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Conserved domains on  [gi|159470529|ref|XP_001693409|]
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myosin heavy chain [Chlamydomonas reinhardtii]

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 ...
1-639 0e+00

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 cd01384:

Pssm-ID: 277568 [Multi-domain]  Cd Length: 647  Bit Score: 806.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPNLYGPAVIERYRSLPVaqggGEagsrLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:cd01384   18 TYTGNILIAVNPFKRLPHLYDAHMMEQYKGAPL----GE----LSPHVFAVADAAYRAMINEGKSQSILVSGESGAGKTE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  81 TAKLIMAGQAAAAAAGTGGGASsgmsgVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPvSGAVTGAAVRTYL 160
Cdd:cd01384   90 TTKMLMQYLAYMGGRAVTEGRS-----VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDD-AGRISGAAIRTYL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 161 LERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPPAASgFAYLARSSCVELPGQSNAEEYQHTRRAMSHIGLSEAQQ 240
Cdd:cd01384  164 LERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQ-FHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISEEEQ 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 241 RAVLGLVAAVLHLGNIAFRDGEhasvggGAEGAVVPPGAPRQALEAAAELLGVGAGALAEALTTRQIQTPEGAITTPLSA 320
Cdd:cd01384  243 DAIFRVVAAILHLGNIEFSKGE------EDDSSVPKDEKSEFHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDP 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 321 QAAADSRDSLAKSLYARLFDWLVAAVNAAVDEAHNGPAaagaahlSIGLLDIYGFESFEVNDLEQLCINLTNEKLQQHFN 400
Cdd:cd01384  317 DAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKR-------LIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFN 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 401 THVFKWEQAEYEREGVDWSYISFRDNADVL-ELLEGRLGLMTLLDEACRLPKATAEGLAHKYATTPavAGSSRFTPLKRP 479
Cdd:cd01384  390 QHVFKMEQEEYTKEEIDWSYIEFVDNQDVLdLIEKKPGGIIALLDEACMFPRSTHETFAQKLYQTL--KDHKRFSKPKLS 467
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 480 AASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWAPETEPagaagggasgggaasgagAGKQQSHV 559
Cdd:cd01384  468 RTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPRE------------------GTSSSSKF 529
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 560 SSVC---RRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYAAFLDHFWQ 636
Cdd:cd01384  530 SSIGsrfKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGL 609

                 ...
gi 159470529 637 LCP 639
Cdd:cd01384  610 LAP 612
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
1-639 0e+00

Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.


:

Pssm-ID: 214580 [Multi-domain]  Cd Length: 677  Bit Score: 707.77  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529     1 TYTGNILIAVNPFKPLPnLYGPAVIERYRslpvaqggGEAGSRLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:smart00242  37 TYIGLVLVAVNPYKQLP-IYTDEVIKKYR--------GKSRGELPPHVFAIADNAYRNMLNDKENQSIIISGESGAGKTE 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529    81 TAKLIMAGQAAAAAAGTGGGAssgmsgVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPvSGAVTGAAVRTYL 160
Cdd:smart00242 108 NTKKIMQYLASVSGSNTEVGS------VEDQILESNPILEAFGNAKTLRNNNSSRFGKFIEIHFDA-KGKIIGAKIETYL 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   161 LERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPPAASgFAYLARSSCVELPGQSNAEEYQHTRRAMSHIGLSEAQQ 240
Cdd:smart00242 181 LEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPED-YRYLNQGGCLTVDGIDDAEEFKETLNAMRVLGFSEEEQ 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   241 RAVLGLVAAVLHLGNIAFRDGehasvgGGAEGAVVPPGapRQALEAAAELLGVGAGALAEALTTRQIQTPEGAITTPLSA 320
Cdd:smart00242 260 ESIFKILAAILHLGNIEFEEG------RNDNAASTVKD--KEELSNAAELLGVDPEELEKALTKRKIKTGGEVITKPLNV 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   321 QAAADSRDSLAKSLYARLFDWLVAAVNAAVDeahngpaAAGAAHLSIGLLDIYGFESFEVNDLEQLCINLTNEKLQQHFN 400
Cdd:smart00242 332 EQALDARDALAKALYSRLFDWLVKRINQSLS-------FKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEKLQQFFN 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   401 THVFKWEQAEYEREGVDWSYISFRDNAD-VLELLEGRLGLMTLLDEACRLPKATAEGLAHKYATTpaVAGSSRFT-PLKR 478
Cdd:smart00242 405 QHVFKLEQEEYEREGIDWTFIDFFDNQDcIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQH--HKKHPHFSkPKKK 482
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   479 PAASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWAPETEpagaagggasgggaaSGAGAGKQQSh 558
Cdd:smart00242 483 GRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVS---------------NAGSKKRFQT- 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   559 VSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYAAFLDHFWQLC 638
Cdd:smart00242 547 VGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLL 626

                   .
gi 159470529   639 P 639
Cdd:smart00242 627 P 627
 
Name Accession Description Interval E-value
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
1-639 0e+00

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


Pssm-ID: 276835 [Multi-domain]  Cd Length: 647  Bit Score: 806.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPNLYGPAVIERYRSLPVaqggGEagsrLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:cd01384   18 TYTGNILIAVNPFKRLPHLYDAHMMEQYKGAPL----GE----LSPHVFAVADAAYRAMINEGKSQSILVSGESGAGKTE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  81 TAKLIMAGQAAAAAAGTGGGASsgmsgVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPvSGAVTGAAVRTYL 160
Cdd:cd01384   90 TTKMLMQYLAYMGGRAVTEGRS-----VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDD-AGRISGAAIRTYL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 161 LERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPPAASgFAYLARSSCVELPGQSNAEEYQHTRRAMSHIGLSEAQQ 240
Cdd:cd01384  164 LERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQ-FHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISEEEQ 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 241 RAVLGLVAAVLHLGNIAFRDGEhasvggGAEGAVVPPGAPRQALEAAAELLGVGAGALAEALTTRQIQTPEGAITTPLSA 320
Cdd:cd01384  243 DAIFRVVAAILHLGNIEFSKGE------EDDSSVPKDEKSEFHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDP 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 321 QAAADSRDSLAKSLYARLFDWLVAAVNAAVDEAHNGPAaagaahlSIGLLDIYGFESFEVNDLEQLCINLTNEKLQQHFN 400
Cdd:cd01384  317 DAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKR-------LIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFN 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 401 THVFKWEQAEYEREGVDWSYISFRDNADVL-ELLEGRLGLMTLLDEACRLPKATAEGLAHKYATTPavAGSSRFTPLKRP 479
Cdd:cd01384  390 QHVFKMEQEEYTKEEIDWSYIEFVDNQDVLdLIEKKPGGIIALLDEACMFPRSTHETFAQKLYQTL--KDHKRFSKPKLS 467
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 480 AASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWAPETEPagaagggasgggaasgagAGKQQSHV 559
Cdd:cd01384  468 RTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPRE------------------GTSSSSKF 529
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 560 SSVC---RRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYAAFLDHFWQ 636
Cdd:cd01384  530 SSIGsrfKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGL 609

                 ...
gi 159470529 637 LCP 639
Cdd:cd01384  610 LAP 612
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
1-639 0e+00

Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.


Pssm-ID: 214580 [Multi-domain]  Cd Length: 677  Bit Score: 707.77  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529     1 TYTGNILIAVNPFKPLPnLYGPAVIERYRslpvaqggGEAGSRLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:smart00242  37 TYIGLVLVAVNPYKQLP-IYTDEVIKKYR--------GKSRGELPPHVFAIADNAYRNMLNDKENQSIIISGESGAGKTE 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529    81 TAKLIMAGQAAAAAAGTGGGAssgmsgVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPvSGAVTGAAVRTYL 160
Cdd:smart00242 108 NTKKIMQYLASVSGSNTEVGS------VEDQILESNPILEAFGNAKTLRNNNSSRFGKFIEIHFDA-KGKIIGAKIETYL 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   161 LERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPPAASgFAYLARSSCVELPGQSNAEEYQHTRRAMSHIGLSEAQQ 240
Cdd:smart00242 181 LEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPED-YRYLNQGGCLTVDGIDDAEEFKETLNAMRVLGFSEEEQ 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   241 RAVLGLVAAVLHLGNIAFRDGehasvgGGAEGAVVPPGapRQALEAAAELLGVGAGALAEALTTRQIQTPEGAITTPLSA 320
Cdd:smart00242 260 ESIFKILAAILHLGNIEFEEG------RNDNAASTVKD--KEELSNAAELLGVDPEELEKALTKRKIKTGGEVITKPLNV 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   321 QAAADSRDSLAKSLYARLFDWLVAAVNAAVDeahngpaAAGAAHLSIGLLDIYGFESFEVNDLEQLCINLTNEKLQQHFN 400
Cdd:smart00242 332 EQALDARDALAKALYSRLFDWLVKRINQSLS-------FKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEKLQQFFN 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   401 THVFKWEQAEYEREGVDWSYISFRDNAD-VLELLEGRLGLMTLLDEACRLPKATAEGLAHKYATTpaVAGSSRFT-PLKR 478
Cdd:smart00242 405 QHVFKLEQEEYEREGIDWTFIDFFDNQDcIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQH--HKKHPHFSkPKKK 482
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   479 PAASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWAPETEpagaagggasgggaaSGAGAGKQQSh 558
Cdd:smart00242 483 GRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVS---------------NAGSKKRFQT- 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   559 VSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYAAFLDHFWQLC 638
Cdd:smart00242 547 VGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLL 626

                   .
gi 159470529   639 P 639
Cdd:smart00242 627 P 627
Myosin_head pfam00063
Myosin head (motor domain);
1-639 0e+00

Myosin head (motor domain);


Pssm-ID: 249554 [Multi-domain]  Cd Length: 679  Bit Score: 589.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529    1 TYTGNILIAVNPFKPLPnLYGPAVIERYRslpvaqggGEAGSRLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:pfam00063  30 TYSGLVLISVNPYKRLP-IYTEEPIGEYR--------GKRRGELPPHIFALADRAYRHMLRDKENQCIVISGESGAGKTE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   81 TAKLIMAGQAAAAAAGTGGGASsgmsgVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPvSGAVTGAAVRTYL 160
Cdd:pfam00063 101 NTKKLMQYLASVSGSTPSAVGP-----LEDQILQANPILEAFGNAKTLRNNNSSRFGKFIEIQFDA-TGSIVGGNIETYL 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  161 LERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPpAASGFAYLARSSCVELPGQSNAEEYQHTRRAMSHIGLSEAQQ 240
Cdd:pfam00063 175 LEKSRVVYQTPGERNFHIFYQLLAGASAQEKKELGLK-DPKDYAYLSQSGCYTVPGIDDAEEFKDTRSALKIIGFTDEEQ 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  241 RAVLGLVAAVLHLGNIAFRDGehasvggGAEGAVVPPGapRQALEAAAELLGVGAGALAEALTTRQIQTPEGAITTPLSA 320
Cdd:pfam00063 254 RSIFRVLAAILHLGNIKFKQD-------QNEEQAVVED--TEELEIIAGLLGVDPEELEKALLKRRIKTGRETVTKPQNV 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  321 QAAADSRDSLAKSLYARLFDWLVAAVNAAVDeahngpAAAGAAHLSIGLLDIYGFESFEVNDLEQLCINLTNEKLQQHFN 400
Cdd:pfam00063 325 EQARYARDALAKAIYSRLFDWIVGKINEALS------AKLQKAAAFIGVLDIYGFEIFEKNSFEQLCINYANEKLQQFFN 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  401 THVFKWEQAEYEREGVDWSYISFR-DNADVLELLEGRLG-LMTLLDEACRLPKATAEGLAHK----YATTPAVAGSSRFt 474
Cdd:pfam00063 399 HHMFKLEQEEYVREGIAWTFIDYGlDNQACIDLIEKKPPgILSLLDEECRFPKATDQTFLEKlldtFSSKHPHFSKPRF- 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  475 plKRPAASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWAPETEPAGAAGGGASGGGAASGAGAGK 554
Cdd:pfam00063 478 --GRGDTSFTVKHYAGDVEYNATGFLEKNKDPLFDDLISLLKSSSDPLVLELFPEEELDEEEFAGRYARLGCGKGKDGKK 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  555 QQ-SHVSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYAAFLDH 633
Cdd:pfam00063 556 SNfETAGSQFKESLGNLMKTLRSTNPHFVRCIKPNEKKAAGPFDSSLVLHQLRCLGVLEGIRIRRAGFPNRITFDEFLQR 635

                  ....*.
gi 159470529  634 FWQLCP 639
Cdd:pfam00063 636 YRLLAP 641
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1-639 1.20e-180

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 554.30  E-value: 1.20e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529    1 TYTGNILIAVNPFKPLPnLYGPAVIERYRSLPVAqgggeagsRLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:COG5022    97 TYSGLVLIAVNPYRDLG-IYTDDIIQSYSGKNRL--------ELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTE 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   81 TAKLIMAGQAAAAAAGTGGGASsgmsgVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPvSGAVTGAAVRTYL 160
Cdd:COG5022   168 NAKRIMQYLASVTSSSTVEISS-----IEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDE-NGEICGAKIETYL 241
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  161 LERSRVVAVNNPERSFHIFYQLVYGASAADRAaWRLPPAASGFAYLARSSCVELPGQSNAEEYQHTRRAMSHIGLSEAQQ 240
Cdd:COG5022   242 LEKSRVVHQNKNERNYHIFYQLLAGDPEELKK-LLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQ 320
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  241 RAVLGLVAAVLHLGNIAFRDGEhasvgggaEGAVVPPGapRQALEAAAELLGVGAGALAEALTTRQIQTPEGAITTPLSA 320
Cdd:COG5022   321 DQIFKILAAILHIGNIEFKEDR--------NGAAIFSD--NSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNL 390
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  321 QAAADSRDSLAKSLYARLFDWLVAAVNAAVDeahnGPAAAGAahlSIGLLDIYGFESFEVNDLEQLCINLTNEKLQQHFN 400
Cdd:COG5022   391 EQALAIRDSLAKALYSNLFDWIVDRINKSLD----HSAAASN---FIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFN 463
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  401 THVFKWEQAEYEREGVDWSYISFRDNADVLELLEGRLGL--MTLLDEACRLPKATAEGLAHKYATTPAVAGSSRFTPLKR 478
Cdd:COG5022   464 QHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKKNPLgiLSLLDEECVMPHATDESFTSKLAQRLNKNSNPKFKKSRF 543
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  479 PAASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWaPETEpagaagggasgggaasgAGAGKQQSH 558
Cdd:COG5022   544 RDNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLF-DDEE-----------------NIESKGRFP 605
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  559 -VSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYAAFLDHFWQL 637
Cdd:COG5022   606 tLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRIL 685

                  ..
gi 159470529  638 CP 639
Cdd:COG5022   686 SP 687
PTZ00014 PTZ00014
myosin-A; Provisional
6-637 2.17e-119

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 377.06  E-value: 2.17e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   6 ILIAVNPFKPLPNLyGPAVIERYRSLPVAqgggeagSRLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTETAKLI 85
Cdd:PTZ00014 132 LLVAINPFKDLGNT-TNDWIRRYRDAKDS-------DKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQI 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  86 MAGQAAAAAAGTGGGassgmsgVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPVSGAVTGAaVRTYLLERSR 165
Cdd:PTZ00014 204 MRYFASSKSGNMDLK-------IQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGS-IVAFLLEKSR 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 166 VVAVNNPERSFHIFYQLVYGASAADRAAWRLPPAaSGFAYLArSSCVELPGQSNAEEYQHTRRAMSHIGLSEAQQRAVLG 245
Cdd:PTZ00014 276 VVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSL-EEYKYIN-PKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFS 353
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 246 LVAAVLHLGNIAFrdgEHASVGGGAEGAVVPPGApRQALEAAAELLGVGAGALAEALTTRQIQTPEGAITTPLSAQAAAD 325
Cdd:PTZ00014 354 ILSGVLLLGNVEI---EGKEEGGLTDAAAISDES-LEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEM 429
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 326 SRDSLAKSLYARLFDWLVAAVNAAVDeahngpaAAGAAHLSIGLLDIYGFESFEVNDLEQLCINLTNEKLQQHFNTHVFK 405
Cdd:PTZ00014 430 LKDSLSKAVYEKLFLWIIRNLNATIE-------PPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFE 502
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 406 WEQAEYEREGVDWSYISFRDNADV-LELLEGRLGLMTLLDEACRLPKATAEGLAHKYATtpAVAGSSRFTPLKR-PAASF 483
Cdd:PTZ00014 503 RESKLYKDEGISTEELEYTSNESViDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNT--NLKNNPKYKPAKVdSNKNF 580
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 484 AVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWApetepagaagggasgGGAASGAGAGKQQShVSSVC 563
Cdd:PTZ00014 581 VIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFE---------------GVEVEKGKLAKGQL-IGSQF 644
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 159470529 564 RRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYAAFLDHFWQL 637
Cdd:PTZ00014 645 LNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYL 718
 
Name Accession Description Interval E-value
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
1-639 0e+00

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


Pssm-ID: 276835 [Multi-domain]  Cd Length: 647  Bit Score: 806.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPNLYGPAVIERYRSLPVaqggGEagsrLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:cd01384   18 TYTGNILIAVNPFKRLPHLYDAHMMEQYKGAPL----GE----LSPHVFAVADAAYRAMINEGKSQSILVSGESGAGKTE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  81 TAKLIMAGQAAAAAAGTGGGASsgmsgVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPvSGAVTGAAVRTYL 160
Cdd:cd01384   90 TTKMLMQYLAYMGGRAVTEGRS-----VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDD-AGRISGAAIRTYL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 161 LERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPPAASgFAYLARSSCVELPGQSNAEEYQHTRRAMSHIGLSEAQQ 240
Cdd:cd01384  164 LERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQ-FHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISEEEQ 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 241 RAVLGLVAAVLHLGNIAFRDGEhasvggGAEGAVVPPGAPRQALEAAAELLGVGAGALAEALTTRQIQTPEGAITTPLSA 320
Cdd:cd01384  243 DAIFRVVAAILHLGNIEFSKGE------EDDSSVPKDEKSEFHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDP 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 321 QAAADSRDSLAKSLYARLFDWLVAAVNAAVDEAHNGPAaagaahlSIGLLDIYGFESFEVNDLEQLCINLTNEKLQQHFN 400
Cdd:cd01384  317 DAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKR-------LIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFN 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 401 THVFKWEQAEYEREGVDWSYISFRDNADVL-ELLEGRLGLMTLLDEACRLPKATAEGLAHKYATTPavAGSSRFTPLKRP 479
Cdd:cd01384  390 QHVFKMEQEEYTKEEIDWSYIEFVDNQDVLdLIEKKPGGIIALLDEACMFPRSTHETFAQKLYQTL--KDHKRFSKPKLS 467
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 480 AASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWAPETEPagaagggasgggaasgagAGKQQSHV 559
Cdd:cd01384  468 RTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPRE------------------GTSSSSKF 529
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 560 SSVC---RRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYAAFLDHFWQ 636
Cdd:cd01384  530 SSIGsrfKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGL 609

                 ...
gi 159470529 637 LCP 639
Cdd:cd01384  610 LAP 612
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
1-639 0e+00

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


Pssm-ID: 276950 [Multi-domain]  Cd Length: 633  Bit Score: 695.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPnLYGPAVIERYRSLPvaqgggeAGSRLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:cd00124   18 TYVGDILVAVNPFKWLP-LYSEEVMEKYRGKG-------RSADLPPHVFAVADAAYRAMLRDGQNQSILISGESGAGKTE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  81 TAKLIMAGQAAAAAAGTGGGASSGMSgVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPvSGAVTGAAVRTYL 160
Cdd:cd00124   90 TTKLVLKYLAALSGSGSSKSSSSASS-IEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDP-TGRLVGASIETYL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 161 LERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPPAASGF---AYLARSSCVELPGQSNAEEYQHTRRAMSHIGLSE 237
Cdd:cd00124  168 LEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYylnDYLNSSGCDRIDGVDDAEEFQELLDALDVLGFSD 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 238 AQQRAVLGLVAAVLHLGNIAFRDGEHASVGGGAEgavvppgAPRQALEAAAELLGVGAGALAEALTTRQIQTPEGAITTP 317
Cdd:cd00124  248 EEQDSIFRILAAILHLGNIEFEEDEEDEDSSAEV-------ADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITKP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 318 LSAQAAADSRDSLAKSLYARLFDWLVAAVNAAVDeahngPAAAGAAHLSIGLLDIYGFESFEVNDLEQLCINLTNEKLQQ 397
Cdd:cd00124  321 LTVEQAEDARDALAKALYSRLFDWLVNRINAALS-----PTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQ 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 398 HFNTHVFKWEQAEYEREGVDWSYISFRDNADVLELLEGRLGL-MTLLDEACRLPKATAEGLAHKYATTPAVAgSSRFTPL 476
Cdd:cd00124  396 FFNQHVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKPLGiLSLLDEECLFPKGTDATFLEKLYSAHGSH-PRFFSKK 474
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 477 KRPAASFAVEHYAGKPWAAAANWLDKNRDYVvaehaalgaaaRQPLVRELwapetepagaagggasgggaasgagagkqq 556
Cdd:cd00124  475 RKAKLEFGIKHYAGDVTYDADGFLEKNKDTL-----------PPDLVDLL------------------------------ 513
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 557 sHVSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYAAFLDHFWQ 636
Cdd:cd00124  514 -RSGSQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRI 592

                 ...
gi 159470529 637 LCP 639
Cdd:cd00124  593 LAP 595
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
2-634 0e+00

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


Pssm-ID: 276834 [Multi-domain]  Cd Length: 647  Bit Score: 573.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   2 YT--GNILIAVNPFKPLPnLYGPAVIERYRSlpvaqgggeaGSRLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKT 79
Cdd:cd01383   17 YTkaGPVLIAVNPFKDVP-LYGNEFITAYRQ----------KLLDSPHVYAVADTAYREMMRDEINQSIIISGESGAGKT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  80 ETAKLIMAGQAAAAAAGTGggassgmsgVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDpVSGAVTGAAVRTY 159
Cdd:cd01383   86 ETAKIAMQYLAALGGGSSG---------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFD-AAGKICGAKIQTY 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 160 LLERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPpAASGFAYLARSSCVELPGQSNAEEYQHTRRAMSHIGLSEAQ 239
Cdd:cd01383  156 LLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLK-SASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKED 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 240 QRAVLGLVAAVLHLGNIAF--RDGEHASVGGGAEgavvppgaprqALEAAAELLGVGAGALAEALTTRQIQTPEGAITTP 317
Cdd:cd01383  235 QEHIFQMLAAVLWLGNISFqvIDNENHVEVVADE-----------AVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKK 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 318 LSAQAAADSRDSLAKSLYARLFDWLVAAVNA--AVDEAHNGpaaagaahLSIGLLDIYGFESFEVNDLEQLCINLTNEKL 395
Cdd:cd01383  304 LTLQQAIDARDALAKAIYASLFDWLVEQINKslEVGKRRTG--------RSISILDIYGFESFQKNSFEQLCINYANERL 375
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 396 QQHFNTHVFKWEQAEYEREGVDWSYISFRDNAD-VLELLEGRLGLMTLLDEACRLPKATAEGLAHKYATtpAVAGSSRFT 474
Cdd:cd01383  376 QQHFNRHLFKLEQEEYELDGIDWTKVDFEDNQEcLDLIEKKPLGLISLLDEESNFPKATDLTFANKLKQ--HLKSNSCFK 453
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 475 plKRPAASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWAPETEpagaagggaSGGGAASGAGAGK 554
Cdd:cd01383  454 --GERGGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFASKMLD---------ASRKALPLTKASG 522
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 555 QQSHVSSVCRR---QLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYAAFL 631
Cdd:cd01383  523 SDSQKQSVATKfkgQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFA 602

                 ...
gi 159470529 632 DHF 634
Cdd:cd01383  603 RRY 605
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
1-639 0e+00

class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276831 [Multi-domain]  Cd Length: 629  Bit Score: 552.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPnLYGPAVIERYRSLPVAQgggeagsrLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:cd01380   19 TYCGIVLVAINPYEDLP-IYGEDIIQAYSGQNMGE--------LDPHIFAIAEEAYRQMARDEKNQSIIVSGESGAGKTV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  81 TAKLIMAGQAAAAAAGTGGGAssgmsgVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPvSGAVTGAAVRTYL 160
Cdd:cd01380   90 SAKYAMRYFATVGGSSSGETQ------VEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDK-NYRIIGANMRTYL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 161 LERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPPAaSGFAYLARSSCVELPGQSNAEEYQHTRRAMSHIGLSEAQQ 240
Cdd:cd01380  163 LEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSA-EDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEEQ 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 241 RAVLGLVAAVLHLGNIAFRDGEHasvgggaEGAVVPPGAPrqALEAAAELLGVGAGALAEALTTRQIQTPEGAITTPLSA 320
Cdd:cd01380  242 MEIFRILAAILHLGNVEIKATRN-------DSASISPDDE--HLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTL 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 321 QAAADSRDSLAKSLYARLFDWLVAAVNAAVDEAhngpaAAGAAHLSIGLLDIYGFESFEVNDLEQLCINLTNEKLQQHFN 400
Cdd:cd01380  313 QQAIVARDALAKHIYAQLFDWIVDRINKALASP-----VKEKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFN 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 401 THVFKWEQAEYEREGVDWSYISFRDNADVLELLEGRLGLMTLLDEACRLPKATAEGLAHKYATTPAVAGSSRFTPLKRPA 480
Cdd:cd01380  388 QHVFKLEQEEYVKEEIEWSFIDFYDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNKHFKKPRFSN 467
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 481 ASFAVEHYAGKPWAAAANWLDKNRDYVVaehaalgaaarQPLVRELWAPEtepagaagggasgggaasgagagKQQSHVS 560
Cdd:cd01380  468 TAFIVKHFADDVEYQVEGFLEKNRDTVS-----------EEHLNVLKASK-----------------------NRKKTVG 513
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 159470529 561 SVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYAAFLDHFWQLCP 639
Cdd:cd01380  514 SQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLP 592
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
1-639 0e+00

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


Pssm-ID: 276849 [Multi-domain]  Cd Length: 661  Bit Score: 544.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPnLYGPAVIERYRslpvaqggGEAGSRLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:cd14883   18 TYTGSILVAVNPYKELP-IYTQDIVKQYF--------GKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGESGAGKTE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  81 TAKLIMAGQAAAAAAGTGggassgmsgVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPvSGAVTGAAVRTYL 160
Cdd:cd14883   89 TTKLILQYLCAVTNNHSW---------VEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDA-SGHIKGAIIQDYL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 161 LERSRVVAVNNPERSFHIFYQLVYGASAAD--RAAWRLPPAASgFAYLARSSCVELPGQSNAEEYQHTRRAMSHIGLSEA 238
Cdd:cd14883  159 LEQSRITFQAPGERNYHVFYQLLAGAKHSKelKEKLKLGEPED-YHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPEE 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 239 QQRAVLGLVAAVLHLGNIAFRDGEhasvggGAEGAVVPpgAPRQALEAAAELLGVGAGALAEALTTRQIQTPEGAITTPL 318
Cdd:cd14883  238 MQEGIFSVLSAILHLGNLTFEDID------GETGALTV--EDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPL 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 319 SAQAAADSRDSLAKSLYARLFDWLVAAVNAAVdeaHNGPAAagaaHLSIGLLDIYGFESFEVNDLEQLCINLTNEKLQQH 398
Cdd:cd14883  310 KVQEARDNRDAMAKALYSRTFAWLVNHINSCT---NPGQKN----SRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKF 382
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 399 FNTHVFKWEQAEYEREGVDWSYISFRDNAD-VLELLEGRLGLMTLLDEACRLPKAT---------AEGLAHKYATTPAva 468
Cdd:cd14883  383 FNHYVFKLEQEEYEKEGINWSHIVFTDNQEcLDLIEKPPLGILKLLDEECRFPKGTdltyleklhAAHEKHPYYEKPD-- 460
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 469 gssrftpLKRPAASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWAPETEpAGAAGGGASGGGAAS 548
Cdd:cd14883  461 -------RRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDL-LALTGLSISLGGDTT 532
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 549 GAGAGKQQSHVSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYA 628
Cdd:cd14883  533 SRGTSKGKPTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFK 612
                        650
                 ....*....|.
gi 159470529 629 AFLDHFWQLCP 639
Cdd:cd14883  613 EFVDRYLCLDP 623
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
1-639 0e+00

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


Pssm-ID: 276829 [Multi-domain]  Cd Length: 652  Bit Score: 539.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPnLYGPAVIERYRslpvaqggGEAGSRLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:cd01378   18 TYIGHVLISVNPFKDLG-IYTDEVLESYR--------GKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGESGAGKTE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  81 TAKLIMAGQAAAAAAGTGGGASsgmsgVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPvSGAVTGAAVRTYL 160
Cdd:cd01378   89 ASKRIMQYIAAVSGGSESEVER-----VKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDF-KGEPVGGHITNYL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 161 LERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPPAASgFAYLARSSCVELPGQSNAEEYQHTRRAMSHIGLSEAQQ 240
Cdd:cd01378  163 LEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQ-YYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEEQ 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 241 RAVLGLVAAVLHLGNIAFRDGEHAsvgggaeGAVVPPGAPrqaLEAAAELLGVGAGALAEALTTRQIQTPEGA---ITTP 317
Cdd:cd01378  242 DSIFRILAAILHLGNIQFAEDEEG-------NAAISDTSV---LDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVP 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 318 LSAQAAADSRDSLAKSLYARLFDWLVAAVNAAVDeahngpAAAGAAHLSIGLLDIYGFESFEVNDLEQLCINLTNEKLQQ 397
Cdd:cd01378  312 LNVEQAAYARDALAKAIYSRLFDWIVERINKSLA------AKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQ 385
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 398 HFNTHVFKWEQAEYEREGVDWSYISFRDNADV-LELLEGRLGLMTLLDEAC-RLPKAT----AEGLAHKYATTP-AVAGS 470
Cdd:cd01378  386 IFIELTLKAEQEEYVREGIEWTPIKYFNNKIIcDLIEEKPPGIFAILDDAClTAGDATdqtfLQKLNQLFSNHPhFECPS 465
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 471 SRFTPlkrPAASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWAPETEPagaagggasgggaasga 550
Cdd:cd01378  466 GHFEL---RRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDL----------------- 525
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 551 GAGKQQSHVSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYAAF 630
Cdd:cd01378  526 DSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKF 605

                 ....*....
gi 159470529 631 LDHFWQLCP 639
Cdd:cd01378  606 LERYKLLSP 614
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
1-631 0e+00

class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276951 [Multi-domain]  Cd Length: 662  Bit Score: 533.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPnLYGPAVIERYRslpvaqggGEAGSRLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:cd01377   18 TYSGLFCVAVNPYKRLP-IYTEEVIDKYK--------GKRREEMPPHIFAIADNAYRNMLQDRENQSILITGESGAGKTE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  81 -TAKLIMAGQAAAAAAGTGGGASSGMSGVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPvSGAVTGAAVRTY 159
Cdd:cd01377   89 nTKKVIQYLASVAASSKKKKESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGS-TGKIAGADIETY 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 160 LLERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPPAASGFAYLaRSSCVELPGQSNAEEYQHTRRAMSHIGLSEAQ 239
Cdd:cd01377  168 LLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFL-SQGELTIDGVDDAEEFKLTDEAFDILGFSEEE 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 240 QRAVLGLVAAVLHLGNIAF---RDGEHASVGGGAEgavvppgaprqaLEAAAELLGVGAGALAEALTTRQIQTPEGAITT 316
Cdd:cd01377  247 KMSIFKIVAAILHLGNIKFkqrRREEQAELDGTEE------------ADKAAHLLGVNSSDLLKALLKPRIKVGREWVTK 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 317 PLSAQAAADSRDSLAKSLYARLFDWLVAAVNAAVDEAHNGpaaagaaHLSIGLLDIYGFESFEVNDLEQLCINLTNEKLQ 396
Cdd:cd01377  315 GQNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKR-------QYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQ 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 397 QHFNTHVFKWEQAEYEREGVDWSYISF------------RDNADVlellegrlglMTLLDEACRLPKATAEGLAHKYATT 464
Cdd:cd01377  388 QFFNHHMFVLEQEEYKKEGIEWTFIDFgldlqptidlieKPNMGI----------LSILDEECVFPKATDKTFVEKLYSN 457
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 465 paVAGSSRFTPLKRP---AASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWAPETEPagaaggga 541
Cdd:cd01377  458 --HLGKSKNFKKPKPkksEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEES-------- 527
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 542 sggGAASGAGAGKQQSH--VSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACA 619
Cdd:cd01377  528 ---GGGGGKKKKKGGSFrtVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRK 604
                        650
                 ....*....|..
gi 159470529 620 GFAYRRPYAAFL 631
Cdd:cd01377  605 GFPNRIIFAEFK 616
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
1-639 6.78e-178

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 [Multi-domain]  Cd Length: 648  Bit Score: 523.36  E-value: 6.78e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPnLYGPAVIERYRSLPVaqggGEagsrLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:cd01381   18 TYTGSILVAVNPYQILP-IYTAEQIRLYRNKKI----GE----LPPHIFAIADNAYTNMKRNKRDQCVVISGESGAGKTE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  81 TAKLIMAGQAAAAAAGTGggassgmsgVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPvSGAVTGAAVRTYL 160
Cdd:cd01381   89 STKLILQYLAAISGQHSW---------IEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNK-NGVIEGAKIEQYL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 161 LERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPpAASGFAYLARSSCVELPGQSNAEEYQHTRRAMSHIGLSEAQQ 240
Cdd:cd01381  159 LEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELG-DASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEEI 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 241 RAVLGLVAAVLHLGNIAFRdgehASVGGGAEGAVVPPGAprqALEAAAELLGVGAGALAEALTTRQIQTPEGAITTPLSA 320
Cdd:cd01381  238 WDIFKLLAAILHLGNIKFE----ATVVDNLDASEVRDPP---NLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSA 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 321 QAAADSRDSLAKSLYARLFDWLVAAVNAAVdeahNGPAAAGAAHLSIGLLDIYGFESFEVNDLEQLCINLTNEKLQQHFN 400
Cdd:cd01381  311 EQALDVRDAFVKGIYGRLFIWIVNKINSAI----YKPRGTDSSRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFV 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 401 THVFKWEQAEYEREGVDWSYISFRDNADVL-ELLEGRLGLMTLLDEACRLPKATAEGLAHKYATTPAvAGSSRFTPLKRP 479
Cdd:cd01381  387 RHIFKLEQEEYDKEGINWQHIEFVDNQDVLdLIALKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHG-NNKNYLKPKSDL 465
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 480 AASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWAPETEPagaagggasgggaasGAGAGKQQSHV 559
Cdd:cd01381  466 NTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISM---------------GSETRKKSPTL 530
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 560 SSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYAAFLDHFWQLCP 639
Cdd:cd01381  531 SSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVP 610
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
1-639 3.61e-172

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: 508.93  E-value: 3.61e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPNLYGPAVIERYRslpvaqggGEAGSRLPPHVYATACNAYRNMMAEGAG----QAILVTGESGA 76
Cdd:cd14890   18 TYVGPILISINPYKSIPDLYSEERMLLYH--------GTTAGELPPHVFAIADHAYTQLIQSGVLdpsnQSIIISGESGA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  77 GKTETAKLIM----------AGQAAAAAAGTGGGASSGMSGVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDp 146
Cdd:cd14890   90 GKTEATKIIMqylaritsgfAQGASGEGEAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGKFIEIQFD- 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 147 VSGAVTGAAVRTYLLERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPPAASGFAYlaRSSCVELPGQSNAEEYQHT 226
Cdd:cd14890  169 HHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYL--RGECSSIPSCDDAKAFAET 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 227 RRAMSHIGLSEAQQRAVLGLVAAVLHLGNIAFRDGEHASVGGGAegavvppgAPRQALEAAAELLGVGAGALAEALTTRQ 306
Cdd:cd14890  247 IRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDA--------TTLQSLKLAAELLGVNEDALEKALLTRQ 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 307 IQTPEGAITTPLSAQAAADSRDSLAKSLYARLFDWLVAAVNAAVDEahnGPAAAGaahlSIGLLDIYGFESFEVNDLEQL 386
Cdd:cd14890  319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISS---PDDKWG----FIGVLDIYGFEKFEWNTFEQL 391
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 387 CINLTNEKLQQHFNTHVFKWEQAEYEREGVDWSYISFRDNAD----VLELLEGRLGLMTLLDEACRLPKATAEG--LAHK 460
Cdd:cd14890  392 CINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQAclelIEGKVNGKPGIFITLDDCWRFKGEEANKkfVSQL 471
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 461 YAT-------TPAVAGSSR----FTPLKRPAASFAVEHYAGKPWAAAANWLDKNRDYVVAEhaalgaaarqplVRELWAP 529
Cdd:cd14890  472 HASfgrksgsGGTRRGSSQhphfVHPKFDADKQFGIKHYAGDVIYDASGFNEKNNETLNAE------------MKELIKQ 539
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 530 ETEPAgaagggasgggaasgagagkQQSHVSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGG 609
Cdd:cd14890  540 SRRSI--------------------REVSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSG 599
                        650       660       670
                 ....*....|....*....|....*....|
gi 159470529 610 VMEAVRIACAGFAYRRPYAAFLDHFWQLCP 639
Cdd:cd14890  600 MMEAIQIRQQGFALREEHDSFFYDFQVLLP 629
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
1-631 7.59e-168

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 [Multi-domain]  Cd Length: 644  Bit Score: 497.38  E-value: 7.59e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPnLYGPAVIERYRSLPVaqgggeagSRLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:cd14872   18 TNVGTILISVNPFKRLP-LYTPTVMDQYMHKGP--------KEMPPHTYNIADDAYRAMIVDAMNQSILISGESGAGKTE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  81 TAKLIMAGQAAAAAAGTGggassgmsgVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDpVSGAVTGAAVRTYL 160
Cdd:cd14872   89 ATKQCLSFFAEVAGSTNG---------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFD-NRGRICGASTENYL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 161 LERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPPAasgFAYLARSSCVELPGQSNAEEYQHTRRAMSHIGLSEAQQ 240
Cdd:cd14872  159 LEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSAA---YGYLSLSGCIEVEGVDDVADFEEVVLAMEQLGFDDADI 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 241 RAVLGLVAAVLHLGNIAFrdgehaSVGGGAEGAVVPPGAPRQALEAAAELLGVGAGALAEALTTRQIQTPEGAIT-TPLS 319
Cdd:cd14872  236 NNVMSLIAAILKLGNIEF------ASGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIKGCDPTrIPLT 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 320 AQAAADSRDSLAKSLYARLFDWLVAAVNAAVDeahngpAAAGAAHLSIGLLDIYGFESFEVNDLEQLCINLTNEKLQQHF 399
Cdd:cd14872  310 PAQATDACDALAKAAYSRLFDWLVKKINESMR------PQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHF 383
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 400 NTHVFKWEQAEYEREGVDWSYISFRDNADVL-ELLEGRLGLMTLLDEACRLPKATAEGLAHKYATTPAVAGSSRFTPLKR 478
Cdd:cd14872  384 NQYTFKLEEALYQSEGVKFEHIDFIDNQPVLdLIEKKQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRT 463
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 479 PAASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWAPetepagaagggasgggaaSGAGAGKQQSH 558
Cdd:cd14872  464 SRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPP------------------SEGDQKTSKVT 525
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 159470529 559 VSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYAAFL 631
Cdd:cd14872  526 LGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFL 598
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
1-639 1.21e-167

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


Pssm-ID: 276866 [Multi-domain]  Cd Length: 655  Bit Score: 497.39  E-value: 1.21e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPnLYGPAVIERYRSLPVAQGGGEagSRLPPHVYATACNAYRNMM----AEGAGQAILVTGESGA 76
Cdd:cd14901   18 TSTGAILVAINPFRRLP-LYDDETKEAYYEHGERRAAGE--RKLPPHVYAVADKAFRAMLfasrGQKCDQSILVSGESGA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  77 GKTETAKLIMAGQAAAAAAGTGGGASSGMSGVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPvSGAVTGAAV 156
Cdd:cd14901   95 GKTETTKIIMNYLASVSSATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRLGFAS-SGSLLGASI 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 157 RTYLLERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPPAASgFAYLARSSCVE-LPGQSNAEEYQHTRRAMSHIGL 235
Cdd:cd14901  174 STYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEE-YKYLNSSQCYDrRDGVDDSVQYAKTRHAMTTIGM 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 236 SEAQQRAVLGLVAAVLHLGNIAFrdgehASVGGGAEGAVVPPGAprqALEAAAELLGVGAGALAEALTTRQIQTPEGAIT 315
Cdd:cd14901  253 SPDEQISVLQLVAAVLHLGNLCF-----VKKDGEGGTFSMSSLA---NVRAACDLLGLDMDVLEKTLCTREIRAGGEYIT 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 316 TPLSAQAAADSRDSLAKSLYARLFDWLVAAVNAAVdeAHNGPaaaGAAHLSIGLLDIYGFESFEVNDLEQLCINLTNEKL 395
Cdd:cd14901  325 MPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESI--AYSES---TGASRFIGIVDIFGFEIFATNSLEQLCINFANEKL 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 396 QQHFNTHVFKWEQAEYEREGVDWSYISFRDN-ADVLELLEGRLGLMTLLDEACRLPKATAEGLAHKYATTpaVAGSSRF- 473
Cdd:cd14901  400 QQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNdACVAMFEARPTGLFSLLDEQCLLPRGNDEKLANKYYDL--LAKHASFs 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 474 -TPLKRPAASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVrelwapetepagaagggasgggaasgaga 552
Cdd:cd14901  478 vSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFL----------------------------- 528
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 553 gkqQSHVSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYAAFLD 632
Cdd:cd14901  529 ---SSTVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVH 605

                 ....*..
gi 159470529 633 HFWQLCP 639
Cdd:cd14901  606 TYSCLAP 612
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
1-628 4.29e-164

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 [Multi-domain]  Cd Length: 649  Bit Score: 487.91  E-value: 4.29e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPNLYGPAVIERYRslpvaqggGEAGSRLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:cd01382   18 TYVANILIAVNPYFDIPKLYSSETIKSYQ--------GKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGESGAGKTE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  81 TAKLIMAGQAAAAAAGTGGgassgmsgVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPvSGAVTGAAVRTYL 160
Cdd:cd01382   90 STKYILRYLTESWGSGAGP--------IEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNE-KSSVVGGFVSHYL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 161 LERSRVVAVNNPERSFHIFYQLVYGASAADRAAwrlppaasgfayLARSSCVElpgqsNAEEYQHTRRAMSHIGLSEAQQ 240
Cdd:cd01382  161 LEKSRICVQSKEERNYHIFYRLCAGAPEDLREK------------LLKDPLLD-----DVGDFIRMDKAMKKIGLSDEEK 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 241 RAVLGLVAAVLHLGNIAFRDgEHASVGGGAEgavVPPGApRQALEAAAELLGVGAGALAEALTTRQIQTPEG-----AIT 315
Cdd:cd01382  224 LDIFRVVAAVLHLGNIEFEE-NGSDSGGGCN---VKPKS-EQSLEYAAELLGLDQDELRVSLTTRVMQTTRGgakgtVIK 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 316 TPLSAQAAADSRDSLAKSLYARLFDWLVAAVNAAVdeahngPAAAGAAhlSIGLLDIYGFESFEVNDLEQLCINLTNEKL 395
Cdd:cd01382  299 VPLKVEEANNARDALAKAIYSKLFDHIVNRINQCI------PFETSSY--FIGVLDIAGFEYFEVNSFEQFCINYCNEKL 370
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 396 QQHFNTHVFKWEQAEYEREGVDWSYISFRDNAD-VLELLEGRLGLMTLLDEACRLPKATAEGLA------HKYATTPAVA 468
Cdd:cd01382  371 QQFFNERILKEEQELYEKEGLGVKEVEYVDNQDcIDLIEAKLVGILDLLDEESKLPKPSDQHFTsavhqkHKNHFRLSIP 450
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 469 GSSRFTPLK--RPAASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWAPETEPagaagggasggga 546
Cdd:cd01382  451 RKSKLKIHRnlRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNN------------- 517
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 547 asgAGAGKQQS------HVSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAG 620
Cdd:cd01382  518 ---NKDSKQKAgklsfiSVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGG 594

                 ....*...
gi 159470529 621 FAYRRPYA 628
Cdd:cd01382  595 FPSRTSFH 602
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
1-639 1.07e-163

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: 487.28  E-value: 1.07e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPNLYGPAVIERYRSlpvaqgggEAGSRlPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:cd14888   18 TFTGPILIAVNPFKTIPGLYSDEMLLKFIQ--------PSISK-SPHVFSTASSAYQGMCNNKKSQTILISGESGAGKTE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  81 TAKLIMAGQAAAAAAGTGGGASsgmsgVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFF--------DPVSGAVT 152
Cdd:cd14888   89 STKYVMKFLACAGSEDIKKRSL-----VEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFsklkskrmSGDRGRLC 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 153 GAAVRTYLLERSRVVAVNNPERSFHIFYQLV--------YGASAADRAAWRLPPAASG--------------FAYLARSS 210
Cdd:cd14888  164 GAKIQTYLLEKVRVCDQQEGERNYHIFYQLCaaareaknTGLSYEENDEKLAKGADAKpisidmssfephlkFRYLTKSS 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 211 CVELPGQSNAEEYQHTRRAMSHIGLSEAQQRAVLGLVAAVLHLGNIAFRDGEHASvgggaEGAVVPPGApRQALEAAAEL 290
Cdd:cd14888  244 CHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACS-----EGAVVSASC-TDDLEKVASL 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 291 LGVGAGALAEALTTRQIQTPEGAITTPLSAQAAADSRDSLAKSLYARLFDWLVAAVNAAVDEAHNGpaaagaAHLSIGLL 370
Cdd:cd14888  318 LGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDN------SLLFCGVL 391
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 371 DIYGFESFEVNDLEQLCINLTNEKLQQHFNTHVFKWEQAEYEREGVDWSYISFRDNAD-VLELLEGRLGLMTLLDEACRL 449
Cdd:cd14888  392 DIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDcVDLLQEKPLGIFCMLDEECFV 471
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 450 PKATAEGLAHKYATTpaVAGSSRFTPLKRPAASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWAP 529
Cdd:cd14888  472 PGGKDQGLCNKLCQK--HKGHKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSA 549
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 530 etepagaagggaSGGGAASGAGAGKQQSHVSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGG 609
Cdd:cd14888  550 ------------YLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGG 617
                        650       660       670
                 ....*....|....*....|....*....|
gi 159470529 610 VMEAVRIACAGFAYRRPYAAFLDHFWQLCP 639
Cdd:cd14888  618 VLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
1-639 2.79e-162

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: 483.51  E-value: 2.79e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPNLYGPAVIERYRSLPVAQgggeagsrLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:cd14903   18 TYTGDICIAVNPYQWLPELYTEEQHSKYLNKPKEE--------LPPHVYATSVAAYNHMKRSGRNQSILVSGESGAGKTE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  81 TAKLIMAGQAAAAAAGTGGGAssgmsgveQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPvSGAVTGAAVRTYL 160
Cdd:cd14903   90 TTKILMNHLATIAGGLNDSTI--------KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDK-NGTLVGAKCRTYL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 161 LERSRVVAVNNPERSFHIFYQLVYGASAADRAAwrlPPAASGFAYLARSSCVELPGQSNAEEYQHTRRAMSHIGLSEAQQ 240
Cdd:cd14903  161 LEKTRVISHERPERNYHIFYQLLASPDVEERLF---LDSANECAYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEEKQ 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 241 RAVLGLVAAVLHLGNIAFR----DGEHASVGGGAEGAVvppgaprqaleAAAELLGVGAGALAEALTTRQIQTPEGAITT 316
Cdd:cd14903  238 EVLFEVLAGILHLGQLQIQskpnDDEKSAIAPGDQGAV-----------YATKLLGLSPEALEKALCSRTMRAAGDVYTV 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 317 PLSAQAAADSRDSLAKSLYARLFDWLVAAVNAAVDeahngpAAAGAAHlSIGLLDIYGFESFEVNDLEQLCINLTNEKLQ 396
Cdd:cd14903  307 PLKKDQAEDCRDALAKAIYSNVFDWLVATINASLG------NDAKMAN-HIGVLDIFGFEHFKHNSFEQFCINYANEKLQ 379
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 397 QHFNTHVFKWEQAEYEREGVDWSYISFRDNADVLELLEGRLGLMTLLDEACRLPKATAEGLAHKYATtpavAGSSRFTPL 476
Cdd:cd14903  380 QKFTQDVFKTVQIEYEEEGIRWAHIDFADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSS----IHKDEQDVI 455
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 477 KRPAAS---FAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWAPETEPAGAAGGGASGGGAASGAGAG 553
Cdd:cd14903  456 EFPRTSrtqFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRGGAL 535
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 554 kQQSHVSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYAAFLDH 633
Cdd:cd14903  536 -TTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDK 614

                 ....*.
gi 159470529 634 FWQLCP 639
Cdd:cd14903  615 FWLFLP 620
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
1-637 8.16e-160

class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276857 [Multi-domain]  Cd Length: 656  Bit Score: 476.94  E-value: 8.16e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPNLYG-PAVIEryrslpvaQGGGEA-GSRLPPHVYATACNAYRNMMAEGAG----QAILVTGES 74
Cdd:cd14892   18 TFTADILISINPYKSIPLLYDvPGFDS--------QRKEEAtASSPPPHVFSIAERAYRAMKGVGKGqgtpQSIVVSGES 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  75 GAGKTETAKLIM----AGQAAAAAAGTGGGASSGMSGVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPvSGA 150
Cdd:cd14892   90 GAGKTEASKYIMkylaTASKLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNS-DGR 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 151 VTGAAVRTYLLERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPPAASgFAYLARSSCVELPGQSNAEEYQHTRRAM 230
Cdd:cd14892  169 IAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAES-FLFLNQGNCVEVDGVDDATEFKQLRDAM 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 231 SHIGLSEAQQRAVLGLVAAVLHLGNIAFRdgEHASVGGgaegaVVPPGAPRQALEAAAELLGVGAGALAEALTTRQIQTP 310
Cdd:cd14892  248 EQLGFDAEFQRPIFEVLAAVLHLGNVRFE--ENADDED-----VFAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTSTA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 311 EGAIT-TPLSAQAAADSRDSLAKSLYARLFDWLVAAVNAAVDE---AHNGPAAAGAAHLSIGLLDIYGFESFEVNDLEQL 386
Cdd:cd14892  321 RGSVLeIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQqtsGVTGGAASPTFSPFIGILDIFGFEIMPTNSFEQL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 387 CINLTNEKLQQHFNTHVFKWEQAEYEREGVDWSYISFRDNAD-VLELLEGRLGLMTLLDEACRLP-KATAEGLAHKY--- 461
Cdd:cd14892  401 CINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDcLDLIQKKPLGLLPLLEEQMLLKrKTTDKQLLTIYhqt 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 462 -ATTPAVAGSSRFTPLKrpaasFAVEHYAGKPWAAAANWLDKNRDYVvaehaalgaaarQPLVRELWapetepagaaggg 540
Cdd:cd14892  481 hLDKHPHYAKPRFECDE-----FVLRHYAGDVTYDVHGFLAKNNDNL------------HDDLRDLL------------- 530
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 541 asgggaasgagagkqqsHVSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAG 620
Cdd:cd14892  531 -----------------RSSSKFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREG 593
                        650
                 ....*....|....*..
gi 159470529 621 FAYRRPYAAFLDHFWQL 637
Cdd:cd14892  594 FPIRRQFEEFYEKFWPL 610
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
1-638 2.50e-153

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: 459.43  E-value: 2.50e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLpNLYGPAVIERYRslpvaqggGEAGSRLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:cd01379   18 TYIGDILIAVNPFQNL-GIYTEEHSRLYR--------GAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGESGAGKTE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  81 TAKLIMAGQAAAAAAGTGGgassgmsgVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPvSGAVTGAAVRTYL 160
Cdd:cd01379   89 SANLLVQQLTVLGKANNRT--------LEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTS-TGAVTGARISEYL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 161 LERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPPAASGFAYLARSSCVELPG---QSNAEEYQHTRRAMSHIGLSE 237
Cdd:cd01379  160 LEKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAKYKLPENKPPRYLQNDGLTVQDIvnnSGNREKFEEIEQCFKVIGFTK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 238 AQQRAVLGLVAAVLHLGNIAFRdgEHASVGGGAEGAVVPPgapRQALEAAAELLGVGAGALAEALTTRQIQTPEGAITTP 317
Cdd:cd01379  240 EEVDSVYSILAAILHIGDIEFT--EVESNHQTDKSSRISN---PEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRN 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 318 LSAQAAADSRDSLAKSLYARLFDWLVAAVNAAVdeAHNGPAAAGAahLSIGLLDIYGFESFEVNDLEQLCINLTNEKLQQ 397
Cdd:cd01379  315 NTVEEATDARDAMAKALYGRLFSWIVNRINSLL--KPDRSASDEP--LSIGILDIFGFENFQKNSFEQLCINIANEQIQY 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 398 HFNTHVFKWEQAEYEREGVDWSYISFRDNADVLELLEGRLGLM-TLLDEACRLPKATAEGLAHKYATTPAvagSSRFTPL 476
Cdd:cd01379  391 YFNQHIFAWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKPMGLlALLDEESRFPKATDQTLVEKFHNNIK---SKYYWRP 467
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 477 KRPAASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELwapetepagaagggasgggaasgagagkqq 556
Cdd:cd01379  468 KSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQT------------------------------ 517
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 557 shVSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYAAFLDHFWQ 636
Cdd:cd01379  518 --VATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYF 595

                 ..
gi 159470529 637 LC 638
Cdd:cd01379  596 LA 597
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
1-637 2.34e-152

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: 458.34  E-value: 2.34e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPNLYGPAVIERYRSLPVAQGGGEAGSRLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:cd14907   18 TYVGPTLIVMNPYKQIDNLFSEEVMQMYKEQIIQNGEYFDIKKEPPHIYAIAALAFKQLFENNKKQAIVISGESGAGKTE 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  81 TAKLIM-----------AGQAAAAAAGTGGGASSGMSGVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPVSG 149
Cdd:cd14907   98 NAKYAMkfltqlsqqeqNSEEVLTLTSSIRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSSRFGKYVSILVDKKKR 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 150 AVTGAAVRTYLLERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPPAASGF--AYLARSSCVELPGQSNAEEYQHTR 227
Cdd:cd14907  178 KILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSGDryDYLKKSNCYEVDTINDEKLFKEVQ 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 228 RAMSHIGLSEAQQRAVLGLVAAVLHLGNIAFRDGEHASVGggaegavVPPGAPRQALEAAAELLGVGAGALAEALTTRQI 307
Cdd:cd14907  258 QSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNS-------PCCVKNKETLQIIAKLLGIDEEELKEALTTKIR 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 308 QTPEGAITTPLSAQAAADSRDSLAKSLYARLFDWLVAAVNAAV-DEAHNGPAAAGAAHLSIGLLDIYGFESFEVNDLEQL 386
Cdd:cd14907  331 KVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImPKDEKDQQLFQNKYLSIGLLDIFGFEVFQNNSFEQL 410
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 387 CINLTNEKLQQHFNTHVFKWEQAEYEREGVD--WSYISFRDNADVLELLEGRLGLM-TLLDEACRLPKATAEGLAHKYAT 463
Cdd:cd14907  411 CINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSYTDNQDVIDLLDKPPIGIfNLLDDSCKLATGTDEKLLNKIKK 490
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 464 TPavAGSSRFT-PLKRPAASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWAPETEpagaagggAS 542
Cdd:cd14907  491 QH--KNNSKLIfPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGEDG--------SQ 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 543 GGGAASGAGAGKQQSHVSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFA 622
Cdd:cd14907  561 QQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYP 640
                        650
                 ....*....|....*
gi 159470529 623 YRRPYAAFLDHFWQL 637
Cdd:cd14907  641 YRKSYEDFYKQYSLL 655
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
1-634 1.77e-150

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: 453.06  E-value: 1.77e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLpNLYGPAVIERYRslpvaqggGEAGSRLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:cd01387   18 TYIGSILVSVNPYKMF-DIYGLEQVQQYS--------GRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGESGSGKTE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  81 TAKLIMAGQAAAAAAGTGGgassgmsgVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDpvSGAVTGAAVRTYL 160
Cdd:cd01387   89 ATKLIMQYLAAVNQRRNNL--------VTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE--GGVIVGAITSQYL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 161 LERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPPAASGFaYLARSSCVELPGQSNAEEYQHTRRAMSHIGLSEAQQ 240
Cdd:cd01387  159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYF-YLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQ 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 241 RAVLGLVAAVLHLGNIAF-----RDG-EHASVGGGAEgavvppgaprqaLEAAAELLGVGAGALAEALTTRQIQTPEGAI 314
Cdd:cd01387  238 DSIFRILASVLHLGNVYFhkrqlRHGqEGVSVGSDAE------------IQWVAHLLQISPEGLQKALTFKVTETRRERI 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 315 TTPLSAQAAADSRDSLAKSLYARLFDWLVAAVNAAVdeaHNGPAAAgaahLSIGLLDIYGFESFEVNDLEQLCINLTNEK 394
Cdd:cd01387  306 FTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIV---YSGTQDT----LSIAILDIFGFEDLSENSFEQLCINYANEN 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 395 LQQHFNTHVFKWEQAEYEREGVDWSYISFRDNADV-LELLEGRLGLMTLLDEACRLPKATAEGLAHKYATTPAVagSSRF 473
Cdd:cd01387  379 LQYYFNKHVFKLEQEEYIREQIDWTEIAFADNQPViNLISKKPVGILHILDDECNFPQATDHSFLEKCHYHHAL--NELY 456
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 474 TPLKRPAASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELwapeTEPAGAAGGGASGGGAASGAGAG 553
Cdd:cd01387  457 SKPRMPLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHL----FSSHRAQTDKAPPRLGKGRFVTM 532
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 554 KQQSH-VSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYAAFLD 632
Cdd:cd01387  533 KPRTPtVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFID 612

                 ..
gi 159470529 633 HF 634
Cdd:cd01387  613 RY 614
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
1-631 5.37e-150

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: 451.56  E-value: 5.37e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPNLYGPAVIERYRSLPVaqggGEagsrLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:cd14873   18 TYIGSILASVNPYQPIAGLYEPATMEQYSRRHL----GE----LPPHIFAIANECYRCLWKRHDNQCILISGESGAGKTE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  81 TAKLIMAGQAAAAAAGTGGGASSGMSGVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPvSGAVTGAAVRTYL 160
Cdd:cd14873   90 STKLILKFLSVISQQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQ-KGNIQGGRIVDYL 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 161 LERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPpAASGFAYLARSSCVELPGQSNAEEYQHTRRAMSHIGLSEAQQ 240
Cdd:cd14873  169 LEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-TPENYHYLNQSGCVEDKTISDQESFREVITAMEVMQFSKEEV 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 241 RAVLGLVAAVLHLGNIAFRDgehasvgggAEGAVVPPgapRQALEAAAELLGVGAGALAEALTTRQIQTPEGAITTPLSA 320
Cdd:cd14873  248 REVSRLLAGILHLGNIEFIT---------AGGAQVSF---KTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNV 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 321 QAAADSRDSLAKSLYARLFDWLVAAVNAAVdeahngpaaAGAAHL-SIGLLDIYGFESFEVNDLEQLCINLTNEKLQQHF 399
Cdd:cd14873  316 QQAVDSRDSLAMALYARCFEWVIKKINSRI---------KGKEDFkSIGILDIFGFENFEVNHFEQFNINYANEKLQEYF 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 400 NTHVFKWEQAEYEREGVDWSYISFRDNADVLELLEGRLGLMTLLDEACRLPKAT----AEGLAHKYATTPavagssrfTP 475
Cdd:cd14873  387 NKHIFSLEQLEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATdstlLEKLHSQHANNH--------FY 458
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 476 LKRPAAS--FAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWapetepagaAGGGASGGGAASGAGAG 553
Cdd:cd14873  459 VKPRVAVnnFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLF---------EHVSSRNNQDTLKCGSK 529
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 159470529 554 KQQSHVSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYAAFL 631
Cdd:cd14873  530 HRRPTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFY 607
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
1-639 3.32e-148

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: 446.44  E-value: 3.32e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPnLYGPAVIERYRSLPVAqgggeagSRLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:cd14897   18 TYIGDILVAVNPCKPLP-IFDKKHHEEYSNLSVR-------SQRPPHLFWIADQAYRRLLETGRNQCILVSGESGAGKTE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  81 TAKLIMAGQAAAAAAGTGGgassgmsgVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPvSGAVTGAAVRTYL 160
Cdd:cd14897   90 STKYMIKHLMKLSPSDDSD--------LLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTE-NGQLLGAKIDDYL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 161 LERSRVVAVNNPERSFHIFYQLVYGASAaDRAAWRLPPAASGFAYLaRSSCVELPGQSNAEEYQHTR-------RAMSHI 233
Cdd:cd14897  161 LEKSRVVHRGNGEKNFHIFYALFAGMSR-DRLLYYFLEDPDCHRIL-RDDNRNRPVFNDSEELEYYRqmfhdltNIMKLI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 234 GLSEAQQRAVLGLVAAVLHLGNIAFRDGEHAsvgggaEGAVVppgAPRQALEAAAELLGVGAGALAEALTTRQIQTPEGA 313
Cdd:cd14897  239 GFSEEDISVIFTILAAILHLTNIVFIPDEDT------DGVTV---ADEYPLHAVAKLLGIDEVELTEALISNVNTIRGER 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 314 ITTPLSAQAAADSRDSLAKSLYARLFDWLVAAVNAAVDEAHNGPAAAGAAhlSIGLLDIYGFESFEVNDLEQLCINLTNE 393
Cdd:cd14897  310 IQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMTRGP--SIGILDMSGFENFKINSFDQLCINLSNE 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 394 KLQQHFNTHVFKWEQAEYEREGVDWSYISFRDNADVLELLEGRLG-LMTLLDEACRLPKATAEGLAHK----YATTPava 468
Cdd:cd14897  388 RLQQYFNDYVFPRERSEYEIEGIEWRDIEYHDNDDVLELFFKKPLgILPLLDEESTFPQSTDSSLVQKlnkyCGESP--- 464
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 469 gssRFTPLKRPAASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWApetepagaagggasgggaas 548
Cdd:cd14897  465 ---RYVASPGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT-------------------- 521
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 549 gagagkqqSHVssvcRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYA 628
Cdd:cd14897  522 --------SYF----KRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYE 589
                        650
                 ....*....|.
gi 159470529 629 AFLDHFWQLCP 639
Cdd:cd14897  590 DFVKRYKEICD 600
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
1-639 4.66e-144

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: 437.42  E-value: 4.66e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPnLYGPAVIERYRSLP-VAQGGGEAGSRLPPHVYATACNAYRNMMAEG-AGQAILVTGESGAGK 78
Cdd:cd14908   18 TWTGPVLIAVNPFQRLP-LYGKEILESYRQEGlLRSQGIESPQALGPHVFAIADRSYRQMMSEIrASQSILISGESGAGK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  79 TETAKLIM---AGQAAAAAAGTGGGASSGMSGVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPvSGAVTGAA 155
Cdd:cd14908   97 TESTKIVMlylTTLGNGEEGAPNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKFIELGFNR-AGNLLGAK 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 156 VRTYLLERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPPAASG-------FAYLARSSCVELPGQSNAEEYQHTRR 228
Cdd:cd14908  176 VQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITGglqlpneFHYTGQGGAPDLREFTDEDGLVYTLK 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 229 AMSHIGLSEAQQRAVLGLVAAVLHLGNIAFRDGEHAsvgGGAEGAVVppgAPRQALEAAAELLGVGAGALAEALTTRQIQ 308
Cdd:cd14908  256 AMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEED---GAAEIAEE---GNEKCLARVAKLLGVDVDKLLRALTSKIIV 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 309 TPEGAITTPLSAQAAADSRDSLAKSLYARLFDWLVAAVNAAVDEAHNGPAAAgaahlSIGLLDIYGFESFEVNDLEQLCI 388
Cdd:cd14908  330 VRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIRS-----SVGVLDIFGFECFAHNSFEQLCI 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 389 NLTNEKLQQHFNTHVFKWEQAEYEREGVDWSYISFRDNAD-VLELLEGRLGLMTLLDEACRLP-----KATAEGLAHKYA 462
Cdd:cd14908  405 NFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDcLDTIQAKKKGILTMLDDECRLGirgsdANYASRLYETYL 484
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 463 TTP--AVAGSSRF--TPLKRPAASFAVEHYAGK-PWAAAANWLDKNRDYVvaehaalgaaarqPL-VRELWAPETEpaga 536
Cdd:cd14908  485 PEKnqTHSENTRFeaTSIQKTKLIFAVRHFAGQvQYTVETTFCEKNKDEI-------------PLtADSLFESGQQ---- 547
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 537 agggasgggaasgagagkqqshvssvCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRI 616
Cdd:cd14908  548 --------------------------FKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRV 601
                        650       660
                 ....*....|....*....|...
gi 159470529 617 ACAGFAYRRPYAAFLDHFWQLCP 639
Cdd:cd14908  602 ARSGYPVRLPHKDFFKRYRMLLP 624
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
1-628 3.40e-142

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 [Multi-domain]  Cd Length: 645  Bit Score: 431.39  E-value: 3.40e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPNlygPAVieryrSLPVAQGGGEAgsrlPPHVYATACNAYRNMMAEGA---GQAILVTGESGAG 77
Cdd:cd14891   20 TFMANVLIAVNPLRRLPE---PDK-----SDYINTPLDPC----PPHPYAIAEMAYQQMCLGSGrmqNQSIVISGESGAG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  78 KTETAKLIM----------AGQAAAAAAGTGGGASSGMSGVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPV 147
Cdd:cd14891   88 KTETSKIILrflttravggKKASGQDIEQSSKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFGKFMKLQFTKD 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 148 SGAVTGAAVRTYLLERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPPAASgFAYLARSSCVELPGQSNAEEYQHTR 227
Cdd:cd14891  168 KFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPED-FIYLNQSGCVSDDNIDDAANFDNVV 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 228 RAMSHIGLSEAQQRAVLGLVAAVLHLGNIAFRDGEHASvgGGAEGAVVppgAPRQALEAAAELLGVGAGALAEALTTRQI 307
Cdd:cd14891  247 SALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSE--GEAEIASE---SDKEALATAAELLGVDEEALEKVITQREI 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 308 QTPEGAITTPLSAQAAADSRDSLAKSLYARLFDWLVAAVNAAVDEahngpaaaGAAHLS-IGLLDIYGFESFE-VNDLEQ 385
Cdd:cd14891  322 VTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH--------DPDPLPyIGVLDIFGFESFEtKNDFEQ 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 386 LCINLTNEKLQQHFNTHVFKWEQAEYEREGVDWSYISFRDNAD-VLELLEGRLGLMTLLDEACRLPKAT----AEGLaHK 460
Cdd:cd14891  394 LLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNREcLDLIASKPNGILPLLDNEARNPNPSdaklNETL-HK 472
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 461 yattpAVAGSSRFtPLKRPA---ASFAVEHYAGKPWAAAANWLDKNRDYVvaehaalgaaarqplvrelwaPETepagaa 537
Cdd:cd14891  473 -----THKRHPCF-PRPHPKdmrEMFIVKHYAGTVSYTIGSFIDKNNDII---------------------PED------ 519
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 538 gggasgggaasgagaGKQQSHVSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIA 617
Cdd:cd14891  520 ---------------FEDLLASSAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVL 584
                        650
                 ....*....|.
gi 159470529 618 CAGFAYRRPYA 628
Cdd:cd14891  585 KVGLPTRVTYA 595
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
1-639 1.19e-141

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: 431.41  E-value: 1.19e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPnLYGPAVIERY--RSLpvaqggGEagsrLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGK 78
Cdd:cd01385   18 TYVGSILIAVNPFKFLP-IYNPKYVKMYqnRRL------GK----LPPHIFAIADVAYHAMLRKKKNQCIVISGESGSGK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  79 TETAKLIMAGQAAAAAAGTGGGassgmsgVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPvSGAVTGAAVRT 158
Cdd:cd01385   87 TESTNFLLHHLTALSQKGYGSG-------VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRE-NGMVRGAVVEK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 159 YLLERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPPAASgFAYLARSSCVELPGQSNAEEYQHTRRAMSHIGLSEA 238
Cdd:cd01385  159 YLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPED-YHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPE 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 239 QQRAVLGLVAAVLHLGNIAF------RDgEHASVGggaegavvppgaPRQALEAAAELLGVGAGALAEALTTRQIQTPEG 312
Cdd:cd01385  238 TQRQIFSVLSAVLHLGNIEYkkkayhRD-ESVTVG------------NPEVLDIISELLRVKEETLLEALTTKKTVTVGE 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 313 AITTPLSAQAAADSRDSLAKSLYARLFDWLVAAVNAAVdeaHNGPAAAGAAHLSIGLLDIYGFESFEVNDLEQLCINLTN 392
Cdd:cd01385  305 TLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHAL---LNKKDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYAN 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 393 EKLQQHFNTHVFKWEQAEYEREGVDWSYISFRDNAD-VLELLEGRLGLMTLLDEACRLPKATAEGLAHKYATTPAVAGSS 471
Cdd:cd01385  382 EHLQYYFNQHIFKLEQEEYKKEGISWHNIEYTDNTGcLQLISKKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYY 461
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 472 RFTPLKRPAasFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVREL------------------------- 526
Cdd:cd01385  462 EKPQVMEPA--FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELigidpvavfrwavlrafframaafr 539
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 527 -----WAPETEPAGAAGGGASGGGAASGAGAGKQQShVSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYS 601
Cdd:cd01385  540 eagrrRAQRTAGHSLTLHDRTTKSLLHLHKKKKPPS-VSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELV 618
                        650       660       670
                 ....*....|....*....|....*....|....*...
gi 159470529 602 LQQLRCGGVMEAVRIACAGFAYRRPYAAFLDHFWQLCP 639
Cdd:cd01385  619 LRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLP 656
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
1-637 6.75e-138

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 [Multi-domain]  Cd Length: 627  Bit Score: 419.71  E-value: 6.75e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPNLYGPAVIERYRSL--PVAQGGGEAGSR-LPPHVYATACNAYRNMM----AEGAGQAILVTGE 73
Cdd:cd14900   18 TNTGAILLAVNPFQKLPGLYSSDTMAKYLLSfeARSSSTRNKGSDpMPPHIYQVAGEAYKAMMlglnGVMSDQSILVSGE 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  74 SGAGKTETAKLIMA--GQAAAAAAGTGGGASSGMSGVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPvSGAV 151
Cdd:cd14900   98 SGSGKTESTKFLMEylAQAGDNNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSRFGKFIKLHFTS-GGRL 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 152 TGAAVRTYLLERSRVVAVNNPERSFHIFYQLVYGASAADRAAwrlppaasgfaylarsscvelpgqsnaEEYQHTRRAMS 231
Cdd:cd14900  177 TGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKR---------------------------DMYRRVMDAMD 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 232 HIGLSEAQQRAVLGLVAAVLHLGNIAFRDGEHASVGGGAEGAVVPpgAPRQALEAAAELLGVGAGALAEALTTRQIQTPE 311
Cdd:cd14900  230 IIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLAP--SSIWSRDAAATLLSVDATKLEKALSVRRIRAGT 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 312 GAITTPLSAQAAADSRDSLAKSLYARLFDWLVAAVNAAVdeAHNGPAAAGAAHLSIGLLDIYGFESFEVNDLEQLCINLT 391
Cdd:cd14900  308 DFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFL--KMDDSSKSHGGLHFIGILDIFGFEVFPKNSFEQLCINFA 385
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 392 NEKLQQHFNTHVFKWEQAEYEREGVDWSYISFRDNAD-VLELLEGRLGLMTLLDEACRLPKATAEGLAHK-YAttpAVAG 469
Cdd:cd14900  386 NETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDcVNLISQRPTGILSLIDEECVMPKGSDTTLASKlYR---ACGS 462
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 470 SSRFTP--LKRPAASFAVEHYAGKPWAAAANWLDKNRDYVvaehaalgaaaRQPLVREL---WAPETepagaagggasgg 544
Cdd:cd14900  463 HPRFSAsrIQRARGLFTIVHYAGHVEYSTDGFLEKNKDVL-----------HQEAVDLFvygLQFKE------------- 518
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 545 gaasgagagkqqshvssvcrrQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYR 624
Cdd:cd14900  519 ---------------------QLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIR 577
                        650
                 ....*....|...
gi 159470529 625 RPYAAFLDHFWQL 637
Cdd:cd14900  578 LLHDEFVARYFSL 590
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
1-624 9.35e-138

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


Pssm-ID: 276869 [Multi-domain]  Cd Length: 653  Bit Score: 420.12  E-value: 9.35e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPNLYGPAVIERYRSLPVaqgggeagSRLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:cd14904   18 TYTNDIVIALNPYKWIDNLYGDHLHEQYLKKPR--------DKLQPHVYATSTAAYKHMLTNEMNQSILVSGESGAGKTE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  81 TAKLIMAGQAAAAAAGTGGGASsgmsgveqKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDpVSGAVTGAAVRTYL 160
Cdd:cd14904   90 TTKIVMNHLASVAGGRKDKTIA--------KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFD-GRGKLIGAKCETYL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 161 LERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPPAASgFAYLARSSC-VELPGQSNAEEYQHTRRAMSHIGLSEAQ 239
Cdd:cd14904  161 LEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQ-YQYLGDSLAqMQIPGLDDAKLFASTQKSLSLIGLDNDA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 240 QRAVLGLVAAVLHLGNIAFRDGehasvggGAEGAVVPPGaprQALEAAAELLGVGAGALAEALTTRQIQTPEGAITTPLS 319
Cdd:cd14904  240 QRTLFKILSGVLHLGEVMFDKS-------DENGSRISNG---SQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLA 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 320 AQAAADSRDSLAKSLYARLFDWLVAAVNAAVDEAHNGPAAagaahlSIGLLDIYGFESFEVNDLEQLCINLTNEKLQQHF 399
Cdd:cd14904  310 PVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKG------QIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKF 383
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 400 NTHVFKWEQAEYEREGVDWSYISFRDNADVLELLEGRLGLMTLLDEACRLPKATAEGLAHKYATTPAVAGSS---RFTPL 476
Cdd:cd14904  384 TTDVFKTVEEEYIREGLQWDHIEYQDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQTKKDNesiDFPKV 463
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 477 KRpaASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWAPETEPagaagggaSGGGAASGAGAGKQQ 556
Cdd:cd14904  464 KR--TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAP--------SETKEGKSGKGTKAP 533
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 159470529 557 SHVSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYR 624
Cdd:cd14904  534 KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSR 601
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
1-634 5.33e-135

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 [Multi-domain]  Cd Length: 659  Bit Score: 413.15  E-value: 5.33e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPnLYGPAVIERYRSlpvaqgggEAGSRLPPHVYATACNAYRNMMAEGA----GQAILVTGESGA 76
Cdd:cd14889   18 TYVGDILVAINPFKYLH-IYEKEVSQKYKC--------EKKSSLPPHIFAVADRAYQSMLGRLArgpkNQCIVISGESGA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  77 GKTETAKLIMAGQAAAAAAGTGggassgmsgVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDpvSGAVTGAAV 156
Cdd:cd14889   89 GKTESTKLLLRQIMELCRGNSQ---------LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR--NGHVKGAKI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 157 RTYLLERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRL-PPAAsgFAYLA-RSSCVELPgQSNAEEYQHTRRAMSHIG 234
Cdd:cd14889  158 NEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLlDPGK--YRYLNnGAGCKREV-QYWKKKYDEVCNAMDMVG 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 235 LSEAQQRAVLGLVAAVLHLGNIAFRDGEhasvgggaEGAVVPPGAPRQALEAAAELLGVGAGALAEALTTRQIQTPEGAI 314
Cdd:cd14889  235 FTEQEEVDMFTILAGILSLGNITFEMDD--------DEALKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQI 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 315 TTPLSAQAAADSRDSLAKSLYARLFDWLVAAVNAAVdeahnGPAAAGAAHLS-IGLLDIYGFESFEVNDLEQLCINLTNE 393
Cdd:cd14889  307 QRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL-----APKDDSSVELReIGILDIFGFENFAVNRFEQACINLANE 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 394 KLQQHFNTHVFKWEQAEYEREGVDWSYISFRDNADVLEL-LEGRLGLMTLLDEACRLPKATAEGLAHKYATTpaVAGSSR 472
Cdd:cd14889  382 QLQYFFNHHIFLMEQKEYKKEGIDWKEITYKDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKLNIH--FKGNSY 459
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 473 FTPLKRPAASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWAPETEPAGAAGGGASGGGAASGAGA 552
Cdd:cd14889  460 YGKSRSKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGSDNFN 539
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 553 GKQQSHVSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYAAFLD 632
Cdd:cd14889  540 STRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAE 619

                 ..
gi 159470529 633 HF 634
Cdd:cd14889  620 RY 621
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
1-634 3.77e-133

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: 410.05  E-value: 3.77e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPNLYGPAVIERYRSLPVAQGGGEAGSRLPPHVYATACNAYRNMM-AEGAGQAILVTGESGAGKT 79
Cdd:cd14902   18 TSIGDILVALNPLKPLPDLYSESQLNAYKASMTSTSPVSQLSELPPHVFAIGGKAFGGLLkPERRNQSILVSGESGSGKT 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  80 ETAKLIMAGQAAAAAAGTGGGASSGMSGVEQK-ILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDpVSGAVTGAAVRT 158
Cdd:cd14902   98 ESTKFLMQFLTSVGRDQSSTEQEGSDAVEIGKrILQTNPILESFGNAQTIRNDNSSRFGKFIKIQFG-ANNEIVGAQIVS 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 159 YLLERSRVVAVNNPERSFHIFYQLVYGASA--AD----RAAWRLPPAASGFAYLARSSCVElpgQSNAEEYQHTRRAMSH 232
Cdd:cd14902  177 YLLEKVRLLHQSPEERSFHIFYELLEGADKtlLDllglQKGGKYELLNSYGPSFARKRAVA---DKYAQLYVETVRAFED 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 233 IGLSEAQQRAVLGLVAAVLHLGNIAFrdgehaSVGGGAEGAVVPPGAPRQALEAAAELLGVGAGALAEALTTRQIQTPEG 312
Cdd:cd14902  254 TGVGELERLDIFKILAALLHLGNVNF------TAENGQEDATAVTAASRFHLAKCAELMGVDVDKLETLLSSREIKAGVE 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 313 AITTPLSAQAAADSRDSLAKSLYARLFDWLVAAVNAAVD--EAHNGPAAAGAAHLSIGLLDIYGFESFEVNDLEQLCINL 390
Cdd:cd14902  328 VMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfDSAVSISDEDEELATIGILDIFGFESLNRNGFEQLCINY 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 391 TNEKLQQHFNTHVFKWEQAEYEREGVDWSYISFRDNADVLELLEGRLGLM-TLLDEACRLPKATAEGLahkyattpavag 469
Cdd:cd14902  408 ANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSNGLfSLLDQECLMPKGSNQAL------------ 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 470 SSRFTPLKRPAASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWAPETepagAAGGGASGGGAASG 549
Cdd:cd14902  476 STKFYRYHGGLGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADEN----RDSPGADNGAAGRR 551
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 550 AGAGKQQSHVSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYAA 629
Cdd:cd14902  552 RYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHAS 631

                 ....*
gi 159470529 630 FLDHF 634
Cdd:cd14902  632 FIELF 636
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
1-639 7.60e-133

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: 407.86  E-value: 7.60e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPnLYGPAVIERYRslpvaqggGEAGSRLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:cd14920   18 TYSGLFCVVINPYKNLP-IYSENIIEMYR--------GKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  81 TAKLIMAGQAAAAAAGTGGGASSGMSGVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDpVSGAVTGAAVRTYL 160
Cdd:cd14920   89 NTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFD-VTGYIVGANIETYL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 161 LERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPPaASGFAYLARSScVELPGQSNAEEYQHTRRAMSHIGLSEAQQ 240
Cdd:cd14920  168 LEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEG-FNNYRFLSNGY-IPIPGQQDKDNFQETMEAMHIMGFSHEEI 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 241 RAVLGLVAAVLHLGNIAFRDGEHasvgggAEGAVVPPGAPRQALeaaAELLGVGAGALAEALTTRQIQTPEGAITTPLSA 320
Cdd:cd14920  246 LSMLKVVSSVLQFGNISFKKERN------TDQASMPENTVAQKL---CHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 321 QAAADSRDSLAKSLYARLFDWLVAAVNAAVDEAHNgpaaAGAAHlsIGLLDIYGFESFEVNDLEQLCINLTNEKLQQHFN 400
Cdd:cd14920  317 EQADFAVEALAKATYERLFRWLVHRINKALDRTKR----QGASF--IGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 401 THVFKWEQAEYEREGVDWSYISF----RDNADVLELLEGRLGLMTLLDEACRLPKATAEGLAHKYAttpAVAGS-SRFTP 475
Cdd:cd14920  391 HTMFILEQEEYQREGIEWNFIDFgldlQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLV---QEQGShSKFQK 467
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 476 LKRP--AASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWAPETEPAGAAGGGASGGGAASGAGAG 553
Cdd:cd14920  468 PRQLkdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKT 547
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 554 KQQ--SHVSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYAAFL 631
Cdd:cd14920  548 KKGmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 627

                 ....*...
gi 159470529 632 DHFWQLCP 639
Cdd:cd14920  628 QRYEILTP 635
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
1-634 8.52e-130

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: 399.61  E-value: 8.52e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPNLYGPAVIERYRSLPVAQGggeagsrLPPHVYATACNAYRNMMA--EGAGQAILVTGESGAGK 78
Cdd:cd14880   18 TNAGCTLVALNPFKPVPQLYSPELMREYHAAPQPQK-------LKPHIFTVGEQTYRNVKSliEPVNQSIVVSGESGAGK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  79 TETAKLIMAGQAAAAAAGTGGGASSGMSGVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPvSGAVTGAAVRT 158
Cdd:cd14880   91 TWTSRCLMKFYAVVAASPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNR-AQQMTGAAVQT 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 159 YLLERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPPAASgFAYLARSscvelpgQSNAEE--YQHTRRAMSHIGLS 236
Cdd:cd14880  170 YLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAA-FSWLPNP-------ERNLEEdcFEVTREAMLHLGID 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 237 EAQQRAVLGLVAAVLHLGNIAFRDGEHASVgggaegAVVPPGAPRQALEAAAELLGVGAGALAEALTTRQIQTPEG--AI 314
Cdd:cd14880  242 TPTQNNIFKVLAGLLHLGNIQFADSEDEAQ------PCQPMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQqqVF 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 315 TTPLSAQAAADSRDSLAKSLYARLFDWLVAAVNAAVdeahngPAAAGAAHLSIGLLDIYGFESFEVNDLEQLCINLTNEK 394
Cdd:cd14880  316 KKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSI------CADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEK 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 395 LQQHFNTHVFKWEQAEYEREGVDWSYISFRDNAD-VLELLEGRLGLMTLLDEACRLPKATAEGLAHKYATTpAVAGSSRF 473
Cdd:cd14880  390 LQQHFVAHYLRAQQEEYAVEGLEWSFINYQDNQTcLDLIEGSPISICSLINEECRLNRPSSAAQLQTRIES-ALAGNPCL 468
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 474 TPLK-RPAASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWAPETEPAGAAGGGASGGGAASGaga 552
Cdd:cd14880  469 GHNKlSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQSRAPVLT--- 545
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 553 gkqqshVSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYAAFLD 632
Cdd:cd14880  546 ------VVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVE 619

                 ..
gi 159470529 633 HF 634
Cdd:cd14880  620 RY 621
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
1-639 2.07e-129

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: 398.97  E-value: 2.07e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPnLYGPAVIERYRslpvaqggGEAGSRLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:cd14911   18 TYSGLFCVVVNPYKKLP-IYTEKIMERYK--------GIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGESGAGKTE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  81 TAKLIMA---------GQAAAAAAGTGGGASSGMSGVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDpVSGAV 151
Cdd:cd14911   89 NTKKVIQflayvaaskPKGSGAVPHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-ASGFI 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 152 TGAAVRTYLLERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPPAASgFAYLaRSSCVELPGQSNAEEYQHTRRAMS 231
Cdd:cd14911  168 SGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKS-YAFL-SNGSLPVPGVDDYAEFQATVKSMN 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 232 HIGLSEAQQRAVLGLVAAVLHLGNIAFRDGEHAsvgggaEGAVVPPGAPRQALeaaAELLGVGAGALAEALTTRQIQTPE 311
Cdd:cd14911  246 IMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNN------DQATLPDNTVAQKI---AHLLGLSVTDMTRAFLTPRIKVGR 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 312 GAITTPLSAQAAADSRDSLAKSLYARLFDWLVAAVNAAVDEAHNgpaaAGAAHlsIGLLDIYGFESFEVNDLEQLCINLT 391
Cdd:cd14911  317 DFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKR----QGASF--IGILDMAGFEIFELNSFEQLCINYT 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 392 NEKLQQHFNTHVFKWEQAEYEREGVDWSYISF-RDNADVLELLEGRLGLMTLLDEACRLPKATAEGLAHKYATTPAVAGS 470
Cdd:cd14911  391 NEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPK 470
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 471 SRFTPLkRPAASFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWApETEPAGAAGGGASGGGAASGA 550
Cdd:cd14911  471 FMKTDF-RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWK-DAEIVGMAQQALTDTQFGART 548
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 551 GAGKQQShVSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRCGGVMEAVRIACAGFAYRRPYAAF 630
Cdd:cd14911  549 RKGMFRT-VSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEF 627

                 ....*....
gi 159470529 631 LDHFWQLCP 639
Cdd:cd14911  628 RQRYELLTP 636
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
3-634 3.09e-128

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: 397.02  E-value: 3.09e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   3 TGNILIAVNPFKPLPNLYGpavIERYRS-LPvaqgggeAGSRLPPHVYATACNAYRNMM-------AEGAGQAILVTGES 74
Cdd:cd14895   20 SGAVLIAVNPFKHIPGLYD---LHKYREeMP-------GWTALPPHVFSIAEGAYRSLRrrlhepgASKKNQTILVSGES 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  75 GAGKTETAKLIMAGQAAAAAAGTGGGASSGMSGVE-QKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDP----VSG 149
Cdd:cd14895   90 GAGKTETTKFIMNYLAESSKHTTATSSSKRRRAISgSELLSANPILESFGNARTLRNDNSSRFGKFVRMFFEGheldTSL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 150 AVTGAAVRTYLLERSRVVAVNNPERSFHIFYQLVYGASAADRAAWRLPP-AASGFAYLARSSC-VELPGQSNAEEYQHTR 227
Cdd:cd14895  170 RMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELlSAQEFQYISGGQCyQRNDGVRDDKQFQLVL 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 228 RAMSHIGLSEAQQRAVLGLVAAVLHLGNIAF---RDGEHASVGGGA----EGAVVPPG--APRQALEAAAELLGVGAGAL 298
Cdd:cd14895  250 QSMKVLGFTDVEQAAIWKILSALLHLGNVLFvasSEDEGEEDNGAAsapcRLASASPSslTVQQHLDIVSKLFAVDQDEL 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 299 AEALTTRQIQTPEGAITTPLSAQAAADSRDSLAKSLYARLFDWLVAAVNAA---VDEAHN-GPAAAGAAHLSIGLLDIYG 374
Cdd:cd14895  330 VSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSAspqRQFALNpNKAANKDTTPCIAVLDIFG 409
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 375 FESFEVNDLEQLCINLTNEKLQQHFNTHVFKWEQAEYEREGVDWSYISFRDNAD-VLELLEGRLGLMTLLDEACRLPKAT 453
Cdd:cd14895  410 FEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVcLEMLEQRPSGIFSLLDEECVVPKGS 489
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 454 AEGLAHKYATTpaVAGSSRFTPLKRPAASFA--VEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWAPet 531
Cdd:cd14895  490 DAGFARKLYQR--LQEHSNFSASRTDQADVAfqIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGKTSDAHLRELFEF-- 565
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 532 epagaAGGGASGGGAASGAGAGKQQSHVSSV-----CRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLR 606
Cdd:cd14895  566 -----FKASESAELSLGQPKLRRRSSVLSSVgigsqFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLR 640
                        650       660
                 ....*....|....*....|....*...
gi 159470529 607 CGGVMEAVRIACAGFAYRRPYAAFLDHF 634
Cdd:cd14895  641 YGGVLKAVEIMRQSYPVRMKHADFVKQY 668
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
1-634 3.06e-125

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: 389.34  E-value: 3.06e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529   1 TYTGNILIAVNPFKPLPNLYGPAVIERYRSLpvaqgggEAGSRLPPHVYATACNAYRNMMAEGAGQAILVTGESGAGKTE 80
Cdd:cd14906   18 TYIGNVLISINPYKDISSIYSNLILNEYKDI-------NQNKSPIPHIYAVALRAYQSMVSEKKNQSIIISGESGSGKTE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529  81 TAKLIMA--GQAAAAAAGTGGGASSGMSGVEQKILESNPLLEAFGNAKTLRNNNSSRFGKYCEIFFDPVSGAVTGAAVRT 158
Cdd:cd14906   91 ASKTILQylINTSSSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSDGKIDGASIET 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 159 YLLERSRVVavNNPER---SFHIFYQLVYGASAADRAAWRLPPAASGFAYL-ARSSCVEL------PGQSNA-------E 221
Cdd:cd14906  171 YLLEKSRIS--HRPDNinlSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLdARDDVISSfksqssNKNSNHnnktesiE 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 222 EYQHTRRAMSHIGLSEAQQRAVLGLVAAVLHLGNIAFRDGEHASVGGGAEGAVvppgapRQALEAAAELLGVGAGALAEA 301
Cdd:cd14906  249 SFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKV------TASLESVSKLLGYIESVFKQA 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 302 LTTRQIQTP-EGAI-TTPLSAQAAADSRDSLAKSLYARLFDWLVAAVNAAVDEAHNGPAAAGAA----HLSIGLLDIYGF 375
Cdd:cd14906  323 LLNRNLKAGgRGSVyCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSNDLAGGSnkknNLFIGVLDIFGF 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 376 ESFEVNDLEQLCINLTNEKLQQHFNTHVFKWEQAEYEREGVDWSYISFRDNAD-VLELLEGRLGLMTLLDEACRLPKATA 454
Cdd:cd14906  403 ENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKEcIELIEKKSDGILSLLDDECIMPKGSE 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 455 EGLAHK----YATTPavagssrfTPLKRPAA--SFAVEHYAGKPWAAAANWLDKNRDYVVAEHAALGAAARQPLVRELWA 528
Cdd:cd14906  483 QSLLEKynkqYHNTN--------QYYQRTLAkgTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQ 554
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159470529 529 P-ETEPAGAAGGGAsgggaasgagagkQQSHVSSVCRRQLGELMGALSALQPHYVRCIKPNPTGAAGLFAPGYSLQQLRC 607
Cdd:cd14906  555 QqITSTTNTTKKQT-------------QSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRN 621
                        650       660
                 ....*....|....*....|....*..
gi 159470529 608 GGVMEAVRIACAGFAYRRPYAAFLDHF 634
Cdd:cd14906  622 VGVLNTIKVRKMGYSYRRDFNQFFSRY 648
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
1-630 1.76e-119

class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276885 [Multi-domain]  Cd Length: 673  Bit Score: 373.20  E-value: 1.76e-119
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gi 159470529