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Conserved domains on  [gi|1200169906]
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Chain A, Myosin-2 heavy chain,Dynamin-A

Protein Classification

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, ...
111-758 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: 1142.20  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITG 190
Cdd:cd01377      1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  191 ESGAGKTENTKKVIQYLASVAGRNQAN-----GSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFIS 265
Cdd:cd01377     81 ESGAGKTENTKKVIQYLASVAASSKKKkesgkKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  266 GASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDSEEFKITRQAMDIV 345
Cdd:cd01377    161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  346 GFSQEEQMSIFKIIAGILHLGNIKF-EKGAGEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEK 424
Cdd:cd01377    241 GFSEEEKMSIFKIVAAILHLGNIKFkQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  425 SSSSRDALVKALYGRLFLWLVKKINNVLCQERK-AYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQE 503
Cdd:cd01377    321 VVFSVGALAKALYERLFLWLVKRINKTLDTKSKrQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQE 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  504 EYLKEKINWTFIDFGLDSQATIDLIDgRQPPGILALLDEQSVFPNATDNTLITKLHSHFSKK--NAKYEEPRFSKTEFGV 581
Cdd:cd01377    401 EYKKEGIEWTFIDFGLDLQPTIDLIE-KPNMGILSILDEECVFPKATDKTFVEKLYSNHLGKskNFKKPKPKKSEAHFIL 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  582 THYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIAS-----RAKKGANFITVAAQYKEQLASLMATL 656
Cdd:cd01377    480 KHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGggggkKKKKGGSFRTVSQLHKEQLNKLMTTL 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  657 ETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPN-VPRDAEDSQKATD 735
Cdd:cd01377    560 RSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNaIPKGFDDGKAACE 639
                          650       660
                   ....*....|....*....|...
gi 1200169906  736 AVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd01377    640 KILKALQLDPELYRIGNTKVFFK 662
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
807-1080 2.16e-149

Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes interferon-induced Mx proteins that inhibit a wide range of viruses by blocking an early stage of the replication cycle. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


:

Pssm-ID: 206738  Cd Length: 278  Bit Score: 447.08  E-value: 2.16e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  807 LDLPQIVVVGSQSSGKSSVLENIVGRDFLPRGSGIVTRRPLILQLTHLPIADDGSQTQEWGEFLHKPNDMFYDFSEIREE 886
Cdd:cd08771      1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSPSESDEDEKEEWGEFLHLKSKEFTDFEELREE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  887 IIRDTDRMTGKNKGISAQPINLKIYSPHVVNLTLVDLPGITKVPVGDQPTDIEQQIRRMVMAYIKKQNAIIVAVTPANTD 966
Cdd:cd08771     81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  967 LANSDALQLAKEVDPEGKRTIGVITKLDLMDKGTDAMEVL---TGRVIPLTLGFIGVINRSQEDIIAKKSIRESLKSEIL 1043
Cdd:cd08771    161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1200169906 1044 YFKNHPIYKS-IANRSGTAYLSKTLNKLLMFHIRDTLP 1080
Cdd:cd08771    241 FFETHPWYKLlPASRVGTPALRKRLSKLLQKHIRESLP 278
Myosin_N pfam02736
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ...
41-87 1.56e-10

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: 460670  Cd Length: 45  Bit Score: 57.06  E-value: 1.56e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1200169906   41 SDKRYIWYnPDPKErdSYECGEIVSETSDSFTFKTVDGQDRQVKKDD 87
Cdd:pfam02736    1 DAKKLVWV-PDPKE--GFVKGEIKEEEGDKVTVETEDGKTVTVKKDD 44
 
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, ...
111-758 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: 1142.20  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITG 190
Cdd:cd01377      1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  191 ESGAGKTENTKKVIQYLASVAGRNQAN-----GSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFIS 265
Cdd:cd01377     81 ESGAGKTENTKKVIQYLASVAASSKKKkesgkKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  266 GASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDSEEFKITRQAMDIV 345
Cdd:cd01377    161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  346 GFSQEEQMSIFKIIAGILHLGNIKF-EKGAGEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEK 424
Cdd:cd01377    241 GFSEEEKMSIFKIVAAILHLGNIKFkQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  425 SSSSRDALVKALYGRLFLWLVKKINNVLCQERK-AYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQE 503
Cdd:cd01377    321 VVFSVGALAKALYERLFLWLVKRINKTLDTKSKrQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQE 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  504 EYLKEKINWTFIDFGLDSQATIDLIDgRQPPGILALLDEQSVFPNATDNTLITKLHSHFSKK--NAKYEEPRFSKTEFGV 581
Cdd:cd01377    401 EYKKEGIEWTFIDFGLDLQPTIDLIE-KPNMGILSILDEECVFPKATDKTFVEKLYSNHLGKskNFKKPKPKKSEAHFIL 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  582 THYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIAS-----RAKKGANFITVAAQYKEQLASLMATL 656
Cdd:cd01377    480 KHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGggggkKKKKGGSFRTVSQLHKEQLNKLMTTL 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  657 ETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPN-VPRDAEDSQKATD 735
Cdd:cd01377    560 RSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNaIPKGFDDGKAACE 639
                          650       660
                   ....*....|....*....|...
gi 1200169906  736 AVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd01377    640 KILKALQLDPELYRIGNTKVFFK 662
Myosin_head pfam00063
Myosin head (motor domain);
99-758 0e+00

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 1121.21  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   99 VEDMSELSYLNEPAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSML 178
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  179 DDRQNQSLLITGESGAGKTENTKKVIQYLASVAGRNQANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQF 258
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  259 NSAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDSEEFKIT 338
Cdd:pfam00063  161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKIT 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  339 RQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFEKGA-GEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVA 417
Cdd:pfam00063  241 DKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERnDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETVS 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  418 QHLNVEKSSSSRDALVKALYGRLFLWLVKKINNVLCQER--KAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNH 495
Cdd:pfam00063  321 KPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTieKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFNH 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  496 HMFKLEQEEYLKEKINWTFIDFGlDSQATIDLIDGRqPPGILALLDEQSVFPNATDNTLITKLHSHFSkKNAKYEEPRF- 574
Cdd:pfam00063  401 HMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK-PLGILSLLDEECLFPKATDQTFLDKLYSTFS-KHPHFQKPRLq 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  575 SKTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIAS------------RAKKGANFITVA 642
Cdd:pfam00063  478 GETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAEsaaanesgkstpKRTKKKRFITVG 557
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  643 AQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPN 722
Cdd:pfam00063  558 SQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPK 637
                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 1200169906  723 V-PRDAEDSQKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:pfam00063  638 TwPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
92-770 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: 1094.90  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906    92 NPIKFDGVEDMSELSYLNEPAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISD 171
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   172 VAYRSMLDDRQNQSLLITGESGAGKTENTKKVIQYLASVAGRNQANGSgvLEQQILQANPILEAFGNAKTTRNNNSSRFG 251
Cdd:smart00242   81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGS--VEDQILESNPILEAFGNAKTLRNNNSSRFG 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   252 KFIEIQFNSAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSD 331
Cdd:smart00242  159 KFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDD 238
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   332 SEEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFEKGAGEGA--VLKDKTALNAASTVFGVNPSVLEKALMEPRI 409
Cdd:smart00242  239 AEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAasTVKDKEELSNAAELLGVDPEELEKALTKRKI 318
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   410 LAGRDLVAQHLNVEKSSSSRDALVKALYGRLFLWLVKKINNVLC-QERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEK 488
Cdd:smart00242  319 KTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSfKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEK 398
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   489 LQQFFNHHMFKLEQEEYLKEKINWTFIDFGlDSQATIDLIDGrQPPGILALLDEQSVFPNATDNTLITKLHSHFSKKNAK 568
Cdd:smart00242  399 LQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEK-KPPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHF 476
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   569 YEEPRFSKTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFndPNIASRAKKGANFITVAAQYKEQ 648
Cdd:smart00242  477 SKPKKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLF--PSGVSNAGSKKRFQTVGSQFKEQ 554
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   649 LASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNV-PRDA 727
Cdd:smart00242  555 LNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTwPPWG 634
                           650       660       670       680
                    ....*....|....*....|....*....|....*....|...
gi 1200169906   728 EDSQKATDAVLKHLNIDPEQYRFGITKIFFRAGQLARIEEARE 770
Cdd:smart00242  635 GDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
COG5022 COG5022
Myosin heavy chain [General function prediction only];
42-778 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 918.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   42 DKRYIWyNPDPKERDSyecGEIVSETSDSFTFKTVDgqdRQVKKDDANQRNPIKFDGVEDMSELSYLNEPAVFHNLRVRY 121
Cdd:COG5022     18 EKGWIW-AEIIKEAFN---KGKVTEEGKKEDGESVS---VKKKVLGNDRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRY 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  122 NQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGESGAGKTENTK 201
Cdd:COG5022     91 NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAK 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  202 KVIQYLASVAGRNQAnGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASIQSYLLEKSRVVF 281
Cdd:COG5022    171 RIMQYLASVTSSSTV-EISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVH 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  282 QSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDSEEFKITRQAMDIVGFSQEEQMSIFKIIAG 361
Cdd:COG5022    250 QNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILAA 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  362 ILHLGNIKFEKGAGEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSSRDALVKALYGRLF 441
Cdd:COG5022    330 ILHIGNIEFKEDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLF 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  442 LWLVKKINNVLCQERKAY-FIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYLKEKINWTFIDFgLD 520
Cdd:COG5022    410 DWIVDRINKSLDHSAAASnFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY-FD 488
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  521 SQATIDLIDGRQPPGILALLDEQSVFPNATDNTLITKLHSHFSK-KNAKYEEPRFSKTEFGVTHYAGQVMYEIQDWLEKN 599
Cdd:COG5022    489 NQPCIDLIEKKNPLGILSLLDEECVMPHATDESFTSKLAQRLNKnSNPKFKKSRFRDNKFVVKHYAGDVEYDVEGFLDKN 568
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  600 KDPLQQDLELCFKDSSDNVVTKLFND-PNIASRAKkganFITVAAQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKL 678
Cdd:COG5022    569 KDPLNDDLLELLKASTNEFVSTLFDDeENIESKGR----FPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTF 644
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  679 EDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPN-----VPRDAEDSQKATDAVLKHLNIDPEQYRFGIT 753
Cdd:COG5022    645 DNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSkswtgEYTWKEDTKNAVKSILEELVIDSSKYQIGNT 724
                          730       740
                   ....*....|....*....|....*
gi 1200169906  754 KIFFRAGQLARIEEAREQRISEITR 778
Cdd:COG5022    725 KVFFKAGVLAALEDMRDAKLDNIAT 749
PTZ00014 PTZ00014
myosin-A; Provisional
55-756 7.98e-156

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 483.76  E-value: 7.98e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   55 RDSYECGEIVSETSDSFTfktvdgqdrqVKKDDA-NQRNPIKFDGVEDMSELSYLNEPAVFHNLRVRYNQDLIYTYSGLF 133
Cdd:PTZ00014    63 GEKLTLKQIDPPTNSTFE----------VKPEHAfNANSQIDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPL 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  134 LVAVNPFKRIPIYTQEMVDIFK-GRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGESGAGKTENTKKVIQYLASVAG 212
Cdd:PTZ00014   133 LVAINPFKDLGNTTNDWIRRYRdAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASSKS 212
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  213 RNqanGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASIQSYLLEKSRVVFQSETERNYHIF 292
Cdd:PTZ00014   213 GN---MDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIF 289
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  293 YQLLAGATAEEKKALHLAGPESFNYLNqSGCVDIKGVSDSEEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFEK 372
Cdd:PTZ00014   290 YQLLKGANDEMKEKYKLKSLEEYKYIN-PKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEG 368
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  373 ----GAGEGAVL--KDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSSRDALVKALYGRLFLWLVK 446
Cdd:PTZ00014   369 keegGLTDAAAIsdESLEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIR 448
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  447 KINNVLCQERK-AYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYLKE-----KINWTfidfglD 520
Cdd:PTZ00014   449 NLNATIEPPGGfKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEgisteELEYT------S 522
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  521 SQATIDLIDGRQpPGILALLDEQSVFPNATDNTLITKLHSHFsKKNAKYEEPRFSKT-EFGVTHYAGQVMYEIQDWLEKN 599
Cdd:PTZ00014   523 NESVIDLLCGKG-KSVLSILEDQCLAPGGTDEKFVSSCNTNL-KNNPKYKPAKVDSNkNFVIKHTIGDIQYCASGFLFKN 600
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  600 KDPLQQDLELCFKDSSDNVVTKLFNDPNI-ASRAKKGaNFITvaAQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKL 678
Cdd:PTZ00014   601 KDVLRPELVEVVKASPNPLVRDLFEGVEVeKGKLAKG-QLIG--SQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDW 677
                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1200169906  679 EDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAE-DSQKATDAVLKHLNIDPEQYRFGITKIF 756
Cdd:PTZ00014   678 NSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSlDPKEKAEKLLERSGLPKDSYAIGKTMVF 756
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
807-1080 2.16e-149

Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes interferon-induced Mx proteins that inhibit a wide range of viruses by blocking an early stage of the replication cycle. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206738  Cd Length: 278  Bit Score: 447.08  E-value: 2.16e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  807 LDLPQIVVVGSQSSGKSSVLENIVGRDFLPRGSGIVTRRPLILQLTHLPIADDGSQTQEWGEFLHKPNDMFYDFSEIREE 886
Cdd:cd08771      1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSPSESDEDEKEEWGEFLHLKSKEFTDFEELREE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  887 IIRDTDRMTGKNKGISAQPINLKIYSPHVVNLTLVDLPGITKVPVGDQPTDIEQQIRRMVMAYIKKQNAIIVAVTPANTD 966
Cdd:cd08771     81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  967 LANSDALQLAKEVDPEGKRTIGVITKLDLMDKGTDAMEVL---TGRVIPLTLGFIGVINRSQEDIIAKKSIRESLKSEIL 1043
Cdd:cd08771    161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1200169906 1044 YFKNHPIYKS-IANRSGTAYLSKTLNKLLMFHIRDTLP 1080
Cdd:cd08771    241 FFETHPWYKLlPASRVGTPALRKRLSKLLQKHIRESLP 278
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
786-1028 1.95e-114

Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the endocytic uptake of receptors, associated ligands, and plasma membrane following an exocytic event.


Pssm-ID: 197491  Cd Length: 240  Bit Score: 354.19  E-value: 1.95e-114
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   786 DQLIPVINKLQDVFNTLG-SDPLDLPQIVVVGSQSSGKSSVLENIVGRDFLPRGSGIVTRRPLILQLThlpiaddgSQTQ 864
Cdd:smart00053    2 EELIPLVNKLQDAFSALGqSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLI--------KSKT 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   865 EWGEFLHKPNDMFYDFSEIREEIIRDTDRMTGKNKGISAQPINLKIYSPHVVNLTLVDLPGITKVPVGDQPTDIEQQIRR 944
Cdd:smart00053   74 EYAEFLHCKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKK 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   945 MVMAYIKKQNAIIVAVTPANTDLANSDALQLAKEVDPEGKRTIGVITKLDLMDKGTDAMEVLTGRVIPLTLGFIGVINRS 1024
Cdd:smart00053  154 MIKQFISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRS 233

                    ....
gi 1200169906  1025 QEDI 1028
Cdd:smart00053  234 QKDI 237
Dynamin_N pfam00350
Dynamin family;
812-993 3.50e-70

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 231.35  E-value: 3.50e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  812 IVVVGSQSSGKSSVLENIVGRDFLPRGSGIVTRRPLILQLTHLPIADDGSQTQEWGEFlhkpNDMFYDFSEIREEIIRDT 891
Cdd:pfam00350    1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESPGASEGAVKVEYKDG----EKKFEDFSELREEIEKET 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  892 DRMTGKNKGISAQPINLKIYSPHVVNLTLVDLPGITKVPVGDQptdieqqirRMVMAYIKKqNAIIVAVTPANTDLANSD 971
Cdd:pfam00350   77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYIKP-ADIILAVTPANVDLSTSE 146
                          170       180
                   ....*....|....*....|..
gi 1200169906  972 ALQLAKEVDPEGKRTIGVITKL 993
Cdd:pfam00350  147 ALFLAREVDPNGKRTIGVLTKA 168
Myosin_N pfam02736
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ...
41-87 1.56e-10

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: 460670  Cd Length: 45  Bit Score: 57.06  E-value: 1.56e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1200169906   41 SDKRYIWYnPDPKErdSYECGEIVSETSDSFTFKTVDGQDRQVKKDD 87
Cdd:pfam02736    1 DAKKLVWV-PDPKE--GFVKGEIKEEEGDKVTVETEDGKTVTVKKDD 44
 
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, ...
111-758 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: 1142.20  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITG 190
Cdd:cd01377      1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  191 ESGAGKTENTKKVIQYLASVAGRNQAN-----GSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFIS 265
Cdd:cd01377     81 ESGAGKTENTKKVIQYLASVAASSKKKkesgkKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  266 GASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDSEEFKITRQAMDIV 345
Cdd:cd01377    161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  346 GFSQEEQMSIFKIIAGILHLGNIKF-EKGAGEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEK 424
Cdd:cd01377    241 GFSEEEKMSIFKIVAAILHLGNIKFkQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  425 SSSSRDALVKALYGRLFLWLVKKINNVLCQERK-AYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQE 503
Cdd:cd01377    321 VVFSVGALAKALYERLFLWLVKRINKTLDTKSKrQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQE 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  504 EYLKEKINWTFIDFGLDSQATIDLIDgRQPPGILALLDEQSVFPNATDNTLITKLHSHFSKK--NAKYEEPRFSKTEFGV 581
Cdd:cd01377    401 EYKKEGIEWTFIDFGLDLQPTIDLIE-KPNMGILSILDEECVFPKATDKTFVEKLYSNHLGKskNFKKPKPKKSEAHFIL 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  582 THYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIAS-----RAKKGANFITVAAQYKEQLASLMATL 656
Cdd:cd01377    480 KHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGggggkKKKKGGSFRTVSQLHKEQLNKLMTTL 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  657 ETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPN-VPRDAEDSQKATD 735
Cdd:cd01377    560 RSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNaIPKGFDDGKAACE 639
                          650       660
                   ....*....|....*....|...
gi 1200169906  736 AVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd01377    640 KILKALQLDPELYRIGNTKVFFK 662
Myosin_head pfam00063
Myosin head (motor domain);
99-758 0e+00

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 1121.21  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   99 VEDMSELSYLNEPAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSML 178
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  179 DDRQNQSLLITGESGAGKTENTKKVIQYLASVAGRNQANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQF 258
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  259 NSAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDSEEFKIT 338
Cdd:pfam00063  161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKIT 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  339 RQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFEKGA-GEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVA 417
Cdd:pfam00063  241 DKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERnDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETVS 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  418 QHLNVEKSSSSRDALVKALYGRLFLWLVKKINNVLCQER--KAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNH 495
Cdd:pfam00063  321 KPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTieKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFNH 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  496 HMFKLEQEEYLKEKINWTFIDFGlDSQATIDLIDGRqPPGILALLDEQSVFPNATDNTLITKLHSHFSkKNAKYEEPRF- 574
Cdd:pfam00063  401 HMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK-PLGILSLLDEECLFPKATDQTFLDKLYSTFS-KHPHFQKPRLq 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  575 SKTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIAS------------RAKKGANFITVA 642
Cdd:pfam00063  478 GETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAEsaaanesgkstpKRTKKKRFITVG 557
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  643 AQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPN 722
Cdd:pfam00063  558 SQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPK 637
                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 1200169906  723 V-PRDAEDSQKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:pfam00063  638 TwPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
92-770 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: 1094.90  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906    92 NPIKFDGVEDMSELSYLNEPAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISD 171
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   172 VAYRSMLDDRQNQSLLITGESGAGKTENTKKVIQYLASVAGRNQANGSgvLEQQILQANPILEAFGNAKTTRNNNSSRFG 251
Cdd:smart00242   81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGS--VEDQILESNPILEAFGNAKTLRNNNSSRFG 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   252 KFIEIQFNSAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSD 331
Cdd:smart00242  159 KFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDD 238
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   332 SEEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFEKGAGEGA--VLKDKTALNAASTVFGVNPSVLEKALMEPRI 409
Cdd:smart00242  239 AEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAasTVKDKEELSNAAELLGVDPEELEKALTKRKI 318
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   410 LAGRDLVAQHLNVEKSSSSRDALVKALYGRLFLWLVKKINNVLC-QERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEK 488
Cdd:smart00242  319 KTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSfKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEK 398
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   489 LQQFFNHHMFKLEQEEYLKEKINWTFIDFGlDSQATIDLIDGrQPPGILALLDEQSVFPNATDNTLITKLHSHFSKKNAK 568
Cdd:smart00242  399 LQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEK-KPPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHF 476
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   569 YEEPRFSKTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFndPNIASRAKKGANFITVAAQYKEQ 648
Cdd:smart00242  477 SKPKKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLF--PSGVSNAGSKKRFQTVGSQFKEQ 554
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   649 LASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNV-PRDA 727
Cdd:smart00242  555 LNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTwPPWG 634
                           650       660       670       680
                    ....*....|....*....|....*....|....*....|...
gi 1200169906   728 EDSQKATDAVLKHLNIDPEQYRFGITKIFFRAGQLARIEEARE 770
Cdd:smart00242  635 GDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
COG5022 COG5022
Myosin heavy chain [General function prediction only];
42-778 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 918.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   42 DKRYIWyNPDPKERDSyecGEIVSETSDSFTFKTVDgqdRQVKKDDANQRNPIKFDGVEDMSELSYLNEPAVFHNLRVRY 121
Cdd:COG5022     18 EKGWIW-AEIIKEAFN---KGKVTEEGKKEDGESVS---VKKKVLGNDRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRY 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  122 NQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGESGAGKTENTK 201
Cdd:COG5022     91 NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAK 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  202 KVIQYLASVAGRNQAnGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASIQSYLLEKSRVVF 281
Cdd:COG5022    171 RIMQYLASVTSSSTV-EISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVH 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  282 QSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDSEEFKITRQAMDIVGFSQEEQMSIFKIIAG 361
Cdd:COG5022    250 QNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILAA 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  362 ILHLGNIKFEKGAGEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSSRDALVKALYGRLF 441
Cdd:COG5022    330 ILHIGNIEFKEDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLF 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  442 LWLVKKINNVLCQERKAY-FIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYLKEKINWTFIDFgLD 520
Cdd:COG5022    410 DWIVDRINKSLDHSAAASnFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY-FD 488
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  521 SQATIDLIDGRQPPGILALLDEQSVFPNATDNTLITKLHSHFSK-KNAKYEEPRFSKTEFGVTHYAGQVMYEIQDWLEKN 599
Cdd:COG5022    489 NQPCIDLIEKKNPLGILSLLDEECVMPHATDESFTSKLAQRLNKnSNPKFKKSRFRDNKFVVKHYAGDVEYDVEGFLDKN 568
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  600 KDPLQQDLELCFKDSSDNVVTKLFND-PNIASRAKkganFITVAAQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKL 678
Cdd:COG5022    569 KDPLNDDLLELLKASTNEFVSTLFDDeENIESKGR----FPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTF 644
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  679 EDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPN-----VPRDAEDSQKATDAVLKHLNIDPEQYRFGIT 753
Cdd:COG5022    645 DNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSkswtgEYTWKEDTKNAVKSILEELVIDSSKYQIGNT 724
                          730       740
                   ....*....|....*....|....*
gi 1200169906  754 KIFFRAGQLARIEEAREQRISEITR 778
Cdd:COG5022    725 KVFFKAGVLAALEDMRDAKLDNIAT 749
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
111-758 0e+00

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


Pssm-ID: 276950 [Multi-domain]  Cd Length: 633  Bit Score: 906.20  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRN-EVAPHIFAISDVAYRSMLDDRQNQSLLIT 189
Cdd:cd00124      1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  190 GESGAGKTENTKKVIQYLASVAGRNQANGSGV---LEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISG 266
Cdd:cd00124     81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSassIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  267 ASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLA----GPESFNYLNQSGCVDIKGVSDSEEFKITRQAM 342
Cdd:cd00124    161 ASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLElllsYYYLNDYLNSSGCDRIDGVDDAEEFQELLDAL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  343 DIVGFSQEEQMSIFKIIAGILHLGNIKFEKGAGEG---AVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQH 419
Cdd:cd00124    241 DVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdssAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITKP 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  420 LNVEKSSSSRDALVKALYGRLFLWLVKKINNVLC---QERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHH 496
Cdd:cd00124    321 LTVEQAEDARDALAKALYSRLFDWLVNRINAALSptdAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQH 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  497 MFKLEQEEYLKEKINWTFIDFgLDSQATIDLIDGRqPPGILALLDEQSVFPNATDNTLITKLHSHFSKKNAKYEEPRFSK 576
Cdd:cd00124    401 VFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK-PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKAK 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  577 TEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSdnvvtklfndpniasrakkganfitvaaQYKEQLASLMATL 656
Cdd:cd00124    479 LEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS----------------------------QFRSQLDALMDTL 530
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  657 ETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAEDSQK-ATD 735
Cdd:cd00124    531 NSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEKASDSKKaAVL 610
                          650       660
                   ....*....|....*....|...
gi 1200169906  736 AVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd00124    611 ALLLLLKLDSSGYQLGKTKVFLR 633
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
111-758 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: 819.86  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRY-NQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLIT 189
Cdd:cd01380      1 PAVLHNLKVRFcQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  190 GESGAGKTENTKKVIQYLASVAGrnQANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASI 269
Cdd:cd01380     81 GESGAGKTVSAKYAMRYFATVGG--SSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANM 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  270 QSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDSEEFKITRQAMDIVGFSQ 349
Cdd:cd01380    159 RTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  350 EEQMSIFKIIAGILHLGNIKFEKGAGEGAVLKDK-TALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSS 428
Cdd:cd01380    239 EEQMEIFRILAAILHLGNVEIKATRNDSASISPDdEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVA 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  429 RDALVKALYGRLFLWLVKKINNVLCQERKA---YFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEY 505
Cdd:cd01380    319 RDALAKHIYAQLFDWIVDRINKALASPVKEkqhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEY 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  506 LKEKINWTFIDFgLDSQATIDLIDGRqpPGILALLDEQSVFPNATDNTLITKLHSHFSKKNAK-YEEPRFSKTEFGVTHY 584
Cdd:cd01380    399 VKEEIEWSFIDF-YDNQPCIDLIEGK--LGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNKhFKKPRFSNTAFIVKHF 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  585 AGQVMYEIQDWLEKNKDPLQQDLELCFKdSSDNvvtklfndpniasrAKKganfiTVAAQYKEQLASLMATLETTNPHFV 664
Cdd:cd01380    476 ADDVEYQVEGFLEKNRDTVSEEHLNVLK-ASKN--------------RKK-----TVGSQFRDSLILLMETLNSTTPHYV 535
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  665 RCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAEDSQKATDAVLKHLNID 744
Cdd:cd01380    536 RCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLRDDKKKTCENILENLILD 615
                          650
                   ....*....|....
gi 1200169906  745 PEQYRFGITKIFFR 758
Cdd:cd01380    616 PDKYQFGKTKIFFR 629
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
111-758 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: 815.76  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIP-IYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLIT 189
Cdd:cd01384      1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  190 GESGAGKTENTKKVIQYLASVAGRNQANGSGVlEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASI 269
Cdd:cd01384     81 GESGAGKTETTKMLMQYLAYMGGRAVTEGRSV-EQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAI 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  270 QSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDSEEFKITRQAMDIVGFSQ 349
Cdd:cd01384    160 RTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  350 EEQMSIFKIIAGILHLGNIKFEKGAG-EGAVLKD---KTALNAASTVFGVNPSVLEKALMEpRILAGRD-LVAQHLNVEK 424
Cdd:cd01384    240 EEQDAIFRVVAAILHLGNIEFSKGEEdDSSVPKDeksEFHLKAAAELLMCDEKALEDALCK-RVIVTPDgIITKPLDPDA 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  425 SSSSRDALVKALYGRLFLWLVKKINNVLCQ-ERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQE 503
Cdd:cd01384    319 ATLSRDALAKTIYSRLFDWLVDKINRSIGQdPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQE 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  504 EYLKEKINWTFIDFgLDSQATIDLIDGRqPPGILALLDEQSVFPNATDNTLITKLHSHFsKKNAKYEEPRFSKTEFGVTH 583
Cdd:cd01384    399 EYTKEEIDWSYIEF-VDNQDVLDLIEKK-PGGIIALLDEACMFPRSTHETFAQKLYQTL-KDHKRFSKPKLSRTDFTIDH 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  584 YAGQVMYEIQDWLEKNKD---PLQQDLelcFKDSSDNVVTKLFnDPNIASRAKKGANFITVAAQYKEQLASLMATLETTN 660
Cdd:cd01384    476 YAGDVTYQTDLFLDKNKDyvvAEHQAL---LNASKCPFVAGLF-PPLPREGTSSSSKFSSIGSRFKQQLQELMETLNTTE 551
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  661 PHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAEDSQKATDAVLKH 740
Cdd:cd01384    552 PHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVLKGSDDEKAACKKILEK 631
                          650
                   ....*....|....*...
gi 1200169906  741 LNIdpEQYRFGITKIFFR 758
Cdd:cd01384    632 AGL--KGYQIGKTKVFLR 647
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
116-758 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: 783.82  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  116 NLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGESGAG 195
Cdd:cd14883      6 NLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGESGAG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  196 KTENTKKVIQYLASVAgrnqaNGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASIQSYLLE 275
Cdd:cd14883     86 KTETTKLILQYLCAVT-----NNHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYLLE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  276 KSRVVFQSETERNYHIFYQLLAGATA--EEKKALHLAGPESFNYLNQSGCVDIKGVSDSEEFKITRQAMDIVGFSQEEQM 353
Cdd:cd14883    161 QSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPEEMQE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  354 SIFKIIAGILHLGNIKFEKGAGEGAVL--KDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSSRDA 431
Cdd:cd14883    241 GIFSVLSAILHLGNLTFEDIDGETGALtvEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDNRDA 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  432 LVKALYGRLFLWLVKKINNVLCQERKAY-FIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYLKEKI 510
Cdd:cd14883    321 MAKALYSRTFAWLVNHINSCTNPGQKNSrFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKEGI 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  511 NWTFIDFGlDSQATIDLIDGRqPPGILALLDEQSVFPNATDNTLITKLHSHFSkKNAKYEEP--RFSKTEFGVTHYAGQV 588
Cdd:cd14883    401 NWSHIVFT-DNQECLDLIEKP-PLGILKLLDEECRFPKGTDLTYLEKLHAAHE-KHPYYEKPdrRRWKTEFGVKHYAGEV 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  589 MYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIAS---------------RAKKGANfiTVAAQYKEQLASLM 653
Cdd:cd14883    478 TYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDLLAltglsislggdttsrGTSKGKP--TVGDTFKHQLQSLV 555
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  654 ATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNvPRDAEDSQK- 732
Cdd:cd14883    556 DVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPR-ARSADHKETc 634
                          650       660
                   ....*....|....*....|....*..
gi 1200169906  733 -ATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14883    635 gAVRALMGLGGLPEDEWQVGKTKVFLR 661
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
111-758 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: 778.42  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFkgRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITG 190
Cdd:cd01383      1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAY--RQKLLDSPHVYAVADTAYREMMRDEINQSIIISG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  191 ESGAGKTENTKKVIQYLASVAGrnqanGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASIQ 270
Cdd:cd01383     79 ESGAGKTETAKIAMQYLAALGG-----GSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQ 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  271 SYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDSEEFKITRQAMDIVGFSQE 350
Cdd:cd01383    154 TYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  351 EQMSIFKIIAGILHLGNIKFEKGAGEGAV-LKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSSR 429
Cdd:cd01383    234 DQEHIFQMLAAVLWLGNISFQVIDNENHVeVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDAR 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  430 DALVKALYGRLFLWLVKKINNVLC--QERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYLK 507
Cdd:cd01383    314 DALAKAIYASLFDWLVEQINKSLEvgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYEL 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  508 EKINWTFIDFgLDSQATIDLIDgRQPPGILALLDEQSVFPNATDNTLITKLHSHFSKKNAKYEEprfSKTEFGVTHYAGQ 587
Cdd:cd01383    394 DGIDWTKVDF-EDNQECLDLIE-KKPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGE---RGGAFTIRHYAGE 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  588 VMYEIQDWLEKNKDPLQQDLeLCFKDSSDNVVTKLFN---------DPNIASRAKKGANFITVAAQYKEQLASLMATLET 658
Cdd:cd01383    469 VTYDTSGFLEKNRDLLHSDL-IQLLSSCSCQLPQLFAskmldasrkALPLTKASGSDSQKQSVATKFKGQLFKLMQRLEN 547
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  659 TNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAEDSQKATDAVL 738
Cdd:cd01383    548 TTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQDPLSTSVAIL 627
                          650       660
                   ....*....|....*....|
gi 1200169906  739 KHLNIDPEQYRFGITKIFFR 758
Cdd:cd01383    628 QQFNILPEMYQVGYTKLFFR 647
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
112-758 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: 755.28  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  112 AVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGE 191
Cdd:cd14911      2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  192 SGAGKTENTKKVIQYLASVA-------------GRNQANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQF 258
Cdd:cd14911     82 SGAGKTENTKKVIQFLAYVAaskpkgsgavphpAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  259 NSAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNqSGCVDIKGVSDSEEFKIT 338
Cdd:cd14911    162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLS-NGSLPVPGVDDYAEFQAT 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  339 RQAMDIVGFSQEEQMSIFKIIAGILHLGNIKF-EKGAGEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVA 417
Cdd:cd14911    241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFrQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  418 QHLNVEKSSSSRDALVKALYGRLFLWLVKKINNVLCQERK--AYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNH 495
Cdd:cd14911    321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRqgASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  496 HMFKLEQEEYLKEKINWTFIDFGLDSQATIDLIDgrQPPGILALLDEQSVFPNATDNTLITKLHShfskknAKYEEPRFS 575
Cdd:cd14911    401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLID--KPGGIMALLDEECWFPKATDKTFVDKLVS------AHSMHPKFM 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  576 KT------EFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNI-------------ASRAKKGA 636
Cdd:cd14911    473 KTdfrgvaDFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIvgmaqqaltdtqfGARTRKGM 552
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  637 nFITVAAQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRY 716
Cdd:cd14911    553 -FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 631
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|...
gi 1200169906  717 YLLAPNV-PRDAEDSQKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14911    632 ELLTPNViPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
112-758 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: 747.99  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  112 AVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGE 191
Cdd:cd14920      2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  192 SGAGKTENTKKVIQYLASVA----GRNQANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGA 267
Cdd:cd14920     82 SGAGKTENTKKVIQYLAHVAsshkGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  268 SIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNqSGCVDIKGVSDSEEFKITRQAMDIVGF 347
Cdd:cd14920    162 NIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIMGF 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  348 SQEEQMSIFKIIAGILHLGNIKFEKGAG-EGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSS 426
Cdd:cd14920    241 SHEEILSMLKVVSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  427 SSRDALVKALYGRLFLWLVKKINNVL--CQERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEE 504
Cdd:cd14920    321 FAVEALAKATYERLFRWLVHRINKALdrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  505 YLKEKINWTFIDFGLDSQATIDLID-GRQPPGILALLDEQSVFPNATDNTLITKL------HSHFSKKnakyEEPRfSKT 577
Cdd:cd14920    401 YQREGIEWNFIDFGLDLQPCIDLIErPANPPGVLALLDEECWFPKATDKTFVEKLvqeqgsHSKFQKP----RQLK-DKA 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  578 EFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPN-----------------IASRAKKGAnFIT 640
Cdd:cd14920    476 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgldqvtgmtetafgSAYKTKKGM-FRT 554
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  641 VAAQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLA 720
Cdd:cd14920    555 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 634
                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 1200169906  721 PN-VPRDAEDSQKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14920    635 PNaIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
116-758 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: 745.14  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  116 NLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGESGAG 195
Cdd:cd01378      6 NLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGESGAG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  196 KTENTKKVIQYLASVAGRNQANGSGVLEQqILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASIQSYLLE 275
Cdd:cd01378     86 KTEASKRIMQYIAAVSGGSESEVERVKDM-LLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYLLE 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  276 KSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDSEEFKITRQAMDIVGFSQEEQMSI 355
Cdd:cd01378    165 KSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEEQDSI 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  356 FKIIAGILHLGNIKFEKGAGEGAVLKDKTALNAASTVFGVNPSVLEKALMEpRILA----GRDLVAQHLNVEKSSSSRDA 431
Cdd:cd01378    245 FRILAAILHLGNIQFAEDEEGNAAISDTSVLDFVAYLLGVDPDQLEKALTH-RTIEtgggGRSVYEVPLNVEQAAYARDA 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  432 LVKALYGRLFLWLVKKINNVL--CQERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYLKEK 509
Cdd:cd01378    324 LAKAIYSRLFDWIVERINKSLaaKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQEEYVREG 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  510 INWTFIDFgLDSQATIDLIDGRqPPGILALLDEQSVFP-NATDNTLITKLHSHFSkKNAKYEEPRFSKT----EFGVTHY 584
Cdd:cd01378    404 IEWTPIKY-FNNKIICDLIEEK-PPGIFAILDDACLTAgDATDQTFLQKLNQLFS-NHPHFECPSGHFElrrgEFRIKHY 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  585 AGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIASRAKKGanfITVAAQYKEQLASLMATLETTNPHFV 664
Cdd:cd01378    481 AGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDSKKRP---PTAGTKFKNSANALVETLMKKQPSYI 557
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  665 RCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNV-PRDAEDSQKATDAVLKHLNI 743
Cdd:cd01378    558 RCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTwPAWDGTWQGGVESILKDLNI 637
                          650
                   ....*....|....*
gi 1200169906  744 DPEQYRFGITKIFFR 758
Cdd:cd01378    638 PPEEYQMGKTKIFIR 652
MYSc_Myh1_insects_crustaceans cd14909
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
111-758 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: 742.43  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITG 190
Cdd:cd14909      1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  191 ESGAGKTENTKKVIQYLASVAGRNQ----ANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISG 266
Cdd:cd14909     81 ESGAGKTENTKKVIAYFATVGASKKtdeaAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  267 ASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDSEEFKITRQAMDIVG 346
Cdd:cd14909    161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  347 FSQEEQMSIFKIIAGILHLGNIKF-EKGAGEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKS 425
Cdd:cd14909    241 FTKQEKEDVYRITAAVMHMGGMKFkQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  426 SSSRDALVKALYGRLFLWLVKKINNVL-CQERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEE 504
Cdd:cd14909    321 TNSIGALCKGVFDRLFKWLVKKCNETLdTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEE 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  505 YLKEKINWTFIDFGLDSQATIDLIDgrQPPGILALLDEQSVFPNATDNTLITKLHSHFSKKNAKYEEPRFSK-----TEF 579
Cdd:cd14909    401 YKREGIDWAFIDFGMDLLACIDLIE--KPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpgqqaAHF 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  580 GVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIAS---------RAKKGANFITVAAQYKEQLA 650
Cdd:cd14909    479 AIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSgggeqakggRGKKGGGFATVSSAYKEQLN 558
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  651 SLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAEDS 730
Cdd:cd14909    559 SLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEEDP 638
                          650       660
                   ....*....|....*....|....*...
gi 1200169906  731 QKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14909    639 KKAAEIILESIALDPDQYRLGHTKVFFR 666
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
112-758 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: 735.21  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  112 AVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGE 191
Cdd:cd01381      2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  192 SGAGKTENTKKVIQYLASVAGRNQAngsgvLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASIQS 271
Cdd:cd01381     82 SGAGKTESTKLILQYLAAISGQHSW-----IEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQ 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  272 YLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDSEEFKITRQAMDIVGFSQEE 351
Cdd:cd01381    157 YLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEE 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  352 QMSIFKIIAGILHLGNIKFEKGAG---EGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSS 428
Cdd:cd01381    237 IWDIFKLLAAILHLGNIKFEATVVdnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDV 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  429 RDALVKALYGRLFLWLVKKINNVLCQERKA----YFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEE 504
Cdd:cd01381    317 RDAFVKGIYGRLFIWIVNKINSAIYKPRGTdssrTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEE 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  505 YLKEKINWTFIDFgLDSQATIDLIdGRQPPGILALLDEQSVFPNATDNTLITKLHSHfSKKNAKYEEPRF-SKTEFGVTH 583
Cdd:cd01381    397 YDKEGINWQHIEF-VDNQDVLDLI-ALKPMNIMSLIDEESKFPKGTDQTMLEKLHST-HGNNKNYLKPKSdLNTSFGINH 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  584 YAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFND--PNIASRAKKGanfITVAAQYKEQLASLMATLETTNP 661
Cdd:cd01381    474 FAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEdiSMGSETRKKS---PTLSSQFRKSLDQLMKTLSACQP 550
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  662 HFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPR-----DAEDSQKATDA 736
Cdd:cd01381    551 FFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPahktdCRAATRKICCA 630
                          650       660
                   ....*....|....*....|..
gi 1200169906  737 VLKHlnidPEQYRFGITKIFFR 758
Cdd:cd01381    631 VLGG----DADYQLGKTKIFLK 648
MYSc_Myh7b cd14927
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...
112-758 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: 726.36  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  112 AVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGE 191
Cdd:cd14927      2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  192 SGAGKTENTKKVIQYLASVAGRNQANG----------SGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSA 261
Cdd:cd14927     82 SGAGKTVNTKRVIQYFAIVAALGDGPGkkaqflatktGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  262 GFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLA-GPESFNYLNQsGCVDIKGVSDSEEFKITRQ 340
Cdd:cd14927    162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSmNPYDYHFCSQ-GVTTVDNMDDGEELMATDH 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  341 AMDIVGFSQEEQMSIFKIIAGILHLGNIKFEKGAGEGAVLKDKT-ALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQH 419
Cdd:cd14927    241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTeSADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  420 LNVEKSSSSRDALVKALYGRLFLWLVKKINNVLCQE-RKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMF 498
Cdd:cd14927    321 QSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKlPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  499 KLEQEEYLKEKINWTFIDFGLDSQATIDLIDgrQPPGILALLDEQSVFPNATDNTLITKLHSHFSKKNAKYEEPRFSK-- 576
Cdd:cd14927    401 ILEQEEYKREGIEWVFIDFGLDLQACIDLIE--KPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKkr 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  577 ---TEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLF---------NDPN--IASRAKKGANFITVA 642
Cdd:cd14927    479 kyeAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYenyvgsdstEDPKsgVKEKRKKAASFQTVS 558
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  643 AQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPN 722
Cdd:cd14927    559 QLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPS 638
                          650       660       670
                   ....*....|....*....|....*....|....*...
gi 1200169906  723 -VPRDA-EDSQKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14927    639 aIPDDKfVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
MYSc_Myh15_mammals cd14929
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...
111-758 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: 704.81  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITG 190
Cdd:cd14929      1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  191 ESGAGKTENTKKVIQYLASVAGRNQANGS-GVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASI 269
Cdd:cd14929     81 ESGAGKTVNTKHIIQYFATIAAMIESKKKlGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  270 QSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNqSGCVDIKGVSDSEEFKITRQAMDIVGFSQ 349
Cdd:cd14929    161 DIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCS-CGAVAVESLDDAEELLATEQAMDILGFLP 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  350 EEQMSIFKIIAGILHLGNIKFEKGAGEGAVLKDKTAlNA--ASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSS 427
Cdd:cd14929    240 DEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTE-NAdkAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVTY 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  428 SRDALVKALYGRLFLWLVKKINNVL-CQERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYL 506
Cdd:cd14929    319 AVGALSKSIYERMFKWLVARINRVLdAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEEYR 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  507 KEKINWTFIDFGLDSQATIDLIDgrQPPGILALLDEQSVFPNATDNTLITKLHSHFSKKNAKYEEPRFSKTEFGV----T 582
Cdd:cd14929    399 KEGIDWVSIDFGLDLQACIDLIE--KPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAhfelV 476
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  583 HYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIASRA--------KKGANFITVAAQYKEQLASLMA 654
Cdd:cd14929    477 HYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSAiqfgekkrKKGASFQTVASLHKENLNKLMT 556
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  655 TLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAE--DSQK 732
Cdd:cd14929    557 NLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKfvSSRK 636
                          650       660
                   ....*....|....*....|....*.
gi 1200169906  733 ATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14929    637 AAEELLGSLEIDHTQYRFGITKVFFK 662
MYSc_Myh3 cd14913
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...
111-758 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: 702.96  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITG 190
Cdd:cd14913      1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  191 ESGAGKTENTKKVIQYLASVAG------RNQANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFI 264
Cdd:cd14913     81 ESGAGKTVNTKRVIQYFATIAAtgdlakKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  265 SGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHL-AGPESFNYLNQsGCVDIKGVSDSEEFKITRQAMD 343
Cdd:cd14913    161 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLItTNPYDYPFISQ-GEILVASIDDAEELLATDSAID 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  344 IVGFSQEEQMSIFKIIAGILHLGNIKF------EKGAGEGAVLKDKTALnaastVFGVNPSVLEKALMEPRILAGRDLVA 417
Cdd:cd14913    240 ILGFTPEEKSGLYKLTGAVMHYGNMKFkqkqreEQAEPDGTEVADKTAY-----LMGLNSSDLLKALCFPRVKVGNEYVT 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  418 QHLNVEKSSSSRDALVKALYGRLFLWLVKKINNVL-CQERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHH 496
Cdd:cd14913    315 KGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLdTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHH 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  497 MFKLEQEEYLKEKINWTFIDFGLDSQATIDLIDgrQPPGILALLDEQSVFPNATDNTLITKLHSHFSKKNAKYEEPRFSK 576
Cdd:cd14913    395 MFVLEQEEYKKEGIEWTFIDFGMDLAACIELIE--KPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVK 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  577 ----TEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLF-----NDPNIASR---AKKGANFITVAAQ 644
Cdd:cd14913    473 graeAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYatfatADADSGKKkvaKKKGSSFQTVSAL 552
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  645 YKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVP 724
Cdd:cd14913    553 FRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAI 632
                          650       660       670
                   ....*....|....*....|....*....|....*.
gi 1200169906  725 RDAE--DSQKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14913    633 PEGQfiDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myh16 cd14934
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...
112-758 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: 692.92  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  112 AVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGE 191
Cdd:cd14934      2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  192 SGAGKTENTKKVIQYLASV--AGRNQANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASI 269
Cdd:cd14934     82 SGAGKTENTKKVIQYFANIggTGKQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGADI 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  270 QSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLA-GPESFNYLNQsGCVDIKGVSDSEEFKITRQAMDIVGFS 348
Cdd:cd14934    162 ESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVpNPKEYHWVSQ-GVTVVDNMDDGEELQITDVAFDVLGFS 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  349 QEEQMSIFKIIAGILHLGNIKFEKGAGEGAVLKDKTAL-NAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSS 427
Cdd:cd14934    241 AEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVaDKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCNN 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  428 SRDALVKALYGRLFLWLVKKINNVL-CQERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYL 506
Cdd:cd14934    321 SIGALGKAVYDKMFKWLVVRINKTLdTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYK 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  507 KEKINWTFIDFGLDSQATIDLIDgrQPPGILALLDEQSVFPNATDNTLITKLHSHFSKKNAKYEEPRFSK-----TEFGV 581
Cdd:cd14934    401 REGIEWVFIDFGLDLQACIDLLE--KPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKgkgpeAHFEL 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  582 THYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIASRAKK---GANFITVAAQYKEQLASLMATLET 658
Cdd:cd14934    479 VHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAGSKKqkrGSSFMTVSNFYREQLNKLMTTLHS 558
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  659 TNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNV-PRDAEDSQKATDAV 737
Cdd:cd14934    559 TAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNViPQGFVDNKKASELL 638
                          650       660
                   ....*....|....*....|.
gi 1200169906  738 LKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14934    639 LGSIDLDVNEYKIGHTKVFFR 659
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
112-758 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: 681.75  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  112 AVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGE 191
Cdd:cd14932      2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  192 SGAGKTENTKKVIQYLASVAG-----RNQANGS---GVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGF 263
Cdd:cd14932     82 SGAGKTENTKKVIQYLAYVASsfktkKDQSSIAlshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  264 ISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNqSGCVDIKGVSDSEEFKITRQAMD 343
Cdd:cd14932    162 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLS-NGNVTIPGQQDKELFAETMEAFR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  344 IVGFSQEEQMSIFKIIAGILHLGNIKFEKGA-GEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNV 422
Cdd:cd14932    241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERnSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  423 EKSSSSRDALVKALYGRLFLWLVKKINNVLCQERK--AYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKL 500
Cdd:cd14932    321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRqgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  501 EQEEYLKEKINWTFIDFGLDSQATIDLIDGRQ-PPGILALLDEQSVFPNATDNTLITKLhSHFSKKNAKYEEPRFSK--T 577
Cdd:cd14932    401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgPPGILALLDEECWFPKATDKSFVEKV-VQEQGNNPKFQKPKKLKddA 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  578 EFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNI----------------ASRAKKGAnFITV 641
Cdd:cd14932    480 DFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRivgldkvagmgeslhgAFKTRKGM-FRTV 558
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  642 AAQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAP 721
Cdd:cd14932    559 GQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 638
                          650       660       670
                   ....*....|....*....|....*....|....*...
gi 1200169906  722 N-VPRDAEDSQKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14932    639 NaIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
112-758 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: 678.28  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  112 AVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGE 191
Cdd:cd14921      2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  192 SGAGKTENTKKVIQYLASVA----GRNQANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGA 267
Cdd:cd14921     82 SGAGKTENTKKVIQYLAVVAsshkGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  268 SIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNqSGCVDIKGVSDSEEFKITRQAMDIVGF 347
Cdd:cd14921    162 NIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLS-NGFVPIPAAQDDEMFQETLEAMSIMGF 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  348 SQEEQMSIFKIIAGILHLGNIKFEKGAG-EGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSS 426
Cdd:cd14921    241 SEEEQLSILKVVSSVLQLGNIVFKKERNtDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  427 SSRDALVKALYGRLFLWLVKKINNVLCQERK--AYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEE 504
Cdd:cd14921    321 FAIEALAKATYERLFRWILTRVNKALDKTHRqgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  505 YLKEKINWTFIDFGLDSQATIDLID-GRQPPGILALLDEQSVFPNATDNTLITKLHSHfSKKNAKYEEPR--FSKTEFGV 581
Cdd:cd14921    401 YQREGIEWNFIDFGLDLQPCIELIErPNNPPGVLALLDEECWFPKATDKSFVEKLCTE-QGNHPKFQKPKqlKDKTEFSI 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  582 THYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPN-----------------IASRAKKGAnFITVAAQ 644
Cdd:cd14921    480 IHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDrivgldqmakmtesslpSASKTKKGM-FRTVGQL 558
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  645 YKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPN-V 723
Cdd:cd14921    559 YKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANaI 638
                          650       660       670
                   ....*....|....*....|....*....|....*
gi 1200169906  724 PRDAEDSQKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14921    639 PKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
MYSc_Myh9 cd14919
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...
112-758 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: 662.94  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  112 AVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGE 191
Cdd:cd14919      2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  192 SGAGKTENTKKVIQYLASVAGRNQA-NGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASIQ 270
Cdd:cd14919     82 SGAGKTENTKKVIQYLAHVASSHKSkKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  271 SYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNqSGCVDIKGVSDSEEFKITRQAMDIVGFSQE 350
Cdd:cd14919    162 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLS-NGHVTIPGQQDKDMFQETMEAMRIMGIPEE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  351 EQMSIFKIIAGILHLGNIKFEKGAG-EGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSSR 429
Cdd:cd14919    241 EQMGLLRVISGVLQLGNIVFKKERNtDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAI 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  430 DALVKALYGRLFLWLVKKINNVLCQERK--AYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYLK 507
Cdd:cd14919    321 EALAKATYERMFRWLVLRINKALDKTKRqgASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  508 EKINWTFIDFGLDSQATIDLIDGRQ-PPGILALLDEQSVFPNATDNTLITKLHSHfSKKNAKYEEPR--FSKTEFGVTHY 584
Cdd:cd14919    401 EGIEWNFIDFGLDLQPCIDLIEKPAgPPGILALLDEECWFPKATDKSFVEKVVQE-QGTHPKFQKPKqlKDKADFCIIHY 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  585 AGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNI-----------------ASRAKKGAnFITVAAQYKE 647
Cdd:cd14919    480 AGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiigldqvagmsetalpgAFKTRKGM-FRTVGQLYKE 558
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  648 QLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPN-VPRD 726
Cdd:cd14919    559 QLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNsIPKG 638
                          650       660       670
                   ....*....|....*....|....*....|..
gi 1200169906  727 AEDSQKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14919    639 FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
MYSc_Myh7 cd14917
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...
111-758 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: 660.64  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITG 190
Cdd:cd14917      1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  191 ESGAGKTENTKKVIQYLASVAG------RNQANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFI 264
Cdd:cd14917     81 ESGAGKTVNTKRVIQYFAVIAAigdrskKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  265 SGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLA-GPESFNYLNQsGCVDIKGVSDSEEFKITRQAMD 343
Cdd:cd14917    161 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITnNPYDYAFISQ-GETTVASIDDAEELMATDNAFD 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  344 IVGFSQEEQMSIFKIIAGILHLGNIKF------EKGAGEGAVLKDKTALnaastVFGVNPSVLEKALMEPRILAGRDLVA 417
Cdd:cd14917    240 VLGFTSEEKNSMYKLTGAIMHFGNMKFkqkqreEQAEPDGTEEADKSAY-----LMGLNSADLLKGLCHPRVKVGNEYVT 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  418 QHLNVEKSSSSRDALVKALYGRLFLWLVKKINNVL-CQERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHH 496
Cdd:cd14917    315 KGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLeTKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHH 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  497 MFKLEQEEYLKEKINWTFIDFGLDSQATIDLIDgrQPPGILALLDEQSVFPNATDNTLITKLHSHFSKKNAKYEEPRFSK 576
Cdd:cd14917    395 MFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIE--KPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIK 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  577 ----TEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIAS--------RAKKGANFITVAAQ 644
Cdd:cd14917    473 gkpeAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADapiekgkgKAKKGSSFQTVSAL 552
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  645 YKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVP 724
Cdd:cd14917    553 HRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAI 632
                          650       660       670
                   ....*....|....*....|....*....|....*.
gi 1200169906  725 RDAE--DSQKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14917    633 PEGQfiDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
116-758 0e+00

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: 655.60  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  116 NLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGESGAG 195
Cdd:cd01385      6 NLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGESGSG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  196 KTENTKKVIQYLASVAGRNQanGSGVlEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASIQSYLLE 275
Cdd:cd01385     86 KTESTNFLLHHLTALSQKGY--GSGV-EQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYLLE 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  276 KSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDSEEFKITRQAMDIVGFSQEEQMSI 355
Cdd:cd01385    163 KSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQRQI 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  356 FKIIAGILHLGNIKFEK---GAGEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSSRDAL 432
Cdd:cd01385    243 FSVLSAVLHLGNIEYKKkayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRDAM 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  433 VKALYGRLFLWLVKKINNVLC-----QERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYLK 507
Cdd:cd01385    323 AKCLYSALFDWIVLRINHALLnkkdlEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYKK 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  508 EKINWTFIDFgLDSQATIDLIDGRqPPGILALLDEQSVFPNATDNTLITKLhSHFSKKNAKYEEPRFSKTEFGVTHYAGQ 587
Cdd:cd01385    403 EGISWHNIEY-TDNTGCLQLISKK-PTGLLCLLDEESNFPGATNQTLLAKF-KQQHKDNKYYEKPQVMEPAFIIAHYAGK 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  588 VMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIA----------------------SRAKKGANF------- 638
Cdd:cd01385    480 VKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDPVAvfrwavlrafframaafreagrRRAQRTAGHsltlhdr 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  639 --------------ITVAAQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFP 704
Cdd:cd01385    560 ttksllhlhkkkkpPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYS 639
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1200169906  705 NRIIYADFVKRYYLLapnVPRDAEDSQKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd01385    640 VRYTFQEFITQFQVL---LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
MYSc_Myh19 cd15896
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...
112-758 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: 654.44  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  112 AVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGE 191
Cdd:cd15896      2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  192 SGAGKTENTKKVIQYLASVAG--------RNQANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGF 263
Cdd:cd15896     82 SGAGKTENTKKVIQYLAHVASshktkkdqNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  264 ISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNqSGCVDIKGVSDSEEFKITRQAMD 343
Cdd:cd15896    162 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLS-NGNVTIPGQQDKDLFTETMEAFR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  344 IVGFSQEEQMSIFKIIAGILHLGNIKFEKGA-GEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNV 422
Cdd:cd15896    241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERhTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  423 EKSSSSRDALVKALYGRLFLWLVKKINNVLCQERK--AYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKL 500
Cdd:cd15896    321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRqgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  501 EQEEYLKEKINWTFIDFGLDSQATIDLIDG-RQPPGILALLDEQSVFPNATDNTLITKLHSHfSKKNAKYEEPRFSKTE- 578
Cdd:cd15896    401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKpASPPGILALLDEECWFPKATDKSFVEKVLQE-QGTHPKFFKPKKLKDEa 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  579 -FGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNI---------------ASRAKKGAnFITVA 642
Cdd:cd15896    480 dFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRivgldkvsgmsempgAFKTRKGM-FRTVG 558
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  643 AQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPN 722
Cdd:cd15896    559 QLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 638
                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 1200169906  723 -VPRDAEDSQKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd15896    639 aIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
111-758 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: 654.15  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITG 190
Cdd:cd14872      1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  191 ESGAGKTENTKKVIQYLASVAGrnqanGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASIQ 270
Cdd:cd14872     81 ESGAGKTEATKQCLSFFAEVAG-----STNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTE 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  271 SYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPEsfNYLNQSGCVDIKGVSDSEEFKITRQAMDIVGFSQE 350
Cdd:cd14872    156 NYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSAAY--GYLSLSGCIEVEGVDDVADFEEVVLAMEQLGFDDA 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  351 EQMSIFKIIAGILHLGNIKFEKGAG----EGAVLKDKTALNAASTVFGVNPSVLEKALMEPRI-LAGRDLVAQHLNVEKS 425
Cdd:cd14872    234 DINNVMSLIAAILKLGNIEFASGGGkslvSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMeIKGCDPTRIPLTPAQA 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  426 SSSRDALVKALYGRLFLWLVKKINNVLCQER--KAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQE 503
Cdd:cd14872    314 TDACDALAKAAYSRLFDWLVKKINESMRPQKgaKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEA 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  504 EYLKEKINWTFIDFgLDSQATIDLIDGRQpPGILALLDEQSVFPNATDNTLITKL-HSHFSKKNAKYEEPRFSKTEFGVT 582
Cdd:cd14872    394 LYQSEGVKFEHIDF-IDNQPVLDLIEKKQ-PGLMLALDDQVKIPKGSDATFMIAAnQTHAAKSTFVYAEVRTSRTEFIVK 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  583 HYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIASRAKKganfITVAAQYKEQLASLMATLETTNPH 662
Cdd:cd14872    472 HYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEGDQKTSK----VTLGGQFRKQLSALMTALNATEPH 547
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  663 FVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRY-YLLAPNVPRDAEDSQKATDAVLKHL 741
Cdd:cd14872    548 YIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYrFLVKTIAKRVGPDDRQRCDLLLKSL 627
                          650
                   ....*....|....*..
gi 1200169906  742 NIDPEQYRFGITKIFFR 758
Cdd:cd14872    628 KQDFSKVQVGKTRVLYR 644
MYSc_Myh6 cd14916
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...
111-758 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: 652.12  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITG 190
Cdd:cd14916      1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  191 ESGAGKTENTKKVIQYLASVAG------RNQANGS-GVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGF 263
Cdd:cd14916     81 ESGAGKTVNTKRVIQYFASIAAigdrskKENPNANkGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  264 ISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLA-GPESFNYLNQsGCVDIKGVSDSEEFKITRQAM 342
Cdd:cd14916    161 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTnNPYDYAFVSQ-GEVSVASIDDSEELLATDSAF 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  343 DIVGFSQEEQMSIFKIIAGILHLGNIKFEKGAGEGAVLKDKTA-LNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLN 421
Cdd:cd14916    240 DVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  422 VEKSSSSRDALVKALYGRLFLWLVKKINNVL-CQERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKL 500
Cdd:cd14916    320 VQQVYYSIGALAKSVYEKMFNWMVTRINATLeTKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  501 EQEEYLKEKINWTFIDFGLDSQATIDLIDgrQPPGILALLDEQSVFPNATDNTLITKLHSHFSKKNAKYEEPRF----SK 576
Cdd:cd14916    400 EQEEYKKEGIEWEFIDFGMDLQACIDLIE--KPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNvkgkQE 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  577 TEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIASRA---------KKGANFITVAAQYKE 647
Cdd:cd14916    478 AHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGdsgkgkggkKKGSSFQTVSALHRE 557
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  648 QLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDA 727
Cdd:cd14916    558 NLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEG 637
                          650       660       670
                   ....*....|....*....|....*....|...
gi 1200169906  728 E--DSQKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14916    638 QfiDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
MYSc_Myh2_mammals cd14912
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
111-758 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: 650.26  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITG 190
Cdd:cd14912      1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  191 ESGAGKTENTKKVIQYLASVAGRNQANG--------SGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAG 262
Cdd:cd14912     81 ESGAGKTVNTKRVIQYFATIAVTGEKKKeeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  263 FISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHL-AGPESFNYLNQsGCVDIKGVSDSEEFKITRQA 341
Cdd:cd14912    161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQ-GEISVASIDDQEELMATDSA 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  342 MDIVGFSQEEQMSIFKIIAGILHLGNIKFEKGAGEGAVLKDKTAL-NAASTVFGVNPSVLEKALMEPRILAGRDLVAQHL 420
Cdd:cd14912    240 IDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVaDKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  421 NVEKSSSSRDALVKALYGRLFLWLVKKINNVL-CQERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFK 499
Cdd:cd14912    320 TVEQVTNAVGALAKAVYEKMFLWMVARINQQLdTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  500 LEQEEYLKEKINWTFIDFGLDSQATIDLIDgrQPPGILALLDEQSVFPNATDNTLITKLHSHFSKKNAKYEEPRFSK--- 576
Cdd:cd14912    400 LEQEEYKKEGIEWTFIDFGMDLAACIELIE--KPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKgka 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  577 -TEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIAS-----------RAKKGANFITVAAQ 644
Cdd:cd14912    478 eAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEgasagggakkgGKKKGSSFQTVSAL 557
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  645 YKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVP 724
Cdd:cd14912    558 FRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAI 637
                          650       660       670
                   ....*....|....*....|....*....|....*.
gi 1200169906  725 RDAE--DSQKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14912    638 PEGQfiDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
MYSc_Myh14_mammals cd14930
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...
112-758 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: 647.54  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  112 AVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGE 191
Cdd:cd14930      2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  192 SGAGKTENTKKVIQYLASVA----GRNQANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGA 267
Cdd:cd14930     82 SGAGKTENTKKVIQYLAHVAsspkGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  268 SIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNqSGCVDIKGvSDSEEFKITRQAMDIVGF 347
Cdd:cd14930    162 NIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLT-NGPSSSPG-QERELFQETLESLRVLGF 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  348 SQEEQMSIFKIIAGILHLGNIKFEKGAG-EGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSS 426
Cdd:cd14930    240 SHEEITSMLRMVSAVLQFGNIVLKRERNtDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  427 SSRDALVKALYGRLFLWLVKKINNVLCQERK--AYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEE 504
Cdd:cd14930    320 FALEALAKATYERLFRWLVLRLNRALDRSPRqgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  505 YLKEKINWTFIDFGLDSQATIDLID-GRQPPGILALLDEQSVFPNATDNTLITKLhSHFSKKNAKYEEPR--FSKTEFGV 581
Cdd:cd14930    400 YQREGIPWTFLDFGLDLQPCIDLIErPANPPGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPKFQRPRhlRDQADFSV 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  582 THYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFND-------PNIAS--------RAKKGAnFITVAAQYK 646
Cdd:cd14930    479 LHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivglEQVSSlgdgppggRPRRGM-FRTVGQLYK 557
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  647 EQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPN-VPR 725
Cdd:cd14930    558 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNaIPK 637
                          650       660       670
                   ....*....|....*....|....*....|...
gi 1200169906  726 DAEDSQKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14930    638 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
112-758 0e+00

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: 642.23  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  112 AVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIP-IYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITG 190
Cdd:cd14873      2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  191 ESGAGKTENTKKVIQYLASVAgrNQANGSGV------LEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFI 264
Cdd:cd14873     82 ESGAGKTESTKLILKFLSVIS--QQSLELSLkektscVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNI 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  265 SGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDSEEFKITRQAMDI 344
Cdd:cd14873    160 QGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEV 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  345 VGFSQEEQMSIFKIIAGILHLGNIKFEKGAgeGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEK 424
Cdd:cd14873    240 MQFSKEEVREVSRLLAGILHLGNIEFITAG--GAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQ 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  425 SSSSRDALVKALYGRLFLWLVKKINNVLCQERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEE 504
Cdd:cd14873    318 AVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLE 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  505 YLKEKINWTFIDFgLDSQATIDLIDGRQppGILALLDEQSVFPNATDNTLITKLHSHFSkKNAKYEEPRFSKTEFGVTHY 584
Cdd:cd14873    398 YSREGLVWEDIDW-IDNGECLDLIEKKL--GLLALINEESHFPQATDSTLLEKLHSQHA-NNHFYVKPRVAVNNFGVKHY 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  585 AGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLF---------NDPNIASRAKKGanfiTVAAQYKEQLASLMAT 655
Cdd:cd14873    474 AGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFehvssrnnqDTLKCGSKHRRP----TVSSQFKDSLHSLMAT 549
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  656 LETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDaEDSQKATD 735
Cdd:cd14873    550 LSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALP-EDVRGKCT 628
                          650       660
                   ....*....|....*....|...
gi 1200169906  736 AVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14873    629 SLLQLYDASNSEWQLGKTKVFLR 651
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
112-758 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: 639.49  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  112 AVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGE 191
Cdd:cd01387      2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  192 SGAGKTENTKKVIQYLASVAGRnqanGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSaGFISGASIQS 271
Cdd:cd01387     82 SGSGKTEATKLIMQYLAAVNQR----RNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFEG-GVIVGAITSQ 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  272 YLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDSEEFKITRQAMDIVGFSQEE 351
Cdd:cd01387    157 YLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEE 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  352 QMSIFKIIAGILHLGNIKFEK----GAGEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSS 427
Cdd:cd01387    237 QDSIFRILASVLHLGNVYFHKrqlrHGQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALD 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  428 SRDALVKALYGRLFLWLVKKINNVLCQERK-AYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYL 506
Cdd:cd01387    317 ARDAIAKALYALLFSWLVTRVNAIVYSGTQdTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYI 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  507 KEKINWTFIDFgLDSQATIDLIdGRQPPGILALLDEQSVFPNATDNTLITKLHSHFSkKNAKYEEPRFSKTEFGVTHYAG 586
Cdd:cd01387    397 REQIDWTEIAF-ADNQPVINLI-SKKPVGILHILDDECNFPQATDHSFLEKCHYHHA-LNELYSKPRMPLPEFTIKHYAG 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  587 QVMYEIQDWLEKNKDPLQQD-LELcFKDSSDNVVTKLFND--PNIASRAKKGAN--FI-------TVAAQYKEQLASLMA 654
Cdd:cd01387    474 QVWYQVHGFLDKNRDQLRQDvLEL-LVSSRTRVVAHLFSShrAQTDKAPPRLGKgrFVtmkprtpTVAARFQDSLLQLLE 552
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  655 TLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRY-YLLAPNVPRDAEDSQKA 733
Cdd:cd01387    553 KMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYrCLVALKLPRPAPGDMCV 632
                          650       660
                   ....*....|....*....|....*.
gi 1200169906  734 TdAVLKHLNIDPE-QYRFGITKIFFR 758
Cdd:cd01387    633 S-LLSRLCTVTPKdMYRLGATKVFLR 657
MYSc_Myh8 cd14918
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...
111-758 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: 639.09  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITG 190
Cdd:cd14918      1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  191 ESGAGKTENTKKVIQYLASVA--GRNQANGS----GVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFI 264
Cdd:cd14918     81 ESGAGKTVNTKRVIQYFATIAvtGEKKKEESgkmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  265 SGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHL-AGPESFNYLNQsGCVDIKGVSDSEEFKITRQAMD 343
Cdd:cd14918    161 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQ-GEITVPSIDDQEELMATDSAID 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  344 IVGFSQEEQMSIFKIIAGILHLGNIKFEKGAGEGAVLKDKTAL-NAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNV 422
Cdd:cd14918    240 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVaDKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  423 EKSSSSRDALVKALYGRLFLWLVKKINNVL-CQERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLE 501
Cdd:cd14918    320 QQVYNAVGALAKAVYEKMFLWMVTRINQQLdTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  502 QEEYLKEKINWTFIDFGLDSQATIDLIDgrQPPGILALLDEQSVFPNATDNTLITKLHSHFSKKNAKYEEPRFSK----T 577
Cdd:cd14918    400 QEEYKKEGIEWTFIDFGMDLAACIELIE--KPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKgkaeA 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  578 EFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIA---SRAKKGA-----NFITVAAQYKEQL 649
Cdd:cd14918    478 HFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAeadSGAKKGAkkkgsSFQTVSALFRENL 557
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  650 ASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAE- 728
Cdd:cd14918    558 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQf 637
                          650       660       670
                   ....*....|....*....|....*....|.
gi 1200169906  729 -DSQKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14918    638 iDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myh4 cd14915
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...
111-758 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: 638.70  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITG 190
Cdd:cd14915      1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  191 ESGAGKTENTKKVIQYLASVA-----GRNQANG---SGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAG 262
Cdd:cd14915     81 ESGAGKTVNTKRVIQYFATIAvtgekKKEEAASgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  263 FISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHL-AGPESFNYLNQsGCVDIKGVSDSEEFKITRQA 341
Cdd:cd14915    161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLItTNPYDFAFVSQ-GEITVPSIDDQEELMATDSA 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  342 MDIVGFSQEEQMSIFKIIAGILHLGNIKFEKGAGEGAVLKDKTAL-NAASTVFGVNPSVLEKALMEPRILAGRDLVAQHL 420
Cdd:cd14915    240 VDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVaDKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  421 NVEKSSSSRDALVKALYGRLFLWLVKKINNVL-CQERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFK 499
Cdd:cd14915    320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLdTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  500 LEQEEYLKEKINWTFIDFGLDSQATIDLIDgrQPPGILALLDEQSVFPNATDNTLITKLHSHFSKKNAKYEEPRFSK--- 576
Cdd:cd14915    400 LEQEEYKKEGIEWEFIDFGMDLAACIELIE--KPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKgka 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  577 -TEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIASR---------AKKGANFITVAAQYK 646
Cdd:cd14915    478 eAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAeggggkkggKKKGSSFQTVSALFR 557
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  647 EQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRD 726
Cdd:cd14915    558 ENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 637
                          650       660       670
                   ....*....|....*....|....*....|....
gi 1200169906  727 AE--DSQKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14915    638 GQfiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh13 cd14923
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...
111-758 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: 636.34  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITG 190
Cdd:cd14923      1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  191 ESGAGKTENTKKVIQYLASVA----GRNQANGS---GVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGF 263
Cdd:cd14923     81 ESGAGKTVNTKRVIQYFATIAvtgdKKKEQQPGkmqGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  264 ISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLA-GPESFNYLNQsGCVDIKGVSDSEEFKITRQAM 342
Cdd:cd14923    161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIStNPFDFPFVSQ-GEVTVASIDDSEELLATDNAI 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  343 DIVGFSQEEQMSIFKIIAGILHLGNIKFEKGAGEGAVLKDKTAL-NAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLN 421
Cdd:cd14923    240 DILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVaDKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  422 VEKSSSSRDALVKALYGRLFLWLVKKINNVL-CQERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKL 500
Cdd:cd14923    320 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLdTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  501 EQEEYLKEKINWTFIDFGLDSQATIDLIDgrQPPGILALLDEQSVFPNATDNTLITKLHSHFSKKNAKYEEPRFSK---- 576
Cdd:cd14923    400 EQEEYKKEGIEWEFIDFGMDLAACIELIE--KPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKgkae 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  577 TEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIASRA----------KKGANFITVAAQYK 646
Cdd:cd14923    478 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGdsggskkggkKKGSSFQTVSAVFR 557
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  647 EQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRD 726
Cdd:cd14923    558 ENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPE 637
                          650       660       670
                   ....*....|....*....|....*....|....
gi 1200169906  727 AE--DSQKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14923    638 GQfiDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
MYSc_Myh1_mammals cd14910
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
111-758 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: 636.00  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITG 190
Cdd:cd14910      1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  191 ESGAGKTENTKKVIQYLASVAGRNQANG--------SGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAG 262
Cdd:cd14910     81 ESGAGKTVNTKRVIQYFATIAVTGEKKKeeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  263 FISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHL-AGPESFNYLNQsGCVDIKGVSDSEEFKITRQA 341
Cdd:cd14910    161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQ-GEITVPSIDDQEELMATDSA 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  342 MDIVGFSQEEQMSIFKIIAGILHLGNIKFEKGAGEGAVLKDKTAL-NAASTVFGVNPSVLEKALMEPRILAGRDLVAQHL 420
Cdd:cd14910    240 IEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVaDKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  421 NVEKSSSSRDALVKALYGRLFLWLVKKINNVL-CQERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFK 499
Cdd:cd14910    320 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLdTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  500 LEQEEYLKEKINWTFIDFGLDSQATIDLIDgrQPPGILALLDEQSVFPNATDNTLITKLHSHFSKKNAKYEEPRFSK--- 576
Cdd:cd14910    400 LEQEEYKKEGIEWEFIDFGMDLAACIELIE--KPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKgkv 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  577 -TEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIASR---------AKKGANFITVAAQYK 646
Cdd:cd14910    478 eAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAeegggkkggKKKGSSFQTVSALFR 557
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  647 EQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRD 726
Cdd:cd14910    558 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 637
                          650       660       670
                   ....*....|....*....|....*....|....
gi 1200169906  727 AE--DSQKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14910    638 GQfiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
112-758 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: 629.88  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  112 AVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIP-IYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLD----DRQNQSL 186
Cdd:cd14890      2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQSI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  187 LITGESGAGKTENTKKVIQYLASVAGRNQANGSGV--------------LEQQILQANPILEAFGNAKTTRNNNSSRFGK 252
Cdd:cd14890     82 IISGESGAGKTEATKIIMQYLARITSGFAQGASGEgeaaseaieqtlgsLEDRVLSSNPLLESFGNAKTLRNDNSSRFGK 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  253 FIEIQFNSAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLnQSGCVDIKGVSDS 332
Cdd:cd14890    162 FIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYL-RGECSSIPSCDDA 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  333 EEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFEKgAGEGAVLKDKTALNA---ASTVFGVNPSVLEKALMEPRI 409
Cdd:cd14890    241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFES-ENDTTVLEDATTLQSlklAAELLGVNEDALEKALLTRQL 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  410 LAGRDLVAQHLNVEKSSSSRDALVKALYGRLFLWLVKKINNVLCQ-ERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEK 488
Cdd:cd14890    320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSpDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEK 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  489 LQQFFNHHMFKLEQEEYLKEKINWTFIDFGlDSQATIDLIDGRQP--PGILALLDEQSVFPNATDNT-LITKLHSHF--- 562
Cdd:cd14890    400 LQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEGKVNgkPGIFITLDDCWRFKGEEANKkFVSQLHASFgrk 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  563 ---------SKKNAKYEEPRFSK-TEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVvtklfndpniasRA 632
Cdd:cd14890    479 sgsggtrrgSSQHPHFVHPKFDAdKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSI------------RE 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  633 kkganfITVAAQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADF 712
Cdd:cd14890    547 ------VSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSF 620
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*.
gi 1200169906  713 VKRYYLLAPnvprDAEDSQKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14890    621 FYDFQVLLP----TAENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
111-756 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: 627.59  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIF------KGRRRNEVAPHIFAISDVAYRSMLDDR--- 181
Cdd:cd14901      1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASrgq 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  182 -QNQSLLITGESGAGKTENTKKVIQYLASVAGRNQANGSGV----LEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEI 256
Cdd:cd14901     81 kCDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATerenVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  257 QFNSAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIK-GVSDSEEF 335
Cdd:cd14901    161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDRRdGVDDSVQY 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  336 KITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFEKGAGEGAVLKDKTALN--AASTVFGVNPSVLEKALMEPRILAGR 413
Cdd:cd14901    241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANvrAACDLLGLDMDVLEKTLCTREIRAGG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  414 DLVAQHLNVEKSSSSRDALVKALYGRLFLWLVKKINNVLCQERKA---YFIGVLDISGFEIFKVNSFEQLCINYTNEKLQ 490
Cdd:cd14901    321 EYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTgasRFIGIVDIFGFEIFATNSLEQLCINFANEKLQ 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  491 QFFNHHMFKLEQEEYLKEKINWTFIDFGlDSQATIDLIDGRqPPGILALLDEQSVFPNATDNTLITKLHSHFSKKnakye 570
Cdd:cd14901    401 QLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFEAR-PTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKH----- 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  571 ePRFS-------KTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKlfndpniasrakkganfiTVAA 643
Cdd:cd14901    474 -ASFSvsklqqgKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS------------------TVVA 534
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  644 QYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNV 723
Cdd:cd14901    535 KFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPDG 614
                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 1200169906  724 PRDAEDSQKATDAVLKHL------NIDPEQYRFGITKIF 756
Cdd:cd14901    615 ASDTWKVNELAERLMSQLqhselnIEHLPPFQVGKTKVF 653
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
114-758 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: 618.11  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  114 FHNLRVRYNQDLIYTYSGLFLVAVNPFKRIP-IYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGES 192
Cdd:cd01382      4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  193 GAGKTENTKKVIQYLASVAGrnqaNGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASIQSY 272
Cdd:cd01382     84 GAGKTESTKYILRYLTESWG----SGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  273 LLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALhlagpesfnylnqsgcVDIKGVSDSEEFKITRQAMDIVGFSQEEQ 352
Cdd:cd01382    160 LLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL----------------LKDPLLDDVGDFIRMDKAMKKIGLSDEEK 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  353 MSIFKIIAGILHLGNIKFEK---GAGEGAVLKDKT--ALNAASTVFGVNPSVLEKAL----MEPRILAGR-DLVAQHLNV 422
Cdd:cd01382    224 LDIFRVVAAVLHLGNIEFEEngsDSGGGCNVKPKSeqSLEYAAELLGLDQDELRVSLttrvMQTTRGGAKgTVIKVPLKV 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  423 EKSSSSRDALVKALYGRLFLWLVKKINNVLCQERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQ 502
Cdd:cd01382    304 EEANNARDALAKAIYSKLFDHIVNRINQCIPFETSSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILKEEQ 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  503 EEYLKEKINWTFIDFgLDSQATIDLIDGRqPPGILALLDEQSVFPNATDNTLITKLHSHfSKKNAKYEEPRFSKTE---- 578
Cdd:cd01382    384 ELYEKEGLGVKEVEY-VDNQDCIDLIEAK-LVGILDLLDEESKLPKPSDQHFTSAVHQK-HKNHFRLSIPRKSKLKihrn 460
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  579 ------FGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLF-----NDPNIASRAKKGaNFITVAAQYKE 647
Cdd:cd01382    461 lrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFesstnNNKDSKQKAGKL-SFISVGNKFKT 539
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  648 QLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRY-YLLAPNVPRd 726
Cdd:cd01382    540 QLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYkKYLPPKLAR- 618
                          650       660       670
                   ....*....|....*....|....*....|..
gi 1200169906  727 aEDSQKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd01382    619 -LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
117-758 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: 607.53  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  117 LRVRYNQDLIYTYSGLFLVAVNPFKRIP-IY-------TQEMVDIFKGRRrnevaPHIFAISDVAYRSMLDDR----QNQ 184
Cdd:cd14892      7 LRRRYERDAIYTFTADILISINPYKSIPlLYdvpgfdsQRKEEATASSPP-----PHVFSIAERAYRAMKGVGkgqgTPQ 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  185 SLLITGESGAGKTENTKKVIQYLASV--------AGRNQANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEI 256
Cdd:cd14892     82 SIVVSGESGAGKTEASKYIMKYLATAsklakgasTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQI 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  257 QFNSAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDSEEFK 336
Cdd:cd14892    162 HYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVDGVDDATEFK 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  337 ITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFE---KGAGEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGR 413
Cdd:cd14892    242 QLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEenaDDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTSTAR 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  414 DLVAQ-HLNVEKSSSSRDALVKALYGRLFLWLVKKINNVLCQE-----------RKAYFIGVLDISGFEIFKVNSFEQLC 481
Cdd:cd14892    322 GSVLEiKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQtsgvtggaaspTFSPFIGILDIFGFEIMPTNSFEQLC 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  482 INYTNEKLQQFFNHHMFKLEQEEYLKEKINWTFIDFGlDSQATIDLIDGRqPPGILALLDEQSVFP-NATDNTLITKLHS 560
Cdd:cd14892    402 INFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK-PLGLLPLLEEQMLLKrKTTDKQLLTIYHQ 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  561 HFSKKNAKYEEPRFSKTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSdnvvtklfndpniasrakkganfit 640
Cdd:cd14892    480 THLDKHPHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS------------------------- 534
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  641 vaaQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLA 720
Cdd:cd14892    535 ---KFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLA 611
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*..
gi 1200169906  721 ---------PNVPRDAEDSQKATDAVLKHLniDPEQYRFGITKIFFR 758
Cdd:cd14892    612 rnkagvaasPDACDATTARKKCEEIVARAL--ERENFQLGRTKVFLR 656
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
111-758 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: 597.91  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIP-IYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLIT 189
Cdd:cd14903      1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  190 GESGAGKTENTKKVIQYLASVAGrnQANGSGVleQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASI 269
Cdd:cd14903     81 GESGAGKTETTKILMNHLATIAG--GLNDSTI--KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKC 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  270 QSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLA--GPESFNYLNQSgcvdIKGVSDSEEFKITRQAMDIVGF 347
Cdd:cd14903    157 RTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSAneCAYTGANKTIK----IEGMSDRKHFARTKEALSLIGV 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  348 SQEEQMSIFKIIAGILHLGNIKFE-KGAGE--GAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEK 424
Cdd:cd14903    233 SEEKQEVLFEVLAGILHLGQLQIQsKPNDDekSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQ 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  425 SSSSRDALVKALYGRLFLWLVKKINNVLCQ-ERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQE 503
Cdd:cd14903    313 AEDCRDALAKAIYSNVFDWLVATINASLGNdAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQI 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  504 EYLKEKINWTFIDFgLDSQATIDLIDGRQppGILALLDEQSVFPNATDNTLITKLHSHFSKKNAKYEEPRFSKTEFGVTH 583
Cdd:cd14903    393 EYEEEGIRWAHIDF-ADNQDVLAVIEDRL--GIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSRTQFTIKH 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  584 YAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDP------------NIASRAKKGA-NFITVAAQYKEQLA 650
Cdd:cd14903    470 YAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKvespaaastslaRGARRRRGGAlTTTTVGTQFKDSLN 549
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  651 SLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAEDS 730
Cdd:cd14903    550 ELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEGRNTDVPV 629
                          650       660
                   ....*....|....*....|....*....
gi 1200169906  731 QKATDAVLKHLNID-PEQYRFGITKIFFR 758
Cdd:cd14903    630 AERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
117-758 0e+00

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: 589.63  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  117 LRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGESGAGK 196
Cdd:cd01379      7 LQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGESGAGK 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  197 TENTKKVIQYLASVAGRNQANgsgvLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASIQSYLLEK 276
Cdd:cd01379     87 TESANLLVQQLTVLGKANNRT----LEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLLEK 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  277 SRVVFQSETERNYHIFYQLLAGaTAEEKKALHLAGPES--FNYLNQSGCVDIKGVSDS---EEFKITRQAMDIVGFSQEE 351
Cdd:cd01379    163 SRVVHQAIGERNFHIFYYIYAG-LAEDKKLAKYKLPENkpPRYLQNDGLTVQDIVNNSgnrEKFEEIEQCFKVIGFTKEE 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  352 QMSIFKIIAGILHLGNIKFEKGAGEG-----AVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSS 426
Cdd:cd01379    242 VDSVYSILAAILHIGDIEFTEVESNHqtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVEEAT 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  427 SSRDALVKALYGRLFLWLVKKINNVLCQER----KAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQ 502
Cdd:cd01379    322 DARDAMAKALYGRLFSWIVNRINSLLKPDRsasdEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIFAWEQ 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  503 EEYLKEKINWTFIDFGlDSQATIDLIDGRqPPGILALLDEQSVFPNATDNTLITKLHSHFSKKNakYEEPRFSKTEFGVT 582
Cdd:cd01379    402 QEYLNEGIDVDLIEYE-DNRPLLDMFLQK-PMGLLALLDEESRFPKATDQTLVEKFHNNIKSKY--YWRPKSNALSFGIH 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  583 HYAGQVMYEIQDWLEKNKDPLQQDLELCFKdSSDNVVTKLfndpniasrakkganfiTVAAQYKEQLASLMATLETTNPH 662
Cdd:cd01379    478 HYAGKVLYDASGFLEKNRDTLPPDVVQLLR-SSENPLVRQ-----------------TVATYFRYSLMDLLSKMVVGQPH 539
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  663 FVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAEDSQKATDAVLKHLN 742
Cdd:cd01379    540 FVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAFKWNEEVVANRENCRLILERLK 619
                          650
                   ....*....|....*.
gi 1200169906  743 IDpeQYRFGITKIFFR 758
Cdd:cd01379    620 LD--NWALGKTKVFLK 633
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
111-758 0e+00

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: 580.11  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIP-IYTQEMVDIFKgRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLIT 189
Cdd:cd14888      1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  190 GESGAGKTENTKKVIQYLASVAGRNQANGSGVlEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFN---------S 260
Cdd:cd14888     80 GESGAGKTESTKYVMKFLACAGSEDIKKRSLV-EAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSklkskrmsgD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  261 AGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGP-----------------------ESFNY 317
Cdd:cd14888    159 RGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENdeklakgadakpisidmssfephLKFRY 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  318 LNQSGCVDIKGVSDSEEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFE--KGAGEGAVLKDKTA--LNAASTVF 393
Cdd:cd14888    239 LTKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFEnnEACSEGAVVSASCTddLEKVASLL 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  394 GVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSSRDALVKALYGRLFLWLVKKINNVL--CQERKAYFIGVLDISGFEI 471
Cdd:cd14888    319 GVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIgySKDNSLLFCGVLDIFGFEC 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  472 FKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYLKEKINWTFIDFGlDSQATIDLIDgRQPPGILALLDEQSVFPNATD 551
Cdd:cd14888    399 FQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ-EKPLGIFCMLDEECFVPGGKD 476
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  552 NTLITKLHSHFsKKNAKYEEPRFSKTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFN----DPN 627
Cdd:cd14888    477 QGLCNKLCQKH-KGHKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSaylrRGT 555
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  628 IASRAKKGanFITVAAQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRI 707
Cdd:cd14888    556 DGNTKKKK--FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRL 633
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1200169906  708 IYADFVKRYYLLAPnvprdaedsqkatdavlKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14888    634 SHAEFYNDYRILLN-----------------GEGKKQLSIWAVGKTLCFFK 667
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
116-758 0e+00

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: 572.40  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  116 NLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRR-RNEVAPHIFAISDVAYRSMLDDRQNQSLLITGESGA 194
Cdd:cd14897      6 TLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSGESGA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  195 GKTENTKKVIQYLASVAGRNQANgsgvLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASIQSYLL 274
Cdd:cd14897     86 GKTESTKYMIKHLMKLSPSDDSD----LLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYLL 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  275 EKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLnQSGCVDIKGVSDSEEFKITRQA-------MDIVGF 347
Cdd:cd14897    162 EKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRIL-RDDNRNRPVFNDSEELEYYRQMfhdltniMKLIGF 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  348 SQEEQMSIFKIIAGILHLGNIKFEK-GAGEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSS 426
Cdd:cd14897    241 SEEDISVIFTILAAILHLTNIVFIPdEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQAN 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  427 SSRDALVKALYGRLFLWLVKKIN-NVLCQERKAYF-----IGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKL 500
Cdd:cd14897    321 DSRDALAKDLYSRLFGWIVGQINrNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVFPR 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  501 EQEEYLKEKINWTFIDFGlDSQATIDLIdGRQPPGILALLDEQSVFPNATDNTLITKLHSHFsKKNAKYEEPRFSKTEFG 580
Cdd:cd14897    401 ERSEYEIEGIEWRDIEYH-DNDDVLELF-FKKPLGILPLLDEESTFPQSTDSSLVQKLNKYC-GESPRYVASPGNRVAFG 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  581 VTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFndpniasrakkganfitvAAQYKEQLASLMATLETTN 660
Cdd:cd14897    478 IRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF------------------TSYFKRSLSDLMTKLNSAD 539
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  661 PHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAEDSQKATDAVLKH 740
Cdd:cd14897    540 PLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFSNKVRSDDLGKCQKILKT 619
                          650
                   ....*....|....*...
gi 1200169906  741 LNIdpEQYRFGITKIFFR 758
Cdd:cd14897    620 AGI--KGYQFGKTKVFLK 635
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
117-758 0e+00

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: 548.74  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  117 LRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLD----DRQNQSLLITGES 192
Cdd:cd14889      7 LKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLGrlarGPKNQCIVISGES 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  193 GAGKTENTKKVIQYLASVAgrnqaNGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSaGFISGASIQSY 272
Cdd:cd14889     87 GAGKTESTKLLLRQIMELC-----RGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFRN-GHVKGAKINEY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  273 LLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLN-QSGCVDIKGVSDSEEFKITrQAMDIVGFSQEE 351
Cdd:cd14889    161 LLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNnGAGCKREVQYWKKKYDEVC-NAMDMVGFTEQE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  352 QMSIFKIIAGILHLGNIKFEKGAGEGAVLKD--KTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSSR 429
Cdd:cd14889    240 EVDMFTILAGILSLGNITFEMDDDEALKVENdsNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQAEDAR 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  430 DALVKALYGRLFLWLVKKINNVLCQER----KAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEY 505
Cdd:cd14889    320 DSIAKVAYGRVFGWIVSKINQLLAPKDdssvELREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLMEQKEY 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  506 LKEKINWTFIDFgLDSQATIDLIDGRqPPGILALLDEQSVFPNATDNTLITKLHSHFsKKNAKYEEPRFSKTEFGVTHYA 585
Cdd:cd14889    400 KKEGIDWKEITY-KDNKPILDLFLNK-PIGILSLLDEQSHFPQATDESFVDKLNIHF-KGNSYYGKSRSKSPKFTVNHYA 476
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  586 GQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNdpniASRAKKGA-------------NF-----ITVAAQYKE 647
Cdd:cd14889    477 GKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFT----ATRSRTGTlmpraklpqagsdNFnstrkQSVGAQFKH 552
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  648 QLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRY--YLLAPNVPR 725
Cdd:cd14889    553 SLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYkiLLCEPALPG 632
                          650       660       670
                   ....*....|....*....|....*....|...
gi 1200169906  726 DAEDSQkatdAVLKHLNIdpEQYRFGITKIFFR 758
Cdd:cd14889    633 TKQSCL----RILKATKL--VGWKCGKTRLFFK 659
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
111-758 0e+00

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: 547.58  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFK--GRRRNE-------VAPHIFAISDVAYRSMLDD- 180
Cdd:cd14908      1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  181 RQNQSLLITGESGAGKTENTKKVIQYLASV-AGRNQA------NGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKF 253
Cdd:cd14908     81 RASQSILISGESGAGKTESTKIVMLYLTTLgNGEEGApnegeeLGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  254 IEIQFNSAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEE--KKALH------LAGPESFNYLNQSGCVD 325
Cdd:cd14908    161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEheKYEFHdgitggLQLPNEFHYTGQGGAPD 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  326 IKGVSDSEEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFEKGAGEGAVLKDKTA----LNAASTVFGVNPSVLE 401
Cdd:cd14908    241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGnekcLARVAKLLGVDVDKLL 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  402 KALMEPRILAGRDLVAQHLNVEKSSSSRDALVKALYGRLFLWLVKKINN-VLCQERKAY--FIGVLDISGFEIFKVNSFE 478
Cdd:cd14908    321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSsINWENDKDIrsSVGVLDIFGFECFAHNSFE 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  479 QLCINYTNEKLQQFFNHHMFKLEQEEYLKEKINWTFIDFGlDSQATIDLIDGRqPPGILALLDEQSVFP-NATDNTLITK 557
Cdd:cd14908    401 QLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQAK-KKGILTMLDDECRLGiRGSDANYASR 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  558 LHSHFSKKNAKY--EEPRFSKTE-------FGVTHYAGQVMYEIQD-WLEKNKDPLQQDLELCFKDSSdnvvtklfndpn 627
Cdd:cd14908    479 LYETYLPEKNQThsENTRFEATSiqktkliFAVRHFAGQVQYTVETtFCEKNKDEIPLTADSLFESGQ------------ 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  628 iasrakkganfitvaaQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRI 707
Cdd:cd14908    547 ----------------QFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRL 610
                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1200169906  708 IYADFVKRYYLLAPNVPRDA-------EDSQKA--------------TDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14908    611 PHKDFFKRYRMLLPLIPEVVlswsmerLDPQKLcvkkmckdlvkgvlSPAMVSMKNIPEDTMQLGKSKVFMR 682
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
111-758 5.09e-179

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: 538.09  E-value: 5.09e-179
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRY---NQDlIYTYSGLFLVAVNPFKRIPiytQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDR---QNQ 184
Cdd:cd14891      1 AGILHNLEERSkldNQR-PYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSgrmQNQ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  185 SLLITGESGAGKTENTKKVIQYLASVAGRNQANGSGV--------------LEQQILQANPILEAFGNAKTTRNNNSSRF 250
Cdd:cd14891     77 SIVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDieqsskkrklsvtsLDERLMDTNPILESFGNAKTLRNHNSSRF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  251 GKFIEIQFNSAGF-ISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGV 329
Cdd:cd14891    157 GKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNI 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  330 SDSEEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKF-----EKGAGEGAVLKDKTALNAASTVFGVNPSVLEKAL 404
Cdd:cd14891    237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFdeedtSEGEAEIASESDKEALATAAELLGVDEEALEKVI 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  405 MEPRILAGRDLVAQHLNVEKSSSSRDALVKALYGRLFLWLVKKINNVLCQERKAY-FIGVLDISGFEIFK-VNSFEQLCI 482
Cdd:cd14891    317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLpYIGVLDIFGFESFEtKNDFEQLLI 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  483 NYTNEKLQQFFNHHMFKLEQEEYLKE-----KINWTfidfglDSQATIDLIDGRqPPGILALLDEQSVFPNATDNTLITK 557
Cdd:cd14891    397 NYANEALQATFNQQVFIAEQELYKSEgidvgVITWP------DNRECLDLIASK-PNGILPLLDNEARNPNPSDAKLNET 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  558 LHSHFsKKNAKY--EEPRFSKTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLElcfkdssdnvvtklfndpniasrakkg 635
Cdd:cd14891    470 LHKTH-KRHPCFprPHPKDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFE--------------------------- 521
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  636 aNFITVAAQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKR 715
Cdd:cd14891    522 -DLLASSAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDV 600
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*
gi 1200169906  716 YY-LLAPNVPRDAEDSQKA-TDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14891    601 YKpVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
111-758 7.04e-176

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: 530.28  E-value: 7.04e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIP-IYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLIT 189
Cdd:cd14904      1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  190 GESGAGKTENTKKVIQYLASVAGRNQANGSGvleqQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASI 269
Cdd:cd14904     81 GESGAGKTETTKIVMNHLASVAGGRKDKTIA----KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKC 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  270 QSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQS-GCVDIKGVSDSEEFKITRQAMDIVGFS 348
Cdd:cd14904    157 ETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSlAQMQIPGLDDAKLFASTQKSLSLIGLD 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  349 QEEQMSIFKIIAGILHLGNIKFEKGAGEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSS 428
Cdd:cd14904    237 NDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEEN 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  429 RDALVKALYGRLFLWLVKKINNVLC--QERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYL 506
Cdd:cd14904    317 RDALAKAIYSKLFDWMVVKINAAIStdDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEEYI 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  507 KEKINWTFIDFGlDSQATIDLIDGRQppGILALLDEQSVFPNATDNTLITKLHSHFS--KKNAKYEEPRFSKTEFGVTHY 584
Cdd:cd14904    397 REGLQWDHIEYQ-DNQGIVEVIDGKM--GIIALMNDHLRQPRGTEEALVNKIRTNHQtkKDNESIDFPKVKRTQFIINHY 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  585 AGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIAS------RAKKGANFITVAAQYKEQLASLMATLET 658
Cdd:cd14904    474 AGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAPSetkegkSGKGTKAPKSLGSQFKTSLSQLMDNIKT 553
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  659 TNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAEDSQKATDAVL 738
Cdd:cd14904    554 TNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSKDVRRTCSVFMT 633
                          650       660
                   ....*....|....*....|
gi 1200169906  739 KHLNIDPEQYRFGITKIFFR 758
Cdd:cd14904    634 AIGRKSPLEYQIGKSLIYFK 653
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
111-758 8.90e-171

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: 516.64  E-value: 8.90e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITG 190
Cdd:cd14896      1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  191 ESGAGKTENTKKVIQYLASVaGRNQANGSGVLEQQILqanPILEAFGNAKTTRNNNSSRFGKFIEIQFNSaGFISGASIQ 270
Cdd:cd14896     81 HSGSGKTEAAKKIVQFLSSL-YQDQTEDRLRQPEDVL---PILESFGHAKTILNANASRFGQVLRLHLQH-GVIVGASVS 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  271 SYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDSEEFKITRQAMDIVGFSQE 350
Cdd:cd14896    156 HYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAE 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  351 EQMSIFKIIAGILHLGNIKF---EKGAGEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSS 427
Cdd:cd14896    236 ELTAIWAVLAAILQLGNICFsssERESQEVAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAID 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  428 SRDALVKALYGRLFLWLVKKINNVLCQERKAYF---IGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEE 504
Cdd:cd14896    316 ARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEEE 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  505 YLKEKINWTFIDfGLDSQATIDLIDGrQPPGILALLDEQSVFPNATDNTLITKLHSHFSkKNAKYEEPRFSKTEFGVTHY 584
Cdd:cd14896    396 CQRELLPWVPIP-QPPRESCLDLLVD-QPHSLLSILDDQTWLSQATDHTFLQKCHYHHG-DHPSYAKPQLPLPVFTVRHY 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  585 AGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIASRAKKGAnfITVAAQYKEQLASLMATLETTNPHFV 664
Cdd:cd14896    473 AGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGK--PTLASRFQQSLGDLTARLGRSHVYFI 550
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  665 RCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAEDSQKATDAVLKHLNID 744
Cdd:cd14896    551 HCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEALSDRERCGAILSQVLGAE 630
                          650
                   ....*....|....
gi 1200169906  745 PEQYRFGITKIFFR 758
Cdd:cd14896    631 SPLYHLGATKVLLK 644
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
116-758 2.03e-169

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: 514.19  E-value: 2.03e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  116 NLRVRYNQDLIYTYSGLFLVAVNPFKRIP-IYTQEMVDIFKGRRRN--------EVAPHIFAISDVAYRSMLDDRQNQSL 186
Cdd:cd14907      6 NLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENNKKQAI 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  187 LITGESGAGKTENTKKVIQYLASVAG---------------RNQANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFG 251
Cdd:cd14907     86 VISGESGAGKTENAKYAMKFLTQLSQqeqnseevltltssiRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSSRFG 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  252 KFIEIQFN-SAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFN---YLNQSGCVDIK 327
Cdd:cd14907    166 KYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSGDrydYLKKSNCYEVD 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  328 GVSDSEEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFEK---GAGEGAVLKDKTALNAASTVFGVNPSVLEKAL 404
Cdd:cd14907    246 TINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDstlDDNSPCCVKNKETLQIIAKLLGIDEEELKEAL 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  405 MEPRILAGRDLVAQHLNVEKSSSSRDALVKALYGRLFLWLVKKINNVLCQE---------RKAYFIGVLDISGFEIFKVN 475
Cdd:cd14907    326 TTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMPKdekdqqlfqNKYLSIGLLDIFGFEVFQNN 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  476 SFEQLCINYTNEKLQQFFNHHMFKLEQEEYLKEKINWTF--IDFgLDSQATIDLIDgRQPPGILALLDEQSVFPNATDNT 553
Cdd:cd14907    406 SFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLD-KPPIGIFNLLDDSCKLATGTDEK 483
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  554 LITKLHSHfSKKNAKYEEPR-FSKTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLF------NDP 626
Cdd:cd14907    484 LLNKIKKQ-HKNNSKLIFPNkINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFsgedgsQQQ 562
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  627 NIASRAKKGANFITVAAQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNR 706
Cdd:cd14907    563 NQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYR 642
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1200169906  707 IIYADFVKRYYLLApnvprdaedsqkatdavlkhlnidpEQYRFGITKIFFR 758
Cdd:cd14907    643 KSYEDFYKQYSLLK-------------------------KNVLFGKTKIFMK 669
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
113-731 4.93e-167

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: 506.38  E-value: 4.93e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  113 VFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIP-IYTQEMVDIF-----------KGRRRNEVAPHIFAISDVAYRSM--- 177
Cdd:cd14900      3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMmlg 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  178 -LDDRQNQSLLITGESGAGKTENTKKVIQYLASvAGRNQA--------NGSGVlEQQILQANPILEAFGNAKTTRNNNSS 248
Cdd:cd14900     83 lNGVMSDQSILVSGESGSGKTESTKFLMEYLAQ-AGDNNLaasvsmgkSTSGI-AAKVLQTNILLESFGNARTLRNDNSS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  249 RFGKFIEIQFNSAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKalhlagpesfnylnqsgcvdikg 328
Cdd:cd14900    161 RFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK----------------------- 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  329 vsdSEEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFEKGAGEGAVLKDKT--------ALNAASTVFGVNPSVL 400
Cdd:cd14900    218 ---RDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSdlapssiwSRDAAATLLSVDATKL 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  401 EKALMEPRILAGRDLVAQHLNVEKSSSSRDALVKALYGRLFLWLVKKIN------NVLCQERKAYFIGVLDISGFEIFKV 474
Cdd:cd14900    295 EKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNaflkmdDSSKSHGGLHFIGILDIFGFEVFPK 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  475 NSFEQLCINYTNEKLQQFFNHHMFKLEQEEYLKEKINWTFIDFGlDSQATIDLIDGRqPPGILALLDEQSVFPNATDNTL 554
Cdd:cd14900    375 NSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLISQR-PTGILSLIDEECVMPKGSDTTL 452
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  555 ITKLHSHFSkknakyEEPRFSKTE-------FGVTHYAGQVMYEIQDWLEKNKDPLQQDLelcfkdssdnvvtklfndpn 627
Cdd:cd14900    453 ASKLYRACG------SHPRFSASRiqrarglFTIVHYAGHVEYSTDGFLEKNKDVLHQEA-------------------- 506
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  628 iasrakkgANFITVAAQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRI 707
Cdd:cd14900    507 --------VDLFVYGLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRL 578
                          650       660
                   ....*....|....*....|....
gi 1200169906  708 IYADFVKRYYLLAPNVPRDAEDSQ 731
Cdd:cd14900    579 LHDEFVARYFSLARAKNRLLAKKQ 602
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
111-749 7.07e-163

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: 498.65  E-value: 7.07e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIP---------IYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLD-D 180
Cdd:cd14902      1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdlysesqlnAYKASMTSTSPVSQLSELPPHVFAIGGKAFGGLLKpE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  181 RQNQSLLITGESGAGKTENTKKVIQYLASVaGRNQA------NGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFI 254
Cdd:cd14902     81 RRNQSILVSGESGSGKTESTKFLMQFLTSV-GRDQSsteqegSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFI 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  255 EIQFNSAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKG----VS 330
Cdd:cd14902    160 KIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSYGPSFARKravaDK 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  331 DSEEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKF--EKGAGEGAVLKDKTA--LNAASTVFGVNPSVLEKALME 406
Cdd:cd14902    240 YAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFtaENGQEDATAVTAASRfhLAKCAELMGVDVDKLETLLSS 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  407 PRILAGRDLVAQHLNVEKSSSSRDALVKALYGRLFLWLVKKINNVLCQERKAYF----------IGVLDISGFEIFKVNS 476
Cdd:cd14902    320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSisdedeelatIGILDIFGFESLNRNG 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  477 FEQLCINYTNEKLQQFFNHHMFKLEQEEYLKEKINWTFIDFGlDSQATIDLIDGRqPPGILALLDEQSVFPNATDNTLIT 556
Cdd:cd14902    400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDK-SNGLFSLLDQECLMPKGSNQALST 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  557 KLHSHFSKKNakyeeprfsktEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIAS------ 630
Cdd:cd14902    478 KFYRYHGGLG-----------QFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRDSpgadng 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  631 ----RAKKGANFITVAAQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNR 706
Cdd:cd14902    547 aagrRRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVR 626
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|...
gi 1200169906  707 IIYADFVKRYYLLAPnvprdaedSQKATDAVLKHLNIDPEQYR 749
Cdd:cd14902    627 LAHASFIELFSGFKC--------FLSTRDRAAKMNNHDLAQAL 661
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
111-758 5.00e-157

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: 483.30  E-value: 5.00e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIP-IYTqemVDIFKGRRRNEVA--PHIFAISDVAYRSML-------DD 180
Cdd:cd14895      1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEMPGWTAlpPHVFSIAEGAYRSLRrrlhepgAS 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  181 RQNQSLLITGESGAGKTENTKKVIQYLASVAGRNQANGS-----GVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIE 255
Cdd:cd14895     78 KKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSskrrrAISGSELLSANPILESFGNARTLRNDNSSRFGKFVR 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  256 IQF-----NSAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAG--PESFNYLNQSGC-VDIK 327
Cdd:cd14895    158 MFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELlsAQEFQYISGGQCyQRND 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  328 GVSDSEEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFEKGAGEGAVLKDKTA-------------------LNA 388
Cdd:cd14895    238 GVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAAsapcrlasaspssltvqqhLDI 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  389 ASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSSRDALVKALYGRLFLWLVKKINNVLCQERKAY--------- 459
Cdd:cd14895    318 VSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALnpnkaankd 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  460 ---FIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYLKEKINWTFIDFGLDSqATIDLIDGRqPPGI 536
Cdd:cd14895    398 ttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNS-VCLEMLEQR-PSGI 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  537 LALLDEQSVFPNATDNTLITKL------HSHFSKKNAKYEEprfskTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELC 610
Cdd:cd14895    476 FSLLDEECVVPKGSDAGFARKLyqrlqeHSNFSASRTDQAD-----VAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSV 550
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  611 FKDSSDNVVTKLFnDPNIAS-------------RAKKGANFITVAAQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAK 677
Cdd:cd14895    551 LGKTSDAHLRELF-EFFKASesaelslgqpklrRRSSVLSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQ 629
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  678 LEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPnvprdaedSQKATD----AVLKHLNIDpeQYRFGIT 753
Cdd:cd14895    630 FDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVA--------AKNASDatasALIETLKVD--HAELGKT 699

                   ....*
gi 1200169906  754 KIFFR 758
Cdd:cd14895    700 RVFLR 704
PTZ00014 PTZ00014
myosin-A; Provisional
55-756 7.98e-156

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 483.76  E-value: 7.98e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   55 RDSYECGEIVSETSDSFTfktvdgqdrqVKKDDA-NQRNPIKFDGVEDMSELSYLNEPAVFHNLRVRYNQDLIYTYSGLF 133
Cdd:PTZ00014    63 GEKLTLKQIDPPTNSTFE----------VKPEHAfNANSQIDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPL 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  134 LVAVNPFKRIPIYTQEMVDIFK-GRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGESGAGKTENTKKVIQYLASVAG 212
Cdd:PTZ00014   133 LVAINPFKDLGNTTNDWIRRYRdAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASSKS 212
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  213 RNqanGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASIQSYLLEKSRVVFQSETERNYHIF 292
Cdd:PTZ00014   213 GN---MDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIF 289
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  293 YQLLAGATAEEKKALHLAGPESFNYLNqSGCVDIKGVSDSEEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFEK 372
Cdd:PTZ00014   290 YQLLKGANDEMKEKYKLKSLEEYKYIN-PKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEG 368
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  373 ----GAGEGAVL--KDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSSRDALVKALYGRLFLWLVK 446
Cdd:PTZ00014   369 keegGLTDAAAIsdESLEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIR 448
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  447 KINNVLCQERK-AYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYLKE-----KINWTfidfglD 520
Cdd:PTZ00014   449 NLNATIEPPGGfKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEgisteELEYT------S 522
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  521 SQATIDLIDGRQpPGILALLDEQSVFPNATDNTLITKLHSHFsKKNAKYEEPRFSKT-EFGVTHYAGQVMYEIQDWLEKN 599
Cdd:PTZ00014   523 NESVIDLLCGKG-KSVLSILEDQCLAPGGTDEKFVSSCNTNL-KNNPKYKPAKVDSNkNFVIKHTIGDIQYCASGFLFKN 600
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  600 KDPLQQDLELCFKDSSDNVVTKLFNDPNI-ASRAKKGaNFITvaAQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKL 678
Cdd:PTZ00014   601 KDVLRPELVEVVKASPNPLVRDLFEGVEVeKGKLAKG-QLIG--SQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDW 677
                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1200169906  679 EDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAE-DSQKATDAVLKHLNIDPEQYRFGITKIF 756
Cdd:PTZ00014   678 NSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSlDPKEKAEKLLERSGLPKDSYAIGKTMVF 756
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
113-756 4.34e-152

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: 468.56  E-value: 4.34e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  113 VFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIP-IYTQE-MVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQ--NQSLLI 188
Cdd:cd14880      3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPElMREYHAAPQPQKLKPHIFTVGEQTYRNVKSLIEpvNQSIVV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  189 TGESGAGKTENTKKVIQYLASVAG-RNQANGSGV---LEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFI 264
Cdd:cd14880     83 SGESGAGKTWTSRCLMKFYAVVAAsPTSWESHKIaerIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQM 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  265 SGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSgcvdiKGVSDSEEFKITRQAMDI 344
Cdd:cd14880    163 TGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNP-----ERNLEEDCFEVTREAMLH 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  345 VGFSQEEQMSIFKIIAGILHLGNIKFEKGAGEGA----VLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHL 420
Cdd:cd14880    238 LGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQpcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQQVFKK 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  421 NVEKS--SSSRDALVKALYGRLFLWLVKKINNVLCQERKAY--FIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHH 496
Cdd:cd14880    318 PCSRAecDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWttFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVAH 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  497 MFKLEQEEYLKEKINWTFIDFGlDSQATIDLIDGrQPPGILALLDEQSVFPNATDNTLI-TKLHSHFSkKNAKYEEPRFS 575
Cdd:cd14880    398 YLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIEG-SPISICSLINEECRLNRPSSAAQLqTRIESALA-GNPCLGHNKLS 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  576 KT-EFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLF-NDPNIAS----RAKKGANFITVAAQYKEQL 649
Cdd:cd14880    475 REpSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFpANPEEKTqeepSGQSRAPVLTVVSKFKASL 554
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  650 ASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAED 729
Cdd:cd14880    555 EQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLRRLRPHTSSG 634
                          650       660
                   ....*....|....*....|....*..
gi 1200169906  730 SQKATDAVLKhlnidPEQYRFGITKIF 756
Cdd:cd14880    635 PHSPYPAKGL-----SEPVHCGRTKVF 656
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
807-1080 2.16e-149

Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes interferon-induced Mx proteins that inhibit a wide range of viruses by blocking an early stage of the replication cycle. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206738  Cd Length: 278  Bit Score: 447.08  E-value: 2.16e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  807 LDLPQIVVVGSQSSGKSSVLENIVGRDFLPRGSGIVTRRPLILQLTHLPIADDGSQTQEWGEFLHKPNDMFYDFSEIREE 886
Cdd:cd08771      1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSPSESDEDEKEEWGEFLHLKSKEFTDFEELREE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  887 IIRDTDRMTGKNKGISAQPINLKIYSPHVVNLTLVDLPGITKVPVGDQPTDIEQQIRRMVMAYIKKQNAIIVAVTPANTD 966
Cdd:cd08771     81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  967 LANSDALQLAKEVDPEGKRTIGVITKLDLMDKGTDAMEVL---TGRVIPLTLGFIGVINRSQEDIIAKKSIRESLKSEIL 1043
Cdd:cd08771    161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1200169906 1044 YFKNHPIYKS-IANRSGTAYLSKTLNKLLMFHIRDTLP 1080
Cdd:cd08771    241 FFETHPWYKLlPASRVGTPALRKRLSKLLQKHIRESLP 278
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
113-732 1.99e-148

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: 460.99  E-value: 1.99e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  113 VFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIP-IYTQEMVDIFKGRRRN-EVAPHIFAISDVAYRSMLDDRQNQSLLITG 190
Cdd:cd14906      3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQNkSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  191 ESGAGKTENTKKVIQYLASVAGRNQA------NGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGF- 263
Cdd:cd14906     83 ESGSGKTEASKTILQYLINTSSSNQQqnnnnnNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSDGk 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  264 ISGASIQSYLLEKSRVVFQSETER-NYHIFYQLLAGATAEEKKALHL-AGPESFNYLNQSGCV-------------DIKG 328
Cdd:cd14906    163 IDGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLnNDPSKYRYLDARDDVissfksqssnknsNHNN 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  329 VSDSEE-FKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFEKGAGEGAVL----KDKTALNAASTVFGVNPSVLEKA 403
Cdd:cd14906    243 KTESIEsFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqkdKVTASLESVSKLLGYIESVFKQA 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  404 LMEPRILA-GRDLV-AQHLNVEKSSSSRDALVKALYGRLFLWLVKKINNVLCQ------------ERKAYFIGVLDISGF 469
Cdd:cd14906    323 LLNRNLKAgGRGSVyCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggsnKKNNLFIGVLDIFGF 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  470 EIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYLKEKINWTFIDFgLDSQATIDLIDgRQPPGILALLDEQSVFPNA 549
Cdd:cd14906    403 ENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIE-KKSDGILSLLDDECIMPKG 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  550 TDNTLITKLHSHFSKKNAKYEEPrFSKTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFN--DPN 627
Cdd:cd14906    481 SEQSLLEKYNKQYHNTNQYYQRT-LAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQqqITS 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  628 IASRAKKGANFITVAAQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRI 707
Cdd:cd14906    560 TTNTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRR 639
                          650       660
                   ....*....|....*....|....*
gi 1200169906  708 IYADFVKRYYLLAPNVPRDAEDSQK 732
Cdd:cd14906    640 DFNQFFSRYKCIVDMYNRKNNNNPK 664
MYSc_Myo14 cd14876
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...
111-756 1.37e-143

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: 445.97  E-value: 1.37e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDifkgRRRN-----EVAPHIFAISDVAYRSMLDDRQNQS 185
Cdd:cd14876      1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIR----KYRDapdltKLPPHVFYTARRALENLHGVNKSQT 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  186 LLITGESGAGKTENTKKVIQYLASVAGrnqANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFIS 265
Cdd:cd14876     77 IIVSGESGAGKTEATKQIMRYFASAKS---GNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIR 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  266 GASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSgCVDIKGVSDSEEFKITRQAMDIV 345
Cdd:cd14876    154 YGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPK-CLDVPGIDDVADFEEVLESLKSM 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  346 GFSQEEQMSIFKIIAGILHLGNIKFEK----GAGEGAVL--KDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQH 419
Cdd:cd14876    233 GLTEEQIDTVFSIVSGVLLLGNVKITGkteqGVDDAAAIsnESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGR 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  420 LNVEKSSSSRDALVKALYGRLFLWLVKKINNVLCQERK-AYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMF 498
Cdd:cd14876    313 WTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGfKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVF 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  499 KLEQEEYLKEKINWTFIDFgLDSQATIDLIDGRQpPGILALLDEQSVFPNATDNTLITKLHSHFsKKNAKYEEPRFSKT- 577
Cdd:cd14876    393 ERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKG-KSVLSILEDQCLAPGGSDEKFVSACVSKL-KSNGKFKPAKVDSNi 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  578 EFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIaSRAK--KGAnfiTVAAQYKEQLASLMAT 655
Cdd:cd14876    470 NFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVV-EKGKiaKGS---LIGSQFLKQLESLMGL 545
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  656 LETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAEDSQK-AT 734
Cdd:cd14876    546 INSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLGIANDKSLDPKvAA 625
                          650       660
                   ....*....|....*....|..
gi 1200169906  735 DAVLKHLNIDPEQYRFGITKIF 756
Cdd:cd14876    626 LKLLESSGLSEDEYAIGKTMVF 647
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
113-758 6.41e-139

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: 434.24  E-value: 6.41e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  113 VFHNLRVRYNQ-DLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNE-VAPHIFAISDVAYRSM-LDDRQNQSLLIT 189
Cdd:cd14875      3 LLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRlLPPHIWQVAHKAFNAIfVQGLGNQSVVIS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  190 GESGAGKTENTKKVIQYLASVAGRNQANGSgvlEQQILQ--------ANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSA 261
Cdd:cd14875     83 GESGSGKTENAKMLIAYLGQLSYMHSSNTS---QRSIADkidenlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  262 -GFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKAL-HLAGPESFNYLNQSGC-----VDIKGVSDSEE 334
Cdd:cd14875    160 sGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTfvrrgVDGKTLDDAHE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  335 FKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFEKGAGEGAVLKDKTALNAASTVFGVNPSVLEKALMeprILAGRD 414
Cdd:cd14875    240 FQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFLTACRLLQLDPAKLRECFL---VKSKTS 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  415 LVAQHLNVEKSSSSRDALVKALYGRLFLWLVKKINNVL-----CQERKayFIGVLDISGFEIFKVNSFEQLCINYTNEKL 489
Cdd:cd14875    317 LVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASItpqgdCSGCK--YIGLLDIFGFENFTRNSFEQLCINYANESL 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  490 QQFFNHHMFKLEQEEYLKEKINWTFIDFGlDSQATIDLIDGRQPpGILALLDEQSVFPNATDNTLITKLHSHFSKKNAKY 569
Cdd:cd14875    395 QNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDQKRT-GIFSMLDEECNFKGGTTERFTTNLWDQWANKSPYF 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  570 EEPRFS-KTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIASRAKKganfiTVAAQYKEQ 648
Cdd:cd14875    473 VLPKSTiPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARRKQ-----TVAIRFQRQ 547
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  649 LASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAE 728
Cdd:cd14875    548 LTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTASLF 627
                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 1200169906  729 DSQKATDAVLKHLNIDPEQYRF-------GITKIFFR 758
Cdd:cd14875    628 KQEKYSEAAKDFLAYYQRLYGWakpnyavGKTKVFLR 664
MYSc_Myo25 cd14886
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...
117-758 1.33e-131

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: 414.67  E-value: 1.33e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  117 LRVRYNQDLIYTYSGLFLVAVNPFKRIP-IYTQEMVDIFKGRRRN-----EVAPHIFAISDVAYRSMLDDRQNQSLLITG 190
Cdd:cd14886      7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  191 ESGAGKTENTKKVIQYLASvagrNQANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASIQ 270
Cdd:cd14886     87 ESGAGKTETAKQLMNFFAY----GHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGKIT 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  271 SYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDSEEFKITRQAMDIVgFSQE 350
Cdd:cd14886    163 SYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKL-FSKN 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  351 EQMSIFKIIAGILHLGNIKFEKgagEGAVLKDKTALNAASTVF-------GVNPSVLEKALMEPRILAGRDLVAQHLNVE 423
Cdd:cd14886    242 EIDSFYKCISGILLAGNIEFSE---EGDMGVINAAKISNDEDFgkmcellGIESSKAAQAIITKVVVINNETIISPVTQA 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  424 KSSSSRDALVKALYGRLFLWLVKKINNVLCQERKAY-FIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQ 502
Cdd:cd14886    319 QAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARpWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEI 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  503 EEYLKEKINWTFIDFGlDSQATIDLIDgRQPPGILALLDEQSVFPNATDNTLITKLHSHFskKNAKYEEPRFSKTEFGVT 582
Cdd:cd14886    399 QEYEIEGIDHSMITFT-DNSNVLAVFD-KPNLSIFSFLEEQCLIQTGSSEKFTSSCKSKI--KNNSFIPGKGSQCNFTIV 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  583 HYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIASRAKKGAnfiTVAAQYKEQLASLMATLETTNPH 662
Cdd:cd14886    475 HTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNMKGK---FLGSTFQLSIDQLMKTLSATKSH 551
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  663 FVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLL---APNVPRDAEDSQKATDAVLK 739
Cdd:cd14886    552 FIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishNSSSQNAGEDLVEAVKSILE 631
                          650
                   ....*....|....*....
gi 1200169906  740 HLNIDPEQYRFGITKIFFR 758
Cdd:cd14886    632 NLGIPCSDYRIGKTKVFLR 650
MYSc_Myo38 cd14899
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...
112-716 6.36e-131

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: 415.26  E-value: 6.36e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  112 AVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIP-IYTQEMVDIFKGRRRNEVA----------PHIFAISDVAYRSMLDD 180
Cdd:cd14899      2 SILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAYDHNSQFGdrvtstdprePHLFAVARAAYIDIVQN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  181 RQNQSLLITGESGAGKTENTKKVIQYLASVAG-------------RNQANGSGVLEQQILQANPILEAFGNAKTTRNNNS 247
Cdd:cd14899     82 GRSQSILISGESGAGKTEATKIIMTYFAVHCGtgnnnltnsesisPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDNS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  248 SRFGKFIEIQF-NSAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAG----ATAEEKKALHLAG-PESFNYLNQS 321
Cdd:cd14899    162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALSGgPQSFRLLNQS 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  322 GCVDIK-GVSDSEEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFEK--GAGEGAVLKDKTALNAAST------- 391
Cdd:cd14899    242 LCSKRRdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMSSTTgafdhft 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  392 ----VFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSSRDALVKALYGRLFLWLVKKINNVLC-------------- 453
Cdd:cd14899    322 kaaeLLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQrqasapwgadesdv 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  454 --QERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYLKEKINWTFIDFGlDSQATIDLIDGR 531
Cdd:cd14899    402 ddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEHR 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  532 qPPGILALLDEQSVFPNATDNTLITKLHSHFSKKNakyEEPRFSK-------TEFGVTHYAGQVMYEIQDWLEKNKD--- 601
Cdd:cd14899    481 -PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKN---SHPHFRSapliqrtTQFVVAHYAGCVTYTIDGFLAKNKDsfc 556
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  602 ------------PLQQDLELCFKDSSDNVVTKLFN-DPNIASRAKKGANFITVAAQYKEQLASLMATLETTNPHFVRCII 668
Cdd:cd14899    557 esaaqllagssnPLIQALAAGSNDEDANGDSELDGfGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIK 636
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*...
gi 1200169906  669 PNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRY 716
Cdd:cd14899    637 PNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
120-758 5.15e-130

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: 410.75  E-value: 5.15e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  120 RYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIF---KGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGESGAGK 196
Cdd:cd14878     10 RFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFILSGERGSGK 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  197 TENTKKVIQYLASVAGRNQAngsgVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQF-NSAGFISGASIQSYLLE 275
Cdd:cd14878     90 TEASKQIMKHLTCRASSSRT----TFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARIYTYMLE 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  276 KSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDS---EEFKITRQAMDIVGFSQEEQ 352
Cdd:cd14878    166 KSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMREDVSTAERSlnrEKLAVLKQALNVVGFSSLEV 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  353 MSIFKIIAGILHLGNIKFEK-GAGEGAVLKDKTALNAASTVFGVNPSVLEKALM-EPRILAGrDLVAQHLNVEKSSSSRD 430
Cdd:cd14878    246 ENLFVILSAILHLGDIRFTAlTEADSAFVSDLQLLEQVAGMLQVSTDELASALTtDIQYFKG-DMIIRRHTIQIAEFYRD 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  431 ALVKALYGRLFLWLVKKINNVLCQER-----KAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEY 505
Cdd:cd14878    325 LLAKSLYSRLFSFLVNTVNCCLQSQDeqksmQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQEQTEC 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  506 LKEKINWTFIdFGLDSQATIDLIDGRQPPGILALLDEQSVFPNATDNTLITKLHSHF--SKKNAKYEE---------PRF 574
Cdd:cd14878    405 VQEGVTMETA-YSPGNQTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLesSNTNAVYSPmkdgngnvaLKD 483
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  575 SKTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNdpniasrakkgANFITVAAQYKEQLASLMA 654
Cdd:cd14878    484 QGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ-----------SKLVTIASQLRKSLADIIG 552
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  655 TLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDaEDSQKAT 734
Cdd:cd14878    553 KLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLGE-KKKQSAE 631
                          650       660
                   ....*....|....*....|....*..
gi 1200169906  735 DA---VLKHLNIdpEQYRFGITKIFFR 758
Cdd:cd14878    632 ERcrlVLQQCKL--QGWQMGVRKVFLK 656
MYSc_Myo18 cd01386
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...
113-758 1.88e-127

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: 404.77  E-value: 1.88e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  113 VFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGES 192
Cdd:cd01386      3 VLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  193 GAGKTENTKKVIQYLASVAGrnqaNGSGVLEQQILQA-NPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASIQS 271
Cdd:cd01386     83 GSGKTTNCRHILEYLVTAAG----SVGGVLSVEKLNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQT 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  272 YLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLagpesfNYLNQSGCVDIKGVSDSEE-------FKITRQAMDI 344
Cdd:cd01386    159 LLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHL------NQLAESNSFGIVPLQKPEDkqkaaaaFSKLQAAMKT 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  345 VGFSQEEQMSIFKIIAGILHLGNIKFEKGAGEG-AVLKDKTALNAASTVFGVNPSVLEKAL----MEPRILAGRDLVAQH 419
Cdd:cd01386    233 LGISEEEQRAIWSILAAIYHLGAAGATKAASAGrKQFARPEWAQRAAYLLGCTLEELSSAIfkhhLSGGPQQSTTSSGQE 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  420 LNVEKSSSSR--------DALVKALYGRLFLWLVKKINNVLC-QERKAYFIGVLDISGFEifkvN----------SFEQL 480
Cdd:cd01386    313 SPARSSSGGPkltgvealEGFAAGLYSELFAAVVSLINRSLSsSHHSTSSITIVDTPGFQ----NpahsgsqrgaTFEDL 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  481 CINYTNEKLQQFFNHHMFKLEQEEYLKEKINWTFIDFGLDSQATIDLIDgrQPP---------------GILALLDEQSV 545
Cdd:cd01386    389 CHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALID--QAPqqalvrsdlrdedrrGLLWLLDEEAL 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  546 FPNATDNTLITKLHSHFSKKNAKYEEPRFSKTE----FGVTHYAGQ--VMYEIQDWLEKNK-DPLQQDLELCFKDSSDNV 618
Cdd:cd01386    467 YPGSSDDTFLERLFSHYGDKEGGKGHSLLRRSEgplqFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQESQKET 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  619 vtklfndpniASRAKKGanfitVAAQYKEQLASLMATLETTNPHFVRCIIPN-------NKQLPAKLEDKvVLD------ 685
Cdd:cd01386    547 ----------AAVKRKS-----PCLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagkdeRSTSSPAAGDE-LLDvpllrs 610
                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1200169906  686 QLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAE------DSQKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd01386    611 QLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevaDERKAVEELLEELDLEKSSYRIGLSQVFFR 689
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
108-757 2.50e-127

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: 403.08  E-value: 2.50e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  108 LNEPAVFHNLRVRYNQDLIYTYSGLF-LVAVNPFKRIPI--------YTQEMVDIFKGRRRnEVAPHIFAISDVAYRSML 178
Cdd:cd14879      1 PSDDAITSHLASRFRSDLPYTRLGSSaLVAVNPYKYLSSnsdaslgeYGSEYYDTTSGSKE-PLPPHAYDLAARAYLRMR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  179 DDRQNQSLLITGESGAGKTENTKKVIQYLASVAGRNQAngSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQF 258
Cdd:cd14879     80 RRSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKK--GTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQF 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  259 NSAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGC---VDIKGVSDSEEF 335
Cdd:cd14879    158 NERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYGChplPLGPGSDDAEGF 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  336 KITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFEK---GAGEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAG 412
Cdd:cd14879    238 QELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYdheGGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTYKTKLVR 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  413 RDLVAQHLNVEKSSSSRDALVKALYGRLFLWLVKKINNVLCQERK--AYFIGVLDISGFEIF---KVNSFEQLCINYTNE 487
Cdd:cd14879    318 KELCTVFLDPEGAAAQRDELARTLYSLLFAWVVETINQKLCAPEDdfATFISLLDFPGFQNRsstGGNSLDQFCVNFANE 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  488 KLQQFFNHHMFKLEQEEYLKEKINWTFIDFgLDSQATIDLIDGRqPPGILALLDEQ-SVFPNATDNTLITKLHSHFSKKN 566
Cdd:cd14879    398 RLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLRGK-PGGLLGILDDQtRRMPKKTDEQMLEALRKRFGNHS 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  567 AKYEEPRFS----KTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLelcfkdssdnvVTkLFNDpniasrakkganfitvA 642
Cdd:cd14879    476 SFIAVGNFAtrsgSASFTVNHYAGEVTYSVEGFLERNGDVLSPDF-----------VN-LLRG----------------A 527
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  643 AQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPn 722
Cdd:cd14879    528 TQLNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR- 606
                          650       660       670
                   ....*....|....*....|....*....|....*
gi 1200169906  723 vprdAEDSQKATDAVLKHLNIDPEQYRFGITKIFF 757
Cdd:cd14879    607 ----GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
786-1028 1.95e-114

Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the endocytic uptake of receptors, associated ligands, and plasma membrane following an exocytic event.


Pssm-ID: 197491  Cd Length: 240  Bit Score: 354.19  E-value: 1.95e-114
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   786 DQLIPVINKLQDVFNTLG-SDPLDLPQIVVVGSQSSGKSSVLENIVGRDFLPRGSGIVTRRPLILQLThlpiaddgSQTQ 864
Cdd:smart00053    2 EELIPLVNKLQDAFSALGqSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLI--------KSKT 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   865 EWGEFLHKPNDMFYDFSEIREEIIRDTDRMTGKNKGISAQPINLKIYSPHVVNLTLVDLPGITKVPVGDQPTDIEQQIRR 944
Cdd:smart00053   74 EYAEFLHCKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKK 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906   945 MVMAYIKKQNAIIVAVTPANTDLANSDALQLAKEVDPEGKRTIGVITKLDLMDKGTDAMEVLTGRVIPLTLGFIGVINRS 1024
Cdd:smart00053  154 MIKQFISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRS 233

                    ....
gi 1200169906  1025 QEDI 1028
Cdd:smart00053  234 QKDI 237
MYSc_Myo26 cd14887
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...
111-758 9.21e-112

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: 364.35  E-value: 9.21e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQ--------DLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQ 182
Cdd:cd14887      1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  183 NQSLLITGESGAGKTENTKKVIQYLASVAGRNQANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAG 262
Cdd:cd14887     81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  263 FISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALhLAGpESFNYlnqsgcvdikgvsdSEEFKITRQAM 342
Cdd:cd14887    161 KLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKS-SAG-EGDPE--------------STDLRRITAAM 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  343 DIVGFSQEEQMSIFKIIAGILHLGNIKFEKGAGEGAVLKDKTA-----------------------------------LN 387
Cdd:cd14887    225 KTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTsvsvgceetaadrshssevkclssglkvteasrkhLK 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  388 AASTVFGVNPSV-----LEKALMEPRILAGRdlvaQHLNVEKSSSSRDALVKALYGRLFLWLVKKINNVLCQE------- 455
Cdd:cd14887    305 TVARLLGLPPGVegeemLRLALVSRSVRETR----SFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSakpsesd 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  456 --------RKAYFIGVLDISGFEIFK---VNSFEQLCINYTNEKLQQFF------NHHMFKLeQEEYLKEKINWTF-IDF 517
Cdd:cd14887    381 sdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLleqlilNEHMLYT-QEGVFQNQDCSAFpFSF 459
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  518 GLDSQ------ATIDLI------------DGRQPPGILALL-DEQSVFPNATDNTLITKLHSHFSKKNA------KYEEP 572
Cdd:cd14887    460 PLASTltsspsSTSPFSptpsfrsssafaTSPSLPSSLSSLsSSLSSSPPVWEGRDNSDLFYEKLNKNIinsakyKNITP 539
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  573 RFSKT--EFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFkdSSDNVVTKLfndpnIASRAKKGANFI-----TVAAQY 645
Cdd:cd14887    540 ALSREnlEFTVSHFACDVTYDARDFCRANREATSDELERLF--LACSTYTRL-----VGSKKNSGVRAIssrrsTLSAQF 612
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  646 KEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPR 725
Cdd:cd14887    613 ASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALR 692
                          730       740       750
                   ....*....|....*....|....*....|...
gi 1200169906  726 DAEDSQKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14887    693 EALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
MYSc_Myo24A cd14937
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
113-758 7.64e-100

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: 329.28  E-value: 7.64e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  113 VFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEmvdiFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGES 192
Cdd:cd14937      3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  193 GAGKTENTKKVIQ-YLASVAGRNQangsgvLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASIQS 271
Cdd:cd14937     79 GSGKTEASKLVIKyYLSGVKEDNE------ISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEI 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  272 YLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYL-NQSgcVDIKGVSDSEEFKITRQAMDIVGFSQE 350
Cdd:cd14937    153 FLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIvNKN--VVIPEIDDAKDFGNLMISFDKMNMHDM 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  351 EQmSIFKIIAGILHLGNIKF---EKGAGEGAVLKDKTAL---NAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEK 424
Cdd:cd14937    231 KD-DLFLTLSGLLLLGNVEYqeiEKGGKTNCSELDKNNLelvNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEE 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  425 SSSSRDALVKALYGRLFLWLVKKINNVLCQERK-AYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQE 503
Cdd:cd14937    310 SVSICKSISKDLYNKIFSYITKRINNFLNNNKElNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETE 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  504 EYLKEKINWTFIDFgLDSQATIDLIDGRQppGILALLDEQSVFPNATDNTLITKLHSHFSkKNAKYEEPRFSKTE-FGVT 582
Cdd:cd14937    390 LYKAEDILIESVKY-TTNESIIDLLRGKT--SIISILEDSCLGPVKNDESIVSVYTNKFS-KHEKYASTKKDINKnFVIK 465
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  583 HYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIA-SRAKKgaNFITVaaQYKEQLASLMATLETTNP 661
Cdd:cd14937    466 HTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSeSLGRK--NLITF--KYLKNLNNIISYLKSTNI 541
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  662 HFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKgFPNRIIYADFVKRYYLLAPNVPRDAEDSQKATDAVLKHL 741
Cdd:cd14937    542 YFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNISFF-FQYKYTFDVFLSYFEYLDYSTSKDSSLTDKEKVSMILQN 620
                          650
                   ....*....|....*..
gi 1200169906  742 NIDPEQYRFGITKIFFR 758
Cdd:cd14937    621 TVDPDLYKVGKTMVFLK 637
MYSc_Myo44 cd14905
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...
117-758 1.77e-97

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: 323.97  E-value: 1.77e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  117 LRVRYNQDLIYTYSGLFLVAVNPFKRIP-IYTQEMVDIFKGRRrnEVAPHIFAISDVAYRSMLDDRQNQSLLITGESGAG 195
Cdd:cd14905      7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRR--GLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  196 KTENTKKVIQYLASVagrnQANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASIQSYLLE 275
Cdd:cd14905     85 KSENTKIIIQYLLTT----DLSRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  276 KSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDSEEFKITRQAMDIVGFSQEEQMSI 355
Cdd:cd14905    161 ENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLI 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  356 FKIIAGILHLGNIKFEKGAGEGAVlKDKTALNAASTVFGVNPSVLEKALMEPRilagrdlvaqHLNVEKSSSSRDALVKA 435
Cdd:cd14905    241 FKTLSFIIILGNVTFFQKNGKTEV-KDRTLIESLSHNITFDSTKLENILISDR----------SMPVNEAVENRDSLARS 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  436 LYGRLFLWLVKKINNVLCQERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYLKEKINW-TF 514
Cdd:cd14905    310 LYSALFHWIIDFLNSKLKPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQTERIPWmTP 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  515 IDFGlDSQATIDLIDgrqppGILALLDEQSVFPNATDNTLITKLHSHFSKKNAKYEEPrfskTEFGVTHYAGQVMYEIQD 594
Cdd:cd14905    390 ISFK-DNEESVEMME-----KIINLLDQESKNINSSDQIFLEKLQNFLSRHHLFGKKP----NKFGIEHYFGQFYYDVRG 459
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  595 WLEKNKDPLQQDLELCFKD-------SSDNV---------VTKLFNDPNIASRAKKGANFITVAAQYKE----------- 647
Cdd:cd14905    460 FIIKNRDEILQRTNVLHKNsitkylfSRDGVfninatvaeLNQMFDAKNTAKKSPLSIVKVLLSCGSNNpnnvnnpnnns 539
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  648 --------------QLASLMATLETTNP---------HFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFP 704
Cdd:cd14905    540 gggggggnsgggsgSGGSTYTTYSSTNKainnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYT 619
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1200169906  705 NRIIYADFVKRYYLLAPNVPRDAEDSQKATDAVLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14905    620 IHYNNKIFFDRFSFFFQNQRNFQNLFEKLKENDINIDSILPPPIQVGNTKIFLR 673
MYSc_Myo37 cd14898
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...
112-721 1.75e-95

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: 315.68  E-value: 1.75e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  112 AVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKgrrRNEVAPHIFAISDVAYRSMLDdRQNQSLLITGE 191
Cdd:cd14898      2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGAMKAYLKN---YSHVEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  192 SGAGKTENTKKVIQYLASvagRNQANGSgvLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNsaGFISGASIQS 271
Cdd:cd14898     78 SGSGKTENAKLVIKYLVE---RTASTTS--IEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFET 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  272 YLLEKSRVVFQSETERNYHIFYQLLAgataeeKKALHLAGpesfNYLNQSGCVDIKG--VSDSEEFKITRQAMDIVGFSQ 349
Cdd:cd14898    151 YLLEKSRVTHHEKGERNFHIFYQFCA------SKRLNIKN----DFIDTSSTAGNKEsiVQLSEKYKMTCSAMKSLGIAN 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  350 EEqmSIFKIIAGILHLGNIKFekgAGEG-AVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSS 428
Cdd:cd14898    221 FK--SIEDCLLGILYLGSIQF---VNDGiLKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTI 295
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  429 RDALVKALYGRLFLWLVKKINNVL-CQERKAyfIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYLK 507
Cdd:cd14898    296 RNSMARLLYSNVFNYITASINNCLeGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKE 373
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  508 EKINWTFIDFGLDSQATIDLidgRQPPGILALLDEQSVFPNATDNTLITKLHSHFSKknakyeeprFSKTEFG----VTH 583
Cdd:cd14898    374 EGIEWPDVEFFDNNQCIRDF---EKPCGLMDLISEESFNAWGNVKNLLVKIKKYLNG---------FINTKARdkikVSH 441
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  584 YAGQVMYEIQDWLEKNKDPLQqdlelcfkdssdnvvTKLFNDPNIASRAKKgANFITVaaqYKEQLASLMATLETTNPHF 663
Cdd:cd14898    442 YAGDVEYDLRDFLDKNREKGQ---------------LLIFKNLLINDEGSK-EDLVKY---FKDSMNKLLNSINETQAKY 502
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1200169906  664 VRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAP 721
Cdd:cd14898    503 IKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGI 560
MYSc_Myo23 cd14884
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ...
111-707 9.41e-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: 316.85  E-value: 9.41e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIP-IYTQEMVDIFKGRRRNEVA-------PHIFAISDVAYRSMLDDRQ 182
Cdd:cd14884      1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAAsaapfpkAHIYDIANMAYKNMRGKLK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  183 NQSLLITGESGAGKTENTKKVIQYLASVAGRNQANGsgvLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNS-- 260
Cdd:cd14884     81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTE---RIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEve 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  261 -------AGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEK---------KALHLAGPESFNYLNQ-SGC 323
Cdd:cd14884    158 ntqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLarrnlvrncGVYGLLNPDESHQKRSvKGT 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  324 VDIKGVS----------DSEEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNikfekgagegavlkdkTALNAASTVF 393
Cdd:cd14884    238 LRLGSDSldpseeekakDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGN----------------RAYKAAAECL 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  394 GVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSSRDALVKALYGRLFLWLVKKIN--NVLCQERKAY-----------F 460
Cdd:cd14884    302 QIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINrnVLKCKEKDESdnediysineaI 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  461 IGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYLKEKINWTFIDFGlDSQATIDLIDgrqppGILALL 540
Cdd:cd14884    382 ISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIA-----KIFRRL 455
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  541 DEQSVFPNA----TDNTLIT----------------------KLHSHFSKKNakyeepRFSKTEFGVTHYAGQVMYEIQD 594
Cdd:cd14884    456 DDITKLKNQgqkkTDDHFFRyllnnerqqqlegkvsygfvlnHDADGTAKKQ------NIKKNIFFIRHYAGLVTYRINN 529
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  595 WLEKNKDPLQQDLELCFKDSSDNVVTKLFNDpniasraKKGANFITVAAQYKEQLASLMATLETTNPHFVRCIIPNNKQL 674
Cdd:cd14884    530 WIDKNSDKIETSIETLISCSSNRFLREANNG-------GNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKML 602
                          650       660       670
                   ....*....|....*....|....*....|...
gi 1200169906  675 PAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRI 707
Cdd:cd14884    603 PNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKI 635
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
112-738 2.44e-93

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: 311.66  E-value: 2.44e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  112 AVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIP-----IYTQEMVDifkgrrrnevAPHIFAISDVAYRSMLDDRQNQSL 186
Cdd:cd14881      2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVGnpltlTSTRSSPL----------APQLLKVVQEAVRQQSETGYPQAI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  187 LITGESGAGKTENTKKVIQYLASVAGrnqangsGVLE----QQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFnSAG 262
Cdd:cd14881     72 ILSGTSGSGKTYASMLLLRQLFDVAG-------GGPEtdafKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDG 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  263 FISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAG--PESFNYLNQSGCVDiKGVSDSEEFKITRQ 340
Cdd:cd14881    144 ALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGysPANLRYLSHGDTRQ-NEAEDAARFQAWKA 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  341 AMDIVG--FSqeeqmSIFKIIAGILHLGNIKFEKGAGEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQ 418
Cdd:cd14881    223 CLGILGipFL-----DVVRVLAAVLLLGNVQFIDGGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKS 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  419 HLNVEKSSSSRDALVKALYGRLFLWLVKKINNVL----CQERKAY--FIGVLDISGFEIFKVNSFEQLCINYTNEKLQQF 492
Cdd:cd14881    298 VCDANMSNMTRDALAKALYCRTVATIVRRANSLKrlgsTLGTHATdgFIGILDMFGFEDPKPSQLEHLCINLCAETMQHF 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  493 FNHHMFKLEQEEYLKEKINwTFIDFG-LDSQATIDLIDGrQPPGILALLDeQSVFPNATDNTLITKLHSHfSKKNAKYEE 571
Cdd:cd14881    378 YNTHIFKSSIESCRDEGIQ-CEVEVDyVDNVPCIDLISS-LRTGLLSMLD-VECSPRGTAESYVAKIKVQ-HRQNPRLFE 453
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  572 PR-FSKTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVvtklfndpniasrakkgaNFITVAAQYKEQLA 650
Cdd:cd14881    454 AKpQDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF------------------GFATHTQDFHTRLD 515
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  651 SLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVP-RDAED 729
Cdd:cd14881    516 NLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLlRRVEE 595

                   ....*....
gi 1200169906  730 SQKATDAVL 738
Cdd:cd14881    596 KALEDCALI 604
MYSc_Myo12 cd14874
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...
112-758 4.95e-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: 274.83  E-value: 4.95e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  112 AVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFkgrrrnevapHIFAISDVAYRSMLDDRQN-QSLLITG 190
Cdd:cd14874      2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGG 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  191 ESGAGKTENTKKVIQYLASvagrnqANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSaGFISGASIQ 270
Cdd:cd14874     72 ESGSGKSYNAFQVFKYLTS------QPKSKVTTKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYKR-NVLTGLNLK 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  271 SYL-LEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDiKGVSDSEEFKITRQAMDIVGFSQ 349
Cdd:cd14874    145 YTVpLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTE-NIQSDVNHFKHLEDALHVLGFSD 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  350 EEQMSIFKIIAGILHLGNIKF--------EKGAGEgavLKDKTALNAASTVFGVNPSVLEKalmeprILAGRDLVAQHLN 421
Cdd:cd14874    224 DHCISIYKIISTILHIGNIYFrtkrnpnvEQDVVE---IGNMSEVKWVAFLLEVDFDQLVN------FLLPKSEDGTTID 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  422 VEKSSSSRDALVKALYGRLFLWLVKKINNVLCQERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLE 501
Cdd:cd14874    295 LNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQ 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  502 QEEYLKEKINwtfIDF----GLDSQATIDLIdGRQPPGILALLDEQSVFPNATDNTLITKLHSHFSKKNAKYEEPRFSKT 577
Cdd:cd14874    375 LVDYAKDGIS---VDYkvpnSIENGKTVELL-FKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARNKERL 450
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  578 EFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNdpNIASRAKKgaNFITVAAQYKEQLASLMATLE 657
Cdd:cd14874    451 EFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE--SYSSNTSD--MIVSQAQFILRGAQEIADKIN 526
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  658 TTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAP-NVPRDAEDSQKATDA 736
Cdd:cd14874    527 GSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLPgDIAMCQNEKEIIQDI 606
                          650       660
                   ....*....|....*....|..
gi 1200169906  737 VLKHLNIDPEQYRFGITKIFFR 758
Cdd:cd14874    607 LQGQGVKYENDFKIGTEYVFLR 628
MYSc_Myo21 cd14882
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...
117-758 7.99e-77

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: 266.22  E-value: 7.99e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  117 LRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGESGAGK 196
Cdd:cd14882      7 LRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGESYSGK 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  197 TENTKKVIQYLASVAGRNQANGsgvleQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASIQSYLLEK 276
Cdd:cd14882     87 TTNARLLIKHLCYLGDGNRGAT-----GRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQLEK 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  277 SRVVFQSETERNYHIFYQLLAGATAEEK-KALHLAGPESFNYLNQSGCVD---IKGVSDS-----EEFKITRQAMDIVGF 347
Cdd:cd14882    162 LRVSTTDGNQSNFHIFYYFYDFIEAQNRlKEYNLKAGRNYRYLRIPPEVPpskLKYRRDDpegnvERYKEFEEILKDLDF 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  348 SQEEQMSIFKIIAGILHLGNIKFEKGAGEgAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSS 427
Cdd:cd14882    242 NEEQLETVRKVLAAILNLGEIRFRQNGGY-AELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRKHTTEEARD 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  428 SRDALVKALYGRLFLWLVKKINNVLCQERKAY----FIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQE 503
Cdd:cd14882    321 ARDVLASTLYSRLVDWIINRINMKMSFPRAVFgdkySISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHYNQRIFISEML 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  504 EYLKEKINWTFIDFgLDSQATIDLIDGRqPPGILALLDEQSVFPNATDNTL--ITKLHSHFSKKNakyeeprfSKTEFGV 581
Cdd:cd14882    401 EMEEEDIPTINLRF-YDNKTAVDQLMTK-PDGLFYIIDDASRSCQDQNYIMdrIKEKHSQFVKKH--------SAHEFSV 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  582 THYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIasrakkgANFITVAAQYK----EQLASLMATLE 657
Cdd:cd14882    471 AHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQV-------RNMRTLAATFRatslELLKMLSIGAN 543
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  658 TTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAEDSQKATDAV 737
Cdd:cd14882    544 SGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLAFDFDETVEMTKDNCRLL 623
                          650       660
                   ....*....|....*....|.
gi 1200169906  738 LKHLNIdpEQYRFGITKIFFR 758
Cdd:cd14882    624 LIRLKM--EGWAIGKTKVFLK 642
MYSc_Myo32 cd14893
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...
114-716 6.37e-74

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: 260.67  E-value: 6.37e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  114 FHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYT----------QEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQN 183
Cdd:cd14893      4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTpdhmqaynksREQTPLYEKDTVNDAPPHVFALAQNALRCMQDAGED 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  184 QSLLITGESGAGKTENTKKVIQYLA----SVAGRNQANG-SGVLE---QQILQANPILEAFGNAKTTRNNNSSRFGKFIE 255
Cdd:cd14893     84 QAVILLGGMGAGKSEAAKLIVQYLCeigdETEPRPDSEGaSGVLHpigQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  256 IQFNSAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEE--KKALHL-AGPESFNYLNQSGCVDIKGVSDS 332
Cdd:cd14893    164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDPtlRDSLEMnKCVNEFVMLKQADPLATNFALDA 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  333 EEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKF----EKGAGEGA------------VLKDKTALNAASTVFGVN 396
Cdd:cd14893    244 RDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpEGGKSVGGansttvsdaqscALKDPAQILLAAKLLEVE 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  397 PSVLEKALMEPRILA--GRDLVA--QHLNVEKSSSSRDALVKALYGRLFLWLVKKINNVLCQERKAYF----------IG 462
Cdd:cd14893    324 PVVLDNYFRTRQFFSkdGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRYEksnivinsqgVH 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  463 VLDISGFEIF--KVNSFEQLCINYTNEKLQQFF-------NHHMFKLEQEEYLKEKINWTFIDFGLDSQATIDLIDgRQP 533
Cdd:cd14893    404 VLDMVGFENLtpSQNSFDQLCFNYWSEKVHHFYvqntlaiNFSFLEDESQQVENRLTVNSNVDITSEQEKCLQLFE-DKP 482
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  534 PGILALLDEQSVFPNATDNTLITKLHS--------HFSKKNAKYEEPRFSKTE-----FGVTHYAGQVMYEIQDWLEKNK 600
Cdd:cd14893    483 FGIFDLLTENCKVRLPNDEDFVNKLFSgneavgglSRPNMGADTTNEYLAPSKdwrllFIVQHHCGKVTYNGKGLSSKNM 562
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  601 DPLQQDLELCFKDSSDNVVTKLFNDPNIASRAKKGA--------------NFITVAAQYKE-----------QLASLMAT 655
Cdd:cd14893    563 LSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKAAkqteergstsskfrKSASSARESKNitdsaatdvynQADALLHA 642
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1200169906  656 LETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRY 716
Cdd:cd14893    643 LNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY 703
Dynamin_N pfam00350
Dynamin family;
812-993 3.50e-70

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 231.35  E-value: 3.50e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  812 IVVVGSQSSGKSSVLENIVGRDFLPRGSGIVTRRPLILQLTHLPIADDGSQTQEWGEFlhkpNDMFYDFSEIREEIIRDT 891
Cdd:pfam00350    1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESPGASEGAVKVEYKDG----EKKFEDFSELREEIEKET 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  892 DRMTGKNKGISAQPINLKIYSPHVVNLTLVDLPGITKVPVGDQptdieqqirRMVMAYIKKqNAIIVAVTPANTDLANSD 971
Cdd:pfam00350   77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYIKP-ADIILAVTPANVDLSTSE 146
                          170       180
                   ....*....|....*....|..
gi 1200169906  972 ALQLAKEVDPEGKRTIGVITKL 993
Cdd:pfam00350  147 ALFLAREVDPNGKRTIGVLTKA 168
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
133-263 9.87e-57

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: 193.72  E-value: 9.87e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  133 FLVAVNPFKRIPIYTQEMVDIF-KGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGESGAGKTENTKKVIQYLASVA 211
Cdd:cd01363      1 VLVRVNPFKELPIYRDSKIIVFyRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1200169906  212 GRNQANGS-----------GVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGF 263
Cdd:cd01363     81 FNGINKGEtegwvylteitVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
MYSc_Myo24B cd14938
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
111-756 1.38e-48

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: 185.42  E-value: 1.38e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  111 PAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFK-GRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLIT 189
Cdd:cd14938      1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIIS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  190 GESGAGKTENTKKVIQYLASVAGRNQANGSGVLEQQ-------------------ILQANPILEAFGNAKTTRNNNSSRF 250
Cdd:cd14938     81 GESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEednihneentdyqfnmsemLKHVNVVMEAFGNAKTVKNNNSSRF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  251 GKFIEIQFNSAGfISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDiKGVS 330
Cdd:cd14938    161 SKFCTIHIENEE-IKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFE-KFSD 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  331 DSEEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIK----------FEKGAGEGAVLKDKTALNA------------ 388
Cdd:cd14938    239 YSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEivkafrkkslLMGKNQCGQNINYETILSElensediglden 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  389 ------ASTVFGVNPSVLEKALMEPRILAGRDLVAQHlNVEKSSSSRDALVKALYGRLFLWLVKKINNVLCQERK----A 458
Cdd:cd14938    319 vknlllACKLLSFDIETFVKYFTTNYIFNDSILIKVH-NETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNininT 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  459 YFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYLKEKINWTFIDFGLDSQATIDLIDGRQPPGILA 538
Cdd:cd14938    398 NYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTEGSLFS 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  539 LLDEQS---VFPNATDNTLITKLHSHFSKKNAKYEEPRFSKTeFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSS 615
Cdd:cd14938    478 LLENVStktIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSE 556
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  616 DNVVTKLF------NDPNIASRAKK---GANFITVAAQY--KEQLA---------SLMATLETTNPHFVRCIIPN-NKQL 674
Cdd:cd14938    557 NEYMRQFCmfynydNSGNIVEEKRRysiQSALKLFKRRYdtKNQMAvsllrnnltELEKLQETTFCHFIVCMKPNeSKRE 636
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  675 PAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLapnvprdAEDSQKATDAVLKHLNIDPEQYRFGITK 754
Cdd:cd14938    637 LCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIK-------NEDLKEKVEALIKSYQISNYEWMIGNNM 709

                   ..
gi 1200169906  755 IF 756
Cdd:cd14938    710 IF 711
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
1001-1100 2.59e-42

Dynamin central region; This is the stalk region which lies between the GTPase domain, see pfam00350, and the pleckstrin homology (PH) domain, see pfam00169. This region dimerizes in a cross-like fashion forming a dynamin dimer in which the two G-domains are oriented in opposite directions.


Pssm-ID: 460033  Cd Length: 287  Bit Score: 156.52  E-value: 2.59e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906 1001 DAMEVLTGRVIPLTLGFIGVINRSQEDIIAKKSIRESLKSEILYFKNHPIYKSIANRSGTAYLSKTLNKLLMFHIRDTLP 1080
Cdd:pfam01031    1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80
                           90       100
                   ....*....|....*....|
gi 1200169906 1081 DLKVKVSKMLSDVQGELSTY 1100
Cdd:pfam01031   81 DLKNKINELLQKTEKELEKY 100
MYSc_Myo33 cd14894
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...
117-700 3.14e-34

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: 142.19  E-value: 3.14e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  117 LRVRYNQDLIYTYSGLFLVAV-NPFKRI------PIYTQEMVDIFKGRRRNE--VAPHIFAISDVAY------------- 174
Cdd:cd14894      7 LTSRFDDDRIYTYINHHTMAVmNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKQSLvrlffdnehtmpl 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  175 -------RSMLDDRqNQSLLITGESGAGKTENTKKVIQYLASVAGRNQANGS---------------------------- 219
Cdd:cd14894     87 pstissnRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAQPALSKGSeetckvsgstrqpkiklftsstkstiqm 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  220 --------GVLEQQ------------------------------------------------------------------ 225
Cdd:cd14894    166 rteeartiALLEAKgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyeklehledeeqlrmyfknphaakk 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  226 ---ILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFnSAGF------ISGASIQSYLLEKSRVVFQ------SETERNYH 290
Cdd:cd14894    246 lsiVLDSNIVLEAFGHATTSMNLNSSRFGKMTTLQV-AFGLhpwefqICGCHISPFLLEKSRVTSErgresgDQNELNFH 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  291 IFYQLLAGATAEE-----KKALHLAGPE--SFNYLNQS-----GCVDIKGV--SDSEEFKITRQAMDIVGFSQEEQMSIF 356
Cdd:cd14894    325 ILYAMVAGVNAFPfmrllAKELHLDGIDcsALTYLGRSdhklaGFVSKEDTwkKDVERWQQVIDGLDELNVSPDEQKTIF 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  357 KIIAGILHLGNIKFEKGAGEGAVLKDKT-ALNAASTVFGV----NPSVLEKALMEPRILAGRDLVAQHLNVEKSSSS--R 429
Cdd:cd14894    405 KVLSAVLWLGNIELDYREVSGKLVMSSTgALNAPQKVVELlelgSVEKLERMLMTKSVSLQSTSETFEVTLEKGQVNhvR 484
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  430 DALVKALYGRLFLWLVKKINNVL------------------CQERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQ 491
Cdd:cd14894    485 DTLARLLYQLAFNYVVFVMNEATkmsalstdgnkhqmdsnaSAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYA 564
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  492 ffnhhmfklEQEEYLKEKINWTFIDFGLDSQATIDLIdGRQPPGILALLDE-----QSVFPNATDNTLITKL--HSHFSK 564
Cdd:cd14894    565 ---------REEQVIAVAYSSRPHLTARDSEKDVLFI-YEHPLGVFASLEEltilhQSENMNAQQEEKRNKLfvRNIYDR 634
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  565 KNAKYEEPR-------------FSKTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFND------ 625
Cdd:cd14894    635 NSSRLPEPPrvlsnakrhtpvlLNVLPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNEssqlgw 714
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200169906  626 -PN-----IASRAKKGANFITVAAQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRIT 699
Cdd:cd14894    715 sPNtnrsmLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEIC 794

                   .
gi 1200169906  700 R 700
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 ...
41-87 1.56e-10

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: 460670  Cd Length: 45  Bit Score: 57.06  E-value: 1.56e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1200169906   41 SDKRYIWYnPDPKErdSYECGEIVSETSDSFTFKTVDGQDRQVKKDD 87
Cdd:pfam02736    1 DAKKLVWV-PDPKE--GFVKGEIKEEEGDKVTVETEDGKTVTVKKDD 44
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
645-669 4.14e-05

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: 45.41  E-value: 4.14e-05
                           10        20
                   ....*....|....*....|....*
gi 1200169906  645 YKEQLASLMATLETTNPHFVRCIIP 669
Cdd:cd01363    146 INESLNTLMNVLRATRPHFVRCISP 170
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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