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Conserved domains on  [gi|755538916|ref|XP_011247387|]
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unconventional myosin-Id isoform X5 [Mus musculus]

Protein Classification

Motor_domain and Myosin_TH1 domain-containing protein( domain architecture ID 11715022)

Motor_domain and Myosin_TH1 domain-containing protein

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 ...
14-183 1.52e-93

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 cd01378:

Pssm-ID: 451428  Cd Length: 652  Bit Score: 297.53  E-value: 1.52e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  14 SYSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGklSITEVTKRPLTAATLFKNSMIALVDNLASKEPYYVRCIKP 93
Cdd:cd01378  485 TYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEG--VDLDSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKP 562
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  94 NDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSDKEAVKKLIERCGFQDDV 173
Cdd:cd01378  563 NDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEY 642
                        170
                 ....*....|
gi 755538916 174 AYGKSKIFIR 183
Cdd:cd01378  643 QMGKTKIFIR 652
Myosin_TH1 pfam06017
Unconventional myosin tail, actin- and lipid-binding; Unconventional myosins, ie those that ...
304-497 4.16e-43

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: 428724  Cd Length: 196  Bit Score: 151.60  E-value: 4.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  304 KVAAMEMLKGQRADLG--LQRAWEGNYLASkpdtpqtSGTFVPVANELKRKD---KYMNVLFSCHVRKVNRFSKVEDRAI 378
Cdd:pfam06017   1 KDYASDLLKGKKERRRfsLLRRFMGDYLGL-------ENNFSGPGPELRKAVgigGDEKVLFSDRVSKFNRSSKPSPRIL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  379 FVTDRHLYKMDPTK-----QYKVMKTIPLYNLTGLSVSNGKDQLVVFHTKDNK--DLIVCLfskqptheSRIGELVGVLV 451
Cdd:pfam06017  74 ILTDKALYLIDPKKfknglQYVLKRRIPLSDITGVSVSPLQDDWVVLHLGSPQkgDLLLEC--------DFKTELVTVLS 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 755538916  452 NHFKSE-KRHLQVNVTNPVQCSLHGKKCTVSVETRLNQPQPDFTKNR 497
Cdd:pfam06017 146 KLYKKKtNKKLNVKISDTIEYRKKKGKIRTVKFVKDEPKGKDSYKSL 192
 
Name Accession Description Interval E-value
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
14-183 1.52e-93

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: 297.53  E-value: 1.52e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  14 SYSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGklSITEVTKRPLTAATLFKNSMIALVDNLASKEPYYVRCIKP 93
Cdd:cd01378  485 TYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEG--VDLDSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKP 562
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  94 NDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSDKEAVKKLIERCGFQDDV 173
Cdd:cd01378  563 NDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEY 642
                        170
                 ....*....|
gi 755538916 174 AYGKSKIFIR 183
Cdd:cd01378  643 QMGKTKIFIR 652
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
14-195 1.27e-73

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: 245.92  E-value: 1.27e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916    14 SYSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLSITeVTKRPLTAATLFKNSMIALVDNLASKEPYYVRCIKP 93
Cdd:smart00242 497 TYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAG-SKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKP 575
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916    94 NDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDlPSDKEAVKKLIERCG-FQDD 172
Cdd:smart00242 576 NEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWG-GDAKKACEALLQSLGlDEDE 654
                          170       180
                   ....*....|....*....|...
gi 755538916   173 VAYGKSKIFIRtPRTLFTLEELR 195
Cdd:smart00242 655 YQLGKTKVFLR-PGQLAELEELR 676
Myosin_head pfam00063
Myosin head (motor domain);
15-183 1.43e-51

Myosin head (motor domain);


Pssm-ID: 395017  Cd Length: 674  Bit Score: 185.95  E-value: 1.43e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916   15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLSITEV-------------TKRPLTAATLFKNSMIALVDNLA 81
Cdd:pfam00063 493 YNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAanesgkstpkrtkKKRFITVGSQFKESLGELMKTLN 572
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916   82 SKEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSdKEAVK 161
Cdd:pfam00063 573 STNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKGDA-KKGCE 651
                         170       180
                  ....*....|....*....|...
gi 755538916  162 KLIERCGFQ-DDVAYGKSKIFIR 183
Cdd:pfam00063 652 AILQSLNLDkEEYQFGKTKIFFR 674
COG5022 COG5022
Myosin heavy chain [General function prediction only];
14-257 6.10e-46

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 172.57  E-value: 6.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916   14 SYSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLsiTEVTKRPLTAATLFKNSMIALVDNLASKEPYYVRCIKP 93
Cdd:COG5022   558 EYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEEN--IESKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKP 635
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916   94 NDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMIS-------EFTWPNhdlpSDKEAVKKLIER 166
Cdd:COG5022   636 NEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSpskswtgEYTWKE----DTKNAVKSILEE 711
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  167 CGFqDDVAY--GKSKIFIRTPrTLFTLEELRAQMLVRVVLFLQKVWRGTLARMRYKRTKAALTII-------RYYRRY-- 235
Cdd:COG5022   712 LVI-DSSKYqiGNTKVFFKAG-VLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIqviqhgfRLRRLVdy 789
                         250       260
                  ....*....|....*....|....*...
gi 755538916  236 --KVKSYIHEvaRRFHGV----KNMRDY 257
Cdd:COG5022   790 elKWRLFIKL--QPLLSLlgsrKEYRSY 815
Myosin_TH1 pfam06017
Unconventional myosin tail, actin- and lipid-binding; Unconventional myosins, ie those that ...
304-497 4.16e-43

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: 428724  Cd Length: 196  Bit Score: 151.60  E-value: 4.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  304 KVAAMEMLKGQRADLG--LQRAWEGNYLASkpdtpqtSGTFVPVANELKRKD---KYMNVLFSCHVRKVNRFSKVEDRAI 378
Cdd:pfam06017   1 KDYASDLLKGKKERRRfsLLRRFMGDYLGL-------ENNFSGPGPELRKAVgigGDEKVLFSDRVSKFNRSSKPSPRIL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  379 FVTDRHLYKMDPTK-----QYKVMKTIPLYNLTGLSVSNGKDQLVVFHTKDNK--DLIVCLfskqptheSRIGELVGVLV 451
Cdd:pfam06017  74 ILTDKALYLIDPKKfknglQYVLKRRIPLSDITGVSVSPLQDDWVVLHLGSPQkgDLLLEC--------DFKTELVTVLS 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 755538916  452 NHFKSE-KRHLQVNVTNPVQCSLHGKKCTVSVETRLNQPQPDFTKNR 497
Cdd:pfam06017 146 KLYKKKtNKKLNVKISDTIEYRKKKGKIRTVKFVKDEPKGKDSYKSL 192
PTZ00014 PTZ00014
myosin-A; Provisional
14-237 1.03e-26

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 114.36  E-value: 1.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  14 SYSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWpEGklsiTEVTKRPLTAATL----FKNSMIALVDNLASKEPYYVR 89
Cdd:PTZ00014 590 QYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLF-EG----VEVEKGKLAKGQLigsqFLNQLDSLMSLINSTEPHFIR 664
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  90 CIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMIseftwpnhDLP-------SDKEAVKK 162
Cdd:PTZ00014 665 CIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYL--------DLAvsndsslDPKEKAEK 736
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916 163 LIERCGF-QDDVAYGKSKIFIrTPRTLFTLEELRAQMLVR---VVLFLQKVWRGTLARMRYKRTKAALTIIR-YYRRYKV 237
Cdd:PTZ00014 737 LLERSGLpKDSYAIGKTMVFL-KKDAAKELTQIQREKLAAwepLVSVLEALILKIKKKRKVRKNIKSLVRIQaHLRRHLV 815
 
Name Accession Description Interval E-value
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
14-183 1.52e-93

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: 297.53  E-value: 1.52e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  14 SYSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGklSITEVTKRPLTAATLFKNSMIALVDNLASKEPYYVRCIKP 93
Cdd:cd01378  485 TYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEG--VDLDSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKP 562
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  94 NDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSDKEAVKKLIERCGFQDDV 173
Cdd:cd01378  563 NDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEY 642
                        170
                 ....*....|
gi 755538916 174 AYGKSKIFIR 183
Cdd:cd01378  643 QMGKTKIFIR 652
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
14-195 1.27e-73

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: 245.92  E-value: 1.27e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916    14 SYSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLSITeVTKRPLTAATLFKNSMIALVDNLASKEPYYVRCIKP 93
Cdd:smart00242 497 TYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAG-SKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKP 575
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916    94 NDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDlPSDKEAVKKLIERCG-FQDD 172
Cdd:smart00242 576 NEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWG-GDAKKACEALLQSLGlDEDE 654
                          170       180
                   ....*....|....*....|...
gi 755538916   173 VAYGKSKIFIRtPRTLFTLEELR 195
Cdd:smart00242 655 YQLGKTKVFLR-PGQLAELEELR 676
Myosin_head pfam00063
Myosin head (motor domain);
15-183 1.43e-51

Myosin head (motor domain);


Pssm-ID: 395017  Cd Length: 674  Bit Score: 185.95  E-value: 1.43e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916   15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLSITEV-------------TKRPLTAATLFKNSMIALVDNLA 81
Cdd:pfam00063 493 YNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAanesgkstpkrtkKKRFITVGSQFKESLGELMKTLN 572
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916   82 SKEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSdKEAVK 161
Cdd:pfam00063 573 STNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKGDA-KKGCE 651
                         170       180
                  ....*....|....*....|...
gi 755538916  162 KLIERCGFQ-DDVAYGKSKIFIR 183
Cdd:pfam00063 652 AILQSLNLDkEEYQFGKTKIFFR 674
COG5022 COG5022
Myosin heavy chain [General function prediction only];
14-257 6.10e-46

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 172.57  E-value: 6.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916   14 SYSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLsiTEVTKRPLTAATLFKNSMIALVDNLASKEPYYVRCIKP 93
Cdd:COG5022   558 EYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEEN--IESKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKP 635
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916   94 NDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMIS-------EFTWPNhdlpSDKEAVKKLIER 166
Cdd:COG5022   636 NEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSpskswtgEYTWKE----DTKNAVKSILEE 711
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  167 CGFqDDVAY--GKSKIFIRTPrTLFTLEELRAQMLVRVVLFLQKVWRGTLARMRYKRTKAALTII-------RYYRRY-- 235
Cdd:COG5022   712 LVI-DSSKYqiGNTKVFFKAG-VLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIqviqhgfRLRRLVdy 789
                         250       260
                  ....*....|....*....|....*...
gi 755538916  236 --KVKSYIHEvaRRFHGV----KNMRDY 257
Cdd:COG5022   790 elKWRLFIKL--QPLLSLlgsrKEYRSY 815
Myosin_TH1 pfam06017
Unconventional myosin tail, actin- and lipid-binding; Unconventional myosins, ie those that ...
304-497 4.16e-43

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: 428724  Cd Length: 196  Bit Score: 151.60  E-value: 4.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  304 KVAAMEMLKGQRADLG--LQRAWEGNYLASkpdtpqtSGTFVPVANELKRKD---KYMNVLFSCHVRKVNRFSKVEDRAI 378
Cdd:pfam06017   1 KDYASDLLKGKKERRRfsLLRRFMGDYLGL-------ENNFSGPGPELRKAVgigGDEKVLFSDRVSKFNRSSKPSPRIL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  379 FVTDRHLYKMDPTK-----QYKVMKTIPLYNLTGLSVSNGKDQLVVFHTKDNK--DLIVCLfskqptheSRIGELVGVLV 451
Cdd:pfam06017  74 ILTDKALYLIDPKKfknglQYVLKRRIPLSDITGVSVSPLQDDWVVLHLGSPQkgDLLLEC--------DFKTELVTVLS 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 755538916  452 NHFKSE-KRHLQVNVTNPVQCSLHGKKCTVSVETRLNQPQPDFTKNR 497
Cdd:pfam06017 146 KLYKKKtNKKLNVKISDTIEYRKKKGKIRTVKFVKDEPKGKDSYKSL 192
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
15-183 1.52e-40

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: 154.72  E-value: 1.52e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLSITEVTKRPLTAATLFKNSMIALVDNLASKEPYYVRCIKPN 94
Cdd:cd01381  480 YDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKSPTLSSQFRKSLDQLMKTLSACQPFFVRCIKPN 559
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  95 DKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHdLPSDKEAVKKLIERC-GFQDDV 173
Cdd:cd01381  560 EYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAH-KTDCRAATRKICCAVlGGDADY 638
                        170
                 ....*....|
gi 755538916 174 AYGKSKIFIR 183
Cdd:cd01381  639 QLGKTKIFLK 648
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
15-183 1.64e-36

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


Pssm-ID: 276950  Cd Length: 633  Bit Score: 143.12  E-value: 1.64e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSnpvlknmwpegklsitevtkrpltaatLFKNSMIALVDNLASKEPYYVRCIKPN 94
Cdd:cd00124  492 YDADGFLEKNKDTLPPDLVDLLRSGS---------------------------QFRSQLDALMDTLNSTQPHFVRCIKPN 544
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  95 DKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSDKEAVKKLIERCGFQDDVA 174
Cdd:cd00124  545 DEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQ 624

                 ....*....
gi 755538916 175 YGKSKIFIR 183
Cdd:cd00124  625 LGKTKVFLR 633
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
15-183 2.10e-32

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: 130.86  E-value: 2.10e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKnmwpegklsitevtkrpLTAATLFKNSMIALVDNLASKEPYYVRCIKPN 94
Cdd:cd01379  485 YDASGFLEKNRDTLPPDVVQLLRSSENPLVR-----------------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPN 547
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  95 DKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISeFTWpNHDLPSDKEAVKKLIERCGFqDDVA 174
Cdd:cd01379  548 DSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLA-FKW-NEEVVANRENCRLILERLKL-DNWA 624

                 ....*....
gi 755538916 175 YGKSKIFIR 183
Cdd:cd01379  625 LGKTKVFLK 633
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
14-183 6.68e-31

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: 126.67  E-value: 6.68e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  14 SYSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLSITEVTKRPL--------------TAATLFKNSMIALVDN 79
Cdd:cd14883  478 TYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDLLALTGLSISLggdttsrgtskgkpTVGDTFKHQLQSLVDV 557
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  80 LASKEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNhDLPSDKEA 159
Cdd:cd14883  558 LSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSA-DHKETCGA 636
                        170       180
                 ....*....|....*....|....*
gi 755538916 160 VKKLIERCGF-QDDVAYGKSKIFIR 183
Cdd:cd14883  637 VRALMGLGGLpEDEWQVGKTKVFLR 661
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
14-183 1.01e-28

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: 119.80  E-value: 1.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  14 SYSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWpegklsitevtkrpltaATLFKNSMIALVDNLASKEPYYVRCIKP 93
Cdd:cd14897  486 TYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF-----------------TSYFKRSLSDLMTKLNSADPLFVRCIKP 548
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  94 NDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFtwPNHDLPSDKEAVKKLIERCGFQdDV 173
Cdd:cd14897  549 NNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDF--SNKVRSDDLGKCQKILKTAGIK-GY 625
                        170
                 ....*....|
gi 755538916 174 AYGKSKIFIR 183
Cdd:cd14897  626 QFGKTKVFLK 635
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
15-183 4.02e-28

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: 118.34  E-value: 4.02e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLSitEVTKRPlTAATLFKNSMIALVDNLASKEPYYVRCIKPN 94
Cdd:cd14872  479 YDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEGD--QKTSKV-TLGGQFRKQLSALMTALNATEPHYIRCVKPN 555
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  95 DKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEfTWPNHDLPSDKEAVKKLIE-RCGFQDDV 173
Cdd:cd14872  556 QEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVK-TIAKRVGPDDRQRCDLLLKsLKQDFSKV 634
                        170
                 ....*....|
gi 755538916 174 AYGKSKIFIR 183
Cdd:cd14872  635 QVGKTRVLYR 644
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
15-183 5.85e-27

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: 114.89  E-value: 5.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWP-------EGKLSITEVTKRPlTAATLFKNSMIALVDNLASKEPYY 87
Cdd:cd14873  479 YDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEhvssrnnQDTLKCGSKHRRP-TVSSQFKDSLHSLMATLSSSNPFF 557
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  88 VRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSDKEAVKKLIERC 167
Cdd:cd14873  558 VRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPEDVRGKCTSLLQLYDAS 637
                        170
                 ....*....|....*.
gi 755538916 168 GfqDDVAYGKSKIFIR 183
Cdd:cd14873  638 N--SEWQLGKTKVFLR 651
PTZ00014 PTZ00014
myosin-A; Provisional
14-237 1.03e-26

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 114.36  E-value: 1.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  14 SYSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWpEGklsiTEVTKRPLTAATL----FKNSMIALVDNLASKEPYYVR 89
Cdd:PTZ00014 590 QYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLF-EG----VEVEKGKLAKGQLigsqFLNQLDSLMSLINSTEPHFIR 664
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  90 CIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMIseftwpnhDLP-------SDKEAVKK 162
Cdd:PTZ00014 665 CIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYL--------DLAvsndsslDPKEKAEK 736
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916 163 LIERCGF-QDDVAYGKSKIFIrTPRTLFTLEELRAQMLVR---VVLFLQKVWRGTLARMRYKRTKAALTIIR-YYRRYKV 237
Cdd:PTZ00014 737 LLERSGLpKDSYAIGKTMVFL-KKDAAKELTQIQREKLAAwepLVSVLEALILKIKKKRKVRKNIKSLVRIQaHLRRHLV 815
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
14-183 3.32e-26

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: 112.25  E-value: 3.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  14 SYSAIGFIDKNKDTLFQDFKRLMYNSSNpvlknmwpegklsitevtKRPlTAATLFKNSMIALVDNLASKEPYYVRCIKP 93
Cdd:cd01380  480 EYQVEGFLEKNRDTVSEEHLNVLKASKN------------------RKK-TVGSQFRDSLILLMETLNSTTPHYVRCIKP 540
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  94 NDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTwpnHDLPSDKEAVKKLIERCGFQDDV 173
Cdd:cd01380  541 NDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSK---EWLRDDKKKTCENILENLILDPD 617
                        170
                 ....*....|..
gi 755538916 174 AY--GKSKIFIR 183
Cdd:cd01380  618 KYqfGKTKIFFR 629
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
9-183 3.74e-25

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: 109.09  E-value: 3.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916   9 EVIfssYSAIGFIDKNKDTLFQDFKRLMYNSSNpvlknmwpegklSITEVTkrpltAATLFKNSMIALVDNLASKEPYYV 88
Cdd:cd14890  513 DVI---YDASGFNEKNNETLNAEMKELIKQSRR------------SIREVS-----VGAQFRTQLQELMAKISLTNPRYV 572
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  89 RCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEftwpnhDLPSDKEAVKKLIERCG 168
Cdd:cd14890  573 RCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLP------TAENIEQLVAVLSKMLG 646
                        170
                 ....*....|....*.
gi 755538916 169 F-QDDVAYGKSKIFIR 183
Cdd:cd14890  647 LgKADWQIGSSKIFLK 662
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
15-183 4.12e-25

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: 108.92  E-value: 4.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEgklSITEVTKRPL---TAATLFKNSMIALVDNLASKEPYYVRCI 91
Cdd:cd01384  482 YQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPP---LPREGTSSSSkfsSIGSRFKQQLQELMETLNTTEPHYIRCI 558
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  92 KPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMIS-EFTWPNHDlpsDKEAVKKLIERC--- 167
Cdd:cd01384  559 KPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLApEVLKGSDD---EKAACKKILEKAglk 635
                        170
                 ....*....|....*.
gi 755538916 168 GFQddvaYGKSKIFIR 183
Cdd:cd01384  636 GYQ----IGKTKVFLR 647
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
2-183 2.33e-24

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: 106.65  E-value: 2.33e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916   2 IHTAIYFEvifssYSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMW-------PEGKLSITEVTKRPLTAATLFKNSMI 74
Cdd:cd14907  512 RHTAKEVE-----YNIEGFREKNKDEISQSIINCIQNSKNRIISSIFsgedgsqQQNQSKQKKSQKKDKFLGSKFRNQMK 586
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  75 ALVDNLASKEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFtwpnhdlp 154
Cdd:cd14907  587 QLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN-------- 658
                        170       180
                 ....*....|....*....|....*....
gi 755538916 155 sdkeavkkliercgfqddVAYGKSKIFIR 183
Cdd:cd14907  659 ------------------VLFGKTKIFMK 669
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
15-183 7.64e-24

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: 105.24  E-value: 7.64e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLSITEVTKR------PLTAATLFKNSMIALVDNLASKEPYYV 88
Cdd:cd01377  488 YNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGGGKKkkkggsFRTVSQLHKEQLNKLMTTLRSTHPHFV 567
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  89 RCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISeftwPN---HDLPSDKEAVKKLIE 165
Cdd:cd01377  568 RCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILA----PNaipKGFDDGKAACEKILK 643
                        170       180
                 ....*....|....*....|.
gi 755538916 166 rcGFQDDVA-Y--GKSKIFIR 183
Cdd:cd01377  644 --ALQLDPElYriGNTKVFFK 662
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
14-183 1.33e-23

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: 104.32  E-value: 1.33e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  14 SYSAIGFIDKNKDTLFQDFKRLMYNSSNPVLK-----------NMWPEGKLSITEVTKRplTAATLFKNSMIALVDNLAS 82
Cdd:cd01383  470 TYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQlfaskmldasrKALPLTKASGSDSQKQ--SVATKFKGQLFKLMQRLEN 547
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  83 KEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDlpsDKEAVKK 162
Cdd:cd01383  548 TTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQ---DPLSTSV 624
                        170       180
                 ....*....|....*....|...
gi 755538916 163 LIER-CGFQDD-VAYGKSKIFIR 183
Cdd:cd01383  625 AILQqFNILPEmYQVGYTKLFFR 647
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
15-183 2.38e-23

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: 103.83  E-value: 2.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKN------------MWPEGKLSITE---VTKRPLTAATLFKNSMIALVDN 79
Cdd:cd14889  481 YNASGFLEKNRDTIPASIRTLFINSATPLLSVlftatrsrtgtlMPRAKLPQAGSdnfNSTRKQSVGAQFKHSLGVLMEK 560
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  80 LASKEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMIseftWPNHDLPSDKEA 159
Cdd:cd14889  561 MFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKIL----LCEPALPGTKQS 636
                        170       180
                 ....*....|....*....|....
gi 755538916 160 VKKLIERCGFQdDVAYGKSKIFIR 183
Cdd:cd14889  637 CLRILKATKLV-GWKCGKTRLFFK 659
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
15-183 3.58e-23

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: 103.29  E-value: 3.58e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMW----------PEGKLSITEVTKRPL--TAATLFKNSMIALVDNLAS 82
Cdd:cd01387  477 YQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFsshraqtdkaPPRLGKGRFVTMKPRtpTVAARFQDSLLQLLEKMER 556
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  83 KEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSDKEAVKK 162
Cdd:cd01387  557 CNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPRPAPGDMCVSLLS 636
                        170       180
                 ....*....|....*....|.
gi 755538916 163 LIERCGFQDDVAYGKSKIFIR 183
Cdd:cd01387  637 RLCTVTPKDMYRLGATKVFLR 657
MYSc_Myo25 cd14886
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...
1-183 2.39e-22

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: 100.73  E-value: 2.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916   1 MIHTAIYFevifsSYSAIGFIDKNKDTLFQDFKRLMYNSSNPVLkNMWPEGKLSITEVTKRPLTAATlFKNSMIALVDNL 80
Cdd:cd14886  473 IVHTAATV-----TYNTEEFVDKNKHKLSVDILELLMGSTNPIV-NKAFSDIPNEDGNMKGKFLGST-FQLSIDQLMKTL 545
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  81 ASKEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSD-KEA 159
Cdd:cd14886  546 SATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILISHNSSSQNAGEDlVEA 625
                        170       180
                 ....*....|....*....|....*
gi 755538916 160 VKKLIERCGF-QDDVAYGKSKIFIR 183
Cdd:cd14886  626 VKSILENLGIpCSDYRIGKTKVFLR 650
MYSc_Myo14 cd14876
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...
14-183 1.07e-21

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: 98.52  E-value: 1.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  14 SYSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWpEGKlsitEVTKRPLTAATL----FKNSMIALVDNLASKEPYYVR 89
Cdd:cd14876  481 QYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALF-EGV----VVEKGKIAKGSLigsqFLKQLESLMGLINSTEPHFIR 555
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  90 CIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMIsEFTWPNHDLPSDKEAVKKLIERCGF 169
Cdd:cd14876  556 CIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFL-DLGIANDKSLDPKVAALKLLESSGL 634
                        170
                 ....*....|....*
gi 755538916 170 Q-DDVAYGKSKIFIR 183
Cdd:cd14876  635 SeDEYAIGKTMVFLK 649
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
59-183 2.59e-21

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: 97.45  E-value: 2.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  59 TKRPLTAATLFKNSMIALVDNLASKEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLH 138
Cdd:cd01385  570 KKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFIT 649
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 755538916 139 RYKMIseftWPNHDLPSdKEAVKKLIERCGFQ-DDVAYGKSKIFIR 183
Cdd:cd01385  650 QFQVL----LPKGLISS-KEDIKDFLEKLNLDrDNYQIGKTKVFLK 690
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
15-183 8.35e-21

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: 95.98  E-value: 8.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNpvlknmwpegklsitevtkrpltaatlFKNSMIALVDNLASKEPYYVRCIKPN 94
Cdd:cd14892  509 YDVHGFLAKNNDNLHDDLRDLLRSSSK---------------------------FRTQLAELMEVLWSTTPSYIKCIKPN 561
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  95 DKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISE-----FTWPNHDLPS-----DKEAVKKLI 164
Cdd:cd14892  562 NLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLARnkagvAASPDACDATtarkkCEEIVARAL 641
                        170
                 ....*....|....*....
gi 755538916 165 ERCGFQddvaYGKSKIFIR 183
Cdd:cd14892  642 ERENFQ----LGRTKVFLR 656
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
15-183 9.51e-21

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: 95.65  E-value: 9.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWpEGKLSitevtkrplTAATLFKNSMIALVDNLASKEPYYVRCIKPN 94
Cdd:cd14878  499 YEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLF-QSKLV---------TIASQLRKSLADIIGKLQKCTPHFIHCIKPN 568
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  95 DKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSDKEAVKKLIERC---GFQd 171
Cdd:cd14878  569 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLGEKKKQSAEERCRLVLQQCklqGWQ- 647
                        170
                 ....*....|..
gi 755538916 172 dvaYGKSKIFIR 183
Cdd:cd14878  648 ---MGVRKVFLK 656
MYSc_Myh3 cd14913
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...
15-183 1.76e-20

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: 94.73  E-value: 1.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLSITEVTKRPL---------TAATLFKNSMIALVDNLASKEP 85
Cdd:cd14913  490 YSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVakkkgssfqTVSALFRENLNKLMSNLRTTHP 569
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  86 YYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSDKEAVKKLIE 165
Cdd:cd14913  570 HFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDSKKACEKLLA 649
                        170
                 ....*....|....*....
gi 755538916 166 RCGF-QDDVAYGKSKIFIR 183
Cdd:cd14913  650 SIDIdHTQYKFGHTKVFFK 668
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
15-182 1.95e-20

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: 94.53  E-value: 1.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWP--EGKLSITEVTKRP----LTAATLFKNSMIALVDNLASKEPYYV 88
Cdd:cd14880  490 YHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPanPEEKTQEEPSGQSrapvLTVVSKFKASLEQLLQVLHSTTPHYI 569
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  89 RCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTwpnhdlPSDKEAVKKLIERCG 168
Cdd:cd14880  570 RCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLRRLR------PHTSSGPHSPYPAKG 643
                        170
                 ....*....|....
gi 755538916 169 FQDDVAYGKSKIFI 182
Cdd:cd14880  644 LSEPVHCGRTKVFM 657
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
14-141 9.20e-20

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: 92.45  E-value: 9.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  14 SYSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLSITEVT---KRPLTAATLFKNSMIALVDNLASKEPYYVRC 90
Cdd:cd14888  513 KYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSAYLRRGTDGNtkkKKFVTVSSEFRNQLDVLMETIDKTEPHFIRC 592
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755538916  91 IKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYK 141
Cdd:cd14888  593 IKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYR 643
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
15-182 1.22e-19

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: 92.16  E-value: 1.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLknmwpegklsitevtkrPLTAATLFKNSMIALVDNLASKEPYYVRCIKPN 94
Cdd:cd14901  499 YATDGFCDKNKDHVHSEALALLRTSSNAFL-----------------SSTVVAKFKVQLSSLLEVLNATEPHFIRCIKPN 561
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  95 DKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEftwpnhDLPSDKEAVKKLIERCGFQ---- 170
Cdd:cd14901  562 DVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAP------DGASDTWKVNELAERLMSQlqhs 635
                        170
                 ....*....|....*....
gi 755538916 171 -------DDVAYGKSKIFI 182
Cdd:cd14901  636 elniehlPPFQVGKTKVFL 654
MYSc_Myh7b cd14927
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...
7-183 1.50e-19

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: 91.94  E-value: 1.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916   7 YFEVIFSS----YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWP---------EGKLSITEVTKRPL---TAATLFK 70
Cdd:cd14927  483 HFEVVHYAgvvpYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYEnyvgsdsteDPKSGVKEKRKKAAsfqTVSQLHK 562
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  71 NSMIALVDNLASKEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPN 150
Cdd:cd14927  563 ENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIPD 642
                        170       180       190
                 ....*....|....*....|....*....|....
gi 755538916 151 HDLPSDKEAVKKLIERCGF-QDDVAYGKSKIFIR 183
Cdd:cd14927  643 DKFVDSRKATEKLLGSLDIdHTQYQFGHTKVFFK 676
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
15-183 1.71e-19

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: 91.88  E-value: 1.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLSITEVT------KRP--LTAATL---FKNSMIALVDNLASK 83
Cdd:cd14902  500 YNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRDSPGADngaagrRRYsmLRAPSVsaqFKSQLDRLIVQIGRT 579
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  84 EPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEF--------TWPNHDL-- 153
Cdd:cd14902  580 EAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFKCFlstrdraaKMNNHDLaq 659
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755538916 154 ----------------PSDKEAVKKLI------ERCGFQDD-----VAYGKSKIFIR 183
Cdd:cd14902  660 alvtvlmdrvlledgvEREEKNPGALTavtgdgSGTAFENDcrrkdVQVGRTLVFCK 716
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
15-167 6.98e-19

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: 89.84  E-value: 6.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMW------PEGKLSITEVTKRP--------LTAATLFKNSMIALVDNL 80
Cdd:cd14903  476 YESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFkekvesPAAASTSLARGARRrrggalttTTVGTQFKDSLNELMTTI 555
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  81 ASKEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMIseftwpnhdLPSDKEAV 160
Cdd:cd14903  556 RSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLF---------LPEGRNTD 626

                 ....*..
gi 755538916 161 KKLIERC 167
Cdd:cd14903  627 VPVAERC 633
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
14-143 9.17e-19

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: 89.65  E-value: 9.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  14 SYSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLSITEVTKRP---LTAATLFKNSMIALVDNLASKEPYYVRC 90
Cdd:cd14906  519 TYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQITSTTNTTKKQtqsNTVSGQFLEQLNQLIQTINSTSVHYIRC 598
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755538916  91 IKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMI 143
Cdd:cd14906  599 IKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCI 651
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
15-160 9.14e-18

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: 86.13  E-value: 9.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNpvlknmwpegklsitevtkrpltaatlFKNSMIALVDNLASKEPYYVRCIKPN 94
Cdd:cd14900  489 YSTDGFLEKNKDVLHQEAVDLFVYGLQ---------------------------FKEQLTTLLETLQQTNPHYVRCLKPN 541
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755538916  95 DKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMI-----------SEFTWPNHDLPSDKEAV 160
Cdd:cd14900  542 DLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSLaraknrllakkQGTSLPDTDSDHGPAVV 618
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
14-140 1.53e-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: 85.76  E-value: 1.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  14 SYSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKL-SITEVTKR------PLTAATLFKNSMIALVDNLASKEPY 86
Cdd:cd14904  478 TYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEApSETKEGKSgkgtkaPKSLGSQFKTSLSQLMDNIKTTNTH 557
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755538916  87 YVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRY 140
Cdd:cd14904  558 YVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRY 611
MYSc_Myh8 cd14918
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...
15-183 1.77e-17

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: 85.56  E-value: 1.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWP-----EGKLSITEVTKRP----LTAATLFKNSMIALVDNLASKEP 85
Cdd:cd14918  490 YNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFStyasaEADSGAKKGAKKKgssfQTVSALFRENLNKLMTNLRSTHP 569
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  86 YYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSDKEAVKKLIE 165
Cdd:cd14918  570 HFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDSKKASEKLLA 649
                        170
                 ....*....|....*....
gi 755538916 166 RCGF-QDDVAYGKSKIFIR 183
Cdd:cd14918  650 SIDIdHTQYKFGHTKVFFK 668
MYSc_Myh4 cd14915
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...
15-183 1.93e-17

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: 85.55  E-value: 1.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLSITE----------VTKRPLTAATLFKNSMIALVDNLASKE 84
Cdd:cd14915  492 YNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEggggkkggkkKGSSFQTVSALFRENLNKLMTNLRSTH 571
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  85 PYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSDKEAVKKLI 164
Cdd:cd14915  572 PHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLL 651
                        170       180
                 ....*....|....*....|
gi 755538916 165 ERCGF-QDDVAYGKSKIFIR 183
Cdd:cd14915  652 GSIDIdHTQYKFGHTKVFFK 671
MYSc_Myh1_mammals cd14910
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
15-183 1.99e-17

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: 85.17  E-value: 1.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPE----------GKLSITEVTKRPLTAATLFKNSMIALVDNLASKE 84
Cdd:cd14910  492 YNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGaaaaeaeeggGKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTH 571
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  85 PYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSDKEAVKKLI 164
Cdd:cd14910  572 PHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLL 651
                        170       180
                 ....*....|....*....|
gi 755538916 165 ERCGF-QDDVAYGKSKIFIR 183
Cdd:cd14910  652 GSIDIdHTQYKFGHTKVFFK 671
MYSc_Myh15_mammals cd14929
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...
5-183 2.04e-17

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: 85.41  E-value: 2.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916   5 AIYFEVIFSS----YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPE-----GKLSITEVTKRPLTA----ATLFKN 71
Cdd:cd14929  470 EAHFELVHYAgvvpYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENyistdSAIQFGEKKRKKGASfqtvASLHKE 549
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  72 SMIALVDNLASKEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNH 151
Cdd:cd14929  550 NLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKS 629
                        170       180       190
                 ....*....|....*....|....*....|....
gi 755538916 152 DLPSDKEAVKKLIERCGFqDDVAY--GKSKIFIR 183
Cdd:cd14929  630 KFVSSRKAAEELLGSLEI-DHTQYrfGITKVFFK 662
MYSc_Myh7 cd14917
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...
15-183 9.65e-17

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: 83.23  E-value: 9.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLSITEVTKRP---------LTAATLFKNSMIALVDNLASKEP 85
Cdd:cd14917  490 YNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAPIEKGKgkakkgssfQTVSALHRENLNKLMTNLRSTHP 569
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  86 YYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSDKEAVKKLIE 165
Cdd:cd14917  570 HFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSRKGAEKLLS 649
                        170
                 ....*....|....*....
gi 755538916 166 RCGF-QDDVAYGKSKIFIR 183
Cdd:cd14917  650 SLDIdHNQYKFGHTKVFFK 668
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
15-183 2.56e-16

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: 81.92  E-value: 2.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLSITEVT----------KRPLTAATL---FKNSMIALVDNLA 81
Cdd:cd14895  530 YQAEGFCEKNKDQPNAELFSVLGKTSDAHLRELFEFFKASESAELslgqpklrrrSSVLSSVGIgsqFKQQLASLLDVVQ 609
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  82 SKEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISefTWPNHDLPSDKEAVK 161
Cdd:cd14895  610 QTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV--AAKNASDATASALIE 687
                        170       180
                 ....*....|....*....|..
gi 755538916 162 KLiercgFQDDVAYGKSKIFIR 183
Cdd:cd14895  688 TL-----KVDHAELGKTRVFLR 704
MYSc_Myh13 cd14923
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...
15-183 2.73e-16

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: 81.65  E-value: 2.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWP--------EGKLSITEVTKRP---LTAATLFKNSMIALVDNLASK 83
Cdd:cd14923  491 YNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSnyagaeagDSGGSKKGGKKKGssfQTVSAVFRENLNKLMTNLRST 570
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  84 EPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSDKEAVKKL 163
Cdd:cd14923  571 HPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQFIDSKNASEKL 650
                        170       180
                 ....*....|....*....|.
gi 755538916 164 IERCGF-QDDVAYGKSKIFIR 183
Cdd:cd14923  651 LNSIDVdREQYRFGHTKVFFK 671
MYSc_Myh2_mammals cd14912
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
15-183 2.77e-16

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: 81.70  E-value: 2.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLSITEVT--------KRP----LTAATLFKNSMIALVDNLAS 82
Cdd:cd14912  492 YNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAgggakkggKKKgssfQTVSALFRENLNKLMTNLRS 571
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  83 KEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSDKEAVKK 162
Cdd:cd14912  572 THPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEK 651
                        170       180
                 ....*....|....*....|..
gi 755538916 163 LIERCGF-QDDVAYGKSKIFIR 183
Cdd:cd14912  652 LLASIDIdHTQYKFGHTKVFFK 673
MYSc_Myo38 cd14899
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...
14-183 2.96e-16

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: 81.68  E-value: 2.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  14 SYSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNM-------------WPEGKLSITEVTKRPLTAA----TLFKNSMIAL 76
Cdd:cd14899  541 TYTIDGFLAKNKDSFCESAAQLLAGSSNPLIQALaagsndedangdsELDGFGGRTRRRAKSAIAAvsvgTQFKIQLNEL 620
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  77 VDNLASKEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYK--MISEFTWPNHDLP 154
Cdd:cd14899  621 LSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYRrvLLSLYKWGDNDFE 700
                        170       180
                 ....*....|....*....|....*....
gi 755538916 155 SDKeavkklieRCGfqddVAYGKSKIFIR 183
Cdd:cd14899  701 RQM--------RCG----VSLGKTRVFFR 717
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
62-183 1.31e-15

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: 79.57  E-value: 1.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  62 PLTAATLF------KNSMIALVDNLASKEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEK 135
Cdd:cd14908  535 PLTADSLFesgqqfKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKD 614
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755538916 136 FLHRYKMI------SEFTWPNHDLPSDKEAVKKLIERCGF--------------QDDVAYGKSKIFIR 183
Cdd:cd14908  615 FFKRYRMLlplipeVVLSWSMERLDPQKLCVKKMCKDLVKgvlspamvsmknipEDTMQLGKSKVFMR 682
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
12-183 2.31e-15

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: 78.70  E-value: 2.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  12 FSSYSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLsiteVTKRPLTAATLFKNSMIALVDNLASKEPYYVRCI 91
Cdd:cd14875  491 FVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKG----LARRKQTVAIRFQRQLTDLRTELESTETQFIRCI 566
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  92 KPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFT----WPNHDLpsdKEAVKKLIERc 167
Cdd:cd14875  567 KPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRStaslFKQEKY---SEAAKDFLAY- 642
                        170       180
                 ....*....|....*....|...
gi 755538916 168 gFQD-------DVAYGKSKIFIR 183
Cdd:cd14875  643 -YQRlygwakpNYAVGKTKVFLR 664
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
15-183 2.70e-15

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: 78.48  E-value: 2.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGK--------LSITEVTKRPL-----TAATLFKNSMIALVDNLA 81
Cdd:cd14911  493 YSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgmaqqaLTDTQFGARTRkgmfrTVSHLYKEQLAKLMDTLR 572
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  82 SKEPYYVRCIKPNDKK------SPQIFDDERCRhqveylGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLpS 155
Cdd:cd14911  573 NTNPNFVRCIIPNHEKragkidAPLVLDQLRCN------GVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFM-D 645
                        170       180
                 ....*....|....*....|....*....
gi 755538916 156 DKEAVKKLIERCGFQDDV-AYGKSKIFIR 183
Cdd:cd14911  646 GKKACEKMIQALELDSNLyRVGQSKIFFR 674
MYSc_Myh6 cd14916
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...
15-183 1.14e-14

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: 76.64  E-value: 1.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPE------GKLSITEVTKRP----LTAATLFKNSMIALVDNLASKE 84
Cdd:cd14916  491 YNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTyasadtGDSGKGKGGKKKgssfQTVSALHRENLNKLMTNLKTTH 570
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  85 PYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSDKEAVKKLI 164
Cdd:cd14916  571 PHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSRKGAEKLL 650
                        170       180
                 ....*....|....*....|
gi 755538916 165 ERCGF-QDDVAYGKSKIFIR 183
Cdd:cd14916  651 GSLDIdHNQYKFGHTKVFFK 670
MYSc_Myo24A cd14937
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
14-183 3.03e-14

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: 75.44  E-value: 3.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  14 SYSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLSiTEVTKRPLTAATLFKNsMIALVDNLASKEPYYVRCIKP 93
Cdd:cd14937  472 TYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVS-ESLGRKNLITFKYLKN-LNNIISYLKSTNIYFIKCIKP 549
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  94 NDKKSPQIFDDERCRHQVEYLGLLENVRVRRAgFAFRQTYEKFLHRYKMISEFTWPNHDLpSDKEAVKKLIERCGFQDDV 173
Cdd:cd14937  550 NENKEKNNFNQKKVFPQLFSLSIIETLNISFF-FQYKYTFDVFLSYFEYLDYSTSKDSSL-TDKEKVSMILQNTVDPDLY 627
                        170
                 ....*....|
gi 755538916 174 AYGKSKIFIR 183
Cdd:cd14937  628 KVGKTMVFLK 637
MYSc_Myh16 cd14934
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...
7-183 1.04e-13

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: 73.52  E-value: 1.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916   7 YFEVIFSS----YSAIGFIDKNKDTLFQDFKRLmYNSSNPVLKNMWPEGKLSITEVTKRP-----LTAATLFKNSMIALV 77
Cdd:cd14934  475 HFELVHYAgtvgYNITGWLEKNKDPLNETVVGL-FQKSSLGLLALLFKEEEAPAGSKKQKrgssfMTVSNFYREQLNKLM 553
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  78 DNLASKEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPnHDLPSDK 157
Cdd:cd14934  554 TTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIP-QGFVDNK 632
                        170       180
                 ....*....|....*....|....*..
gi 755538916 158 EAVKKLIERCGF-QDDVAYGKSKIFIR 183
Cdd:cd14934  633 KASELLLGSIDLdVNEYKIGHTKVFFR 659
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
15-183 3.88e-13

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: 71.97  E-value: 3.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPE--------GKLSITEV-------TKRPL--TAATLFKNSMIALV 77
Cdd:cd14920  488 YKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrivgldQVTGMTETafgsaykTKKGMfrTVGQLYKESLTKLM 567
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  78 DNLASKEPYYVRCIKPNDKK-----SPQ-IFDDERCRhqveylGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNh 151
Cdd:cd14920  568 ATLRNTNPNFVRCIIPNHEKragklDPHlVLDQLRCN------GVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK- 640
                        170       180       190
                 ....*....|....*....|....*....|...
gi 755538916 152 DLPSDKEAVKKLIERCGFQDDV-AYGKSKIFIR 183
Cdd:cd14920  641 GFMDGKQACERMIRALELDPNLyRIGQSKIFFR 673
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
14-183 3.48e-12

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: 68.65  E-value: 3.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  14 SYSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLSITEVTKRPlTAATLFKNSMIALVDNLASKEPYYVRCIKP 93
Cdd:cd14896  477 TYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP-TLASRFQQSLGDLTARLGRSHVYFIHCLNP 555
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  94 NDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHdlpSDKEAVKKLIERC-GFQDD 172
Cdd:cd14896  556 NPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEAL---SDRERCGAILSQVlGAESP 632
                        170
                 ....*....|..
gi 755538916 173 VAY-GKSKIFIR 183
Cdd:cd14896  633 LYHlGATKVLLK 644
MYSc_Myo21 cd14882
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...
15-183 5.97e-12

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: 67.84  E-value: 5.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKlsitevTKRPLTAATLFKNSMIALVDNLA----SKEPYYVRC 90
Cdd:cd14882  479 YDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQ------VRNMRTLAATFRATSLELLKMLSiganSGGTHFVRC 552
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  91 IKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMIS-EFtwpNHDLPSDKEAVKKLIERCGF 169
Cdd:cd14882  553 IRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLAfDF---DETVEMTKDNCRLLLIRLKM 629
                        170
                 ....*....|....
gi 755538916 170 QdDVAYGKSKIFIR 183
Cdd:cd14882  630 E-GWAIGKTKVFLK 642
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
14-182 4.68e-11

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: 65.26  E-value: 4.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  14 SYSAIGFIDKNKDTLFQDFKRLmynssnpvlknmwpegklsitevtkrpLTAATLFKNSMIALVDNLASKEPYYVRCIKP 93
Cdd:cd14879  502 TYSVEGFLERNGDVLSPDFVNL---------------------------LRGATQLNAALSELLDTLDRTRLWSVFCIRP 554
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  94 NDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMisefTWPNHDLPSDKEAVKKLIERCGFqdDV 173
Cdd:cd14879  555 NDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKS----TLRGSAAERIRQCARANGWWEGR--DY 628

                 ....*....
gi 755538916 174 AYGKSKIFI 182
Cdd:cd14879  629 VLGNTKVFL 637
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
15-183 5.75e-11

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: 64.96  E-value: 5.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPE------------GKLSITEVTKRpltaatlFKNSMIALVDNLAS 82
Cdd:cd01382  478 YETAQFIEKNNDALHASLESLICESKDKFIRSLFESstnnnkdskqkaGKLSFISVGNK-------FKTQLNLLMDKLRS 550
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  83 KEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKmiseftwpnHDLPSDKEAVK- 161
Cdd:cd01382  551 TGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYK---------KYLPPKLARLDp 621
                        170       180
                 ....*....|....*....|....*...
gi 755538916 162 KLIERCGFQ------DDVAYGKSKIFIR 183
Cdd:cd01382  622 RLFCKALFKalglneNDFKFGLTKVFFR 649
MYSc_Myo12 cd14874
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...
15-183 1.60e-10

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: 63.35  E-value: 1.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLSITEVTkrpLTAATLFKNSMIALVDNLASKEPYYVRCIKPN 94
Cdd:cd14874  463 YNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDMI---VSQAQFILRGAQEIADKINGSHAHFVRCIKSN 539
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  95 DKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMIseftwpnhdLPSD-------KEAVKKLIERC 167
Cdd:cd14874  540 NERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL---------LPGDiamcqneKEIIQDILQGQ 610
                        170
                 ....*....|....*...
gi 755538916 168 G--FQDDVAYGKSKIFIR 183
Cdd:cd14874  611 GvkYENDFKIGTEYVFLR 628
MYSc_Myo37 cd14898
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...
53-143 1.58e-09

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: 60.30  E-value: 1.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  53 LSITEVTKRPLTaaTLFKNSMIALVDNLASKEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQT 132
Cdd:cd14898  470 LINDEGSKEDLV--KYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIP 547
                         90
                 ....*....|.
gi 755538916 133 YEKFLHRYKMI 143
Cdd:cd14898  548 KDRFEERYRIL 558
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
14-141 5.96e-09

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: 58.52  E-value: 5.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  14 SYSAIGFIDKNKDTLFQDFKRLmynssnpvlknmwpegklsitevtkrpLTAATLFKNSMIALVDNLASKEPYYVRCIKP 93
Cdd:cd14891  502 SYTIGSFIDKNNDIIPEDFEDL---------------------------LASSAKFSDQMQELVDTLEATRCNFIRCIKP 554
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 755538916  94 NDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYK 141
Cdd:cd14891  555 NAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYK 602
MYSc_Myo26 cd14887
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...
15-183 2.35e-07

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: 53.50  E-value: 2.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  15 YSAIGFIDKNKDTLFQDFKRLmYNSSNPVLKNMWPEGKLSITEVTKRPLTAATLFKNSMIALVDNLASKEPYYVRCIKPN 94
Cdd:cd14887  559 YDARDFCRANREATSDELERL-FLACSTYTRLVGSKKNSGVRAISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPN 637
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  95 DKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHdLPSDKEAVKKLIERCGFQDDVA 174
Cdd:cd14887  638 RVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALREA-LTPKMFCKIVLMFLEINSNSYT 716

                 ....*....
gi 755538916 175 YGKSKIFIR 183
Cdd:cd14887  717 FGKTKIFFR 725
MYSc_Myo23 cd14884
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ...
14-181 2.53e-07

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: 53.37  E-value: 2.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  14 SYSAIGFIDKNKDTLFQDFKRLMYNSSNPVL-KNMWPEGKLSITEVTKRpltaatlFKNSMIALVDNLASKEPYYVRCIK 92
Cdd:cd14884  524 TYRINNWIDKNSDKIETSIETLISCSSNRFLrEANNGGNKGNFLSVSKK-------YIKELDNLFTQLQSTDMYYIRCFL 596
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  93 PNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAfrqtyekflHRYKMiseftwpNHDLPSDKEAVKKLIERCGFQDD 172
Cdd:cd14884  597 PNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLS---------HKIPK-------KETAAALKEQIAKELEKCNSNTD 660

                 ....*....
gi 755538916 173 VAYGKSKIF 181
Cdd:cd14884  661 IEYQRRLAA 669
MYSc_Myo44 cd14905
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...
86-183 1.11e-05

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: 48.16  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  86 YYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEftwpnhdlpsDKEAVKKLIE 165
Cdd:cd14905  577 HFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQ----------NQRNFQNLFE 646
                         90       100
                 ....*....|....*....|....*..
gi 755538916 166 RCGFQD---------DVAYGKSKIFIR 183
Cdd:cd14905  647 KLKENDinidsilppPIQVGNTKIFLR 673
MYSc_Myo32 cd14893
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...
64-143 1.22e-03

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: 41.50  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755538916  64 TAATLFKNSMIALVDNLASKEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMI 143
Cdd:cd14893  627 SAATDVYNQADALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYKNV 706
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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