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Conserved domains on  [gi|254839636]
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Chain A, Myosin heavy chain isoform A

Protein Classification

Myosin_N and MYSc_class_II domain-containing protein( domain architecture ID 10498520)

protein containing domains Myosin_N, MYSc_class_II, and IQ

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
97-765 0e+00

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


:

Pssm-ID: 276951 [Multi-domain]  Cd Length: 662  Bit Score: 1345.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITG 176
Cdd:cd01377    1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 177 ESGAGKTENTKKVIQYFALVAASLAGKKDKKEEEkkkdekkGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHF 256
Cdd:cd01377   81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKK-------GTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHF 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 257 GTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKILAVPDPGLYGFINQGTLTVDGIDDEEEMGLT 336
Cdd:cd01377  154 GSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLT 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 337 DTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQ--RGEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVT 414
Cdd:cd01377  234 DEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQrrREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVT 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 415 QGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHH 494
Cdd:cd01377  314 KGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHH 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 495 MFVLEQEEYKKEGIVWEFIDFGLDLQACIELIEKP-MGILSILEEECMFPKASDTSFKNKLYDNHLGKNPMFGKPKPPKA 573
Cdd:cd01377  394 MFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKPKKS 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 574 gcaEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRILTPGGKKKKGKSAAFQTISSVHKE 653
Cdd:cd01377  474 ---EAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGGGKKKKKGGSFRTVSQLHKE 550
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 654 SLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNAVPSG 733
Cdd:cd01377  551 QLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKG 630
                        650       660       670
                 ....*....|....*....|....*....|..
gi 254839636 734 FADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd01377  631 FDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
Myosin_N pfam02736
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ...
29-74 2.13e-17

Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.


:

Pssm-ID: 426949  Cd Length: 45  Bit Score: 76.32  E-value: 2.13e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 254839636   29 DGKKNCWVPDPDFGFVGAEIQSTKGDEVTVKTDkTQETRVVKKDDI 74
Cdd:pfam02736   1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETE-DGKTVTVKKDDV 45
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
779-801 7.91e-05

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


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 40.00  E-value: 7.91e-05
                           10        20
                   ....*....|....*....|...
gi 254839636   779 RLSKIISMFQAHIRGYLMRKAYK 801
Cdd:smart00015   1 RLTRAAIIIQAAWRGYLARKRYK 23
 
Name Accession Description Interval E-value
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
97-765 0e+00

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


Pssm-ID: 276951 [Multi-domain]  Cd Length: 662  Bit Score: 1345.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITG 176
Cdd:cd01377    1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 177 ESGAGKTENTKKVIQYFALVAASLAGKKDKKEEEkkkdekkGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHF 256
Cdd:cd01377   81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKK-------GTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHF 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 257 GTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKILAVPDPGLYGFINQGTLTVDGIDDEEEMGLT 336
Cdd:cd01377  154 GSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLT 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 337 DTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQ--RGEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVT 414
Cdd:cd01377  234 DEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQrrREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVT 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 415 QGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHH 494
Cdd:cd01377  314 KGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHH 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 495 MFVLEQEEYKKEGIVWEFIDFGLDLQACIELIEKP-MGILSILEEECMFPKASDTSFKNKLYDNHLGKNPMFGKPKPPKA 573
Cdd:cd01377  394 MFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKPKKS 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 574 gcaEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRILTPGGKKKKGKSAAFQTISSVHKE 653
Cdd:cd01377  474 ---EAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGGGKKKKKGGSFRTVSQLHKE 550
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 654 SLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNAVPSG 733
Cdd:cd01377  551 QLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKG 630
                        650       660       670
                 ....*....|....*....|....*....|..
gi 254839636 734 FADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd01377  631 FDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
Myosin_head pfam00063
Myosin head (motor domain);
87-765 0e+00

Myosin head (motor domain);


Pssm-ID: 395017  Cd Length: 674  Bit Score: 1024.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636   87 DMANLTFLNEASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQD 166
Cdd:pfam00063   3 DMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  167 RENQSMLITGESGAGKTENTKKVIQYFALVAASlagkkdkkeeekKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSS 246
Cdd:pfam00063  83 KENQSILISGESGAGKTENTKKIMQYLASVSGS------------GSAGNVGRLEEQILQSNPILEAFGNAKTVRNNNSS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  247 RFGKFIRIHFGTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKiLAVPDPGLYGFINQ-GTLTVD 325
Cdd:pfam00063 151 RFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKE-LRLTNPKDYHYLSQsGCYTID 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  326 GIDDEEEMGLTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQ--RGEQAEADGTAEAEKVAFLLGVNAGDLLKCLLK 403
Cdd:pfam00063 230 GIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKerNDEQAVPDDTENLQKAASLLGIDSTELEKALCK 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  404 PKIKVGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKA-KRQFFIGVLDIAGFEIFDFNSFEQLCINY 482
Cdd:pfam00063 310 RRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINY 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  483 TNERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGlDLQACIELIE-KPMGILSILEEECMFPKASDTSFKNKLYDNHlGK 561
Cdd:pfam00063 390 VNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SK 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  562 NPMFGKPKPPKagcaEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRILTPGGKKKKGKS 641
Cdd:pfam00063 468 HPHFQKPRLQG----ETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKS 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  642 AA-------FQTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRII 714
Cdd:pfam00063 544 TPkrtkkkrFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRIT 623
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|.
gi 254839636  715 YSEFKQRYSILAPNAVPSGFADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:pfam00063 624 FQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
78-777 0e+00

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


Pssm-ID: 214580 [Multi-domain]  Cd Length: 677  Bit Score: 1015.16  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636    78 NPPKFEMNMDMANLTFLNEASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIAD 157
Cdd:smart00242   1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636   158 NAYQYMLQDRENQSMLITGESGAGKTENTKKVIQYFALVAASlagkkdkkeeekkkDEKKGTLEDQIVQCNPVLEAYGNA 237
Cdd:smart00242  81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGS--------------NTEVGSVEDQILESNPILEAFGNA 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636   238 KTTRNNNSSRFGKFIRIHFGTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKiLAVPDPGLYGFI 317
Cdd:smart00242 147 KTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKE-LGLKSPEDYRYL 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636   318 NQG-TLTVDGIDDEEEMGLTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQRGE---QAEADGTAEAEKVAFLLGVN 393
Cdd:smart00242 226 NQGgCLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNdnaASTVKDKEELSNAAELLGVD 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636   394 AGDLLKCLLKPKIKVGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFN 473
Cdd:smart00242 306 PEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVN 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636   474 SFEQLCINYTNERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGlDLQACIELIE-KPMGILSILEEECMFPKASDTSFKN 552
Cdd:smart00242 386 SFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLE 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636   553 KLYdNHLGKNPMFGKPKPPkagcAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFtppriltP 632
Cdd:smart00242 465 KLN-QHHKKHPHFSKPKKK----GRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLF-------P 532
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636   633 GGKKKKGKSAAFQTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNR 712
Cdd:smart00242 533 SGVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYR 612
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254839636   713 IIYSEFKQRYSILAPNAVPSGFADGKVVTDKALSALQLDPNEYRLGNTKVFFKAGVLGMLEDMRD 777
Cdd:smart00242 613 LPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
COG5022 COG5022
Myosin heavy chain [General function prediction only];
24-839 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 922.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636   24 TSIPFDGKKNCWVPDPDFGFVGAEIQST---KGDEVTVKTDKTQETRVVKKDDIGQ--RNPPKFEMNMDMANLTFLNEAS 98
Cdd:COG5022     2 STTNAEVGSGCWIPDEEKGWIWAEIIKEafnKGKVTEEGKKEDGESVSVKKKVLGNdrIKLPKFDGVDDLTELSYLNEPA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636   99 ILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITGES 178
Cdd:COG5022    82 VLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGES 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  179 GAGKTENTKKVIQYFALVAASlagkkdkkeeekkKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHFGT 258
Cdd:COG5022   162 GAGKTENAKRIMQYLASVTSS-------------STVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  259 QGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAfPENIEKILAVPDPGLYGFINQGTLT-VDGIDDEEEMGLTD 337
Cdd:COG5022   229 NGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGD-PEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITL 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  338 TAFDVLGFTDEEKLSMYKCTGCILHLG--EMKwKQRGEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVTQ 415
Cdd:COG5022   308 DALKTIGIDEEEQDQIFKILAAILHIGniEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVV 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  416 GRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHM 495
Cdd:COG5022   387 PLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHM 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  496 FVLEQEEYKKEGIVWEFIDFgLDLQACIELIEK--PMGILSILEEECMFPKASDTSFKNKLYDN-HLGKNPMFGKPKppk 572
Cdd:COG5022   467 FKLEQEEYVKEGIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSR--- 542
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  573 agCAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFtppriltpGGKKKKGKSAAFQTISSVHK 652
Cdd:COG5022   543 --FRDNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLF--------DDEENIESKGRFPTLGSRFK 612
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  653 ESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNAVPS 732
Cdd:COG5022   613 ESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWT 692
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  733 G----FADGKVVTDKALSALQLDPNEYRLGNTKVFFKAGVLGMLEDMRDERLSKIISMFQAHIRGYLMRKAY-KKLQDQR 807
Cdd:COG5022   693 GeytwKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYlQALKRIK 772
                         810       820       830
                  ....*....|....*....|....*....|..
gi 254839636  808 iGLTLIQRNVRKWLVLRNWEWWRLFNKVKPLL 839
Cdd:COG5022   773 -KIQVIQHGFRLRRLVDYELKWRLFIKLQPLL 803
PTZ00014 PTZ00014
myosin-A; Provisional
38-822 3.26e-148

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 456.03  E-value: 3.26e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  38 DPDFGFVGAEIQ-STKGDEVTVK--TDKTQETRVVKKDDIGQRNPPkFEMNM--DMANLTFLNEASILHNLRSRYESGFI 112
Cdd:PTZ00014  47 DPDLMFAKCLVLpGSTGEKLTLKqiDPPTNSTFEVKPEHAFNANSQ-IDPMTygDIGLLPHTNIPCVLDFLKHRYLKNQI 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 113 YTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAE-MPPHLFSIADNAYQYMLQDRENQSMLITGESGAGKTENTKKVIQ 191
Cdd:PTZ00014 126 YTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMR 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 192 YFAlvaASLAGKKDkkeeekkkdekkGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHFGTQGKIAGADIETYL 271
Cdd:PTZ00014 206 YFA---SSKSGNMD------------LKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFL 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 272 LEKSRVTYQQSAERNYHIFYQLLSPAFPENIEK--ILAVPDpglYGFINQGTLTVDGIDDEEEMGLTDTAFDVLGFTDEE 349
Cdd:PTZ00014 271 LEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKykLKSLEE---YKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQ 347
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 350 KLSMYKCTGCILHLG--EMKWKQRGEQAEADGTAEAEKVAF-----LLGVNAGDLLKCLLKPKIKVGTEYVTQGRNKDQV 422
Cdd:PTZ00014 348 IEDIFSILSGVLLLGnvEIEGKEEGGLTDAAAISDESLEVFneaceLLFLDYESLKKELTVKVTYAGNQKIEGPWSKDES 427
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 423 TNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFVLEQEE 502
Cdd:PTZ00014 428 EMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKL 507
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 503 YKKEGIVWEFIDFGLDLQACIELIEKPMGILSILEEECMFPKASDTSFKNKLYdNHLGKNPMFGKPKPPKAGCaeahFCL 582
Cdd:PTZ00014 508 YKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCN-TNLKNNPKYKPAKVDSNKN----FVI 582
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 583 HHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRIltpggkkKKGKSAAFQTISSVHKESLNKLMKNL 662
Cdd:PTZ00014 583 KHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEV-------EKGKLAKGQLIGSQFLNQLDSLMSLI 655
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 663 YSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNAVPSGFADGKVVTD 742
Cdd:PTZ00014 656 NSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAE 735
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 743 KALSALQLDPNEYRLGNTKVFFKAGVLGMLEDMRDERLSK---IISMFQAHIRGYLMRKAYKK-LQDqrigLTLIQRNVR 818
Cdd:PTZ00014 736 KLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQREKLAAwepLVSVLEALILKIKKKRKVRKnIKS----LVRIQAHLR 811

                 ....
gi 254839636 819 KWLV 822
Cdd:PTZ00014 812 RHLV 815
Myosin_N pfam02736
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ...
29-74 2.13e-17

Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.


Pssm-ID: 426949  Cd Length: 45  Bit Score: 76.32  E-value: 2.13e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 254839636   29 DGKKNCWVPDPDFGFVGAEIQSTKGDEVTVKTDkTQETRVVKKDDI 74
Cdd:pfam02736   1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETE-DGKTVTVKKDDV 45
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
779-801 7.91e-05

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 40.00  E-value: 7.91e-05
                           10        20
                   ....*....|....*....|...
gi 254839636   779 RLSKIISMFQAHIRGYLMRKAYK 801
Cdd:smart00015   1 RLTRAAIIIQAAWRGYLARKRYK 23
 
Name Accession Description Interval E-value
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
97-765 0e+00

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


Pssm-ID: 276951 [Multi-domain]  Cd Length: 662  Bit Score: 1345.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITG 176
Cdd:cd01377    1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 177 ESGAGKTENTKKVIQYFALVAASLAGKKDKKEEEkkkdekkGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHF 256
Cdd:cd01377   81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKK-------GTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHF 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 257 GTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKILAVPDPGLYGFINQGTLTVDGIDDEEEMGLT 336
Cdd:cd01377  154 GSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLT 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 337 DTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQ--RGEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVT 414
Cdd:cd01377  234 DEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQrrREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVT 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 415 QGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHH 494
Cdd:cd01377  314 KGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHH 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 495 MFVLEQEEYKKEGIVWEFIDFGLDLQACIELIEKP-MGILSILEEECMFPKASDTSFKNKLYDNHLGKNPMFGKPKPPKA 573
Cdd:cd01377  394 MFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKPKKS 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 574 gcaEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRILTPGGKKKKGKSAAFQTISSVHKE 653
Cdd:cd01377  474 ---EAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGGGKKKKKGGSFRTVSQLHKE 550
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 654 SLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNAVPSG 733
Cdd:cd01377  551 QLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKG 630
                        650       660       670
                 ....*....|....*....|....*....|..
gi 254839636 734 FADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd01377  631 FDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
Myosin_head pfam00063
Myosin head (motor domain);
87-765 0e+00

Myosin head (motor domain);


Pssm-ID: 395017  Cd Length: 674  Bit Score: 1024.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636   87 DMANLTFLNEASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQD 166
Cdd:pfam00063   3 DMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  167 RENQSMLITGESGAGKTENTKKVIQYFALVAASlagkkdkkeeekKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSS 246
Cdd:pfam00063  83 KENQSILISGESGAGKTENTKKIMQYLASVSGS------------GSAGNVGRLEEQILQSNPILEAFGNAKTVRNNNSS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  247 RFGKFIRIHFGTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKiLAVPDPGLYGFINQ-GTLTVD 325
Cdd:pfam00063 151 RFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKE-LRLTNPKDYHYLSQsGCYTID 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  326 GIDDEEEMGLTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQ--RGEQAEADGTAEAEKVAFLLGVNAGDLLKCLLK 403
Cdd:pfam00063 230 GIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKerNDEQAVPDDTENLQKAASLLGIDSTELEKALCK 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  404 PKIKVGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKA-KRQFFIGVLDIAGFEIFDFNSFEQLCINY 482
Cdd:pfam00063 310 RRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINY 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  483 TNERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGlDLQACIELIE-KPMGILSILEEECMFPKASDTSFKNKLYDNHlGK 561
Cdd:pfam00063 390 VNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SK 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  562 NPMFGKPKPPKagcaEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRILTPGGKKKKGKS 641
Cdd:pfam00063 468 HPHFQKPRLQG----ETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKS 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  642 AA-------FQTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRII 714
Cdd:pfam00063 544 TPkrtkkkrFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRIT 623
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|.
gi 254839636  715 YSEFKQRYSILAPNAVPSGFADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:pfam00063 624 FQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
78-777 0e+00

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


Pssm-ID: 214580 [Multi-domain]  Cd Length: 677  Bit Score: 1015.16  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636    78 NPPKFEMNMDMANLTFLNEASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIAD 157
Cdd:smart00242   1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636   158 NAYQYMLQDRENQSMLITGESGAGKTENTKKVIQYFALVAASlagkkdkkeeekkkDEKKGTLEDQIVQCNPVLEAYGNA 237
Cdd:smart00242  81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGS--------------NTEVGSVEDQILESNPILEAFGNA 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636   238 KTTRNNNSSRFGKFIRIHFGTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKiLAVPDPGLYGFI 317
Cdd:smart00242 147 KTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKE-LGLKSPEDYRYL 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636   318 NQG-TLTVDGIDDEEEMGLTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQRGE---QAEADGTAEAEKVAFLLGVN 393
Cdd:smart00242 226 NQGgCLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNdnaASTVKDKEELSNAAELLGVD 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636   394 AGDLLKCLLKPKIKVGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFN 473
Cdd:smart00242 306 PEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVN 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636   474 SFEQLCINYTNERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGlDLQACIELIE-KPMGILSILEEECMFPKASDTSFKN 552
Cdd:smart00242 386 SFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLE 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636   553 KLYdNHLGKNPMFGKPKPPkagcAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFtppriltP 632
Cdd:smart00242 465 KLN-QHHKKHPHFSKPKKK----GRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLF-------P 532
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636   633 GGKKKKGKSAAFQTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNR 712
Cdd:smart00242 533 SGVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYR 612
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254839636   713 IIYSEFKQRYSILAPNAVPSGFADGKVVTDKALSALQLDPNEYRLGNTKVFFKAGVLGMLEDMRD 777
Cdd:smart00242 613 LPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
MYSc_Myh7b cd14927
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...
97-765 0e+00

class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276953 [Multi-domain]  Cd Length: 676  Bit Score: 999.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITG 176
Cdd:cd14927    1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 177 ESGAGKTENTKKVIQYFALVAAslAGKKDKKEEEKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHF 256
Cdd:cd14927   81 ESGAGKTVNTKRVIQYFAIVAA--LGDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 257 GTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKILAVPDPGLYGFINQGTLTVDGIDDEEEMGLT 336
Cdd:cd14927  159 GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMAT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 337 DTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWK--QRGEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVT 414
Cdd:cd14927  239 DHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKqkQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVT 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 415 QGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHH 494
Cdd:cd14927  319 KGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 495 MFVLEQEEYKKEGIVWEFIDFGLDLQACIELIEKPMGILSILEEECMFPKASDTSFKNKLYDNHLGKNPMFGKPKPPKAG 574
Cdd:cd14927  399 MFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKR 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 575 CAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLF---------TPPRILTpggKKKKGKSAAFQ 645
Cdd:cd14927  479 KYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYenyvgsdstEDPKSGV---KEKRKKAASFQ 555
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 646 TISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSIL 725
Cdd:cd14927  556 TVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRIL 635
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|.
gi 254839636 726 APNAVP-SGFADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14927  636 NPSAIPdDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
MYSc_Myh1_insects_crustaceans cd14909
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
97-765 0e+00

class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276874  Cd Length: 666  Bit Score: 985.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITG 176
Cdd:cd14909    1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 177 ESGAGKTENTKKVIQYFALVAASlagkkdkkEEEKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHF 256
Cdd:cd14909   81 ESGAGKTENTKKVIAYFATVGAS--------KKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 257 GTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKILAVPDPGLYGFINQGTLTVDGIDDEEEMGLT 336
Cdd:cd14909  153 GPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLT 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 337 DTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQRG--EQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVT 414
Cdd:cd14909  233 DQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGreEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVT 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 415 QGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHH 494
Cdd:cd14909  313 QGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHH 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 495 MFVLEQEEYKKEGIVWEFIDFGLDLQACIELIEKPMGILSILEEECMFPKASDTSFKNKLYDNHLGKNPMFGKPKPPKAG 574
Cdd:cd14909  393 MFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPG 472
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 575 CAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFT--PPRILTPGGKK--KKGKSAAFQTISSV 650
Cdd:cd14909  473 QQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAdhAGQSGGGEQAKggRGKKGGGFATVSSA 552
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 651 HKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNAV 730
Cdd:cd14909  553 YKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGI 632
                        650       660       670
                 ....*....|....*....|....*....|....*
gi 254839636 731 pSGFADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14909  633 -QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
MYSc_Myh3 cd14913
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...
98-765 0e+00

class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276878 [Multi-domain]  Cd Length: 668  Bit Score: 975.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  98 SILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITGE 177
Cdd:cd14913    2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 178 SGAGKTENTKKVIQYFALVAASlagkkdKKEEEKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHFG 257
Cdd:cd14913   82 SGAGKTVNTKRVIQYFATIAAT------GDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 258 TQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKILAVPDPGLYGFINQGTLTVDGIDDEEEMGLTD 337
Cdd:cd14913  156 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 338 TAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQ--RGEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVTQ 415
Cdd:cd14913  236 SAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQkqREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTK 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 416 GRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHM 495
Cdd:cd14913  316 GQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHM 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 496 FVLEQEEYKKEGIVWEFIDFGLDLQACIELIEKPMGILSILEEECMFPKASDTSFKNKLYDNHLGKNPMFGKPKPPKaGC 575
Cdd:cd14913  396 FVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVK-GR 474
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 576 AEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRILTPGGKKKKGKS---AAFQTISSVHK 652
Cdd:cd14913  475 AEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAKkkgSSFQTVSALFR 554
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 653 ESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNAVPS 732
Cdd:cd14913  555 ENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPE 634
                        650       660       670
                 ....*....|....*....|....*....|....
gi 254839636 733 G-FADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14913  635 GqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myh16 cd14934
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...
97-765 0e+00

class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.


Pssm-ID: 276896 [Multi-domain]  Cd Length: 659  Bit Score: 958.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITG 176
Cdd:cd14934    1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 177 ESGAGKTENTKKVIQYFALVAASlagkkdkkeeEKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHF 256
Cdd:cd14934   81 ESGAGKTENTKKVIQYFANIGGT----------GKQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHF 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 257 GTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKILAVPDPGLYGFINQGTLTVDGIDDEEEMGLT 336
Cdd:cd14934  151 GTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQIT 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 337 DTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQ--RGEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVT 414
Cdd:cd14934  231 DVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQkpREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQ 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 415 QGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHH 494
Cdd:cd14934  311 KGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 495 MFVLEQEEYKKEGIVWEFIDFGLDLQACIELIEKPMGILSILEEECMFPKASDTSFKNKLYDNHLGKNPMFGKPKPPKAG 574
Cdd:cd14934  391 MFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGK 470
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 575 CAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRilTPGGKKKKGKSAAFQTISSVHKES 654
Cdd:cd14934  471 GPEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEE--APAGSKKQKRGSSFMTVSNFYREQ 548
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 655 LNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNAVPSGF 734
Cdd:cd14934  549 LNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQGF 628
                        650       660       670
                 ....*....|....*....|....*....|.
gi 254839636 735 ADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14934  629 VDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
COG5022 COG5022
Myosin heavy chain [General function prediction only];
24-839 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 922.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636   24 TSIPFDGKKNCWVPDPDFGFVGAEIQST---KGDEVTVKTDKTQETRVVKKDDIGQ--RNPPKFEMNMDMANLTFLNEAS 98
Cdd:COG5022     2 STTNAEVGSGCWIPDEEKGWIWAEIIKEafnKGKVTEEGKKEDGESVSVKKKVLGNdrIKLPKFDGVDDLTELSYLNEPA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636   99 ILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITGES 178
Cdd:COG5022    82 VLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGES 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  179 GAGKTENTKKVIQYFALVAASlagkkdkkeeekkKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHFGT 258
Cdd:COG5022   162 GAGKTENAKRIMQYLASVTSS-------------STVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  259 QGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAfPENIEKILAVPDPGLYGFINQGTLT-VDGIDDEEEMGLTD 337
Cdd:COG5022   229 NGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGD-PEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITL 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  338 TAFDVLGFTDEEKLSMYKCTGCILHLG--EMKwKQRGEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVTQ 415
Cdd:COG5022   308 DALKTIGIDEEEQDQIFKILAAILHIGniEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVV 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  416 GRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHM 495
Cdd:COG5022   387 PLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHM 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  496 FVLEQEEYKKEGIVWEFIDFgLDLQACIELIEK--PMGILSILEEECMFPKASDTSFKNKLYDN-HLGKNPMFGKPKppk 572
Cdd:COG5022   467 FKLEQEEYVKEGIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSR--- 542
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  573 agCAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFtppriltpGGKKKKGKSAAFQTISSVHK 652
Cdd:COG5022   543 --FRDNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLF--------DDEENIESKGRFPTLGSRFK 612
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  653 ESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNAVPS 732
Cdd:COG5022   613 ESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWT 692
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  733 G----FADGKVVTDKALSALQLDPNEYRLGNTKVFFKAGVLGMLEDMRDERLSKIISMFQAHIRGYLMRKAY-KKLQDQR 807
Cdd:COG5022   693 GeytwKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYlQALKRIK 772
                         810       820       830
                  ....*....|....*....|....*....|..
gi 254839636  808 iGLTLIQRNVRKWLVLRNWEWWRLFNKVKPLL 839
Cdd:COG5022   773 -KIQVIQHGFRLRRLVDYELKWRLFIKLQPLL 803
MYSc_Myh7 cd14917
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...
98-765 0e+00

class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276881 [Multi-domain]  Cd Length: 668  Bit Score: 912.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  98 SILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITGE 177
Cdd:cd14917    2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 178 SGAGKTENTKKVIQYFALVAAslagkkDKKEEEKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHFG 257
Cdd:cd14917   82 SGAGKTVNTKRVIQYFAVIAA------IGDRSKKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 258 TQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKILAVPDPGLYGFINQGTLTVDGIDDEEEMGLTD 337
Cdd:cd14917  156 ATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 338 TAFDVLGFTDEEKLSMYKCTGCILHLGEMKWK--QRGEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVTQ 415
Cdd:cd14917  236 NAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKqkQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTK 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 416 GRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHM 495
Cdd:cd14917  316 GQNVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 496 FVLEQEEYKKEGIVWEFIDFGLDLQACIELIEKPMGILSILEEECMFPKASDTSFKNKLYDNHLGKNPMFGKPKPPKaGC 575
Cdd:cd14917  396 FVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIK-GK 474
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 576 AEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTP---PRILTPGGKKKKGKSAAFQTISSVHK 652
Cdd:cd14917  475 PEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANyagADAPIEKGKGKAKKGSSFQTVSALHR 554
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 653 ESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNAVPS 732
Cdd:cd14917  555 ENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPE 634
                        650       660       670
                 ....*....|....*....|....*....|....
gi 254839636 733 G-FADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14917  635 GqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
MYSc_Myh15_mammals cd14929
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...
97-765 0e+00

class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276892 [Multi-domain]  Cd Length: 662  Bit Score: 906.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITG 176
Cdd:cd14929    1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 177 ESGAGKTENTKKVIQYFALVAAslagkkdkkeeEKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHF 256
Cdd:cd14929   81 ESGAGKTVNTKHIIQYFATIAA-----------MIESKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHF 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 257 GTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSpAFPENIEKILAVPDPGLYGFINQGTLTVDGIDDEEEMGLT 336
Cdd:cd14929  150 GARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILS-GKKELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLAT 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 337 DTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQ--RGEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVT 414
Cdd:cd14929  229 EQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQkpREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVT 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 415 QGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHH 494
Cdd:cd14929  309 RSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQH 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 495 MFVLEQEEYKKEGIVWEFIDFGLDLQACIELIEKPMGILSILEEECMFPKASDTSFKNKLYDNHLGKNPMFGKPKPPKAG 574
Cdd:cd14929  389 MFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKK 468
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 575 cAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRI---LTPGGKKKKGKSAAFQTISSVH 651
Cdd:cd14929  469 -FEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYIStdsAIQFGEKKRKKGASFQTVASLH 547
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 652 KESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNAVP 731
Cdd:cd14929  548 KENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFP 627
                        650       660       670
                 ....*....|....*....|....*....|....*
gi 254839636 732 -SGFADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14929  628 kSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
MYSc_Myh13 cd14923
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...
98-765 0e+00

class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276887 [Multi-domain]  Cd Length: 671  Bit Score: 905.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  98 SILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITGE 177
Cdd:cd14923    2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 178 SGAGKTENTKKVIQYFALVAASlagkkDKKEEEKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHFG 257
Cdd:cd14923   82 SGAGKTVNTKRVIQYFATIAVT-----GDKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 258 TQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKILAVPDPGLYGFINQGTLTVDGIDDEEEMGLTD 337
Cdd:cd14923  157 ATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATD 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 338 TAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQ--RGEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVTQ 415
Cdd:cd14923  237 NAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQkqREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTK 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 416 GRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHM 495
Cdd:cd14923  317 GQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 496 FVLEQEEYKKEGIVWEFIDFGLDLQACIELIEKPMGILSILEEECMFPKASDTSFKNKLYDNHLGKNPMFGKPKPPKaGC 575
Cdd:cd14923  397 FVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAK-GK 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 576 AEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRILTP-----GGKKKKGKSAAFQTISSV 650
Cdd:cd14923  476 AEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAgdsggSKKGGKKKGSSFQTVSAV 555
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 651 HKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNAV 730
Cdd:cd14923  556 FRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAI 635
                        650       660       670
                 ....*....|....*....|....*....|....*.
gi 254839636 731 PSG-FADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14923  636 PEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
MYSc_Myh1_mammals cd14910
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
98-765 0e+00

class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276875 [Multi-domain]  Cd Length: 671  Bit Score: 901.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  98 SILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITGE 177
Cdd:cd14910    2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 178 SGAGKTENTKKVIQYFALVAASlagkKDKKEEEKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHFG 257
Cdd:cd14910   82 SGAGKTVNTKRVIQYFATIAVT----GEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 258 TQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKILAVPDPGLYGFINQGTLTVDGIDDEEEMGLTD 337
Cdd:cd14910  158 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATD 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 338 TAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQ--RGEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVTQ 415
Cdd:cd14910  238 SAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQkqREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTK 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 416 GRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHM 495
Cdd:cd14910  318 GQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 496 FVLEQEEYKKEGIVWEFIDFGLDLQACIELIEKPMGILSILEEECMFPKASDTSFKNKLYDNHLGKNPMFGKPKPPKaGC 575
Cdd:cd14910  398 FVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAK-GK 476
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 576 AEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRILTPG----GKKKKGKSAAFQTISSVH 651
Cdd:cd14910  477 VEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEegggKKGGKKKGSSFQTVSALF 556
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 652 KESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNAVP 731
Cdd:cd14910  557 RENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 636
                        650       660       670
                 ....*....|....*....|....*....|....*
gi 254839636 732 SG-FADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14910  637 EGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh4 cd14915
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...
98-765 0e+00

class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276879 [Multi-domain]  Cd Length: 671  Bit Score: 900.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  98 SILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITGE 177
Cdd:cd14915    2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 178 SGAGKTENTKKVIQYFALVAASlagkKDKKEEEKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHFG 257
Cdd:cd14915   82 SGAGKTVNTKRVIQYFATIAVT----GEKKKEEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 258 TQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKILAVPDPGLYGFINQGTLTVDGIDDEEEMGLTD 337
Cdd:cd14915  158 ATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATD 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 338 TAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQ--RGEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVTQ 415
Cdd:cd14915  238 SAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQkqREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTK 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 416 GRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHM 495
Cdd:cd14915  318 GQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 496 FVLEQEEYKKEGIVWEFIDFGLDLQACIELIEKPMGILSILEEECMFPKASDTSFKNKLYDNHLGKNPMFGKPKPPKaGC 575
Cdd:cd14915  398 FVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAK-GK 476
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 576 AEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRILTPG----GKKKKGKSAAFQTISSVH 651
Cdd:cd14915  477 AEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEggggKKGGKKKGSSFQTVSALF 556
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 652 KESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNAVP 731
Cdd:cd14915  557 RENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 636
                        650       660       670
                 ....*....|....*....|....*....|....*
gi 254839636 732 SG-FADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14915  637 EGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh8 cd14918
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...
99-765 0e+00

class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276882 [Multi-domain]  Cd Length: 668  Bit Score: 899.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  99 ILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITGES 178
Cdd:cd14918    3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 179 GAGKTENTKKVIQYFALVAASlagkkdKKEEEKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHFGT 258
Cdd:cd14918   83 GAGKTVNTKRVIQYFATIAVT------GEKKKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 259 QGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKILAVPDPGLYGFINQGTLTVDGIDDEEEMGLTDT 338
Cdd:cd14918  157 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDS 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 339 AFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQ--RGEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVTQG 416
Cdd:cd14918  237 AIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQkqREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 417 RNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMF 496
Cdd:cd14918  317 QTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 497 VLEQEEYKKEGIVWEFIDFGLDLQACIELIEKPMGILSILEEECMFPKASDTSFKNKLYDNHLGKNPMFGKPKPPKaGCA 576
Cdd:cd14918  397 VLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVK-GKA 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 577 EAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFT---PPRILTPGGKKKKGKSAAFQTISSVHKE 653
Cdd:cd14918  476 EAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFStyaSAEADSGAKKGAKKKGSSFQTVSALFRE 555
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 654 SLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNAVPSG 733
Cdd:cd14918  556 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEG 635
                        650       660       670
                 ....*....|....*....|....*....|...
gi 254839636 734 -FADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14918  636 qFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myh2_mammals cd14912
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
98-765 0e+00

class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276877 [Multi-domain]  Cd Length: 673  Bit Score: 897.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  98 SILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITGE 177
Cdd:cd14912    2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 178 SGAGKTENTKKVIQYFALVAASlagkKDKKEEEKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHFG 257
Cdd:cd14912   82 SGAGKTVNTKRVIQYFATIAVT----GEKKKEEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 258 TQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKILAVPDPGLYGFINQGTLTVDGIDDEEEMGLTD 337
Cdd:cd14912  158 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATD 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 338 TAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQ--RGEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVTQ 415
Cdd:cd14912  238 SAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQkqREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTK 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 416 GRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHM 495
Cdd:cd14912  318 GQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 496 FVLEQEEYKKEGIVWEFIDFGLDLQACIELIEKPMGILSILEEECMFPKASDTSFKNKLYDNHLGKNPMFGKPKPPKaGC 575
Cdd:cd14912  398 FVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVK-GK 476
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 576 AEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRILT------PGGKKKKGKSAAFQTISS 649
Cdd:cd14912  477 AEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEgasaggGAKKGGKKKGSSFQTVSA 556
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 650 VHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNA 729
Cdd:cd14912  557 LFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASA 636
                        650       660       670
                 ....*....|....*....|....*....|....*..
gi 254839636 730 VPSG-FADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14912  637 IPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
MYSc_Myh6 cd14916
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...
98-765 0e+00

class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276880 [Multi-domain]  Cd Length: 670  Bit Score: 895.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  98 SILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITGE 177
Cdd:cd14916    2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 178 SGAGKTENTKKVIQYFALVAAslagkKDKKEEEKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHFG 257
Cdd:cd14916   82 SGAGKTVNTKRVIQYFASIAA-----IGDRSKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 258 TQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKILAVPDPGLYGFINQGTLTVDGIDDEEEMGLTD 337
Cdd:cd14916  157 ATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATD 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 338 TAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQ--RGEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVTQ 415
Cdd:cd14916  237 SAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQkqREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTK 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 416 GRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHM 495
Cdd:cd14916  317 GQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 496 FVLEQEEYKKEGIVWEFIDFGLDLQACIELIEKPMGILSILEEECMFPKASDTSFKNKLYDNHLGKNPMFGKPKPPKaGC 575
Cdd:cd14916  397 FVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVK-GK 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 576 AEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRIL----TPGGKKKKGKSAAFQTISSVH 651
Cdd:cd14916  476 QEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASAdtgdSGKGKGGKKKGSSFQTVSALH 555
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 652 KESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNAVP 731
Cdd:cd14916  556 RENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIP 635
                        650       660       670
                 ....*....|....*....|....*....|....*
gi 254839636 732 SG-FADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14916  636 EGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
97-765 0e+00

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


Pssm-ID: 276950  Cd Length: 633  Bit Score: 855.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRR-AEMPPHLFSIADNAYQYMLQDRENQSMLIT 175
Cdd:cd00124    1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 176 GESGAGKTENTKKVIQYFALVAASLAGKKDKKEeekkkdekkGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIH 255
Cdd:cd00124   81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSA---------SSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQ 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 256 FGTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLL---SPAFPENIEKILAVPDPGLYGFINQGTL-TVDGIDDEE 331
Cdd:cd00124  152 FDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLaglSDGAREELKLELLLSYYYLNDYLNSSGCdRIDGVDDAE 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 332 EMGLTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQRGE----QAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIK 407
Cdd:cd00124  232 EFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEdedsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIK 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 408 VGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQF--FIGVLDIAGFEIFDFNSFEQLCINYTNE 485
Cdd:cd00124  312 VGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEStsFIGILDIFGFENFEVNSFEQLCINYANE 391
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 486 RLQQFFNHHMFVLEQEEYKKEGIVWEFIDFgLDLQACIELIE-KPMGILSILEEECMFPKASDTSFKNKLYDNHLGKNPM 564
Cdd:cd00124  392 KLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRF 470
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 565 FGKPKPpkagcAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNskepivkmlftppriltpggkkkkgksaaf 644
Cdd:cd00124  471 FSKKRK-----AKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRS------------------------------ 515
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 645 qtiSSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSI 724
Cdd:cd00124  516 ---GSQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRI 592
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|.
gi 254839636 725 LAPNAVPSGFADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd00124  593 LAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
97-765 0e+00

class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276876 [Multi-domain]  Cd Length: 674  Bit Score: 834.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITG 176
Cdd:cd14911    1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 177 ESGAGKTENTKKVIQYFALVAASLA-GKKDKKEEEKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIH 255
Cdd:cd14911   81 ESGAGKTENTKKVIQFLAYVAASKPkGSGAVPHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 256 FGTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKILaVPDPGLYGFINQGTLTVDGIDDEEEMGL 335
Cdd:cd14911  161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFI-LDDVKSYAFLSNGSLPVPGVDDYAEFQA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 336 TDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQR--GEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYV 413
Cdd:cd14911  240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQErnNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 414 TQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDtKAKRQ--FFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFF 491
Cdd:cd14911  320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLD-RTKRQgaSFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLF 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 492 NHHMFVLEQEEYKKEGIVWEFIDFGLDLQACIELIEKPMGILSILEEECMFPKASDTSFKNKLYDNHlGKNPMFGKPKpp 571
Cdd:cd14911  399 NHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFMKTD-- 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 572 KAGCAEahFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRI-------LTPGGKKKKGKSAAF 644
Cdd:cd14911  476 FRGVAD--FAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIvgmaqqaLTDTQFGARTRKGMF 553
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 645 QTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSI 724
Cdd:cd14911  554 RTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEL 633
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|.
gi 254839636 725 LAPNAVPSGFADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14911  634 LTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
97-765 0e+00

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: 794.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITG 176
Cdd:cd14920    1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 177 ESGAGKTENTKKVIQYFALVAASLAGKKDKKEEekkkdekkGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHF 256
Cdd:cd14920   81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIP--------GELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 257 GTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAfPENIEKILAVPDPGLYGFINQGTLTVDGIDDEEEMGLT 336
Cdd:cd14920  153 DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGA-GEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQET 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 337 DTAFDVLGFTDEEKLSMYKCTGCILHLGE---MKWKQRGEQAEADGTAeAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYV 413
Cdd:cd14920  232 MEAMHIMGFSHEEILSMLKVVSSVLQFGNisfKKERNTDQASMPENTV-AQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 414 TQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDtKAKRQ--FFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFF 491
Cdd:cd14920  311 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD-RTKRQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 492 NHHMFVLEQEEYKKEGIVWEFIDFGLDLQACIELIEKPM---GILSILEEECMFPKASDTSFKNKLyDNHLGKNPMFGKP 568
Cdd:cd14920  390 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKL-VQEQGSHSKFQKP 468
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 569 KPPKAgcaEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTP-PRIL----------TPGGKKK 637
Cdd:cd14920  469 RQLKD---KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvDRIVgldqvtgmteTAFGSAY 545
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 638 KGKSAAFQTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSE 717
Cdd:cd14920  546 KTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 625
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....*...
gi 254839636 718 FKQRYSILAPNAVPSGFADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14920  626 FRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
97-765 0e+00

class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276895 [Multi-domain]  Cd Length: 676  Bit Score: 755.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITG 176
Cdd:cd14932    1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 177 ESGAGKTENTKKVIQYFALVAASLagkkDKKEEEKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHF 256
Cdd:cd14932   81 ESGAGKTENTKKVIQYLAYVASSF----KTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 257 GTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAfPENIEKILAVPDPGLYGFINQGTLTVDGIDDEEEMGLT 336
Cdd:cd14932  157 DVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGA-GDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAET 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 337 DTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQR--GEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVT 414
Cdd:cd14932  236 MEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKErnSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQ 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 415 QGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDtKAKRQ--FFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFN 492
Cdd:cd14932  316 KAQTQEQAEFAVEALAKASYERMFRWLVMRINKALD-KTKRQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 493 HHMFVLEQEEYKKEGIVWEFIDFGLDLQACIELIEKPM---GILSILEEECMFPKASDTSFKNKLYdNHLGKNPMFGKPK 569
Cdd:cd14932  395 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKPK 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 570 PPKagcAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTP-PRILTPGGKKKKGKSAA----- 643
Cdd:cd14932  474 KLK---DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDvDRIVGLDKVAGMGESLHgafkt 550
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 644 ----FQTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFK 719
Cdd:cd14932  551 rkgmFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 630
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....*.
gi 254839636 720 QRYSILAPNAVPSGFADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14932  631 QRYEILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
97-765 0e+00

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


Pssm-ID: 276885 [Multi-domain]  Cd Length: 673  Bit Score: 733.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITG 176
Cdd:cd14921    1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 177 ESGAGKTENTKKVIQYFALVAASLAGkkdkkeeeKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHF 256
Cdd:cd14921   81 ESGAGKTENTKKVIQYLAVVASSHKG--------KKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 257 GTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKILaVPDPGLYGFINQGTLTVDGIDDEEEMGLT 336
Cdd:cd14921  153 DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLL-LEGFNNYTFLSNGFVPIPAAQDDEMFQET 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 337 DTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQR--GEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVT 414
Cdd:cd14921  232 LEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKErnTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQ 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 415 QGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDtKAKRQ--FFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFN 492
Cdd:cd14921  312 KAQTKEQADFAIEALAKATYERLFRWILTRVNKALD-KTHRQgaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFN 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 493 HHMFVLEQEEYKKEGIVWEFIDFGLDLQACIELIEKPM---GILSILEEECMFPKASDTSFKNKLYDNHlGKNPMFGKPK 569
Cdd:cd14921  391 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKPK 469
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 570 PPKagcAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTP-PRILTPGGKKKKGKSA------ 642
Cdd:cd14921  470 QLK---DKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDvDRIVGLDQMAKMTESSlpsask 546
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 643 ----AFQTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEF 718
Cdd:cd14921  547 tkkgMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEF 626
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....*..
gi 254839636 719 KQRYSILAPNAVPSGFADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14921  627 RQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
MYSc_Myh19 cd15896
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...
97-765 0e+00

class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276899 [Multi-domain]  Cd Length: 675  Bit Score: 714.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITG 176
Cdd:cd15896    1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 177 ESGAGKTENTKKVIQYFALVAASlagkKDKKEEEKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHF 256
Cdd:cd15896   81 ESGAGKTENTKKVIQYLAHVASS----HKTKKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 257 GTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAfPENIEKILAVPDPGLYGFINQGTLTVDGIDDEEEMGLT 336
Cdd:cd15896  157 DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGA-GDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTET 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 337 DTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQR--GEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVT 414
Cdd:cd15896  236 MEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKErhTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQ 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 415 QGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDtKAKRQ--FFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFN 492
Cdd:cd15896  316 KAQTQEQAEFAVEALAKATYERMFRWLVMRINKALD-KTKRQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 493 HHMFVLEQEEYKKEGIVWEFIDFGLDLQACIELIEKPM---GILSILEEECMFPKASDTSFKNKLYDNHlGKNPMFGKPK 569
Cdd:cd15896  395 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKPK 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 570 PPKagcAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTP-PRI--------LTPGGKKKKGK 640
Cdd:cd15896  474 KLK---DEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDvDRIvgldkvsgMSEMPGAFKTR 550
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 641 SAAFQTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQ 720
Cdd:cd15896  551 KGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 630
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....*
gi 254839636 721 RYSILAPNAVPSGFADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd15896  631 RYEILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
MYSc_Myh9 cd14919
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...
97-765 0e+00

class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276883 [Multi-domain]  Cd Length: 670  Bit Score: 713.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITG 176
Cdd:cd14919    1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 177 ESGAGKTENTKKVIQYFALVAASlagkkdkkeeeKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHF 256
Cdd:cd14919   81 ESGAGKTENTKKVIQYLAHVASS-----------HKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 257 GTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAfPENIEKILAVPDPGLYGFINQGTLTVDGIDDEEEMGLT 336
Cdd:cd14919  150 DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGA-GEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQET 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 337 DTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQR--GEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVT 414
Cdd:cd14919  229 MEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKErnTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQ 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 415 QGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDtKAKRQ--FFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFN 492
Cdd:cd14919  309 KAQTKEQADFAIEALAKATYERMFRWLVLRINKALD-KTKRQgaSFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFN 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 493 HHMFVLEQEEYKKEGIVWEFIDFGLDLQACIELIEKPM---GILSILEEECMFPKASDTSFKNKLYDNHlGKNPMFGKPK 569
Cdd:cd14919  388 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPK 466
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 570 PPKagcAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTP-PRIL----------TPGGKKKK 638
Cdd:cd14919  467 QLK---DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvDRIIgldqvagmseTALPGAFK 543
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 639 GKSAAFQTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEF 718
Cdd:cd14919  544 TRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEF 623
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....*..
gi 254839636 719 KQRYSILAPNAVPSGFADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14919  624 RQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
98-765 0e+00

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


Pssm-ID: 276831 [Multi-domain]  Cd Length: 629  Bit Score: 703.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  98 SILHNLRSRYESG-FIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITG 176
Cdd:cd01380    2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 177 ESGAGKTENTKKVIQYFALVAASLAGKKdkkeeekkkdekkgTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHF 256
Cdd:cd01380   82 ESGAGKTVSAKYAMRYFATVGGSSSGET--------------QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILF 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 257 GTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSpAFPENIEKILAVPDPGLYGFINQG-TLTVDGIDDEEEMGL 335
Cdd:cd01380  148 DKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCA-AASLPELKELHLGSAEDFFYTNQGgSPVIDGVDDAAEFEE 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 336 TDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQ-RGEQAEADGTAEAEKVAF-LLGVNAGDLLKCLLKPKIKVGTEYV 413
Cdd:cd01380  227 TRKALTLLGISEEEQMEIFRILAAILHLGNVEIKAtRNDSASISPDDEHLQIACeLLGIDESQLAKWLCKRKIVTRSEVI 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 414 TQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDT--KAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFF 491
Cdd:cd01380  307 VKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASpvKEKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQF 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 492 NHHMFVLEQEEYKKEGIVWEFIDFgLDLQACIELIEKPMGILSILEEECMFPKASDTSFKNKLYDNHLGK-NPMFGKPKP 570
Cdd:cd01380  387 NQHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRF 465
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 571 PKAGcaeahFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKepivkmlFTPPriltpggkkkkgksaafqTISSV 650
Cdd:cd01380  466 SNTA-----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASK-------NRKK------------------TVGSQ 515
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 651 HKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNAV 730
Cdd:cd01380  516 FRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKE 595
                        650       660       670
                 ....*....|....*....|....*....|....*
gi 254839636 731 PSGfADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd01380  596 WLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
MYSc_Myh14_mammals cd14930
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...
97-765 0e+00

class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.


Pssm-ID: 276893 [Multi-domain]  Cd Length: 670  Bit Score: 691.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITG 176
Cdd:cd14930    1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 177 ESGAGKTENTKKVIQYFALVAASLAGKKDKKEEekkkdekkGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHF 256
Cdd:cd14930   81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP--------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 257 GTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAfPENIEKILAVPDPGLYGFINQGTLTVDGiDDEEEMGLT 336
Cdd:cd14930  153 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGA-GEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQET 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 337 DTAFDVLGFTDEEKLSMYKCTGCILHLGE--MKWKQRGEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVT 414
Cdd:cd14930  231 LESLRVLGFSHEEITSMLRMVSAVLQFGNivLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 415 QGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDtKAKRQ--FFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFN 492
Cdd:cd14930  311 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 493 HHMFVLEQEEYKKEGIVWEFIDFGLDLQACIELIEKPM---GILSILEEECMFPKASDTSFKNKLYDNHlGKNPMFGKPK 569
Cdd:cd14930  390 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPR 468
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 570 PPKAgcaEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRILTPGGKKKKG---------K 640
Cdd:cd14930  469 HLRD---QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLgdgppggrpR 545
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 641 SAAFQTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQ 720
Cdd:cd14930  546 RGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQ 625
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....*
gi 254839636 721 RYSILAPNAVPSGFADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14930  626 RYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
98-765 0e+00

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


Pssm-ID: 276849 [Multi-domain]  Cd Length: 661  Bit Score: 666.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  98 SILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITGE 177
Cdd:cd14883    2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 178 SGAGKTENTKKVIQYFALVAAslagkkdkkeeekkkdeKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHFG 257
Cdd:cd14883   82 SGAGKTETTKLILQYLCAVTN-----------------NHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFD 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 258 TQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPA-FPENIEKILAVPDPGLYGFINQ-GTLTVDGIDDEEEMGL 335
Cdd:cd14883  145 ASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAkHSKELKEKLKLGEPEDYHYLNQsGCIRIDNINDKKDFDH 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 336 TDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQ-RGEQAE--ADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEY 412
Cdd:cd14883  225 LRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGAltVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNV 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 413 VTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFN 492
Cdd:cd14883  305 TEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFN 384
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 493 HHMFVLEQEEYKKEGIVWEFIDFGlDLQACIELIEK-PMGILSILEEECMFPKASDTSFKNKLYDNHlGKNPMFGKPKPP 571
Cdd:cd14883  385 HYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPDRR 462
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 572 KagcAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRILTPGGKKKKGKSAAFQ------ 645
Cdd:cd14883  463 R---WKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDLLALTGLSISLGGDTTSrgtskg 539
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 646 --TISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYS 723
Cdd:cd14883  540 kpTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYL 619
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|..
gi 254839636 724 ILAPNAVPSGFADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14883  620 CLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
97-765 0e+00

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


Pssm-ID: 276832  Cd Length: 648  Bit Score: 656.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITG 176
Cdd:cd01381    1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 177 ESGAGKTENTKKVIQYFALVAAslagkkdkkeeekkkdeKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHF 256
Cdd:cd01381   81 ESGAGKTESTKLILQYLAAISG-----------------QHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHF 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 257 GTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENiEKILAVPDPGLYGFINQG-TLTVDGIDDEEEMGL 335
Cdd:cd01381  144 NKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEE-KKKLELGDASDYYYLTQGnCLTCEGRDDAAEFAD 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 336 TDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQRG----EQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTE 411
Cdd:cd01381  223 IRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEATVvdnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGE 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 412 YVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQT----LDTKAKRQfFIGVLDIAGFEIFDFNSFEQLCINYTNERL 487
Cdd:cd01381  303 TVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAiykpRGTDSSRT-SIGVLDIFGFENFEVNSFEQLCINFANENL 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 488 QQFFNHHMFVLEQEEYKKEGIVWEFIDFgLDLQACIELI-EKPMGILSILEEECMFPKASDTSFKNKLYDNHlGKNPMFG 566
Cdd:cd01381  382 QQFFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYL 459
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 567 KPKPPkagcAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRiltpggKKKKGKSAAFQT 646
Cdd:cd01381  460 KPKSD----LNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDI------SMGSETRKKSPT 529
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 647 ISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILA 726
Cdd:cd01381  530 LSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLV 609
                        650       660       670
                 ....*....|....*....|....*....|....*....
gi 254839636 727 PNAVPSGFADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd01381  610 PGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
97-765 0e+00

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


Pssm-ID: 276835  Cd Length: 647  Bit Score: 655.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLP-IYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLIT 175
Cdd:cd01384    1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 176 GESGAGKTENTKKVIQYFALVAASLAGKKDkkeeekkkdekkgTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIH 255
Cdd:cd01384   81 GESGAGKTETTKMLMQYLAYMGGRAVTEGR-------------SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQ 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 256 FGTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKiLAVPDPGLYGFINQ-GTLTVDGIDDEEEMG 334
Cdd:cd01384  148 FDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREK-YKLKDPKQFHYLNQsKCFELDGVDDAEEYR 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 335 LTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKqRGEQAEADGTA------EAEKVAFLLGVNAGDLLKCLLKPKIKV 408
Cdd:cd01384  227 ATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFS-KGEEDDSSVPKdeksefHLKAAAELLMCDEKALEDALCKRVIVT 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 409 GTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQ 488
Cdd:cd01384  306 PDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQ 385
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 489 QFFNHHMFVLEQEEYKKEGIVWEFIDFgLDLQACIELIE-KPMGILSILEEECMFPKASDTSFKNKLYDNhLGKNPMFGK 567
Cdd:cd01384  386 QHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSK 463
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 568 PKPPKAGcaeahFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFtpprilTPGGKKKKGKSAAFQTI 647
Cdd:cd01384  464 PKLSRTD-----FTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLF------PPLPREGTSSSSKFSSI 532
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 648 SSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAP 727
Cdd:cd01384  533 GSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAP 612
                        650       660       670
                 ....*....|....*....|....*....|....*...
gi 254839636 728 NaVPSGFADGKVVTDKALSALQLdpNEYRLGNTKVFFK 765
Cdd:cd01384  613 E-VLKGSDDEKAACKKILEKAGL--KGYQIGKTKVFLR 647
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
98-765 0e+00

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


Pssm-ID: 276829  Cd Length: 652  Bit Score: 648.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  98 SILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITGE 177
Cdd:cd01378    2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 178 SGAGKTENTKKVIQYFALVAASlagkkdkkeeekkKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHFG 257
Cdd:cd01378   82 SGAGKTEASKRIMQYIAAVSGG-------------SESEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFD 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 258 TQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKILAVPDPGLYGFINQGTLTVDGIDDEEEMGLTD 337
Cdd:cd01378  149 FKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVL 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 338 TAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQRGEQ-AEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVTQ- 415
Cdd:cd01378  229 NAMKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGnAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGRSVy 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 416 --GRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQ-FFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFN 492
Cdd:cd01378  309 evPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFI 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 493 HhmFVL--EQEEYKKEGIVWEFIDFgLDLQACIELIE-KPMGILSILEEECMFP-KASDTSFKNKLyDNHLGKNPMFGKP 568
Cdd:cd01378  389 E--LTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECP 464
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 569 KPPKAGcAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRILT----PggkkkkgKSAAF 644
Cdd:cd01378  465 SGHFEL-RRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDskkrP-------PTAGT 536
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 645 QTissvhKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSI 724
Cdd:cd01378  537 KF-----KNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKL 611
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|.
gi 254839636 725 LAPNAVPSGFADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd01378  612 LSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
98-765 0e+00

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


Pssm-ID: 276834  Cd Length: 647  Bit Score: 640.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  98 SILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRgkRRAEMPPHLFSIADNAYQYMLQDRENQSMLITGE 177
Cdd:cd01383    2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 178 SGAGKTENTKKVIQYFALVAASLAGkkdkkeeekkkdekkgtLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHFG 257
Cdd:cd01383   80 SGAGKTETAKIAMQYLAALGGGSSG-----------------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFD 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 258 TQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKiLAVPDPGLYGFINQ-GTLTVDGIDDEEEMGLT 336
Cdd:cd01383  143 AAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREK-LNLKSASEYKYLNQsNCLTIDGVDDAKKFHEL 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 337 DTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQRGEQ--AEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVT 414
Cdd:cd01383  222 KEALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNEnhVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIV 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 415 QGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDT-KAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNH 493
Cdd:cd01383  302 KKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNR 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 494 HMFVLEQEEYKKEGIVWEFIDFgLDLQACIELIE-KPMGILSILEEECMFPKASDTSFKNKLyDNHLGKNPMFGKPKppk 572
Cdd:cd01383  382 HLFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCFKGER--- 456
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 573 agcaEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVK----MLFTPPRILTPGGKKKKGKSAAfQTIS 648
Cdd:cd01383  457 ----GGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQlfasKMLDASRKALPLTKASGSDSQK-QSVA 531
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 649 SVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPN 728
Cdd:cd01383  532 TKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPE 611
                        650       660       670
                 ....*....|....*....|....*....|....*..
gi 254839636 729 AVpSGFADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd01383  612 DV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
97-765 0e+00

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


Pssm-ID: 276839  Cd Length: 644  Bit Score: 575.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITG 176
Cdd:cd14872    1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 177 ESGAGKTENTKKVIQYFALVAASLAGkkdkkeeekkkdekkgtLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHF 256
Cdd:cd14872   81 ESGAGKTEATKQCLSFFAEVAGSTNG-----------------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHF 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 257 GTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKilaVPDPGLYGFINQ-GTLTVDGIDDEEEMGL 335
Cdd:cd14872  144 DNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGG---WGSSAAYGYLSLsGCIEVEGVDDVADFEE 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 336 TDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQRGEQAEADGTA-----EAEKVAFLLGVNAGDLLKCLLKPKIKV-G 409
Cdd:cd14872  221 VVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTvanrdVLKEVATLLGVDAATLEEALTSRLMEIkG 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 410 TEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLD-TKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQ 488
Cdd:cd14872  301 CDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQ 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 489 QFFNHHMFVLEQEEYKKEGIVWEFIDFgLDLQACIELIEK-PMGILSILEEECMFPKASDTSFKNKLyDNHLGKNPMFgk 567
Cdd:cd14872  381 QHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAA-NQTHAAKSTF-- 456
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 568 pKPPKAGCAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPpriltpggkKKKGKSAAFQTI 647
Cdd:cd14872  457 -VYAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPP---------SEGDQKTSKVTL 526
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 648 SSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAP 727
Cdd:cd14872  527 GGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVK 606
                        650       660       670
                 ....*....|....*....|....*....|....*...
gi 254839636 728 NAVPSGFADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14872  607 TIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
97-765 0e+00

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


Pssm-ID: 276833  Cd Length: 649  Bit Score: 566.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLP-IYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLIT 175
Cdd:cd01382    1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 176 GESGAGKTENTKKVIQYFALVAASLAGkkdkkeeekkkdekkgTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIH 255
Cdd:cd01382   81 GESGAGKTESTKYILRYLTESWGSGAG----------------PIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIH 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 256 FGTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAfPENIEKILavpdpglygfinqgtLTVDGIDDEEEMGL 335
Cdd:cd01382  145 FNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGA-PEDLREKL---------------LKDPLLDDVGDFIR 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 336 TDTAFDVLGFTDEEKLSMYKCTGCILHLG-----EMKWKQRGEQAEADGTAEA-EKVAFLLGVNAGDLLKCLL------- 402
Cdd:cd01382  209 MDKAMKKIGLSDEEKLDIFRVVAAVLHLGniefeENGSDSGGGCNVKPKSEQSlEYAAELLGLDQDELRVSLTtrvmqtt 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 403 KPKIKvGTEYVTQGRnKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKaKRQFFIGVLDIAGFEIFDFNSFEQLCINY 482
Cdd:cd01382  289 RGGAK-GTVIKVPLK-VEEANNARDALAKAIYSKLFDHIVNRINQCIPFE-TSSYFIGVLDIAGFEYFEVNSFEQFCINY 365
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 483 TNERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFgLDLQACIELIE-KPMGILSILEEECMFPKASDTSFKNKLYDNHLgK 561
Cdd:cd01382  366 CNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK-N 443
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 562 NPMFGKPKPPKagcAEAH--------FCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTppriLTPG 633
Cdd:cd01382  444 HFRLSIPRKSK---LKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFE----SSTN 516
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 634 GKKKKGKSA---AFQTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFP 710
Cdd:cd01382  517 NNKDSKQKAgklSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFP 596
                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 711 NRIIYSEFKQRY-SILAPNAV---PSGFAdgkvvtdKAL-SALQLDPNEYRLGNTKVFFK 765
Cdd:cd01382  597 SRTSFHDLYNMYkKYLPPKLArldPRLFC-------KALfKALGLNENDFKFGLTKVFFR 649
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
97-765 0e+00

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: 550.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLP-IYTQGLVDKYRG--KRRAEMPPHLFSIADNAYQYMLQDR----EN 169
Cdd:cd14892    1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPlLYDVPGFDSQRKeeATASSPPPHVFSIAERAYRAMKGVGkgqgTP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 170 QSMLITGESGAGKTENTKKVIQYFALVAASLAGKKDKKEEEKKKDEkkgtLEDQIVQCNPVLEAYGNAKTTRNNNSSRFG 249
Cdd:cd14892   81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAHES----IEECVLLSNLILEAFGNAKTIRNDNSSRFG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 250 KFIRIHFGTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSpAFPENIEKILAVPDPGLYGFINQGT-LTVDGID 328
Cdd:cd14892  157 KYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLA-GLDANENAALELTPAESFLFLNQGNcVEVDGVD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 329 DEEEMGLTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKW----KQRGEQAEADGTAEAEKVAFLLGVNAGDLLKcllkp 404
Cdd:cd14892  236 DATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFeenaDDEDVFAQSADGVNVAKAAGLLGVDAAELMF----- 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 405 kiKVGTEYVTQGRNK--------DQVTNSIAALAKSLYDRMFNWLVRRVN-----QTL-----DTKAKRQFFIGVLDIAG 466
Cdd:cd14892  311 --KLVTQTTSTARGSvleikltaREAKNALDALCKYLYGELFDWLISRINachkqQTSgvtggAASPTFSPFIGILDIFG 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 467 FEIFDFNSFEQLCINYTNERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGlDLQACIELIEK-PMGILSILEEECMFP-K 544
Cdd:cd14892  389 FEIMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKkPLGLLPLLEEQMLLKrK 467
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 545 ASDTSFKNKLYDNHLGKNPMFgkpKPPKAGCaeAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEpivkmlf 624
Cdd:cd14892  468 TTDKQLLTIYHQTHLDKHPHY---AKPRFEC--DEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------- 535
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 625 tppriltpggkkkkgksaaFQTissvhkeSLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRI 704
Cdd:cd14892  536 -------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRI 589
                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254839636 705 CRKGFPNRIIYSEFKQRYSILAPN---AVPSGFADGKVVTDKA---LSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14892  590 RREGFPIRRQFEEFYEKFWPLARNkagVAASPDACDATTARKKceeIVARALERENFQLGRTKVFLR 656
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
97-765 0e+00

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


Pssm-ID: 276868 [Multi-domain]  Cd Length: 658  Bit Score: 548.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLP-IYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLIT 175
Cdd:cd14903    1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 176 GESGAGKTENTKKVIQYFALVAaslagkkdkkeeekkkdekkGTLED----QIVQCNPVLEAYGNAKTTRNNNSSRFGKF 251
Cdd:cd14903   81 GESGAGKTETTKILMNHLATIA--------------------GGLNDstikKIIEVNPLLESFGNAKTVRNDNSSRFGKF 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 252 IRIHFGTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPEnieKILAVPDPGLYGFINQGTLT-VDGIDDE 330
Cdd:cd14903  141 TQLQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVE---ERLFLDSANECAYTGANKTIkIEGMSDR 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 331 EEMGLTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQRGEQAEAD----GTAEAEKVAFLLGVNAGDLLKCLLKPKI 406
Cdd:cd14903  218 KHFARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiapGDQGAVYATKLLGLSPEALEKALCSRTM 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 407 KVGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNER 486
Cdd:cd14903  298 RAAGDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEK 377
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 487 LQQFFNHHMFVLEQEEYKKEGIVWEFIDFgLDLQACIELIEKPMGILSILEEECMFPKASDTSFKNKLYDNHLGKNPMFG 566
Cdd:cd14903  378 LQQKFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIE 456
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 567 KPKppkagCAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRILTPGGKKKKGKSAAFQT 646
Cdd:cd14903  457 FPR-----TSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRR 531
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 647 ISSVH--------KESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEF 718
Cdd:cd14903  532 GGALTtttvgtqfKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEF 611
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|.
gi 254839636 719 KQRYSILapnaVPSGFADGKVVTDKA---LSALQLD-PNEYRLGNTKVFFK 765
Cdd:cd14903  612 LDKFWLF----LPEGRNTDVPVAERCealMKKLKLEsPEQYQMGLTRIYFQ 658
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
97-765 0e+00

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


Pssm-ID: 276838 [Multi-domain]  Cd Length: 657  Bit Score: 548.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITG 176
Cdd:cd01387    1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 177 ESGAGKTENTKKVIQYFALVAASlagkkdkkeeekkkdeKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHF 256
Cdd:cd01387   81 ESGSGKTEATKLIMQYLAAVNQR----------------RNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 257 gTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSpAFPENIEKILAVPDPGLYGFINQG-TLTVDGIDDEEEMGL 335
Cdd:cd01387  145 -EGGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLA-GLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRR 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 336 TDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQR-----GEQAEADGTAEAEKVAFLLGVNAGDLLKCLlkpkikvgT 410
Cdd:cd01387  223 LLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRqlrhgQEGVSVGSDAEIQWVAHLLQISPEGLQKAL--------T 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 411 EYVTQGRNK--------DQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINY 482
Cdd:cd01387  295 FKVTETRREriftpltiDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINY 374
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 483 TNERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFgLDLQACIELI-EKPMGILSILEEECMFPKASDTSFKNKLYDNHlGK 561
Cdd:cd01387  375 ANENLQYYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-AL 452
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 562 NPMFGKPKPPkagcaEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRILTPGGKKKKGKS 641
Cdd:cd01387  453 NELYSKPRMP-----LPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKAPPRLGKG 527
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 642 AAFQ------TISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIY 715
Cdd:cd01387  528 RFVTmkprtpTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPF 607
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|.
gi 254839636 716 SEFKQRYSILAPNAVPSGfADGKVVTDKALSALQLDP-NEYRLGNTKVFFK 765
Cdd:cd01387  608 QVFIDRYRCLVALKLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
97-763 0e+00

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


Pssm-ID: 276866 [Multi-domain]  Cd Length: 655  Bit Score: 542.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKY--RGKRRA----EMPPHLFSIADNAYQYMLQDRE-- 168
Cdd:cd14901    1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyeHGERRAagerKLPPHVYAVADKAFRAMLFASRgq 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 169 --NQSMLITGESGAGKTENTKKVIQYFALVAAslagkkdkKEEEKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSS 246
Cdd:cd14901   81 kcDQSILVSGESGAGKTETTKIIMNYLASVSS--------ATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 247 RFGKFIRIHFGTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIE--KILAVPDpglYGFIN--QGTL 322
Cdd:cd14901  153 RFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHalGLTHVEE---YKYLNssQCYD 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 323 TVDGIDDEEEMGLTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQRGEQAEADGT---AEAEKVAFLLGVNAGDLLK 399
Cdd:cd14901  230 RRDGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMsslANVRAACDLLGLDMDVLEK 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 400 CLLKPKIKVGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTL--DTKAKRQFFIGVLDIAGFEIFDFNSFEQ 477
Cdd:cd14901  310 TLCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIaySESTGASRFIGIVDIFGFEIFATNSLEQ 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 478 LCINYTNERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGlDLQACIELIE-KPMGILSILEEECMFPKASDTSFKNKLYD 556
Cdd:cd14901  390 LCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYD 468
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 557 NhLGKNPMFGKPKPPKagcAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKmlftppriltpggkk 636
Cdd:cd14901  469 L-LAKHASFSVSKLQQ---GKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS--------------- 529
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 637 kkgksaafQTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYS 716
Cdd:cd14901  530 --------STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHD 601
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|..
gi 254839636 717 EFKQRYSILAPN-AVPSGFADGKVVTDKALSALQLDPNE----YRLGNTKVF 763
Cdd:cd14901  602 AFVHTYSCLAPDgASDTWKVNELAERLMSQLQHSELNIEhlppFQVGKTKVF 653
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
97-765 0e+00

class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276855 [Multi-domain]  Cd Length: 662  Bit Score: 542.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLP-IYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQ----DRENQS 171
Cdd:cd14890    1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 172 MLITGESGAGKTENTKKVIQYFALVAA--SLAGKKDKKEEEKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFG 249
Cdd:cd14890   81 IIISGESGAGKTEATKIIMQYLARITSgfAQGASGEGEAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 250 KFIRIHFGTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAfPENIEKILAVPDPGLYGFINQGTLTVDGIDD 329
Cdd:cd14890  161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGA-DEALRERLKLQTPVEYFYLRGECSSIPSCDD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 330 EEEMGLTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWK--QRGEQAEADGTAEA-EKVAFLLGVNAGDLLKCLLKPKI 406
Cdd:cd14890  240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFEseNDTTVLEDATTLQSlKLAAELLGVNEDALEKALLTRQL 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 407 KVGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNER 486
Cdd:cd14890  320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEK 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 487 LQQFFNHHMFVLEQEEYKKEGIVWEFIDFGlDLQACIELIE-KPMGILSILE--EECMFPKAS--DTSFKNKLYDNHLGK 561
Cdd:cd14890  400 LQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFItlDDCWRFKGEeaNKKFVSQLHASFGRK 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 562 NPMFGKPKP---------PKAGcAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMlftppriltp 632
Cdd:cd14890  479 SGSGGTRRGssqhphfvhPKFD-ADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSIREV---------- 547
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 633 ggkkkkgksaafqTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNR 712
Cdd:cd14890  548 -------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALR 614
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|...
gi 254839636 713 IIYSEFKQRYSILAPNAvpsgfADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14890  615 EEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
97-765 3.33e-180

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


Pssm-ID: 276853 [Multi-domain]  Cd Length: 667  Bit Score: 533.50  E-value: 3.33e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLP-IYTQGLVDKYRGKRRaEMPPHLFSIADNAYQYMLQDRENQSMLIT 175
Cdd:cd14888    1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFIQPSI-SKSPHVFSTASSAYQGMCNNKKSQTILIS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 176 GESGAGKTENTKKVIQYFALVAASlagkkdkkeeekkKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIH 255
Cdd:cd14888   80 GESGAGKTESTKYVMKFLACAGSE-------------DIKKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQ 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 256 F---------GTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPA-----------------FPENIEKILAVP 309
Cdd:cd14888  147 FsklkskrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAreakntglsyeendeklAKGADAKPISID 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 310 DPGLYGFINQGTLTV------DGIDDEEEMGLTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKW-----KQRGEQAEAD 378
Cdd:cd14888  227 MSSFEPHLKFRYLTKsschelPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFenneaCSEGAVVSAS 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 379 GTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLD-TKAKRQF 457
Cdd:cd14888  307 CTDDLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLL 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 458 FIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGlDLQACIELI-EKPMGILSIL 536
Cdd:cd14888  387 FCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCML 465
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 537 EEECMFPKASDTSFKNKLYDNHLGkNPMFGKPKpPKAGCaeahFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSK 616
Cdd:cd14888  466 DEECFVPGGKDQGLCNKLCQKHKG-HKRFDVVK-TDPNS----FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSK 539
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 617 EPIVKMLFTPpriLTPGGKKKKGKSAAFQTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCN 696
Cdd:cd14888  540 NPFISNLFSA---YLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYG 616
                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254839636 697 GVLEGIRICRKGFPNRIIYSEFKQRYSILAPnavpsgfadgkvvtdkalSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14888  617 GVLQAVQVSRAGYPVRLSHAEFYNDYRILLN------------------GEGKKQLSIWAVGKTLCFFK 667
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
97-765 3.85e-180

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: 532.83  E-value: 3.85e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLP-IYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLIT 175
Cdd:cd14873    1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 176 GESGAGKTENTKKVIQYFALVAASLAGKKDKKEEEkkkdekkgTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIH 255
Cdd:cd14873   81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTS--------CVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 256 FGTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEkILAVPDPGLYGFINQ-GTLTVDGIDDEEEMG 334
Cdd:cd14873  153 ICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEERE-EFYLSTPENYHYLNQsGCVEDKTISDQESFR 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 335 LTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQRGEQAEADGTAeAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVT 414
Cdd:cd14873  232 EVITAMEVMQFSKEEVREVSRLLAGILHLGNIEFITAGGAQVSFKTA-LGRSAELLGLDPTQLTDALTQRSMFLRGEEIL 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 415 QGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLdtKAKRQF-FIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNH 493
Cdd:cd14873  311 TPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFkSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNK 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 494 HMFVLEQEEYKKEGIVWEFIDFgLDLQACIELIEKPMGILSILEEECMFPKASDTSFKNKLYDNHlGKNPMFGKPKppka 573
Cdd:cd14873  389 HIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-ANNHFYVKPR---- 462
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 574 gCAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRILTPGGKKKKGKSAAFQTISSVHKE 653
Cdd:cd14873  463 -VAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRPTVSSQFKD 541
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 654 SLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNAvpsg 733
Cdd:cd14873  542 SLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNL---- 617
                        650       660       670
                 ....*....|....*....|....*....|....*
gi 254839636 734 fADGKVVTDKALSALQL-DPN--EYRLGNTKVFFK 765
Cdd:cd14873  618 -ALPEDVRGKCTSLLQLyDASnsEWQLGKTKVFLR 651
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
97-765 6.26e-179

class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276836 [Multi-domain]  Cd Length: 690  Bit Score: 531.18  E-value: 6.26e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITG 176
Cdd:cd01385    1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 177 ESGAGKTENTKKVIQYfaLVAASLAGKKDkkeeekkkdekkgTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHF 256
Cdd:cd01385   81 ESGSGKTESTNFLLHH--LTALSQKGYGS-------------GVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNY 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 257 GTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAfPENIEKILAVPDPGLYGFINQGT-LTVDGIDDEEEMGL 335
Cdd:cd01385  146 RENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGA-SEEERKELHLKQPEDYHYLNQSDcYTLEGEDEKYEFER 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 336 TDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQRGEQAEADGTAEAEKV----AFLLGVNAGDLLKCLLKPKIKVGTE 411
Cdd:cd01385  225 LKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAYHRDESVTVGNPEVldiiSELLRVKEETLLEALTTKKTVTVGE 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 412 YVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTL----DTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERL 487
Cdd:cd01385  305 TLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHL 384
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 488 QQFFNHHMFVLEQEEYKKEGIVWEFIDFgLDLQACIELIE-KPMGILSILEEECMFPKASDTSFKNKlYDNHLGKNPMFg 566
Cdd:cd01385  385 QYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYY- 461
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 567 kPKPPKagcAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLF---------------------- 624
Cdd:cd01385  462 -EKPQV---MEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIgidpvavfrwavlrafframaa 537
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 625 -----------------TPPRILTPGGKKKKGKSAAfQTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAA 687
Cdd:cd01385  538 freagrrraqrtaghslTLHDRTTKSLLHLHKKKKP-PSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDE 616
                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254839636 688 LVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNAVPSGFADGKVVtdkaLSALQLDPNEYRLGNTKVFFK 765
Cdd:cd01385  617 LVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDF----LEKLNLDRDNYQIGKTKVFLK 690
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
98-765 1.90e-176

class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276830 [Multi-domain]  Cd Length: 633  Bit Score: 522.61  E-value: 1.90e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  98 SILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITGE 177
Cdd:cd01379    2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 178 SGAGKTENTKKVIQYfaLVAASLAGKkdkkeeekkkdekkGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHFG 257
Cdd:cd01379   82 SGAGKTESANLLVQQ--LTVLGKANN--------------RTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFT 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 258 TQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKILAVPDPGLYGFINQGTLTV-DGIDDE---EEM 333
Cdd:cd01379  146 STGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAKYKLPENKPPRYLQNDGLTVqDIVNNSgnrEKF 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 334 GLTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWK------QRGEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIK 407
Cdd:cd01379  226 EEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTevesnhQTDKSSRISNPEALNNVAKLLGIEADELQEALTSHSVV 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 408 VGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTL--DTKAK-RQFFIGVLDIAGFEIFDFNSFEQLCINYTN 484
Cdd:cd01379  306 TRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASdEPLSIGILDIFGFENFQKNSFEQLCINIAN 385
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 485 ERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFG-----LDLqacieLIEKPMGILSILEEECMFPKASDTSFKNKLYDNHl 559
Cdd:cd01379  386 EQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI- 459
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 560 gKNPMFGKPKPpkagcAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKmlftppriltpggkkkkg 639
Cdd:cd01379  460 -KSKYYWRPKS-----NALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR------------------ 515
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 640 ksaafQTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFK 719
Cdd:cd01379  516 -----QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFL 590
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|.
gi 254839636 720 QRYSILAPNavpsgfADGKVVTDKA-----LSALQLDpnEYRLGNTKVFFK 765
Cdd:cd01379  591 KRYYFLAFK------WNEEVVANREncrliLERLKLD--NWALGKTKVFLK 633
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
97-765 1.20e-167

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: 499.99  E-value: 1.20e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKR-RAEMPPHLFSIADNAYQYMLQDRENQSMLIT 175
Cdd:cd14897    1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 176 GESGAGKTENTKKVIQYFALVAASlagkkdkkeeekkkdeKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIH 255
Cdd:cd14897   81 GESGAGKTESTKYMIKHLMKLSPS----------------DDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELH 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 256 FGTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIeKILAVPDPGLYGFINQGTLTVDGIDDEEEMGL 335
Cdd:cd14897  145 FTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRL-LYYFLEDPDCHRILRDDNRNRPVFNDSEELEY 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 336 TDTAFDVL-------GFTDEEKLSMYKCTGCILHLGEMKWKqrgEQAEADG-----TAEAEKVAFLLGVNAGDLLKCLLK 403
Cdd:cd14897  224 YRQMFHDLtnimkliGFSEEDISVIFTILAAILHLTNIVFI---PDEDTDGvtvadEYPLHAVAKLLGIDEVELTEALIS 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 404 PKIKVGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFF-----IGVLDIAGFEIFDFNSFEQL 478
Cdd:cd14897  301 NVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQL 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 479 CINYTNERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGlDLQACIELI-EKPMGILSILEEECMFPKASDTSFKNKLyDN 557
Cdd:cd14897  381 CINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NK 458
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 558 HLGKNPMFgkpKPPKAGCAEahFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTppriltpggkkk 637
Cdd:cd14897  459 YCGESPRY---VASPGNRVA--FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT------------ 521
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 638 kgksaafqtisSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSE 717
Cdd:cd14897  522 -----------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYED 590
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....*....
gi 254839636 718 FKQRYSILAPNAVPSGFADgkvvTDKALSALQ-LDPNEYRLGNTKVFFK 765
Cdd:cd14897  591 FVKRYKEICDFSNKVRSDD----LGKCQKILKtAGIKGYQFGKTKVFLK 635
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
97-765 1.23e-165

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


Pssm-ID: 276872 [Multi-domain]  Cd Length: 669  Bit Score: 496.09  E-value: 1.23e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLP-IYTQGLVDKYRGK--------RRAEMPPHLFSIADNAYQYMLQDR 167
Cdd:cd14907    1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 168 ENQSMLITGESGAGKTENTK---KVIQYFALVAASLAGKKDKKEEEKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNN 244
Cdd:cd14907   81 KKQAIVISGESGAGKTENAKyamKFLTQLSQQEQNSEEVLTLTSSIRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 245 SSRFGKFIRIHFG-TQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKILAVPDPG--LYGFINQGT 321
Cdd:cd14907  161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSgdRYDYLKKSN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 322 -LTVDGIDDEEEMGLTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQR----GEQAEADGTAEAEKVAFLLGVNAGD 396
Cdd:cd14907  241 cYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDStlddNSPCCVKNKETLQIIAKLLGIDEEE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 397 LLKCLLKPKIKVGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTL--------DTKAKRQFFIGVLDIAGFE 468
Cdd:cd14907  321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFE 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 469 IFDFNSFEQLCINYTNERLQQFFNHHMFVLEQEEYKKEGIVWEF--IDFgLDLQACIELIEK-PMGILSILEEECMFPKA 545
Cdd:cd14907  401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATG 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 546 SDTSFKNKLYDNHlGKNPMFGKPKPPKAgcaeAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFT 625
Cdd:cd14907  480 TDEKLLNKIKKQH-KNNSKLIFPNKINK----DTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFS 554
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 626 PP-RILTPGGKKKKGKSAAFQTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRI 704
Cdd:cd14907  555 GEdGSQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRV 634
                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254839636 705 CRKGFPNRIIYSEFKQRYSILapnavpsgfadgkvvtdkalsalqldpNEYRL-GNTKVFFK 765
Cdd:cd14907  635 RKQGYPYRKSYEDFYKQYSLL---------------------------KKNVLfGKTKIFMK 669
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
97-765 6.87e-164

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


Pssm-ID: 276856  Cd Length: 645  Bit Score: 490.71  E-value: 6.87e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNL--RSRYESGFIYTYSGLFCIAINPYRRLPiytQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRE---NQS 171
Cdd:cd14891    1 AGILHNLeeRSKLDNQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 172 MLITGESGAGKTENTKKVIQYFAL--VAASLAGKKDKKEEEKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFG 249
Cdd:cd14891   78 IVISGESGAGKTETSKIILRFLTTraVGGKKASGQDIEQSSKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 250 KFIRIHFGTQG-KIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENI-EKILAVPDPGLYgfINQ-GTLTVDG 326
Cdd:cd14891  158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLkELLLLSPEDFIY--LNQsGCVSDDN 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 327 IDDEEEMGLTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQR-GEQAEADGTAEAEKVAF-----LLGVNAGDLLKC 400
Cdd:cd14891  236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEdTSEGEAEIASESDKEALataaeLLGVDEEALEKV 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 401 LLKPKIKVGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFD-FNSFEQLC 479
Cdd:cd14891  316 ITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLL 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 480 INYTNERLQQFFNHHMFVLEQEEYKKEGI-----VWEfidfglDLQACIELI-EKPMGILSILEEECMFPKASDTSFKNK 553
Cdd:cd14891  396 INYANEALQATFNQQVFIAEQELYKSEGIdvgviTWP------DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNET 469
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 554 LYDNHlGKNPMFGKPKPPKagcAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKepivkmlftppriltpg 633
Cdd:cd14891  470 LHKTH-KRHPCFPRPHPKD---MREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASSA----------------- 528
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 634 gkkkkgksaAFQtissvhkESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRI 713
Cdd:cd14891  529 ---------KFS-------DQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRV 592
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|...
gi 254839636 714 IYSEFKQRYSILAPNAVPSGFAD-GKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14891  593 TYAELVDVYKPVLPPSVTRLFAEnDRTLTQAILWAFRVPSDAYRLGRTRVFFR 645
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
99-765 9.09e-164

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: 490.96  E-value: 9.09e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  99 ILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYML----QDRENQSMLI 174
Cdd:cd14889    3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 175 TGESGAGKTENTKKVI-QYFALVAASlagkkdkkeeekkkdekkGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIR 253
Cdd:cd14889   83 SGESGAGKTESTKLLLrQIMELCRGN------------------SQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQ 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 254 IHFgTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENiEKILAVPDPGLYGFINqgtltvDGIDDEEEM 333
Cdd:cd14889  145 LRF-RNGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAED-RENYGLLDPGKYRYLN------NGAGCKREV 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 334 GLTDT-------AFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQRGEQA---EADGTAEAEKVAFLLGVNAGDLLKCLLK 403
Cdd:cd14889  217 QYWKKkydevcnAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlkvENDSNGWLKAAAGQFGVSEEDLLKTLTC 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 404 PKIKVGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQF---FIGVLDIAGFEIFDFNSFEQLCI 480
Cdd:cd14889  297 TVTFTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSVelrEIGILDIFGFENFAVNRFEQACI 376
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 481 NYTNERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFgLDLQACIEL-IEKPMGILSILEEECMFPKASDTSFKNKLyDNHL 559
Cdd:cd14889  377 NLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHF 454
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 560 GKNPMFGKP--KPPKagcaeahFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPR----ILTPG 633
Cdd:cd14889  455 KGNSYYGKSrsKSPK-------FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRsrtgTLMPR 527
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 634 GKKKKGKSAAF-----QTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKG 708
Cdd:cd14889  528 AKLPQAGSDNFnstrkQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREG 607
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 254839636 709 FPNRIIYSEFKQRYSILAPNAVPSGfadgkvVTDKALSALQ-LDPNEYRLGNTKVFFK 765
Cdd:cd14889  608 FSWRPSFAEFAERYKILLCEPALPG------TKQSCLRILKaTKLVGWKCGKTRLFFK 659
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
98-726 1.17e-158

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


Pssm-ID: 276865  Cd Length: 627  Bit Score: 476.72  E-value: 1.17e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  98 SILHNLRSRYESGFIYTYSGLFCIAINPYRRLP-IYTQGLVDKY-----------RGKRRAEMPPHLFSIADNAYQYM-- 163
Cdd:cd14900    2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 164 --LQDRENQSMLITGESGAGKTENTKKVIQYFALVAASLAGKKDKKEEEKKkdekkgTLEDQIVQCNPVLEAYGNAKTTR 241
Cdd:cd14900   82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSMGKSTS------GIAAKVLQTNILLESFGNARTLR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 242 NNNSSRFGKFIRIHFGTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPE-----NIEKILAvpdpglygf 316
Cdd:cd14900  156 NDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAarkrdMYRRVMD--------- 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 317 inqgtltvdgiddeeemgltdtAFDVLGFTDEEKLSMYKCTGCILHLGEMKWkQRGEQAEADGT----------AEAEKV 386
Cdd:cd14900  227 ----------------------AMDIIGFTPHERAGIFDLLAALLHIGNLTF-EHDENSDRLGQlksdlapssiWSRDAA 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 387 AFLLGVNAGDLLKCLLKPKIKVGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQ-----FFIGV 461
Cdd:cd14900  284 ATLLSVDATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKshgglHFIGI 363
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 462 LDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGlDLQACIELI-EKPMGILSILEEEC 540
Cdd:cd14900  364 LDIFGFEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIsQRPTGILSLIDEEC 442
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 541 MFPKASDTSFKNKLYdNHLGKNPMFGKPKPPKagcAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEpiv 620
Cdd:cd14900  443 VMPKGSDTTLASKLY-RACGSHPRFSASRIQR---ARGLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVYGLQ--- 515
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 621 kmlftppriltpggkkkkgksaafqtissvHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLE 700
Cdd:cd14900  516 ------------------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVME 565
                        650       660
                 ....*....|....*....|....*.
gi 254839636 701 GIRICRKGFPNRIIYSEFKQRYSILA 726
Cdd:cd14900  566 AVRVARAGFPIRLLHDEFVARYFSLA 591
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
97-760 1.93e-151

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: 461.28  E-value: 1.93e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLP---------IYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQ-D 166
Cdd:cd14902    1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdlysesqlnAYKASMTSTSPVSQLSELPPHVFAIGGKAFGGLLKpE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 167 RENQSMLITGESGAGKTENTKKVIQYFALVAASLAGKKDKKEEEKKkdekkgtLEDQIVQCNPVLEAYGNAKTTRNNNSS 246
Cdd:cd14902   81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAVE-------IGKRILQTNPILESFGNAQTIRNDNSS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 247 RFGKFIRIHFGTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAfPENIEKILAVPDPGLYGFINQGTLT--- 323
Cdd:cd14902  154 RFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGA-DKTLLDLLGLQKGGKYELLNSYGPSfar 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 324 --VDGIDDEEEMGLTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQRGEQAEADGTAEA-----EKVAFLLGVNAGD 396
Cdd:cd14902  233 krAVADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAAsrfhlAKCAELMGVDVDK 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 397 LLKCLLKPKIKVGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFF---------IGVLDIAGF 467
Cdd:cd14902  313 LETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSIsdedeelatIGILDIFGF 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 468 EIFDFNSFEQLCINYTNERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGlDLQACIELIE-KPMGILSILEEECMFPKAS 546
Cdd:cd14902  393 ESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGS 471
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 547 DTSFKNKLYDNHLGknpmfgkpkppkagcaEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTP 626
Cdd:cd14902  472 NQALSTKFYRYHGG----------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGAD 535
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 627 PRILTPGGKKKKGKSAAFQT-----ISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEG 701
Cdd:cd14902  536 ENRDSPGADNGAAGRRRYSMlrapsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEA 615
                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 702 IRICRKGFPNRIIYSEFKQRYSIL-----------APNAVPSGFADGKVVTDKALSALQLDPNEYRLGNT 760
Cdd:cd14902  616 VRIARHGYSVRLAHASFIELFSGFkcflstrdraaKMNNHDLAQALVTVLMDRVLLEDGVEREEKNPGAL 685
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
97-765 2.44e-150

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: 456.33  E-value: 2.44e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLP-IYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLIT 175
Cdd:cd14904    1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 176 GESGAGKTENTKKVIQYFALVAASLAGKKDkkeeekkkdekkgtleDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIH 255
Cdd:cd14904   81 GESGAGKTETTKIVMNHLASVAGGRKDKTI----------------AKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQ 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 256 FGTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKILAVPDPG-LYGFINQGTLTVDGIDDEEEMG 334
Cdd:cd14904  145 FDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQyQYLGDSLAQMQIPGLDDAKLFA 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 335 LTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQRGEQAEADGTAEA-EKVAFLLGVNAGDLLKCLLKPKIKVGTEYV 413
Cdd:cd14904  225 STQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQlSQVAKMLGLPTTRIEEALCNRSVVTRNESV 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 414 TQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQF-FIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFN 492
Cdd:cd14904  305 TVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFT 384
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 493 HHMFVLEQEEYKKEGIVWEFIDFGlDLQACIELIEKPMGILSILEEECMFPKASDTSFKNKLYDNH--LGKNPMFGKPKP 570
Cdd:cd14904  385 TDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKV 463
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 571 PKagcaeAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRILTPGGKKKKGKS-AAFQTISS 649
Cdd:cd14904  464 KR-----TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAPSETKEGKSGKGtKAPKSLGS 538
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 650 VHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNA 729
Cdd:cd14904  539 QFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPS 618
                        650       660       670
                 ....*....|....*....|....*....|....*..
gi 254839636 730 VPSGfaDGKVVTDKALSAL-QLDPNEYRLGNTKVFFK 765
Cdd:cd14904  619 MHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
97-727 1.09e-148

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


Pssm-ID: 276873 [Multi-domain]  Cd Length: 682  Bit Score: 452.83  E-value: 1.09e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYR--GKRRAE-------MPPHLFSIADNAYQYMLQD- 166
Cdd:cd14908    1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 167 RENQSMLITGESGAGKTENTKKVIQYFALVaaslaGKKDKKEEEKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSS 246
Cdd:cd14908   81 RASQSILISGESGAGKTESTKIVMLYLTTL-----GNGEEGAPNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 247 RFGKFIRIHFGTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEK-------ILAVPDPGLYGFINQ 319
Cdd:cd14908  156 RFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKyefhdgiTGGLQLPNEFHYTGQ 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 320 G-TLTVDGIDDEEEMGLTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQRGEQAEADGTAEAE-----KVAFLLGVN 393
Cdd:cd14908  236 GgAPDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNekclaRVAKLLGVD 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 394 AGDLLKCLLKPKIKVGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQF--FIGVLDIAGFEIFD 471
Cdd:cd14908  316 VDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrsSVGVLDIFGFECFA 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 472 FNSFEQLCINYTNERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGlDLQACIELIE-KPMGILSILEEECMFP-KASDTS 549
Cdd:cd14908  396 HNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDAN 474
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 550 FKNKLYDNHL-------GKNPMFGKPKPPKA-GCaeahFCLHHYAGSVSYSI-AGWLDKNKDPINENVVELLQNSKEpiv 620
Cdd:cd14908  475 YASRLYETYLpeknqthSENTRFEATSIQKTkLI----FAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFESGQQ--- 547
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 621 kmlftppriltpggkkkkgksaafqtissvHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLE 700
Cdd:cd14908  548 ------------------------------FKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLE 597
                        650       660
                 ....*....|....*....|....*..
gi 254839636 701 GIRICRKGFPNRIIYSEFKQRYSILAP 727
Cdd:cd14908  598 AVRVARSGYPVRLPHKDFFKRYRMLLP 624
PTZ00014 PTZ00014
myosin-A; Provisional
38-822 3.26e-148

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 456.03  E-value: 3.26e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  38 DPDFGFVGAEIQ-STKGDEVTVK--TDKTQETRVVKKDDIGQRNPPkFEMNM--DMANLTFLNEASILHNLRSRYESGFI 112
Cdd:PTZ00014  47 DPDLMFAKCLVLpGSTGEKLTLKqiDPPTNSTFEVKPEHAFNANSQ-IDPMTygDIGLLPHTNIPCVLDFLKHRYLKNQI 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 113 YTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAE-MPPHLFSIADNAYQYMLQDRENQSMLITGESGAGKTENTKKVIQ 191
Cdd:PTZ00014 126 YTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMR 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 192 YFAlvaASLAGKKDkkeeekkkdekkGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHFGTQGKIAGADIETYL 271
Cdd:PTZ00014 206 YFA---SSKSGNMD------------LKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFL 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 272 LEKSRVTYQQSAERNYHIFYQLLSPAFPENIEK--ILAVPDpglYGFINQGTLTVDGIDDEEEMGLTDTAFDVLGFTDEE 349
Cdd:PTZ00014 271 LEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKykLKSLEE---YKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQ 347
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 350 KLSMYKCTGCILHLG--EMKWKQRGEQAEADGTAEAEKVAF-----LLGVNAGDLLKCLLKPKIKVGTEYVTQGRNKDQV 422
Cdd:PTZ00014 348 IEDIFSILSGVLLLGnvEIEGKEEGGLTDAAAISDESLEVFneaceLLFLDYESLKKELTVKVTYAGNQKIEGPWSKDES 427
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 423 TNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFVLEQEE 502
Cdd:PTZ00014 428 EMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKL 507
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 503 YKKEGIVWEFIDFGLDLQACIELIEKPMGILSILEEECMFPKASDTSFKNKLYdNHLGKNPMFGKPKPPKAGCaeahFCL 582
Cdd:PTZ00014 508 YKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCN-TNLKNNPKYKPAKVDSNKN----FVI 582
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 583 HHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRIltpggkkKKGKSAAFQTISSVHKESLNKLMKNL 662
Cdd:PTZ00014 583 KHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEV-------EKGKLAKGQLIGSQFLNQLDSLMSLI 655
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 663 YSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNAVPSGFADGKVVTD 742
Cdd:PTZ00014 656 NSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAE 735
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 743 KALSALQLDPNEYRLGNTKVFFKAGVLGMLEDMRDERLSK---IISMFQAHIRGYLMRKAYKK-LQDqrigLTLIQRNVR 818
Cdd:PTZ00014 736 KLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQREKLAAwepLVSVLEALILKIKKKRKVRKnIKS----LVRIQAHLR 811

                 ....
gi 254839636 819 KWLV 822
Cdd:PTZ00014 812 RHLV 815
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
98-765 1.17e-143

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


Pssm-ID: 276860 [Multi-domain]  Cd Length: 704  Bit Score: 440.54  E-value: 1.17e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  98 SILHNLRSRYESGFIYTYSGLFCIAINPYRRLPiytqGL--VDKYRGKRRAEM--PPHLFSIADNAYQYMLQ-------D 166
Cdd:cd14895    2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP----GLydLHKYREEMPGWTalPPHVFSIAEGAYRSLRRrlhepgaS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 167 RENQSMLITGESGAGKTENTKKVIQYFALVAASLAGKKDKKEEEkkkdekkGTLEDQIVQCNPVLEAYGNAKTTRNNNSS 246
Cdd:cd14895   78 KKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRR-------AISGSELLSANPILESFGNARTLRNDNSS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 247 RFGKFIRIHFGTQG-----KIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKI-LAVPDPGLYGFINQG 320
Cdd:cd14895  151 RFGKFVRMFFEGHEldtslRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELqLELLSAQEFQYISGG 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 321 TLTV--DGIDDEEEMGLTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKW-KQRGEQAEADGTAEAEK------------ 385
Cdd:cd14895  231 QCYQrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFvASSEDEGEEDNGAASAPcrlasaspsslt 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 386 -------VAFLLGVNAGDLLKCLLKPKIKVGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLdtkAKRQF- 457
Cdd:cd14895  311 vqqhldiVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSAS---PQRQFa 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 458 -------------FIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGLDlQACIE 524
Cdd:cd14895  388 lnpnkaankdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLE 466
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 525 LIE-KPMGILSILEEECMFPKASDTSFKNKLYdNHLGKNPMFGKPKPPKAGCAeahFCLHHYAGSVSYSIAGWLDKNKDP 603
Cdd:cd14895  467 MLEqRPSGIFSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASRTDQADVA---FQIHHYAGAVRYQAEGFCEKNKDQ 542
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 604 INENVVELLQNSKEPIVKMLFTPPRILTPGGKKK-------KGKSAAFQTISSVHKESLNKLMKNLYSTHPHFVRCIIPN 676
Cdd:cd14895  543 PNAELFSVLGKTSDAHLRELFEFFKASESAELSLgqpklrrRSSVLSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIKPN 622
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 677 ELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNAVPSGFADGKVvtdkaLSALQLDPNEyr 756
Cdd:cd14895  623 DESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASAL-----IETLKVDHAE-- 695

                 ....*....
gi 254839636 757 LGNTKVFFK 765
Cdd:cd14895  696 LGKTRVFLR 704
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
97-765 2.89e-137

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: 421.88  E-value: 2.89e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITG 176
Cdd:cd14896    1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 177 ESGAGKTENTKKVIQYFALVAASlagkkdkkeeekkkdekkgTLEDQIVQ-CN--PVLEAYGNAKTTRNNNSSRFGKFIR 253
Cdd:cd14896   81 HSGSGKTEAAKKIVQFLSSLYQD-------------------QTEDRLRQpEDvlPILESFGHAKTILNANASRFGQVLR 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 254 IHFgTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKiLAVPDPGLYGFINQG-TLTVDGIDDEEE 332
Cdd:cd14896  142 LHL-QHGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQ-LSLQGPETYYYLNQGgACRLQGKEDAQD 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 333 MGLTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKW----KQRGEQAEADGTAEAEKVAFLLGVNAgDLLKCLLKPKIKV 408
Cdd:cd14896  220 FEGLLKALQGLGLCAEELTAIWAVLAAILQLGNICFssseRESQEVAAVSSWAEIHTAARLLQVPP-ERLEGAVTHRVTE 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 409 gTEYvtqgrnkDQVTNSIA---------ALAKSLYDRMFNWLVRRVNQTLDTKAKRQFF--IGVLDIAGFEIFDFNSFEQ 477
Cdd:cd14896  299 -TPY-------GRVSRPLPvegaidardALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQ 370
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 478 LCINYTNERLQQFFNHHMFVLEQEEYKKEGIVWEFIDfGLDLQACIELI-EKPMGILSILEEECMFPKASDTSFKNKLYD 556
Cdd:cd14896  371 LCINLASERLQLFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHY 449
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 557 NHlGKNPMFGKPKPPKagcaeAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFtppRILTPGGKK 636
Cdd:cd14896  450 HH-GDHPSYAKPQLPL-----PVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLF---QEAEPQYGL 520
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 637 KKGKSaafqTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYS 716
Cdd:cd14896  521 GQGKP----TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQ 596
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|.
gi 254839636 717 EFKQRYSILAPNAVPSGFADGK--VVTDKALSAlqlDPNEYRLGNTKVFFK 765
Cdd:cd14896  597 AFLARFGALGSERQEALSDRERcgAILSQVLGA---ESPLYHLGATKVLLK 644
MYSc_Myo14 cd14876
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...
97-765 5.71e-134

class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276843  Cd Length: 649  Bit Score: 413.61  E-value: 5.71e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRG-KRRAEMPPHLFSIA----DNAYQYmlqdRENQS 171
Cdd:cd14876    1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTArralENLHGV----NKSQT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 172 MLITGESGAGKTENTKKVIQYFAlvAASlagkkdkkeeekkKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKF 251
Cdd:cd14876   77 IIVSGESGAGKTEATKQIMRYFA--SAK-------------SGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRF 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 252 IRIHFGTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKiLAVPDPGLYGFINQGTLTVDGIDDEE 331
Cdd:cd14876  142 MQLDVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSK-YHLLGLKEYKFLNPKCLDVPGIDDVA 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 332 EMGLTDTAFDVLGFTDEEKLSMYKCTGCILHLG--EMKWKQRGEQAEADGTAEAEKVAF-----LLGVNAGDLLKCLLKP 404
Cdd:cd14876  221 DFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGnvKITGKTEQGVDDAAAISNESLEVFkeacsLLFLDPEALKRELTVK 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 405 KIKVGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTN 484
Cdd:cd14876  301 VTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITN 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 485 ERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGLDLQACIELIEKPMGILSILEEECMFPKASDTSFKNKLYDNhLGKNpm 564
Cdd:cd14876  381 EMLQKNFIDIVFERESKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSK-LKSN-- 457
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 565 fGKPKPPKAGcAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRIltpggkkKKGKSAAF 644
Cdd:cd14876  458 -GKFKPAKVD-SNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVV-------EKGKIAKG 528
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 645 QTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSI 724
Cdd:cd14876  529 SLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKF 608
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|.
gi 254839636 725 LAPNAVPSGFADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14876  609 LDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
97-763 4.07e-132

class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276846 [Multi-domain]  Cd Length: 658  Bit Score: 409.24  E-value: 4.07e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLP-IYTQGLVDKYRGKRRAE-MPPHLFSIADNAYQYMLQDRE--NQSM 172
Cdd:cd14880    1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQkLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 173 LITGESGAGKTENTKKVIQYFALVAASLAGKKDKKEEEKkkdekkgtLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFI 252
Cdd:cd14880   81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAER--------IEQRILNSNPVMEAFGNACTLRNNNSSRFGKFI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 253 RIHFGTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKiLAVPDPGLYGFINQGTLTVdgidDEEE 332
Cdd:cd14880  153 QLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQ-WHLPEGAAFSWLPNPERNL----EEDC 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 333 MGLTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQRGEQAEA----DGTAEAEKV-AFLLGVNAGDLLKCLLKPKIK 407
Cdd:cd14880  228 FEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpmDDTKESVRTsALLLKLPEDHLLETLQIRTIR 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 408 VGTEYVTQGR--NKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKR-QFFIGVLDIAGFEIFDFNSFEQLCINYTN 484
Cdd:cd14880  308 AGKQQQVFKKpcSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYAN 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 485 ERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGlDLQACIELIE-KPMGILSILEEECMFPKASDTSFKNKLYDNHLGKNP 563
Cdd:cd14880  388 EKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAGNP 466
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 564 MFGKPKPPKagcaEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLF-TPPRILTPGGKKKKGKSA 642
Cdd:cd14880  467 CLGHNKLSR----EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFpANPEEKTQEEPSGQSRAP 542
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 643 AFqTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRY 722
Cdd:cd14880  543 VL-TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERY 621
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|...
gi 254839636 723 SILAPN--AVPSGFADgkvvtdkaLSALQLDPNEYRLGNTKVF 763
Cdd:cd14880  622 KLLRRLrpHTSSGPHS--------PYPAKGLSEPVHCGRTKVF 656
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
97-728 2.46e-129

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: 403.59  E-value: 2.46e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLP-IYTQGLVDKYRGKRR-AEMPPHLFSIADNAYQYMLQDRENQSMLI 174
Cdd:cd14906    1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 175 TGESGAGKTENTKKVIQYfaLVAASlagkKDKKEEEKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRI 254
Cdd:cd14906   81 SGESGSGKTEASKTILQY--LINTS----SSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 255 HF-GTQGKIAGADIETYLLEKSRVTYQ-QSAERNYHIFYQLLSPAFPENIEKILAVPDPGLYGFINQGTLTVDGI----- 327
Cdd:cd14906  155 EFrSSDGKIDGASIETYLLEKSRISHRpDNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFksqss 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 328 ----------DDEEEMGLTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQ-----RGEQAEADGTAEAEKVAFLLGV 392
Cdd:cd14906  235 nknsnhnnktESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEdsdfsKYAYQKDKVTASLESVSKLLGY 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 393 NAGDLLKCLLKPKIKVGTEYVTQGRNKD--QVTNSIAALAKSLYDRMFNWLVRRVNQTLD-----------TKAKRQFFI 459
Cdd:cd14906  315 IESVFKQALLNRNLKAGGRGSVYCRPMEvaQSEQTRDALSKSLYVRLFKYIVEKINRKFNqntqsndlaggSNKKNNLFI 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 460 GVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFgLDLQACIELIE-KPMGILSILEE 538
Cdd:cd14906  395 GVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDD 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 539 ECMFPKASDTSF---KNKLYDNhlgknpmfgKPKPPKAGCAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNS 615
Cdd:cd14906  474 ECIMPKGSEQSLlekYNKQYHN---------TNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLAS 544
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 616 KEPIVKMLFTPPRILTPGGKKKKGKSAafqTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRC 695
Cdd:cd14906  545 SNFLKKSLFQQQITSTTNTTKKQTQSN---TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRN 621
                        650       660       670
                 ....*....|....*....|....*....|...
gi 254839636 696 NGVLEGIRICRKGFPNRIIYSEFKQRYSILAPN 728
Cdd:cd14906  622 VGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
MYSc_Myo25 cd14886
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...
97-765 4.26e-125

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


Pssm-ID: 276851  Cd Length: 650  Bit Score: 390.40  E-value: 4.26e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLP-IYTQGLVDKYRGKRRA-----EMPPHLFSIADNAYQYMLQDRENQ 170
Cdd:cd14886    1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 171 SMLITGESGAGKTENTKKVIQYFALVAASlagkkdkkeeekkkdeKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGK 250
Cdd:cd14886   81 SCIVSGESGAGKTETAKQLMNFFAYGHST----------------SSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGK 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 251 FIRIHFGTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENiEKILAVPDPGLYGFINQGT-LTVDGIDD 329
Cdd:cd14886  145 FIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEE-KKSLGFKSLESYNFLNASKcYDAPGIDD 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 330 EEEMGLTDTAFDVLgFTDEEKLSMYKCTGCILHLGEMKWKQRGEQ-----AEADGTAEAEKVAFLLGVNAGDLLKCLLKP 404
Cdd:cd14886  224 QKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDMgvinaAKISNDEDFGKMCELLGIESSKAAQAIITK 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 405 KIKVGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTN 484
Cdd:cd14886  303 VVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYAN 382
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 485 ERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGlDLQACIELIEKP-MGILSILEEECMFPKASDTSF----KNKLYDNHL 559
Cdd:cd14886  383 ERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFtsscKSKIKNNSF 461
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 560 gknpmfgkpkPPKAGcAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRILTPGGKKkkg 639
Cdd:cd14886  462 ----------IPGKG-SQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNMKG--- 527
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 640 ksaafQTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFK 719
Cdd:cd14886  528 -----KFLGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFF 602
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....*...
gi 254839636 720 QRYSILA--PNAVPSGFADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14886  603 HRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
97-765 5.22e-122

class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276842 [Multi-domain]  Cd Length: 664  Bit Score: 383.01  E-value: 5.22e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFI-YTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEM-PPHLFSIADNAY-QYMLQDRENQSML 173
Cdd:cd14875    1 ATLLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFnAIFVQGLGNQSVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 174 ITGESGAGKTENTKKVIQYFALVAASLAGKKDKKeeekkkdekkgTLEDQIVQC----NPVLEAYGNAKTTRNNNSSRFG 249
Cdd:cd14875   81 ISGESGSGKTENAKMLIAYLGQLSYMHSSNTSQR-----------SIADKIDENlkwsNPVMESFGNARTVRNDNSSRFG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 250 KFIRIHF-GTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKILAVPDPGLYGFINQG-TLT---V 324
Cdd:cd14875  150 KYIKLYFdPTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGnTFVrrgV 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 325 DG--IDDEEEMGLTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQ-RGEQAE-ADGTAEAEKVAfLLGVNAGDLLKC 400
Cdd:cd14875  230 DGktLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESdQNDKAQiADETPFLTACR-LLQLDPAKLREC 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 401 LLkpkIKVGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTK--AKRQFFIGVLDIAGFEIFDFNSFEQL 478
Cdd:cd14875  309 FL---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQgdCSGCKYIGLLDIFGFENFTRNSFEQL 385
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 479 CINYTNERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGlDLQACIELIE-KPMGILSILEEECMFPKASDTSFKNKLYDN 557
Cdd:cd14875  386 CINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQ 464
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 558 HLGKNPMFGKPKppkaGCAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRILTPGGkkk 637
Cdd:cd14875  465 WANKSPYFVLPK----STIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARRK--- 537
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 638 kgksaafQTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSE 717
Cdd:cd14875  538 -------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQ 610
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 254839636 718 FKQRYSILAPNAVPSGFADGKvVTDKALSALQL--------DPNeYRLGNTKVFFK 765
Cdd:cd14875  611 FCRYFYLIMPRSTASLFKQEK-YSEAAKDFLAYyqrlygwaKPN-YAVGKTKVFLR 664
MYSc_Myo38 cd14899
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...
97-722 6.39e-122

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


Pssm-ID: 276864 [Multi-domain]  Cd Length: 717  Bit Score: 384.45  E-value: 6.39e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLP-IYTQGLVDKYRGKRRAEM----------PPHLFSIADNAYQYMLQ 165
Cdd:cd14899    1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAYDHNSQFgdrvtstdprEPHLFAVARAAYIDIVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 166 DRENQSMLITGESGAGKTENTKKVIQYFALVAASLAGKKDKKEEEKKKDEKK-GTLEDQIVQCNPVLEAYGNAKTTRNNN 244
Cdd:cd14899   81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISPPASPSrTTIEEQVLQSNPILEAFGNARTVRNDN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 245 SSRFGKFIRIHFGTQG-KIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSP---AFPENIEKILAVPD-PGLYGFINQ 319
Cdd:cd14899  161 SSRFGKFIELRFRDERrRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnnCVSKEQKQVLALSGgPQSFRLLNQ 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 320 GTLTV--DGIDDEEEMGLTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQRGEQAEADGTAEAEKVAF--------- 388
Cdd:cd14899  241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKGDDTVFADEARVMSsttgafdhf 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 389 -----LLGVNAGDLLKCLLKPKIKVGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQF------ 457
Cdd:cd14899  321 tkaaeLLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASAPWgadesd 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 458 ---------FIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGlDLQACIELIE- 527
Cdd:cd14899  401 vddeedatdFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEh 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 528 KPMGILSILEEECMFPKASDTSFKNKLYDNHLGK--NPMFgkpKPPKAGCAEAHFCLHHYAGSVSYSIAGWLDKNKDPIN 605
Cdd:cd14899  480 RPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKnsHPHF---RSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFC 556
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 606 ENVVELLQNSKEPIVKMLFT-----------PPRILTPGGKKKKGKSAAFQTISSVHKESLNKLMKNLYSTHPHFVRCII 674
Cdd:cd14899  557 ESAAQLLAGSSNPLIQALAAgsndedangdsELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIK 636
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....*...
gi 254839636 675 PNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRY 722
Cdd:cd14899  637 PNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
MYSc_Myo18 cd01386
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...
97-765 7.72e-110

class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276837 [Multi-domain]  Cd Length: 689  Bit Score: 351.61  E-value: 7.72e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITG 176
Cdd:cd01386    1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 177 ESGAGKTENTKKVIQYFALVAASLAGKKDKkeeekkkdekkgtleDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHF 256
Cdd:cd01386   81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSV---------------EKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDF 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 257 GTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPE-----NIEKILAVPDPGLYGFINQGtltvDGIDDEE 331
Cdd:cd01386  146 DQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAAlrtelHLNQLAESNSFGIVPLQKPE----DKQKAAA 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 332 EMGLTDTAFDVLGFTDEEKLSMYKCTGCILHL---GEMKWKQRGEQAEADGTAeAEKVAFLLGVNAGDLLKCLLKPKIKV 408
Cdd:cd01386  222 AFSKLQAAMKTLGISEEEQRAIWSILAAIYHLgaaGATKAASAGRKQFARPEW-AQRAAYLLGCTLEELSSAIFKHHLSG 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 409 GTEYVTQGRNKDQVTNS------------IAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFN--- 473
Cdd:cd01386  301 GPQQSTTSSGQESPARSssggpkltgveaLEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsq 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 474 ---SFEQLCINYTNERLQQFFNHHMFVLEQEEYKKEGIVwefIDFGLD---LQACIELIEK---------------PMGI 532
Cdd:cd01386  381 rgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVE---VDFDLPelsPGALVALIDQapqqalvrsdlrdedRRGL 457
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 533 LSILEEECMFPKASDTSFKNKLYdNHLGKNPMFGKPKPPKAGCAEAHFCLHHYAGS--VSYSIAGWLDKNK-DPINENVV 609
Cdd:cd01386  458 LWLLDEEALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLRRSEGPLQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNAT 536
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 610 ELLQNSKEPIVKMlftppriltpggkkkKGKSAAFQTissvhKESLNKLMKNLYSTHPHFVRCIIPN------ELKTPG- 682
Cdd:cd01386  537 QLLQESQKETAAV---------------KRKSPCLQI-----KFQVDALIDTLRRTGLHFVHCLLPQhnagkdERSTSSp 596
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 683 -----LIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAP-----NAVPSGFADGKVVTDKALSALQLDP 752
Cdd:cd01386  597 aagdeLLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPpltkkLGLNSEVADERKAVEELLEELDLEK 676
                        730
                 ....*....|...
gi 254839636 753 NEYRLGNTKVFFK 765
Cdd:cd01386  677 SSYRIGLSQVFFR 689
MYSc_Myo37 cd14898
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...
98-729 2.92e-102

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


Pssm-ID: 276863  Cd Length: 578  Bit Score: 328.40  E-value: 2.92e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  98 SILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGlvdKYRGKRRAEMPPHLFSIADNAYQYMLQdRENQSMLITGE 177
Cdd:cd14898    2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGAM---KAYLKNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 178 SGAGKTENTKKVIQYFALVAASlagkkdkkeeekkkdekKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHFg 257
Cdd:cd14898   78 SGSGKTENAKLVIKYLVERTAS-----------------TTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF- 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 258 tQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSpafpeniEKILAVPDpglyGFINQGTLTVDG---IDDEEEMG 334
Cdd:cd14898  140 -DGKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCA-------SKRLNIKN----DFIDTSSTAGNKesiVQLSEKYK 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 335 LTDTAFDVLGFTDEEklSMYKCTGCILHLGEMKWKQRGeQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVT 414
Cdd:cd14898  208 MTCSAMKSLGIANFK--SIEDCLLGILYLGSIQFVNDG-ILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIE 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 415 QGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQffIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHH 494
Cdd:cd14898  285 VFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKK 362
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 495 MFVLEQEEYKKEGIVWEFIDFgLDLQACIELIEKPMGILSILEEECMFP--KASDTSFKNKLYDNHLGKNPMFGKPKppk 572
Cdd:cd14898  363 MFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAwgNVKNLLVKIKKYLNGFINTKARDKIK--- 438
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 573 agcaeahfcLHHYAGSVSYSIAGWLDKNKDP----INENVVELLQNSKEPIVKMLftppriltpggkkkkgksaafqtis 648
Cdd:cd14898  439 ---------VSHYAGDVEYDLRDFLDKNREKgqllIFKNLLINDEGSKEDLVKYF------------------------- 484
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 649 svhKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPN 728
Cdd:cd14898  485 ---KDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGIT 561

                 .
gi 254839636 729 A 729
Cdd:cd14898  562 L 562
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
97-765 6.41e-100

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: 324.46  E-value: 6.41e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYR---GKRRAEMPPHLFSIADNAYQYMLQDRENQSML 173
Cdd:cd14878    1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 174 ITGESGAGKTENTKKVIQYFALVAASlagkkdkkeeekkkdeKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIR 253
Cdd:cd14878   81 LSGERGSGKTEASKQIMKHLTCRASS----------------SRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFE 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 254 IHFGTQGK-IAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPEniEKI-LAVPDPGLYGFINQG----TLTVDGI 327
Cdd:cd14878  145 LQFCERKKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAE--EKYgLHLNNLCAHRYLNQTmredVSTAERS 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 328 DDEEEMGLTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWK--QRGEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPK 405
Cdd:cd14878  223 LNREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTalTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDI 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 406 IKVGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTL----DTKAKRQFFIGVLDIAGFEIFDFNSFEQLCIN 481
Cdd:cd14878  303 QYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVN 382
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 482 YTNERLQQFFNHHMFVLEQEEYKKEGIVWEFIdFGLDLQACIE--LIEKPMGILSILEEECM--------FPKA----SD 547
Cdd:cd14878  383 MTNEKMHHYINEVLFLQEQTECVQEGVTMETA-YSPGNQTGVLdfFFQKPSGFLSLLDEESQmiwsvepnLPKKlqslLE 461
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 548 TSFKNKLYDNHLGKNpmfGKPKPPKAGCAeahFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFtpp 627
Cdd:cd14878  462 SSNTNAVYSPMKDGN---GNVALKDQGTA---FTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLF--- 532
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 628 riltpggkkkkgkSAAFQTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRK 707
Cdd:cd14878  533 -------------QSKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRY 599
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 254839636 708 GFPNRIIYSEFKQRYSILAPNAVpsGFADGKVVTDKALSALQLDPNE-YRLGNTKVFFK 765
Cdd:cd14878  600 GYPVRLSFSDFLSRYKPLADTLL--GEKKKQSAEERCRLVLQQCKLQgWQMGVRKVFLK 656
MYSc_Myo26 cd14887
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...
97-765 1.68e-98

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


Pssm-ID: 276852  Cd Length: 725  Bit Score: 322.75  E-value: 1.68e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGF--------IYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRE 168
Cdd:cd14887    1 PNLLENLYQRYNKAYinkenrncIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 169 NQSMLITGESGAGKTENTKKVIQYFALVAASLAGKKDKkeeekkkdekkgTLEDQIVQCNPVLEAYGNAKTTRNNNSSRF 248
Cdd:cd14887   81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQ------------GLEARLLQSGPVLEAFGNAHTVLNANSSRF 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 249 GKFIRIHFGTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKILA-VPDPGLYG--FINQGTLTVD 325
Cdd:cd14887  149 GKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAgEGDPESTDlrRITAAMKTVG 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 326 -GIDDEEEMGLTDTAFDVLG---FT---DEEKLSMYKCT----GCI------LHLGEMKWKQRGEQAEADGTAEAEKVAF 388
Cdd:cd14887  229 iGGGEQADIFKLLAAILHLGnveFTtdqEPETSKKRKLTsvsvGCEetaadrSHSSEVKCLSSGLKVTEASRKHLKTVAR 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 389 LLGVNAGDLLKCLLKPKIKVGTEYVTQGR-NKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQF---------- 457
Cdd:cd14887  309 LLGLPPGVEGEEMLRLALVSRSVRETRSFfDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKPSEsdsdedtpst 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 458 ----FIGVLDIAGFEIF---DFNSFEQLCINYTNERLQQFFNHHMFVLEQEEYKKEGIVWEFI--DFGLDLQACIELIEK 528
Cdd:cd14887  389 tgtqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsAFPFSFPLASTLTSS 468
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 529 P------------------------MGILSILEEE-CMFPKASDTSFKNKLYDNHLGK---NPMFGKPKPPKAGCAEAHF 580
Cdd:cd14887  469 PsstspfsptpsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKniiNSAKYKNITPALSRENLEF 548
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 581 CLHHYAGSVSYSIAGWLDKNKDpINENVVELLQNSKEPIVKMlftpprILTPGGKKKKGKSAAFQTISSVHKESLNKLMK 660
Cdd:cd14887  549 TVSHFACDVTYDARDFCRANRE-ATSDELERLFLACSTYTRL------VGSKKNSGVRAISSRRSTLSAQFASQLQQVLK 621
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 661 NLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNAVPSgFADGKVV 740
Cdd:cd14887  622 ALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALRE-ALTPKMF 700
                        730       740
                 ....*....|....*....|....*
gi 254839636 741 TDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14887  701 CKIVLMFLEINSNSYTFGKTKIFFR 725
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
94-774 1.08e-97

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: 318.34  E-value: 1.08e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  94 LNEASILHNLRSRYESGFIYTY---SGLfcIAINPYRRLPIYTQGLVDKYR-------GKRRAEMPPHLFSIADNAYQYM 163
Cdd:cd14879    1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 164 LQDRENQSMLITGESGAGKTENTKKVIQyfALVAASLAGKKdkkeeekkkdekkGT-LEDQIVQCNPVLEAYGNAKTTRN 242
Cdd:cd14879   79 RRRSEDQAVVFLGETGSGKSESRRLLLR--QLLRLSSHSKK-------------GTkLSSQISAAEFVLDSFGNAKTLTN 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 243 NNSSRFGKFIRIHFGTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPEniEK-ILAVPDPGLYGFI---- 317
Cdd:cd14879  144 PNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPE--ERqHLGLDDPSDYALLasyg 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 318 -NQGTLTVdGIDDEEEMGLTDTAFDVLGFTDEEKLSMYKCTGCILHLG--EMKWKQRGEQAEA--DGTAEAEKVAFLLGV 392
Cdd:cd14879  222 cHPLPLGP-GSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGnlEFTYDHEGGEESAvvKNTDVLDIVAAFLGV 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 393 NAGDLLKCL-LKPKIkVGTEYVT------QGR-NKDQvtnsiaaLAKSLYDRMFNWLVRRVNQTLdTKAKRQF--FIGVL 462
Cdd:cd14879  301 SPEDLETSLtYKTKL-VRKELCTvfldpeGAAaQRDE-------LARTLYSLLFAWVVETINQKL-CAPEDDFatFISLL 371
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 463 DIAGFEIFD---FNSFEQLCINYTNERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFgLDLQACIELI-EKPMGILSILEE 538
Cdd:cd14879  372 DFPGFQNRSstgGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDD 450
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 539 EC-MFPKASDTSFKNKLyDNHLGKNPMFGKPKPPKAGCAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKE 617
Cdd:cd14879  451 QTrRMPKKTDEQMLEAL-RKRFGNHSSFIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLLRGATQ 529
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 618 pivkmlftppriltpggkkkkgksaafqtissvHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNG 697
Cdd:cd14879  530 ---------------------------------LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLG 576
                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254839636 698 VLEGIRICRKGFPNRIIYSEFKQRYSILAPnavpsgFADGKVVTDKALSALQLDPNEYRLGNTKVFFKAGVLGMLED 774
Cdd:cd14879  577 LPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFLSYAAWRMLED 647
MYSc_Myo24A cd14937
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
97-765 1.02e-96

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: 315.42  E-value: 1.02e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYtqglVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITG 176
Cdd:cd14937    1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 177 ESGAGKTENTKKVIQYFalvaasLAGKKDKKEEEKkkdekkgTLEDQivqcNPVLEAYGNAKTTRNNNSSRFGKFIRIHF 256
Cdd:cd14937   77 ESGSGKTEASKLVIKYY------LSGVKEDNEISN-------TLWDS----NFILEAFGNAKTLKNNNSSRYGKYIKIEL 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 257 GTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSpAFPENIEKILAVPDPGLYGFINQGTLTVDGIDDEEEMGLT 336
Cdd:cd14937  140 DEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFN-GMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNL 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 337 DTAFDVLGFTDEEKLSMYKCTGCILhLGEMKWkQRGEQAEADGTAEAEK--------VAFLLGVNAGDLLKCLLKPKIKV 408
Cdd:cd14937  219 MISFDKMNMHDMKDDLFLTLSGLLL-LGNVEY-QEIEKGGKTNCSELDKnnlelvneISNLLGINYENLKDCLVFTEKTI 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 409 GTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQ 488
Cdd:cd14937  297 ANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIH 376
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 489 QFFNHHMFVLEQEEYKKEGIVWEFIDFGLDlQACIELIEKPMGILSILEEECMFPKASDTSFKNkLYDNHLGKNPMFGKP 568
Cdd:cd14937  377 SIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESIVS-VYTNKFSKHEKYAST 454
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 569 KPPkagcAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRILTPGGKKkkgksaafQTIS 648
Cdd:cd14937  455 KKD----INKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRK--------NLIT 522
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 649 SVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRIcRKGFPNRIIYSEFKQRYSILAPN 728
Cdd:cd14937  523 FKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYS 601
                        650       660       670
                 ....*....|....*....|....*....|....*....
gi 254839636 729 AVPSGFADGKvvtDKALSALQ--LDPNEYRLGNTKVFFK 765
Cdd:cd14937  602 TSKDSSLTDK---EKVSMILQntVDPDLYKVGKTMVFLK 637
MYSc_Myo23 cd14884
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ...
97-717 6.88e-95

class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276850 [Multi-domain]  Cd Length: 685  Bit Score: 311.84  E-value: 6.88e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLP-IYTQGLVDKYRGKR-------RAEMPPHLFSIADNAYQYMLQDRE 168
Cdd:cd14884    1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKsnsaasaAPFPKAHIYDIANMAYKNMRGKLK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 169 NQSMLITGESGAGKTENTKKVIQYFALVaaslagkkdkkeeekKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRF 248
Cdd:cd14884   81 RQTIVVSGHSGSGKTENCKFLFKYFHYI---------------QTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRC 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 249 GKFIRIHFGT---------QGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKILAVPDPGLYGFIN- 318
Cdd:cd14884  146 GRINLLIFEEventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNp 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 319 ---------QGTLTVDGID---DEEEMGLTDTAFDVL--GFT----DEEKLS-MYKCTGCILHLGEMKWKQRGEqaeadg 379
Cdd:cd14884  226 deshqkrsvKGTLRLGSDSldpSEEEKAKDEKNFVALlhGLHyikyDERQINeFFDIIAGILHLGNRAYKAAAE------ 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 380 taeaekvafLLGVNAGDLLKCLLKPKIKVGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQT-LDTKAKRQF- 457
Cdd:cd14884  300 ---------CLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNvLKCKEKDESd 370
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 458 ----------FIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFVLEQEEYKKEGIVW--EFIDFGLDLQACIEL 525
Cdd:cd14884  371 nediysineaIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICcsDVAPSYSDTLIFIAK 450
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 526 IEKPMGILSILEEECMfpKASDTSFKNKLYDN----HLGKNPMFGKPKP-------PKAGCAEAHFCLHHYAGSVSYSIA 594
Cdd:cd14884  451 IFRRLDDITKLKNQGQ--KKTDDHFFRYLLNNerqqQLEGKVSYGFVLNhdadgtaKKQNIKKNIFFIRHYAGLVTYRIN 528
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 595 GWLDKNKDPINENVVELLQNSKepivkmlftpprILTPGGKKKKGKSAAFQTISSVHKESLNKLMKNLYSTHPHFVRCII 674
Cdd:cd14884  529 NWIDKNSDKIETSIETLISCSS------------NRFLREANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFL 596
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|...
gi 254839636 675 PNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSE 717
Cdd:cd14884  597 PNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
MYSc_Myo12 cd14874
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...
97-765 1.02e-80

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


Pssm-ID: 276841 [Multi-domain]  Cd Length: 628  Bit Score: 272.13  E-value: 1.02e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  97 ASILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYrgkrraemppHLFSIADNAYQYMLQDRENQSMLI-T 175
Cdd:cd14874    1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNAESIVfG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 176 GESGAGKTENTKKVIQYfaLVAASlagkkdkkeeekkkDEKKGTLEDQIVQCnpVLEAYGNAKTTRNNNSSRFGKFIRIH 255
Cdd:cd14874   71 GESGSGKSYNAFQVFKY--LTSQP--------------KSKVTTKHSSAIES--VFKSFGCAKTLKNDEATRFGCSIDLL 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 256 FgTQGKIAGADIE-TYLLEKSRVTYQQSAERNYHIFYQLLSpAFPENIEKILAVPDPGLYGFINQGTLTVDGIDDEEEMG 334
Cdd:cd14874  133 Y-KRNVLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYH-GLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFK 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 335 LTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWK-QRGEQAEAD-----GTAEAEKVAFLLGVNAGDLLKCLLkPKIKV 408
Cdd:cd14874  211 HLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRtKRNPNVEQDvveigNMSEVKWVAFLLEVDFDQLVNFLL-PKSED 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 409 GTEYvtqgrNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTkAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQ 488
Cdd:cd14874  290 GTTI-----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKC-PLHTGVISILDHYGFEKYNNNGVEEFLINSVNERIE 363
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 489 QFFNHHMFVLEQEEYKKEGIVWEF-IDFGLDLQACIELI-EKPMGILSILEEECMFPKASDTSFKNKLYDNHLGKNpMFG 566
Cdd:cd14874  364 NLFVKHSFHDQLVDYAKDGISVDYkVPNSIENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRS-SYG 442
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 567 KPKPPKagcaEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFtppRILTPGGKKKKGKSAAFQT 646
Cdd:cd14874  443 KARNKE----RLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLF---ESYSSNTSDMIVSQAQFIL 515
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 647 ISSvhKESLNKLMKnlysTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILA 726
Cdd:cd14874  516 RGA--QEIADKING----SHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLL 589
                        650       660       670
                 ....*....|....*....|....*....|....*....
gi 254839636 727 PNAVPSGFADGKVVTDKALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14874  590 PGDIAMCQNEKEIIQDILQGQGVKYENDFKIGTEYVFLR 628
MYSc_Myo44 cd14905
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...
98-765 2.25e-77

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: 264.26  E-value: 2.25e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  98 SILHNLRSRYESGFIYTYSGLFCIAINPYRRLP-IYTQGLVDKYRGKRraEMPPHLFSIADNAYQYMLQDRENQSMLITG 176
Cdd:cd14905    2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRR--GLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 177 ESGAGKTENTKKVIQYFALVAASLAGKkdkkeeekkkdekkgtLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHF 256
Cdd:cd14905   80 ESGSGKSENTKIIIQYLLTTDLSRSKY----------------LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFY 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 257 GTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENiEKILAVPDPGLYGFINQG-TLTVDGIDDEEEMGL 335
Cdd:cd14905  144 SLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEE-KAAYQLGDINSYHYLNQGgSISVESIDDNRVFDR 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 336 TDTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQRGEQAEADGTAEAEKVAFLLGVNAGDLLKCLLKPKIKVGTEYVtq 415
Cdd:cd14905  223 LKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNGKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAV-- 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 416 gRNKDqvtnsiaALAKSLYDRMFNWLVRRVNQTLdTKAKRQFFIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHM 495
Cdd:cd14905  301 -ENRD-------SLARSLYSALFHWIIDFLNSKL-KPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTV 371
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 496 FVLEQEEYKKEGIVWEFIDFGLDLQACIELIEKpmgILSILEEECMFPKASDTSFKNKLyDNHLGKNPMFGKpKPPKagc 575
Cdd:cd14905  372 LKQEQREYQTERIPWMTPISFKDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL-QNFLSRHHLFGK-KPNK--- 443
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 576 aeahFCLHHYAGSVSYSIAGWLDKNKDPI-------------------------NENVVELLQ-------NSKEP--IVK 621
Cdd:cd14905  444 ----FGIEHYFGQFYYDVRGFIIKNRDEIlqrtnvlhknsitkylfsrdgvfniNATVAELNQmfdakntAKKSPlsIVK 519
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 622 MLFT-----PPRILTPGGKK------------KKGKSAAFQTISSVHKESLNKlmknlySTHPHFVRCIIPNELKTPGLI 684
Cdd:cd14905  520 VLLScgsnnPNNVNNPNNNSgggggggnsgggSGSGGSTYTTYSSTNKAINNS------NCDFHFIRCIKPNSKKTHLTF 593
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 685 DAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILAPNAvpSGFAD-GKVVTDKALSALQLDPNEYRLGNTKVF 763
Cdd:cd14905  594 DVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQ--RNFQNlFEKLKENDINIDSILPPPIQVGNTKIF 671

                 ..
gi 254839636 764 FK 765
Cdd:cd14905  672 LR 673
MYSc_Myo21 cd14882
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...
98-765 3.59e-75

class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276848  Cd Length: 642  Bit Score: 257.75  E-value: 3.59e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  98 SILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITGE 177
Cdd:cd14882    2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 178 SGAGKTENTKKVIQYFALVAASLAGKKDkkeeekkkdekkgtledQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRIHFG 257
Cdd:cd14882   82 SYSGKTTNARLLIKHLCYLGDGNRGATG-----------------RVESSIKAILALVNAGTPLNADSTRCILQYQLTFG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 258 TQGKIAGADIETYLLEKSRVTYQQSAERNYHIFY----------QLLSPAFPEN-----IEKILAVPDPGLYGFINQGTL 322
Cdd:cd14882  145 STGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYyfydfieaqnRLKEYNLKAGrnyryLRIPPEVPPSKLKYRRDDPEG 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 323 TVDGIDDEEEMgltdtaFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQRGEQAEADGTAEAEKVAFLLGVNAGDLLKCLL 402
Cdd:cd14882  225 NVERYKEFEEI------LKDLDFNEEQLETVRKVLAAILNLGEIRFRQNGGYAELENTEIASRVAELLRLDEKKFMWALT 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 403 KPKIKVGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLD-TKA--KRQFFIGVLDIAGFEIFDFNSFEQLC 479
Cdd:cd14882  299 NYCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSfPRAvfGDKYSISIHDMFGFECFHRNRLEQLM 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 480 INYTNERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGLDLQACIELIEKPMGILSILEEecmfpkASDTSF-KNKLYDNH 558
Cdd:cd14882  379 VNTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD------ASRSCQdQNYIMDRI 452
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 559 LGKNPMFGKPkppkagcAEAH-FCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIVKMLFTPPRIltpggkkk 637
Cdd:cd14882  453 KEKHSQFVKK-------HSAHeFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQV-------- 517
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 638 kgksAAFQTISSVHKESLNKLMKNLY----STHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRI 713
Cdd:cd14882  518 ----RNMRTLAATFRATSLELLKMLSiganSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRI 593
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 254839636 714 IYSEFKQRYSILAPNavpsgfADGKVVTDK---ALSALQLDPNEYRLGNTKVFFK 765
Cdd:cd14882  594 PFQEFLRRYQFLAFD------FDETVEMTKdncRLLLIRLKMEGWAIGKTKVFLK 642
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
98-764 1.53e-73

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: 252.73  E-value: 1.53e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  98 SILHNLRSRYESGFIYTYSGLFCIAINPYR-----RLPIYTQGLVDKyrgkrraempPHLFSIADNAYQYMLQDRENQSM 172
Cdd:cd14881    2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRdvgnpLTLTSTRSSPLA----------PQLLKVVQEAVRQQSETGYPQAI 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 173 LITGESGAGKTENTKKVI-QYFALvaaslAGkkdkkeeekkkdekkGTLE----DQIVQCNPVLEAYGNAKTTRNNNSSR 247
Cdd:cd14881   72 ILSGTSGSGKTYASMLLLrQLFDV-----AG---------------GGPEtdafKHLAAAFTVLRSLGSAKTATNSESSR 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 248 FGKFIRIHFgTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAFPENIEKI-LAVPDPGLYGFINQGTLTVDG 326
Cdd:cd14881  132 IGHFIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLhLDGYSPANLRYLSHGDTRQNE 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 327 IDDEEEMGLTDTAFDVLG--FTDeeklsMYKCTGCILHLGEMKWKQRGE-QAEADGTAEAEKVAFLLGVNAGDLLKCLlk 403
Cdd:cd14881  211 AEDAARFQAWKACLGILGipFLD-----VVRVLAAVLLLGNVQFIDGGGlEVDVKGETELKSVAALLGVSGAALFRGL-- 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 404 pkikvgteyVTQGRN-KDQVTNSIA----------ALAKSLYDRMFNWLVRRVNQ------TLDTKAKRQFfIGVLDIAG 466
Cdd:cd14881  284 ---------TTRTHNaRGQLVKSVCdanmsnmtrdALAKALYCRTVATIVRRANSlkrlgsTLGTHATDGF-IGILDMFG 353
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 467 FEIFDFNSFEQLCINYTNERLQQFFNHHMFVLEQEEYKKEGIVWEF-IDFgLDLQACIELIEK-PMGILSILEEECMfPK 544
Cdd:cd14881  354 FEDPKPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLISSlRTGLLSMLDVECS-PR 431
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 545 ASDTSFKNKLYDNHLGkNPMFGKPKPPkagcAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELL--QNSkepivkm 622
Cdd:cd14881  432 GTAESYVAKIKVQHRQ-NPRLFEAKPQ----DDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFykQNC------- 499
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 623 lftppriltpggkkkkgkSAAFQTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGI 702
Cdd:cd14881  500 ------------------NFGFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETV 561
                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254839636 703 RICRKGFPNRIIYSEFKQRYSILAPNAVPSGfADGKVVTDKALSA-------LQLDPNE---YRLGNTKVFF 764
Cdd:cd14881  562 NLMAGGYPHRMRFKAFNARYRLLAPFRLLRR-VEEKALEDCALILqfleaqpPSKLSSVstsWALGKRHIFL 632
MYSc_Myo32 cd14893
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...
100-722 2.72e-67

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


Pssm-ID: 276858  Cd Length: 741  Bit Score: 237.95  E-value: 2.72e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 100 LHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRA----------EMPPHLFSIADNAYQYMLQDREN 169
Cdd:cd14893    4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQtplyekdtvnDAPPHVFALAQNALRCMQDAGED 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 170 QSMLITGESGAGKTENTKKVIQYFALVAASLAgkkdKKEEEKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFG 249
Cdd:cd14893   84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETE----PRPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 250 KFIRIHFGTQGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLS-----PAFPENIE--------KILAVPDPGLygf 316
Cdd:cd14893  160 KMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAgvqhdPTLRDSLEmnkcvnefVMLKQADPLA--- 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 317 inqGTLTVDGIDDEEEMgltdTAFDVLGFTDEEKLSMYKCTGCILHLGEMKWKQRGEQAEADGTAEAEKVAFLLGVNAGD 396
Cdd:cd14893  237 ---TNFALDARDYRDLM----SSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGANSTTVSDAQSCALKD 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 397 LLKCLLKPKIkVGTEYVT--------QGRNKDQ---------VTNSIAALA-----KSLYDRMFNWLVRRVNQTL----D 450
Cdd:cd14893  310 PAQILLAAKL-LEVEPVVldnyfrtrQFFSKDGnktvsslkvVTVHQARKArdtfvRSLYESLFNFLVETLNGILggifD 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 451 TKAKRQFFIG-----VLDIAGFEIFD--FNSFEQLCINYTNERLQQFFNHHMFV-----LEQEEYKKEG--IVWEFIDFG 516
Cdd:cd14893  389 RYEKSNIVINsqgvhVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrlTVNSNVDIT 468
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 517 LDLQACIELIE-KPMGILSILEEECMFPKASDTSFKNKLYDNH----------LGKNPMFGKPKPPKAGcaEAHFCLHHY 585
Cdd:cd14893  469 SEQEKCLQLFEdKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNeavgglsrpnMGADTTNEYLAPSKDW--RLLFIVQHH 546
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 586 AGSVSYSIAGWLDKNKDPINENVVELLQNSKEPIV------KMLFTPPRILTPGGKKKKGKSAAFQTISSVHKESLN--- 656
Cdd:cd14893  547 CGKVTYNGKGLSSKNMLSISSTCAAIMQSSKNAVLhavgaaQMAAASSEKAAKQTEERGSTSSKFRKSASSARESKNitd 626
                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254839636 657 -----------KLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRY 722
Cdd:cd14893  627 saatdvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY 703
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
119-254 4.88e-55

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 187.55  E-value: 4.88e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 119 FCIAINPYRRLPIYTQGLVDK-YRGKRRAEMPPHLFSIADNAYQYMLQDRENQSMLITGESGAGKTENTKKVIQYFALVA 197
Cdd:cd01363    1 VLVRVNPFKELPIYRDSKIIVfYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 254839636 198 ASlAGKKDKKEEEKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFGKFIRI 254
Cdd:cd01363   81 FN-GINKGETEGWVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
MYSc_Myo24B cd14938
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
98-763 2.46e-46

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


Pssm-ID: 276898 [Multi-domain]  Cd Length: 713  Bit Score: 177.34  E-value: 2.46e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636  98 SILHNLRSRYESGFIYTYSGLFCIAINPYRRLPIYTQGLVDKYRGKRRAE-MPPHLFSIADNAYQYMLQDRENQSMLITG 176
Cdd:cd14938    2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEdLSLNEYHVVHNALKNLNELKRNQSIIISG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 177 ESGAGKTENTKKVIQYFA-------LVAASLAGKKDKKEEEKKKDEKKGTLEDQIVQCNPVLEAYGNAKTTRNNNSSRFG 249
Cdd:cd14938   82 ESGSGKSEIAKNIINFIAyqvkgsrRLPTNLNDQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 250 KFIRIHFGTQgKIAGADIETYLLEKSRVTYQQSAERNYHIFYQLLSPAfPENIEKILAVPDPGLYGFINQGTLTVDGIDD 329
Cdd:cd14938  162 KFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGS-SDKFKKMYFLKNIENYSMLNNEKGFEKFSDY 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 330 EEEMGLTDTAFDVLGFTDEEKLSMYKCTGCILHLGEMK-----------WKQRGEQ--------------AEADGTAEAE 384
Cdd:cd14938  240 SGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEivkafrkksllMGKNQCGqninyetilselenSEDIGLDENV 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 385 KVAFL----LGVNAGDLLKCLLKPKIkVGTEYVTQGRNKDQVTNSIAALAKSLYDRMFNWLVRRVNQTLDTKAKRQFF-- 458
Cdd:cd14938  320 KNLLLacklLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNININtn 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 459 -IGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFVLEQEEYKKEGIVWEFIDFGLD-LQACIELIEKPMGILSIL 536
Cdd:cd14938  399 yINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDnEPLYNLLVGPTEGSLFSL 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 537 EEECMFPKASDTSFKNKLYDNHLGKNPMFGKPKPPKAgcAEAHFCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSK 616
Cdd:cd14938  479 LENVSTKTIFDKSNLHSSIIRKFSRNSKYIKKDDITG--NKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSE 556
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 617 EPIVKMLFTPPR---------------ILTPGGKKKKGKSAAFQTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTP 681
Cdd:cd14938  557 NEYMRQFCMFYNydnsgniveekrrysIQSALKLFKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESKRE 636
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 682 -GLIDAALVLHQLRCNGVLEGIRICRKGFPNRIIYSEFKQRYSILApnavpsgfADGKVVTDKALSALQLDPNEYRLGNT 760
Cdd:cd14938  637 lCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKN--------EDLKEKVEALIKSYQISNYEWMIGNN 708

                 ...
gi 254839636 761 KVF 763
Cdd:cd14938  709 MIF 711
MYSc_Myo33 cd14894
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...
103-706 5.91e-33

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


Pssm-ID: 276859 [Multi-domain]  Cd Length: 871  Bit Score: 136.80  E-value: 5.91e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 103 LRSRYESGFIYTYSGLFCIAI-NPYRRL------PIYTQGLVDKYRGKRRAE--MPPHLFSIADNAYQYMLQDREN---- 169
Cdd:cd14894    7 LTSRFDDDRIYTYINHHTMAVmNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKQSLVRLFFDNEHtmpl 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 170 ---------------QSMLITGESGAGKTENTKKVIQYFALVA-----------ASLAGKKDKKEEEKKKDEKKGT---- 219
Cdd:cd14894   87 pstissnrsmtegrgQSLFLCGESGSGKTELAKDLLKYLVLVAqpalskgseetCKVSGSTRQPKIKLFTSSTKSTiqmr 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 220 ------------------------------------------------------------LEDQ---------------- 223
Cdd:cd14894  167 teeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyeklehLEDEeqlrmyfknphaakkl 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 224 --IVQCNPVLEAYGNAKTTRNNNSSRFGKF--IRIHFGT---QGKIAGADIETYLLEKSRVTYQQSAER------NYHIF 290
Cdd:cd14894  247 siVLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLhpwEFQICGCHISPFLLEKSRVTSERGRESgdqnelNFHIL 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 291 YQLLS--PAFPenIEKILAvPDPGLYGfINQGTLTVDGIDDEEEMGLT---DT-------------AFDVLGFTDEEKLS 352
Cdd:cd14894  327 YAMVAgvNAFP--FMRLLA-KELHLDG-IDCSALTYLGRSDHKLAGFVskeDTwkkdverwqqvidGLDELNVSPDEQKT 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 353 MYKCTGCILHLGEMKWKQRGEQAE----ADGTAEA-EKVAFLLGVNAGDLLKCLLKPK---IKVGTEYVTQGRNKDQVTN 424
Cdd:cd14894  403 IFKVLSAVLWLGNIELDYREVSGKlvmsSTGALNApQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLEKGQVNH 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 425 SIAALAKSLYDRMFNWLVRRVNQTLDTKA------KRQF-----------FIGVLDIAGFEIFDFNSFEQLCINYTNERL 487
Cdd:cd14894  483 VRDTLARLLYQLAFNYVVFVMNEATKMSAlstdgnKHQMdsnasapeavsLLKIVDVFGFEDLTHNSLDQLCINYLSEKL 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 488 qqfFNHHMFVLEQEEYKKEGIVWEfiDFGLDLqacIELIEKPMGILSILEEECMFPKASDTSF-----KNKLYDNHLGKN 562
Cdd:cd14894  563 ---YAREEQVIAVAYSSRPHLTAR--DSEKDV---LFIYEHPLGVFASLEELTILHQSENMNAqqeekRNKLFVRNIYDR 634
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 563 PMFGKPKPPKA-GCAEAH---------FCLHHYAGSVSYSIAGWLDKNKDPINENVVELLQNSKEP-IVKMLFTPPRI-L 630
Cdd:cd14894  635 NSSRLPEPPRVlSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSShFCRMLNESSQLgW 714
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254839636 631 TPGGKKKKGKSA-----AFQTISSVHKESLNKLMKNLYSTHPHFVRCIIPNELKTPGLIDAALVLHQLRCNGVLEGIRIC 705
Cdd:cd14894  715 SPNTNRSMLGSAesrlsGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEIC 794

                 .
gi 254839636 706 R 706
Cdd:cd14894  795 R 795
Myosin_N pfam02736
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ...
29-74 2.13e-17

Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.


Pssm-ID: 426949  Cd Length: 45  Bit Score: 76.32  E-value: 2.13e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 254839636   29 DGKKNCWVPDPDFGFVGAEIQSTKGDEVTVKTDkTQETRVVKKDDI 74
Cdd:pfam02736   1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETE-DGKTVTVKKDDV 45
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
648-675 4.68e-08

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 53.50  E-value: 4.68e-08
                         10        20
                 ....*....|....*....|....*...
gi 254839636 648 SSVHKESLNKLMKNLYSTHPHFVRCIIP 675
Cdd:cd01363  143 FEIINESLNTLMNVLRATRPHFVRCISP 170
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
779-801 7.91e-05

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 40.00  E-value: 7.91e-05
                           10        20
                   ....*....|....*....|...
gi 254839636   779 RLSKIISMFQAHIRGYLMRKAYK 801
Cdd:smart00015   1 RLTRAAIIIQAAWRGYLARKRYK 23
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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