461 ---GQLLIFKNLLINDEGSKEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRL 537
                        490       500
                 ....*....|....*....|...
gi 78706810  863 CRTGHCYHLLHVKFFHRYKLLNS 885
Cdd:cd14898  538 SKQCFPQEIPKDRFEERYRILGI 560
MYSc_Myo14 cd14876
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...
391-884 4.67e-59

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: 216.01  E-value: 4.67e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  391 RMRECVTCADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGAD 470
Cdd:cd14876  109 RIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGAD 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  471 LQLLKSLKLyRNVEKYELLrNTTAME----EDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPiTNIDGT 546
Cdd:cd14876  189 SEMKSKYHL-LGLKEYKFL-NPKCLDvpgiDDVADFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITG-KTEQGV 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  547 E--GCQVSNVYEVQETA-QLLNMEAQILINCLTRANSTNSAQEDVGcEMDARQAATNRNTLCRTLYSRLFTWLVNKINES 623
Cdd:cd14876  266 DdaAAISNESLEVFKEAcSLLFLDPEALKRELTVKVTKAGGQEIEG-RWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNST 344
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  624 LKSTQREKN-LALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKP 702
Cdd:cd14876  345 IEPPGGFKNfMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERESKLYKDEGIPTAELEYTSNAEVIDVLCGK 424
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  703 SYGILSLINEPHLN--SNDALLlrVQQCCA-----GHPNFMTTGSNSMcFQIRHYASVVNYSIHRFLEKNSDMLPKYISA 775
Cdd:cd14876  425 GKSVLSILEDQCLApgGSDEKF--VSACVSklksnGKFKPAKVDSNIN-FIVVHTIGDIQYNAEGFLFKNKDVLRAELVE 501
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  776 AFYQSKLSLVQSLFpEGNPrrqVTK----KPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQV 851
Cdd:cd14876  502 VVQASTNPVVKALF-EGVV---VEKgkiaKGSLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQL 577
                        490       500       510
                 ....*....|....*....|....*....|...
gi 78706810  852 RYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLN 884
Cdd:cd14876  578 HALSILEALQLRQLGYSYRRPFEEFLYQFKFLD 610
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
382-867 2.02e-54

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: 202.73  E-value: 2.02e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  382 HRRHKSPTQR-----MRECVTCADVFLEAMGNACTLKNNNSSRYGKLFDIEID-FKGDPMGVHITHYMLEKTRITDPIIG 455
Cdd:cd14875  105 YMHSSNTSQRsiadkIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPG 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  456 ERNFHIFYQLLLGADLQLLKSLKLYRNVEKYELLR--NTTAME-------EDRMNFHYTKRSLDVLGLSCEESNSIFRVI 526
Cdd:cd14875  185 ERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNggNTFVRRgvdgktlDDAHEFQNVRHALSMIGVELETQNSIFRVL 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  527 AVVLKLGNFIFVPitniDGTEGCQVSNVYEVQETAQLLNMEAQILINCLTRANSTNSaqedVGCEMDARQAATNRNTLCR 606
Cdd:cd14875  265 ASILHLMEVEFES----DQNDKAQIADETPFLTACRLLQLDPAKLRECFLVKSKTSL----VTILANKTEAEGFRNAFCK 336
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  607 TLYSRLFTWLVNKINESLK---STQREKNLALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLE 683
Cdd:cd14875  337 AIYVGLFDRLVEFVNASITpqgDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQNHYNKYTFINDEEECRREGIQ 416
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  684 WSRIDYFDNESICELIDKPSYGILSLI-NEPHLN--SNDALLLRVQQCCAGHPNFM----TTGSNSmcFQIRHYASVVNY 756
Cdd:cd14875  417 IPKIEFPDNSECVNMFDQKRTGIFSMLdEECNFKggTTERFTTNLWDQWANKSPYFvlpkSTIPNQ--FGVNHYAAFVNY 494
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  757 SIHRFLEKNSDMLPKYISAAFYQSKLSLVQSLFPEGnprRQVTKKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEG 836
Cdd:cd14875  495 NTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTE---KGLARRKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNME 571
                        490       500       510
                 ....*....|....*....|....*....|.
gi 78706810  837 KQPHQFDMALVQHQVRYMSLMPLVHLCRTGH 867
Cdd:cd14875  572 ASPSFLDNLLVGSQLESAGVLQTIALKRQGY 602
MYSc_Myo24A cd14937
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
399-881 1.06e-53

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: 199.86  E-value: 1.06e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  399 ADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLK 478
Cdd:cd14937  110 SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYK 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  479 LyRNVEKYELLRNTTAM---EEDRMNFHYTKRSLDVLGLScEESNSIFRVIAVVLKLGNFIFVPITNiDGTEGCQV---S 552
Cdd:cd14937  190 I-RSENEYKYIVNKNVVipeIDDAKDFGNLMISFDKMNMH-DMKDDLFLTLSGLLLLGNVEYQEIEK-GGKTNCSEldkN 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  553 NVYEVQETAQLLNMEAQILINCLTRANSTnSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQREKN 632
Cdd:cd14937  267 NLELVNEISNLLGINYENLKDCLVFTEKT-IANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNN 345
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  633 -LALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIdKPSYGILSLIN 711
Cdd:cd14937  346 yIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETELYKAEDILIESVKYTTNESIIDLL-RGKTSIISILE 424
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  712 EPHLN--SNDALLLRV-QQCCAGHPNFMTTGSN-SMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLSLVQS 787
Cdd:cd14937  425 DSCLGpvKNDESIVSVyTNKFSKHEKYASTKKDiNKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRS 504
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  788 LFPEGNPRRQVTKKpSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMplvhlcrtgh 867
Cdd:cd14937  505 LYEDVEVSESLGRK-NLITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSII---------- 573
                        490
                 ....*....|....
gi 78706810  868 cyHLLHVKFFHRYK 881
Cdd:cd14937  574 --ETLNISFFFQYK 585
MYSc_Myo38 cd14899
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...
392-881 2.12e-50

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: 191.46  E-value: 2.12e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  392 MRECVTCADVFLEAMGNACTLKNNNSSRYGKLFDIEI-DFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGAD 470
Cdd:cd14899  136 IEEQVLQSNPILEAFGNARTVRNDNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADN 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  471 LQLLK----SLKLYRNVEKYELLRNTTAME-----EDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPIT 541
Cdd:cd14899  216 NCVSKeqkqVLALSGGPQSFRLLNQSLCSKrrdgvKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIP 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  542 -----NIDGTEG---CQVSNVYE-VQETAQLLNMEAQILINCLTRaNSTNSAQEDVGCEMDARQAATNRNTLCRTLYSRL 612
Cdd:cd14899  296 hkgddTVFADEArvmSSTTGAFDhFTKAAELLGVSTEALDHALTK-RWLHASNETLVVGVDVAHARNTRNALTMECYRLL 374
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  613 FTWLVNKINESLkstQREKN-------------------LALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSE 673
Cdd:cd14899  375 FEWLVARVNNKL---QRQASapwgadesdvddeedatdfIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEE 451
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  674 QELYIREGLEWSRIDYFDNESICELIDKPSYGILSLINEPHL---NSNDALLLRVQ---QCCAGHPNFMTTG--SNSMCF 745
Cdd:cd14899  452 QRLYRDEGIRWSFVDFPNNRACLELFEHRPIGIFSLTDQECVfpqGTDRALVAKYYlefEKKNSHPHFRSAPliQRTTQF 531
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  746 QIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLSLVQSL----------------FPEGNPRRQVTKKPSTLS--S 807
Cdd:cd14899  532 VVAHYAGCVTYTIDGFLAKNKDSFCESAAQLLAGSSNPLIQALaagsndedangdseldGFGGRTRRRAKSAIAAVSvgT 611
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78706810  808 NIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYK 881
Cdd:cd14899  612 QFKIQLNELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
MYSc_Myo12 cd14874
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...
403-883 7.70e-48

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: 181.99  E-value: 7.70e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGklFDIEIDFKGDPM-GVHITHYM-LEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLKLy 480
Cdd:cd14874  108 FKSFGCAKTLKNDEATRFG--CSIDLLYKRNVLtGLNLKYTVpLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGI- 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  481 RNVEKYELL---RNTTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNIDGTEGC-QVSNVYE 556
Cdd:cd14874  185 KGLQKFFYInqgNSTENIQSDVNHFKHLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPNVEQDVvEIGNMSE 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  557 VQETAQLLNMEAQILINCLTranstnsAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINESLKSTQREKNLALL 636
Cdd:cd14874  265 VKWVAFLLEVDFDQLVNFLL-------PKSEDGTTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGVISIL 337
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  637 DFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEwsrIDY-----FDNESICELIDKPSYGILSLIN 711
Cdd:cd14874  338 DHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQLVDYAKDGIS---VDYkvpnsIENGKTVELLFKKPYGLLPLLT 414
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  712 E----PHLNSNDALllrvQQCCAGHPNFMTTGS----NSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLS 783
Cdd:cd14874  415 DeckfPKGSHESYL----EHCNLNHTDRSSYGKarnkERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNP 490
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  784 LVQSLFPE--GNPRRQVTkkpsTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLVH 861
Cdd:cd14874  491 IIGLLFESysSNTSDMIV----SQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLS 566
                        490       500
                 ....*....|....*....|..
gi 78706810  862 LCRTGHCYHLLHVKFFHRYKLL 883
Cdd:cd14874  567 FRIKGYPVKISKTTFARQYRCL 588
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
403-922 7.75e-48

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: 182.24  E-value: 7.75e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLfdIEIDF-KGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLKL-- 479
Cdd:cd14881  115 LRSLGSAKTATNSESSRIGHF--IEVQVtDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLdg 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  480 Y--RNVeKYeLLRNTTAME--EDRMNFHYTKRSLDVLGLSCEEsnsIFRVIAVVLKLGNFIFVpitNIDGTEGCQVSNVy 555
Cdd:cd14881  193 YspANL-RY-LSHGDTRQNeaEDAARFQAWKACLGILGIPFLD---VVRVLAAVLLLGNVQFI---DGGGLEVDVKGET- 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  556 EVQETAQLLNMEAQILINCLTrANSTNSAQEDVGCEMDARQAATNRNTLCRTLYSRLFTWLVNKINeSLK---STQREKN 632
Cdd:cd14881  264 ELKSVAALLGVSGAALFRGLT-TRTHNARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRAN-SLKrlgSTLGTHA 341
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  633 ----LALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEWS-RIDYFDNESICELIDKPSYGIL 707
Cdd:cd14881  342 tdgfIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEvEVDYVDNVPCIDLISSLRTGLL 421
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  708 SLIN---------EPHLNSndallLRVQQccAGHPNFMTTGSNSM-CFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAF 777
Cdd:cd14881  422 SMLDvecsprgtaESYVAK-----IKVQH--RQNPRLFEAKPQDDrMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVF 494
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  778 YQSKLSLVqslFpegnprrqvtkkpSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLM 857
Cdd:cd14881  495 YKQNCNFG---F-------------ATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVL 558
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78706810  858 PLVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPHFHGGSQVEGIALIIRNL------PLPSA--EFTIGTKNVF 922
Cdd:cd14881  559 ETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILQFLeaqppsKLSSVstSWALGKRHIF 631
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
399-924 1.14e-46

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: 179.24  E-value: 1.14e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  399 ADVFLEAMGNACTLKNNNSSRYGKLFDIEI-DFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSL 477
Cdd:cd14878  118 VNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGL 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  478 KLyRNVEKYELLrNTTAMEE--------DRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVPITNidgTEGC 549
Cdd:cd14878  198 HL-NNLCAHRYL-NQTMREDvstaerslNREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTE---ADSA 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  550 QVSNVYEVQETAQLLNMEAQILINCLTranstnsaqEDVGC---EMDARQ-----AATNRNTLCRTLYSRLFTWLVNKIN 621
Cdd:cd14878  273 FVSDLQLLEQVAGMLQVSTDELASALT---------TDIQYfkgDMIIRRhtiqiAEFYRDLLAKSLYSRLFSFLVNTVN 343
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  622 ESLKSTQREKN-----LALLDFYGFEALDHNSFEQFAINYSAEKIHQnFVFHVL-RSEQELYIREGLEWSRIDYFDNES- 694
Cdd:cd14878  344 CCLQSQDEQKSmqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHH-YINEVLfLQEQTECVQEGVTMETAYSPGNQTg 422
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  695 -ICELIDKPSyGILSLINE---------PHLNSNDALLLRVQQCCA---------GHPNFMTTGSnsmCFQIRHYASVVN 755
Cdd:cd14878  423 vLDFFFQKPS-GFLSLLDEesqmiwsvePNLPKKLQSLLESSNTNAvyspmkdgnGNVALKDQGT---AFTVMHYAGRVM 498
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  756 YSIHRFLEKNSDMLPKYISAAFYQSKLSLVQSLFpegnprrqvTKKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNE 835
Cdd:cd14878  499 YEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLF---------QSKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNN 569
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  836 GKQPHQFDMALVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNSLTWPHFHGGSQVEGIALIIRNLPLPSaeFT 915
Cdd:cd14878  570 SKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLGEKKKQSAEERCRLVLQQCKLQG--WQ 647

                 ....*....
gi 78706810  916 IGTKNVFVR 924
Cdd:cd14878  648 MGVRKVFLK 656
MYSc_Myo26 cd14887
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...
382-924 4.71e-46

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: 178.30  E-value: 4.71e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  382 HRRHKSPTQRMRECVTCADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHI 461
Cdd:cd14887  110 DRRHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHI 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  462 FYQL-LLGADLQLLKSLKLYRNVEKYELLRNTTAMeedrmnfhytkRSLDVLGLSCEEsnsIFRVIAVVLKLGNFIFVPI 540
Cdd:cd14887  190 FYALcNAAVAAATQKSSAGEGDPESTDLRRITAAM-----------KTVGIGGGEQAD---IFKLLAAILHLGNVEFTTD 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  541 TN-------------IDGTEGC-QVSNVYEVQETAQLLNMEAQILINCLTRANSTNSAQEDVGCEM-------------- 592
Cdd:cd14887  256 QEpetskkrkltsvsVGCEETAaDRSHSSEVKCLSSGLKVTEASRKHLKTVARLLGLPPGVEGEEMlrlalvsrsvretr 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  593 ---DARQAATNRNTLCRTLYSRLFTWLVNKINESL---------------KSTQREKNLALLDFYGFEALDH---NSFEQ 651
Cdd:cd14887  336 sffDLDGAAAARDAACKNLYSRAFDAVVARINAGLqrsakpsesdsdedtPSTTGTQTIGILDLFGFEDLRNhskNRLEQ 415
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  652 FAINYSAEKIHQNFVFHVLRSEQELYIREGLEWSRIDYFDN-------------ESICELIDKPS--------------- 703
Cdd:cd14887  416 LCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAFPfsfplastltsspSSTSPFSPTPSfrsssafatspslps 495
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  704 -YGILS---LINEPHLNSNDALLLRVQQCCAGHPNFMTTGSNS-------MCFQIRHYASVVNYSIHRFLEKNSDMLPKY 772
Cdd:cd14887  496 sLSSLSsslSSSPPVWEGRDNSDLFYEKLNKNIINSAKYKNITpalsrenLEFTVSHFACDVTYDARDFCRANREATSDE 575
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  773 ISAAFYQSKLSLVQSLFPEGNPRRQVTKKPSTLSSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVR 852
Cdd:cd14887  576 LERLFLACSTYTRLVGSKKNSGVRAISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLR 655
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78706810  853 YMSLMPLVHLCRTGHCYHLLHVKFFHRY--KLLNSLTwphfHGGSQVEGIALIIRNLPLPSAEFTIGTKNVFVR 924
Cdd:cd14887  656 CSGMSDLLRVMADGFPCRLPYVELWRRYetKLPMALR----EALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
MYSc_Myo44 cd14905
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...
387-883 7.99e-46

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: 176.82  E-value: 7.99e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  387 SPTQRMRECVTCADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLL 466
Cdd:cd14905  102 SRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFL 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  467 LGADLQLLKSLKLyRNVEKYELLRNTTAME----EDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVpitn 542
Cdd:cd14905  182 KGITDEEKAAYQL-GDINSYHYLNQGGSISvesiDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFF---- 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  543 idgtegcQVSNVYEVQETAQLLNMEAQILINCLTRANSTNSAQEdvgceMDARQAATNRNTLCRTLYSRLFTWLVNKINE 622
Cdd:cd14905  257 -------QKNGKTEVKDRTLIESLSHNITFDSTKLENILISDRS-----MPVNEAVENRDSLARSLYSALFHWIIDFLNS 324
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  623 SLKSTQREKNLALLDFYGFEALDHNSFEQFAINYSAEKIHQNFVFHVLRSEQELYIREGLEW-SRIDYFDNESICELIDK 701
Cdd:cd14905  325 KLKPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQTERIPWmTPISFKDNEESVEMMEK 404
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  702 psygILSLINE--PHLNSNDALLL-RVQQCCAGHPNFmttGSNSMCFQIRHYASVVNYSIHRFLEKNSD----------- 767
Cdd:cd14905  405 ----IINLLDQesKNINSSDQIFLeKLQNFLSRHHLF---GKKPNKFGIEHYFGQFYYDVRGFIIKNRDeilqrtnvlhk 477
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  768 -MLPKY---------ISAAFYQ-------------SKLSLVQSLFPEGNPRRQVTKKPSTLS-----------------S 807
Cdd:cd14905  478 nSITKYlfsrdgvfnINATVAElnqmfdakntakkSPLSIVKVLLSCGSNNPNNVNNPNNNSgggggggnsgggsgsggS 557
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78706810  808 NIRTQLQTLLAIVKHRRS-HYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLL 883
Cdd:cd14905  558 TYTTYSSTNKAINNSNCDfHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFF 634
MYSc_Myo32 cd14893
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...
403-881 8.14e-42

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: 165.53  E-value: 8.14e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADL--QLLKSLKLY 480
Cdd:cd14893  141 LEAFGNAATRQNRNSSRFAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdpTLRDSLEMN 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  481 RNVEKYELLRNttaMEEDRMNFHYTKR-------SLDVLGLSCEESNSIFRVIAVVLKLGNFIFVP------------IT 541
Cdd:cd14893  221 KCVNEFVMLKQ---ADPLATNFALDARdyrdlmsSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPdpeggksvgganST 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  542 NIDGTEGCQVSNVYEVQETAQLLNMEAQILIN------CLTRANSTNSAQEDVGCEMDARQAatnRNTLCRTLYSRLFTW 615
Cdd:cd14893  298 TVSDAQSCALKDPAQILLAAKLLEVEPVVLDNyfrtrqFFSKDGNKTVSSLKVVTVHQARKA---RDTFVRSLYESLFNF 374
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  616 LVNKIN----------ESLKSTQREKNLALLDFYGFEALD--HNSFEQFAINYSAEKIHQNFV-------FHVLRSEQEL 676
Cdd:cd14893  375 LVETLNgilggifdryEKSNIVINSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVqntlainFSFLEDESQQ 454
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  677 YIREGLEWSRIDYFDNESIC-ELIDKPSYGILSLINE------PHLNSNDALLLRVQQCCAG--HPNFMTTGSNS----- 742
Cdd:cd14893  455 VENRLTVNSNVDITSEQEKClQLFEDKPFGIFDLLTEnckvrlPNDEDFVNKLFSGNEAVGGlsRPNMGADTTNEylaps 534
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  743 ----MCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLSLVQSL--------------FPEGNPRRQVTKKPST 804
Cdd:cd14893  535 kdwrLLFIVQHHCGKVTYNGKGLSSKNMLSISSTCAAIMQSSKNAVLHAVgaaqmaaassekaaKQTEERGSTSSKFRKS 614
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  805 LSS-------------NIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLVHLCRTGHCYHL 871
Cdd:cd14893  615 ASSaresknitdsaatDVYNQADALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHL 694
                        570
                 ....*....|
gi 78706810  872 LHVKFFHRYK 881
Cdd:cd14893  695 TYGHFFRRYK 704
MYSc_Myo23 cd14884
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ...
389-882 1.71e-41

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: 163.92  E-value: 1.71e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  389 TQRMRECVTCADVfLEAMGNACTLKNNNSSRYGKLFDIEID---------FKGDPMGVHITHYMLEKTRITDPIIGERNF 459
Cdd:cd14884  115 TERIDKLIYINNI-LESMSNATTIKNNNSSRCGRINLLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNF 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  460 HIFYQLLLGADLQLLKSLKLYRNVEKYELLRNTTAMEE-----------------------DRMNFHYTKRSLDVLGLSC 516
Cdd:cd14884  194 HVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDESHQKrsvkgtlrlgsdsldpseeekakDEKNFVALLHGLHYIKYDE 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  517 EESNSIFRVIAVVLKLGNfifvpitnidgtegcqvsnvYEVQETAQLLNMEAQILINCLtRANSTNSAQEDVGCEMDARQ 596
Cdd:cd14884  274 RQINEFFDIIAGILHLGN--------------------RAYKAAAECLQIEEEDLENVI-KYKNIRVSHEVIRTERRKEN 332
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  597 AATNRNTLCRTLYSRLFTWLVNKINESLKSTQREKN-------------LALLDFYGFEALDHNSFEQFAINYSAEKIHQ 663
Cdd:cd14884  333 ATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdnediysineaiISILDIYGFEELSGNDFDQLCINLANEKLNN 412
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  664 NFVFHVLRSEQELYIREGLEWSRIDYFDNESICELIDKPSYG---ILSLINEPHLNS-----NDALLLRVQQCCAG---- 731
Cdd:cd14884  413 YYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAKIFRRlddITKLKNQGQKKTddhffRYLLNNERQQQLEGkvsy 492
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  732 -----HPNFMTTGSNSM---CFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLSLVQSLFPEGNPRR--QVTKK 801
Cdd:cd14884  493 gfvlnHDADGTAKKQNIkknIFFIRHYAGLVTYRINNWIDKNSDKIETSIETLISCSSNRFLREANNGGNKGNflSVSKK 572
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  802 PSTLSSNIRTQLQTLlaivkhrRSHYVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLVhlcrtghcyHLLHVKFFHRYK 881
Cdd:cd14884  573 YIKELDNLFTQLQST-------DMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMI---------KILNRGLSHKIP 636

                 .
gi 78706810  882 L 882
Cdd:cd14884  637 K 637
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
3-123 6.72e-35

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: 143.45  E-value: 6.72e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810       3 QEIGTWDSVLLENLSEDSFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAY 82
Cdd:smart00242    4 KFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIADNAY 83
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 78706810      83 QSLKDQSEDQCVLLTGESGAGKTETFKMIVNFLTHIQDRSH 123
Cdd:smart00242   84 RNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNT 124
MYSc_Myo21 cd14882
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...
402-883 1.64e-32

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: 135.64  E-value: 1.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  402 FLEAMGNACTLKNNNSSRygKLFDIEIDF--KGDPMGVHITHYMLEKTRITDPIIGERNFHIFY------------QLLL 467
Cdd:cd14882  117 AILALVNAGTPLNADSTR--CILQYQLTFgsTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYyfydfieaqnrlKEYN 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  468 GADLQLLKSLKLYRNVEKYELLRNTTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNFIFVpitniDGTE 547
Cdd:cd14882  195 LKAGRNYRYLRIPPEVPPSKLKYRRDDPEGNVERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFR-----QNGG 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  548 GCQVSNVYEVQETAQLLNMEAQ----ILIN-CLTRANSTNSAQEDvgCEmDARQAatnRNTLCRTLYSRLFTWLVNKINE 622
Cdd:cd14882  270 YAELENTEIASRVAELLRLDEKkfmwALTNyCLIKGGSAERRKHT--TE-EARDA---RDVLASTLYSRLVDWIINRINM 343
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  623 SL---KSTQREKN-LALLDFYGFEALDHNSFEQFAINYSAEKIH-----QNFVFHVLrsEQElyiREGLEWSRIDYFDN- 692
Cdd:cd14882  344 KMsfpRAVFGDKYsISIHDMFGFECFHRNRLEQLMVNTLNEQMQyhynqRIFISEML--EME---EEDIPTINLRFYDNk 418
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  693 ESICELIDKPSyGILSLINEPHLNSNDA--LLLRVQqccAGHPNFMTTGSNSMcFQIRHYASVVNYSIHRFLEKNSDMLP 770
Cdd:cd14882  419 TAVDQLMTKPD-GLFYIIDDASRSCQDQnyIMDRIK---EKHSQFVKKHSAHE-FSVAHYTGRIIYDAREFADKNRDFVP 493
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  771 KYISAAFYQSKLSLVQSLFPEGNprrqvTKKPSTLSSNIR-TQLQTL--LAI-VKHRRSHYVFCIKPNEGKQPHQFDMAL 846
Cdd:cd14882  494 PEMIETMRSSLDESVKLMFTNSQ-----VRNMRTLAATFRaTSLELLkmLSIgANSGGTHFVRCIRSDLEYKPRGFHSEV 568
                        490       500       510
                 ....*....|....*....|....*....|....*..
gi 78706810  847 VQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLL 883
Cdd:cd14882  569 VRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFL 605
Myosin_TH1 pfam06017
Unconventional myosin tail, actin- and lipid-binding; Unconventional myosins, ie those that ...
1092-1288 7.17e-32

Unconventional myosin tail, actin- and lipid-binding; Unconventional myosins, ie those that are not found in muscle, have the common, classical-type head domain, sometimes a neck with the IQ calmodulin-binding motifs, and then non-standard tails. These tails determine the subcellular localization of the unconventional myosins and also help determine their individual functions. The family carries several different unconventional myosins, eg. Myo1f is expressed mainly in immune cells as well as in the inner ear where it can be associated with deafness, Myo1d has a lipid-binding module in their tail and is implicated in endosome vesicle recycling in epithelial cells. Myo1a, b, c and g from various eukaryotes are also found in this family.


Pssm-ID: 461801  Cd Length: 196  Bit Score: 123.48  E-value: 7.17e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   1092 KVTASIIFKDRKASYGRSVGHPFVGDYVRLRHN-----QQWKKICAETNDQYVVFADIINKIARSSgKFVP--------- 1157
Cdd:pfam06017    1 KDYASDLLKGRKERRRFSLLRRFMGDYLGLENNfsgpgPKLRKAVGIGGDEKVLFSDRVSKFNRSS-KPSPrililtdka 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   1158 ---ILLVLSTssllllDQRTLQIKYRVPASEIYRMSLSPYLDDIAVFHVKASEfgrkKGDFVFQTGHVIEIVTKMFLVIQ 1234
Cdd:pfam06017   80 vylIDQKKLK------NGLQYVLKRRIPLSDITGVSVSPLQDDWVVLHLGSPQ----KGDLLLECDFKTELVTHLSKAYK 149
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 78706810   1235 NATGKPPEIHISTEFEANFG---QQTVIFSfkyggmsdlaQGPPKVTRKANRMEIIV 1288
Cdd:pfam06017  150 KKTNRKLNVKIGDTIEYRKKkgkIRTVKFV----------KDEPKGKDSYKSGTVSV 196
Myosin_head pfam00063
Myosin head (motor domain);
9-122 2.14e-31

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 132.40  E-value: 2.14e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810      9 DSVLLENLSEDSFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQ 88
Cdd:pfam00063    3 DMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQD 82
                           90       100       110
                   ....*....|....*....|....*....|....
gi 78706810     89 SEDQCVLLTGESGAGKTETFKMIVNFLTHIQDRS 122
Cdd:pfam00063   83 KENQSILISGESGAGKTENTKKIMQYLASVSGSG 116
MYSc_Myo18 cd01386
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...
403-924 4.55e-31

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: 131.28  E-value: 4.55e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGADLQLLKSLKLYRN 482
Cdd:cd01386  120 LEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQL 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  483 VEKYELLRNTTAMEEDR----MNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNfifvpitnidgTEGCQVSNVYEVQ 558
Cdd:cd01386  200 AESNSFGIVPLQKPEDKqkaaAAFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGA-----------AGATKAASAGRKQ 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  559 ----ETAQllnmEAQILINC----LTRA------------NSTNSAQEDVGCEMDARQAAT---NRNTLCRTLYSRLFTW 615
Cdd:cd01386  269 farpEWAQ----RAAYLLGCtleeLSSAifkhhlsggpqqSTTSSGQESPARSSSGGPKLTgveALEGFAAGLYSELFAA 344
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  616 LVNKINESLKSTQREK-NLALLDFYGFEALDHN------SFEQFAINYSAEKIHQnfVFH--VLRSEQELYIREGLEwsr 686
Cdd:cd01386  345 VVSLINRSLSSSHHSTsSITIVDTPGFQNPAHSgsqrgaTFEDLCHNYAQERLQL--LFHerTFVAPLERYKQENVE--- 419
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  687 IDYFDNES----ICELIDKPSY--------------GILSLINEPHL--NSNDALLL-RV------QQCCAGHPnFMTTG 739
Cdd:cd01386  420 VDFDLPELspgaLVALIDQAPQqalvrsdlrdedrrGLLWLLDEEALypGSSDDTFLeRLfshygdKEGGKGHS-LLRRS 498
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  740 SNSMCFQIRHY--ASVVNYSIHRFLEKNSDMLPkyisaafYQSKLSLVQSlfpEGNPRRQVTKKpsTLSSNIRTQLQTLL 817
Cdd:cd01386  499 EGPLQFVLGHLlgTNPVEYDVSGWLKAAKENPS-------AQNATQLLQE---SQKETAAVKRK--SPCLQIKFQVDALI 566
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  818 AIVKHRRSHYVFCIKPNEGKQPH------------QFDMALVQHQVRYMSLMPLVHLCRTGHCYHLLHVKFFHRYKLLNs 885
Cdd:cd01386  567 DTLRRTGLHFVHCLLPQHNAGKDerstsspaagdeLLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLA- 645
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*..
gi 78706810  886 ltwPHFHGGSQVEGIAL--------IIRNLPLPSAEFTIGTKNVFVR 924
Cdd:cd01386  646 ---PPLTKKLGLNSEVAderkaveeLLEELDLEKSSYRIGLSQVFFR 689
COG5022 COG5022
Myosin heavy chain [General function prediction only];
3-123 7.21e-30

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 129.43  E-value: 7.21e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810    3 QEIGTWDSVLLENLSEDSFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAY 82
Cdd:COG5022   64 KFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAY 143
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 78706810   83 QSLKDQSEDQCVLLTGESGAGKTETFKMIVNFLTHIQDRSH 123
Cdd:COG5022  144 RNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSST 184
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
19-118 6.40e-29

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: 124.19  E-value: 6.40e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   19 DSFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTG 98
Cdd:cd01378    1 EAINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
                         90       100
                 ....*....|....*....|
gi 78706810   99 ESGAGKTETFKMIVNFLTHI 118
Cdd:cd01378   81 ESGAGKTEASKRIMQYIAAV 100
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
19-118 3.10e-28

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


Pssm-ID: 276950 [Multi-domain]  Cd Length: 633  Bit Score: 121.93  E-value: 3.10e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   19 DSFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGI-FQLPPHIYGLTNLAYQSLKDQSEDQCVLLT 97
Cdd:cd00124    1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
                         90       100
                 ....*....|....*....|.
gi 78706810   98 GESGAGKTETFKMIVNFLTHI 118
Cdd:cd00124   81 GESGAGKTETTKLVLKYLAAL 101
MYSc_Myo24B cd14938
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
391-856 5.90e-28

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: 121.87  E-value: 5.90e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  391 RMRECVTCADVFLEAMGNACTLKNNNSSRYGKLFDIEIDfKGDPMGVHITHYMLEKTRITDPIIGERNFHIFYQLLLGAD 470
Cdd:cd14938  131 NMSEMLKHVNVVMEAFGNAKTVKNNNSSRFSKFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSS 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  471 LQLLKSLKLyRNVEKYELLRNTTAME---EDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVLKLGNF----IFVPITNI 543
Cdd:cd14938  210 DKFKKMYFL-KNIENYSMLNNEKGFEkfsDYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkAFRKKSLL 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  544 DGTEGCQVSNVYEV-------QETAQLLNMEAQILINC---------LTRANSTNSAQED-----VGCEMDARQAATNrn 602
Cdd:cd14938  289 MGKNQCGQNINYETilselenSEDIGLDENVKNLLLACkllsfdietFVKYFTTNYIFNDsilikVHNETKIQKKLEN-- 366
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  603 tLCRTLYSRLFTWLVNKINESLKSTQREKN----LALLDFYGFEALDHNSFEQFAINYSAE---KIHQNFVFhvlRSEQE 675
Cdd:cd14938  367 -FIKTCYEELFNWIIYKINEKCTQLQNINIntnyINVLDMAYFENSKDNSLEQLLINTTNEeiiKIKNDCLY---KKRVL 442
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  676 LYIREGLEWS-RIDYFDNESICELIDKPSYGIL-SLINEPHL-----NSN-DALLLRVQQCCAGHPNFMTTGSNSMCFQI 747
Cdd:cd14938  443 SYNEDGIFCEyNSENIDNEPLYNLLVGPTEGSLfSLLENVSTktifdKSNlHSSIIRKFSRNSKYIKKDDITGNKKTFVI 522
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  748 RHYASVVNYSIHRFLEKNSDMLPK-YI-----SAAFYQSKLSLVQSLFPEGNP----------------RRQVTKKPSTL 805
Cdd:cd14938  523 THSCGDIIYNAENFVEKNIDILTNrFIdmvkqSENEYMRQFCMFYNYDNSGNIveekrrysiqsalklfKRRYDTKNQMA 602
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 78706810  806 SSNIRTQLQTLLAIVKHRRSHYVFCIKPNEGKQP-HQFDMALVQHQVRYMSL 856
Cdd:cd14938  603 VSLLRNNLTELEKLQETTFCHFIVCMKPNESKRElCSFDANIVLRQVRNFSI 654
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
24-118 2.27e-26

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: 116.20  E-value: 2.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   24 NIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGESGAG 103
Cdd:cd01381    6 NLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGESGAG 85
                         90
                 ....*....|....*
gi 78706810  104 KTETFKMIVNFLTHI 118
Cdd:cd01381   86 KTESTKLILQYLAAI 100
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
24-116 5.54e-25

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: 112.03  E-value: 5.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   24 NIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGESGAG 103
Cdd:cd14883    6 NLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGESGAG 85
                         90
                 ....*....|...
gi 78706810  104 KTETFKMIVNFLT 116
Cdd:cd14883   86 KTETTKLILQYLC 98
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
20-122 6.17e-25

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: 111.81  E-value: 6.17e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISE-HSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTG 98
Cdd:cd14873    2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAGlYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
                         90       100
                 ....*....|....*....|....
gi 78706810   99 ESGAGKTETFKMIVNFLTHIQDRS 122
Cdd:cd14873   82 ESGAGKTESTKLILKFLSVISQQS 105
MYSc_Myo33 cd14894
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...
399-864 8.33e-24

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: 109.06  E-value: 8.33e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  399 ADVFLEAMGNACTLKNNNSSRYGKLFDIEIDFKGDPM-----GVHITHYMLEKTRITDPI------IGERNFHIFYQLLL 467
Cdd:cd14894  252 SNIVLEAFGHATTSMNLNSSRFGKMTTLQVAFGLHPWefqicGCHISPFLLEKSRVTSERgresgdQNELNFHILYAMVA 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  468 GADL-----QLLKSLKL---------YRNVEKYEL---LRNTTAMEEDRMNFHYTKRSLDVLGLSCEESNSIFRVIAVVL 530
Cdd:cd14894  332 GVNAfpfmrLLAKELHLdgidcsaltYLGRSDHKLagfVSKEDTWKKDVERWQQVIDGLDELNVSPDEQKTIFKVLSAVL 411
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  531 KLGNfIFVPITNIDGTEGCQVSNVYEV-QETAQLLNMEA--QILINCLTRANSTNSAQEDVGCEMDARQAATNRNTLCRT 607
Cdd:cd14894  412 WLGN-IELDYREVSGKLVMSSTGALNApQKVVELLELGSveKLERMLMTKSVSLQSTSETFEVTLEKGQVNHVRDTLARL 490
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  608 LYSRLFTWLVNKINESLKST---------QREKN---------LALLDFYGFEALDHNSFEQFAINYSAEKIHQnfvfhv 669
Cdd:cd14894  491 LYQLAFNYVVFVMNEATKMSalstdgnkhQMDSNasapeavslLKIVDVFGFEDLTHNSLDQLCINYLSEKLYA------ 564
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  670 lRSEQELYIREGLEWSRIDYfDNESICELIDKPSYGILSLINE-------PHLNS-----------------NDALLLRV 725
Cdd:cd14894  565 -REEQVIAVAYSSRPHLTAR-DSEKDVLFIYEHPLGVFASLEEltilhqsENMNAqqeekrnklfvrniydrNSSRLPEP 642
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810  726 QQCCAGHPNFMTTGSNSMCFQIRHYASVVNYSIHRFLEKNSDMLPKYISAAFYQSKLSLVQSLFPEGNprrQVTKKPSTL 805
Cdd:cd14894  643 PRVLSNAKRHTPVLLNVLPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESS---QLGWSPNTN 719
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78706810  806 SSNI---RTQLQTLLAIVKHRRSH--------------YVFCIKPNEGKQPHQFDMALVQHQVRYMSLMPLVHLCR 864
Cdd:cd14894  720 RSMLgsaESRLSGTKSFVGQFRSHvnvltsqddknmpfYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICR 795
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
20-117 5.33e-23

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: 105.79  E-value: 5.33e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISE-HSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTG 98
Cdd:cd01382    2 TLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPKlYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSG 81
                         90
                 ....*....|....*....
gi 78706810   99 ESGAGKTETFKMIVNFLTH 117
Cdd:cd01382   82 ESGAGKTESTKYILRYLTE 100
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
20-118 3.21e-22

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: 103.31  E-value: 3.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGE 99
Cdd:cd01377    2 SVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITGE 81
                         90
                 ....*....|....*....
gi 78706810  100 SGAGKTETFKMIVNFLTHI 118
Cdd:cd01377   82 SGAGKTENTKKVIQYLASV 100
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
20-118 4.97e-21

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: 99.33  E-value: 4.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGE 99
Cdd:cd14932    2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
                         90
                 ....*....|....*....
gi 78706810  100 SGAGKTETFKMIVNFLTHI 118
Cdd:cd14932   82 SGAGKTENTKKVIQYLAYV 100
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
16-118 6.97e-21

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: 98.78  E-value: 6.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   16 LSEDSFINNIHQRYKRDHIYTYIGTSV-VALNPYHHISEHSLDNVRNYGDK-------GIFQLPPHIYGLTNLAYQSLKD 87
Cdd:cd14879    1 PSDDAITSHLASRFRSDLPYTRLGSSAlVAVNPYKYLSSNSDASLGEYGSEyydttsgSKEPLPPHAYDLAARAYLRMRR 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 78706810   88 QSEDQCVLLTGESGAGKTETFKMIVNFLTHI 118
Cdd:cd14879   81 RSEDQAVVFLGETGSGKSESRRLLLRQLLRL 111
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
19-116 1.14e-20

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: 98.12  E-value: 1.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   19 DSFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTG 98
Cdd:cd01379    1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
                         90
                 ....*....|....*...
gi 78706810   99 ESGAGKTETFKMIVNFLT 116
Cdd:cd01379   81 ESGAGKTESANLLVQQLT 98
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
22-141 1.73e-20

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: 97.79  E-value: 1.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   22 INNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNV-RNYGDKGI--------FQLPPHIYGLTNLAYQSLKDQSEDQ 92
Cdd:cd14907    4 LINLKKRYQQDKIFTYVGPTLIVMNPYKQIDNLFSEEVmQMYKEQIIqngeyfdiKKEPPHIYAIAALAFKQLFENNKKQ 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 78706810   93 CVLLTGESGAGKTETFKMIVNFLTHIQDRSHCPPTPNVLRKQSSTSSAS 141
Cdd:cd14907   84 AIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSSIRATSKS 132
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
20-115 6.44e-20

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: 95.98  E-value: 6.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGE 99
Cdd:cd01387    2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
                         90
                 ....*....|....*.
gi 78706810  100 SGAGKTETFKMIVNFL 115
Cdd:cd01387   82 SGSGKTEATKLIMQYL 97
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
20-115 1.04e-19

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: 95.23  E-value: 1.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGE 99
Cdd:cd14872    2 MIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISGE 81
                         90
                 ....*....|....*.
gi 78706810  100 SGAGKTETFKMIVNFL 115
Cdd:cd14872   82 SGAGKTEATKQCLSFF 97
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
20-123 1.68e-19

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: 94.69  E-value: 1.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGE 99
Cdd:cd14920    2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
                         90       100
                 ....*....|....*....|....
gi 78706810  100 SGAGKTETFKMIVNFLTHIQDrSH 123
Cdd:cd14920   82 SGAGKTENTKKVIQYLAHVAS-SH 104
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
22-118 4.81e-19

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: 92.83  E-value: 4.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   22 INNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGI-FQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGES 100
Cdd:cd14897    4 VQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVrSQRPPHLFWIADQAYRRLLETGRNQCILVSGES 83
                         90
                 ....*....|....*...
gi 78706810  101 GAGKTETFKMIVNFLTHI 118
Cdd:cd14897   84 GAGKTESTKYMIKHLMKL 101
MYSc_Myh19 cd15896
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...
20-134 5.91e-19

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: 92.82  E-value: 5.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGE 99
Cdd:cd15896    2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 78706810  100 SGAGKTETFKMIVNFLTHI-------QDRSHCPPTPNVLRKQ 134
Cdd:cd15896   82 SGAGKTENTKKVIQYLAHVasshktkKDQNSLALSHGELEKQ 123
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
20-118 8.42e-19

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: 92.15  E-value: 8.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISE-HSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKD----QSEDQCV 94
Cdd:cd14890    2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPDlYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQSI 81
                         90       100
                 ....*....|....*....|....
gi 78706810   95 LLTGESGAGKTETFKMIVNFLTHI 118
Cdd:cd14890   82 IISGESGAGKTEATKIIMQYLARI 105
MYSc_Myh9 cd14919
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...
20-118 1.17e-18

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: 91.69  E-value: 1.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGE 99
Cdd:cd14919    2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
                         90
                 ....*....|....*....
gi 78706810  100 SGAGKTETFKMIVNFLTHI 118
Cdd:cd14919   82 SGAGKTENTKKVIQYLAHV 100
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
20-115 1.56e-18

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: 91.58  E-value: 1.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRN-YGDKG-IFQLPPHIYGLTNLAYQSLKDQSEDQCVLLT 97
Cdd:cd14906    2 IILNNLGKRYKSDSIYTYIGNVLISINPYKDISSIYSNLILNeYKDINqNKSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
                         90
                 ....*....|....*...
gi 78706810   98 GESGAGKTETFKMIVNFL 115
Cdd:cd14906   82 GESGSGKTEASKTILQYL 99
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
24-122 1.87e-18

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: 91.20  E-value: 1.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   24 NIHQRYKRDHIYTYIGTSVVALNPY----HHISEHSLDNvrnYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGE 99
Cdd:cd01384    6 NLKVRYELDEIYTYTGNILIAVNPFkrlpHLYDAHMMEQ---YKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVSGE 82
                         90       100
                 ....*....|....*....|...
gi 78706810  100 SGAGKTETFKMIVNFLTHIQDRS 122
Cdd:cd01384   83 SGAGKTETTKMLMQYLAYMGGRA 105
MYSc_Myh14_mammals cd14930
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...
20-134 5.53e-18

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: 89.77  E-value: 5.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGE 99
Cdd:cd14930    2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 78706810  100 SGAGKTETFKMIVNFLTHIQDRSHC---PPTPNVLRKQ 134
Cdd:cd14930   82 SGAGKTENTKKVIQYLAHVASSPKGrkePGVPGELERQ 119
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
20-118 2.14e-17

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: 87.73  E-value: 2.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGE 99
Cdd:cd14911    2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
                         90
                 ....*....|....*....
gi 78706810  100 SGAGKTETFKMIVNFLTHI 118
Cdd:cd14911   82 SGAGKTENTKKVIQFLAYV 100
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
24-118 3.06e-17

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: 87.14  E-value: 3.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   24 NIHQRYKRDHIYTYIGTSVVALNPYHHISE-HSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGESGA 102
Cdd:cd14903    6 NVKKRFLRKLPYTYTGDICIAVNPYQWLPElYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVSGESGA 85
                         90
                 ....*....|....*.
gi 78706810  103 GKTETFKMIVNFLTHI 118
Cdd:cd14903   86 GKTETTKILMNHLATI 101
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
12-117 3.44e-17

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: 87.05  E-value: 3.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   12 LLENLSedsfinnihQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSED 91
Cdd:cd01385    3 LLENLR---------ARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKN 73
                         90       100
                 ....*....|....*....|....*.
gi 78706810   92 QCVLLTGESGAGKTETfkmiVNFLTH 117
Cdd:cd01385   74 QCIVISGESGSGKTES----TNFLLH 95
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
20-118 5.87e-17

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: 86.15  E-value: 5.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHIsehslDNVrnYGD--------KGIFQLPPHIYGLTNLAYQSLKDQSED 91
Cdd:cd14904    2 SILFNLKKRFAASKPYTYTNDIVIALNPYKWI-----DNL--YGDhlheqylkKPRDKLQPHVYATSTAAYKHMLTNEMN 74
                         90       100
                 ....*....|....*....|....*..
gi 78706810   92 QCVLLTGESGAGKTETFKMIVNFLTHI 118
Cdd:cd14904   75 QSILVSGESGAGKTETTKIVMNHLASV 101
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
20-115 9.45e-17

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: 85.84  E-value: 9.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGE 99
Cdd:cd14921    2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
                         90
                 ....*....|....*.
gi 78706810  100 SGAGKTETFKMIVNFL 115
Cdd:cd14921   82 SGAGKTENTKKVIQYL 97
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
20-116 1.12e-16

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: 85.51  E-value: 1.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGE 99
Cdd:cd14888    2 SILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPGLYSDEMLLKFIQPSISKSPHVFSTASSAYQGMCNNKKSQTILISGE 81
                         90
                 ....*....|....*..
gi 78706810  100 SGAGKTETFKMIVNFLT 116
Cdd:cd14888   82 SGAGKTESTKYVMKFLA 98
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
20-122 4.29e-16

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: 83.68  E-value: 4.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGE 99
Cdd:cd14896    2 SVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSGH 81
                         90       100
                 ....*....|....*....|...
gi 78706810  100 SGAGKTETFKMIVNFLTHIQDRS 122
Cdd:cd14896   82 SGSGKTEAAKKIVQFLSSLYQDQ 104
MYSc_Myo44 cd14905
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...
19-115 7.61e-16

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: 82.83  E-value: 7.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   19 DSFINNIHQRYKRDHIYTYIGTSVVALNPYHHIS-EHSLDNVRNYGDKGifQLPPHIYGLTNLAYQSLKDQSEDQCVLLT 97
Cdd:cd14905    1 DTLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRR--GLPPHLFALAAKAISDMQDFRRDQLIFIG 78
                         90
                 ....*....|....*...
gi 78706810   98 GESGAGKTETFKMIVNFL 115
Cdd:cd14905   79 GESGSGKSENTKIIIQYL 96
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
11-112 9.14e-16

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: 82.65  E-value: 9.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   11 VLLENLSedsfinnihQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQS----LK 86
Cdd:cd14889    2 VLLEVLK---------VRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSmlgrLA 72
                         90       100
                 ....*....|....*....|....*.
gi 78706810   87 DQSEDQCVLLTGESGAGKTETFKMIV 112
Cdd:cd14889   73 RGPKNQCIVISGESGAGKTESTKLLL 98
MYSc_Myh16 cd14934
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...
20-118 1.56e-15

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: 81.61  E-value: 1.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGE 99
Cdd:cd14934    2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
                         90
                 ....*....|....*....
gi 78706810  100 SGAGKTETFKMIVNFLTHI 118
Cdd:cd14934   82 SGAGKTENTKKVIQYFANI 100
MYSc_Myo26 cd14887
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...
22-123 1.80e-15

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: 81.62  E-value: 1.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   22 INNIHQRY--------KRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQC 93
Cdd:cd14887    4 LENLYQRYnkayinkeNRNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRRSQS 83
                         90       100       110
                 ....*....|....*....|....*....|
gi 78706810   94 VLLTGESGAGKTETFKMIVNFLTHIQDRSH 123
Cdd:cd14887   84 ILISGESGAGKTETSKHVLTYLAAVSDRRH 113
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
20-115 2.06e-15

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: 81.21  E-value: 2.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIfqLPPHIYGLTNLAYQSLKDQSEDQCVLLTGE 99
Cdd:cd01383    2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKLL--DSPHVYAVADTAYREMMRDEINQSIIISGE 79
                         90
                 ....*....|....*.
gi 78706810  100 SGAGKTETFKMIVNFL 115
Cdd:cd01383   80 SGAGKTETAKIAMQYL 95
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
25-129 4.17e-15

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: 80.32  E-value: 4.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   25 IHQRYKRDHIYTYIGTSVVALNPYHHISE-HSLDNVRNY--------GDKGIFQLPPHIYGLTNLAYQSL-KDQSEDQCV 94
Cdd:cd14902    7 LSERFEHDQIYTSIGDILVALNPLKPLPDlYSESQLNAYkasmtstsPVSQLSELPPHVFAIGGKAFGGLlKPERRNQSI 86
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 78706810   95 LLTGESGAGKTETFKMIVNFLTHIQDRSHCPPTPN 129
Cdd:cd14902   87 LVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEG 121
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
23-116 4.99e-15

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: 79.89  E-value: 4.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   23 NNIHQRY-KRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGESG 101
Cdd:cd01380    5 HNLKVRFcQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSGESG 84
                         90
                 ....*....|....*
gi 78706810  102 AGKTETFKMIVNFLT 116
Cdd:cd01380   85 AGKTVSAKYAMRYFA 99
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
20-116 1.19e-14

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: 78.68  E-value: 1.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHI---SEHSLDNVRNYGDK---GIFQLPPHIYGLTNLAYQSL----KDQS 89
Cdd:cd14901    2 SILHVLRRRFAHGLIYTSTGAILVAINPFRRLplyDDETKEAYYEHGERraaGERKLPPHVYAVADKAFRAMlfasRGQK 81
                         90       100
                 ....*....|....*....|....*..
gi 78706810   90 EDQCVLLTGESGAGKTETFKMIVNFLT 116
Cdd:cd14901   82 CDQSILVSGESGAGKTETTKIIMNYLA 108
MYSc_Myh1_insects_crustaceans cd14909
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
20-116 1.20e-14

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: 78.73  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGE 99
Cdd:cd14909    2 SVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGE 81
                         90
                 ....*....|....*...
gi 78706810  100 SGAGKTE-TFKMIVNFLT 116
Cdd:cd14909   82 SGAGKTEnTKKVIAYFAT 99
MYSc_Myh7b cd14927
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...
20-115 2.49e-14

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: 77.69  E-value: 2.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGE 99
Cdd:cd14927    2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
                         90
                 ....*....|....*.
gi 78706810  100 SGAGKTETFKMIVNFL 115
Cdd:cd14927   82 SGAGKTVNTKRVIQYF 97
MYSc_Myh3 cd14913
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...
24-118 4.06e-14

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: 77.01  E-value: 4.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   24 NIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGESGAG 103
Cdd:cd14913    6 NLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 85
                         90
                 ....*....|....*
gi 78706810  104 KTETFKMIVNFLTHI 118
Cdd:cd14913   86 KTVNTKRVIQYFATI 100
MYSc_Myh15_mammals cd14929
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...
20-118 5.08e-14

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: 76.94  E-value: 5.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGE 99
Cdd:cd14929    2 SVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 81
                         90
                 ....*....|....*....
gi 78706810  100 SGAGKTETFKMIVNFLTHI 118
Cdd:cd14929   82 SGAGKTVNTKHIIQYFATI 100
MYSc_Myo23 cd14884
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ...
20-122 7.75e-14

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: 76.48  E-value: 7.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISE-HSLDNVRNYGDK-------GIFQLPPHIYGLTNLAYQSLKDQSED 91
Cdd:cd14884    2 NVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKElYDQDVMNVYLHKksnsaasAAPFPKAHIYDIANMAYKNMRGKLKR 81
                         90       100       110
                 ....*....|....*....|....*....|.
gi 78706810   92 QCVLLTGESGAGKTETFKMIVNFLTHIQDRS 122
Cdd:cd14884   82 QTIVVSGHSGSGKTENCKFLFKYFHYIQTDS 112
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
12-142 1.74e-13

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: 75.08  E-value: 1.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   12 LLENLSEDSFINNihQRykrdhIYTYIGTSVVALNPYHHISEhslDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSED 91
Cdd:cd14891    3 ILHNLEERSKLDN--QR-----PYTFMANVLIAVNPLRRLPE---PDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGR 72
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 78706810   92 QC---VLLTGESGAGKTETFKMIVNFLTHiqdRSHCPPTpnvLRKQSSTSSASG 142
Cdd:cd14891   73 MQnqsIVISGESGAGKTETSKIILRFLTT---RAVGGKK---ASGQDIEQSSKK 120
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
20-139 2.16e-13

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: 74.99  E-value: 2.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISehSLDNVRNYGDK--GIFQLPPHIYGLTNLAYQSLK-------DQSE 90
Cdd:cd14895    2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP--GLYDLHKYREEmpGWTALPPHVFSIAEGAYRSLRrrlhepgASKK 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 78706810   91 DQCVLLTGESGAGKTETFKMIVNFLThiQDRSHCPPTPNVLRKQSSTSS 139
Cdd:cd14895   80 NQTILVSGESGAGKTETTKFIMNYLA--ESSKHTTATSSSKRRRAISGS 126
MYSc_Myh7 cd14917
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...
24-128 3.25e-13

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: 74.37  E-value: 3.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   24 NIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGESGAG 103
Cdd:cd14917    6 NLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAG 85
                         90       100
                 ....*....|....*....|....*...
gi 78706810  104 KTETFKMIVNF---LTHIQDRSHCPPTP 128
Cdd:cd14917   86 KTVNTKRVIQYfavIAAIGDRSKKDQTP 113
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
22-115 3.28e-13

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: 74.03  E-value: 3.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   22 INNIHQRYKRDHIYTYIGTSVVALNPYHHISehSLDNVRNYGDKGIFQL-----PPHIYGLTNLAYQSLK----DQSEDQ 92
Cdd:cd14892    4 LDVLRRRYERDAIYTFTADILISINPYKSIP--LLYDVPGFDSQRKEEAtasspPPHVFSIAERAYRAMKgvgkGQGTPQ 81
                         90       100
                 ....*....|....*....|...
gi 78706810   93 CVLLTGESGAGKTETFKMIVNFL 115
Cdd:cd14892   82 SIVVSGESGAGKTEASKYIMKYL 104
MYSc_Myh6 cd14916
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...
24-118 5.07e-13

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: 73.55  E-value: 5.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   24 NIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGESGAG 103
Cdd:cd14916    6 NLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAG 85
                         90
                 ....*....|....*
gi 78706810  104 KTETFKMIVNFLTHI 118
Cdd:cd14916   86 KTVNTKRVIQYFASI 100
MYSc_Myh1_mammals cd14910
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
24-118 5.09e-13

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: 73.61  E-value: 5.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   24 NIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGESGAG 103
Cdd:cd14910    6 NLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 85
                         90
                 ....*....|....*
gi 78706810  104 KTETFKMIVNFLTHI 118
Cdd:cd14910   86 KTVNTKRVIQYFATI 100
MYSc_Myh4 cd14915
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...
24-118 6.65e-13

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: 73.22  E-value: 6.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   24 NIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGESGAG 103
Cdd:cd14915    6 NLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 85
                         90
                 ....*....|....*
gi 78706810  104 KTETFKMIVNFLTHI 118
Cdd:cd14915   86 KTVNTKRVIQYFATI 100
MYSc_Myh2_mammals cd14912
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
24-118 9.86e-13

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: 72.84  E-value: 9.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   24 NIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGESGAG 103
Cdd:cd14912    6 NLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 85
                         90
                 ....*....|....*
gi 78706810  104 KTETFKMIVNFLTHI 118
Cdd:cd14912   86 KTVNTKRVIQYFATI 100
MYSc_Myh8 cd14918
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...
24-118 1.08e-12

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: 72.46  E-value: 1.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   24 NIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGESGAG 103
Cdd:cd14918    6 NLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 85
                         90
                 ....*....|....*
gi 78706810  104 KTETFKMIVNFLTHI 118
Cdd:cd14918   86 KTVNTKRVIQYFATI 100
MYSc_Myh13 cd14923
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...
24-118 1.64e-12

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: 72.02  E-value: 1.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   24 NIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGESGAG 103
Cdd:cd14923    6 NLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGESGAG 85
                         90
                 ....*....|....*
gi 78706810  104 KTETFKMIVNFLTHI 118
Cdd:cd14923   86 KTVNTKRVIQYFATI 100
PTZ00014 PTZ00014
myosin-A; Provisional
27-115 2.83e-12

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 71.21  E-value: 2.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810    27 QRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGD-KGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGESGAGKT 105
Cdd:PTZ00014  118 HRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDaKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKT 197
                          90
                  ....*....|
gi 78706810   106 ETFKMIVNFL 115
Cdd:PTZ00014  198 EATKQIMRYF 207
MYSc_Myo18 cd01386
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...
27-118 3.20e-12

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: 71.19  E-value: 3.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   27 QRYKRDHIYTYIGTSVVALNPYHHISEhsldnvrnYGDKGI--F------QLPPHIYGLTNLAYQSLKDQSEDQCVLLTG 98
Cdd:cd01386    9 QRYGANLIHTYAGPSLIVINPRHPLAV--------YSEKVAkmFkgcrreDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
                         90       100
                 ....*....|....*....|
gi 78706810   99 ESGAGKTETFKMIVNFLTHI 118
Cdd:cd01386   81 RSGSGKTTNCRHILEYLVTA 100
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
19-148 8.04e-12

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: 69.56  E-value: 8.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   19 DSFINNIHQRYKRDHIYTYIGTSVVALNPYHHISE-HSLDNVRNY-----------GDKGIFQLPPHIYGLTNLAYQS-- 84
Cdd:cd14900    1 TTILSALETRFYAQKIYTNTGAILLAVNPFQKLPGlYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAmm 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78706810   85 --LKDQSEDQCVLLTGESGAGKTETFKMIVNFLTHIQDrshcPPTPNVLRKQSSTSSASGLVMHAH 148
Cdd:cd14900   81 lgLNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGD----NNLAASVSMGKSTSGIAAKVLQTN 142
MYSc_Myo25 cd14886
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...
22-122 1.04e-11

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: 69.53  E-value: 1.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   22 INNIHQRYKRDHIYTYIGTSVVALNPYHHIS----EHSLDNVRNYGDKGIF--QLPPHIYGLTNLAYQSLKDQSEDQCVL 95
Cdd:cd14886    4 IDILRDRFAKDKIYTYAGKLLVALNPFKQIRnlygTEVIGRYRQADTSRGFpsDLPPHSYAVAQSALNGLISDGISQSCI 83
                         90       100
                 ....*....|....*....|....*..
gi 78706810   96 LTGESGAGKTETFKMIVNFLTHIQDRS 122
Cdd:cd14886   84 VSGESGAGKTETAKQLMNFFAYGHSTS 110
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
42-118 1.34e-11

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: 64.29  E-value: 1.34e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78706810   42 VVALNPYHHISEHSLDNVRN-YGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGESGAGKTETFKMIVNFLTHI 118
Cdd:cd01363    2 LVRVNPFKELPIYRDSKIIVfYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASV 79
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
20-116 1.54e-11

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: 68.78  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQ---------LPPHIYGLTNLAY-QSLKDQS 89
Cdd:cd14908    2 AILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRQEGLLRsqgiespqaLGPHVFAIADRSYrQMMSEIR 81
                         90       100
                 ....*....|....*....|....*..
gi 78706810   90 EDQCVLLTGESGAGKTETFKMIVNFLT 116
Cdd:cd14908   82 ASQSILISGESGAGKTESTKIVMLYLT 108
MYSc_Myo24A cd14937
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
22-114 1.98e-11

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: 68.50  E-value: 1.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   22 INNIHQRYKRDHIYTYIGTSVVALNPYHHISEhsldNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGESG 101
Cdd:cd14937    4 LNMLALRYKKNYIYTIAEPMLISINPYQVIDV----DINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGESG 79
                         90
                 ....*....|...
gi 78706810  102 AGKTETFKMIVNF 114
Cdd:cd14937   80 SGKTEASKLVIKY 92
MYSc_Myo38 cd14899
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...
20-139 3.86e-11

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: 67.43  E-value: 3.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISE---------HSLDNVRNYGDKGIFQLP--PHIYGLTNLAYQSLKDQ 88
Cdd:cd14899    2 SILNALRLRYERHAIYTHIGDILISINPFQDLPQlygdeilrgYAYDHNSQFGDRVTSTDPrePHLFAVARAAYIDIVQN 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 78706810   89 SEDQCVLLTGESGAGKTETFKMIVNFLThiqdrSHCPPtPNVLRKQSSTSS 139
Cdd:cd14899   82 GRSQSILISGESGAGKTEATKIIMTYFA-----VHCGT-GNNNLTNSESIS 126
MYSc_Myo32 cd14893
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...
28-147 8.15e-11

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: 66.53  E-value: 8.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   28 RYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDK----------GIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLT 97
Cdd:cd14893   10 RYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSreqtplyekdTVNDAPPHVFALAQNALRCMQDAGEDQAVILL 89
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 78706810   98 GESGAGKTETFKMIVNFLTHIQDRSHcpPTPNVLRKQSSTSSASGLVMHA 147
Cdd:cd14893   90 GGMGAGKSEAAKLIVQYLCEIGDETE--PRPDSEGASGVLHPIGQQILHA 137
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
20-116 9.95e-11

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: 65.99  E-value: 9.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNY---GDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLL 96
Cdd:cd14878    2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81
                         90       100
                 ....*....|....*....|
gi 78706810   97 TGESGAGKTETFKMIVNFLT 116
Cdd:cd14878   82 SGERGSGKTEASKQIMKHLT 101
MYSc_Myo14 cd14876
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...
27-115 1.45e-10

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: 65.78  E-value: 1.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   27 QRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGD-KGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTGESGAGKT 105
Cdd:cd14876    9 HRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVSGESGAGKT 88
                         90
                 ....*....|
gi 78706810  106 ETFKMIVNFL 115
Cdd:cd14876   89 EATKQIMRYF 98
MYSc_Myo21 cd14882
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...
19-123 5.05e-09

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: 60.52  E-value: 5.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   19 DSFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYGDKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTG 98
Cdd:cd14882    1 ENILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSG 80
                         90       100
                 ....*....|....*....|....*
gi 78706810   99 ESGAGKTETFKMIVNFLTHIQDRSH 123
Cdd:cd14882   81 ESYSGKTTNARLLIKHLCYLGDGNR 105
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
28-114 1.11e-08

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: 59.48  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   28 RYKRDHIYTYIGTSVVALNPYHHISE-HSLDNVRNYGDKGIFQ-LPPHIYGLTNLAYQSLKDQSE--DQCVLLTGESGAG 103
Cdd:cd14880   10 RYTADTFYTNAGCTLVALNPFKPVPQlYSPELMREYHAAPQPQkLKPHIFTVGEQTYRNVKSLIEpvNQSIVVSGESGAG 89
                         90
                 ....*....|.
gi 78706810  104 KTETFKMIVNF 114
Cdd:cd14880   90 KTWTSRCLMKF 100
MYSc_Myo37 cd14898
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...
19-115 2.13e-07

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: 55.29  E-value: 2.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   19 DSFINNIHQRYKRDHIYTYIGTSVVALNPYhhisehslDNVRNYGDKGIFQ-----LPPHIYGLTNLAYQSLKDQSeDQC 93
Cdd:cd14898    1 NATLEILEKRYASGKIYTKSGLVFLALNPY--------ETIYGAGAMKAYLknyshVEPHVYDVAEASVQDLLVHG-NQT 71
                         90       100
                 ....*....|....*....|..
gi 78706810   94 VLLTGESGAGKTETFKMIVNFL 115
Cdd:cd14898   72 IVISGESGSGKTENAKLVIKYL 93
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
25-115 2.43e-07

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: 55.20  E-value: 2.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   25 IHQRYKRDHI-YTYIGTSVVALNPYHHISEHSLDNVRNY-GDKGIFQLPPHIYGLTNLAYQSLKDQSED-QCVLLTGESG 101
Cdd:cd14875    7 IKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIFVQGLGnQSVVISGESG 86
                         90
                 ....*....|....
gi 78706810  102 AGKTETFKMIVNFL 115
Cdd:cd14875   87 SGKTENAKMLIAYL 100
MYSc_Myo24B cd14938
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
20-127 9.36e-06

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: 50.22  E-value: 9.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   20 SFINNIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYG-DKGIFQLPPHIYGLTNLAYQSLKDQSEDQCVLLTG 98
Cdd:cd14938    2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
                         90       100
                 ....*....|....*....|....*....
gi 78706810   99 ESGAGKTETFKMIVNFLTHIQDRSHCPPT 127
Cdd:cd14938   82 ESGSGKSEIAKNIINFIAYQVKGSRRLPT 110
MYSc_Myo12 cd14874
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...
24-116 1.42e-05

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: 49.48  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   24 NIHQRYKRDHIYTYIGTSVVALNPYHHISEHSLDNVRNYgdkgifqlppHIYGLTNLAYQSLKD-QSEDQCVLLTGESGA 102
Cdd:cd14874    6 NLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSmSSNAESIVFGGESGS 75
                         90
                 ....*....|....
gi 78706810  103 GKTETFKMIVNFLT 116
Cdd:cd14874   76 GKSYNAFQVFKYLT 89
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
19-107 3.69e-04

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: 44.72  E-value: 3.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706810   19 DSFINNIHQRYKRDHIYTYIGTSVVALNPYHHISehsldNVRNYGDKGIFQLPPHiygLTNLAYQSLKDQSED---QCVL 95
Cdd:cd14881    1 DAVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG-----NPLTLTSTRSSPLAPQ---LLKVVQEAVRQQSETgypQAII 72
                         90
                 ....*....|..
gi 78706810   96 LTGESGAGKTET 107
Cdd:cd14881   73 LSGTSGSGKTYA 84
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
403-432 4.62e-04

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: 42.33  E-value: 4.62e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 78706810  403 LEAMGNACTLKNNNSSRYGKLFDIEIDFKG 432
Cdd:cd01363  113 LEAFGNAKTTRNENSSRFGKFIEILLDIAG 142
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
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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