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Conserved domains on  [gi|392925914|ref|NP_508817|]
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Myosin motor domain-containing protein [Caenorhabditis elegans]

Protein Classification

myosin/kinesin family protein( domain architecture ID 366212)

myosin/kinesin family protein; contains an ATPase-containing motor domain found in myosins and kinesins that provides the driving force in myosin and kinesin mediated processes

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 ...
250-679 1.86e-21

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 cd14881:

Pssm-ID: 473979 [Multi-domain]  Cd Length: 633  Bit Score: 99.80  E-value: 1.86e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 250 DAINK----RFTQGQCWFSRGGQLFFVNPFNTVSSPRC----NFYSVIPTITSSLFEA---KSST-----LFLRGVSGSG 313
Cdd:cd14881    1 DAVMKclqaRFYAKEFFTNVGPILLSVNPYRDVGNPLTltstRSSPLAPQLLKVVQEAvrqQSETgypqaIILSGTSGSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 314 KSHVAelicMDIVKRL---DNQGQLSHLFK---ISITILRPFLTANNAYNNQCSKaVLHYM-FQTKENRLHRISLkHFPI 386
Cdd:cd14881   81 KTYAS----MLLLRQLfdvAGGGPETDAFKhlaAAFTVLRSLGSAKTATNSESSR-IGHFIeVQVTDGALYRTKI-HCYF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 387 ESMSRGCRA-------NIFAIVANDLTETEKEKYRIAGFRLR------------ETTFNYGNFEEIKAAMSIIGIDMADI 447
Cdd:cd14881  155 LDQTRVIRPlpgeknyHIFYQMLAGLSQEERVKLHLDGYSPAnlrylshgdtrqNEAEDAARFQAWKACLGILGIPFLDV 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 448 LKIISACILLNNINFkTDNTSSEVDNI--ADLEDASSLLGVSALTMYRFM--------------VSDALIdSRLIRDNLV 511
Cdd:cd14881  235 VRVLAAVLLLGNVQF-IDGGGLEVDVKgeTELKSVAALLGVSGAALFRGLttrthnargqlvksVCDANM-SNMTRDALA 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 512 TALYARTVKYILDKINLLLDAGSdpyDRGSVVTDSGISvgtinesnhtvhIVDIPGYVRSTQNSLNELIVNAANDIVQ-- 589
Cdd:cd14881  313 KALYCRTVATIVRRANSLKRLGS---TLGTHATDGFIG------------ILDMFGFEDPKPSQLEHLCINLCAETMQhf 377
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 590 ------------CTDSDMVHE-------------LLKS----------VEIATRND-EVWT----------------ESK 617
Cdd:cd14881  378 ynthifkssiesCRDEGIQCEvevdyvdnvpcidLISSlrtgllsmldVECSPRGTaESYVakikvqhrqnprlfeaKPQ 457
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392925914 618 SPKM--IKHctEAFEIHYDLRLMIERNSNRVSRELVNLFDFRTCTFPFAVNLfqQDIESMIvDN 679
Cdd:cd14881  458 DDRMfgIRH--FAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNFGFATHT--QDFHTRL-DN 516
 
Name Accession Description Interval E-value
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
250-679 1.86e-21

class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276847 [Multi-domain]  Cd Length: 633  Bit Score: 99.80  E-value: 1.86e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 250 DAINK----RFTQGQCWFSRGGQLFFVNPFNTVSSPRC----NFYSVIPTITSSLFEA---KSST-----LFLRGVSGSG 313
Cdd:cd14881    1 DAVMKclqaRFYAKEFFTNVGPILLSVNPYRDVGNPLTltstRSSPLAPQLLKVVQEAvrqQSETgypqaIILSGTSGSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 314 KSHVAelicMDIVKRL---DNQGQLSHLFK---ISITILRPFLTANNAYNNQCSKaVLHYM-FQTKENRLHRISLkHFPI 386
Cdd:cd14881   81 KTYAS----MLLLRQLfdvAGGGPETDAFKhlaAAFTVLRSLGSAKTATNSESSR-IGHFIeVQVTDGALYRTKI-HCYF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 387 ESMSRGCRA-------NIFAIVANDLTETEKEKYRIAGFRLR------------ETTFNYGNFEEIKAAMSIIGIDMADI 447
Cdd:cd14881  155 LDQTRVIRPlpgeknyHIFYQMLAGLSQEERVKLHLDGYSPAnlrylshgdtrqNEAEDAARFQAWKACLGILGIPFLDV 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 448 LKIISACILLNNINFkTDNTSSEVDNI--ADLEDASSLLGVSALTMYRFM--------------VSDALIdSRLIRDNLV 511
Cdd:cd14881  235 VRVLAAVLLLGNVQF-IDGGGLEVDVKgeTELKSVAALLGVSGAALFRGLttrthnargqlvksVCDANM-SNMTRDALA 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 512 TALYARTVKYILDKINLLLDAGSdpyDRGSVVTDSGISvgtinesnhtvhIVDIPGYVRSTQNSLNELIVNAANDIVQ-- 589
Cdd:cd14881  313 KALYCRTVATIVRRANSLKRLGS---TLGTHATDGFIG------------ILDMFGFEDPKPSQLEHLCINLCAETMQhf 377
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 590 ------------CTDSDMVHE-------------LLKS----------VEIATRND-EVWT----------------ESK 617
Cdd:cd14881  378 ynthifkssiesCRDEGIQCEvevdyvdnvpcidLISSlrtgllsmldVECSPRGTaESYVakikvqhrqnprlfeaKPQ 457
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392925914 618 SPKM--IKHctEAFEIHYDLRLMIERNSNRVSRELVNLFDFRTCTFPFAVNLfqQDIESMIvDN 679
Cdd:cd14881  458 DDRMfgIRH--FAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNFGFATHT--QDFHTRL-DN 516
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
429-671 8.61e-16

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: 81.82  E-value: 8.61e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914   429 NFEEIKAAMSIIGI---DMADILKIISACILLNNINFKT---DNTSSEVDNIADLEDASSLLGVS------ALTMYRFMV 496
Cdd:smart00242 241 EFKETLNAMRVLGFseeEQESIFKILAAILHLGNIEFEEgrnDNAASTVKDKEELSNAAELLGVDpeelekALTKRKIKT 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914   497 SDALIDSRL-------IRDNLVTALYARTVKYILDKINLLLDAGsdpydrgsvvtdsgisvgtiNESNHTVHIVDIPGYV 569
Cdd:smart00242 321 GGEVITKPLnveqaldARDALAKALYSRLFDWLVKRINQSLSFK--------------------DGSTYFIGVLDIYGFE 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914   570 RSTQNSLNELIVNAANDIVQ--CTDS--DMVHELLKSVEIATRN----------------------------------DE 611
Cdd:smart00242 381 IFEVNSFEQLCINYANEKLQqfFNQHvfKLEQEEYEREGIDWTFidffdnqdcidliekkppgilslldeecrfpkgtDQ 460
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392925914   612 VWTE------------SKSPKM------IKHCteAFEIHYDLRLMIERNSNRVSRELVNLfdFRTCTFPFAVNLFQQD 671
Cdd:smart00242 461 TFLEklnqhhkkhphfSKPKKKgrtefiIKHY--AGDVTYDVTGFLEKNKDTLSDDLIEL--LQSSKNPLIASLFPSG 534
Myosin_head pfam00063
Myosin head (motor domain);
427-589 9.30e-11

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 65.38  E-value: 9.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914  427 YGNFEEIKAAMSIIGI---DMADILKIISACILLNNINFKTD--NTSSEVDNIADLEDASSLLGVSALTMYRFMVSDALI 501
Cdd:pfam00063 234 SEEFKITDKAMDILGFsdeEQMGIFRIVAAILHLGNIEFKKErnDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIK 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914  502 DSR-------------LIRDNLVTALYARTVKYILDKINLLLDAGSdpydrgsvvtdsgisvgtiNESNHTVHIVDIPGY 568
Cdd:pfam00063 314 TGRetvskpqnveqanYARDALAKAIYSRLFDWLVDRINKSLDVKT-------------------IEKASFIGVLDIYGF 374
                         170       180
                  ....*....|....*....|.
gi 392925914  569 VRSTQNSLNELIVNAANDIVQ 589
Cdd:pfam00063 375 EIFEKNSFEQLCINYVNEKLQ 395
COG5022 COG5022
Myosin heavy chain [General function prediction only];
429-674 1.96e-08

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 58.55  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914  429 NFEEIKAAMSIIGID---MADILKIISACILLNNINFKTD-NTSSEVDNIADLEDASSLLGVSALTMYRFMV-------S 497
Cdd:COG5022   302 EFKITLDALKTIGIDeeeQDQIFKILAAILHIGNIEFKEDrNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVkrqiktgG 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914  498 DALIDSR------LIRDNLVTALYARTVKYILDKINLLLDAGSdpydrgsvVTDSGISVgtinesnhtvhiVDIPGYVRS 571
Cdd:COG5022   382 EWIVVPLnleqalAIRDSLAKALYSNLFDWIVDRINKSLDHSA--------AASNFIGV------------LDIYGFEIF 441
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914  572 TQNSLNELIVNAAN--------------------------DIVQCTDSDMVHELLKSVE-------------IATRNDEV 612
Cdd:COG5022   442 EKNSFEQLCINYTNeklqqffnqhmfkleqeeyvkegiewSFIDYFDNQPCIDLIEKKNplgilslldeecvMPHATDES 521
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914  613 WTE--------SKSPK-----------MIKHctEAFEIHYDLRLMIERNSNRVSRELVNLfdFRTCTFPFAVNLFQ--QD 671
Cdd:COG5022   522 FTSklaqrlnkNSNPKfkksrfrdnkfVVKH--YAGDVEYDVEGFLDKNKDPLNDDLLEL--LKASTNEFVSTLFDdeEN 597

                  ...
gi 392925914  672 IES 674
Cdd:COG5022   598 IES 600
PTZ00014 PTZ00014
myosin-A; Provisional
430-618 2.36e-04

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 45.02  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 430 FEEIKAAMSIIGI---DMADILKIISACILLNNINF-------KTDNTSSEVDNIADLEDASSLLGVSA------LTMYR 493
Cdd:PTZ00014 331 FEEVMESFDSMGLsesQIEDIFSILSGVLLLGNVEIegkeeggLTDAAAISDESLEVFNEACELLFLDYeslkkeLTVKV 410
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 494 FMVSDALI-------DSRLIRDNLVTALYARTVKYILDKINLLLDAgSDPYDrgsvvtdsgISVGtinesnhtvhIVDIP 566
Cdd:PTZ00014 411 TYAGNQKIegpwskdESEMLKDSLSKAVYEKLFLWIIRNLNATIEP-PGGFK---------VFIG----------MLDIF 470
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 392925914 567 GYVRSTQNSLNELIVNAANDIVQCTDSDMVHE----LLKSVEIATRNDEvWTESKS 618
Cdd:PTZ00014 471 GFEVFKNNSLEQLFINITNEMLQKNFVDIVFEreskLYKDEGISTEELE-YTSNES 525
 
Name Accession Description Interval E-value
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
250-679 1.86e-21

class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276847 [Multi-domain]  Cd Length: 633  Bit Score: 99.80  E-value: 1.86e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 250 DAINK----RFTQGQCWFSRGGQLFFVNPFNTVSSPRC----NFYSVIPTITSSLFEA---KSST-----LFLRGVSGSG 313
Cdd:cd14881    1 DAVMKclqaRFYAKEFFTNVGPILLSVNPYRDVGNPLTltstRSSPLAPQLLKVVQEAvrqQSETgypqaIILSGTSGSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 314 KSHVAelicMDIVKRL---DNQGQLSHLFK---ISITILRPFLTANNAYNNQCSKaVLHYM-FQTKENRLHRISLkHFPI 386
Cdd:cd14881   81 KTYAS----MLLLRQLfdvAGGGPETDAFKhlaAAFTVLRSLGSAKTATNSESSR-IGHFIeVQVTDGALYRTKI-HCYF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 387 ESMSRGCRA-------NIFAIVANDLTETEKEKYRIAGFRLR------------ETTFNYGNFEEIKAAMSIIGIDMADI 447
Cdd:cd14881  155 LDQTRVIRPlpgeknyHIFYQMLAGLSQEERVKLHLDGYSPAnlrylshgdtrqNEAEDAARFQAWKACLGILGIPFLDV 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 448 LKIISACILLNNINFkTDNTSSEVDNI--ADLEDASSLLGVSALTMYRFM--------------VSDALIdSRLIRDNLV 511
Cdd:cd14881  235 VRVLAAVLLLGNVQF-IDGGGLEVDVKgeTELKSVAALLGVSGAALFRGLttrthnargqlvksVCDANM-SNMTRDALA 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 512 TALYARTVKYILDKINLLLDAGSdpyDRGSVVTDSGISvgtinesnhtvhIVDIPGYVRSTQNSLNELIVNAANDIVQ-- 589
Cdd:cd14881  313 KALYCRTVATIVRRANSLKRLGS---TLGTHATDGFIG------------ILDMFGFEDPKPSQLEHLCINLCAETMQhf 377
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 590 ------------CTDSDMVHE-------------LLKS----------VEIATRND-EVWT----------------ESK 617
Cdd:cd14881  378 ynthifkssiesCRDEGIQCEvevdyvdnvpcidLISSlrtgllsmldVECSPRGTaESYVakikvqhrqnprlfeaKPQ 457
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392925914 618 SPKM--IKHctEAFEIHYDLRLMIERNSNRVSRELVNLFDFRTCTFPFAVNLfqQDIESMIvDN 679
Cdd:cd14881  458 DDRMfgIRH--FAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNFGFATHT--QDFHTRL-DN 516
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
429-585 1.37e-16

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: 84.18  E-value: 1.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 429 NFEEIKAAMSIIGI---DMADILKIISACILLNNINFKTDN----TSSEVDNIADLEDASSLLGVS------ALTMYRFM 495
Cdd:cd00124  232 EFQELLDALDVLGFsdeEQDSIFRILAAILHLGNIEFEEDEededSSAEVADDESLKAAAKLLGVDaedleeALTTRTIK 311
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 496 VSDALIDSRL-------IRDNLVTALYARTVKYILDKINLLLDAGSDpydrgsvvtdsgisvgtiNESNHTVHIVDIPGY 568
Cdd:cd00124  312 VGGETITKPLtveqaedARDALAKALYSRLFDWLVNRINAALSPTDA------------------AESTSFIGILDIFGF 373
                        170
                 ....*....|....*..
gi 392925914 569 VRSTQNSLNELIVNAAN 585
Cdd:cd00124  374 ENFEVNSFEQLCINYAN 390
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
429-671 8.61e-16

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: 81.82  E-value: 8.61e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914   429 NFEEIKAAMSIIGI---DMADILKIISACILLNNINFKT---DNTSSEVDNIADLEDASSLLGVS------ALTMYRFMV 496
Cdd:smart00242 241 EFKETLNAMRVLGFseeEQESIFKILAAILHLGNIEFEEgrnDNAASTVKDKEELSNAAELLGVDpeelekALTKRKIKT 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914   497 SDALIDSRL-------IRDNLVTALYARTVKYILDKINLLLDAGsdpydrgsvvtdsgisvgtiNESNHTVHIVDIPGYV 569
Cdd:smart00242 321 GGEVITKPLnveqaldARDALAKALYSRLFDWLVKRINQSLSFK--------------------DGSTYFIGVLDIYGFE 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914   570 RSTQNSLNELIVNAANDIVQ--CTDS--DMVHELLKSVEIATRN----------------------------------DE 611
Cdd:smart00242 381 IFEVNSFEQLCINYANEKLQqfFNQHvfKLEQEEYEREGIDWTFidffdnqdcidliekkppgilslldeecrfpkgtDQ 460
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392925914   612 VWTE------------SKSPKM------IKHCteAFEIHYDLRLMIERNSNRVSRELVNLfdFRTCTFPFAVNLFQQD 671
Cdd:smart00242 461 TFLEklnqhhkkhphfSKPKKKgrtefiIKHY--AGDVTYDVTGFLEKNKDTLSDDLIEL--LQSSKNPLIASLFPSG 534
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
430-654 2.17e-12

class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276845 [Multi-domain]  Cd Length: 647  Bit Score: 70.66  E-value: 2.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 430 FEEIKAAMSIIGI---DMADILKIISACILLNNINFKTDNTSSE----VDNIADLEDASSLLGVS------ALT----MY 492
Cdd:cd14879  237 FQELKTALKTLGFkrkHVAQICQLLAAILHLGNLEFTYDHEGGEesavVKNTDVLDIVAAFLGVSpedletSLTyktkLV 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 493 RFMVSDALID---SRLIRDNLVTALYARTVKYILDKINLLLDAGSDpydrgsvvtdsgiSVGTinesnhTVHIVDIPGY- 568
Cdd:cd14879  317 RKELCTVFLDpegAAAQRDELARTLYSLLFAWVVETINQKLCAPED-------------DFAT------FISLLDFPGFq 377
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 569 --VRSTQNSLNELIVNAANDIVQ--------------------------------C------------------------ 590
Cdd:cd14879  378 nrSSTGGNSLDQFCVNFANERLHnyvlrsfferkaeeleaegvsvpatsyfdnsdCvrllrgkpggllgilddqtrrmpk 457
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392925914 591 -TDSDMVHELLKSVE-----IATRNDEvwTESKSPKM-IKHCteAFEIHYDLRLMIERNSNRVSRELVNLF 654
Cdd:cd14879  458 kTDEQMLEALRKRFGnhssfIAVGNFA--TRSGSASFtVNHY--AGEVTYSVEGFLERNGDVLSPDFVNLL 524
MYSc_Myo12 cd14874
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...
252-586 8.86e-11

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


Pssm-ID: 276841 [Multi-domain]  Cd Length: 628  Bit Score: 65.66  E-value: 8.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 252 INKRFTQGQCWFSRGGQLFFVNPFNTVSS------PRCNFYSVIPTITSSLFEAKSS--TLFLRGVSGSGKSHVAELICM 323
Cdd:cd14874    7 LHERFKKGQTYTKASNVLVFVNDFNKLSIqdqlviKKCHISGVAENALDRIKSMSSNaeSIVFGGESGSGKSYNAFQVFK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 324 DIVKRLDNQGQLSHLFKISiTILRPFLTANNAYNNQCSKAVLHYMFQTKENRLHRISLKH-FPIE-----SMSRGCRA-N 396
Cdd:cd14874   87 YLTSQPKSKVTTKHSSAIE-SVFKSFGCAKTLKNDEATRFGCSIDLLYKRNVLTGLNLKYtVPLEvprviSQKPGERNfN 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 397 IFAIVANDLTETEKEKYRIAG----FRLRE------TTFNYGNFEEIKAAMSIIGID---MADILKIISACILLNNINFK 463
Cdd:cd14874  166 VFYEVYHGLNDEMKAKFGIKGlqkfFYINQgnstenIQSDVNHFKHLEDALHVLGFSddhCISIYKIISTILHIGNIYFR 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 464 TDNTSS------EVDNIADLEDASSLLGVSALTMYRFMVSDALIDSRL-------IRDNLVTALYARTVKYILDKINLLL 530
Cdd:cd14874  246 TKRNPNveqdvvEIGNMSEVKWVAFLLEVDFDQLVNFLLPKSEDGTTIdlnaaldNRDSFAMLIYEELFKWVLNRIGLHL 325
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 392925914 531 DAgsdpydrgsvvtdsgisvgtineSNHT--VHIVDIPGYVRSTQNSLNELIVNAAND 586
Cdd:cd14874  326 KC-----------------------PLHTgvISILDHYGFEKYNNNGVEEFLINSVNE 360
Myosin_head pfam00063
Myosin head (motor domain);
427-589 9.30e-11

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 65.38  E-value: 9.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914  427 YGNFEEIKAAMSIIGI---DMADILKIISACILLNNINFKTD--NTSSEVDNIADLEDASSLLGVSALTMYRFMVSDALI 501
Cdd:pfam00063 234 SEEFKITDKAMDILGFsdeEQMGIFRIVAAILHLGNIEFKKErnDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIK 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914  502 DSR-------------LIRDNLVTALYARTVKYILDKINLLLDAGSdpydrgsvvtdsgisvgtiNESNHTVHIVDIPGY 568
Cdd:pfam00063 314 TGRetvskpqnveqanYARDALAKAIYSRLFDWLVDRINKSLDVKT-------------------IEKASFIGVLDIYGF 374
                         170       180
                  ....*....|....*....|.
gi 392925914  569 VRSTQNSLNELIVNAANDIVQ 589
Cdd:pfam00063 375 EIFEKNSFEQLCINYVNEKLQ 395
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
429-535 1.16e-10

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: 65.18  E-value: 1.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 429 NFEEIKAAMSIIGI---DMADILKIISACILLNNINFKTDNTS--SEVDNIADLEDASSLLGVS------ALTMYRFMVS 497
Cdd:cd01377  229 EFKLTDEAFDILGFseeEKMSIFKIVAAILHLGNIKFKQRRREeqAELDGTEEADKAAHLLGVNssdllkALLKPRIKVG 308
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 392925914 498 DALI-------DSRLIRDNLVTALYARTVKYILDKINLLLDAGSD 535
Cdd:cd01377  309 REWVtkgqnkeQVVFSVGALAKALYERLFLWLVKRINKTLDTKSK 353
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
428-589 1.48e-10

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


Pssm-ID: 276832  Cd Length: 648  Bit Score: 64.97  E-value: 1.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 428 GNFEEIKAAMSIIGI---DMADILKIISACILLNNINFKT---DNT-SSEVDNIADLEDASSLLGVS------ALTMYRF 494
Cdd:cd01381  218 AEFADIRSAMKVLMFtdeEIWDIFKLLAAILHLGNIKFEAtvvDNLdASEVRDPPNLERAAKLLEVPkqdlvdALTTRTI 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 495 MVSDALIDSRL-------IRDNLVTALYARTVKYILDKINlllDAGSDPYDRGSVVTdsgiSVGtinesnhtvhIVDIPG 567
Cdd:cd01381  298 FTRGETVVSPLsaeqaldVRDAFVKGIYGRLFIWIVNKIN---SAIYKPRGTDSSRT----SIG----------VLDIFG 360
                        170       180
                 ....*....|....*....|..
gi 392925914 568 YVRSTQNSLNELIVNAANDIVQ 589
Cdd:cd01381  361 FENFEVNSFEQLCINFANENLQ 382
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
420-678 1.15e-09

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: 62.02  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 420 LRETTFNYGNFEEIKAAMSIIGI---DMADILKIISACILLNNINFKTDNTSSEVdNIAD---LEDASSLLGVSALTMyr 493
Cdd:cd14897  218 SEELEYYRQMFHDLTNIMKLIGFseeDISVIFTILAAILHLTNIVFIPDEDTDGV-TVADeypLHAVAKLLGIDEVEL-- 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 494 fmvSDALIDSRLI------------------RDNLVTALYARTVKYILDKINLLLDAGSDPydrgsvvtdsgisvgTINE 555
Cdd:cd14897  295 ---TEALISNVNTirgeriqswkslrqandsRDALAKDLYSRLFGWIVGQINRNLWPDKDF---------------QIMT 356
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 556 SNHTVHIVDIPGYVRSTQNSLNELIVNAANDIVQC--------------------------TDSDMVHELL--KSVEIAT 607
Cdd:cd14897  357 RGPSIGILDMSGFENFKINSFDQLCINLSNERLQQyfndyvfprerseyeiegiewrdieyHDNDDVLELFfkKPLGILP 436
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 608 RNDEvwtESKSP---------KMIKHCTE------------AFEIH-------YDLRLMIERNSNRVSRELVNLfdFRTC 659
Cdd:cd14897  437 LLDE---ESTFPqstdsslvqKLNKYCGEspryvaspgnrvAFGIRhyaeqvtYDADGFLEKNRDNLSSDIVGC--LLNS 511
                        330
                 ....*....|....*....
gi 392925914 660 TFPFAVNLFQQDIESMIVD 678
Cdd:cd14897  512 NNEFISDLFTSYFKRSLSD 530
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
397-589 1.60e-09

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: 61.33  E-value: 1.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 397 IFAIVANDLTETEKEKYRIAGFRLRETTF------NYGNFEEIKAAMSIIGIDMAD---ILKIISACILLNNINFKTDNT 467
Cdd:cd14890  204 LLAGADEALRERLKLQTPVEYFYLRGECSsipscdDAKAFAETIRCLSTIGISEENqdaVFGLLAAVLHLGNVDFESEND 283
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 468 SSEVDNIADLED---ASSLLGVSALTMYRFMVSDAL-IDSRLI------------RDNLVTALYARTVKYILDKINLLLD 531
Cdd:cd14890  284 TTVLEDATTLQSlklAAELLGVNEDALEKALLTRQLfVGGKTIvqpqnveqardkRDALAKALYSSLFLWLVSELNRTIS 363
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 392925914 532 AGSDPYdrgsvvtdsgisvGTINesnhtvhIVDIPGYVRSTQNSLNELIVNAANDIVQ 589
Cdd:cd14890  364 SPDDKW-------------GFIG-------VLDIYGFEKFEWNTFEQLCINYANEKLQ 401
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
430-589 2.16e-09

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: 60.96  E-value: 2.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 430 FEEIKAAMSIIGID---MADILKIISACILLNNINFKT---DNTSSEVDNIADLEDASSLLGVSALTMYRFMVSDALI-- 501
Cdd:cd14901  240 YAKTRHAMTTIGMSpdeQISVLQLVAAVLHLGNLCFVKkdgEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRag 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 502 -----------DSRLIRDNLVTALYARTVKYILDKINLLLdAGSDPYDrgsvvtdsgisvgtineSNHTVHIVDIPGYVR 570
Cdd:cd14901  320 geyitmplsveQALLTRDVVAKTLYAQLFDWLVDRINESI-AYSESTG-----------------ASRFIGIVDIFGFEI 381
                        170
                 ....*....|....*....
gi 392925914 571 STQNSLNELIVNAANDIVQ 589
Cdd:cd14901  382 FATNSLEQLCINFANEKLQ 400
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
422-589 2.62e-09

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: 60.76  E-value: 2.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 422 ETTFNYGNFEEIKAAMSIIGIDMADILKIISACILLNNINFKTDNTSSEVDNIAD-----LEDASSLLGVSALtmyrfMV 496
Cdd:cd14906  245 ESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDkvtasLESVSKLLGYIES-----VF 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 497 SDALIDSRL--------------------IRDNLVTALYARTVKYILDKINLLLDAGSDPYDrgsvvtdsgISVGTINES 556
Cdd:cd14906  320 KQALLNRNLkaggrgsvycrpmevaqseqTRDALSKSLYVRLFKYIVEKINRKFNQNTQSND---------LAGGSNKKN 390
                        170       180       190
                 ....*....|....*....|....*....|...
gi 392925914 557 NHTVHIVDIPGYVRSTQNSLNELIVNAANDIVQ 589
Cdd:cd14906  391 NLFIGVLDIFGFENLSSNSLEQLLINFTNEKLQ 423
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
342-589 8.56e-09

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: 59.00  E-value: 8.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 342 SITILRPFLTANNAYNNQCSK----AVLHYmfqTKENRLHRISLKHFPIESmSR--GCRAN-----IFAIVANDLTETEK 410
Cdd:cd14892  134 SNLILEAFGNAKTIRNDNSSRfgkyIQIHY---NSDGRIAGASTDHFLLEK-SRlvGPDANernyhIFYQLLAGLDANEN 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 411 EKYRIAgfRLRETTF-NYGN------------FEEIKAAMSIIGID------MADILkiisACIL-LNNINF----KTDN 466
Cdd:cd14892  210 AALELT--PAESFLFlNQGNcvevdgvddateFKQLRDAMEQLGFDaefqrpIFEVL----AAVLhLGNVRFeenaDDED 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 467 TSSEVDNIADLEDASSLLGVSALTMYRFMVSDALI--------------DSRLIRDNLVTALYARTVKYILDKINLLlda 532
Cdd:cd14892  284 VFAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTStargsvleikltarEAKNALDALCKYLYGELFDWLISRINAC--- 360
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 392925914 533 gsdpydRGSVVTDSGISVGTINESNHtVHIVDIPGYVRSTQNSLNELIVNAANDIVQ 589
Cdd:cd14892  361 ------HKQQTSGVTGGAASPTFSPF-IGILDIFGFEIMPTNSFEQLCINFTNEMLQ 410
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
390-589 1.51e-08

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


Pssm-ID: 276835  Cd Length: 647  Bit Score: 58.46  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 390 SRGCRAN-------IFAIVANDLTETEKEKYRIAGFRlretTFNYGN---------------FEEIKAAMSIIGIDMAD- 446
Cdd:cd01384  167 SRVVQVSdpernyhCFYQLCAGAPPEDREKYKLKDPK----QFHYLNqskcfeldgvddaeeYRATRRAMDVVGISEEEq 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 447 --ILKIISACILLNNINFkTDNTSSEVDNIAD------LEDASSLLGV------SALTMyRFMVS-DALIDSRL------ 505
Cdd:cd01384  243 daIFRVVAAILHLGNIEF-SKGEEDDSSVPKDeksefhLKAAAELLMCdekaleDALCK-RVIVTpDGIITKPLdpdaat 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 506 -IRDNLVTALYARTVKYILDKINllldagsdpydrgsvvtdsgISVGTINESNHTVHIVDIPGYVRSTQNSLNELIVNAA 584
Cdd:cd01384  321 lSRDALAKTIYSRLFDWLVDKIN--------------------RSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLA 380

                 ....*
gi 392925914 585 NDIVQ 589
Cdd:cd01384  381 NEKLQ 385
COG5022 COG5022
Myosin heavy chain [General function prediction only];
429-674 1.96e-08

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 58.55  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914  429 NFEEIKAAMSIIGID---MADILKIISACILLNNINFKTD-NTSSEVDNIADLEDASSLLGVSALTMYRFMV-------S 497
Cdd:COG5022   302 EFKITLDALKTIGIDeeeQDQIFKILAAILHIGNIEFKEDrNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVkrqiktgG 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914  498 DALIDSR------LIRDNLVTALYARTVKYILDKINLLLDAGSdpydrgsvVTDSGISVgtinesnhtvhiVDIPGYVRS 571
Cdd:COG5022   382 EWIVVPLnleqalAIRDSLAKALYSNLFDWIVDRINKSLDHSA--------AASNFIGV------------LDIYGFEIF 441
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914  572 TQNSLNELIVNAAN--------------------------DIVQCTDSDMVHELLKSVE-------------IATRNDEV 612
Cdd:COG5022   442 EKNSFEQLCINYTNeklqqffnqhmfkleqeeyvkegiewSFIDYFDNQPCIDLIEKKNplgilslldeecvMPHATDES 521
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914  613 WTE--------SKSPK-----------MIKHctEAFEIHYDLRLMIERNSNRVSRELVNLfdFRTCTFPFAVNLFQ--QD 671
Cdd:COG5022   522 FTSklaqrlnkNSNPKfkksrfrdnkfVVKH--YAGDVEYDVEGFLDKNKDPLNDDLLEL--LKASTNEFVSTLFDdeEN 597

                  ...
gi 392925914  672 IES 674
Cdd:COG5022   598 IES 600
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
252-586 2.04e-08

class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276844 [Multi-domain]  Cd Length: 656  Bit Score: 57.90  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 252 INKRFTQGQCWFSRGGQLFFVNPF--------------NTVSSPRCNfySVIPTITSS-------LF-EAKSSTLFLRGV 309
Cdd:cd14878    7 IQKRFGNNQIYTFIGDILLLVNPYkelpiystmvsqlyLSSSGQLCS--SLPPHLFSCaerafhqLFqERRPQCFILSGE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 310 SGSGKSHVaeliCMDIVKRL-----DNQGQLSHLFKISITILRPFLTANNAYNNQCSKAVLHYMFQTKENRLH----RIS 380
Cdd:cd14878   85 RGSGKTEA----SKQIMKHLtcrasSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERKKHltgaRIY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 381 ---LKHFPIESMSRG-CRANIFAIVANDLTETEK----------EKYRIAGFR----LRETTFNYGNFEEIKAAMSIIG- 441
Cdd:cd14878  161 tymLEKSRLVSQPPGqSNFLIFYLLMDGLSAEEKyglhlnnlcaHRYLNQTMRedvsTAERSLNREKLAVLKQALNVVGf 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 442 --IDMADILKIISACILLNNINFK--TDNTSSEVDNIADLEDASSLLGVS------ALTM-YRFMVSDALIDSRLI---- 506
Cdd:cd14878  241 ssLEVENLFVILSAILHLGDIRFTalTEADSAFVSDLQLLEQVAGMLQVStdelasALTTdIQYFKGDMIIRRHTIqiae 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 507 --RDNLVTALYARTVKYILDKINLLLDAGSDPydrgsvVTDSGISVGtinesnhtvhIVDIPGYVRSTQNSLNELIVNAA 584
Cdd:cd14878  321 fyRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQ------KSMQTLDIG----------ILDIFGFEEFQKNEFEQLCVNMT 384

                 ..
gi 392925914 585 ND 586
Cdd:cd14878  385 NE 386
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
429-589 2.69e-08

class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276839  Cd Length: 644  Bit Score: 57.48  E-value: 2.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 429 NFEEIKAAMSIIGIDMADI---LKIISACILLNNINF-----KTDNTSSEVDNIADLEDASSLLGVSALTMYRFMVSDAL 500
Cdd:cd14872  217 DFEEVVLAMEQLGFDDADInnvMSLIAAILKLGNIEFasgggKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLM 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 501 ----IDSRLI----------RDNLVTALYARTVKYILDKINLLLDAGSdpydrgsvvtdsgisvgtiNESNHTVHIVDIP 566
Cdd:cd14872  297 eikgCDPTRIpltpaqatdaCDALAKAAYSRLFDWLVKKINESMRPQK-------------------GAKTTFIGVLDIF 357
                        170       180
                 ....*....|....*....|...
gi 392925914 567 GYVRSTQNSLNELIVNAANDIVQ 589
Cdd:cd14872  358 GFEIFEKNSFEQLCINFTNEKLQ 380
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
254-611 2.71e-08

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


Pssm-ID: 276861 [Multi-domain]  Cd Length: 644  Bit Score: 57.48  E-value: 2.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 254 KRFTQGQCWFSRGGQLFFVNPFNTVS----------SPRcNFYSVIP---TITSSLFEAKSST-----LFLRGVSGSGKS 315
Cdd:cd14896    9 KRFHLGRIYTFGGPILLSLNPHRSLPlfseevlasyHPR-KALNTTPhifAIAASAYRLSQSTgqdqcILLSGHSGSGKT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 316 HVAElicmDIVKRLDNQGQLSHLFKIS-----ITILRPFLTANNAYNNQCSK--AVLHYMFQtkenrlHRI----SLKHF 384
Cdd:cd14896   88 EAAK----KIVQFLSSLYQDQTEDRLRqpedvLPILESFGHAKTILNANASRfgQVLRLHLQ------HGVivgaSVSHY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 385 PIES-----MSRGCRA-NIFAIVANDLTETEKEKYRIAGfrlRETTF--NYG------------NFEEIKAAMSIIGI-- 442
Cdd:cd14896  158 LLETsrvvfQAQAERSfHVFYELLAGLDPEEREQLSLQG---PETYYylNQGgacrlqgkedaqDFEGLLKALQGLGLca 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 443 -DMADILKIISACILLNNINFKT-DNTSSEVDNI---ADLEDASSLLGVSALTM----------------YRFMVSDALI 501
Cdd:cd14896  235 eELTAIWAVLAAILQLGNICFSSsERESQEVAAVsswAEIHTAARLLQVPPERLegavthrvtetpygrvSRPLPVEGAI 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 502 DSRlirDNLVTALYARTVKYILDKINLLLDagsdPYDRGsvvtdsgisvgtinESNHTVHIVDIPGYVRSTQNSLNELIV 581
Cdd:cd14896  315 DAR---DALAKTLYSRLFTWLLKRINAWLA----PPGEA--------------ESDATIGVVDAYGFEALRVNGLEQLCI 373
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 392925914 582 NAANDIVQCTDSDMV---------HELLKSVEIATRNDE 611
Cdd:cd14896  374 NLASERLQLFSSQTLlaqeeeecqRELLPWVPIPQPPRE 412
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
430-724 6.30e-08

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: 56.34  E-value: 6.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 430 FEEIKAAMSIIGI---DMADILKIISACILLNNINFKTDNTSSEVDNIAdLEDASSLLGVSAltmyrFMVSDALIDSRLI 506
Cdd:cd14873  230 FREVITAMEVMQFskeEVREVSRLLAGILHLGNIEFITAGGAQVSFKTA-LGRSAELLGLDP-----TQLTDALTQRSMF 303
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 507 ------------------RDNLVTALYARTVKYILDKINLLLdagsdpydRGsvvtdsgisvgtiNESNHTVHIVDIPGY 568
Cdd:cd14873  304 lrgeeiltplnvqqavdsRDSLAMALYARCFEWVIKKINSRI--------KG-------------KEDFKSIGILDIFGF 362
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 569 VRSTQNSLNELIVNAANDIVQctdsDMVHELLKSVEIATRNDE--VWT--------------------------ESKSPK 620
Cdd:cd14873  363 ENFEVNHFEQFNINYANEKLQ----EYFNKHIFSLEQLEYSREglVWEdidwidngecldliekklgllalineESHFPQ 438
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 621 ----------MIKHCTEAF------------------EIHYDLRLMIERNSNRVSRELVNLfdFRTCTFPFAVNLFQQDI 672
Cdd:cd14873  439 atdstlleklHSQHANNHFyvkprvavnnfgvkhyagEVQYDVRGILEKNRDTFRDDLLNL--LRESRFDFIYDLFEHVS 516
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 392925914 673 ESmivdNNYAPSAINWPNNGKTVIQNVIESIRMLKKDIADNNSQQIICLKSN 724
Cdd:cd14873  517 SR----NNQDTLKCGSKHRRPTVSSQFKDSLHSLMATLSSSNPFFVRCIKPN 564
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
446-596 1.34e-07

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: 55.28  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 446 DILKIISACILLNNINFKTDNTSSEVDNIAD-----LEDASSLLGVSALTMYRFMVSDALIDSRL-------------IR 507
Cdd:cd14902  263 DIFKILAALLHLGNVNFTAENGQEDATAVTAasrfhLAKCAELMGVDVDKLETLLSSREIKAGVEvmvlkltpeqakeIC 342
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 508 DNLVTALYARTVKYILDKINLLLDAGsdpydrgsvvtDSGISVGTINESNHTVHIVDIPGYVRSTQNSLNELIVNAANDI 587
Cdd:cd14902  343 GSLAKAIYGRLFTWLVRRLSDEINYF-----------DSAVSISDEDEELATIGILDIFGFESLNRNGFEQLCINYANER 411

                 ....*....
gi 392925914 588 VQCTDSDMV 596
Cdd:cd14902  412 LQAQFNEFV 420
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
429-538 2.19e-07

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


Pssm-ID: 276829  Cd Length: 652  Bit Score: 54.47  E-value: 2.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 429 NFEEIKAAMSIIGI---DMADILKIISACILLNNINFKTD-NTSSEVDNIADLEDASSLLGV------SALTmYRFMVS- 497
Cdd:cd01378  223 DFKEVLNAMKVIGFteeEQDSIFRILAAILHLGNIQFAEDeEGNAAISDTSVLDFVAYLLGVdpdqleKALT-HRTIETg 301
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 392925914 498 ---DALIDSRL-------IRDNLVTALYARTVKYILDKINLLLDAGSDPYD 538
Cdd:cd01378  302 gggRSVYEVPLnveqaayARDALAKAIYSRLFDWIVERINKSLAAKSGGKK 352
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
248-589 1.55e-06

class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276854  Cd Length: 659  Bit Score: 51.83  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 248 FVDAINKRFTQGQCWFSRGGQLFFVNPF-------NTVSSP-RCNFYSVIPT-ITSSLFEAKSSTL------------FL 306
Cdd:cd14889    3 LLEVLKVRFMQSNIYTYVGDILVAINPFkylhiyeKEVSQKyKCEKKSSLPPhIFAVADRAYQSMLgrlargpknqciVI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 307 RGVSGSGKSHVAELICMDIVKRLDNQGQLSHLFKISITILRPFLTANNAYNNQCSKAVLHYMFQTKENRLHRISLKHFPI 386
Cdd:cd14889   83 SGESGAGKTESTKLLLRQIMELCRGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFRNGHVKGAKINEYLL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 387 ESmSRGCRAN-------IFAIVANDLTETEKEKYRIAGFRL-RETTFNYGN----------FEEIKAAMSIIGI---DMA 445
Cdd:cd14889  163 EK-SRVVHQDggeenfhIFYYMFAGISAEDRENYGLLDPGKyRYLNNGAGCkrevqywkkkYDEVCNAMDMVGFteqEEV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 446 DILKIISACILLNNINFKTDNTSS---EVDNIADLEDASSLLGVSA----------LTMYR----------FMVSDAlid 502
Cdd:cd14889  242 DMFTILAGILSLGNITFEMDDDEAlkvENDSNGWLKAAAGQFGVSEedllktltctVTFTRgeqiqrhhtkQQAEDA--- 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 503 srliRDNLVTALYARTVKYILDKINLLLdagsDPYDRGSVvtdsgisvgTINEsnhtVHIVDIPGYVRSTQNSLNELIVN 582
Cdd:cd14889  319 ----RDSIAKVAYGRVFGWIVSKINQLL----APKDDSSV---------ELRE----IGILDIFGFENFAVNRFEQACIN 377

                 ....*..
gi 392925914 583 AANDIVQ 589
Cdd:cd14889  378 LANEQLQ 384
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
430-589 2.78e-06

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: 51.17  E-value: 2.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 430 FEEIKAAMSIIGI--DMAD-ILKIISACILLNNINFKT---DNTSSEVDNIADLEDASSLLGV------SALTMYRFMVS 497
Cdd:cd14883  222 FDHLRLAMNVLGIpeEMQEgIFSVLSAILHLGNLTFEDidgETGALTVEDKEILKIVAKLLGVdpdklkKALTIRQINVR 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 498 DALID-------SRLIRDNLVTALYARTVKYILDKINLLLDAGSdpydrgsvvtdsgisvgtinESNHTVHIVDIPGYVR 570
Cdd:cd14883  302 GNVTEiplkvqeARDNRDAMAKALYSRTFAWLVNHINSCTNPGQ--------------------KNSRFIGVLDIFGFEN 361
                        170
                 ....*....|....*....
gi 392925914 571 STQNSLNELIVNAANDIVQ 589
Cdd:cd14883  362 FKVNSFEQLCINYTNEKLH 380
MYSc_Myo24A cd14937
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
301-586 3.53e-06

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


Pssm-ID: 276897  Cd Length: 637  Bit Score: 50.78  E-value: 3.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 301 SSTLFLRGVSGSGKSHVAELICMDIVKRLDNQGQLSHLFKISITILRPFLTANNAYNNQCSKAVLHYMFQTKENR-LHRI 379
Cdd:cd14937   69 NQSIIISGESGSGKTEASKLVIKYYLSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQnIVSS 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 380 SLKHFPIESM--------SRGcrANIFAIVANDLTETEKEKYRIAGfrlrETTFNY--------------GNFEEIKAAM 437
Cdd:cd14937  149 SIEIFLLENIrvvsqeeeERG--YHIFYQIFNGMSQELKNKYKIRS----ENEYKYivnknvvipeiddaKDFGNLMISF 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 438 SIIGI-DMADILKI-ISACILLNNINF-------KTDNTSSEVDNIADLEDASSLLGV------SALTMYRFMVSDALID 502
Cdd:cd14937  223 DKMNMhDMKDDLFLtLSGLLLLGNVEYqeiekggKTNCSELDKNNLELVNEISNLLGInyenlkDCLVFTEKTIANQKIE 302
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 503 SRLIRDNLVTA-------LYARTVKYILDKINLLLDAGsdpydrgsvvtdsgisvgtiNESNHTVHIVDIPGYVRSTQNS 575
Cdd:cd14937  303 IPLSVEESVSIcksiskdLYNKIFSYITKRINNFLNNN--------------------KELNNYIGILDIFGFEIFSKNS 362
                        330
                 ....*....|.
gi 392925914 576 LNELIVNAAND 586
Cdd:cd14937  363 LEQLLINIANE 373
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
430-604 2.40e-05

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


Pssm-ID: 276869  Cd Length: 653  Bit Score: 48.01  E-value: 2.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 430 FEEIKAAMSIIGIDMAD---ILKIISACILLNNINF-KTDNTSSEVDNIADLEDASSLLGVSALTMY------------- 492
Cdd:cd14904  223 FASTQKSLSLIGLDNDAqrtLFKILSGVLHLGEVMFdKSDENGSRISNGSQLSQVAKMLGLPTTRIEealcnrsvvtrne 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 493 RFMVSDALIDSRLIRDNLVTALYARTVKYILDKINllldagsdpydrGSVVTDSGISVGTINesnhtvhIVDIPGYVRST 572
Cdd:cd14904  303 SVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKIN------------AAISTDDDRIKGQIG-------VLDIFGFEDFA 363
                        170       180       190
                 ....*....|....*....|....*....|..
gi 392925914 573 QNSLNELIVNAANDIVQctdSDMVHELLKSVE 604
Cdd:cd14904  364 HNGFEQFCINYANEKLQ---QKFTTDVFKTVE 392
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
419-613 2.42e-05

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: 47.85  E-value: 2.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 419 RLRETTFNYGNFEEIKAAMSIIGIDMA---DILKIISACILLNNINFKTDNTSSEVDNIADLED----ASSLLGVSALTM 491
Cdd:cd14903  209 IKIEGMSDRKHFARTKEALSLIGVSEEkqeVLFEVLAGILHLGQLQIQSKPNDDEKSAIAPGDQgavyATKLLGLSPEAL 288
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 492 YRFMVS---DALIDSRLI----------RDNLVTALYARTVKYILDKINLLLdaGSDPydrgsvvtdsgisvgtinESNH 558
Cdd:cd14903  289 EKALCSrtmRAAGDVYTVplkkdqaedcRDALAKAIYSNVFDWLVATINASL--GNDA------------------KMAN 348
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 392925914 559 TVHIVDIPGYVRSTQNSLNELIVNAANDIVQctdSDMVHELLKSVEIATRNDEV-W 613
Cdd:cd14903  349 HIGVLDIFGFEHFKHNSFEQFCINYANEKLQ---QKFTQDVFKTVQIEYEEEGIrW 401
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
429-534 7.32e-05

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: 46.38  E-value: 7.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 429 NFEEIKAAMSIIGI---DMADILKIISACILLNNINFK-TDNTSSEVD-NIADLEDASSLLGVSALTMYRF-------MV 496
Cdd:cd01380  223 EFEETRKALTLLGIseeEQMEIFRILAAILHLGNVEIKaTRNDSASISpDDEHLQIACELLGIDESQLAKWlckrkivTR 302
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 392925914 497 SDALIDSRLI------RDNLVTALYARTVKYILDKINLLLDAGS 534
Cdd:cd01380  303 SEVIVKPLTLqqaivaRDALAKHIYAQLFDWIVDRINKALASPV 346
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
429-589 1.74e-04

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: 45.39  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 429 NFEEIKAAMSIIGI---DMADILKIISACILLNNINFKTD---NTSSEVDNIAdLEDASSLLGVSALTMYRFMVSDALID 502
Cdd:cd14920  227 NFQETMEAMHIMGFsheEILSMLKVVSSVLQFGNISFKKErntDQASMPENTV-AQKLCHLLGMNVMEFTRAILTPRIKV 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 503 SR-------------LIRDNLVTALYARTVKYILDKINLLLDAgsdpydrgsvvtdsgisvgTINESNHTVHIVDIPGYV 569
Cdd:cd14920  306 GRdyvqkaqtkeqadFAVEALAKATYERLFRWLVHRINKALDR-------------------TKRQGASFIGILDIAGFE 366
                        170       180
                 ....*....|....*....|
gi 392925914 570 RSTQNSLNELIVNAANDIVQ 589
Cdd:cd14920  367 IFELNSFEQLCINYTNEKLQ 386
PTZ00014 PTZ00014
myosin-A; Provisional
430-618 2.36e-04

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 45.02  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 430 FEEIKAAMSIIGI---DMADILKIISACILLNNINF-------KTDNTSSEVDNIADLEDASSLLGVSA------LTMYR 493
Cdd:PTZ00014 331 FEEVMESFDSMGLsesQIEDIFSILSGVLLLGNVEIegkeeggLTDAAAISDESLEVFNEACELLFLDYeslkkeLTVKV 410
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 494 FMVSDALI-------DSRLIRDNLVTALYARTVKYILDKINLLLDAgSDPYDrgsvvtdsgISVGtinesnhtvhIVDIP 566
Cdd:PTZ00014 411 TYAGNQKIegpwskdESEMLKDSLSKAVYEKLFLWIIRNLNATIEP-PGGFK---------VFIG----------MLDIF 470
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 392925914 567 GYVRSTQNSLNELIVNAANDIVQCTDSDMVHE----LLKSVEIATRNDEvWTESKS 618
Cdd:PTZ00014 471 GFEVFKNNSLEQLFINITNEMLQKNFVDIVFEreskLYKDEGISTEELE-YTSNES 525
MYSc_Myo44 cd14905
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...
300-589 6.35e-04

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


Pssm-ID: 276870  Cd Length: 673  Bit Score: 43.54  E-value: 6.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 300 KSSTLFLRGVSGSGKSHVAELICMDIVKR-LDNQGQLSHLFKISITILRPFLTANNAYNNQCSKAVLHY-MF-----QTK 372
Cdd:cd14905   71 RDQLIFIGGESGSGKSENTKIIIQYLLTTdLSRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFeMFyslygEIQ 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 373 ENRLHRISLKHFPIESMSRGCRA-NIFAIVANDLTETEKEKYRIAGFrlreTTFNYGN---------------FEEIKaa 436
Cdd:cd14905  151 GAKLYSYFLDENRVTYQNKGERNfHIFYQFLKGITDEEKAAYQLGDI----NSYHYLNqggsisvesiddnrvFDRLK-- 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 437 MSIIGIDMAD-----ILKIISACILLNNINFKTDNTSSEVDNIADLEDASSLLGVSALTMYRFMVSDALI---DSRLIRD 508
Cdd:cd14905  225 MSFVFFDFPSekidlIFKTLSFIIILGNVTFFQKNGKTEVKDRTLIESLSHNITFDSTKLENILISDRSMpvnEAVENRD 304
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392925914 509 NLVTALYARTVKYILDKINLLLDAgsdpydrgsvvtdsgisvgtiNESNHTVHIVDIPGYVRSTQNSLNELIVNAANDIV 588
Cdd:cd14905  305 SLARSLYSALFHWIIDFLNSKLKP---------------------TQYSHTLGILDLFGQESSQLNGYEQFSINFLEERL 363

                 .
gi 392925914 589 Q 589
Cdd:cd14905  364 Q 364
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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