NCBI Conserved Domain Search

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

871-1044

2.25e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 2.25e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  871 RQKLAKREfRKLKQVANEAGALRLAKTKLEKRLEDLEWRLQlEKRLRTSGEEAKSSEISK----LQKTLESFSLKLDAAR 946
Cdd:TIGR02168  781 EAEIEELE-AQIEQLKEELKALREALDELRAELTLLNEEAA-NLRERLESLERRIAATERrledLEEQIEELSEDIESLA 858

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  947 LAtINECNKN-AVLEKQLDISMKEKSAVERELngmvelkkdnALLKNSMNSLEKKNRVLEKELLNAKTNCNNTLQKLKEA 1025
Cdd:TIGR02168  859 AE-IEELEELiEELESELEALLNERASLEEAL----------ALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927

                          170
                   ....*....|....*....
gi 1063726492 1026 EKRCSELQTSVQSLEEKLS 1044
Cdd:TIGR02168  928 ELRLEGLEVRIDNLQERLS 946

Myosin_N

pfam02736

Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ...

17-56

9.26e-06

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: 43.96 E-value: 9.26e-06

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1063726492   17 VWVEDKDLAWIAADVLDSFDNKLHVETSTGKKVFVSPEKL 56
Cdd:pfam02736    6 VWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

872-1059

2.11e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 2.11e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  872 QKLAKREFRKLKQVANEAGALRLAKTKLEKRLEDLEwRLQLEKRLRTSGEEAKSSEISKLQKTLESFSLKLDAARlATIN 951
Cdd:COG4372      6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELD-KLQEELEQLREELEQAREELEQLEEELEQARSELEQLE-EELE 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  952 EcnknavLEKQLDISMKEKSAVERELNgmvELKKDNALLKNSMNSLEKKNRVLEKELLNAKTNCNNTLQKLKEAEKRCSE 1031
Cdd:COG4372     84 E------LNEQLQAAQAELAQAQEELE---SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE 154

                          170       180
                   ....*....|....*....|....*...
gi 1063726492 1032 LQTSVQSLEEKLSHLENENQVLMQKTLI 1059
Cdd:COG4372    155 LEEQLESLQEELAALEQELQALSEAEAE 182

STAT5_CCD

cd16855

Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...

911-1061

5.20e-04

Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.

Pssm-ID: 341080 [Multi-domain] Cd Length: 194 Bit Score: 43.02 E-value: 5.20e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  911 QLEKRLRTSGEEaksseISKLQKTLESF------SLKLDA--ARLATiNECNKNAVLEKQLdisMKEKSAVERELNGMVe 982
Cdd:cd16855     12 ELRQRTQETEND-----LRNLQQKQESFviqyqeSQKIQAqlQQLQQ-QPQNERIELEQQL---QQQKEQLEQLLNAKA- 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  983 lkkdNALLKNSMNSLEK-----------KNRVLEKELL----------NAKTNCNN-----------------TLQKLKE 1024
Cdd:cd16855     82 ----QELLQLRMELADKfkktiqllsklQSRVLDEELIqwkrqqqlagNGAPFESNldtiqewceslaeiiwqNRQQIKR 157

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1063726492 1025 AEKRCSELQTSV-QSLEEKLSHLENENQVLMqKTLITS 1061
Cdd:cd16855    158 AERLKQKLPIPLpPEQKDMLPILNKQITDLL-SSLVTS 194

IQCD

cd23767

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...

834-862

1.99e-03

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.

Pssm-ID: 467745 [Multi-domain] Cd Length: 37 Bit Score: 37.14 E-value: 1.99e-03

                           10        20
                   ....*....|....*....|....*....
gi 1063726492  834 QKEHRAASLIQAHWRIHKFRSAFRHRQSS 862
Cdd:cd23767      6 QRMNRAATLIQALWRGYKVRKELKKKKKK 34

Name

Accession

Description

Interval

E-value

MYSc_Myo11

cd01384

class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...

81-725

0e+00

Pssm-ID: 276835 Cd Length: 647 Bit Score: 1309.58 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPHLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS 160
Cdd:cd01384      1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPHLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  161 GESGAGKTETTKLIMQYLTFVGGRATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAAIR 240
Cdd:cd01384     81 GESGAGKTETTKMLMQYLAYMGGRAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  241 TYLLERSRVVRITDPERNYHCFYQLC--ASGNDAEKYKLSNPRQFHYLNQSKTYELEGVSSAEEYKNTRRAMDIVGISQD 318
Cdd:cd01384    161 TYLLERSRVVQVSDPERNYHCFYQLCagAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISEE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  319 EQEGIFRTLAAILHLGNVEFSSGREHDSSVVKDPESRHHLQMAADLFKCDANLLLASLCTRSILTREGIIIKALDPNAAV 398
Cdd:cd01384    241 EQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAAT 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  399 TSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKMEQDEY 478
Cdd:cd01384    321 LSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEEY 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  479 RKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKPKFSETDFTLSHYAGKV 558
Cdd:cd01384    401 TKEEIDWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPKLSRTDFTIDHYAGDV 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  559 TYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSAPEESTRSSYKFSSVSSRFKQQLQALMETLSKTEPHYVRCVKP 638
Cdd:cd01384    481 TYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREGTSSSSKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKP 560

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  639 NSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMDESNDEQALTEKILSKLGLGNYQLG 718
Cdd:cd01384    561 NNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVLKGSDDEKAACKKILEKAGLKGYQIG 640


                   ....*..
gi 1063726492  719 RTKVFLR 725
Cdd:cd01384    641 KTKVFLR 647

MYSc

smart00242

Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...

65-736

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: 984.35 E-value: 0e+00

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492    65 EHNGVDDMTKLTYLHEAGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVA 144
Cdd:smart00242    4 KFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLP-IYTDEVIKKYRGKSRGELPPHVFAIADNA 82

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   145 YRAMIDDSRSQSILVSGESGAGKTETTKLIMQYLTFVGGRaTDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFV 224
Cdd:smart00242   83 YRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGS-NTEVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKFI 161

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   225 EIQFDTNGRISGAAIRTYLLERSRVVRITDPERNYHCFYQLCASGNDAEK--YKLSNPRQFHYLNQSKTYELEGVSSAEE 302
Cdd:smart00242  162 EIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKkeLGLKSPEDYRYLNQGGCLTVDGIDDAEE 241

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   303 YKNTRRAMDIVGISQDEQEGIFRTLAAILHLGNVEFSSGR-EHDSSVVKDPEsrhHLQMAADLFKCDANLLLASLCTRSI 381
Cdd:smart00242  242 FKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRnDNAASTVKDKE---ELSNAAELLGVDPEELEKALTKRKI 318

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   382 LTREGIIIKALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEK 461
Cdd:smart00242  319 KTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEK 398

                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   462 LQQHFNEHVFKMEQDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEK 541
Cdd:smart00242  399 LQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFSK 478

                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   542 P-KFSETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSApEESTRSSYKFSSVSSRFKQQLQA 620
Cdd:smart00242  479 PkKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG-VSNAGSKKRFQTVGSQFKEQLNE 557

                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   621 LMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFM-DESNDE 699
Cdd:smart00242  558 LMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWpPWGGDA 637

                           650       660       670
                    ....*....|....*....|....*....|....*....
gi 1063726492   700 QALTEKILSKLGL--GNYQLGRTKVFLRAGQIGILDSRR 736
Cdd:smart00242  638 KKACEALLQSLGLdeDEYQLGKTKVFLRPGQLAELEELR 676

MYSc

cd00124

Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...

81-725

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: 890.02 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFG-ELSPHVFAVSDVAYRAMIDDSRSQSILV 159
Cdd:cd00124      1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLP-LYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  160 SGESGAGKTETTKLIMQYLTFVGGRATDDDR----SVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRIS 235
Cdd:cd00124     80 SGESGAGKTETTKLVLKYLAALSGSGSSKSSssasSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  236 GAAIRTYLLERSRVVRITDPERNYHCFYQLCASGNDAEK------YKLSNPRQFHYLNQSKTYELEGVSSAEEYKNTRRA 309
Cdd:cd00124    160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAReelkleLLLSYYYLNDYLNSSGCDRIDGVDDAEEFQELLDA 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  310 MDIVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSVVkDPESRHHLQMAADLFKCDANLLLASLCTRSILTREGIII 389
Cdd:cd00124    240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEDSSA-EVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETIT 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  390 KALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQ--IGVLDIYGFECFKNNSFEQFCINFANEKLQQHFN 467
Cdd:cd00124    319 KPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAESTsfIGILDIFGFENFEVNSFEQLCINYANEKLQQFFN 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  468 EHVFKMEQDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRL-EKPKFSE 546
Cdd:cd00124    399 QHVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFfSKKRKAK 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  547 TDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKcpfvagifpsapeestrssykfssvssRFKQQLQALMETLS 626
Cdd:cd00124    479 LEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS---------------------------QFRSQLDALMDTLN 531

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  627 KTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFM---DESNDEQALT 703
Cdd:cd00124    532 STQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATekaSDSKKAAVLA 611

                          650       660
                   ....*....|....*....|..
gi 1063726492  704 EKILSKLGLGNYQLGRTKVFLR 725
Cdd:cd00124    612 LLLLLKLDSSGYQLGKTKVFLR 633

COG5022

Myosin heavy chain [General function prediction only];

10-1073

0e+00

Myosin heavy chain [General function prediction only];

Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 875.94 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   10 NLRKGDKVWVEDKDLAWIAADVLDSFDNK----LHVETSTGKKVFVSPEKL--FRRDPDDEEhnGVDDMTKLTYLHEAGV 83
Cdd:COG5022      5 NAEVGSGCWIPDEEKGWIWAEIIKEAFNKgkvtEEGKKEDGESVSVKKKVLgnDRIKLPKFD--GVDDLTELSYLNEPAV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   84 LYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVSGES 163
Cdd:COG5022     83 LHNLEKRYNNGQIYTYSGLVLIAVNPYRDLG-IYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGES 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  164 GAGKTETTKLIMQYLTFVGGRATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAAIRTYL 243
Cdd:COG5022    162 GAGKTENAKRIMQYLASVTSSSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYL 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  244 LERSRVVRITDPERNYHCFYQLCASgnDAEKYK----LSNPRQFHYLNQSKTYELEGVSSAEEYKNTRRAMDIVGISQDE 319
Cdd:COG5022    242 LEKSRVVHQNKNERNYHIFYQLLAG--DPEELKklllLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEE 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  320 QEGIFRTLAAILHLGNVEFSSGREHDSSVVKDPEsrhhLQMAADLFKCDANLLLASLCTRSILTREGIIIKALDPNAAVT 399
Cdd:COG5022    320 QDQIFKILAAILHIGNIEFKEDRNGAAIFSDNSV----LDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALA 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  400 SRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKMEQDEYR 479
Cdd:COG5022    396 IRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYV 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  480 KEEINWSYIEFIDNQDVLDLIEKK-PIGVIALLDEACMFPRSTHESFSMKLFQNFRFH--PRLEKPKFSETDFTLSHYAG 556
Cdd:COG5022    476 KEGIEWSFIDYFDNQPCIDLIEKKnPLGILSLLDEECVMPHATDESFTSKLAQRLNKNsnPKFKKSRFRDNKFVVKHYAG 555

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  557 KVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSAPEESTRssYKFSSVSSRFKQQLQALMETLSKTEPHYVRCV 636
Cdd:COG5022    556 DVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIESK--GRFPTLGSRFKESLNSLMSTLNSTQPHYIRCI 633

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  637 KPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFM---DESNDEQAL--TEKILSKLG 711
Cdd:COG5022    634 KPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSwtgEYTWKEDTKnaVKSILEELV 713

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  712 L--GNYQLGRTKVFLRAGQIGILDSRRAEVLDASARLIQRRLRTFVTHQNFISARASAISIQAYCRGCLSRNAYATRRNA 789
Cdd:COG5022    714 IdsSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKW 793

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  790 AAAVLVQKHVRRWLSRCAFVKLVSAAIVLQ-SCIRADSTRLKFSHQKEHRAASLIQAHWRIHKFRSAFRHRQSSIIAIQC 868
Cdd:COG5022    794 RLFIKLQPLLSLLGSRKEYRSYLACIIKLQkTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQS 873

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  869 RWRQKLAKREFRKLKQVANEAGALRLAKTKLEKRLEDLEWRLQLEKRLRTsgeEAKSSEISKLQKTLESFSLKLdaarla 948
Cdd:COG5022    874 AQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENL---EFKTELIARLKKLLNNIDLEE------ 944

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  949 tinecnknavlekQLDISMKEKSAVERELNGMVELKKDNALLKNSMNSLEKknrvLEKELLNAKTNCNNTLQKLKEAEKR 1028
Cdd:COG5022    945 -------------GPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTI----LVREGNKANSELKNFKKELAELSKQ 1007

                         1050      1060      1070      1080
                   ....*....|....*....|....*....|....*....|....*
gi 1063726492 1029 CSELQTSVQSLEEKLSHLENENQVlmQKTLITSPERIGQILGEQK 1073
Cdd:COG5022   1008 YGALQESTKQLKELPVEVAELQSA--SKIISSESTELSILKPLQK 1050

Myosin_head

pfam00063

Myosin head (motor domain);

69-725

0e+00

Myosin head (motor domain);

Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 849.65 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   69 VDDMTKLTYLHEAGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAM 148
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLP-IYSEDMIKAYRGKRRGELPPHIFAIADEAYRSM 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  149 IDDSRSQSILVSGESGAGKTETTKLIMQYLTFVGGRATDDDR-SVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQ 227
Cdd:pfam00063   80 LQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNVgRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQ 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  228 FDTNGRISGAAIRTYLLERSRVVRITDPERNYHCFYQLCAsGNDAE---KYKLSNPRQFHYLNQSKTYELEGVSSAEEYK 304
Cdd:pfam00063  160 FDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLA-GASAQlkkELRLTNPKDYHYLSQSGCYTIDGIDDSEEFK 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  305 NTRRAMDIVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSVVKDPESrhhLQMAADLFKCDANLLLASLCTRSILTR 384
Cdd:pfam00063  239 ITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTEN---LQKAASLLGIDSTELEKALCKRRIKTG 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  385 EGIIIKALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQ-DPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQ 463
Cdd:pfam00063  316 RETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVkTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQ 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  464 QHFNEHVFKMEQDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKPK 543
Cdd:pfam00063  396 QFFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQKPR 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  544 -FSETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSAPEESTRSSYKFSSVSS---------- 612
Cdd:pfam00063  476 lQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTPkrtkkkrfit 555

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  613 ---RFKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLA 689
Cdd:pfam00063  556 vgsQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILA 635

                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 1063726492  690 PEFMDESN-DEQALTEKILSKLGL--GNYQLGRTKVFLR 725
Cdd:pfam00063  636 PKTWPKWKgDAKKGCEAILQSLNLdkEEYQFGKTKIFFR 674

MYSc_Myo5

cd01380

class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...

83-725

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: 820.63 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   83 VLYNLQRRYA-LNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVSG 161
Cdd:cd01380      3 VLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLP-IYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  162 ESGAGKTETTKLIMQYLTFVGGrATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAAIRT 241
Cdd:cd01380     82 ESGAGKTVSAKYAMRYFATVGG-SSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  242 YLLERSRVVRITDPERNYHCFYQLCASGNDAE--KYKLSNPRQFHYLNQSKTYELEGVSSAEEYKNTRRAMDIVGISQDE 319
Cdd:cd01380    161 YLLEKSRVVFQAEEERNYHIFYQLCAAASLPElkELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  320 QEGIFRTLAAILHLGNVEFSSGREHDSSVvkdPESRHHLQMAADLFKCDANLLLASLCTRSILTREGIIIKALDPNAAVT 399
Cdd:cd01380    241 QMEIFRILAAILHLGNVEIKATRNDSASI---SPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIV 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  400 SRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQ--IGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKMEQDE 477
Cdd:cd01380    318 ARDALAKHIYAQLFDWIVDRINKALASPVKEKQHsfIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEE 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  478 YRKEEINWSYIEFIDNQDVLDLIEKKPiGVIALLDEACMFPRSTHESFSMKLFQNF--RFHPRLEKPKFSETDFTLSHYA 555
Cdd:cd01380    398 YVKEEIEWSFIDFYDNQPCIDLIEGKL-GILDLLDEECRLPKGSDENWAQKLYNQHlkKPNKHFKKPRFSNTAFIVKHFA 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  556 GKVTYQTEAFLDKNRDYTIVEHCNLLSSSKC--PFVAGIfpsapeestrssykfssvssrFKQQLQALMETLSKTEPHYV 633
Cdd:cd01380    477 DDVEYQVEGFLEKNRDTVSEEHLNVLKASKNrkKTVGSQ---------------------FRDSLILLMETLNSTTPHYV 535

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  634 RCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMDESNDEQALTEKILSKLGL- 712
Cdd:cd01380    536 RCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLRDDKKKTCENILENLILd 615

                          650
                   ....*....|....
gi 1063726492  713 -GNYQLGRTKVFLR 725
Cdd:cd01380    616 pDKYQFGKTKIFFR 629

MYSc_class_II

cd01377

class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...

81-725

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: 772.02 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS 160
Cdd:cd01377      1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLP-IYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  161 GESGAGKTETTKLIMQYLTFVGGRATDDDR------SVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRI 234
Cdd:cd01377     80 GESGAGKTENTKKVIQYLASVAASSKKKKEsgkkkgTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  235 SGAAIRTYLLERSRVVRITDPERNYHCFYQLCASGNDAEKYKL---SNPRQFHYLNQSKtYELEGVSSAEEYKNTRRAMD 311
Cdd:cd01377    160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLlltGDPSYYFFLSQGE-LTIDGVDDAEEFKLTDEAFD 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  312 IVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSVVKDPESrhhLQMAADLFKCDANLLLASLCT-RSILTREgIIIK 390
Cdd:cd01377    239 ILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEE---ADKAAHLLGVNSSDLLKALLKpRIKVGRE-WVTK 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  391 ALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHV 470
Cdd:cd01377    315 GQNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHM 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  471 FKMEQDEYRKEEINWSYIEF-IDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHP---RLEKPKFSE 546
Cdd:cd01377    395 FVLEQEEYKKEGIEWTFIDFgLDLQPTIDLIEKPNMGILSILDEECVFPKATDKTFVEKLYSNHLGKSknfKKPKPKKSE 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  547 TDFTLSHYAGKVTYQTEAFLDKNRDyTIVEHC-NLLSSSKCPFVAGIFPSAPEESTRSSYKFSSVSS------RFKQQLQ 619
Cdd:cd01377    475 AHFILKHYAGDVEYNIDGWLEKNKD-PLNENVvALLKKSSDPLVASLFKDYEESGGGGGKKKKKGGSfrtvsqLHKEQLN 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  620 ALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMDES-ND 698
Cdd:cd01377    554 KLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGfDD 633

                          650       660
                   ....*....|....*....|....*....
gi 1063726492  699 EQALTEKILSKLGL--GNYQLGRTKVFLR 725
Cdd:cd01377    634 GKAACEKILKALQLdpELYRIGNTKVFFK 662

MYSc_Myo8

cd01383

class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...

83-725

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: 769.18 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   83 VLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYmgAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVSGE 162
Cdd:cd01383      3 VLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVP-LYGNEFITAY--RQKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  163 SGAGKTETTKLIMQYLTFVGGratdDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAAIRTY 242
Cdd:cd01383     80 SGAGKTETAKIAMQYLAALGG----GSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTY 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  243 LLERSRVVRITDPERNYHCFYQLCASGNDA--EKYKLSNPRQFHYLNQSKTYELEGVSSAEEYKNTRRAMDIVGISQDEQ 320
Cdd:cd01383    156 LLEKSRVVQLANGERSYHIFYQLCAGASPAlrEKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKEDQ 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  321 EGIFRTLAAILHLGNVEFSSGREHDSSVVKDPESrhhLQMAADLFKCDANLLLASLCTRSILTREGIIIKALDPNAAVTS 400
Cdd:cd01383    236 EHIFQMLAAVLWLGNISFQVIDNENHVEVVADEA---VSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDA 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  401 RDTLAKTVYAHLFDWLVDKINKS--VGQDPESRFqIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKMEQDEY 478
Cdd:cd01383    313 RDALAKAIYASLFDWLVEQINKSleVGKRRTGRS-ISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEY 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  479 RKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKPKfsETDFTLSHYAGKV 558
Cdd:cd01383    392 ELDGIDWTKVDFEDNQECLDLIEKKPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGER--GGAFTIRHYAGEV 469

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  559 TYQTEAFLDKNRDYTIVEHCNLLSSSKCPFV---------AGIFPSAPEESTRSSYKFSSVSSRFKQQLQALMETLSKTE 629
Cdd:cd01383    470 TYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPqlfaskmldASRKALPLTKASGSDSQKQSVATKFKGQLFKLMQRLENTT 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  630 PHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMDESNDEQALTEKILSK 709
Cdd:cd01383    550 PHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQDPLSTSVAILQQ 629

                          650
                   ....*....|....*...
gi 1063726492  710 LGL--GNYQLGRTKVFLR 725
Cdd:cd01383    630 FNIlpEMYQVGYTKLFFR 647

MYSc_Myo22

cd14883

class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...

82-725

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: 741.83 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   82 GVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVSG 161
Cdd:cd14883      2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELP-IYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  162 ESGAGKTETTKLIMQYLTFVGGRATdddrSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAAIRT 241
Cdd:cd14883     81 ESGAGKTETTKLILQYLCAVTNNHS----WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  242 YLLERSRVVRITDPERNYHCFYQLCASGN----DAEKYKLSNPRQFHYLNQSKTYELEGVSSAEEYKNTRRAMDIVGISQ 317
Cdd:cd14883    157 YLLEQSRITFQAPGERNYHVFYQLLAGAKhskeLKEKLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPE 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  318 DEQEGIFRTLAAILHLGNVEFSSG-REHDSSVVKDPESrhhLQMAADLFKCDANLLLASLCTRSILTREGIIIKALDPNA 396
Cdd:cd14883    237 EMQEGIFSVLSAILHLGNLTFEDIdGETGALTVEDKEI---LKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQE 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  397 AVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKMEQD 476
Cdd:cd14883    314 ARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQE 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  477 EYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKP--KFSETDFTLSHY 554
Cdd:cd14883    394 EYEKEGINWSHIVFTDNQECLDLIEKPPLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPdrRRWKTEFGVKHY 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  555 AGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSAPEESTRSSYKFSSVSS--------------RFKQQLQA 620
Cdd:cd14883    474 AGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDLLALTGLSISLGGDTtsrgtskgkptvgdTFKHQLQS 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  621 LMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMDESNDEQ 700
Cdd:cd14883    554 LVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSADHKET 633

                          650       660
                   ....*....|....*....|....*...
gi 1063726492  701 ALTEKILSKLGLGN---YQLGRTKVFLR 725
Cdd:cd14883    634 CGAVRALMGLGGLPedeWQVGKTKVFLR 661

MYSc_Myo1

cd01378

class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...

86-725

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: 726.26 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   86 NLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVSGESGA 165
Cdd:cd01378      6 NLKKRFENDEIYTYIGHVLISVNPFKDLG-IYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGESGA 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  166 GKTETTKLIMQYLTFVGGRATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAAIRTYLLE 245
Cdd:cd01378     85 GKTEASKRIMQYIAAVSGGSESEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYLLE 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  246 RSRVVRITDPERNYHCFYQLCASGNDAEK--YKLSNPRQFHYLNQSKTYELEGVSSAEEYKNTRRAMDIVGISQDEQEGI 323
Cdd:cd01378    165 KSRVVGQIKGERNFHIFYQLLKGASQEYLqeLGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEEQDSI 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  324 FRTLAAILHLGNVEFSSGrEHDSSVVKDPEsrhHLQMAADLFKCDANLLLASLCTRSILTREG---IIIKALDPNAAVTS 400
Cdd:cd01378    245 FRILAAILHLGNIQFAED-EEGNAAISDTS---VLDFVAYLLGVDPDQLEKALTHRTIETGGGgrsVYEVPLNVEQAAYA 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  401 RDTLAKTVYAHLFDWLVDKINKSV-GQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKMEQDEYR 479
Cdd:cd01378    321 RDALAKAIYSRLFDWIVERINKSLaAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQEEYV 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  480 KEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFP-RSTHESFSMKLFQNFRFHPRLEKPKFSET----DFTLSHY 554
Cdd:cd01378    401 REGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGHFElrrgEFRIKHY 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  555 AGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSAPEESTRssYKFSSVSSRFKQQLQALMETLSKTEPHYVR 634
Cdd:cd01378    481 AGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDSK--KRPPTAGTKFKNSANALVETLMKKQPSYIR 558

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  635 CVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPE------FMDESNDEQALTEKILS 708
Cdd:cd01378    559 CIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKtwpawdGTWQGGVESILKDLNIP 638

                          650
                   ....*....|....*..
gi 1063726492  709 KlglGNYQLGRTKVFLR 725
Cdd:cd01378    639 P---EEYQMGKTKIFIR 652

MYSc_Myo7

cd01381

class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...

81-725

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: 718.65 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS 160
Cdd:cd01381      1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILP-IYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVIS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  161 GESGAGKTETTKLIMQYLTFVGGRatddDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAAIR 240
Cdd:cd01381     80 GESGAGKTESTKLILQYLAAISGQ----HSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  241 TYLLERSRVVRITDPERNYHCFYQLCA--SGNDAEKYKLSNPRQFHYLNQSKTYELEGVSSAEEYKNTRRAMDIVGISQD 318
Cdd:cd01381    156 QYLLEKSRIVSQAPDERNYHIFYCMLAglSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDE 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  319 EQEGIFRTLAAILHLGNVEFSSGREH--DSSVVKDPEsrhHLQMAADLFKCDANLLLASLCTRSILTREGIIIKALDPNA 396
Cdd:cd01381    236 EIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPP---NLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQ 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  397 AVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPE---SRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKM 473
Cdd:cd01381    313 ALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGtdsSRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKL 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  474 EQDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKPKF-SETDFTLS 552
Cdd:cd01381    393 EQEEYDKEGINWQHIEFVDNQDVLDLIALKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSdLNTSFGIN 472

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  553 HYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSAPEESTRSSYKFSSVSSRFKQQLQALMETLSKTEPHY 632
Cdd:cd01381    473 HFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKSPTLSSQFRKSLDQLMKTLSACQPFF 552

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  633 VRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEF--MDESNDEQALTEKILSKL 710
Cdd:cd01381    553 VRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIppAHKTDCRAATRKICCAVL 632

                          650
                   ....*....|....*.
gi 1063726492  711 GLG-NYQLGRTKVFLR 725
Cdd:cd01381    633 GGDaDYQLGKTKIFLK 648

MYSc_Myo27

cd14888

class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...

81-691

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: 654.45 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPHLYNGHMMEQYMgAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS 160
Cdd:cd14888      1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPGLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  161 GESGAGKTETTKLIMQYLTFVGGRATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTN--------- 231
Cdd:cd14888     80 GESGAGKTESTKYVMKFLACAGSEDIKKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLkskrmsgdr 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  232 GRISGAAIRTYLLERSRVVRITDPERNYHCFYQLCASG-----------NDAEKYKLSNPRQ--------------FHYL 286
Cdd:cd14888    160 GRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAreakntglsyeENDEKLAKGADAKpisidmssfephlkFRYL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  287 NQSKTYELEGVSSAEEYKNTRRAMDIVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSVVKDPESRHHLQMAADLFK 366
Cdd:cd14888    240 TKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDDLEKVASLLG 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  367 CDANLLLASLCTRSILTREGIIIKALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPE-SRFQIGVLDIYGFECF 445
Cdd:cd14888    320 VDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDnSLLFCGVLDIFGFECF 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  446 KNNSFEQFCINFANEKLQQHFNEHVFKMEQDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESF 525
Cdd:cd14888    400 QLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKPLGIFCMLDEECFVPGGKDQGL 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  526 SMKLFQNFRFHPRLEKPKFSETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPS---APEESTR 602
Cdd:cd14888    480 CNKLCQKHKGHKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSAylrRGTDGNT 559

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  603 SSYKFSSVSSRFKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFV 682
Cdd:cd14888    560 KKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFY 639


                   ....*....
gi 1063726492  683 DRFGLLAPE 691
Cdd:cd14888    640 NDYRILLNG 648

MYSc_Myo4

cd14872

class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...

81-725

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: 649.53 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS 160
Cdd:cd14872      1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLP-LYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILIS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  161 GESGAGKTETTKLIMQYLTFVGGratdDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAAIR 240
Cdd:cd14872     80 GESGAGKTEATKQCLSFFAEVAG----STNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  241 TYLLERSRVVRITDPERNYHCFYQLCASGNDAEKYKLSNPRQFHYLNQSKTYELEGVSSAEEYKNTRRAMDIVGISQDEQ 320
Cdd:cd14872    156 NYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSAAYGYLSLSGCIEVEGVDDVADFEEVVLAMEQLGFDDADI 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  321 EGIFRTLAAILHLGNVEFSSGREHDSSVVKDPESRHHLQMAADLFKCDANLLLASLCTRSILTREG-IIIKALDPNAAVT 399
Cdd:cd14872    236 NNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIKGCdPTRIPLTPAQATD 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  400 SRDTLAKTVYAHLFDWLVDKINKSV-GQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKMEQDEY 478
Cdd:cd14872    316 ACDALAKAAYSRLFDWLVKKINESMrPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEALY 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  479 RKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFR----FHPrlEKPKFSETDFTLSHY 554
Cdd:cd14872    396 QSEGVKFEHIDFIDNQPVLDLIEKKQPGLMLALDDQVKIPKGSDATFMIAANQTHAakstFVY--AEVRTSRTEFIVKHY 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  555 AGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFP-SAPEESTRssykFSSVSSRFKQQLQALMETLSKTEPHYV 633
Cdd:cd14872    474 AGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPpSEGDQKTS----KVTLGGQFRKQLSALMTALNATEPHYI 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  634 RCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFG-LLAPEFMDESNDEQALTEKILSKLG- 711
Cdd:cd14872    550 RCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRfLVKTIAKRVGPDDRQRCDLLLKSLKq 629

                          650
                   ....*....|....*
gi 1063726492  712 -LGNYQLGRTKVFLR 725
Cdd:cd14872    630 dFSKVQVGKTRVLYR 644

MYSc_Myo42

cd14903

class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...

81-725

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: 641.83 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPHLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS 160
Cdd:cd14903      1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPELYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  161 GESGAGKTETTKLIMQYLTFVGGratDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAAIR 240
Cdd:cd14903     81 GESGAGKTETTKILMNHLATIAG---GLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  241 TYLLERSRVVRITDPERNYHCFYQLCASGNDAEKYKLSNPRQFHYLNQSKTYELEGVSSAEEYKNTRRAMDIVGISQDEQ 320
Cdd:cd14903    158 TYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANECAYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEEKQ 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  321 EGIFRTLAAILHLGNVEFSSGREHDSSVVKDPeSRHHLQMAADLFKCDANLLLASLCTRSILTREGIIIKALDPNAAVTS 400
Cdd:cd14903    238 EVLFEVLAGILHLGQLQIQSKPNDDEKSAIAP-GDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDC 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  401 RDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKMEQDEYRK 480
Cdd:cd14903    317 RDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEE 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  481 EEINWSYIEFIDNQDVLDLIEKKpIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRL-EKPKFSETDFTLSHYAGKVT 559
Cdd:cd14903    397 EGIRWAHIDFADNQDVLAVIEDR-LGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDViEFPRTSRTQFTIKHYAGPVT 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  560 YQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSAPEESTRSSYKFSSVSSR--------------FKQQLQALMETL 625
Cdd:cd14903    476 YESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRrrggalttttvgtqFKDSLNELMTTI 555

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  626 SKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMDESNDEQALTEK 705
Cdd:cd14903    556 RSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEGRNTDVPVAERCEA 635

                          650       660
                   ....*....|....*....|...
gi 1063726492  706 ILSKLGLG---NYQLGRTKVFLR 725
Cdd:cd14903    636 LMKKLKLEspeQYQMGLTRIYFQ 658

MYSc_Myo29

cd14890

class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...

81-725

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: 636.05 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPHLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMID----DSRSQS 156
Cdd:cd14890      1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPDLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  157 ILVSGESGAGKTETTKLIMQYLTFV----------GGRATDDDR-----SVEQQVLESNPLLEAFGNAKTVRNDNSSRFG 221
Cdd:cd14890     81 IIISGESGAGKTEATKIIMQYLARItsgfaqgasgEGEAASEAIeqtlgSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  222 KFVEIQFDTNGRISGAAIRTYLLERSRVVRITDPERNYHCFYQLCASGNDA--EKYKLSNPRQFHYLnQSKTYELEGVSS 299
Cdd:cd14890    161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEAlrERLKLQTPVEYFYL-RGECSSIPSCDD 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  300 AEEYKNTRRAMDIVGISQDEQEGIFRTLAAILHLGNVEFSSgrEHDSSVVKDPESRHHLQMAADLFKCDANLLLASLCTR 379
Cdd:cd14890    240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFES--ENDTTVLEDATTLQSLKLAAELLGVNEDALEKALLTR 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  380 SILTREGIIIKALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQdPESRFQ-IGVLDIYGFECFKNNSFEQFCINFA 458
Cdd:cd14890    318 QLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISS-PDDKWGfIGVLDIYGFEKFEWNTFEQLCINYA 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  459 NEKLQQHFNEHVFKMEQDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALL-----------DEACM-FPRSTHESF- 525
Cdd:cd14890    397 NEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVNGKPGIFitlddcwrfkgEEANKkFVSQLHASFg 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  526 ----SMKLFQNFRFHPRLEKPKF-SETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSkcpfvagifpsapees 600
Cdd:cd14890    477 rksgSGGTRRGSSQHPHFVHPKFdADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQS---------------- 540

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  601 tRSSYKFSSVSSRFKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSD 680
Cdd:cd14890    541 -RRSIREVSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDS 619

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*...
gi 1063726492  681 FVDRFGLLAPefmDESNDEQALteKILSK-LGLGN--YQLGRTKVFLR 725
Cdd:cd14890    620 FFYDFQVLLP---TAENIEQLV--AVLSKmLGLGKadWQIGSSKIFLK 662

MYSc_Myo40

cd14901

class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...

81-724

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: 635.68 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYM------GAPFGELSPHVFAVSDVAYRAMIDDSR- 153
Cdd:cd14901      1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLP-LYDDETKEAYYehgerrAAGERKLPPHVYAVADKAFRAMLFASRg 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  154 ---SQSILVSGESGAGKTETTKLIMQYLTFVGGRATDDDRSVEQ-----QVLESNPLLEAFGNAKTVRNDNSSRFGKFVE 225
Cdd:cd14901     80 qkcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERenvrdRVLESNPILEAFGNARTNRNNNSSRFGKFIR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  226 IQFDTNGRISGAAIRTYLLERSRVVRITDPERNYHCFYQLC--ASGNDAEKYKLSNPRQFHYLNQSKTYE-LEGVSSAEE 302
Cdd:cd14901    160 LGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLrgASSDELHALGLTHVEEYKYLNSSQCYDrRDGVDDSVQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  303 YKNTRRAMDIVGISQDEQEGIFRTLAAILHLGNVEF-SSGREHDSSvvkdpESRHHLQMAA--DLFKCDANLLLASLCTR 379
Cdd:cd14901    240 YAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTF-----SMSSLANVRAacDLLGLDMDVLEKTLCTR 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  380 SILTREGIIIKALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDP---ESRFqIGVLDIYGFECFKNNSFEQFCIN 456
Cdd:cd14901    315 EIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEstgASRF-IGIVDIFGFEIFATNSLEQLCIN 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  457 FANEKLQQHFNEHVFKMEQDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFH 536
Cdd:cd14901    394 FANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKH 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  537 PRLEKPKFSE--TDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAgifpsapeeSTrssykfssVSSRF 614
Cdd:cd14901    474 ASFSVSKLQQgkRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS---------ST--------VVAKF 536

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  615 KQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPE--- 691
Cdd:cd14901    537 KVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPDgas 616

                          650       660       670
                   ....*....|....*....|....*....|....*...
gi 1063726492  692 -----FMDESNDEQALTEKILSKLGLGNYQLGRTKVFL 724
Cdd:cd14901    617 dtwkvNELAERLMSQLQHSELNIEHLPPFQVGKTKVFL 654

MYSc_Myo6

cd01382

class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...

81-725

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: 632.36 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPHLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS 160
Cdd:cd01382      1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPKLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  161 GESGAGKTETTKLIMQYLTFVGGRATDDdrsVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAAIR 240
Cdd:cd01382     81 GESGAGKTESTKYILRYLTESWGSGAGP---IEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVS 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  241 TYLLERSRVVRITDPERNYHCFYQLCASGNDAEKYKLSNPRQfhylnqsktyelegVSSAEEYKNTRRAMDIVGISQDEQ 320
Cdd:cd01382    158 HYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPL--------------LDDVGDFIRMDKAMKKIGLSDEEK 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  321 EGIFRTLAAILHLGNVEFSSGREHDSSVVK-DPESRHHLQMAADLFKCDANLLLASLCTRSILTREG-----IIIKALDP 394
Cdd:cd01382    224 LDIFRVVAAVLHLGNIEFEENGSDSGGGCNvKPKSEQSLEYAAELLGLDQDELRVSLTTRVMQTTRGgakgtVIKVPLKV 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  395 NAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDpESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKME 474
Cdd:cd01382    304 EEANNARDALAKAIYSKLFDHIVNRINQCIPFE-TSSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILKEE 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  475 QDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKPKFS--------- 545
Cdd:cd01382    383 QELYEKEGLGVKEVEYVDNQDCIDLIEAKLVGILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSIPRKSklkihrnlr 462

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  546 -ETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSAPEESTRSSYKFSSVS-----SRFKQQLQ 619
Cdd:cd01382    463 dDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNKDSKQKAGKLSfisvgNKFKTQLN 542

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  620 ALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRF-GLLAPEFmdESND 698
Cdd:cd01382    543 LLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYkKYLPPKL--ARLD 620

                          650       660
                   ....*....|....*....|....*....
gi 1063726492  699 EQALTEKILSKLGLGN--YQLGRTKVFLR 725
Cdd:cd01382    621 PRLFCKALFKALGLNEndFKFGLTKVFFR 649

MYSc_Myo31

cd14892

class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...

81-725

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: 631.79 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPHLYN--GHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDD----SRS 154
Cdd:cd14892      1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDvpGFDSQRKEEATASSPPPHVFSIAERAYRAMKGVgkgqGTP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  155 QSILVSGESGAGKTETTKLIMQYL---------TFVGGRATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVE 225
Cdd:cd14892     81 QSIVVSGESGAGKTEASKYIMKYLatasklakgASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  226 IQFDTNGRISGAAIRTYLLERSRVVRITDPERNYHCFYQLCA--SGNDAEKYKLSNPRQFHYLNQSKTYELEGVSSAEEY 303
Cdd:cd14892    161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAglDANENAALELTPAESFLFLNQGNCVEVDGVDDATEF 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  304 KNTRRAMDIVGISQDEQEGIFRTLAAILHLGNVEFSSgREHDSSVvkDPESRHHLQMA--ADLFKCDANLLLASLCTRSI 381
Cdd:cd14892    241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEE-NADDEDV--FAQSADGVNVAkaAGLLGVDAAELMFKLVTQTT 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  382 LTREGIIIK-ALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQ-----------DPESRFqIGVLDIYGFECFKNNS 449
Cdd:cd14892    318 STARGSVLEiKLTAREAKNALDALCKYLYGELFDWLISRINACHKQqtsgvtggaasPTFSPF-IGILDIFGFEIMPTNS 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  450 FEQFCINFANEKLQQHFNEHVFKMEQDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPR-STHESFSMK 528
Cdd:cd14892    397 FEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKPLGLLPLLEEQMLLKRkTTDKQLLTI 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  529 LFQN-FRFHPRLEKPKFSETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKcpfvagifpsapeestrssykf 607
Cdd:cd14892    477 YHQThLDKHPHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS---------------------- 534

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  608 ssvssRFKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGL 687
Cdd:cd14892    535 -----KFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWP 609

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*..
gi 1063726492  688 LA---------PEFMDESNDEQALTEKILSKLGLGNYQLGRTKVFLR 725
Cdd:cd14892    610 LArnkagvaasPDACDATTARKKCEEIVARALERENFQLGRTKVFLR 656

MYSc_Myo15

cd01387

class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...

81-725

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: 602.90 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLpHLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS 160
Cdd:cd01387      1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMF-DIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVIS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  161 GESGAGKTETTKLIMQYLTFVGGRATDDdrsVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDtNGRISGAAIR 240
Cdd:cd01387     80 GESGSGKTEATKLIMQYLAAVNQRRNNL---VTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVGAITS 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  241 TYLLERSRVVRITDPERNYHCFYQLCA--SGNDAEKYKLSNPRQFHYLNQSKTYELEGVSSAEEYKNTRRAMDIVGISQD 318
Cdd:cd01387    156 QYLLEKSRIVTQAKNERNYHVFYELLAglPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSE 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  319 EQEGIFRTLAAILHLGNVEFSSGREHDS----SVVKDPEsrhhLQMAADLFKCDANLLLASLCTRSILTREGIIIKALDP 394
Cdd:cd01387    236 EQDSIFRILASVLHLGNVYFHKRQLRHGqegvSVGSDAE----IQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTI 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  395 NAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKME 474
Cdd:cd01387    312 DQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLE 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  475 QDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKPKFSETDFTLSHY 554
Cdd:cd01387    392 QEEYIREQIDWTEIAFADNQPVINLISKKPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRMPLPEFTIKHY 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  555 AGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSAPEESTRSSYKFSS------------VSSRFKQQLQALM 622
Cdd:cd01387    472 AGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKAPPRLGKgrfvtmkprtptVAARFQDSLLQLL 551

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  623 ETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMDESNDEQaL 702
Cdd:cd01387    552 EKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPRPAPGD-M 630

                          650       660
                   ....*....|....*....|....*..
gi 1063726492  703 TEKILSKL----GLGNYQLGRTKVFLR 725
Cdd:cd01387    631 CVSLLSRLctvtPKDMYRLGATKVFLR 657

MYSc_Myo9

cd01385

class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...

84-725

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: 600.90 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   84 LYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVSGES 163
Cdd:cd01385      4 LENLRARFKHGKIYTYVGSILIAVNPFKFLP-IYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGES 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  164 GAGKTETTKLIMQYLTFVGGRATDddRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAAIRTYL 243
Cdd:cd01385     83 GSGKTESTNFLLHHLTALSQKGYG--SGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  244 LERSRVVRITDPERNYHCFYQLCASGNDAEK--YKLSNPRQFHYLNQSKTYELEGVSSAEEYKNTRRAMDIVGISQDEQE 321
Cdd:cd01385    161 LEKSRIVSQEKNERNYHVFYYLLAGASEEERkeLHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQR 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  322 GIFRTLAAILHLGNVEFSS-GREHDSSV-VKDPESrhhLQMAADLFKCDANLLLASLCTRSILTR-EGIIIKALDPnAAV 398
Cdd:cd01385    241 QIFSVLSAVLHLGNIEYKKkAYHRDESVtVGNPEV---LDIISELLRVKEETLLEALTTKKTVTVgETLILPYKLP-EAI 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  399 TSRDTLAKTVYAHLFDWLVDKINKSV-GQDPESRFQ---IGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKME 474
Cdd:cd01385    317 ATRDAMAKCLYSALFDWIVLRINHALlNKKDLEEAKglsIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLE 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  475 QDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKPKFSETDFTLSHY 554
Cdd:cd01385    397 QEEYKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQVMEPAFIIAHY 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  555 AGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFV---AGIFP-----------------------------SAPEESTR 602
Cdd:cd01385    477 AGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVrelIGIDPvavfrwavlrafframaafreagrrraqrTAGHSLTL 556

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  603 SSYKFSSVSSR------------FKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLA 670
Cdd:cd01385    557 HDRTTKSLLHLhkkkkppsvsaqFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRS 636

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063726492  671 GYPTRRNYSDFVDRFGLLAPEFMDES-NDEQALTEKIlsKLGLGNYQLGRTKVFLR 725
Cdd:cd01385    637 GYSVRYTFQEFITQFQVLLPKGLISSkEDIKDFLEKL--NLDRDNYQIGKTKVFLK 690

MyosinXI_CBD

cd15475

cargo binding domain of myosin XI; Class XI myosins are a plant specific group, homologous to ...

1116-1480

0e+00

Pssm-ID: 271259 Cd Length: 326 Bit Score: 600.33 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492 1116 ERNLENYELLSRCIKENLGFNDDKPLAACVIYKCLLHWRAFESESTAIFNIIIEGINEALKGGDENGVLPYWLSNASALL 1195
Cdd:cd15475      1 ERQQENVDALIKCVSENLGFSEGKPVAAFTIYKCLLHWKSFEAEKTSVFDRIIQTIGSAIEDQDNNDHLAYWLSNTSTLL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492 1196 CLLQRNLrsnsflnasaqrsgraaygvkspfklhgpddgashiearyPALLFKQQLTACVEKIYGLIRDNLKKELSPLLG 1275
Cdd:cd15475     81 FLLQRSL----------------------------------------PALLFKQQLTAYVEKIYGIIRDNLKKELSPLLS 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492 1276 SCIQAPKASRGIAGKS-RSPGGVPQQSPSSQWESILKFLDSLMSRLRENHVPSFFIRKLVTQVFSFINLSLFNSLLLRRE 1354
Cdd:cd15475    121 LCIQAPRTSRGSSSKSsSSANSLGQQSPSSHWQSIIKSLNSLLSTLKENHVPPFLVQKIFTQVFSFINVQLFNSLLLRRE 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492 1355 CCTFSNGEYVKSGISELEKWIANAKEEFAGTSWHELNYIRQAVGFLVIHQKKKKSLDEIRQDLCPVLTIRQIYRISTMYW 1434
Cdd:cd15475    201 CCSFSNGEYVKAGLAELELWCSQATEEYAGSSWDELKHIRQAVGFLVIHQKSRKSYDEITNDLCPVLSVQQLYRICTMYW 280

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1063726492 1435 DDKYGTQSVSSEVVSQMRVLVDKDNQKQTSNSFLLDDDMSIPFSAE 1480
Cdd:cd15475    281 DDKYGTQSVSPEVISSMRVLMTEDSNNAVSNSFLLDDDSSIPFSVE 326

MYSc_Myo3

cd01379

class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...

83-725

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: 594.25 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   83 VLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVSGE 162
Cdd:cd01379      3 IVSQLQKRYSRDQIYTYIGDILIAVNPFQNLG-IYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  163 SGAGKTETTKLIMQYLTFVGgRATDddRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAAIRTY 242
Cdd:cd01379     82 SGAGKTESANLLVQQLTVLG-KANN--RTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEY 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  243 LLERSRVVRITDPERNYHCFYQLCA---SGNDAEKYKLSNPRQFHYLNQSKTYELEGVSSA---EEYKNTRRAMDIVGIS 316
Cdd:cd01379    159 LLEKSRVVHQAIGERNFHIFYYIYAglaEDKKLAKYKLPENKPPRYLQNDGLTVQDIVNNSgnrEKFEEIEQCFKVIGFT 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  317 QDEQEGIFRTLAAILHLGNVEF----SSGREHDSSVVKDPESrhhLQMAADLFKCDANLLLASLCTRSILTREGIIIKAL 392
Cdd:cd01379    239 KEEVDSVYSILAAILHIGDIEFteveSNHQTDKSSRISNPEA---LNNVAKLLGIEADELQEALTSHSVVTRGETIIRNN 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  393 DPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESR---FQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEH 469
Cdd:cd01379    316 TVEEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSASdepLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQH 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  470 VFKMEQDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPrLEKPKFSETDF 549
Cdd:cd01379    396 IFAWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNIKSKY-YWRPKSNALSF 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  550 TLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPF----VAGIFpsapeestrssykfssvssRFkqqlqALMETL 625
Cdd:cd01379    475 GIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLvrqtVATYF-------------------RY-----SLMDLL 530

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  626 SKT---EPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMDESNDEQAL 702
Cdd:cd01379    531 SKMvvgQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAFKWNEEVVANREN 610

                          650       660
                   ....*....|....*....|...
gi 1063726492  703 TEKILSKLGLGNYQLGRTKVFLR 725
Cdd:cd01379    611 CRLILERLKLDNWALGKTKVFLK 633

MYSc_Myo10

cd14873

class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...

81-725

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: 584.06 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPHLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS 160
Cdd:cd14873      1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAGLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  161 GESGAGKTETTKLIMQYL-----TFVGGRATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRIS 235
Cdd:cd14873     81 GESGAGKTESTKLILKFLsvisqQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  236 GAAIRTYLLERSRVVRITDPERNYHCFYQLCASGNDAEKYK--LSNPRQFHYLNQSKTYELEGVSSAEEYKNTRRAMDIV 313
Cdd:cd14873    161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEfyLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEVM 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  314 GISQDEQEGIFRTLAAILHLGNVEF-SSGREHDSsvvkdpeSRHHLQMAADLFKCDANLLLASLCTRSILTREGIIIKAL 392
Cdd:cd14873    241 QFSKEEVREVSRLLAGILHLGNIEFiTAGGAQVS-------FKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPL 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  393 DPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVgQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFK 472
Cdd:cd14873    314 NVQQAVDSRDSLAMALYARCFEWVIKKINSRI-KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFS 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  473 MEQDEYRKEEINWSYIEFIDNQDVLDLIEKKpIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKPKFSETDFTLS 552
Cdd:cd14873    393 LEQLEYSREGLVWEDIDWIDNGECLDLIEKK-LGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNNFGVK 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  553 HYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSAPEESTRSSYKFSSVSSR------FKQQLQALMETLS 626
Cdd:cd14873    472 HYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRptvssqFKDSLHSLMATLS 551

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  627 KTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPeFMDESNDEQALTEKI 706
Cdd:cd14873    552 SSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMR-NLALPEDVRGKCTSL 630

                          650       660
                   ....*....|....*....|.
gi 1063726492  707 LSKLGLGN--YQLGRTKVFLR 725
Cdd:cd14873    631 LQLYDASNseWQLGKTKVFLR 651

MYSc_Myo36

cd14897

class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...

83-725

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: 563.54 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   83 VLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPF-GELSPHVFAVSDVAYRAMIDDSRSQSILVSG 161
Cdd:cd14897      3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLP-IFDKKHHEEYSNLSVrSQRPPHLFWIADQAYRRLLETGRNQCILVSG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  162 ESGAGKTETTKLIMQYLTFVGGRatdDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAAIRT 241
Cdd:cd14897     82 ESGAGKTESTKYMIKHLMKLSPS---DDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDD 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  242 YLLERSRVVRITDPERNYHCFYQLCAsGNDAEK---YKLSNPRQFHYLnQSKTYELEGVSSAEEYKNTR-------RAMD 311
Cdd:cd14897    159 YLLEKSRVVHRGNGEKNFHIFYALFA-GMSRDRllyYFLEDPDCHRIL-RDDNRNRPVFNDSEELEYYRqmfhdltNIMK 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  312 IVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSVVKDpesRHHLQMAADLFKCDANLLLASLCTRSILTREGIIIKA 391
Cdd:cd14897    237 LIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVAD---EYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSW 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  392 LDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVgqDPESRFQ-------IGVLDIYGFECFKNNSFEQFCINFANEKLQQ 464
Cdd:cd14897    314 KSLRQANDSRDALAKDLYSRLFGWIVGQINRNL--WPDKDFQimtrgpsIGILDMSGFENFKINSFDQLCINLSNERLQQ 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  465 HFNEHVFKMEQDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKPKF 544
Cdd:cd14897    392 YFNDYVFPRERSEYEIEGIEWRDIEYHDNDDVLELFFKKPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVASPG 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  545 SETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSapeestrssykfssvssRFKQQLQALMET 624
Cdd:cd14897    472 NRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTS-----------------YFKRSLSDLMTK 534

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  625 LSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMDESNDEQALTE 704
Cdd:cd14897    535 LNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFSNKVRSDDLGKCQ 614

                          650       660
                   ....*....|....*....|.
gi 1063726492  705 KILSKLGLGNYQLGRTKVFLR 725
Cdd:cd14897    615 KILKTAGIKGYQFGKTKVFLK 635

MYSc_Myo43

cd14904

class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...

81-725

0e+00

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: 558.79 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPHLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS 160
Cdd:cd14904      1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  161 GESGAGKTETTKLIMQYLTFV-GGRatdDDRSVEqQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAAI 239
Cdd:cd14904     81 GESGAGKTETTKIVMNHLASVaGGR---KDKTIA-KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKC 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  240 RTYLLERSRVVRITDPERNYHCFYQLCA--SGNDAEKYKLSNPRQFHYLNQS-KTYELEGVSSAEEYKNTRRAMDIVGIS 316
Cdd:cd14904    157 ETYLLEKSRVVSIAEGERNYHIFYQLLAglSSEERKEFGLDPNCQYQYLGDSlAQMQIPGLDDAKLFASTQKSLSLIGLD 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  317 QDEQEGIFRTLAAILHLGNVEFSSGREHDSSVvkdpESRHHLQMAADLFKCDANLLLASLCTRSILTREGIIIKALDPNA 396
Cdd:cd14904    237 NDAQRTLFKILSGVLHLGEVMFDKSDENGSRI----SNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVE 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  397 AVTSRDTLAKTVYAHLFDWLVDKINKSVGQDpESRF--QIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKME 474
Cdd:cd14904    313 AEENRDALAKAIYSKLFDWMVVKINAAISTD-DDRIkgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTV 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  475 QDEYRKEEINWSYIEFIDNQDVLDLIEKKpIGVIALLDEACMFPRSTHESFSMKLFQNFRF---HPRLEKPKFSETDFTL 551
Cdd:cd14904    392 EEEYIREGLQWDHIEYQDNQGIVEVIDGK-MGIIALMNDHLRQPRGTEEALVNKIRTNHQTkkdNESIDFPKVKRTQFII 470

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  552 SHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPS--APEEST-----RSSYKFSSVSSRFKQQLQALMET 624
Cdd:cd14904    471 NHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSseAPSETKegksgKGTKAPKSLGSQFKTSLSQLMDN 550

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  625 LSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMdESNDEQALTE 704
Cdd:cd14904    551 IKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSM-HSKDVRRTCS 629

                          650       660
                   ....*....|....*....|....
gi 1063726492  705 KILSKLGLGN---YQLGRTKVFLR 725
Cdd:cd14904    630 VFMTAIGRKSpleYQIGKSLIYFK 653

MYSc_Myo30

cd14891

class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...

81-725

0e+00

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: 556.19 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDI--YTYTGSILIAVNPFKKLPhlyNGHMMEqYMGAPFGELSPHVFAVSDVAYRAMIDDSRS---Q 155
Cdd:cd14891      1 AGILHNLEERSKLDNQrpYTFMANVLIAVNPLRRLP---EPDKSD-YINTPLDPCPPHPYAIAEMAYQQMCLGSGRmqnQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  156 SILVSGESGAGKTETTKLIMQYLTF--VGGRATDDDR-------------SVEQQVLESNPLLEAFGNAKTVRNDNSSRF 220
Cdd:cd14891     77 SIVISGESGAGKTETSKIILRFLTTraVGGKKASGQDieqsskkrklsvtSLDERLMDTNPILESFGNAKTLRNHNSSRF 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  221 GKFVEIQFDTNG-RISGAAIRTYLLERSRVVRITDPERNYHCFYQLCASGNDA--EKYKLSNPRQFHYLNQSKTYELEGV 297
Cdd:cd14891    157 GKFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAEllKELLLLSPEDFIYLNQSGCVSDDNI 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  298 SSAEEYKNTRRAMDIVGISQDEQEGIFRTLAAILHLGNVEFSSgREHD--SSVVKDPESRHHLQMAADLFKCDANLLLAS 375
Cdd:cd14891    237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDE-EDTSegEAEIASESDKEALATAAELLGVDEEALEKV 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  376 LCTRSILTREGIIIKALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFECFK-NNSFEQFC 454
Cdd:cd14891    316 ITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLL 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  455 INFANEKLQQHFNEHVFKMEQDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFR 534
Cdd:cd14891    396 INYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPNGILPLLDNEARNPNPSDAKLNETLHKTHK 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  535 FHPR--LEKPKFSETDFTLSHYAGKVTYQTEAFLDKNRDyTIVEHC-NLLSSSKcpfvagifpsapeestrssykfssvs 611
Cdd:cd14891    476 RHPCfpRPHPKDMREMFIVKHYAGTVSYTIGSFIDKNND-IIPEDFeDLLASSA-------------------------- 528

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  612 sRFKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAP- 690
Cdd:cd14891    529 -KFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLPp 607

                          650       660       670
                   ....*....|....*....|....*....|....*...
gi 1063726492  691 -EFMDESNDEQALTEKILSKLGLGN--YQLGRTKVFLR 725
Cdd:cd14891    608 sVTRLFAENDRTLTQAILWAFRVPSdaYRLGRTRVFFR 645

MYSc_Myo47

cd14908

class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...

81-725

8.57e-179

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: 550.28 E-value: 8.57e-179

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQY--MG-------APFGELSPHVFAVSDVAYRAMIDD 151
Cdd:cd14908      1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLP-LYGKEILESYrqEGllrsqgiESPQALGPHVFAIADRSYRQMMSE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  152 SR-SQSILVSGESGAGKTETTKLIMQYLTFVG---GRATDDDR-----SVEQQVLESNPLLEAFGNAKTVRNDNSSRFGK 222
Cdd:cd14908     80 IRaSQSILISGESGAGKTESTKIVMLYLTTLGngeEGAPNEGEelgklSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  223 FVEIQFDTNGRISGAAIRTYLLERSRVVRITDPERNYHCFYQLCASGNDAEKYK----------LSNPRQFHYLNQSKTY 292
Cdd:cd14908    160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKyefhdgitggLQLPNEFHYTGQGGAP 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  293 ELEGVSSAEEYKNTRRAMDIVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSVVKDPESRHHLQMAADLFKCDANLL 372
Cdd:cd14908    240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARVAKLLGVDVDKL 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  373 LASLCTRSILTREGIIIKALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVG--QDPESRFQIGVLDIYGFECFKNNSF 450
Cdd:cd14908    320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINweNDKDIRSSVGVLDIFGFECFAHNSF 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  451 EQFCINFANEKLQQHFNEHVFKMEQDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFP-RSTHESFSMKL 529
Cdd:cd14908    400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAKKKGILTMLDDECRLGiRGSDANYASRL 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  530 FQNFRFHPRL---EKPKFSETD-------FTLSHYAGKVTYQTEA-FLDKNRDYTIVEHCNLLSSSKcpfvagifpsape 598
Cdd:cd14908    480 YETYLPEKNQthsENTRFEATSiqktkliFAVRHFAGQVQYTVETtFCEKNKDEIPLTADSLFESGQ------------- 546

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  599 estrssykfssvssRFKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNY 678
Cdd:cd14908    547 --------------QFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPH 612

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  679 SDFVDRFGLLAP---------------------EFMDESNDEQALTEKILSKLGL--GNYQLGRTKVFLR 725
Cdd:cd14908    613 KDFFKRYRMLLPlipevvlswsmerldpqklcvKKMCKDLVKGVLSPAMVSMKNIpeDTMQLGKSKVFMR 682

MYSc_Myh2_insects_mollusks

cd14911

class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...

81-725

1.43e-172

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: 533.40 E-value: 1.43e-172

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS 160
Cdd:cd14911      1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  161 GESGAGKTETTKLIMQYLTFV------GGRATDDDR--------SVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEI 226
Cdd:cd14911     80 GESGAGKTENTKKVIQFLAYVaaskpkGSGAVPHPAvnpavligELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  227 QFDTNGRISGAAIRTYLLERSRVVRITDPERNYHCFYQLCASGNDAEK--YKLSNPRQFHYLNqSKTYELEGVSSAEEYK 304
Cdd:cd14911    160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQRekFILDDVKSYAFLS-NGSLPVPGVDDYAEFQ 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  305 NTRRAMDIVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSVVKDPESRhhlQMAADLFKCDANLLLASLCTRSILTR 384
Cdd:cd14911    239 ATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVA---QKIAHLLGLSVTDMTRAFLTPRIKVG 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  385 EGIIIKALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPE--SRFqIGVLDIYGFECFKNNSFEQFCINFANEKL 462
Cdd:cd14911    316 RDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRqgASF-IGILDMAGFEIFELNSFEQLCINYTNEKL 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  463 QQHFNEHVFKMEQDEYRKEEINWSYIEF-IDNQDVLDLIEkKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEK 541
Cdd:cd14911    395 QQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLID-KPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  542 PKFSET-DFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSA--------PEESTRSSYKFSSVSS 612
Cdd:cd14911    474 TDFRGVaDFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAeivgmaqqALTDTQFGARTRKGMF 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  613 R-----FKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGL 687
Cdd:cd14911    554 RtvshlYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEL 633

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 1063726492  688 LAPEFMDES-NDEQALTEKILSKLGLGN--YQLGRTKVFLR 725
Cdd:cd14911    634 LTPNVIPKGfMDGKKACEKMIQALELDSnlYRVGQSKIFFR 674

MYSc_Myo46

cd14907

class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...

81-725

2.41e-172

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: 532.68 E-value: 2.41e-172

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPHLYNGHMMEQYM-----GAPFGELS---PHVFAVSDVAYRAMIDDS 152
Cdd:cd14907      1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDNLFSEEVMQMYKeqiiqNGEYFDIKkepPHIYAIAALAFKQLFENN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  153 RSQSILVSGESGAGKTETTKLIMQYLTFVGGRATDDDR----------------SVEQQVLESNPLLEAFGNAKTVRNDN 216
Cdd:cd14907     81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEvltltssiratskstkSIEQKILSCNPILEAFGNAKTVRNDN 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  217 SSRFGKFVEIQFD-TNGRISGAAIRTYLLERSRVVRITDPERNYHCFYQL--CASGNDAEKYKLSNPR---QFHYLNQSK 290
Cdd:cd14907    161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLlyGADQQLLQQLGLKNQLsgdRYDYLKKSN 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  291 TYELEGVSSAEEYKNTRRAMDIVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSS--VVKDPESrhhLQMAADLFKCD 368
Cdd:cd14907    241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSpcCVKNKET---LQIIAKLLGID 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  369 ANLLLASLCTRSILTREGIIIKALDPNAAVTSRDTLAKTVYAHLFDWLVDKINK------SVGQDPESRF--QIGVLDIY 440
Cdd:cd14907    318 EEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDtimpkdEKDQQLFQNKylSIGLLDIF 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  441 GFECFKNNSFEQFCINFANEKLQQHFNEHVFKMEQDEYRKEEIN--WSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFP 518
Cdd:cd14907    398 GFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSYTDNQDVIDLLDKPPIGIFNLLDDSCKLA 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  519 RSTHESFSMKL------FQNFRFHPRLEKPKfsetdFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGI 592
Cdd:cd14907    478 TGTDEKLLNKIkkqhknNSKLIFPNKINKDT-----FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSI 552

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  593 FPSAPEESTRSSYKFSSVSS-------RFKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAV 665
Cdd:cd14907    553 FSGEDGSQQQNQSKQKKSQKkdkflgsKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESI 632

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  666 RISLAGYPTRRNYSDFVDRFGLLapefmdesndeqaltekilsklgLGNYQLGRTKVFLR 725
Cdd:cd14907    633 RVRKQGYPYRKSYEDFYKQYSLL-----------------------KKNVLFGKTKIFMK 669

MYSc_Myh7b

cd14927

class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...

81-725

3.78e-168

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: 521.82 E-value: 3.78e-168

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS 160
Cdd:cd14927      1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  161 GESGAGKTETTKLIMQYLTFV-----------GGRATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFD 229
Cdd:cd14927     80 GESGAGKTVNTKRVIQYFAIVaalgdgpgkkaQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  230 TNGRISGAAIRTYLLERSRVVRITDPERNYHCFYQLcASGNDAEKYKL----SNPRQFHYLNQSKTyELEGVSSAEEYKN 305
Cdd:cd14927    160 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQI-LSGKKPELQDMllvsMNPYDYHFCSQGVT-TVDNMDDGEELMA 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  306 TRRAMDIVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSVVKDPESrhhLQMAADLFKCDANLLLASLCTRSILTRE 385
Cdd:cd14927    238 TDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTES---ADKAAYLMGVSSADLLKGLLHPRVKVGN 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  386 GIIIKALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQH 465
Cdd:cd14927    315 EYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQF 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  466 FNEHVFKMEQDEYRKEEINWSYIEF-IDNQDVLDLIEkKPIGVIALLDEACMFPRSTHESFSMKLFQ-------NFRfHP 537
Cdd:cd14927    395 FNHHMFILEQEEYKREGIEWVFIDFgLDLQACIDLIE-KPLGILSILEEECMFPKASDASFKAKLYDnhlgkspNFQ-KP 472

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  538 RLEKPKFSETDFTLSHYAGKVTYQTEAFLDKNRD---YTIVEhcnLLSSSKCPFVAGIF------------PSAPEESTR 602
Cdd:cd14927    473 RPDKKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDplnETVVA---IFQKSQNKLLATLYenyvgsdstedpKSGVKEKRK 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  603 SSYKFSSVSSRFKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFV 682
Cdd:cd14927    550 KAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFK 629

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*..
gi 1063726492  683 DRFGLLAPEFMDESN--DEQALTEKILSKLGLGN--YQLGRTKVFLR 725
Cdd:cd14927    630 QRYRILNPSAIPDDKfvDSRKATEKLLGSLDIDHtqYQFGHTKVFFK 676

MYSc_Myh1_insects_crustaceans

cd14909

class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...

81-725

7.28e-166

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: 515.54 E-value: 7.28e-166

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS 160
Cdd:cd14909      1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYP-VYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  161 GESGAGKTETTKLIMQYLTFVGGRATDDDR-----SVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRIS 235
Cdd:cd14909     80 GESGAGKTENTKKVIAYFATVGASKKTDEAakskgSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  236 GAAIRTYLLERSRVVRITDPERNYHCFYQLCA---SGNDAEKYKLSNPRQFHYLNQSKTyELEGVSSAEEYKNTRRAMDI 312
Cdd:cd14909    160 GADIETYLLEKARVISQQSLERSYHIFYQIMSgsvPGVKEMCLLSDNIYDYYIVSQGKV-TVPNVDDGEEFSLTDQAFDI 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  313 VGISQDEQEGIFRTLAAILHLGNVEFSS-GREHDSsvvkDPESRHHLQMAADLFKCDANLLLASLCTRSILTREGIIIKA 391
Cdd:cd14909    239 LGFTKQEKEDVYRITAAVMHMGGMKFKQrGREEQA----EQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQG 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  392 LDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVF 471
Cdd:cd14909    315 RNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMF 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  472 KMEQDEYRKEEINWSYIEF-IDNQDVLDLIEkKPIGVIALLDEACMFPRSTHESFSMKLFQN-------FRfHPRLEKPK 543
Cdd:cd14909    395 VLEQEEYKREGIDWAFIDFgMDLLACIDLIE-KPMGILSILEEESMFPKATDQTFSEKLTNThlgksapFQ-KPKPPKPG 472

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  544 FSETDFTLSHYAGKVTYQTEAFLDKNRDY---TIVEhcnLLSSSKCPFVAGIFPSAPEESTRSSYKFSSVSSR------- 613
Cdd:cd14909    473 QQAAHFAIAHYAGCVSYNITGWLEKNKDPlndTVVD---QFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKgggfatv 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  614 ---FKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAP 690
Cdd:cd14909    550 ssaYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNP 629

                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 1063726492  691 EFMDESNDEQALTEKILSKLGLG--NYQLGRTKVFLR 725
Cdd:cd14909    630 AGIQGEEDPKKAAEIILESIALDpdQYRLGHTKVFFR 666

MYSc_Myo39

cd14900

class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...

83-689

8.03e-166

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: 513.70 E-value: 8.03e-166

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   83 VLYNLQRRYALNDIYTYTGSILIAVNPFKKLPHLYNGHMMEQYMgAPFGELS------------PHVFAVSDVAYRAMID 150
Cdd:cd14900      3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPGLYSSDTMAKYL-LSFEARSsstrnkgsdpmpPHIYQVAGEAYKAMML 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  151 ----DSRSQSILVSGESGAGKTETTKLIMQYLTFVGG-------RATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSR 219
Cdd:cd14900     82 glngVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDnnlaasvSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  220 FGKFVEIQFDTNGRISGAAIRTYLLERSRVVRITDPERNYHCFYQLCASGNDAEKyklsnprqfhylnqsktyelegvsS 299
Cdd:cd14900    162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAAR------------------------K 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  300 AEEYKNTRRAMDIVGISQDEQEGIFRTLAAILHLGNVEFssgrEHDSSVVKD--------PESRHHLQMAADLFKCDANL 371
Cdd:cd14900    218 RDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTF----EHDENSDRLgqlksdlaPSSIWSRDAAATLLSVDATK 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  372 LLASLCTRSILTREGIIIKALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQ-----IGVLDIYGFECFK 446
Cdd:cd14900    294 LEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKSHgglhfIGILDIFGFEVFP 373

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  447 NNSFEQFCINFANEKLQQHFNEHVFKMEQDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFS 526
Cdd:cd14900    374 KNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRPTGILSLIDEECVMPKGSDTTLA 453

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  527 MKLFQNFRFHPRLEKPKFSETD--FTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLlssskcpFVAGIfpsapeestrss 604
Cdd:cd14900    454 SKLYRACGSHPRFSASRIQRARglFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDL-------FVYGL------------ 514

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  605 ykfssvssRFKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDR 684
Cdd:cd14900    515 --------QFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVAR 586


                   ....*
gi 1063726492  685 FGLLA 689
Cdd:cd14900    587 YFSLA 591

MYSc_Myo19

cd14880

class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...

81-724

6.54e-162

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: 504.77 E-value: 6.54e-162

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPHLYNGHMMEQYMGAPFGE-LSPHVFAVSDVAYRAM--IDDSRSQSI 157
Cdd:cd14880      1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPQLYSPELMREYHAAPQPQkLKPHIFTVGEQTYRNVksLIEPVNQSI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  158 LVSGESGAGKTETTKLIMQYLTFVGGRATDDDRS-----VEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNG 232
Cdd:cd14880     81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHkiaerIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  233 RISGAAIRTYLLERSRVVRITDPERNYHCFYQLC--ASGNDAEKYKLSNPRQFHYLNQSKtyelegvSSAEE--YKNTRR 308
Cdd:cd14880    161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICkgASADERLQWHLPEGAAFSWLPNPE-------RNLEEdcFEVTRE 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  309 AMDIVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSVVKDPESRHHLQMAADLFKCDANLLLASLCTRSILT-REGI 387
Cdd:cd14880    234 AMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAgKQQQ 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  388 IIKALDPNAAV-TSRDTLAKTVYAHLFDWLVDKINKSVGQDPES--RFqIGVLDIYGFECFKNNSFEQFCINFANEKLQQ 464
Cdd:cd14880    314 VFKKPCSRAECdTRRDCLAKLIYARLFDWLVSVINSSICADTDSwtTF-IGLLDVYGFESFPENSLEQLCINYANEKLQQ 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  465 HFNEHVFKMEQDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHES-FSMKLFQNFRFHPRLEKPK 543
Cdd:cd14880    393 HFVAHYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSPISICSLINEECRLNRPSSAAqLQTRIESALAGNPCLGHNK 472

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  544 FS-ETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSAPEE------STRSSYKFSSVSSRFKQ 616
Cdd:cd14880    473 LSrEPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEktqeepSGQSRAPVLTVVSKFKA 552

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  617 QLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMDES 696
Cdd:cd14880    553 SLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLRRLRPHTS 632

                          650       660
                   ....*....|....*....|....*...
gi 1063726492  697 NDEQALTEkilSKLGLGNYQLGRTKVFL 724
Cdd:cd14880    633 SGPHSPYP---AKGLSEPVHCGRTKVFM 657

MYSc_Myo34

cd14895

class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...

87-725

9.82e-162

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: 505.64 E-value: 9.82e-162

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   87 LQRRYALNDIYTYTGSILIAVNPFKKLPHLYNGHMMEQYMGApFGELSPHVFAVSDVAYRAM-------IDDSRSQSILV 159
Cdd:cd14895      7 LAQRYGVDQVYCRSGAVLIAVNPFKHIPGLYDLHKYREEMPG-WTALPPHVFSIAEGAYRSLrrrlhepGASKKNQTILV 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  160 SGESGAGKTETTKLIMQYL------TFVGGRATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQF----- 228
Cdd:cd14895     86 SGESGAGKTETTKFIMNYLaesskhTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFVRMFFeghel 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  229 DTNGRISGAAIRTYLLERSRVVRITDPERNYHCFYQLCASGNDAEKYKLS----NPRQFHYLNQSKTYEL-EGVSSAEEY 303
Cdd:cd14895    166 DTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQlellSAQEFQYISGGQCYQRnDGVRDDKQF 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  304 KNTRRAMDIVGISQDEQEGIFRTLAAILHLGNVEFSSGRE----HDSSVVKDP-----------ESRHHLQMAADLFKCD 368
Cdd:cd14895    246 QLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEdegeEDNGAASAPcrlasaspsslTVQQHLDIVSKLFAVD 325

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  369 ANLLLASLCTRSILTREGIIIKALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQ-----------IGVL 437
Cdd:cd14895    326 QDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNPnkaankdttpcIAVL 405

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  438 DIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKMEQDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMF 517
Cdd:cd14895    406 DIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRPSGIFSLLDEECVV 485

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  518 PRSTHESFSMKLFQNFRFHPRLEKPKFSETD--FTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIF-P 594
Cdd:cd14895    486 PKGSDAGFARKLYQRLQEHSNFSASRTDQADvaFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGKTSDAHLRELFeF 565

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  595 SAPEESTRSSYKFSSVSSR------------FKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVL 662
Cdd:cd14895    566 FKASESAELSLGQPKLRRRssvlssvgigsqFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVL 645

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063726492  663 EAVRISLAGYPTRRNYSDFVDRFGLLAPEFMDESNDEQALTEKiLSKLGLgnyQLGRTKVFLR 725
Cdd:cd14895    646 KAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIET-LKVDHA---ELGKTRVFLR 704

MYSc_Myh10

cd14920

class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...

81-725

1.12e-161

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: 504.54 E-value: 1.12e-161

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS 160
Cdd:cd14920      1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  161 GESGAGKTETTKLIMQYLTFV-----GGRATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRIS 235
Cdd:cd14920     80 GESGAGKTENTKKVIQYLAHVasshkGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  236 GAAIRTYLLERSRVVRITDPERNYHCFYQ-LCASGNDAEKYKLSNP-RQFHYLNQSkTYELEGVSSAEEYKNTRRAMDIV 313
Cdd:cd14920    160 GANIETYLLEKSRAVRQAKDERTFHIFYQlLSGAGEHLKSDLLLEGfNNYRFLSNG-YIPIPGQQDKDNFQETMEAMHIM 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  314 GISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSVVKDPESRHHLqmaadlfkCDANLLLASLCTRSILT------REgI 387
Cdd:cd14920    239 GFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL--------CHLLGMNVMEFTRAILTprikvgRD-Y 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  388 IIKALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVG--QDPESRFqIGVLDIYGFECFKNNSFEQFCINFANEKLQQH 465
Cdd:cd14920    310 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrtKRQGASF-IGILDIAGFEIFELNSFEQLCINYTNEKLQQL 388

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  466 FNEHVFKMEQDEYRKEEINWSYIEF-IDNQDVLDLIEK--KPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKP 542
Cdd:cd14920    389 FNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKP 468

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  543 K--FSETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIF------------PSAPEESTRSSYKFS 608
Cdd:cd14920    469 RqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdvdrivgldqvTGMTETAFGSAYKTK 548

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  609 SVSSR-----FKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVD 683
Cdd:cd14920    549 KGMFRtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 628

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 1063726492  684 RFGLLAPE-----FMDesnDEQAlTEKILSKLGLGN--YQLGRTKVFLR 725
Cdd:cd14920    629 RYEILTPNaipkgFMD---GKQA-CERMIRALELDPnlYRIGQSKIFFR 673

MYSc_Myo41

cd14902

class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...

81-690

4.04e-161

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: 504.43 E-value: 4.04e-161

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPHLYNGHMMEQY--------MGAPFGELSPHVFAVSDVAYRAMIDDS 152
Cdd:cd14902      1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPDLYSESQLNAYkasmtstsPVSQLSELPPHVFAIGGKAFGGLLKPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  153 R-SQSILVSGESGAGKTETTKLIMQYLTFVG------GRATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVE 225
Cdd:cd14902     81 RrNQSILVSGESGSGKTESTKFLMQFLTSVGrdqsstEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  226 IQFDTNGRISGAAIRTYLLERSRVVRITDPERNYHCFYQLCASGND--AEKYKLSNPRQFHYLNQSKTYE----LEGVSS 299
Cdd:cd14902    161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKtlLDLLGLQKGGKYELLNSYGPSFarkrAVADKY 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  300 AEEYKNTRRAMDIVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSVVKDPESRHHLQMAADLFKCDANLLLASLCTR 379
Cdd:cd14902    241 AQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRFHLAKCAELMGVDVDKLETLLSSR 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  380 SILTREGIIIKALDPNAAVTSRDTLAKTVYAHLFDWLVDKINK---------SVGQDPESRFQIGVLDIYGFECFKNNSF 450
Cdd:cd14902    321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDeinyfdsavSISDEDEELATIGILDIFGFESLNRNGF 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  451 EQFCINFANEKLQQHFNEHVFKMEQDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLf 530
Cdd:cd14902    401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSNGLFSLLDQECLMPKGSNQALSTKF- 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  531 qnFRFHPRLEKpkfsetdFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIF-------PSAPEESTRS 603
Cdd:cd14902    480 --YRYHGGLGQ-------FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGadenrdsPGADNGAAGR 550

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  604 SYKFS----SVSSRFKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYS 679
Cdd:cd14902    551 RRYSMlrapSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHA 630

                          650
                   ....*....|.
gi 1063726492  680 DFVDRFGLLAP 690
Cdd:cd14902    631 SFIELFSGFKC 641

MYSc_Myo28

cd14889

class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...

83-725

2.50e-160

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: 500.59 E-value: 2.50e-160

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   83 VLYNLQRRYALNDIYTYTGSILIAVNPFKKLpHLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMID----DSRSQSIL 158
Cdd:cd14889      3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYL-HIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLGrlarGPKNQCIV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  159 VSGESGAGKTETTKLIMQYLTfvggRATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFdTNGRISGAA 238
Cdd:cd14889     82 ISGESGAGKTESTKLLLRQIM----ELCRGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAK 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  239 IRTYLLERSRVVRITDPERNYHCFYQLCA--SGNDAEKYKLSNPRQFHYLNQSKTYELEGVSSAEEYKNTRRAMDIVGIS 316
Cdd:cd14889    157 INEYLLEKSRVVHQDGGEENFHIFYYMFAgiSAEDRENYGLLDPGKYRYLNNGAGCKREVQYWKKKYDEVCNAMDMVGFT 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  317 QDEQEGIFRTLAAILHLGNVEFSSgreHDSSVVK-DPESRHHLQMAADLFKCDANLLLASLCTRSILTREGIIIKALDPN 395
Cdd:cd14889    237 EQEEVDMFTILAGILSLGNITFEM---DDDEALKvENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQ 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  396 AAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRF---QIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFK 472
Cdd:cd14889    314 QAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSVelrEIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFL 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  473 MEQDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKPKFSETDFTLS 552
Cdd:cd14889    394 MEQKEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYYGKSRSKSPKFTVN 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  553 HYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIF----------------PSAPEE---STRssykFSSVSSR 613
Cdd:cd14889    474 HYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFtatrsrtgtlmpraklPQAGSDnfnSTR----KQSVGAQ 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  614 FKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFM 693
Cdd:cd14889    550 FKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILLCEPA 629

                          650       660       670
                   ....*....|....*....|....*....|..
gi 1063726492  694 DESNDEQALteKILSKLGLGNYQLGRTKVFLR 725
Cdd:cd14889    630 LPGTKQSCL--RILKATKLVGWKCGKTRLFFK 659

MYSc_Myh3

cd14913

class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...

82-725

4.50e-158

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: 494.95 E-value: 4.50e-158

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   82 GVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVSG 161
Cdd:cd14913      2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  162 ESGAGKTETTKLIMQY---LTFVGGRATDDDRS----VEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRI 234
Cdd:cd14913     81 ESGAGKTVNTKRVIQYfatIAATGDLAKKKDSKmkgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  235 SGAAIRTYLLERSRVVRITDPERNYHCFYQLCaSGNDAEKYKL----SNPRQFHYLNQSKTyELEGVSSAEEYKNTRRAM 310
Cdd:cd14913    161 ASADIETYLLEKSRVTFQLKAERSYHIFYQIL-SNKKPELIELllitTNPYDYPFISQGEI-LVASIDDAEELLATDSAI 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  311 DIVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSvvkDPESRHHLQMAADLFKCDANLLLASLCTRSILTREGIIIK 390
Cdd:cd14913    239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQA---EPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTK 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  391 ALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQD-PESRFqIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEH 469
Cdd:cd14913    316 GQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKlPRQHF-IGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHH 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  470 VFKMEQDEYRKEEINWSYIEF-IDNQDVLDLIEkKPIGVIALLDEACMFPRSTHESFSMKLF-QNFRFHPRLEKPKF--- 544
Cdd:cd14913    395 MFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKVvkg 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  545 -SETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGI---FPSAPEESTRSSYKF------SSVSSRF 614
Cdd:cd14913    474 rAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLyatFATADADSGKKKVAKkkgssfQTVSALF 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  615 KQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMD 694
Cdd:cd14913    554 RENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIP 633

                          650       660       670
                   ....*....|....*....|....*....|....*
gi 1063726492  695 ESN--DEQALTEKILSKLGLGN--YQLGRTKVFLR 725
Cdd:cd14913    634 EGQfiDSKKACEKLLASIDIDHtqYKFGHTKVFFK 668

MYSc_Myh15_mammals

cd14929

class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...

81-725

2.48e-157

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: 492.57 E-value: 2.48e-157

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS 160
Cdd:cd14929      1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  161 GESGAGKTETTKLIMQYLTFVGGRATDDDR--SVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAA 238
Cdd:cd14929     80 GESGAGKTVNTKHIIQYFATIAAMIESKKKlgALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSAD 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  239 IRTYLLERSRVVRITDPERNYHCFYQLCASGNDAEKYKL--SNPRQFHYLNQSkTYELEGVSSAEEYKNTRRAMDIVGIS 316
Cdd:cd14929    160 IDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLvsANPSDFHFCSCG-AVAVESLDDAEELLATEQAMDILGFL 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  317 QDEQEGIFRTLAAILHLGNVEFSSG-REHDSsvvkDPESRHHLQMAADLFKCDANLLLASLCTRSILTREGIIIKALDPN 395
Cdd:cd14929    239 PDEKYGCYKLTGAIMHFGNMKFKQKpREEQL----EADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIE 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  396 AAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKMEQ 475
Cdd:cd14929    315 QVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQ 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  476 DEYRKEEINWSYIEF-IDNQDVLDLIEkKPIGVIALLDEACMFPRSTHESFSMKLFQN-FRFHPRLEKPKFS----ETDF 549
Cdd:cd14929    395 EEYRKEGIDWVSIDFgLDLQACIDLIE-KPMGIFSILEEECMFPKATDLTFKTKLFDNhFGKSVHFQKPKPDkkkfEAHF 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  550 TLSHYAGKVTYQTEAFLDKNRDY---TIVEhcnLLSSSKCPFVAGIFP------SAP---EESTRSSYKFSSVSSRFKQQ 617
Cdd:cd14929    474 ELVHYAGVVPYNISGWLEKNKDLlneTVVA---VFQKSSNRLLASLFEnyistdSAIqfgEKKRKKGASFQTVASLHKEN 550

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  618 LQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMDESN 697
Cdd:cd14929    551 LNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSK 630

                          650       660       670
                   ....*....|....*....|....*....|..
gi 1063726492  698 --DEQALTEKILSKLGLGN--YQLGRTKVFLR 725
Cdd:cd14929    631 fvSSRKAAEELLGSLEIDHtqYRFGITKVFFK 662

PTZ00014

myosin-A; Provisional

10-803

2.14e-154

myosin-A; Provisional

Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 490.31 E-value: 2.14e-154

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   10 NLRKGDKVWV-------EDKDLAWIAADVL-DSFDNKLH---VETSTGKKVFVSPEKLFRRDpddeehNGVDDMT----- 73
Cdd:PTZ00014    29 NVLKGFYVWTdkapavkEDPDLMFAKCLVLpGSTGEKLTlkqIDPPTNSTFEVKPEHAFNAN------SQIDPMTygdig 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   74 KLTYLHEAGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPHLYNgHMMEQYMGAP-FGELSPHVFAVSDVAYRAMIDDS 152
Cdd:PTZ00014   103 LLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTN-DWIRRYRDAKdSDKLPPHVFTTARRALENLHGVK 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  153 RSQSILVSGESGAGKTETTKLIMQYltFVGGRATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNG 232
Cdd:PTZ00014   182 KSQTIIVSGESGAGKTEATKQIMRY--FASSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEG 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  233 RISGAAIRTYLLERSRVVRITDPERNYHCFYQLCASGNDA--EKYKLSNPRQFHYLNqSKTYELEGVSSAEEYKNTRRAM 310
Cdd:PTZ00014   260 GIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEmkEKYKLKSLEEYKYIN-PKCLDVPGIDDVKDFEEVMESF 338

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  311 DIVGISQDEQEGIFRTLAAILHLGNVEFSS---GREHDSSVVkDPESRHHLQMAADLFKCDANLLLASLCTRSILTREGI 387
Cdd:PTZ00014   339 DSMGLSESQIEDIFSILSGVLLLGNVEIEGkeeGGLTDAAAI-SDESLEVFNEACELLFLDYESLKKELTVKVTYAGNQK 417

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  388 IIKALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVgqDPESRFQ--IGVLDIYGFECFKNNSFEQFCINFANEKLQQH 465
Cdd:PTZ00014   418 IEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATI--EPPGGFKvfIGMLDIFGFEVFKNNSLEQLFINITNEMLQKN 495

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  466 FNEHVFKMEQDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKPKFS 545
Cdd:PTZ00014   496 FVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVD 575

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  546 ET-DFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSAPEESTRsSYKFSSVSSRFKQQLQALMET 624
Cdd:PTZ00014   576 SNkNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKGK-LAKGQLIGSQFLNQLDSLMSL 654

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  625 LSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLL-APEFMDESNDEQALT 703
Cdd:PTZ00014   655 INSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLdLAVSNDSSLDPKEKA 734

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  704 EKILSKLGLGN--YQLGRTKVFLRAGQIGILdsrraevldasARLIQRRLRTFvthQNFISARASAISIQAYCRgclsrn 781
Cdd:PTZ00014   735 EKLLERSGLPKdsYAIGKTMVFLKKDAAKEL-----------TQIQREKLAAW---EPLVSVLEALILKIKKKR------ 794

                          810       820
                   ....*....|....*....|..
gi 1063726492  782 ayATRRNAAAAVLVQKHVRRWL 803
Cdd:PTZ00014   795 --KVRKNIKSLVRIQAHLRRHL 814

MYSc_Myh16

cd14934

class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...

81-725

7.59e-154

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: 483.38 E-value: 7.59e-154

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS 160
Cdd:cd14934      1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLP-IYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  161 GESGAGKTETTKLIMQYLTFVGG---RATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGA 237
Cdd:cd14934     80 GESGAGKTENTKKVIQYFANIGGtgkQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  238 AIRTYLLERSRVVRITDPERNYHCFYQLCASGNDAEKYKL---SNPRQFHYLNQSKTYeLEGVSSAEEYKNTRRAMDIVG 314
Cdd:cd14934    160 DIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLllvPNPKEYHWVSQGVTV-VDNMDDGEELQITDVAFDVLG 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  315 ISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSVVKDPESRHHLqmaADLFKCDANLLLASLCTRSILTREGIIIKALDP 394
Cdd:cd14934    239 FSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKV---AHLMGLNSGELQKGITRPRVKVGNEFVQKGQNM 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  395 NAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKME 474
Cdd:cd14934    316 EQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLE 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  475 QDEYRKEEINWSYIEF-IDNQDVLDLIEkKPIGVIALLDEACMFPRSTHESFSMKLFQNFR------FHPRLEKPKFSET 547
Cdd:cd14934    396 QEEYKREGIEWVFIDFgLDLQACIDLLE-KPMGIFSILEEQCVFPKATDATFKAALYDNHLgkssnfLKPKGGKGKGPEA 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  548 DFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIF-----PSAPEESTRSSYKFSSVSSrFKQQLQALM 622
Cdd:cd14934    475 HFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFkeeeaPAGSKKQKRGSSFMTVSNF-YREQLNKLM 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  623 ETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMDES-NDEQA 701
Cdd:cd14934    554 TTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQGfVDNKK 633

                          650       660
                   ....*....|....*....|....*.
gi 1063726492  702 LTEKILSKLGLG--NYQLGRTKVFLR 725
Cdd:cd14934    634 ASELLLGSIDLDvnEYKIGHTKVFFR 659

MYSc_Myh18

cd14932

class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...

81-725

6.30e-152

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: 478.75 E-value: 6.30e-152

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS 160
Cdd:cd14932      1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLP-IYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  161 GESGAGKTETTKLIMQYLTFVG---------GRATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTN 231
Cdd:cd14932     80 GESGAGKTENTKKVIQYLAYVAssfktkkdqSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  232 GRISGAAIRTYLLERSRVVRITDPERNYHCFYQLCASGNDAEKYK--LSNPRQFHYLNQSKTyELEGVSSAEEYKNTRRA 309
Cdd:cd14932    160 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSElcLEDYSKYRFLSNGNV-TIPGQQDKELFAETMEA 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  310 MDIVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSVVKDPESRhhlQMAADLFKCDANLLLASLCTRSILTREGIII 389
Cdd:cd14932    239 FRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAA---QKVCHLLGMNVTDFTRAILSPRIKVGRDYVQ 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  390 KALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQ-IGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNE 468
Cdd:cd14932    316 KAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASfIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  469 HVFKMEQDEYRKEEINWSYIEF-IDNQDVLDLIEKK--PIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKPK-- 543
Cdd:cd14932    396 TMFILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKkl 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  544 FSETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPF----------------VAGIFPSAPEESTRSSYKF 607
Cdd:cd14932    476 KDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFvselwkdvdrivgldkVAGMGESLHGAFKTRKGMF 555

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  608 SSVSSRFKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGL 687
Cdd:cd14932    556 RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 635

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....
gi 1063726492  688 LAPE-----FMDesnDEQALTEKILS-KLGLGNYQLGRTKVFLR 725
Cdd:cd14932    636 LTPNaipkgFMD---GKQACVLMVKAlELDPNLYRIGQSKVFFR 676

MYSc_Myo35

cd14896

class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...

83-725

4.22e-151

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: 475.42 E-value: 4.22e-151

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   83 VLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVSGE 162
Cdd:cd14896      3 VLLCLKKRFHLGRIYTFGGPILLSLNPHRSLP-LFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSGH 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  163 SGAGKTETTKLIMQYLTFVGGRATDDDRSVEQQVLesnPLLEAFGNAKTVRNDNSSRFGKFVEIQFdTNGRISGAAIRTY 242
Cdd:cd14896     82 SGSGKTEAAKKIVQFLSSLYQDQTEDRLRQPEDVL---PILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVSHY 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  243 LLERSRVVRITDPERNYHCFYQLCASGNDAEKYKLS--NPRQFHYLNQSKTYELEGVSSAEEYKNTRRAMDIVGISQDEQ 320
Cdd:cd14896    158 LLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSlqGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAEEL 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  321 EGIFRTLAAILHLGNVEFSSgREHDSSVVKDPESRHHLQMAADLFKCDANLLLASLCTRSILTREGIIIKALDPNAAVTS 400
Cdd:cd14896    238 TAIWAVLAAILQLGNICFSS-SERESQEVAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAIDA 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  401 RDTLAKTVYAHLFDWLVDKINK--SVGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKMEQDEY 478
Cdd:cd14896    317 RDALAKTLYSRLFTWLLKRINAwlAPPGEAESDATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEEEC 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  479 RKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKPKFSETDFTLSHYAGKV 558
Cdd:cd14896    397 QRELLPWVPIPQPPRESCLDLLVDQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQLPLPVFTVRHYAGTV 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  559 TYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSApEESTRSSYKFSSVSSRFKQQLQALMETLSKTEPHYVRCVKP 638
Cdd:cd14896    477 TYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEA-EPQYGLGQGKPTLASRFQQSLGDLTARLGRSHVYFIHCLNP 555

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  639 NSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMDESNDEQALTeKILSKLgLGN---- 714
Cdd:cd14896    556 NPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEALSDRERCG-AILSQV-LGAespl 633

                          650
                   ....*....|.
gi 1063726492  715 YQLGRTKVFLR 725
Cdd:cd14896    634 YHLGATKVLLK 644

MYSc_Myh7

cd14917

class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...

82-725

8.30e-150

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: 472.67 E-value: 8.30e-150

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   82 GVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVSG 161
Cdd:cd14917      2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  162 ESGAGKTETTKLIMQYLTFV---GGRATDDDR----SVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRI 234
Cdd:cd14917     81 ESGAGKTVNTKRVIQYFAVIaaiGDRSKKDQTpgkgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  235 SGAAIRTYLLERSRVVRITDPERNYHCFYQLCaSGNDAEKYKL----SNPRQFHYLNQSKTyELEGVSSAEEYKNTRRAM 310
Cdd:cd14917    161 ASADIETYLLEKSRVIFQLKAERDYHIFYQIL-SNKKPELLDMllitNNPYDYAFISQGET-TVASIDDAEELMATDNAF 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  311 DIVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSvvkDPESRHHLQMAADLFKCDANLLLASLCTRSILTREGIIIK 390
Cdd:cd14917    239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQA---EPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTK 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  391 ALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHV 470
Cdd:cd14917    316 GQNVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  471 FKMEQDEYRKEEINWSYIEF-IDNQDVLDLIEkKPIGVIALLDEACMFPRSTHESFSMKLFQN-FRFHPRLEKPKF---- 544
Cdd:cd14917    396 FVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNhLGKSNNFQKPRNikgk 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  545 SETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPS-----APEE----STRSSYKFSSVSSRFK 615
Cdd:cd14917    475 PEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANyagadAPIEkgkgKAKKGSSFQTVSALHR 554

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  616 QQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMDE 695
Cdd:cd14917    555 ENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPE 634

                          650       660       670
                   ....*....|....*....|....*....|....
gi 1063726492  696 SN--DEQALTEKILSKLGL--GNYQLGRTKVFLR 725
Cdd:cd14917    635 GQfiDSRKGAEKLLSSLDIdhNQYKFGHTKVFFK 668

MYSc_Myh8

cd14918

class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...

82-725

3.02e-149

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: 471.14 E-value: 3.02e-149

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   82 GVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVSG 161
Cdd:cd14918      2 GVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  162 ESGAGKTETTKLIMQYLTFVG--GRATDDDR-----SVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRI 234
Cdd:cd14918     81 ESGAGKTVNTKRVIQYFATIAvtGEKKKEESgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  235 SGAAIRTYLLERSRVVRITDPERNYHCFYQLCASGN-DAEKYKL--SNPRQFHYLNQSKTyELEGVSSAEEYKNTRRAMD 311
Cdd:cd14918    161 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpDLIEMLLitTNPYDYAFVSQGEI-TVPSIDDQEELMATDSAID 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  312 IVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSvvkDPESRHHLQMAADLFKCDANLLLASLCTRSILTREGIIIKA 391
Cdd:cd14918    240 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQA---EPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  392 LDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVF 471
Cdd:cd14918    317 QTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  472 KMEQDEYRKEEINWSYIEF-IDNQDVLDLIEkKPIGVIALLDEACMFPRSTHESFSMKLF-QNFRFHPRLEKPKF----S 545
Cdd:cd14918    397 VLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVvkgkA 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  546 ETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIF---------PSAPEESTRSSYKFSSVSSRFKQ 616
Cdd:cd14918    476 EAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFstyasaeadSGAKKGAKKKGSSFQTVSALFRE 555

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  617 QLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMDES 696
Cdd:cd14918    556 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEG 635

                          650       660       670
                   ....*....|....*....|....*....|...
gi 1063726492  697 N--DEQALTEKILSKLGLGN--YQLGRTKVFLR 725
Cdd:cd14918    636 QfiDSKKASEKLLASIDIDHtqYKFGHTKVFFK 668

MYSc_Myh4

cd14915

class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...

82-725

5.43e-148

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: 468.05 E-value: 5.43e-148

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   82 GVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVSG 161
Cdd:cd14915      2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  162 ESGAGKTETTKLIMQYLTFV---GGRATDDDRS------VEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNG 232
Cdd:cd14915     81 ESGAGKTVNTKRVIQYFATIavtGEKKKEEAASgkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  233 RISGAAIRTYLLERSRVVRITDPERNYHCFYQLcASGNDAEKYKL----SNPRQFHYLNQSKTyELEGVSSAEEYKNTRR 308
Cdd:cd14915    161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQI-MSNKKPELIEMllitTNPYDFAFVSQGEI-TVPSIDDQEELMATDS 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  309 AMDIVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSvvkDPESRHHLQMAADLFKCDANLLLASLCTRSILTREGII 388
Cdd:cd14915    239 AVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQA---EPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYV 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  389 IKALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNE 468
Cdd:cd14915    316 TKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  469 HVFKMEQDEYRKEEINWSYIEF-IDNQDVLDLIEkKPIGVIALLDEACMFPRSTHESFSMKLF-QNFRFHPRLEKPK--- 543
Cdd:cd14915    396 HMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYeQHLGKSNNFQKPKpak 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  544 -FSETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFP---SAPEE-------STRSSYKFSSVSS 612
Cdd:cd14915    475 gKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSggqTAEAEggggkkgGKKKGSSFQTVSA 554

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  613 RFKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEF 692
Cdd:cd14915    555 LFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASA 634

                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 1063726492  693 MDESN--DEQALTEKILSKLGLGN--YQLGRTKVFLR 725
Cdd:cd14915    635 IPEGQfiDSKKASEKLLGSIDIDHtqYKFGHTKVFFK 671

MYSc_Myh1_mammals

cd14910

class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...

82-725

1.10e-147

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: 467.29 E-value: 1.10e-147

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   82 GVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVSG 161
Cdd:cd14910      2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  162 ESGAGKTETTKLIMQYLTFVGgrATDDDR-----------SVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDT 230
Cdd:cd14910     81 ESGAGKTVNTKRVIQYFATIA--VTGEKKkeeatsgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  231 NGRISGAAIRTYLLERSRVVRITDPERNYHCFYQLCASGN-DAEKYKL--SNPRQFHYLNQSKTyELEGVSSAEEYKNTR 307
Cdd:cd14910    159 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKpDLIEMLLitTNPYDYAFVSQGEI-TVPSIDDQEELMATD 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  308 RAMDIVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSvvkDPESRHHLQMAADLFKCDANLLLASLCTRSILTREGI 387
Cdd:cd14910    238 SAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQA---EPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEY 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  388 IIKALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFN 467
Cdd:cd14910    315 VTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  468 EHVFKMEQDEYRKEEINWSYIEF-IDNQDVLDLIEkKPIGVIALLDEACMFPRSTHESFSMKLF-QNFRFHPRLEKPKFS 545
Cdd:cd14910    395 HHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYeQHLGKSNNFQKPKPA 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  546 ----ETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSAPEEST----------RSSYKFSSVS 611
Cdd:cd14910    474 kgkvEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAeegggkkggkKKGSSFQTVS 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  612 SRFKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPE 691
Cdd:cd14910    554 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAS 633

                          650       660       670
                   ....*....|....*....|....*....|....*...
gi 1063726492  692 FMDESN--DEQALTEKILSKLGLGN--YQLGRTKVFLR 725
Cdd:cd14910    634 AIPEGQfiDSKKASEKLLGSIDIDHtqYKFGHTKVFFK 671

MYSc_Myh9

cd14919

class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...

81-725

3.30e-147

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: 465.72 E-value: 3.30e-147

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS 160
Cdd:cd14919      1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  161 GESGAGKTETTKLIMQYLTFVGG--RATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAA 238
Cdd:cd14919     80 GESGAGKTENTKKVIQYLAHVASshKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  239 IRTYLLERSRVVRITDPERNYHCFYQLCASGNDAEKYK-LSNPRQFHYLNQSKTYELEGVSSAEEYKNTRRAMDIVGISQ 317
Cdd:cd14919    160 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDlLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  318 DEQEGIFRTLAAILHLGNVEFSSGREHDSSVVKDPESRhhlQMAADLFKCDANLLLASLCTRSILTREGIIIKALDPNAA 397
Cdd:cd14919    240 EEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAA---QKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQA 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  398 VTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQ-IGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKMEQD 476
Cdd:cd14919    317 DFAIEALAKATYERMFRWLVLRINKALDKTKRQGASfIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQE 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  477 EYRKEEINWSYIEF-IDNQDVLDLIEKK--PIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKPK--FSETDFTL 551
Cdd:cd14919    397 EYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKqlKDKADFCI 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  552 SHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPF----------------VAGIFPSA-PEESTRSSYKFSSVSSRF 614
Cdd:cd14919    477 IHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFvselwkdvdriigldqVAGMSETAlPGAFKTRKGMFRTVGQLY 556

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  615 KQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPE--- 691
Cdd:cd14919    557 KEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNsip 636

                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 1063726492  692 --FMDesnDEQALTEKILS-KLGLGNYQLGRTKVFLR 725
Cdd:cd14919    637 kgFMD---GKQACVLMIKAlELDSNLYRIGQSKVFFR 670

MYSc_Myo45

cd14906

class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...

81-724

7.49e-147

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: 466.38 E-value: 7.49e-147

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPHLYNGHMMEQYMGAPF-GELSPHVFAVSDVAYRAMIDDSRSQSILV 159
Cdd:cd14906      1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISSIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  160 SGESGAGKTETTKLIMQYLTFVGGRAT-------DDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFD-TN 231
Cdd:cd14906     81 SGESGSGKTEASKTILQYLINTSSSNQqqnnnnnNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRsSD 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  232 GRISGAAIRTYLLERSRVVRITDPER-NYHCFYQLC--ASGNDAEKYKL-SNPRQFHYLNQSK--------------TYE 293
Cdd:cd14906    161 GKIDGASIETYLLEKSRISHRPDNINlSYHIFYYLVygASKDERSKWGLnNDPSKYRYLDARDdvissfksqssnknSNH 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  294 LEGVSSAEEYKNTRRAMDIVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSVVKDPESRHHLQMAADLFKCDANLLL 373
Cdd:cd14906    241 NNKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLESVSKLLGYIESVFK 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  374 ASLCTRSILT--REGIIIKALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESR-----------FQIGVLDIY 440
Cdd:cd14906    321 QALLNRNLKAggRGSVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSNdlaggsnkknnLFIGVLDIF 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  441 GFECFKNNSFEQFCINFANEKLQQHFNEHVFKMEQDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRS 520
Cdd:cd14906    401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKSDGILSLLDDECIMPKG 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  521 THESFSMKLFQNFRFHPRLEKPKFSETDFTLSHYAGKVTYQTEAFLDKNRD--YTIVEhcNLLSSSKCPFVAGIFP---S 595
Cdd:cd14906    481 SEQSLLEKYNKQYHNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDslYSDVE--DLLLASSNFLKKSLFQqqiT 558

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  596 APEESTRSSYKFSSVSSRFKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTR 675
Cdd:cd14906    559 STTNTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYR 638

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063726492  676 RNYSDFVDRFGLLAPEFMDESNDEQAL--------TEKILSKLGLGN-------------------YQLGRTKVFL 724
Cdd:cd14906    639 RDFNQFFSRYKCIVDMYNRKNNNNPKLasqlilqnIQSKLKTMGISNnkkknnsnsnsnttndkplFQIGKTKIFI 714

MYSc_Myh6

cd14916

class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...

82-725

2.28e-146

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: 463.76 E-value: 2.28e-146

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   82 GVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVSG 161
Cdd:cd14916      2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  162 ESGAGKTETTKLIMQY---LTFVGGRATDDDR-----SVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGR 233
Cdd:cd14916     81 ESGAGKTVNTKRVIQYfasIAAIGDRSKKENPnankgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  234 ISGAAIRTYLLERSRVVRITDPERNYHCFYQLCaSGNDAEKYKL----SNPRQFHYLNQSKTyELEGVSSAEEYKNTRRA 309
Cdd:cd14916    161 LASADIETYLLEKSRVIFQLKAERNYHIFYQIL-SNKKPELLDMllvtNNPYDYAFVSQGEV-SVASIDDSEELLATDSA 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  310 MDIVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSvvkDPESRHHLQMAADLFKCDANLLLASLCTRSILTREGIII 389
Cdd:cd14916    239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQA---EPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVT 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  390 KALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEH 469
Cdd:cd14916    316 KGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHH 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  470 VFKMEQDEYRKEEINWSYIEF-IDNQDVLDLIEkKPIGVIALLDEACMFPRSTHESFSMKLFQNF-----RFH-PRLEKP 542
Cdd:cd14916    396 MFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKASDMTFKAKLYDNHlgksnNFQkPRNVKG 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  543 KfSETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSAPEEST----------RSSYKFSSVSS 612
Cdd:cd14916    475 K-QEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTgdsgkgkggkKKGSSFQTVSA 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  613 RFKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEF 692
Cdd:cd14916    554 LHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAA 633

                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 1063726492  693 MDESN--DEQALTEKILSKLGL--GNYQLGRTKVFLR 725
Cdd:cd14916    634 IPEGQfiDSRKGAEKLLGSLDIdhNQYKFGHTKVFFK 670

MYSc_Myh11

cd14921

class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...

81-725

2.74e-146

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: 463.33 E-value: 2.74e-146

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS 160
Cdd:cd14921      1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  161 GESGAGKTETTKLIMQYLTFV-----GGRATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRIS 235
Cdd:cd14921     80 GESGAGKTENTKKVIQYLAVVasshkGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  236 GAAIRTYLLERSRVVRITDPERNYHCFYQLCASGNDAEKYKLSNPRQFHYLNQSKTY-ELEGVSSAEEYKNTRRAMDIVG 314
Cdd:cd14921    160 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFvPIPAAQDDEMFQETLEAMSIMG 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  315 ISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSVVKDPESRhhlQMAADLFKCDANLLLASLCTRSILTREGIIIKALDP 394
Cdd:cd14921    240 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAA---QKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTK 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  395 NAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQ-IGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKM 473
Cdd:cd14921    317 EQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASfLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFIL 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  474 EQDEYRKEEINWSYIEF-IDNQDVLDLIEK--KPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKPK--FSETD 548
Cdd:cd14921    397 EQEEYQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKqlKDKTE 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  549 FTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIF-----------------PSAPEESTRSSYKFSSVS 611
Cdd:cd14921    477 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWkdvdrivgldqmakmteSSLPSASKTKKGMFRTVG 556

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  612 SRFKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPE 691
Cdd:cd14921    557 QLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAN 636

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|
gi 1063726492  692 -----FMDesnDEQALTEKILS-KLGLGNYQLGRTKVFLR 725
Cdd:cd14921    637 aipkgFMD---GKQACILMIKAlELDPNLYRIGQSKIFFR 673

MYSc_Myh2_mammals

cd14912

class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...

82-725

5.43e-146

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: 462.66 E-value: 5.43e-146

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   82 GVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVSG 161
Cdd:cd14912      2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  162 ESGAGKTETTKLIMQYLTFV---GGRATDDDRS------VEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNG 232
Cdd:cd14912     81 ESGAGKTVNTKRVIQYFATIavtGEKKKEEITSgkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  233 RISGAAIRTYLLERSRVVRITDPERNYHCFYQLcASGNDAEKYKL----SNPRQFHYLNQSKTyELEGVSSAEEYKNTRR 308
Cdd:cd14912    161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQI-TSNKKPELIEMllitTNPYDYPFVSQGEI-SVASIDDQEELMATDS 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  309 AMDIVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSvvkDPESRHHLQMAADLFKCDANLLLASLCTRSILTREGII 388
Cdd:cd14912    239 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQA---EPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYV 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  389 IKALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNE 468
Cdd:cd14912    316 TKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  469 HVFKMEQDEYRKEEINWSYIEF-IDNQDVLDLIEkKPIGVIALLDEACMFPRSTHESFSMKLF-QNFRFHPRLEKPKF-- 544
Cdd:cd14912    396 HMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPKVvk 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  545 --SETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFP------------SAPEESTRSSYKFSSV 610
Cdd:cd14912    475 gkAEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSgaqtaegasaggGAKKGGKKKGSSFQTV 554

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  611 SSRFKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAP 690
Cdd:cd14912    555 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNA 634

                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 1063726492  691 EFMDESN--DEQALTEKILSKLGLGN--YQLGRTKVFLR 725
Cdd:cd14912    635 SAIPEGQfiDSKKASEKLLASIDIDHtqYKFGHTKVFFK 673

MYSc_Myh13

cd14923

class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...

82-725

1.89e-144

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: 458.38 E-value: 1.89e-144

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   82 GVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVSG 161
Cdd:cd14923      2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  162 ESGAGKTETTKLIMQYLTF--VGGRATDDDR------SVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGR 233
Cdd:cd14923     81 ESGAGKTVNTKRVIQYFATiaVTGDKKKEQQpgkmqgTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  234 ISGAAIRTYLLERSRVVRITDPERNYHCFYQLcASGNDAEKYKL----SNPRQFHYLNQSKTyELEGVSSAEEYKNTRRA 309
Cdd:cd14923    161 LASADIETYLLEKSRVTFQLSSERSYHIFYQI-MSNKKPELIDLllisTNPFDFPFVSQGEV-TVASIDDSEELLATDNA 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  310 MDIVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSvvkDPESRHHLQMAADLFKCDANLLLASLCTRSILTREGIII 389
Cdd:cd14923    239 IDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQA---EPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVT 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  390 KALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEH 469
Cdd:cd14923    316 KGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  470 VFKMEQDEYRKEEINWSYIEF-IDNQDVLDLIEkKPIGVIALLDEACMFPRSTHESFSMKLF-QNFRFHPRLEKPK---- 543
Cdd:cd14923    396 MFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKpakg 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  544 FSETDFTLSHYAGKVTYQTEAFLDKNRD-----------YTIVEHCNLLSSSKCPFVAGIFPSAPEESTRSSYKFSSVSS 612
Cdd:cd14923    475 KAEAHFSLVHYAGTVDYNIAGWLDKNKDplnetvvglyqKSSLKLLSFLFSNYAGAEAGDSGGSKKGGKKKGSSFQTVSA 554

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  613 RFKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEF 692
Cdd:cd14923    555 VFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASA 634

                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 1063726492  693 MDESN--DEQALTEKILSKLGL--GNYQLGRTKVFLR 725
Cdd:cd14923    635 IPEGQfiDSKNASEKLLNSIDVdrEQYRFGHTKVFFK 671

MYSc_Myo14

cd14876

class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...

83-725

1.11e-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: 455.60 E-value: 1.11e-143

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   83 VLYNLQRRYALNDIYTYTGSILIAVNPFKKLPHLYNgHMMEQYMGAP-FGELSPHVFAVSDVAYRAMIDDSRSQSILVSG 161
Cdd:cd14876      3 VLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATD-EWIRKYRDAPdLTKLPPHVFYTARRALENLHGVNKSQTIIVSG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  162 ESGAGKTETTKLIMQYltFVGGRATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAAIRT 241
Cdd:cd14876     82 ESGAGKTEATKQIMRY--FASAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  242 YLLERSRVVRITDPERNYHCFYQLC--ASGNDAEKYKLSNPRQFHYLNqSKTYELEGVSSAEEYKNTRRAMDIVGISQDE 319
Cdd:cd14876    160 FLLEKSRIVTQDDNERSYHIFYQLLkgADSEMKSKYHLLGLKEYKFLN-PKCLDVPGIDDVADFEEVLESLKSMGLTEEQ 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  320 QEGIFRTLAAILHLGNVEFSSGREH--DSSVVKDPESRHHLQMAADLFKCDANLLLASLCTRSILTREGIIIKALDPNAA 397
Cdd:cd14876    239 IDTVFSIVSGVLLLGNVKITGKTEQgvDDAAAISNESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDDA 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  398 VTSRDTLAKTVYAHLFDWLVDKINKSVgqDPESRFQ--IGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKMEQ 475
Cdd:cd14876    319 EMLKLSLAKAMYDKLFLWIIRNLNSTI--EPPGGFKnfMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERES 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  476 DEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKPKF-SETDFTLSHY 554
Cdd:cd14876    397 KLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKVdSNINFIVVHT 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  555 AGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSAPEESTRsSYKFSSVSSRFKQQLQALMETLSKTEPHYVR 634
Cdd:cd14876    477 IGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKGK-IAKGSLIGSQFLKQLESLMGLINSTEPHFIR 555

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  635 CVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFM-DESNDEQALTEKIL--SKLG 711
Cdd:cd14876    556 CIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLGIAnDKSLDPKVAALKLLesSGLS 635

                          650
                   ....*....|....
gi 1063726492  712 LGNYQLGRTKVFLR 725
Cdd:cd14876    636 EDEYAIGKTMVFLK 649

MYSc_Myh19

cd15896

class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...

81-725

9.04e-143

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: 454.14 E-value: 9.04e-143

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS 160
Cdd:cd15896      1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  161 GESGAGKTETTKLIMQYLTFVGG-RATDDDRS--------VEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTN 231
Cdd:cd15896     80 GESGAGKTENTKKVIQYLAHVASsHKTKKDQNslalshgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  232 GRISGAAIRTYLLERSRVVRITDPERNYHCFYQLCASGNDAEKYK--LSNPRQFHYLNQSKTyELEGVSSAEEYKNTRRA 309
Cdd:cd15896    160 GYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSEllLENYNNYRFLSNGNV-TIPGQQDKDLFTETMEA 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  310 MDIVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSVVKDPESRhhlQMAADLFKCDANLLLASLCTRSILTREGIII 389
Cdd:cd15896    239 FRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAA---QKVCHLMGMNVTDFTRAILSPRIKVGRDYVQ 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  390 KALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQ-IGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNE 468
Cdd:cd15896    316 KAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASfIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  469 HVFKMEQDEYRKEEINWSYIEF-IDNQDVLDLIEK--KPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKPK-- 543
Cdd:cd15896    396 TMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIEKpaSPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKkl 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  544 FSETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSAP-----EESTRSSYKFSSVSSR----- 613
Cdd:cd15896    476 KDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDrivglDKVSGMSEMPGAFKTRkgmfr 555

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  614 -----FKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLL 688
Cdd:cd15896    556 tvgqlYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 635

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|...
gi 1063726492  689 APE-----FMDesnDEQALTEKILS-KLGLGNYQLGRTKVFLR 725
Cdd:cd15896    636 TPNaipkgFMD---GKQACVLMIKSlELDPNLYRIGQSKVFFR 675

MYSc_Myh14_mammals

cd14930

class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...

81-725

1.39e-138

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: 442.61 E-value: 1.39e-138

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS 160
Cdd:cd14930      1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  161 GESGAGKTETTKLIMQYLTFV-----GGRATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRIS 235
Cdd:cd14930     80 GESGAGKTENTKKVIQYLAHVasspkGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  236 GAAIRTYLLERSRVVRITDPERNYHCFYQLCASGNDAEKYKLSNPRQFHYlnqskTYELEGVSSA-----EEYKNTRRAM 310
Cdd:cd14930    160 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHY-----RFLTNGPSSSpgqerELFQETLESL 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  311 DIVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSVVKDPESRHHLQMAADLFKCDANlllASLCTRSILTREGIIIK 390
Cdd:cd14930    235 RVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFS---RALLTPRIKVGRDYVQK 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  391 ALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQ-IGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEH 469
Cdd:cd14930    312 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASfLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  470 VFKMEQDEYRKEEINWSYIEF-IDNQDVLDLIEK--KPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKPK--F 544
Cdd:cd14930    392 MFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRhlR 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  545 SETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFP---------------SAPEESTRSSYKFSS 609
Cdd:cd14930    472 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdvegivgleqvsslgDGPPGGRPRRGMFRT 551

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  610 VSSRFKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLA 689
Cdd:cd14930    552 VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 631

                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 1063726492  690 PEFMDES-NDEQALTEKILSKLGLGN--YQLGRTKVFLR 725
Cdd:cd14930    632 PNAIPKGfMDGKQACEKMIQALELDPnlYRVGQSKIFFR 670

MYSc_Myo25

cd14886

class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...

81-725

6.94e-137

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: 437.40 E-value: 6.94e-137

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPHLYNGHMMEQYMGA--PFG---ELSPHVFAVSDVAYRAMIDDSRSQ 155
Cdd:cd14886      1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRNLYGTEVIGRYRQAdtSRGfpsDLPPHSYAVAQSALNGLISDGISQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  156 SILVSGESGAGKTETTKLIMQYLTFvgGRATDDDrSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRIS 235
Cdd:cd14886     81 SCIVSGESGAGKTETAKQLMNFFAY--GHSTSST-DVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  236 GAAIRTYLLERSRVVRITDPERNYHCFYQlCASGNDAEK---YKLSNPRQFHYLNQSKTYELEGVSSAEEYKNTRRAMDI 312
Cdd:cd14886    158 GGKITSYMLELSRIEFQSTNERNYHIFYQ-CIKGLSPEEkksLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEK 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  313 VgISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSVVKDPESRHHLQMAADLFKCDANLLLASLCTRSILTREGIIIKAL 392
Cdd:cd14886    237 L-FSKNEIDSFYKCISGILLAGNIEFSEEGDMGVINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPV 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  393 DPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFK 472
Cdd:cd14886    316 TQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFK 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  473 MEQDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSM---KLFQNFRFHPrlekPKFSETDF 549
Cdd:cd14886    396 SEIQEYEIEGIDHSMITFTDNSNVLAVFDKPNLSIFSFLEEQCLIQTGSSEKFTSsckSKIKNNSFIP----GKGSQCNF 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  550 TLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSAPEEStrSSYKFSSVSSRFKQQLQALMETLSKTE 629
Cdd:cd14886    472 TIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNED--GNMKGKFLGSTFQLSIDQLMKTLSATK 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  630 PHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLL---APEFMDESNDEQALTEKI 706
Cdd:cd14886    550 SHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishNSSSQNAGEDLVEAVKSI 629

                          650       660
                   ....*....|....*....|.
gi 1063726492  707 LSKLGL--GNYQLGRTKVFLR 725
Cdd:cd14886    630 LENLGIpcSDYRIGKTKVFLR 650

MYSc_Myo38

cd14899

class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...

81-685

2.26e-134

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: 432.98 E-value: 2.26e-134

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPHLYNGHMMEQYM---GAPFGE-------LSPHVFAVSDVAYRAMID 150
Cdd:cd14899      1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPQLYGDEILRGYAydhNSQFGDrvtstdpREPHLFAVARAAYIDIVQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  151 DSRSQSILVSGESGAGKTETTKLIMQYLTFVGG--------------RATDDDRSVEQQVLESNPLLEAFGNAKTVRNDN 216
Cdd:cd14899     81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGtgnnnltnsesispPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  217 SSRFGKFVEIQF-DTNGRISGAAIRTYLLERSRVVRITDPERNYHCFYQL------CASGNDAEKYKLSN-PRQFHYLNQ 288
Cdd:cd14899    161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELlsadnnCVSKEQKQVLALSGgPQSFRLLNQ 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  289 SK-TYELEGVSSAEEYKNTRRAMDIVGISQDEQEGIFRTLAAILHLGNVEFS--SGREHDSSVVKDPESRH-------HL 358
Cdd:cd14899    241 SLcSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEqiPHKGDDTVFADEARVMSsttgafdHF 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  359 QMAADLFKCDANLLLASLCTRSILTREGIIIKALDPNAAVTSRDTLAKTVYAHLFDWLVDKIN---------------KS 423
Cdd:cd14899    321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNnklqrqasapwgadeSD 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  424 VGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKMEQDEYRKEEINWSYIEFIDNQDVLDLIEKK 503
Cdd:cd14899    401 VDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELFEHR 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  504 PIGVIALLDEACMFPRSTHESFSMKLFQNF---RFHPRLEKPKFSE--TDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHC 578
Cdd:cd14899    481 PIGIFSLTDQECVFPQGTDRALVAKYYLEFekkNSHPHFRSAPLIQrtTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  579 NLLSSSKCPFVAGIFPSAPEESTRSSYKFSSVSSR-----------------FKQQLQALMETLSKTEPHYVRCVKPNSL 641
Cdd:cd14899    561 QLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRtrrraksaiaavsvgtqFKIQLNELLSTVRATTPRYVRCIKPNDS 640

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....
gi 1063726492  642 NRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRF 685
Cdd:cd14899    641 HVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684

MYSc_Myo13

cd14875

class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...

81-725

1.24e-133

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: 428.84 E-value: 1.24e-133

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYA-LNDIYTYTGSILIAVNPFKKLPhlYNGHM-MEQYMGAPFGE-LSPHVFAVSDVAYRAM-IDDSRSQS 156
Cdd:cd14875      1 ATLLHCIKERFEkLHQQYSLMGEMVLSVNPFRLMP--FNSEEeRKKYLALPDPRlLPPHIWQVAHKAFNAIfVQGLGNQS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  157 ILVSGESGAGKTETTKLIMQYLTFVGGRATDDD--RSVEQQVLE----SNPLLEAFGNAKTVRNDNSSRFGKFVEIQFD- 229
Cdd:cd14875     79 VVISGESGSGKTENAKMLIAYLGQLSYMHSSNTsqRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDp 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  230 TNGRISGAAIRTYLLERSRVVRITDPERNYHCFYQLCASGNDAEKYKLSN---PRQFHYLNQSKTYELEGV-----SSAE 301
Cdd:cd14875    159 TSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGlktAQDYKCLNGGNTFVRRGVdgktlDDAH 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  302 EYKNTRRAMDIVGISQDEQEGIFRTLAAILHLGNVEFSSGrEHDSSVVKDPESrhhLQMAADLFKCDANLLLASLCTRSi 381
Cdd:cd14875    239 EFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESD-QNDKAQIADETP---FLTACRLLQLDPAKLRECFLVKS- 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  382 ltREGIIIKALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVG-QDPESRFQ-IGVLDIYGFECFKNNSFEQFCINFAN 459
Cdd:cd14875    314 --KTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKyIGLLDIFGFENFTRNSFEQLCINYAN 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  460 EKLQQHFNEHVFKMEQDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFR-FHPR 538
Cdd:cd14875    392 ESLQNHYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKRTGIFSMLDEECNFKGGTTERFTTNLWDQWAnKSPY 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  539 LEKPKFS-ETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSAPEESTRssykFSSVSSRFKQQ 617
Cdd:cd14875    472 FVLPKSTiPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARR----KQTVAIRFQRQ 547

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  618 LQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAP------- 690
Cdd:cd14875    548 LTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPrstaslf 627

                          650       660       670
                   ....*....|....*....|....*....|....*...
gi 1063726492  691 ---EFMDESNDEQALTEKiLSKLGLGNYQLGRTKVFLR 725
Cdd:cd14875    628 kqeKYSEAAKDFLAYYQR-LYGWAKPNYAVGKTKVFLR 664

MYSc_Myo17

cd14879

class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...

87-724

3.28e-115

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: 378.05 E-value: 3.28e-115

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   87 LQRRYALNDIYTYTGS-ILIAVNPFKKLPhLYNGHMMEQY-------MGAPFGELSPHVFAVSDVAYRAMIDDSRSQSIL 158
Cdd:cd14879     10 LASRFRSDLPYTRLGSsALVAVNPYKYLS-SNSDASLGEYgseyydtTSGSKEPLPPHAYDLAARAYLRMRRRSEDQAVV 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  159 VSGESGAGKTETTKLIMQYLTFVGGRATDDDRsVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAA 238
Cdd:cd14879     89 FLGETGSGKSESRRLLLRQLLRLSSHSKKGTK-LSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNERGRLIGAK 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  239 IRTYLLERSRVVRITDPERNYHCFYQLCASGNDAEK--YKLSNPRQFHYLNQSKTYELE---GVSSAEEYKNTRRAMDIV 313
Cdd:cd14879    168 VLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERqhLGLDDPSDYALLASYGCHPLPlgpGSDDAEGFQELKTALKTL 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  314 GISQDEQEGIFRTLAAILHLGNVEF--SSGREHDSSVVKDPESrhhLQMAADLFKCDANLLLASLCTRSILTREGIIIKA 391
Cdd:cd14879    248 GFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVVKNTDV---LDIVAAFLGVSPEDLETSLTYKTKLVRKELCTVF 324

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  392 LDPNAAVTSRDTLAKTVYAHLFDWLVDKIN-KSVGQDPESRFQIGVLDIYGFECF---KNNSFEQFCINFANEKLQQHFN 467
Cdd:cd14879    325 LDPEGAAAQRDELARTLYSLLFAWVVETINqKLCAPEDDFATFISLLDFPGFQNRsstGGNSLDQFCVNFANERLHNYVL 404

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  468 EHVFKMEQDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEAC-MFPRSTHESFSMKLFQNFRFHPRL-EKPKFS 545
Cdd:cd14879    405 RSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKPGGLLGILDDQTrRMPKKTDEQMLEALRKRFGNHSSFiAVGNFA 484

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  546 ETD----FTLSHYAGKVTYQTEAFLDKNRDytivehcnLLSSSkcpFVAgIFPSAPEestrssykfssvssrFKQQLQAL 621
Cdd:cd14879    485 TRSgsasFTVNHYAGEVTYSVEGFLERNGD--------VLSPD---FVN-LLRGATQ---------------LNAALSEL 537

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  622 METLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMDESNDEQA 701
Cdd:cd14879    538 LDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLRGSAAERIRQCA 617

                          650       660
                   ....*....|....*....|...
gi 1063726492  702 LTEKILSKLGlgnYQLGRTKVFL 724
Cdd:cd14879    618 RANGWWEGRD---YVLGNTKVFL 637

MYSc_Myo16

cd14878

class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...

83-725

8.25e-110

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: 363.37 E-value: 8.25e-110

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   83 VLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYM---GAPFGELSPHVFAVSDVAYRAMIDDSRSQSILV 159
Cdd:cd14878      3 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  160 SGESGAGKTETTKLIMQYLTFvggRATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQF-DTNGRISGAA 238
Cdd:cd14878     82 SGERGSGKTEASKQIMKHLTC---RASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGAR 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  239 IRTYLLERSRVVRITDPERNYHCFYQLCASGNDAEKYKL--SNPRQFHYLNQSktyELEGVSSAEEYKNTRR------AM 310
Cdd:cd14878    159 IYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLhlNNLCAHRYLNQT---MREDVSTAERSLNREKlavlkqAL 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  311 DIVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSVVKDPESrhhLQMAADLFKCDANLLLASLCTRSILTREGIIIK 390
Cdd:cd14878    236 NVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQL---LEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  391 ALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESR----FQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHF 466
Cdd:cd14878    313 RHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKsmqtLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  467 NEHVFKMEQDEYRKEEINWSYIEFIDNQD-VLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLfqnfrfHPRLEK---- 541
Cdd:cd14878    393 NEVLFLQEQTECVQEGVTMETAYSPGNQTgVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKL------QSLLESsntn 466

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  542 --------------PKFSETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSapeestrssyKF 607
Cdd:cd14878    467 avyspmkdgngnvaLKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQS----------KL 536

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  608 SSVSSRFKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGL 687
Cdd:cd14878    537 VTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKP 616

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 1063726492  688 LAPEFMDESNdEQALTEK---ILSKLGLGNYQLGRTKVFLR 725
Cdd:cd14878    617 LADTLLGEKK-KQSAEERcrlVLQQCKLQGWQMGVRKVFLK 656

MYSc_Myo26

cd14887

class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...

81-725

1.26e-104

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: 350.87 E-value: 1.26e-104

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYA--------LNDIYTYTGSILIAVNPFKKLpHLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDS 152
Cdd:cd14887      1 PNLLENLYQRYNkayinkenRNCIYTYTGTLLIAVNPYRFF-NLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  153 RSQSILVSGESGAGKTETTKLIMQYLTFVGGRATD-DDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTN 231
Cdd:cd14887     80 RSQSILISGESGAGKTETSKHVLTYLAAVSDRRHGaDSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  232 GRISGAAIRTYLLERSRVVRITDPERNYHCFYQLCASGNDAEKYKLSNPRQFHYLnqsktYELEGVSsaeeykntrRAMD 311
Cdd:cd14887    160 GKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAGEGDPES-----TDLRRIT---------AAMK 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  312 IVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSVVKD--PESRHHLQMAADL-----FKCDANLLLASLCTRSILT- 383
Cdd:cd14887    226 TVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKltSVSVGCEETAADRshsseVKCLSSGLKVTEASRKHLKt 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  384 -----------------REGIIIKAL-------DPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQ---------DPES 430
Cdd:cd14887    306 varllglppgvegeemlRLALVSRSVretrsffDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRsakpsesdsDEDT 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  431 RFQ-----IGVLDIYGFECFKN---NSFEQFCINFANEKLQQHFNEHVFKMEQDEYRKEEINWSYIEFIDNQD--VLDLI 500
Cdd:cd14887    386 PSTtgtqtIGILDLFGFEDLRNhskNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAFPFSfpLASTL 465

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  501 EKKPIGVIALL-------------------------DEACMFP-----RSTHESFSMKLFQNFRFHPRLEKP----KFSE 546
Cdd:cd14887    466 TSSPSSTSPFSptpsfrsssafatspslpsslsslsSSLSSSPpvwegRDNSDLFYEKLNKNIINSAKYKNItpalSREN 545

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  547 TDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSskCPFVAGIFPSAPEESTRSSYKFSSV-SSRFKQQLQALMETL 625
Cdd:cd14887    546 LEFTVSHFACDVTYDARDFCRANREATSDELERLFLA--CSTYTRLVGSKKNSGVRAISSRRSTlSAQFASQLQQVLKAL 623

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  626 SKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMDEsndeqALTEK 705
Cdd:cd14887    624 QETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALRE-----ALTPK 698

                          730       740
                   ....*....|....*....|....*..
gi 1063726492  706 ILSKLGL-------GNYQLGRTKVFLR 725
Cdd:cd14887    699 MFCKIVLmfleinsNSYTFGKTKIFFR 725

MYSc_Myo37

cd14898

class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...

83-694

4.56e-101

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: 336.10 E-value: 4.56e-101

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   83 VLYNLQRRYALNDIYTYTGSILIAVNPFKKLphlyNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSrSQSILVSGE 162
Cdd:cd14898      3 TLEILEKRYASGKIYTKSGLVFLALNPYETI----YGAGAMKAYLKNYSHVEPHVYDVAEASVQDLLVHG-NQTIVISGE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  163 SGAGKTETTKLIMQYLTFvggrATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDtnGRISGAAIRTY 242
Cdd:cd14898     78 SGSGKTENAKLVIKYLVE----RTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETY 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  243 LLERSRVVRITDPERNYHCFYQLCASgndaEKYKLSNprqfHYLNQSKTY--ELEGVSSAEEYKNTRRAMDIVGISQDEQ 320
Cdd:cd14898    152 LLEKSRVTHHEKGERNFHIFYQFCAS----KRLNIKN----DFIDTSSTAgnKESIVQLSEKYKMTCSAMKSLGIANFKS 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  321 egIFRTLAAILHLGNVEFSsgrehDSSVVKdPESRHHLQMAADLFKCDANLLLASLCTRSILTReGIIIKALDP-NAAVT 399
Cdd:cd14898    224 --IEDCLLGILYLGSIQFV-----NDGILK-LQRNESFTEFCKLHNIQEEDFEESLVKFSIQVK-GETIEVFNTlKQART 294

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  400 SRDTLAKTVYAHLFDWLVDKINKSVGQDPEsrFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKMEQDEYR 479
Cdd:cd14898    295 IRNSMARLLYSNVFNYITASINNCLEGSGE--RSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYK 372

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  480 KEEINWSYIEFIDNQDVLDLIEkKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRlekPKFSETdFTLSHYAGKVT 559
Cdd:cd14898    373 EEGIEWPDVEFFDNNQCIRDFE-KPCGLMDLISEESFNAWGNVKNLLVKIKKYLNGFIN---TKARDK-IKVSHYAGDVE 447

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  560 YQTEAFLDKNRdytivEHCNLLssskcPFvaGIFPSAPEESTRSSYKFssvssrFKQQLQALMETLSKTEPHYVRCVKPN 639
Cdd:cd14898    448 YDLRDFLDKNR-----EKGQLL-----IF--KNLLINDEGSKEDLVKY------FKDSMNKLLNSINETQAKYIKCIRPN 509

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1063726492  640 SLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMD 694
Cdd:cd14898    510 EECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITLFE 564

MYSc_Myo20

cd14881

class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...

83-724

1.12e-94

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: 320.14 E-value: 1.12e-94

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   83 VLYNLQRRYALNDIYTYTGSILIAVNPFKKLP---HLYNGHMMEQYmgapfgelsPHVFAVSDVAYRAMIDDSRSQSILV 159
Cdd:cd14881      3 VMKCLQARFYAKEFFTNVGPILLSVNPYRDVGnplTLTSTRSSPLA---------PQLLKVVQEAVRQQSETGYPQAIIL 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  160 SGESGAGKTETTKLIMQYLTFV--GGRATDddrsVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFdTNGRISGA 237
Cdd:cd14881     74 SGTSGSGKTYASMLLLRQLFDVagGGPETD----AFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDGALYRT 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  238 AIRTYLLERSRVVRITDPERNYHCFYQLCASGNDAEKYKLS----NPRQFHYLNQSKTYELEGvSSAEEYKNTRRAMDIV 313
Cdd:cd14881    149 KIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHldgySPANLRYLSHGDTRQNEA-EDAARFQAWKACLGIL 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  314 GISQDEqegIFRTLAAILHLGNVEFSSGREHDSSVVKDPEsrhhLQMAADLFKCDANLLLASLCTRSILTReGIIIKAL- 392
Cdd:cd14881    228 GIPFLD---VVRVLAAVLLLGNVQFIDGGGLEVDVKGETE----LKSVAALLGVSGAALFRGLTTRTHNAR-GQLVKSVc 299

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  393 DPNAAVTSRDTLAKTVYAHLFDWLVDKINK------SVGQDPESRFqIGVLDIYGFECFKNNSFEQFCINFANEKLQQHF 466
Cdd:cd14881    300 DANMSNMTRDALAKALYCRTVATIVRRANSlkrlgsTLGTHATDGF-IGILDMFGFEDPKPSQLEHLCINLCAETMQHFY 378

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  467 NEHVFKMEQDEYRKEEINWSY-IEFIDNQDVLDLIEKKPIGVIALLDEACMfPRSTHESFSMKLFQNFRFHPRLEKPK-F 544
Cdd:cd14881    379 NTHIFKSSIESCRDEGIQCEVeVDYVDNVPCIDLISSLRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLFEAKpQ 457

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  545 SETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVagiFPSAPEEstrssykfssvssrFKQQLQALMET 624
Cdd:cd14881    458 DDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNFG---FATHTQD--------------FHTRLDNLLRT 520

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  625 LSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMDESNDEQALT- 703
Cdd:cd14881    521 LVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEd 600

                          650       660       670
                   ....*....|....*....|....*....|..
gi 1063726492  704 EKIL---------SKLGLG--NYQLGRTKVFL 724
Cdd:cd14881    601 CALIlqfleaqppSKLSSVstSWALGKRHIFL 632

MYSc_Myo12

cd14874

class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...

81-725

9.76e-91

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: 308.72 E-value: 9.76e-91

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYmgapfgelspHVFAVSDVAYRAMID-DSRSQSILV 159
Cdd:cd14874      1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLS-IQDQLVIKKC----------HISGVAENALDRIKSmSSNAESIVF 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  160 SGESGAGKTETTKLIMQYLTfvggrATDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNgRISGAAI 239
Cdd:cd14874     70 GGESGSGKSYNAFQVFKYLT-----SQPKSKVTTKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYKRN-VLTGLNL 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  240 R-TYLLERSRVVRITDPERNYHCFYQLCASGNDA--EKYKLSNPRQFHYLNQSKTYELEgVSSAEEYKNTRRAMDIVGIS 316
Cdd:cd14874    144 KyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEmkAKFGIKGLQKFFYINQGNSTENI-QSDVNHFKHLEDALHVLGFS 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  317 QDEQEGIFRTLAAILHLGNVEFSSGR----EHDSSVVKDPEsrhHLQMAADLFKCDANLLLAslctrsILTREGIIIKAL 392
Cdd:cd14874    223 DDHCISIYKIISTILHIGNIYFRTKRnpnvEQDVVEIGNMS---EVKWVAFLLEVDFDQLVN------FLLPKSEDGTTI 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  393 DPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVgQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFK 472
Cdd:cd14874    294 DLNAALDNRDSFAMLIYEELFKWVLNRIGLHL-KCPLHTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFH 372

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  473 MEQDEYRKEEINWSYI--EFIDNQDVLDLIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKPKFSE-TDF 549
Cdd:cd14874    373 DQLVDYAKDGISVDYKvpNSIENGKTVELLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARNKErLEF 452

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  550 TLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSAPEESTRSSYKFSSVSSRFKQQlqaLMETLSKTE 629
Cdd:cd14874    453 GVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDMIVSQAQFILRGAQE---IADKINGSH 529

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  630 PHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMDESNDEQALTEKILSK 709
Cdd:cd14874    530 AHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLPGDIAMCQNEKEIIQDILQG 609

                          650
                   ....*....|....*....
gi 1063726492  710 LGL---GNYQLGRTKVFLR 725
Cdd:cd14874    610 QGVkyeNDFKIGTEYVFLR 628

MYSc_Myo18

cd01386

class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...

81-725

1.20e-89

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: 307.31 E-value: 1.20e-89

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS 160
Cdd:cd01386      1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLA-VYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  161 GESGAGKTETTKLIMQYLTFVGGrATDDDRSVEqqVLES-NPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAAI 239
Cdd:cd01386     80 GRSGSGKTTNCRHILEYLVTAAG-SVGGVLSVE--KLNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASI 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  240 RTYLLERSRVVRITDPERNYHCFYQLCAsGNDAEkykLSNPRQFHYLNQSKTYELEGVSSAEE-------YKNTRRAMDI 312
Cdd:cd01386    157 QTLLLERSRVARRPEGESNFNVFYYLLA-GADAA---LRTELHLNQLAESNSFGIVPLQKPEDkqkaaaaFSKLQAAMKT 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  313 VGISQDEQEGIFRTLAAILHLGNvefsSGREHDSSVVKDPESRH-HLQMAADLFKCDANlLLASLC------------TR 379
Cdd:cd01386    233 LGISEEEQRAIWSILAAIYHLGA----AGATKAASAGRKQFARPeWAQRAAYLLGCTLE-ELSSAIfkhhlsggpqqsTT 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  380 SILTREGIIIKALDPNA-AVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFE----CFKNN--SFEQ 452
Cdd:cd01386    308 SSGQESPARSSSGGPKLtGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQnpahSGSQRgaTFED 387

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  453 FCINFANEKLQQHFNEHVFKMEQDEYRKE--EINWSYIEFIDNQDVlDLIEKKPI--------------GVIALLDEACM 516
Cdd:cd01386    388 LCHNYAQERLQLLFHERTFVAPLERYKQEnvEVDFDLPELSPGALV-ALIDQAPQqalvrsdlrdedrrGLLWLLDEEAL 466

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  517 FPRSTHESFSMKLF-----QNFRFHPRLEKPKFSETDFTLSHYAGK--VTYQTEAFLDKNR-DYTIVEHCNLLSSSKCPF 588
Cdd:cd01386    467 YPGSSDDTFLERLFshygdKEGGKGHSLLRRSEGPLQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQESQKET 546

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  589 vAGIFPSAPeestrssykfssvSSRFKQQLQALMETLSKTEPHYVRCVKPN---------SLNRPQKFESLSV---LHQL 656
Cdd:cd01386    547 -AAVKRKSP-------------CLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagkdersTSSPAAGDELLDVpllRSQL 612

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063726492  657 RCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFMDESN------DEQALTEKILSKLGL--GNYQLGRTKVFLR 725
Cdd:cd01386    613 RGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevaDERKAVEELLEELDLekSSYRIGLSQVFFR 689

MYSc_Myo23

cd14884

class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ...

81-675

1.20e-88

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: 304.52 E-value: 1.20e-88

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPHLYNGHMMEQYM---------GAPFgeLSPHVFAVSDVAYRAMIDD 151
Cdd:cd14884      1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKELYDQDVMNVYLhkksnsaasAAPF--PKAHIYDIANMAYKNMRGK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  152 SRSQSILVSGESGAGKTETTKLIMQYLTFVGGRATDDDRsvEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDT- 230
Cdd:cd14884     79 LKRQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTER--IDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEv 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  231 --------NGRISGAAIRTYLLERSRVVRITDPERNYHCFYQLCASGNDAE-----------KYKLSNPRQFHYLNQSKT 291
Cdd:cd14884    157 entqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDlarrnlvrncgVYGLLNPDESHQKRSVKG 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  292 -----------YELEGVSSAEEYKNTRRAMDIVGISQDEQEGIFRTLAAILHLGNvefssgrehdssvvkdpesrHHLQM 360
Cdd:cd14884    237 tlrlgsdsldpSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGN--------------------RAYKA 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  361 AADLFKCDANLLLASLCTRSILTREGIIIKALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQ------- 433
Cdd:cd14884    297 AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDESdnediys 376

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  434 -----IGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKMEQDEYRKEEINWSYIEFIDNQDVLDLIEKkpigVI 508
Cdd:cd14884    377 ineaiISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAK----IF 452

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  509 ALLDEACMFPRSTHE----SFSMKLFQNFR------------FHPRLE-----KPKFSETDFTLSHYAGKVTYQTEAFLD 567
Cdd:cd14884    453 RRLDDITKLKNQGQKktddHFFRYLLNNERqqqlegkvsygfVLNHDAdgtakKQNIKKNIFFIRHYAGLVTYRINNWID 532

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  568 KNRDYTIVEHCNLLSSSKCPFVagifpsAPEESTRSSYKFSSVSSRFKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKF 647
Cdd:cd14884    533 KNSDKIETSIETLISCSSNRFL------REANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTF 606

                          650       660
                   ....*....|....*....|....*...
gi 1063726492  648 ESLSVLHQLRCGGVLEAVRISLAGYPTR 675
Cdd:cd14884    607 KRLLVYRQLKQCGSNEMIKILNRGLSHK 634

MYSc_Myo24A

cd14937

class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...

81-725

7.14e-87

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: 297.70 E-value: 7.14e-87

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   81 AGVLYNLQRRYALNDIYTYTGSILIAVNPFKKLPHLYNghmmeQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVS 160
Cdd:cd14937      1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDIN-----EYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIIS 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  161 GESGAGKTETTKLIMQYltFVGGRATDDDrsVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAAIR 240
Cdd:cd14937     76 GESGSGKTEASKLVIKY--YLSGVKEDNE--ISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIE 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  241 TYLLERSRVVRITDPERNYHCFYQLCASGND--AEKYKLSNPRQFHYLNqSKTYELEGVSSAEEYKNTRRAMDIVGISqD 318
Cdd:cd14937    152 IFLLENIRVVSQEEEERGYHIFYQIFNGMSQelKNKYKIRSENEYKYIV-NKNVVIPEIDDAKDFGNLMISFDKMNMH-D 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  319 EQEGIFRTLAAILHLGNVEFSS----GREHDSSVvkDPESRHHLQMAADLFKCDANLLLASLC-TRSILTREGIIIkALD 393
Cdd:cd14937    230 MKDDLFLTLSGLLLLGNVEYQEiekgGKTNCSEL--DKNNLELVNEISNLLGINYENLKDCLVfTEKTIANQKIEI-PLS 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  394 PNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKM 473
Cdd:cd14937    307 VEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEK 386

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  474 EQDEYRKEEINWSYIEFIDNQDVLDLIEKKpIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKPKFSET-DFTLS 552
Cdd:cd14937    387 ETELYKAEDILIESVKYTTNESIIDLLRGK-TSIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINkNFVIK 465

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  553 HYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSApeESTRSSYKFSSVSSRFKQQLQALMETLSKTEPHY 632
Cdd:cd14937    466 HTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDV--EVSESLGRKNLITFKYLKNLNNIISYLKSTNIYF 543

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  633 VRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAgYPTRRNYSDFVDRFgllapEFMDES-NDEQALTEKILSKLG 711
Cdd:cd14937    544 IKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNISFF-FQYKYTFDVFLSYF-----EYLDYStSKDSSLTDKEKVSMI 617

                          650       660
                   ....*....|....*....|
gi 1063726492  712 LGN------YQLGRTKVFLR 725
Cdd:cd14937    618 LQNtvdpdlYKVGKTMVFLK 637

MYSc_Myo44

cd14905

class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...

87-725

6.14e-85

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: 293.15 E-value: 6.14e-85

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   87 LQRRYALNDIYTYTGSILIAVNPFKKLPHLYNGHMMEQY---MGAPfgelsPHVFAVSDVAYRAMIDDSRSQSILVSGES 163
Cdd:cd14905      7 IQARYKKEIIYTYIGPILVSVNPLRYLPFLHSQELVRNYnqrRGLP-----PHLFALAAKAISDMQDFRRDQLIFIGGES 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  164 GAGKTETTKLIMQYLTfvggrATDDDRS--VEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAAIRT 241
Cdd:cd14905     82 GSGKSENTKIIIQYLL-----TTDLSRSkyLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYS 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  242 YLLERSRVVRITDPERNYHCFYQLCASGNDAEK--YKLSNPRQFHYLNQSKTYELEGVSSAEEYKNTRRAMDIVGISQDE 319
Cdd:cd14905    157 YFLDENRVTYQNKGERNFHIFYQFLKGITDEEKaaYQLGDINSYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDFPSEK 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  320 QEGIFRTLAAILHLGNVEFSsgREHDSSVVKDP---ESRHHlqmaadlfkcdaNLLLASLCTRSILTREgiiiKALDPNA 396
Cdd:cd14905    237 IDLIFKTLSFIIILGNVTFF--QKNGKTEVKDRtliESLSH------------NITFDSTKLENILISD----RSMPVNE 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  397 AVTSRDTLAKTVYAHLFDWLVDKINKSVgQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKMEQD 476
Cdd:cd14905    299 AVENRDSLARSLYSALFHWIIDFLNSKL-KPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQR 377

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  477 EYRKEEINW-SYIEFIDNQDVLDLIEKkpigVIALLDEACMFPRSTHESFSMKLfQNF--RFHPRLEKPkfseTDFTLSH 553
Cdd:cd14905    378 EYQTERIPWmTPISFKDNEESVEMMEK----IINLLDQESKNINSSDQIFLEKL-QNFlsRHHLFGKKP----NKFGIEH 448

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  554 YAGKVTYQTEAFLDKNRDyTIVEHCNLL---SSSKCPFVA-GIFP-SAPEESTRSSYKFSSVSSRFKQQLQALMETLSKT 628
Cdd:cd14905    449 YFGQFYYDVRGFIIKNRD-EILQRTNVLhknSITKYLFSRdGVFNiNATVAELNQMFDAKNTAKKSPLSIVKVLLSCGSN 527

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  629 EP-----------------------------------------------HYVRCVKPNSLNRPQKFESLSVLHQLRCGGV 661
Cdd:cd14905    528 NPnnvnnpnnnsgggggggnsgggsgsggstyttysstnkainnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCL 607

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  662 LEAVRISLAGYPTRRNYSDFVDRFGLlapeFMDESNDEQALTEKI------LSKLGLGNYQLGRTKVFLR 725
Cdd:cd14905    608 LETTRIQRFGYTIHYNNKIFFDRFSF----FFQNQRNFQNLFEKLkendinIDSILPPPIQVGNTKIFLR 673

MYSc_Myo21

cd14882

class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...

83-725

4.46e-82

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: 283.94 E-value: 4.46e-82

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   83 VLYNLQRRYALNDIYTYTGSILIAVNPfKKLPHLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVSGE 162
Cdd:cd14882      3 ILEELRHRYLMGESYTFIGDILLSLNP-NEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  163 SGAGKTETTKLIMQYLTFVGgratDDDRSVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDTNGRISGAAIRTY 242
Cdd:cd14882     82 SYSGKTTNARLLIKHLCYLG----DGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMY 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  243 LLERSRVVRITDPERNYHCFYQL---CASGNDAEKYKLSNPRQFHYLNQSKTYELEG-----------VSSAEEYKNTRR 308
Cdd:cd14882    158 QLEKLRVSTTDGNQSNFHIFYYFydfIEAQNRLKEYNLKAGRNYRYLRIPPEVPPSKlkyrrddpegnVERYKEFEEILK 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  309 AMDIvgiSQDEQEGIFRTLAAILHLGNVEFSSGRehDSSVVKDPESRHHLqmaADLFKCDANLLLASLCTRSILTREGII 388
Cdd:cd14882    238 DLDF---NEEQLETVRKVLAAILNLGEIRFRQNG--GYAELENTEIASRV---AELLRLDEKKFMWALTNYCLIKGGSAE 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  389 IKALDPNAAVTSRDTLAKTVYAHLFDWLVDKIN------KSVGQDPESrfqIGVLDIYGFECFKNNSFEQFCINFANEKL 462
Cdd:cd14882    310 RRKHTTEEARDARDVLASTLYSRLVDWIINRINmkmsfpRAVFGDKYS---ISIHDMFGFECFHRNRLEQLMVNTLNEQM 386

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  463 QQHFNEHVFKMEQDEYRKEEINWSYIEFIDNQDVLDLIEKKPIGVIALLDEAcmfPRSTHEsfsmklfQNFRFHPRLEK- 541
Cdd:cd14882    387 QYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDA---SRSCQD-------QNYIMDRIKEKh 456

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  542 ----PKFSETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPFVAGIFPSAPEESTRSSYKFssvssrFKQQ 617
Cdd:cd14882    457 sqfvKKHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQVRNMRTLAAT------FRAT 530

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  618 LQALMETLS----KTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLAPEFm 693
Cdd:cd14882    531 SLELLKMLSiganSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLAFDF- 609

                          650       660       670
                   ....*....|....*....|....*....|...
gi 1063726492  694 DESNDEQALTEKIL-SKLGLGNYQLGRTKVFLR 725
Cdd:cd14882    610 DETVEMTKDNCRLLlIRLKMEGWAIGKTKVFLK 642

MYSc_Myo32

cd14893

class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...

84-685

5.39e-70

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: 251.04 E-value: 5.39e-70

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   84 LYNLQRRYALNDIYTYTGSILIAVNPFKKLPhLYNGHMMEQYMGA----PFGELS------PHVFAVSDVAYRAMIDDSR 153
Cdd:cd14893      4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLP-IYTPDHMQAYNKSreqtPLYEKDtvndapPHVFALAQNALRCMQDAGE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  154 SQSILVSGESGAGKTETTKLIMQYLTFVGGRATDDDRS---------VEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFV 224
Cdd:cd14893     83 DQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSegasgvlhpIGQQILHAFTILEAFGNAATRQNRNSSRFAKMI 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  225 EIQFDTNGRISGAAIRTYLLERSRVVRITDPERNYHCFYQLCAS-------GNDAEKYKLSNprQFHYLNQSKTYELEGV 297
Cdd:cd14893    163 SVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGvqhdptlRDSLEMNKCVN--EFVMLKQADPLATNFA 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  298 SSAEEYKNTRRAMDIVGISQDEQEGIFRTLAAILHLGNVEF----------SSGR-----EHDSSVVKDPEsrhHLQMAA 362
Cdd:cd14893    241 LDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggksvGGANsttvsDAQSCALKDPA---QILLAA 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  363 DLFKCDANLLLASLCTRSILTREG----IIIKALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVG----QDPESRFQI 434
Cdd:cd14893    318 KLLEVEPVVLDNYFRTRQFFSKDGnktvSSLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILGgifdRYEKSNIVI 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  435 G-----VLDIYGFECF--KNNSFEQFCINFANEKLqQHF--------NEHVFKMEQDEYRKEEINWSYIEFIDNQD-VLD 498
Cdd:cd14893    398 NsqgvhVLDMVGFENLtpSQNSFDQLCFNYWSEKV-HHFyvqntlaiNFSFLEDESQQVENRLTVNSNVDITSEQEkCLQ 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  499 LIEKKPIGVIALLDEACMFPRSTHESFSMKLFQNFRFHPRLEKPKF-SETD-------------FTLSHYAGKVTYQTEA 564
Cdd:cd14893    477 LFEDKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMgADTTneylapskdwrllFIVQHHCGKVTYNGKG 556

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  565 FLDKNRdYTIVEHC-NLLSSSKCPFVAGI------------FPSAPEESTRSSYKFSSVSSRFKQ--------------Q 617
Cdd:cd14893    557 LSSKNM-LSISSTCaAIMQSSKNAVLHAVgaaqmaaassekAAKQTEERGSTSSKFRKSASSAREsknitdsaatdvynQ 635

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063726492  618 LQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRF 685
Cdd:cd14893    636 ADALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY 703

Myo5-like_CBD

cd14945

Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied ...

1120-1454

2.07e-50

Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5 a,b,c) in vertebrates and two (myo2 and myo4) in fungi and related to plant class XI myosins. Their C-terminal cargo binding domains is important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. MyoV-CBDs interact with several adaptor proteins that in turn interact with the cargo.

Pssm-ID: 271253 [Multi-domain] Cd Length: 288 Bit Score: 180.67 E-value: 2.07e-50

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492 1120 ENYELLSRCIKENLGFN--DDKPLAACVIYKCLLHWRAF--ESESTAIFNIIIEGINEAL-KGGDENGVLPYWLSNASAL 1194
Cdd:cd14945      1 SEEDSLLRGIVTDFEPSsgDHKLTPAYILYLCIRHAASNglTGQSTSLLNKVLKTIQQVVqQHNDDMQLLAFWLSNASEL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492 1195 LCLLQRNLRsnsflnasaqrsgraAYGvkspFKLHGPDDGASHIEARYPALLFKQQLTACVEKIYGLIRDNLKKELSPll 1274
Cdd:cd14945     81 LYFLKQDSK---------------LYG----AAGEAPQKEEEQKLTVSDLNELKQDLEAVSIKIYQQALKYLNKNLQP-- 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492 1275 gsciqapkasrgiagksrspggvpqqspssQWESILKFLDSLMSRLRENHVPSFFIRKLVTQVFSFINLSLFNSLLLRRE 1354
Cdd:cd14945    140 ------------------------------KIRDIVKFLNSFLDLLKSFHVHPEIRSQVFTQLFSFINARLFNQLITKKD 189

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492 1355 CCTFSNGEYVKSGISELEKWIANAKEEfaGTSWHELNYIRQAVGFLVIHQKKKKSLDEIRqDLCPVLTIRQIYRISTMYW 1434
Cdd:cd14945    190 ALSWSRGMQIRANISRLEEWCEGRGLE--HLAVDFLSKLIQAVQLLQLKKYTQEDIEILC-ELCPSLNPAQLQAILTQYQ 266

                          330       340
                   ....*....|....*....|
gi 1063726492 1435 DDKYGTQSVSSEVvsqMRVL 1454
Cdd:cd14945    267 PANYGESPVPKEI---LRTL 283

MYSc_Myo24B

cd14938

class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...

83-724

1.25e-47

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: 183.50 E-value: 1.25e-47

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492   83 VLYNLQRRYALNDIYTYTGSILIAVNPFKKLpHLYNGHMMEQY-MGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVSG 161
Cdd:cd14938      3 VLYHLKERFKNNKFYTKMGPLLIFINPKINN-NINNEETIEKYkCIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  162 ESGAGKTETTKLIMQYLTF-----------VGGRATDDDRSVEQQ---------VLESNPLLEAFGNAKTVRNDNSSRFG 221
Cdd:cd14938     82 ESGSGKSEIAKNIINFIAYqvkgsrrlptnLNDQEEDNIHNEENTdyqfnmsemLKHVNVVMEAFGNAKTVKNNNSSRFS 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  222 KFVEIQFDtNGRISGAAIRTYLLERSRVVRITDPERNYHCFYQLC--ASGNDAEKYKLSNPRQFHYLNQSKTYELEGvSS 299
Cdd:cd14938    162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIIngSSDKFKKMYFLKNIENYSMLNNEKGFEKFS-DY 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  300 AEEYKNTRRAMDIVGISQDEQEGIFRTLAAILHLGNVEFSSGREHDSSVVK---DPESRHHLQMAADLFKC--------D 368
Cdd:cd14938    240 SGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKAFRKKSLLMGknqCGQNINYETILSELENSedigldenV 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  369 ANLLLAS--LC----------TRSILTREGIIIKALDPNAAVTSRDTLAKTVYAHLFDWLVDKINKSVGQ---DPESRFQ 433
Cdd:cd14938    320 KNLLLACklLSfdietfvkyfTTNYIFNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQlqnININTNY 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  434 IGVLDIYGFECFKNNSFEQFCINFANEKLQQHFNEHVFKMEQDEYRKEEINWSY-IEFIDNQDVLDLIEKKPIG-VIALL 511
Cdd:cd14938    400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYnSENIDNEPLYNLLVGPTEGsLFSLL 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  512 DEAC---MFPRSTHESFSMKLFQNFRFHPRLEKPKFSETDFTLSHYAGKVTYQTEAFLDKNRDYTIVEHCNLLSSSKCPF 588
Cdd:cd14938    480 ENVStktIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSENEY 559

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  589 VAGIFPSAP--------EESTRSSYKFSSVSSR-------------FKQQLQALMETLSKTEPHYVRCVKPNSLNRP-QK 646
Cdd:cd14938    560 MRQFCMFYNydnsgnivEEKRRYSIQSALKLFKrrydtknqmavslLRNNLTELEKLQETTFCHFIVCMKPNESKRElCS 639

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  647 FESLSVLHQLRCGGVLEAVRISLAGYPTRRNYSDFVDRFGLLapefmdeSNDEQALTEKILSKLGLGNYQ--LGRTKVFL 724
Cdd:cd14938    640 FDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIK-------NEDLKEKVEALIKSYQISNYEwmIGNNMIFL 712

Motor_domain

cd01363

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...

103-255

6.69e-43

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: 154.42 E-value: 6.69e-43

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  103 ILIAVNPFKKLPHLYNGHMMEQYMGAPFGELSPHVFAVSDVAYRAMIDDSRSQSILVSGESGAGKTETTKLIMQYLTFVG 182
Cdd:cd01363      1 VLVRVNPFKELPIYRDSKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  183 GRATDDDR------------SVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDtngrISGA-AIRTYLLERSRV 249
Cdd:cd01363     81 FNGINKGEtegwvylteitvTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLD----IAGFeIINESLNTLMNV 156


                   ....*.
gi 1063726492  250 VRITDP 255
Cdd:cd01363    157 LRATRP 162

MYSc_Myo33

cd14894

class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...

196-667

6.44e-28

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: 122.54 E-value: 6.44e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  196 VLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDT-----NGRISGAAIRTYLLERSRVVRITDPER------NYHCFYQ 264
Cdd:cd14894    249 VLDSNIVLEAFGHATTSMNLNSSRFGKMTTLQVAFglhpwEFQICGCHISPFLLEKSRVTSERGRESgdqnelNFHILYA 328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  265 LCAsGNDAEKYKLSNPRQFH----------YLNQSKtYELEGVSSAEEY--KNTRR------AMDIVGISQDEQEGIFRT 326
Cdd:cd14894    329 MVA-GVNAFPFMRLLAKELHldgidcsaltYLGRSD-HKLAGFVSKEDTwkKDVERwqqvidGLDELNVSPDEQKTIFKV 406

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  327 LAAILHLGNVEFS----SGREHDSSV--VKDPESRHHLQMAADLFKCDANLLLASLCTRSilTREGIIIkALDPNAAVTS 400
Cdd:cd14894    407 LSAVLWLGNIELDyrevSGKLVMSSTgaLNAPQKVVELLELGSVEKLERMLMTKSVSLQS--TSETFEV-TLEKGQVNHV 483

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  401 RDTLAKTVYAHLFDWLVDKINKSV-----------------GQDPESRFQIGVLDIYGFECFKNNSFEQFCINFANEKLq 463
Cdd:cd14894    484 RDTLARLLYQLAFNYVVFVMNEATkmsalstdgnkhqmdsnASAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL- 562

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  464 qhfnehvfkmeqdeYRKEE--INWSY------IEFIDNQDVLdLIEKKPIGVIALLDEACMFPRS-----THESFSMKLF 530
Cdd:cd14894    563 --------------YAREEqvIAVAYssrphlTARDSEKDVL-FIYEHPLGVFASLEELTILHQSenmnaQQEEKRNKLF 627

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  531 -QNF--RFHPRLEKPK-------------FSETDFTLSHYAGKVTYQTEAFLDKNRDYTIV------------EHCNLLS 582
Cdd:cd14894    628 vRNIydRNSSRLPEPPrvlsnakrhtpvlLNVLPFVIPHTRGNVIYDANDFVKKNSDFVYAnllvglktsnssHFCRMLN 707

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  583 -SSKCPFVAGIFPSAPEESTRSSYKFSSVSSRFKQQLQALMETLSKTEPHYVRCVKPNSLNRPQKFESLSVLHQLRCGGV 661
Cdd:cd14894    708 eSSQLGWSPNTNRSMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRL 787


                   ....*.
gi 1063726492  662 LEAVRI 667
Cdd:cd14894    788 IRQMEI 793

DIL

pfam01843

DIL domain; The DIL domain has no known function.

1332-1436

8.59e-21

DIL domain; The DIL domain has no known function.

Pssm-ID: 460359 [Multi-domain] Cd Length: 103 Bit Score: 88.80 E-value: 8.59e-21

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492 1332 KLVTQVFSFINLSLFNSLLLRRECCTFSNGEYVKSGISELEKWIANAKEEFAgtSWHELNYIRQAVGFLVIHQKKKKSLD 1411
Cdd:pfam01843    1 QLFSQLFYFINAELFNRLLLRKKYCSWSKGMQIRYNLSRLEEWARSNGLESE--ARDHLAPLIQAAQLLQLRKSTLEDLD 78

                           90       100
                   ....*....|....*....|....*
gi 1063726492 1412 EIRQdLCPVLTIRQIYRISTMYWDD 1436
Cdd:pfam01843   79 SILQ-VCPALNPLQLHRLLTLYQPD 102

Myo5_CBD

cd15470

Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, ...

1141-1433

6.43e-09

Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. The MyoV-CBDs directly interact with several adaptor proteins, in case of Myo5a, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin, and in case of Myo5b, Rab11-family interacting protein 2.

Pssm-ID: 271254 [Multi-domain] Cd Length: 332 Bit Score: 59.53 E-value: 6.43e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492 1141 LAACVIYKCLLHWRAFESES--TAIFNIIIEGINEALK-GGDENGVLPYWLSNAsallCLLQRNLRsnsflnasaQRSGR 1217
Cdd:cd15470     26 LPAYILFMCIRHADYVNDEAkvRSLLTATINAIKKVLKkHSEDFEMLSFWLVNT----CRLLNCLK---------QYSGE 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492 1218 AAYGVkspfklHGPDDGASHIEARYPALLFKQQLTACVEKIY-GLIRdNLKKELSPllgsciqapkasrgiagksrspgg 1296
Cdd:cd15470     93 EEFMK------HNTPKQNEHCLKNFDLSEYRQVLSDLAIQIYqQLIK-RAEEILQP------------------------ 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492 1297 vpqqspssQWESILKFLDSLMSRLRENHVPSFFIRKLVTQVFSFINLSLFNSLLLRRECCTFSNGEYVKSGISELEKWIA 1376
Cdd:cd15470    142 --------TLDSLLQQLNSFHTTLTQHGLDPELIKQVFRQLFYLICASTLNNLLLRKDLCSWSKGMQIRYNVSQLEEWLR 213

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063726492 1377 NAK--EEFAGTSWHELNyirQAVGFLvihQKKKKSLDEIRQ--DLCPVLTIRQIYRISTMY 1433
Cdd:cd15470    214 DKGlqDSGARETLEPLI---QAAQLL---QVKKTTEEDAQSicEMCTKLTTAQIVKILNLY 268

Myo5a_CBD

cd15478

Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, ...

1141-1478

6.66e-09

Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. They interact with several adaptor proteins, in case of Myo5a-CBD, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin. Mutations in human Myo5a (many of which map to the cargo binding domain) lead to Griscelli syndrome, a severe neurological disease.

Pssm-ID: 271262 Cd Length: 375 Bit Score: 59.66 E-value: 6.66e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492 1141 LAACVIYKCLLHWRAFESEST--AIFNIIIEGINEALKG-GDENGVLPYWLSNASALL-CLLQrnlrsnsflnasaqrsg 1216
Cdd:cd15478     28 LPAYILFMCVRHADYLNDDQKvrSLLTSTINSIKKVLKKrGDDFETVSFWLSNTCRFLhCLKQ----------------- 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492 1217 raaYGVKSPFKLHGPDDGASHIEARYPALLFKQQLTACVEKIYGLIRDNLKKELSPLLGSCIQAPKASRGIAGKSrsPGG 1296
Cdd:cd15478     91 ---YSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSGVK--PTG 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492 1297 VPQQSPSSQWE------SILKFLDSLMSRLRENHVPSFFIRKLVTQVFSFINLSLFNSLLLRRECCTFSNGEYVKSGISE 1370
Cdd:cd15478    166 LRKRTSSIADEgtytldSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRYNVSQ 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492 1371 LEKWIANAKEEFAGTSwHELNYIRQAVGFLVIHQKKKKSLDEIrQDLCPVLTIRQIYRISTMYWDDKYGTQSVSsevVSQ 1450
Cdd:cd15478    246 LEEWLRDKNLMNSGAK-ETLEPLIQAAQLLQVKKKTDDDAEAI-CSMCNALTTAQIVKVLNLYTPVNEFEERVS---VSF 320

                          330       340
                   ....*....|....*....|....*...
gi 1063726492 1451 MRVLVDKDNQKQTSNSFLLDDDMSIPFS 1478
Cdd:cd15478    321 IRTIQMRLRDRKDSPQLLMDAKHIFPVT 348

Tropomyosin_1

pfam12718

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...

891-1041

3.35e-08

Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 53.85 E-value: 3.35e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  891 ALRLAKTKLEKRLEDLEWRL-QLEKRLrtsgeEAKSSEISKLQKtlesfslkldaarlatinecnKNAVLEKQLDismke 969
Cdd:pfam12718    4 SLKLEAENAQERAEELEEKVkELEQEN-----LEKEQEIKSLTH---------------------KNQQLEEEVE----- 52

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063726492  970 ksAVERELNGMVELKKDNALLKNSMNSLEKKNRVLEKELLNAKTNCNNTLQKLKEAEKRCSELQTSVQSLEE 1041
Cdd:pfam12718   53 --KLEEQLKEAKEKAEESEKLKTNNENLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQ 122

PRK03918

DNA double-strand break repair ATPase Rad50;

871-1049

5.10e-08

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 5.10e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  871 RQKLAKREFRKLKQVANEAGALRLAKTKLEKRLEDLEWRLQLEKRLRTSGEEAKssEISKLQKTLESFSL-KLDAARlat 949
Cdd:PRK03918   450 RKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE--QLKELEEKLKKYNLeELEKKA--- 524

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  950 iNECNKnavLEKQLDISMKEKSAVERELNGMVELKKDNALLKNSMNSLEKKNRVLEKELLNAKTNC----NNTLQKLKEA 1025
Cdd:PRK03918   525 -EEYEK---LKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESveelEERLKELEPF 600

                          170       180
                   ....*....|....*....|....
gi 1063726492 1026 EKRCSELQTSVQSLEEKLSHLENE 1049
Cdd:PRK03918   601 YNEYLELKDAEKELEREEKELKKL 624

PRK03918

DNA double-strand break repair ATPase Rad50;

871-1065

6.25e-08

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 6.25e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  871 RQKLAK--REFRKLKQVANEAGALRLAKTKLEKRLEDLEWRL-QLEKRLRtsGEEAKSSEISKLQKTLESfsLKLDAARL 947
Cdd:PRK03918   220 REELEKleKEVKELEELKEEIEELEKELESLEGSKRKLEEKIrELEERIE--ELKKEIEELEEKVKELKE--LKEKAEEY 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  948 ATINECnKNAVLEKQLDISmKEKSAVERELNGMVELKKDnallknsmnsLEKKNRVLEKellnaktncnnTLQKLKEAEK 1027
Cdd:PRK03918   296 IKLSEF-YEEYLDELREIE-KRLSRLEEEINGIEERIKE----------LEEKEERLEE-----------LKKKLKELEK 352

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1063726492 1028 RCSELQTSVQSLEEKLSHLENENQvLMQKTLITSPERI 1065
Cdd:PRK03918   353 RLEELEERHELYEEAKAKKEELER-LKKRLTGLTPEKL 389

SMC_N

pfam02463

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...

866-1085

2.65e-07

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.

Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 55.75 E-value: 2.65e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  866 IQCRWRQKLAKREFRKLKQVANEAgaLRLAKTKLEKRLEDLEWRLQLEKRLRTSGEEAKSSEISKLQKTLESfSLKLDAA 945
Cdd:pfam02463  186 AELIIDLEELKLQELKLKEQAKKA--LEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIES-SKQEIEK 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  946 RLATINECNKNAVLEKQLDISMKEKSAV-----ERELNGMVELKKDNALLKNSMNSLEKKNRVLEKELLNAKTNCNNTLQ 1020
Cdd:pfam02463  263 EEEKLAQVLKENKEEEKEKKLQEEELKLlakeeEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEK 342

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063726492 1021 KLKEAEKRCSELQTSVQSLEEKLSHLENENQVLMQKTLITSPERI-GQILGEQKHSSAVVPAQNDR 1085
Cdd:pfam02463  343 ELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSsAAKLKEEELELKSEEEKEAQ 408

DUF5401

pfam17380

Family of unknown function (DUF5401); This is a family of unknown function found in ...

814-1100

8.96e-07

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.

Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.59 E-value: 8.96e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  814 AAIVLQSCIRADSTRLKFSHQKEhraASLIQAHwriHKFRSAFRHRQSSIIAIQCRWRQ--KLAKREFRKLKQVANEAGA 891
Cdd:pfam17380  327 AEMDRQAAIYAEQERMAMERERE---LERIRQE---ERKRELERIRQEEIAMEISRMREleRLQMERQQKNERVRQELEA 400

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  892 LRLAKTKLEKRLEDLEWRLQLEKRLRTSGEEAKSSEISKLQktlESFSLKLDAARLATINECNKNAVLEKQLDISMKEKS 971
Cdd:pfam17380  401 ARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLE---EERAREMERVRLEEQERQQQVERLRQQEEERKRKKL 477

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  972 AVERElngmvelKKDNALLKnsmnslEKKNRVLEKELLNAKTNCNNTLQKLKEAEKRCSELQTSV-------QSLEEKLS 1044
Cdd:pfam17380  478 ELEKE-------KRDRKRAE------EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIyeeerrrEAEEERRK 544

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063726492 1045 HLENENQVLMQKTLITSPE---RIGQILGEQKHSSAVVPAQNDRRSvFETPTPSKHIMP 1100
Cdd:pfam17380  545 QQEMEERRRIQEQMRKATEersRLEAMEREREMMRQIVESEKARAE-YEATTPITTIKP 602

CCDC158

pfam15921

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

751-1056

1.10e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.

Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.58 E-value: 1.10e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  751 LRTFVTHQNFISARASAI--SIQAYCRGCLSRNAYATR-RNAA----AAVLVQKHVRRWLSRCAFVKLVSAAIVLQSCIR 823
Cdd:pfam15921  417 LRRELDDRNMEVQRLEALlkAMKSECQGQMERQMAAIQgKNESlekvSSLTAQLESTKEMLRKVVEELTAKKMTLESSER 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  824 ADSTrLKFSHQKEHRAASLIQAHwrIHKFRSA-----------------FRHRQSSIIAIQCRWRQK-----LAKREFRK 881
Cdd:pfam15921  497 TVSD-LTASLQEKERAIEATNAE--ITKLRSRvdlklqelqhlknegdhLRNVQTECEALKLQMAEKdkvieILRQQIEN 573

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  882 LKQVANE----AGALRLAKTKLEKRLEDLEWRLQLEKRLRtsgeEAKSSEISKLQKTLEsfSLKLDAARLATINECNKNA 957
Cdd:pfam15921  574 MTQLVGQhgrtAGAMQVEKAQLEKEINDRRLELQEFKILK----DKKDAKIRELEARVS--DLELEKVKLVNAGSERLRA 647

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  958 V--LEKQLDISMKEKSAVERELNGMVE----LKKDnalLKNSMNSLEKKNRVLEKELLNAKTNCNNTLQKLKEAE----- 1026
Cdd:pfam15921  648 VkdIKQERDQLLNEVKTSRNELNSLSEdyevLKRN---FRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgsdgh 724

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1063726492 1027 --------------KR--CSELQTSVQSLEEKLSHLENENQVLMQK 1056
Cdd:pfam15921  725 amkvamgmqkqitaKRgqIDALQSKIQFLEEAMTNANKEKHFLKEE 770

Myo5b_CBD

cd15477

Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, ...

1141-1433

1.99e-06

Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. They interact with several adaptor proteins, in case of Myo5b-CBD, Rab11-family interacting protein 2.

Pssm-ID: 271261 Cd Length: 372 Bit Score: 51.79 E-value: 1.99e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492 1141 LAACVIYKCLLH--WRAFESESTAIFNIIIEGINEALK-GGDENGVLPYWLSNASALL-CLlqrnlrsnsflnasAQRSG 1216
Cdd:cd15477     27 LPAYILYMCIRHadYINDDQKVHSLLTSTINGIKKVLKkHNDDFEMTSFWLANTCRLLhCL--------------KQYSG 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492 1217 RAAYGVKSPFKLHgpddgaSHIEARYPALLFKQQLTACVEKIYGLIRDNLKKELSPLLGSCIQAPKASRGIA-----GKS 1291
Cdd:cd15477     93 DEGFMTQNTAKQN------EHCLKNFDLTEYRQVLSDLSIQIYQQLIKIAEGILQPMIVSAMLENESIQGLSgvkpmGYR 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492 1292 RSPGGVPQQSPSSQWESILKFLDSLMSRLRENHVPSFFIRKLVTQVFSFINLSLFNSLLLRRECCTFSNGEYVKSGISEL 1371
Cdd:cd15477    167 KRSSSMADGDNSYTLEALIRQLNTFHSIMCDQGLDPEIIQQVFKQLFYMINAVTLNNLLLRKDVCSWSTGMQLRYNISQL 246

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063726492 1372 EKWIaNAKEEFAGTSWHELNYIRQAVGFLVIhqKKKKSLD-EIRQDLCPVLTIRQIYRISTMY 1433
Cdd:cd15477    247 EEWL-RGRNLHQSGAAQTMEPLIQAAQLLQL--KKKTSEDaEAICSLCTALSTQQIVKILNLY 306

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

871-1044

2.25e-06

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 2.25e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  871 RQKLAKREfRKLKQVANEAGALRLAKTKLEKRLEDLEWRLQlEKRLRTSGEEAKSSEISK----LQKTLESFSLKLDAAR 946
Cdd:TIGR02168  781 EAEIEELE-AQIEQLKEELKALREALDELRAELTLLNEEAA-NLRERLESLERRIAATERrledLEEQIEELSEDIESLA 858

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  947 LAtINECNKN-AVLEKQLDISMKEKSAVERELngmvelkkdnALLKNSMNSLEKKNRVLEKELLNAKTNCNNTLQKLKEA 1025
Cdd:TIGR02168  859 AE-IEELEELiEELESELEALLNERASLEEAL----------ALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927

                          170
                   ....*....|....*....
gi 1063726492 1026 EKRCSELQTSVQSLEEKLS 1044
Cdd:TIGR02168  928 ELRLEGLEVRIDNLQERLS 946

SMC_prok_A

TIGR02169

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

834-1050

6.56e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 6.56e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  834 QKEHRAASLIQAHW-RIHKFRSAFRHRQSSIIAIQCRWRQKLAKREfRKLKQVANEAGALRLAKTKLEKRLEDLEWRLqL 912
Cdd:TIGR02169  712 SDASRKIGEIEKEIeQLEQEEEKLKERLEELEEDLSSLEQEIENVK-SELKELEARIEELEEDLHKLEEALNDLEARL-S 789

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  913 EKRLRTSGEEAKS--SEISKLQKTLESFSLKLDAARL-ATINECNKNAVLEKQLDISMKEKSAVERELNGMVELKKDNAL 989
Cdd:TIGR02169  790 HSRIPEIQAELSKleEEVSRIEARLREIEQKLNRLTLeKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063726492  990 LKNsmnsLEKKNRVLEKELLNAKTNCNNTLQKLKEAEKRCSELQTSVQ-------SLEEKLSHLENEN 1050
Cdd:TIGR02169  870 LEE----LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEkkrkrlsELKAKLEALEEEL 933

Myosin_N

pfam02736

Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ...

17-56

9.26e-06

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: 43.96 E-value: 9.26e-06

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1063726492   17 VWVEDKDLAWIAADVLDSFDNKLHVETSTGKKVFVSPEKL 56
Cdd:pfam02736    6 VWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

872-1059

2.11e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 2.11e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  872 QKLAKREFRKLKQVANEAGALRLAKTKLEKRLEDLEwRLQLEKRLRTSGEEAKSSEISKLQKTLESFSLKLDAARlATIN 951
Cdd:COG4372      6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELD-KLQEELEQLREELEQAREELEQLEEELEQARSELEQLE-EELE 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  952 EcnknavLEKQLDISMKEKSAVERELNgmvELKKDNALLKNSMNSLEKKNRVLEKELLNAKTNCNNTLQKLKEAEKRCSE 1031
Cdd:COG4372     84 E------LNEQLQAAQAELAQAQEELE---SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE 154

                          170       180
                   ....*....|....*....|....*...
gi 1063726492 1032 LQTSVQSLEEKLSHLENENQVLMQKTLI 1059
Cdd:COG4372    155 LEEQLESLQEELAALEQELQALSEAEAE 182

Smc

COG1196

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...

850-1056

3.06e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 3.06e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  850 HKFRSAFRHRQSSIIAIQCRWRQKLAKREFRKLKQVANEAGALRLAKTKLEKRLEDLEWRLQ-LEKRLRTSGEE--AKSS 926
Cdd:COG1196    216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEeLELELEEAQAEeyELLA 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  927 EISKLQKTLESFSLKLDAARlATINEcnknavLEKQLDISMKEKSAVERELngmVELKKDNALLKNSMNSLEKKNRVLEK 1006
Cdd:COG1196    296 ELARLEQDIARLEERRRELE-ERLEE------LEEELAELEEELEELEEEL---EELEEELEEAEEELEEAEAELAEAEE 365

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1063726492 1007 ELLNAKTNCNNTLQKLKEAEKRCSELQTSVQSLEEKLSHLENENQVLMQK 1056
Cdd:COG1196    366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415

COG1340

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];

878-1050

3.18e-05

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];

Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 3.18e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  878 EFRKLKQVANEAGALRLAKTKLEKRLEDLEWRLQLEKrLRTSGEEAKSSEISKLQKTLEsfslkldaARLATINECNKNA 957
Cdd:COG1340     93 ELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEV-LSPEEEKELVEKIKELEKELE--------KAKKALEKNEKLK 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  958 VLEKQLDISMKEKSAVERELNGMVElKKDNalLKNSMNSLEKKNRVLEKELLNAKTNCNNTLQKLKEAEKRCSELQTSVQ 1037
Cdd:COG1340    164 ELRAELKELRKEAEEIHKKIKELAE-EAQE--LHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240

                          170
                   ....*....|...
gi 1063726492 1038 SLEEKLSHLENEN 1050
Cdd:COG1340    241 ELRKELKKLRKKQ 253

Smc

COG1196

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...

871-1056

3.22e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 3.22e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  871 RQKLAKREFRKLKQVANEAgALRLAKTKLEKRLEDLEwRLQLEKRLRTSGEEAKSSEISKLQKTLESFSLKLDAARLAtI 950
Cdd:COG1196    207 RQAEKAERYRELKEELKEL-EAELLLLKLRELEAELE-ELEAELEELEAELEELEAELAELEAELEELRLELEELELE-L 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  951 NECNKN--------AVLEKQLDISMKEKSAVERELNGM----VELKKDNALLKNSMNSLEKKNRVLEKELLNAKTNCNNT 1018
Cdd:COG1196    284 EEAQAEeyellaelARLEQDIARLEERRRELEERLEELeeelAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1063726492 1019 LQKLKEAEKRCSELQTSVQSLEEKLSHLENENQVLMQK 1056
Cdd:COG1196    364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401

GAS

pfam13851

Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...

956-1056

5.13e-05

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.

Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 46.05 E-value: 5.13e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  956 NAVLEKQLDI--SMKEKsaverelngMVELKKDNALLKNSMNSLEKKNRVLEKELLNAKTNCNNTLQKLKEAEKRCSELQ 1033
Cdd:pfam13851   18 NDITRNNLELikSLKEE---------IAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLK 88

                           90       100
                   ....*....|....*....|....*.
gi 1063726492 1034 TS---VQSLEEKLSHLENENQVLMQK 1056
Cdd:pfam13851   89 NLkarLKVLEKELKDLKWEHEVLEQR 114

Myosin_tail_1

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

893-1050

7.90e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.48 E-value: 7.90e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  893 RLAKTKLEKRLEDLEWRL-----QLEKRLRTSG--EEAKS---SEISKLQKTLESFSlKLDAARLATINECNKNAV--LE 960
Cdd:pfam01576  284 RAARNKAEKQRRDLGEELealktELEDTLDTTAaqQELRSkreQEVTELKKALEEET-RSHEAQLQEMRQKHTQALeeLT 362

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  961 KQLDISMKEKSAVERELNGmveLKKDNALLKNSMNSL-------EKKNRVLEKELLNAKTNCNNTLQKLKEAEKRCSELQ 1033
Cdd:pfam01576  363 EQLEQAKRNKANLEKAKQA---LESENAELQAELRTLqqakqdsEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQ 439

                          170
                   ....*....|....*..
gi 1063726492 1034 TSVQSLEEKLSHLENEN 1050
Cdd:pfam01576  440 SELESVSSLLNEAEGKN 456

EnvC

COG4942

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

871-1049

8.54e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 8.54e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  871 RQKLAKREfRKLKQVANEAGALRLAKTKLEKRLEDLEWRLQ-LEKRLRTSGEE--AKSSEISKLQKTLESFSLKLdAARL 947
Cdd:COG4942     33 QQEIAELE-KELAALKKEEKALLKQLAALERRIAALARRIRaLEQELAALEAElaELEKEIAELRAELEAQKEEL-AELL 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  948 ATI------------------NECNKNAVLEKQLDISMKEK-SAVERELNGMVELKKDNALLKNSMNSLEKKNRVLEKEL 1008
Cdd:COG4942    111 RALyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQaEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1063726492 1009 LNAKTNCNNTLQKL----KEAEKRCSELQTSVQSLEEKLSHLENE 1049
Cdd:COG4942    191 EALKAERQKLLARLekelAELAAELAELQQEAEELEALIARLEAE 235

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

866-1047

9.57e-05

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 9.57e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  866 IQCRwRQKLAKREfRKLKQVANEAGALRLAKTKLEKRLEDLEwrlqLEKRLRTSGEEAKSSEISKLQKTLESFSLKLD-- 943
Cdd:TIGR02168  672 ILER-RREIEELE-EKIEELEEKIAELEKALAELRKELEELE----EELEQLRKELEELSRQISALRKDLARLEAEVEql 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  944 AARLATINECNKNA-----VLEKQLDISMKEKSAVERElngMVELKKDNALLKNSMNSLEKKNRVLEKELLNAKTNCNNT 1018
Cdd:TIGR02168  746 EERIAQLSKELTELeaeieELEERLEEAEEELAEAEAE---IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822

                          170       180
                   ....*....|....*....|....*....
gi 1063726492 1019 LQKLKEAEKRCSELQTSVQSLEEKLSHLE 1047
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELS 851

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

894-1056

1.03e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 1.03e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  894 LAKTKLEKRLEDLEWRLQLEKRLR-----TSGEEAKSSEISKLQKTLESFSLKLDaarlatiNECNKNAVLEKQLDISMK 968
Cdd:TIGR04523  347 LKKELTNSESENSEKQRELEEKQNeieklKKENQSYKQEIKNLESQINDLESKIQ-------NQEKLNQQKDEQIKKLQQ 419

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  969 EKSAVEREL-----------NGMVELKKDNALLKNSMNSL-------EKKNRVLEKELLNAKTNCNNTLQKLKEAEKRCS 1030
Cdd:TIGR04523  420 EKELLEKEIerlketiiknnSEIKDLTNQDSVKELIIKNLdntreslETQLKVLSRSINKIKQNLEQKQKELKSKEKELK 499

                          170       180
                   ....*....|....*....|....*.
gi 1063726492 1031 ELQTSVQSLEEKLSHLENENQVLMQK 1056
Cdd:TIGR04523  500 KLNEEKKELEEKVKDLTKKISSLKEK 525

DR0291

COG1579

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

877-1085

2.27e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];

Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 2.27e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  877 REFRKLKQVANEAGALRLAKTKLEKRLEDLEWRL-QLEKRLrtsgeEAKSSEISKLQKTLESFSLKLDAARlatinecNK 955
Cdd:COG1579      7 RALLDLQELDSELDRLEHRLKELPAELAELEDELaALEARL-----EAAKTELEDLEKEIKRLELEIEEVE-------AR 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  956 NAVLEKQLD--ISMKEKSAVERELngmvelkkdnALLKNSMNSLEKKNRVLEKELLNAKTNCNNTLQKLKEAEKRCSELQ 1033
Cdd:COG1579     75 IKKYEEQLGnvRNNKEYEALQKEI----------ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK 144

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063726492 1034 TSVQS----LEEKLSHLENENQVL---MQKTLITSPERIgqilGEQKHSSAVVPAQNDR 1085
Cdd:COG1579    145 AELDEelaeLEAELEELEAEREELaakIPPELLALYERI----RKRKNGLAVVPVEGGA 199

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

897-1053

4.66e-04

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 4.66e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  897 TKLEKRLEDLEWRLQLEKRLRTSGEEAK---SSEISKLQKTLESFSLKLDAA--RLATINECN-KNAVLEKQLdismkek 970
Cdd:TIGR04523  148 KKKEKELEKLNNKYNDLKKQKEELENELnllEKEKLNIQKNIDKIKNKLLKLelLLSNLKKKIqKNKSLESQI------- 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  971 saverelngmVELKKDNALLKNSMNSLEKKNRVLEKELLNAKTNCNNTLQKLKEAEKRCSELQTSVQSLEEKLSHLENEN 1050
Cdd:TIGR04523  221 ----------SELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL 290


                   ...
gi 1063726492 1051 QVL 1053
Cdd:TIGR04523  291 NQL 293

STAT5_CCD

cd16855

Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...

911-1061

5.20e-04

Pssm-ID: 341080 [Multi-domain] Cd Length: 194 Bit Score: 43.02 E-value: 5.20e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  911 QLEKRLRTSGEEaksseISKLQKTLESF------SLKLDA--ARLATiNECNKNAVLEKQLdisMKEKSAVERELNGMVe 982
Cdd:cd16855     12 ELRQRTQETEND-----LRNLQQKQESFviqyqeSQKIQAqlQQLQQ-QPQNERIELEQQL---QQQKEQLEQLLNAKA- 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  983 lkkdNALLKNSMNSLEK-----------KNRVLEKELL----------NAKTNCNN-----------------TLQKLKE 1024
Cdd:cd16855     82 ----QELLQLRMELADKfkktiqllsklQSRVLDEELIqwkrqqqlagNGAPFESNldtiqewceslaeiiwqNRQQIKR 157

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1063726492 1025 AEKRCSELQTSV-QSLEEKLSHLENENQVLMqKTLITS 1061
Cdd:cd16855    158 AERLKQKLPIPLpPEQKDMLPILNKQITDLL-SSLVTS 194

Motor_domain

cd01363

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...

613-638

6.31e-04

Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 42.33 E-value: 6.31e-04

                           10        20
                   ....*....|....*....|....*.
gi 1063726492  613 RFKQQLQALMETLSKTEPHYVRCVKP 638
Cdd:cd01363    145 IINESLNTLMNVLRATRPHFVRCISP 170

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

875-1087

6.56e-04

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 6.56e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  875 AKREFRKLKQVANEAGA----LRLAKTKLEKRLEDLEWRLQlekrlrtsgeeAKSSEISKLQKTLESFSLKLDAARlati 950
Cdd:TIGR02168  251 AEEELEELTAELQELEEkleeLRLEVSELEEEIEELQKELY-----------ALANEISRLEQQKQILRERLANLE---- 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  951 necNKNAVLEKQLDISMKEKSAVERELNgmvELKKDNALLKNSMNSLEKKNRVLEKELlnaktncnntlqklKEAEKRCS 1030
Cdd:TIGR02168  316 ---RQLEELEAQLEELESKLDELAEELA---ELEEKLEELKEELESLEAELEELEAEL--------------EELESRLE 375

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063726492 1031 ELQTSVQSLEEKLSHLENENQVLmQKTLITSPERIGQILGEQKHSSAVVPAQNDRRS 1087
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLELQIASL-NNEIERLEARLERLEDRRERLQQEIEELLKKLE 431

HMMR_N

pfam15905

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...

877-1052

8.83e-04

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.

Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 43.26 E-value: 8.83e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  877 REFRKLKQVANEAGALRLAKTKLEKRLEDLEwrlqlekrlrtsgEEAKSSEiSKLQKTLESfSLKLDAArlatinecnkN 956
Cdd:pfam15905   70 KESKDQKELEKEIRALVQERGEQDKRLQALE-------------EELEKVE-AKLNAAVRE-KTSLSAS----------V 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  957 AVLEKQLdismkeksaverelngmVELKKDNALLKN--SMNSLEKKNRVLEKELLNAKTNCNNTLQ-----------KLK 1023
Cdd:pfam15905  125 ASLEKQL-----------------LELTRVNELLKAkfSEDGTQKKMSSLSMELMKLRNKLEAKMKevmakqegmegKLQ 187

                          170       180
                   ....*....|....*....|....*....
gi 1063726492 1024 EAEKRCSELQTSVQSLEEKLSHLENENQV 1052
Cdd:pfam15905  188 VTQKNLEHSKGKVAQLEEKLVSTEKEKIE 216

PRK03918

DNA double-strand break repair ATPase Rad50;

863-1049

1.03e-03

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 1.03e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  863 IIAIQCRWRQKLAKREFRKLKQVANEAGALRLAKTKLEKRLEDLEWRL----QLEKRLRTSGEEAKSS------------ 926
Cdd:PRK03918   367 AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIgelkKEIKELKKAIEELKKAkgkcpvcgrelt 446

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  927 -------------EISKLQKTLESFSLKLDAARlatINECNKNAVLEKQLDISMKEKSA-----VERELNG--MVELKKD 986
Cdd:PRK03918   447 eehrkelleeytaELKRIEKELKEIEEKERKLR---KELRELEKVLKKESELIKLKELAeqlkeLEEKLKKynLEELEKK 523

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063726492  987 NAL---LKNSMNSLEKKNRVLEKEllnaktncnntLQKLKEAEKRCSELQTSVQSLEEKLSHLENE 1049
Cdd:PRK03918   524 AEEyekLKEKLIKLKGEIKSLKKE-----------LEKLEELKKKLAELEKKLDELEEELAELLKE 578

PRK03918

DNA double-strand break repair ATPase Rad50;

871-1089

1.31e-03

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.31e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  871 RQKLAKREFRKLKQVANEAGALRLAKTKLEKRLEDLEWRL---------QLEKRLRTSGE------EAKSS--EISKLQK 933
Cdd:PRK03918   540 EIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELeelgfesveELEERLKELEPfyneylELKDAekELEREEK 619

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  934 TLESFSLKLDAARlATINECNKNA-VLEKQLDISMKEKSAVERE--LNGMVELKKDNALLKNSMNSLEKKNRVLEKelln 1010
Cdd:PRK03918   620 ELKKLEEELDKAF-EELAETEKRLeELRKELEELEKKYSEEEYEelREEYLELSRELAGLRAELEELEKRREEIKK---- 694

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492 1011 aktncnnTLQKLKEAEKRCSELQTSVQSLEEKLSHLEN-ENQVLMQKTLIT--SPERIGQI-------LGEQKHSSAVVP 1080
Cdd:PRK03918   695 -------TLEKLKEELEEREKAKKELEKLEKALERVEElREKVKKYKALLKerALSKVGEIaseifeeLTEGKYSGVRVK 767


                   ....*....
gi 1063726492 1081 AQNDRRSVF 1089
Cdd:PRK03918   768 AEENKVKLF 776

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

881-1091

1.38e-03

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 1.38e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  881 KLKQVANEAGaLRLAKTK--LEkRLEDLewRLQLEKRLRTSGEEAKSSEISK-LQKTLESFSLKLDAARLATINEcnKNA 957
Cdd:TIGR02168  169 KYKERRKETE-RKLERTRenLD-RLEDI--LNELERQLKSLERQAEKAERYKeLKAELRELELALLVLRLEELRE--ELE 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  958 VLEKQLDISMKEKSAVERELNgmvELKKDNALLKNSMNSLEKKNRVLEKELLNAKTNCNNTLQKLKEAEKRCSELQTSVQ 1037
Cdd:TIGR02168  243 ELQEELKEAEEELEELTAELQ---ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1063726492 1038 SLEEKLSHLENENQVLmQKTLITSPERIGQILGEQKHSSAVVPAQNDRRSVFET 1091
Cdd:TIGR02168  320 ELEAQLEELESKLDEL-AEELAELEEKLEELKEELESLEAELEELEAELEELES 372

Myosin_tail_1

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

896-1056

1.66e-03

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 1.66e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  896 KTKLEKRLEDLEWRLQLEKRLRTSGEEAK---SSEISKLQKTLESFSLKLDAARLATINECNKNAVLEKQLDISMKEKSA 972
Cdd:pfam01576  182 KNKHEAMISDLEERLKKEEKGRQELEKAKrklEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNN 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  973 VE---REL-NGMVELKKDNALLKNSMNSLEKKNRVLEKELLNAKTNCNNTL------QKLKeaEKRCSELQTSVQSLEEK 1042
Cdd:pfam01576  262 ALkkiRELeAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLdttaaqQELR--SKREQEVTELKKALEEE 339

                          170
                   ....*....|....
gi 1063726492 1043 LSHLENENQVLMQK 1056
Cdd:pfam01576  340 TRSHEAQLQEMRQK 353

IQCD

cd23767

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...

834-862

1.99e-03

Pssm-ID: 467745 [Multi-domain] Cd Length: 37 Bit Score: 37.14 E-value: 1.99e-03

                           10        20
                   ....*....|....*....|....*....
gi 1063726492  834 QKEHRAASLIQAHWRIHKFRSAFRHRQSS 862
Cdd:cd23767      6 QRMNRAATLIQALWRGYKVRKELKKKKKK 34

HMMR_N

pfam15905

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...

876-1056

2.19e-03

Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.11 E-value: 2.19e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  876 KREFRKLKQVaNEAGALRLAKTKLEKRLEDLEWRL-QLEKRLrtsgeEAKSSEISKLQKTLES------FSLKLDAARLA 948
Cdd:pfam15905  128 EKQLLELTRV-NELLKAKFSEDGTQKKMSSLSMELmKLRNKL-----EAKMKEVMAKQEGMEGklqvtqKNLEHSKGKVA 201

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  949 TINEcnKNAVLEKQldiSMKEKSAVERELNGMVEL----------KKDNALLKNSMNSLEKKNRVLEKEL------LNAK 1012
Cdd:pfam15905  202 QLEE--KLVSTEKE---KIEEKSETEKLLEYITELscvseqvekyKLDIAQLEELLKEKNDEIESLKQSLeekeqeLSKQ 276

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1063726492 1013 TNCNNTLQKLKEAEK---------RCSELQTSVQSLEEKLSHLENENQVLMQK 1056
Cdd:pfam15905  277 IKDLNEKCKLLESEKeellreyeeKEQTLNAELEELKEKLTLEEQEHQKLQQK 329

APG6_N

pfam17675

Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...

952-1056

2.37e-03

Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.

Pssm-ID: 465452 [Multi-domain] Cd Length: 127 Bit Score: 39.50 E-value: 2.37e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  952 ECNKNAV--LEKQLDISMKEKSAVERelngmvelkkdnaLLKNSMNSLEKKNRVLEKELLNAKTNCNNTLQKLKEAEKRC 1029
Cdd:pfam17675    5 ECTDLLLeeLDKQLEDAEKERDAYIS-------------FLKKLEKETPEELEELEKELEKLEKEEEELLQELEELEKER 71

                           90       100
                   ....*....|....*....|....*..
gi 1063726492 1030 SELQTSVQSLEEKLSHLENENQVLMQK 1056
Cdd:pfam17675   72 EELDAELEALEEELEALDEEEEEFWRE 98

Myosin_tail_1

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

895-1082

2.48e-03

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 2.48e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  895 AKTKLEKRLEDLEWRLQLEKRLRtsgEEAkSSEISKLQKTLESFSLKLDAAR------LATINECNKNA------VLEKQ 962
Cdd:pfam01576  771 AKKKLELDLKELEAQIDAANKGR---EEA-VKQLKKLQAQMKDLQRELEEARasrdeiLAQSKESEKKLknleaeLLQLQ 846

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  963 LDISMKE--KSAVERELNGMVELKKDNALLKNSMnsLEKKNRV------LEKELLNAKTNCNNTLQKLKEAEKRCSELQT 1034
Cdd:pfam01576  847 EDLAASEraRRQAQQERDELADEIASGASGKSAL--QDEKRRLeariaqLEEELEEEQSNTELLNDRLRKSTLQVEQLTT 924

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1063726492 1035 -------SVQSLEEKLSHLENENQVLMQKTlitsPERIGQILGEQKHSSAVVPAQ 1082
Cdd:pfam01576  925 elaaersTSQKSESARQQLERQNKELKAKL----QEMEGTVKSKFKSSIAALEAK 975

PRK03918

DNA double-strand break repair ATPase Rad50;

850-1053

2.83e-03

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 2.83e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  850 HKFRSAFRHRQSSIIAI--QCRWRQKLAKR---------EFRKLKQVANEAGALRLAKTKLEKRLEDLEWRL-QLEKRLr 917
Cdd:PRK03918   124 HVFLNAIYIRQGEIDAIleSDESREKVVRQilglddyenAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIkEKEKEL- 202

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  918 tsgeEAKSSEISKLQKTLESFSLKLDAAR---------LATINECNK-NAVLE----------KQLDISMKEKSAVEREL 977
Cdd:PRK03918   203 ----EEVLREINEISSELPELREELEKLEkevkeleelKEEIEELEKeLESLEgskrkleekiRELEERIEELKKEIEEL 278

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  978 NGMV----ELKKDNAL---LKNSMNSLEKKNRVLEKELLNAKTNCNNTLQKLKEAEKRCSELqtsvQSLEEKLSHLENEN 1050
Cdd:PRK03918   279 EEKVkelkELKEKAEEyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL----EELKKKLKELEKRL 354


                   ...
gi 1063726492 1051 QVL 1053
Cdd:PRK03918   355 EEL 357

Smc

COG1196

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...

823-1049

3.68e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 3.68e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  823 RADSTRLKFSHQKEHRAASLIQAHWRIHKFRSAFRHRQSSIIAIQcrwrQKLAKREfRKLKQVANEAGALRLAKTKLEKR 902
Cdd:COG1196    250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL----AELARLE-QDIARLEERRRELEERLEELEEE 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  903 LEDLEWRLQLEKRLRTSGEEAKSSEISKLQKTLESFSLKLDAARLATINECNKNAVLEKQLDISMKEKSAVERELNGMVE 982
Cdd:COG1196    325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063726492  983 LKKDNALLKNSMNSLEKKNRVLEKELLNAKTNCNNTLQKLKEAEKRCSELQTSVQSLEEKLSHLENE 1049
Cdd:COG1196    405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471

YhaN

COG4717

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

871-1070

3.70e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 3.70e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  871 RQKLAKREFRKLKQVANEAGALRLAKTKLEKRLEDLEwrlQLEKRLRTSGE--EAKSSEISKLQKTLESFSLKLDAARLA 948
Cdd:COG4717     55 ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYA---ELQEELEELEEelEELEAELEELREELEKLEKLLQLLPLY 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  949 tinecNKNAVLEKQLDISMKEKSAVERELNGMVELKKDNALLKNSMNSLEKK--------NRVLEKELLNAKTNCNNTLQ 1020
Cdd:COG4717    132 -----QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEEleelleqlSLATEEELQDLAEELEELQQ 206

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1063726492 1021 KLKEAEKRCSELQTSVQSLEEKLSHLENENQVLMQKTLITSPERIGQILG 1070
Cdd:COG4717    207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAA 256

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

871-1069

3.79e-03

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 3.79e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  871 RQKLAKREfRKLKQVANEAGALRLAKTKLEKRLEDLEWRLQLEKrlrtSGEEAKSSEISKLQKTLESFSLKLDaarlaTI 950
Cdd:TIGR04523  481 KQNLEQKQ-KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLK----EKIEKLESEKKEKESKISDLEDELN-----KD 550

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  951 NECNKNAVLEKQLDISMKEksaverelngMVELKKDNallknsmNSLEKKNRVLEkELLNAKTncnntlQKLKEAEKRCS 1030
Cdd:TIGR04523  551 DFELKKENLEKEIDEKNKE----------IEELKQTQ-------KSLKKKQEEKQ-ELIDQKE------KEKKDLIKEIE 606

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1063726492 1031 ELQTSVQSLEEKLSHLENENQ--VLMQKTLITSPERIGQIL 1069
Cdd:TIGR04523  607 EKEKKISSLEKELEKAKKENEklSSIIKNIKSKKNKLKQEV 647

PRK03918

DNA double-strand break repair ATPase Rad50;

876-1047

4.32e-03

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 4.32e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  876 KREFRKLKQVANEAGALRLAKTKLEKRLEDLEWRL-QLEKRLRTSG---EEAKSSEISKLQKTLESFsLKLDAARLATIN 951
Cdd:PRK03918   538 KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELaELLKELEELGfesVEELEERLKELEPFYNEY-LELKDAEKELER 616

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  952 ECNKNAVLEKQLDISMKEKSAVERELNgmvELKKDNALLKNSMNslEKKNRVLEKELLNAKTNCNNTLQKLKEAEKRCSE 1031
Cdd:PRK03918   617 EEKELKKLEEELDKAFEELAETEKRLE---ELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREE 691

                          170
                   ....*....|....*.
gi 1063726492 1032 LQTSVQSLEEKLSHLE 1047
Cdd:PRK03918   692 IKKTLEKLKEELEERE 707

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

881-1074

4.46e-03

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 4.46e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  881 KLKQVANEAgalrlaKTKlEKRLEDLEWRLQL-EKRLRTSGEEAK--SSEISKLQKTLESFSLKLDA--ARLATINECNK 955
Cdd:TIGR04523   41 KLKTIKNEL------KNK-EKELKNLDKNLNKdEEKINNSNNKIKilEQQIKDLNDKLKKNKDKINKlnSDLSKINSEIK 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  956 N-----AVLEKQLDISMKEKSAVERELNG-MVELKKDNALLKNSMN----------SLEKKNRVLEKELLNAKTNCNNT- 1018
Cdd:TIGR04523  114 NdkeqkNKLEVELNKLEKQKKENKKNIDKfLTEIKKKEKELEKLNNkyndlkkqkeELENELNLLEKEKLNIQKNIDKIk 193

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063726492 1019 ---------LQKLKEAEKRCSELQTSVQSLEEKLSHLEN----ENQVLMQKTLI--TSPERIGQILGEQKH 1074
Cdd:TIGR04523  194 nkllklellLSNLKKKIQKNKSLESQISELKKQNNQLKDniekKQQEINEKTTEisNTQTQLNQLKDEQNK 264

PRK12704

phosphodiesterase; Provisional

923-1046

4.66e-03

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 4.66e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  923 AKSSEISKLQKTLESFSLKLDAARlATINECNKNAVLEKQLDIsMKEKSAVERELNGM-VELKKDNALLKNSMNSLEKKN 1001
Cdd:PRK12704    25 RKKIAEAKIKEAEEEAKRILEEAK-KEAEAIKKEALLEAKEEI-HKLRNEFEKELRERrNELQKLEKRLLQKEENLDRKL 102

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1063726492 1002 RVLEKELLNAKTNCNNTLQKLKEAEKRCSELQTSVQSLEEKLSHL 1046
Cdd:PRK12704   103 ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147

EnvC

COG4942

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

871-1049

4.80e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 4.80e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  871 RQKLAKREfRKLKQVANEAGALRLAKTKLEKRLEDLEWRL-----QLEKRLRTSgeeAKSSEISKLQKTLESFSLkLDAA 945
Cdd:COG4942     61 ERRIAALA-RRIRALEQELAALEAELAELEKEIAELRAELeaqkeELAELLRAL---YRLGRQPPLALLLSPEDF-LDAV 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  946 R----LATINECNKNAV--LEKQLDISMKEKSAVERELNGMVELKKDNALLKNSMNSLEKKNRVLEKELLNAKTNCNNTL 1019
Cdd:COG4942    136 RrlqyLKYLAPARREQAeeLRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215

                          170       180       190
                   ....*....|....*....|....*....|
gi 1063726492 1020 QKLKEAEKRcseLQTSVQSLEEKLSHLENE 1049
Cdd:COG4942    216 AELQQEAEE---LEALIARLEAEAAAAAER 242

CALCOCO1

pfam07888

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...

869-1053

5.16e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.

Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 5.16e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  869 RWRQKLAKREFRKLKQVANEAGALRLAKTKLEKRLEDLEWRLQ-LEKRLRTSGEeaKSSEISKLQKTLESFSLKLDAAR- 946
Cdd:pfam07888   41 QERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAeLKEELRQSRE--KHEELEEKYKELSASSEELSEEKd 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726492  947 -LATINECNKNAVLEKQLDISMKEKSAVERElngmVELKKdnallknsMNSLEKKNRVLEKEllnaktncnntlqklKEA 1025
Cdd:pfam07888  119 aLLAQRAAHEARIRELEEDIKTLTQRVLERE----TELER--------MKERAKKAGAQRKE---------------EEA 171

                          170       180
                   ....*....|....*....|....*...
gi 1063726492 1026 EKRcsELQTSVQSLEEKLSHLENENQVL 1053
Cdd:pfam07888  172 ERK--QLQAKLQQTEEELRSLSKEFQEL 197

Myosin_tail_1