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Conserved domains on  [gi|755522197|ref|XP_011239990|]
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unconventional myosin-VIIa isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
108-764 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: 1373.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQ 187
Cdd:cd01381     1 AGILRNLLIRYREKLIYT------YTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  188 CCIISGESGAGKTESTKLILQFLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKI 267
Cdd:cd01381    75 CVVISGESGAGKTESTKLILQYLAAISGQHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  268 EQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTD 347
Cdd:cd01381   155 EQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTD 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  348 TENWEISKLLAAILHMGNLQYEARTFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQAL 427
Cdd:cd01381   235 EEIWDIFKLLAAILHLGNIKFEATVVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQAL 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  428 DVRDAFVKGIYGRLFVWIVEKINAAIYKPPPLEvkNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHVFKL 507
Cdd:cd01381   315 DVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTD--SSRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKL 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  508 EQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANYVPPKNSHETQFGIN 587
Cdd:cd01381   393 EQEEYDKEGINWQHIEFVDNQDVLDLIALKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNTSFGIN 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  588 HFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAETRKRSPTLSSQFKRSLELLMRTLGACQPFF 667
Cdd:cd01381   473 HFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKSPTLSSQFRKSLDQLMKTLSACQPFF 552
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  668 VRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPGVKPAYKQGDLRGTCQrMAEAV 747
Cdd:cd01381   553 VRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTDCRAATRK-ICCAV 631
                         650
                  ....*....|....*..
gi 755522197  748 LGTHDDWQIGKTKIFLK 764
Cdd:cd01381   632 LGGDADYQLGKTKIFLK 648
FERM_C2_MyoVII cd13199
FERM domain C-lobe, repeat 2, of Myosin VII (MyoVII, Myo7); MyoVII, a MyTH-FERM myosin, is an ...
2146-2241 1.94e-66

FERM domain C-lobe, repeat 2, of Myosin VII (MyoVII, Myo7); MyoVII, a MyTH-FERM myosin, is an actin-based motor protein essential for a variety of biological processes in the actin cytoskeleton function. Mutations in MyoVII leads to problems in sensory perception: deafness and blindness in humans (Usher Syndrome), retinal defects and deafness in mice (shaker 1), and aberrant auditory and vestibular function in zebrafish. Myosin VIIAs have plus (barbed) end-directed motor activity on actin filaments and a characteristic actin-activated ATPase activity. MyoVII consists of a conserved spectrin-like, SH3 subdomain N-terminal region, a motor/head region, a neck made of 4-5 IQ motifs, and a tail consisting of a coiled-coil domain, followed by a tandem repeat of myosin tail homology 4 (MyTH4) domains and partial FERM domains that are separated by an SH3 subdomain and are thought to mediate dimerization and binding to other proteins or cargo. Members include: MyoVIIa, MyoVIIb, and MyoVII members that do not have distinct myosin VIIA and myosin VIIB genes. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


:

Pssm-ID: 270020  Cd Length: 96  Bit Score: 219.44  E-value: 1.94e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 2146 GSAFFEVKQTTEPNFPEILLIAINKYGVSLIDPRTKDILTTHPFTKISNWSSGNTYFHITIGNLVRGSKLLCETSLGYKM 2225
Cdd:cd13199     1 GSAFFEVKQTTDPSLPEILLIAINKNGVSLIDPKTKEILATHPFSKISNWSSGNTYFHMTIGNLVRGSKLLCETSLGYKM 80
                          90
                  ....*....|....*.
gi 755522197 2226 DDLLTSYISQMLTAMS 2241
Cdd:cd13199    81 DDLLTSYISLLLSNMK 96
FERM1_F1_Myosin-VII cd17092
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, ...
1292-1390 8.23e-66

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of the myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in the MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the first FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


:

Pssm-ID: 340612  Cd Length: 99  Bit Score: 217.51  E-value: 8.23e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 1292 PIMLPVTFMDGTTKTLLTDSATTARELCNALADKISLKDRFGFSLYIALFDKVSSLGSGSDHVMDAISQCEQYAKEQGAQ 1371
Cdd:cd17092     1 PIMLPVTFMDGSTKTVEVDSATTARELCRQLAEKLGLKDTFGFSLYIALFDKVSSLGSGTDHVMDAISQCEQYAKEKGAQ 80
                          90
                  ....*....|....*....
gi 755522197 1372 ERNAPWRLFFRKEVFTPWH 1390
Cdd:cd17092    81 EREAPWRLYFRKEIFAPWH 99
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
1782-1931 6.44e-64

Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 other myosins.


:

Pssm-ID: 214535  Cd Length: 152  Bit Score: 214.53  E-value: 6.44e-64
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   1782 HTREPLKQALLKKIlgSEELSQEACMAFVAVLKYMGDYPSKRMRSVNELTDQIFEWALKAEPLKDEAYVQILKQLTDNHI 1861
Cdd:smart00139    1 YTKDPIKTSLLKLE--SDELQKEAVKIFKAILKFMGDIPLPRPDSHLDLVQFILQKGLDHPELRDEIYCQLIKQLTDNPS 78
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755522197   1862 RYSEERGWELLWLCTGLFPPSNILLPHVQRFLQSRKHC----PLAIDCLQRLQKALRNGSRKYPPHLVEVEAIQ 1931
Cdd:smart00139   79 RQSEERGWQLLYLCTSLFPPSERLLPYLLQFLSRRADPgseqGLAKYCLYRLERTLKNGARKQPPSRLELEAIL 152
FERM2_F1_Myosin-VII cd17093
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, ...
1936-2033 1.59e-63

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the second FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


:

Pssm-ID: 340613  Cd Length: 98  Bit Score: 210.94  E-value: 1.59e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 1936 QIFHKVYFPDDTDEAFEVESSTKAKDFCQNIASRLLLKSSEGFSLFVKIADKVISVPENDFFFDFVRHLTDWIKKARPIK 2015
Cdd:cd17093     1 QIFHKVYFPDDTDEAFEVDSSTRARDLCQNIASRLGLKSSEGFSLFVKIADKVISLPEGDFFFDFIRHLTDWIKKARPTK 80
                          90
                  ....*....|....*...
gi 755522197 2016 DGIVPSLTYQVFFMKKLW 2033
Cdd:cd17093    81 DGPKPSLTYQVFFMRKLW 98
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
1052-1288 2.20e-55

Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 other myosins.


:

Pssm-ID: 214535  Cd Length: 152  Bit Score: 189.88  E-value: 2.20e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   1052 YTRRPLKQPLLYHDDEGDQLAALAVWITILRFMGDLPEPkyhtamsdgsekipvmtkiyetlgkktykrelqalqgeget 1131
Cdd:smart00139    1 YTKDPIKTSLLKLESDELQKEAVKIFKAILKFMGDIPLP----------------------------------------- 39
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   1132 qlpegqkktsvrhklvhltlkkksklteevtkrlndgestvqgnsmledRPTSNLEKLHFIIGNGILRPALRDEIYCQIS 1211
Cdd:smart00139   40 -------------------------------------------------RPDSHLDLVQFILQKGLDHPELRDEIYCQLI 70
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   1212 KQLTHNPSKSSYARGWILVSLCVGCFAPSEKFVKYLRNFIHGGPP-----GYAPYCEERLRRTFVNGTRTQPPSWLELQA 1286
Cdd:smart00139   71 KQLTDNPSRQSEERGWQLLYLCTSLFPPSERLLPYLLQFLSRRADpgseqGLAKYCLYRLERTLKNGARKQPPSRLELEA 150

                    ..
gi 755522197   1287 TK 1288
Cdd:smart00139  151 IL 152
FERM_C1_MyoVII cd13198
FERM domain C-lobe, repeat 1, of Myosin VII (MyoVII/Myo7); MyoVII, a MyTH-FERM myosin, is an ...
1503-1639 4.56e-52

FERM domain C-lobe, repeat 1, of Myosin VII (MyoVII/Myo7); MyoVII, a MyTH-FERM myosin, is an actin-based motor protein essential for a variety of biological processes in the actin cytoskeleton function. Mutations in MyoVII leads to problems in sensory perception: deafness and blindness in humans (Usher Syndrome), retinal defects and deafness in mice (shaker 1), and aberrant auditory and vestibular function in zebrafish. Myosin VIIAs have plus (barbed) end-directed motor activity on actin filaments and a characteristic actin-activated ATPase activity. MyoVII consists of a conserved spectrin-like, SH3 subdomain N-terminal region, a motor/head region, a neck made of 4-5 IQ motifs, and a tail consisting of a coiled-coil domain, followed by a tandem repeat of myosin tail homology 4 (MyTH4) domains and partial FERM domains that are separated by an SH3 subdomain and are thought to mediate dimerization and binding to other proteins or cargo. Members include: MyoVIIa, MyoVIIb, and MyoVII members that do not have distinct myosin VIIA and myosin VIIB genes. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


:

Pssm-ID: 270019  Cd Length: 99  Bit Score: 178.18  E-value: 4.56e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 1503 LLFSRFYEAYKFSGPPLPKSDVIVAVNWTGVYFVDEQEQVLLELSFPEIMAVSSSrecrvllslgcsdlgcatcqsgrag 1582
Cdd:cd13198     1 LLFSRFFEATKFSGPSLPKSEVIIAVNWTGIYFVDEQEQVLLELSFPEITGVSSS------------------------- 55
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755522197 1583 ltpagpcspcwscRGTKMMAPSFTLATIKGDEYTFTSSNAEDIRDLVVTFLEGLRKR 1639
Cdd:cd13198    56 -------------RGKRDGGQSFTLTTIQGEEFVFQSPNAEDIAELVNYFLEGLRKR 99
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
1938-2150 1.91e-46

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


:

Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 166.32  E-value: 1.91e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   1938 FHKVYFPDDTDEAFEVESSTKAKDFCQNIASRLLLKSSEGFSLFVKIADKVISvpendfffdfvrhltDWIKKARPIKDG 2017
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLR---------------HWLDPAKTLLDQ 65
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   2018 IVPSLTYQVFFMKKLWTTTV--PGKDPMADsIFHYYQELPKYLRGYHKCTREEVLQLGALIYRVKFEEDKSYFPSIPK-- 2093
Cdd:smart00295   66 DVKSEPLTLYFRVKFYPPDPnqLKEDPTRL-NLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDLRGel 144
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 755522197   2094 LLRELVPQDLIRQVSPDDWKRSIVAYFNKHAGKSKEEAKLAFLKLIFKWPTFGSAFF 2150
Cdd:smart00295  145 SLKRFLPKQLLDSRKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
1294-1509 2.52e-38

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


:

Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 143.20  E-value: 2.52e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   1294 MLPVTFMDGTTKTLLTDSATTARELCNALADKISLKDRFGFSLYIALFDKVsslgsgsdhvmdaISQCEQYAKEQGAQER 1373
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDED-------------LRHWLDPAKTLLDQDV 67
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   1374 N-APWRLFFRKEVFTPWHN-PSEDNVATNLIYQQVVRGVKFGEYRCEKEdDLAELASQQYFVDYG---SEMILERLLSLV 1448
Cdd:smart00295   68 KsEPLTLYFRVKFYPPDPNqLKEDPTRLNLLYLQVRNDILEGRLPCPEE-EALLLAALALQAEFGdydEELHDLRGELSL 146
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755522197   1449 PTYIPDREITPLKnLEKWAQLAIAAHKKGIYaQRRTDSqKVKedVVNYARfKWPLLFSRFY 1509
Cdd:smart00295  147 KRFLPKQLLDSRK-LKEWRERIVELHKELIG-LSPEEA-KLK--YLELAR-KLPTYGVELF 201
SH3_MYO7A cd11881
Src Homology 3 domain of Myosin VIIa and similar proteins; Myo7A is an uncoventional myosin ...
1640-1704 4.50e-36

Src Homology 3 domain of Myosin VIIa and similar proteins; Myo7A is an uncoventional myosin that is involved in organelle transport. It is required for sensory function in both Drosophila and mammals. Mutations in the Myo7A gene cause both syndromic deaf-blindness [Usher syndrome I (USH1)] and nonsyndromic (DFNB2 and DFNA11) deafness in humans. It contains an N-terminal motor domain, light chain-binding IQ motifs, a coiled-coil region for heavy chain dimerization, and a tail consisting of a pair of MyTH4-FERM tandems separated by a SH3 domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


:

Pssm-ID: 212814  Cd Length: 64  Bit Score: 131.48  E-value: 4.50e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755522197 1640 SKYVVALQDNPNPAGEeSGFLSFAKGDLIILDHDTGEQVMNSGWANGINERTKQRGDFPTDCVYV 1704
Cdd:cd11881     1 SKYVVALQDYPNPSDG-SSFLSFAKGDLIILDQDTGEQVMNSGWCNGRNDRTGQRGDFPADCVYV 64
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
892-970 2.21e-10

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


:

Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 61.21  E-value: 2.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   892 RRLRVEYQRRLEAERM-RLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKKELLEQME-KARH 969
Cdd:pfam05672   33 ERLEKEEEERLRKEELrRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEaKARE 112

                   .
gi 755522197   970 E 970
Cdd:pfam05672  113 E 113
PTZ00121 super family cl31754
MAEBL; Provisional
838-1010 4.89e-08

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 4.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  838 SRKLHKQYRLARQRIIEfQARcRAYLVRKAFRHRlwaviTVQAYARGMIARRLHRRLRVEYQRRLE----AERMRLAEE- 912
Cdd:PTZ00121 1115 RKAEEAKKKAEDARKAE-EAR-KAEDARKAEEAR-----KAEDAKRVEIARKAEDARKAEEARKAEdakkAEAARKAEEv 1187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  913 ---EKLRKEMSAKKAkEEAERKHQERLAQLAR--EDAER--ELKEKEEARRKKELLEQMEKARHEPINHSDMVDKMFGFL 985
Cdd:PTZ00121 1188 rkaEELRKAEDARKA-EAARKAEEERKAEEARkaEDAKKaeAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFA 1266
                         170       180
                  ....*....|....*....|....*
gi 755522197  986 GTSGSLPGQEGQAPSGFEDLERGRR 1010
Cdd:PTZ00121 1267 RRQAAIKAEEARKADELKKAEEKKK 1291
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
801-822 1.02e-04

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


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 41.16  E-value: 1.02e-04
                            10        20
                    ....*....|....*....|..
gi 755522197    801 RLKSAATLIQRHWRGHHCRKNY 822
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRY 22
 
Name Accession Description Interval E-value
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
108-764 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: 1373.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQ 187
Cdd:cd01381     1 AGILRNLLIRYREKLIYT------YTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  188 CCIISGESGAGKTESTKLILQFLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKI 267
Cdd:cd01381    75 CVVISGESGAGKTESTKLILQYLAAISGQHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  268 EQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTD 347
Cdd:cd01381   155 EQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTD 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  348 TENWEISKLLAAILHMGNLQYEARTFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQAL 427
Cdd:cd01381   235 EEIWDIFKLLAAILHLGNIKFEATVVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQAL 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  428 DVRDAFVKGIYGRLFVWIVEKINAAIYKPPPLEvkNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHVFKL 507
Cdd:cd01381   315 DVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTD--SSRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKL 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  508 EQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANYVPPKNSHETQFGIN 587
Cdd:cd01381   393 EQEEYDKEGINWQHIEFVDNQDVLDLIALKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNTSFGIN 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  588 HFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAETRKRSPTLSSQFKRSLELLMRTLGACQPFF 667
Cdd:cd01381   473 HFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKSPTLSSQFRKSLDQLMKTLSACQPFF 552
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  668 VRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPGVKPAYKQGDLRGTCQrMAEAV 747
Cdd:cd01381   553 VRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTDCRAATRK-ICCAV 631
                         650
                  ....*....|....*..
gi 755522197  748 LGTHDDWQIGKTKIFLK 764
Cdd:cd01381   632 LGGDADYQLGKTKIFLK 648
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
89-776 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: 1024.79  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197     89 HPTSVHGVEDMIRLGDLNEAGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPH 168
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYT------YIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPH 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197    169 IFAIADNCYFNMKRNNRDQCCIISGESGAGKTESTKLILQFLAAISGQ---HSWIEQQVLEATPILEAFGNAKTIRNDNS 245
Cdd:smart00242   75 VFAIADNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSnteVGSVEDQILESNPILEAFGNAKTLRNNNS 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197    246 SRFGKYIDIHFNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCE 325
Cdd:smart00242  155 SRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVD 234
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197    326 GRVDSQEYANIRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFENlDACEVLFSPSLATAASLLEVNPPDLMSCL 405
Cdd:smart00242  235 GIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDN-AASTVKDKEELSNAAELLGVDPEELEKAL 313
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197    406 TSRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPpplevKNSRRSIGLLDIFGFENFTVNSFE 485
Cdd:smart00242  314 TKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFK-----DGSTYFIGVLDIYGFEIFEVNSFE 388
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197    486 QLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNS 565
Cdd:smart00242  389 QLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQ 468
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197    566 QHKLNANYVPPKNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQaDVAMGAETRKRSPTL 645
Cdd:smart00242  469 HHKKHPHFSKPKKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFP-SGVSNAGSKKRFQTV 547
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197    646 SSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLP 725
Cdd:smart00242  548 GSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLP 627
                           650       660       670       680       690
                    ....*....|....*....|....*....|....*....|....*....|.
gi 755522197    726 GVKPAyKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLKDHHDMLLEVERD 776
Cdd:smart00242  628 DTWPP-WGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
Myosin_head pfam00063
Myosin head (motor domain);
96-764 0e+00

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 840.02  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197    96 VEDMIRLGDLNEAGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADN 175
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYT------YSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADE 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   176 CYFNMKRNNRDQCCIISGESGAGKTESTKLILQFLAAISGQHSW-----IEQQVLEATPILEAFGNAKTIRNDNSSRFGK 250
Cdd:pfam00063   75 AYRSMLQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAgnvgrLEEQILQSNPILEAFGNAKTVRNNNSSRFGK 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   251 YIDIHFNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCEGRVDS 330
Cdd:pfam00063  155 YIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDS 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   331 QEYANIRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARtfENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTL 410
Cdd:pfam00063  235 EEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKE--RNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRI 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   411 ITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPpplevKNSRRS-IGLLDIFGFENFTVNSFEQLCI 489
Cdd:pfam00063  313 KTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVK-----TIEKASfIGVLDIYGFEIFEKNSFEQLCI 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   490 NFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKL 569
Cdd:pfam00063  388 NYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPKATDQTFLDKLYSTFSK 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   570 NANYVPPKNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ------------ADVAMGAE 637
Cdd:pfam00063  468 HPHFQKPRLQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPdyetaesaaaneSGKSTPKR 547
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   638 TRKRSP-TLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEF 716
Cdd:pfam00063  548 TKKKRFiTVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEF 627
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*...
gi 755522197   717 VERYRVLLPGVKPAYKqGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:pfam00063  628 VQRYRILAPKTWPKWK-GDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
COG5022 COG5022
Myosin heavy chain [General function prediction only];
88-981 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 791.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   88 MHPTSVHGVEDMIRLGDLNEAGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPP 167
Cdd:COG5022    60 IKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYT------YSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEP 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  168 HIFAIADNCYFNMKRNNRDQCCIISGESGAGKTESTKLILQFLAAISGQHSW----IEQQVLEATPILEAFGNAKTIRND 243
Cdd:COG5022   134 HVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTVeissIEKQILATNPILEAFGNAKTVRND 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  244 NSSRFGKYIDIHFNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCIT 323
Cdd:COG5022   214 NSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDK 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  324 CEGRVDSQEYANIRSAMKVLMFTDTENWEISKLLAAILHMGNLQY-EARTfenlDACEVLFSPSLATAASLLEVNPPDLM 402
Cdd:COG5022   294 IDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFkEDRN----GAAIFSDNSVLDKACYLLGIDPSLFV 369
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  403 SCLTSRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPplEVKNsrrSIGLLDIFGFENFTVN 482
Cdd:COG5022   370 KWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSA--AASN---FIGVLDIYGFEIFEKN 444
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  483 SFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMI-ANRPMNVISLIDEESKFPKGTDATMLH 561
Cdd:COG5022   445 SFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIeKKNPLGILSLLDEECVMPHATDESFTS 524
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  562 KLNSQHKLNAN--YVPPKNShETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFqaDVAMGAETR 639
Cdd:COG5022   525 KLAQRLNKNSNpkFKKSRFR-DNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLF--DDEENIESK 601
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  640 KRSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVER 719
Cdd:COG5022   602 GRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQR 681
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  720 YRVLLPGVKPAY---KQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLKDHHDMLLEVERDKAITDRVILLQKVIRGFKDR 796
Cdd:COG5022   682 YRILSPSKSWTGeytWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLR 761
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  797 SNFLR-LKS--AATLIQRHWRgHHCRKNYELIRLGFLRLQALHRSRKLHKQYRLARQRIIEFQARCRAYLVRK-----AF 868
Cdd:COG5022   762 RRYLQaLKRikKIQVIQHGFR-LRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLReteevEF 840
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  869 RHRlwAVITVQAYARGMIARRLHRRL-----RVEYQRRLEAERMRLAEEEKLRKEMSAKKAK------------------ 925
Cdd:COG5022   841 SLK--AEVLIQKFGRSLKAKKRFSLLkketiYLQSAQRVELAERQLQELKIDVKSISSLKLVnleleseiielkkslssd 918
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755522197  926 EEAERKHQ-ERLAQLAREDAEREL-----KEKEEARRKKELLEQMEKARHEPINHSDMVDKM 981
Cdd:COG5022   919 LIENLEFKtELIARLKKLLNNIDLeegpsIEYVKLPELNKLHEVESKLKETSEEYEDLLKKS 980
PTZ00014 PTZ00014
myosin-A; Provisional
102-816 7.74e-153

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 495.70  E-value: 7.74e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  102 LGDL---NEAGILRNLLIRYRDHLIYTScggrtyTGSILVAVNPYQLLSIYSPEHIRQY-TNKKIGEMPPHIFAIADNCY 177
Cdd:PTZ00014  101 IGLLphtNIPCVLDFLKHRYLKNQIYTT------ADPLLVAINPFKDLGNTTNDWIRRYrDAKDSDKLPPHVFTTARRAL 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  178 FNMKRNNRDQCCIISGESGAGKTESTKLILQFLAAISGQH--SWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIH 255
Cdd:PTZ00014  175 ENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNmdLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQ 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  256 FNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAmGNCITCEGRVDSQEYAN 335
Cdd:PTZ00014  255 LGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYIN-PKCLDVPGIDDVKDFEE 333
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  336 IRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFENLDACEVLFSPSLAT---AASLLEVNPPDLMSCLTSRTLIT 412
Cdd:PTZ00014  334 VMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDAAAISDESLEVfneACELLFLDYESLKKELTVKVTYA 413
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  413 RGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPPLEVknsrrSIGLLDIFGFENFTVNSFEQLCINFA 492
Cdd:PTZ00014  414 GNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-----FIGMLDIFGFEVFKNNSLEQLFINIT 488
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  493 NEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNAN 572
Cdd:PTZ00014  489 NEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPK 568
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  573 YVPPKNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAETRKRSpTLSSQFKRS 652
Cdd:PTZ00014  569 YKPAKVDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKGKLAKGQ-LIGSQFLNQ 647
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  653 LELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVL-LPGVKPay 731
Cdd:PTZ00014  648 LDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLdLAVSND-- 725
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  732 KQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK-DHHDMLLEVERDK--------AITDRVILLQKVIRGFKDRSNFLrl 802
Cdd:PTZ00014  726 SSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkDAAKELTQIQREKlaaweplvSVLEALILKIKKKRKVRKNIKSL-- 803
                         730
                  ....*....|....
gi 755522197  803 ksaaTLIQRHWRGH 816
Cdd:PTZ00014  804 ----VRIQAHLRRH 813
FERM_C2_MyoVII cd13199
FERM domain C-lobe, repeat 2, of Myosin VII (MyoVII, Myo7); MyoVII, a MyTH-FERM myosin, is an ...
2146-2241 1.94e-66

FERM domain C-lobe, repeat 2, of Myosin VII (MyoVII, Myo7); MyoVII, a MyTH-FERM myosin, is an actin-based motor protein essential for a variety of biological processes in the actin cytoskeleton function. Mutations in MyoVII leads to problems in sensory perception: deafness and blindness in humans (Usher Syndrome), retinal defects and deafness in mice (shaker 1), and aberrant auditory and vestibular function in zebrafish. Myosin VIIAs have plus (barbed) end-directed motor activity on actin filaments and a characteristic actin-activated ATPase activity. MyoVII consists of a conserved spectrin-like, SH3 subdomain N-terminal region, a motor/head region, a neck made of 4-5 IQ motifs, and a tail consisting of a coiled-coil domain, followed by a tandem repeat of myosin tail homology 4 (MyTH4) domains and partial FERM domains that are separated by an SH3 subdomain and are thought to mediate dimerization and binding to other proteins or cargo. Members include: MyoVIIa, MyoVIIb, and MyoVII members that do not have distinct myosin VIIA and myosin VIIB genes. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270020  Cd Length: 96  Bit Score: 219.44  E-value: 1.94e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 2146 GSAFFEVKQTTEPNFPEILLIAINKYGVSLIDPRTKDILTTHPFTKISNWSSGNTYFHITIGNLVRGSKLLCETSLGYKM 2225
Cdd:cd13199     1 GSAFFEVKQTTDPSLPEILLIAINKNGVSLIDPKTKEILATHPFSKISNWSSGNTYFHMTIGNLVRGSKLLCETSLGYKM 80
                          90
                  ....*....|....*.
gi 755522197 2226 DDLLTSYISQMLTAMS 2241
Cdd:cd13199    81 DDLLTSYISLLLSNMK 96
FERM1_F1_Myosin-VII cd17092
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, ...
1292-1390 8.23e-66

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of the myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in the MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the first FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340612  Cd Length: 99  Bit Score: 217.51  E-value: 8.23e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 1292 PIMLPVTFMDGTTKTLLTDSATTARELCNALADKISLKDRFGFSLYIALFDKVSSLGSGSDHVMDAISQCEQYAKEQGAQ 1371
Cdd:cd17092     1 PIMLPVTFMDGSTKTVEVDSATTARELCRQLAEKLGLKDTFGFSLYIALFDKVSSLGSGTDHVMDAISQCEQYAKEKGAQ 80
                          90
                  ....*....|....*....
gi 755522197 1372 ERNAPWRLFFRKEVFTPWH 1390
Cdd:cd17092    81 EREAPWRLYFRKEIFAPWH 99
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
1782-1931 6.44e-64

Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 214535  Cd Length: 152  Bit Score: 214.53  E-value: 6.44e-64
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   1782 HTREPLKQALLKKIlgSEELSQEACMAFVAVLKYMGDYPSKRMRSVNELTDQIFEWALKAEPLKDEAYVQILKQLTDNHI 1861
Cdd:smart00139    1 YTKDPIKTSLLKLE--SDELQKEAVKIFKAILKFMGDIPLPRPDSHLDLVQFILQKGLDHPELRDEIYCQLIKQLTDNPS 78
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755522197   1862 RYSEERGWELLWLCTGLFPPSNILLPHVQRFLQSRKHC----PLAIDCLQRLQKALRNGSRKYPPHLVEVEAIQ 1931
Cdd:smart00139   79 RQSEERGWQLLYLCTSLFPPSERLLPYLLQFLSRRADPgseqGLAKYCLYRLERTLKNGARKQPPSRLELEAIL 152
FERM2_F1_Myosin-VII cd17093
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, ...
1936-2033 1.59e-63

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the second FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340613  Cd Length: 98  Bit Score: 210.94  E-value: 1.59e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 1936 QIFHKVYFPDDTDEAFEVESSTKAKDFCQNIASRLLLKSSEGFSLFVKIADKVISVPENDFFFDFVRHLTDWIKKARPIK 2015
Cdd:cd17093     1 QIFHKVYFPDDTDEAFEVDSSTRARDLCQNIASRLGLKSSEGFSLFVKIADKVISLPEGDFFFDFIRHLTDWIKKARPTK 80
                          90
                  ....*....|....*...
gi 755522197 2016 DGIVPSLTYQVFFMKKLW 2033
Cdd:cd17093    81 DGPKPSLTYQVFFMRKLW 98
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
1052-1288 2.20e-55

Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 214535  Cd Length: 152  Bit Score: 189.88  E-value: 2.20e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   1052 YTRRPLKQPLLYHDDEGDQLAALAVWITILRFMGDLPEPkyhtamsdgsekipvmtkiyetlgkktykrelqalqgeget 1131
Cdd:smart00139    1 YTKDPIKTSLLKLESDELQKEAVKIFKAILKFMGDIPLP----------------------------------------- 39
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   1132 qlpegqkktsvrhklvhltlkkksklteevtkrlndgestvqgnsmledRPTSNLEKLHFIIGNGILRPALRDEIYCQIS 1211
Cdd:smart00139   40 -------------------------------------------------RPDSHLDLVQFILQKGLDHPELRDEIYCQLI 70
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   1212 KQLTHNPSKSSYARGWILVSLCVGCFAPSEKFVKYLRNFIHGGPP-----GYAPYCEERLRRTFVNGTRTQPPSWLELQA 1286
Cdd:smart00139   71 KQLTDNPSRQSEERGWQLLYLCTSLFPPSERLLPYLLQFLSRRADpgseqGLAKYCLYRLERTLKNGARKQPPSRLELEA 150

                    ..
gi 755522197   1287 TK 1288
Cdd:smart00139  151 IL 152
FERM_C1_MyoVII cd13198
FERM domain C-lobe, repeat 1, of Myosin VII (MyoVII/Myo7); MyoVII, a MyTH-FERM myosin, is an ...
1503-1639 4.56e-52

FERM domain C-lobe, repeat 1, of Myosin VII (MyoVII/Myo7); MyoVII, a MyTH-FERM myosin, is an actin-based motor protein essential for a variety of biological processes in the actin cytoskeleton function. Mutations in MyoVII leads to problems in sensory perception: deafness and blindness in humans (Usher Syndrome), retinal defects and deafness in mice (shaker 1), and aberrant auditory and vestibular function in zebrafish. Myosin VIIAs have plus (barbed) end-directed motor activity on actin filaments and a characteristic actin-activated ATPase activity. MyoVII consists of a conserved spectrin-like, SH3 subdomain N-terminal region, a motor/head region, a neck made of 4-5 IQ motifs, and a tail consisting of a coiled-coil domain, followed by a tandem repeat of myosin tail homology 4 (MyTH4) domains and partial FERM domains that are separated by an SH3 subdomain and are thought to mediate dimerization and binding to other proteins or cargo. Members include: MyoVIIa, MyoVIIb, and MyoVII members that do not have distinct myosin VIIA and myosin VIIB genes. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270019  Cd Length: 99  Bit Score: 178.18  E-value: 4.56e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 1503 LLFSRFYEAYKFSGPPLPKSDVIVAVNWTGVYFVDEQEQVLLELSFPEIMAVSSSrecrvllslgcsdlgcatcqsgrag 1582
Cdd:cd13198     1 LLFSRFFEATKFSGPSLPKSEVIIAVNWTGIYFVDEQEQVLLELSFPEITGVSSS------------------------- 55
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755522197 1583 ltpagpcspcwscRGTKMMAPSFTLATIKGDEYTFTSSNAEDIRDLVVTFLEGLRKR 1639
Cdd:cd13198    56 -------------RGKRDGGQSFTLTTIQGEEFVFQSPNAEDIAELVNYFLEGLRKR 99
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
1938-2150 1.91e-46

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 166.32  E-value: 1.91e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   1938 FHKVYFPDDTDEAFEVESSTKAKDFCQNIASRLLLKSSEGFSLFVKIADKVISvpendfffdfvrhltDWIKKARPIKDG 2017
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLR---------------HWLDPAKTLLDQ 65
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   2018 IVPSLTYQVFFMKKLWTTTV--PGKDPMADsIFHYYQELPKYLRGYHKCTREEVLQLGALIYRVKFEEDKSYFPSIPK-- 2093
Cdd:smart00295   66 DVKSEPLTLYFRVKFYPPDPnqLKEDPTRL-NLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDLRGel 144
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 755522197   2094 LLRELVPQDLIRQVSPDDWKRSIVAYFNKHAGKSKEEAKLAFLKLIFKWPTFGSAFF 2150
Cdd:smart00295  145 SLKRFLPKQLLDSRKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
MyTH4 pfam00784
MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also ...
1189-1286 8.43e-42

MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 459939  Cd Length: 105  Bit Score: 149.27  E-value: 8.43e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  1189 LHFIIGNGILRPALRDEIYCQISKQLTHNPSKSSYARGWILVSLCVGCFAPSEKFVKYLRNFIH-------GGPPGYAPY 1261
Cdd:pfam00784    1 AQNILQKGLKRPELRDEIYCQLIKQTTNNPKPESLLRGWQLLALCLGTFPPSKKLLKYLLKFLKrhaddpsREVGKYAQF 80
                           90       100
                   ....*....|....*....|....*
gi 755522197  1262 CEERLRRTFVNGTRTQPPSWLELQA 1286
Cdd:pfam00784   81 CLKRLKRTLKNGGRKYPPSREEIEA 105
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
1294-1509 2.52e-38

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 143.20  E-value: 2.52e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   1294 MLPVTFMDGTTKTLLTDSATTARELCNALADKISLKDRFGFSLYIALFDKVsslgsgsdhvmdaISQCEQYAKEQGAQER 1373
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDED-------------LRHWLDPAKTLLDQDV 67
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   1374 N-APWRLFFRKEVFTPWHN-PSEDNVATNLIYQQVVRGVKFGEYRCEKEdDLAELASQQYFVDYG---SEMILERLLSLV 1448
Cdd:smart00295   68 KsEPLTLYFRVKFYPPDPNqLKEDPTRLNLLYLQVRNDILEGRLPCPEE-EALLLAALALQAEFGdydEELHDLRGELSL 146
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755522197   1449 PTYIPDREITPLKnLEKWAQLAIAAHKKGIYaQRRTDSqKVKedVVNYARfKWPLLFSRFY 1509
Cdd:smart00295  147 KRFLPKQLLDSRK-LKEWRERIVELHKELIG-LSPEEA-KLK--YLELAR-KLPTYGVELF 201
MyTH4 pfam00784
MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also ...
1831-1929 2.78e-37

MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 459939  Cd Length: 105  Bit Score: 136.17  E-value: 2.78e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  1831 TDQIFEWALKAEPLKDEAYVQILKQLTDNHIRYSEERGWELLWLCTGLFPPSNILLPHVQRFLQ------SRKHCPLAID 1904
Cdd:pfam00784    1 AQNILQKGLKRPELRDEIYCQLIKQTTNNPKPESLLRGWQLLALCLGTFPPSKKLLKYLLKFLKrhaddpSREVGKYAQF 80
                           90       100
                   ....*....|....*....|....*
gi 755522197  1905 CLQRLQKALRNGSRKYPPHLVEVEA 1929
Cdd:pfam00784   81 CLKRLKRTLKNGGRKYPPSREEIEA 105
SH3_MYO7A cd11881
Src Homology 3 domain of Myosin VIIa and similar proteins; Myo7A is an uncoventional myosin ...
1640-1704 4.50e-36

Src Homology 3 domain of Myosin VIIa and similar proteins; Myo7A is an uncoventional myosin that is involved in organelle transport. It is required for sensory function in both Drosophila and mammals. Mutations in the Myo7A gene cause both syndromic deaf-blindness [Usher syndrome I (USH1)] and nonsyndromic (DFNB2 and DFNA11) deafness in humans. It contains an N-terminal motor domain, light chain-binding IQ motifs, a coiled-coil region for heavy chain dimerization, and a tail consisting of a pair of MyTH4-FERM tandems separated by a SH3 domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212814  Cd Length: 64  Bit Score: 131.48  E-value: 4.50e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755522197 1640 SKYVVALQDNPNPAGEeSGFLSFAKGDLIILDHDTGEQVMNSGWANGINERTKQRGDFPTDCVYV 1704
Cdd:cd11881     1 SKYVVALQDYPNPSDG-SSFLSFAKGDLIILDQDTGEQVMNSGWCNGRNDRTGQRGDFPADCVYV 64
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
2048-2150 3.42e-20

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 88.10  E-value: 3.42e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  2048 FHYYQELPKYLRGYHKCTREEVLQLGALIYRVKF--EEDKSYFPSIPKLLReLVPQDLIRQVSPDDWKRSIVAYFNKHAG 2125
Cdd:pfam00373   14 LLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFgdYQPSSHTSEYLSLES-FLPKQLLRKMKSKELEKRVLEAHKNLRG 92
                           90       100
                   ....*....|....*....|....*
gi 755522197  2126 KSKEEAKLAFLKLIFKWPTFGSAFF 2150
Cdd:pfam00373   93 LSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
2048-2142 1.23e-18

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 83.06  E-value: 1.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 2048 FHYYQELPKYLRGYHKCTREEVLQLGALIYRVKF-EEDKSYFPSIPKLLRELVPQDLIRQVSPDDWKRSIVAYFNKHAGK 2126
Cdd:cd14473     4 LLYLQVKRDILEGRLPCSEETAALLAALALQAEYgDYDPSEHKPKYLSLKRFLPKQLLKQRKPEEWEKRIVELHKKLRGL 83
                          90
                  ....*....|....*.
gi 755522197 2127 SKEEAKLAFLKLIFKW 2142
Cdd:cd14473    84 SPAEAKLKYLKIARKL 99
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
1398-1498 6.28e-11

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 61.11  E-value: 6.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 1398 ATNLIYQQVVRGVKFGEYRCeKEDDLAELASQQYFVDYG--SEMILERLLSLVPTYIPDREITPLKNlEKWAQLAIAAHK 1475
Cdd:cd14473     1 TRYLLYLQVKRDILEGRLPC-SEETAALLAALALQAEYGdyDPSEHKPKYLSLKRFLPKQLLKQRKP-EEWEKRIVELHK 78
                          90       100
                  ....*....|....*....|...
gi 755522197 1476 KgiyaQRRTDSQKVKEDVVNYAR 1498
Cdd:cd14473    79 K----LRGLSPAEAKLKYLKIAR 97
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
892-970 2.21e-10

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 61.21  E-value: 2.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   892 RRLRVEYQRRLEAERM-RLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKKELLEQME-KARH 969
Cdd:pfam05672   33 ERLEKEEEERLRKEELrRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEaKARE 112

                   .
gi 755522197   970 E 970
Cdd:pfam05672  113 E 113
PTZ00121 PTZ00121
MAEBL; Provisional
838-1010 4.89e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 4.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  838 SRKLHKQYRLARQRIIEfQARcRAYLVRKAFRHRlwaviTVQAYARGMIARRLHRRLRVEYQRRLE----AERMRLAEE- 912
Cdd:PTZ00121 1115 RKAEEAKKKAEDARKAE-EAR-KAEDARKAEEAR-----KAEDAKRVEIARKAEDARKAEEARKAEdakkAEAARKAEEv 1187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  913 ---EKLRKEMSAKKAkEEAERKHQERLAQLAR--EDAER--ELKEKEEARRKKELLEQMEKARHEPINHSDMVDKMFGFL 985
Cdd:PTZ00121 1188 rkaEELRKAEDARKA-EAARKAEEERKAEEARkaEDAKKaeAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFA 1266
                         170       180
                  ....*....|....*....|....*
gi 755522197  986 GTSGSLPGQEGQAPSGFEDLERGRR 1010
Cdd:PTZ00121 1267 RRQAAIKAEEARKADELKKAEEKKK 1291
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
809-966 1.91e-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: 56.67  E-value: 1.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   809 IQRHWRGHHCRKNYELIRLgfLRLQALHRSRKLHKQYRLARQrIIEFQARCRAYLVRKAFRHRlwavitvqayargmiAR 888
Cdd:pfam17380  385 MERQQKNERVRQELEAARK--VKILEEERQRKIQQQKVEMEQ-IRAEQEEARQREVRRLEEER---------------AR 446
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755522197   889 RLHRRLRVEYQRRLEAERMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKKELLEQMEK 966
Cdd:pfam17380  447 EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEE 524
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
895-959 2.91e-07

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 54.85  E-value: 2.91e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   895 RVEYQRRLEAERMRLAEEEKLRKEMSAKKAKEE-----AERKHQERLAQLAREDAERELKEKEEARRKKE 959
Cdd:TIGR02794   84 RAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEkqkqaEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE 153
PTZ00121 PTZ00121
MAEBL; Provisional
860-970 4.10e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.92  E-value: 4.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  860 RAYLVRKAFRHRLWAVITVQAYARGMIARRLhrrlRVEYQRRLEAERMRLAEEEKLRKEMSAKKAKEE---AE--RKHQE 934
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEA----KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEkkkAEelKKAEE 1657
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 755522197  935 ----RLAQLAREDAE-----RELKEKEEARRKKEllEQMEKARHE 970
Cdd:PTZ00121 1658 enkiKAAEEAKKAEEdkkkaEEAKKAEEDEKKAA--EALKKEAEE 1700
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
909-968 1.22e-06

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 47.65  E-value: 1.22e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  909 LAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKKELLEQMEKAR 968
Cdd:cd22249     1 LSKPGEIREEYEAQLKKLEEERRKEREEEEKASEELIRKLQEEEERQRKREREEQLKQDE 60
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
834-967 1.32e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  834 ALHRSRKLHKQYRLARQRIIEFQARCRAYLVRKAFRHRLWAVITVQAYArgmIARRLHRRLRVEYQ--RRLEAERMRLAE 911
Cdd:COG1196   230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE---LELELEEAQAEEYEllAELARLEQDIAR 306
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 755522197  912 EEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKKELLEQMEKA 967
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
801-822 1.02e-04

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 41.16  E-value: 1.02e-04
                            10        20
                    ....*....|....*....|..
gi 755522197    801 RLKSAATLIQRHWRGHHCRKNY 822
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRY 22
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
1639-1702 3.23e-04

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 40.60  E-value: 3.23e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755522197   1639 RSKYVVALQDNPnpaGEESGFLSFAKGDLIILDHDTgeqvmNSGWANGINERtKQRGDFPTDCV 1702
Cdd:smart00326    1 EGPQVRALYDYT---AQDPDELSFKKGDIITVLEKS-----DDGWWKGRLGR-GKEGLFPSNYV 55
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
887-1091 5.27e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 45.03  E-value: 5.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  887 ARRLHR--RLRVEYQRRLEAERMRLAE--EEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKKELLE 962
Cdd:COG3064    76 AKKLAEaeKAAAEAEKKAAAEKAKAAKeaEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAE 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  963 QMEKARHEPINHSDMVDKMFGFLGTSGSLPGQEGQAPSGFEDLERGRREMVEEDVDAALPLPDEDEEDLSEYKFAKFAAT 1042
Cdd:COG3064   156 AARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALA 235
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 755522197 1043 YFQGTTTHSYTRRPLKQPLLYHDDEGDQLAALAVWITILRFMGDLPEPK 1091
Cdd:COG3064   236 AVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAA 284
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
1394-1476 1.41e-03

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 40.72  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  1394 EDNVATNLIYQQVVRGVKFGEYRCEkEDDLAELASQQYFVDYGS------EMILERLLSLVPtyipdREITPLKNLEKWA 1467
Cdd:pfam00373    7 QDEVTRHLLYLQAKDDILEGRLPCS-EEEALLLAALQLQAEFGDyqpsshTSEYLSLESFLP-----KQLLRKMKSKELE 80

                   ....*....
gi 755522197  1468 QLAIAAHKK 1476
Cdd:pfam00373   81 KRVLEAHKN 89
growth_prot_Scy NF041483
polarized growth protein Scy;
901-970 1.55e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 44.05  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  901 RLEAERMR-----LAEEEKLRKEMSAKKAKEEAERKHQERLAQLARE------DAERELKEKEEA---------RRKKEL 960
Cdd:NF041483  530 RAEAERLRaeaeeQAEEVRAAAERAARELREETERAIAARQAEAAEEltrlhtEAEERLTAAEEAladaraeaeRIRREA 609
                          90
                  ....*....|
gi 755522197  961 LEQMEKARHE 970
Cdd:NF041483  610 AEETERLRTE 619
growth_prot_Scy NF041483
polarized growth protein Scy;
903-976 1.59e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 44.05  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  903 EAERMRlAEE-----------EKLRKEmsAKKAKEEAERKhQERLAQLAREDAERELKE--KEEARRKKELLEQMEKARH 969
Cdd:NF041483  969 EAERLR-AEAaetvgsaqqhaERIRTE--AERVKAEAAAE-AERLRTEAREEADRTLDEarKDANKRRSEAAEQADTLIT 1044

                  ....*..
gi 755522197  970 EPINHSD 976
Cdd:NF041483 1045 EAAAEAD 1051
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
803-822 2.99e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 36.91  E-value: 2.99e-03
                           10        20
                   ....*....|....*....|
gi 755522197   803 KSAATLIQRHWRGHHCRKNY 822
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRY 20
 
Name Accession Description Interval E-value
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
108-764 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: 1373.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQ 187
Cdd:cd01381     1 AGILRNLLIRYREKLIYT------YTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  188 CCIISGESGAGKTESTKLILQFLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKI 267
Cdd:cd01381    75 CVVISGESGAGKTESTKLILQYLAAISGQHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  268 EQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTD 347
Cdd:cd01381   155 EQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTD 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  348 TENWEISKLLAAILHMGNLQYEARTFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQAL 427
Cdd:cd01381   235 EEIWDIFKLLAAILHLGNIKFEATVVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQAL 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  428 DVRDAFVKGIYGRLFVWIVEKINAAIYKPPPLEvkNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHVFKL 507
Cdd:cd01381   315 DVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTD--SSRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKL 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  508 EQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANYVPPKNSHETQFGIN 587
Cdd:cd01381   393 EQEEYDKEGINWQHIEFVDNQDVLDLIALKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNTSFGIN 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  588 HFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAETRKRSPTLSSQFKRSLELLMRTLGACQPFF 667
Cdd:cd01381   473 HFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKSPTLSSQFRKSLDQLMKTLSACQPFF 552
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  668 VRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPGVKPAYKQGDLRGTCQrMAEAV 747
Cdd:cd01381   553 VRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTDCRAATRK-ICCAV 631
                         650
                  ....*....|....*..
gi 755522197  748 LGTHDDWQIGKTKIFLK 764
Cdd:cd01381   632 LGGDADYQLGKTKIFLK 648
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
89-776 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: 1024.79  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197     89 HPTSVHGVEDMIRLGDLNEAGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPH 168
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYT------YIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPH 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197    169 IFAIADNCYFNMKRNNRDQCCIISGESGAGKTESTKLILQFLAAISGQ---HSWIEQQVLEATPILEAFGNAKTIRNDNS 245
Cdd:smart00242   75 VFAIADNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSnteVGSVEDQILESNPILEAFGNAKTLRNNNS 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197    246 SRFGKYIDIHFNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCE 325
Cdd:smart00242  155 SRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVD 234
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197    326 GRVDSQEYANIRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFENlDACEVLFSPSLATAASLLEVNPPDLMSCL 405
Cdd:smart00242  235 GIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDN-AASTVKDKEELSNAAELLGVDPEELEKAL 313
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197    406 TSRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPpplevKNSRRSIGLLDIFGFENFTVNSFE 485
Cdd:smart00242  314 TKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFK-----DGSTYFIGVLDIYGFEIFEVNSFE 388
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197    486 QLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNS 565
Cdd:smart00242  389 QLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQ 468
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197    566 QHKLNANYVPPKNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQaDVAMGAETRKRSPTL 645
Cdd:smart00242  469 HHKKHPHFSKPKKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFP-SGVSNAGSKKRFQTV 547
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197    646 SSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLP 725
Cdd:smart00242  548 GSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLP 627
                           650       660       670       680       690
                    ....*....|....*....|....*....|....*....|....*....|.
gi 755522197    726 GVKPAyKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLKDHHDMLLEVERD 776
Cdd:smart00242  628 DTWPP-WGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
108-764 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: 903.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIG-EMPPHIFAIADNCYFNMKRNNRD 186
Cdd:cd00124     1 AAILHNLRERYARDLIYT------YVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  187 QCCIISGESGAGKTESTKLILQFLAAISGQH--------SWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNK 258
Cdd:cd00124    75 QSILISGESGAGKTETTKLVLKYLAALSGSGsskssssaSSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  259 RGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADY----NYLAMGNCITCEGRVDSQEYA 334
Cdd:cd00124   155 TGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYyylnDYLNSSGCDRIDGVDDAEEFQ 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  335 NIRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRG 414
Cdd:cd00124   235 ELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGG 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  415 ETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIyKPPPLEVKNSrrSIGLLDIFGFENFTVNSFEQLCINFANE 494
Cdd:cd00124   315 ETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAAL-SPTDAAESTS--FIGILDIFGFENFEVNSFEQLCINYANE 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  495 HLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANYV 574
Cdd:cd00124   392 KLQQFFNQHVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFF 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  575 PPKNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSsrnkfikqifqadvamgaetrkrsptlSSQFKRSLE 654
Cdd:cd00124   472 SKKRKAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRS---------------------------GSQFRSQLD 524
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  655 LLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPGVKPAYKQG 734
Cdd:cd00124   525 ALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEKASDS 604
                         650       660       670
                  ....*....|....*....|....*....|
gi 755522197  735 DLRgTCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd00124   605 KKA-AVLALLLLLKLDSSGYQLGKTKVFLR 633
Myosin_head pfam00063
Myosin head (motor domain);
96-764 0e+00

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 840.02  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197    96 VEDMIRLGDLNEAGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADN 175
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYT------YSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADE 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   176 CYFNMKRNNRDQCCIISGESGAGKTESTKLILQFLAAISGQHSW-----IEQQVLEATPILEAFGNAKTIRNDNSSRFGK 250
Cdd:pfam00063   75 AYRSMLQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAgnvgrLEEQILQSNPILEAFGNAKTVRNNNSSRFGK 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   251 YIDIHFNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCEGRVDS 330
Cdd:pfam00063  155 YIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDS 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   331 QEYANIRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARtfENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTL 410
Cdd:pfam00063  235 EEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKE--RNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRI 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   411 ITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPpplevKNSRRS-IGLLDIFGFENFTVNSFEQLCI 489
Cdd:pfam00063  313 KTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVK-----TIEKASfIGVLDIYGFEIFEKNSFEQLCI 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   490 NFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKL 569
Cdd:pfam00063  388 NYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPKATDQTFLDKLYSTFSK 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   570 NANYVPPKNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ------------ADVAMGAE 637
Cdd:pfam00063  468 HPHFQKPRLQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPdyetaesaaaneSGKSTPKR 547
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   638 TRKRSP-TLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEF 716
Cdd:pfam00063  548 TKKKRFiTVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEF 627
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*...
gi 755522197   717 VERYRVLLPGVKPAYKqGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:pfam00063  628 VQRYRILAPKTWPKWK-GDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
109-764 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: 826.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  109 GILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQC 188
Cdd:cd14883     2 GINTNLKVRYKKDLIYT------YTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  189 CIISGESGAGKTESTKLILQFLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIE 268
Cdd:cd14883    76 VIISGESGAGKTETTKLILQYLCAVTNNHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  269 QYLLEKSRVCRQAPDERNYHVFYCMLEG--MNEEEKKKLGLGQAADYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFT 346
Cdd:cd14883   156 DYLLEQSRITFQAPGERNYHVFYQLLAGakHSKELKEKLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  347 DTENWEISKLLAAILHMGNLQyeartFENLDACEVLFSPS----LATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLS 422
Cdd:cd14883   236 EEMQEGIFSVLSAILHLGNLT-----FEDIDGETGALTVEdkeiLKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLK 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  423 REQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPplevkNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVR 502
Cdd:cd14883   311 VQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQ-----KNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNH 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  503 HVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANYV-PPKNSHE 581
Cdd:cd14883   386 YVFKLEQEEYEKEGINWSHIVFTDNQECLDLIEKPPLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEkPDRRRWK 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  582 TQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIF--QADVA------------MGAETRKRSPTLSS 647
Cdd:cd14883   466 TEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtyPDLLAltglsislggdtTSRGTSKGKPTVGD 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  648 QFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPGV 727
Cdd:cd14883   546 TFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRA 625
                         650       660       670
                  ....*....|....*....|....*....|....*..
gi 755522197  728 KPAYKQGDlRGTCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd14883   626 RSADHKET-CGAVRALMGLGGLPEDEWQVGKTKVFLR 661
COG5022 COG5022
Myosin heavy chain [General function prediction only];
88-981 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 791.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   88 MHPTSVHGVEDMIRLGDLNEAGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPP 167
Cdd:COG5022    60 IKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYT------YSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEP 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  168 HIFAIADNCYFNMKRNNRDQCCIISGESGAGKTESTKLILQFLAAISGQHSW----IEQQVLEATPILEAFGNAKTIRND 243
Cdd:COG5022   134 HVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTVeissIEKQILATNPILEAFGNAKTVRND 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  244 NSSRFGKYIDIHFNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCIT 323
Cdd:COG5022   214 NSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDK 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  324 CEGRVDSQEYANIRSAMKVLMFTDTENWEISKLLAAILHMGNLQY-EARTfenlDACEVLFSPSLATAASLLEVNPPDLM 402
Cdd:COG5022   294 IDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFkEDRN----GAAIFSDNSVLDKACYLLGIDPSLFV 369
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  403 SCLTSRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPplEVKNsrrSIGLLDIFGFENFTVN 482
Cdd:COG5022   370 KWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSA--AASN---FIGVLDIYGFEIFEKN 444
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  483 SFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMI-ANRPMNVISLIDEESKFPKGTDATMLH 561
Cdd:COG5022   445 SFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIeKKNPLGILSLLDEECVMPHATDESFTS 524
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  562 KLNSQHKLNAN--YVPPKNShETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFqaDVAMGAETR 639
Cdd:COG5022   525 KLAQRLNKNSNpkFKKSRFR-DNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLF--DDEENIESK 601
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  640 KRSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVER 719
Cdd:COG5022   602 GRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQR 681
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  720 YRVLLPGVKPAY---KQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLKDHHDMLLEVERDKAITDRVILLQKVIRGFKDR 796
Cdd:COG5022   682 YRILSPSKSWTGeytWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLR 761
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  797 SNFLR-LKS--AATLIQRHWRgHHCRKNYELIRLGFLRLQALHRSRKLHKQYRLARQRIIEFQARCRAYLVRK-----AF 868
Cdd:COG5022   762 RRYLQaLKRikKIQVIQHGFR-LRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLReteevEF 840
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  869 RHRlwAVITVQAYARGMIARRLHRRL-----RVEYQRRLEAERMRLAEEEKLRKEMSAKKAK------------------ 925
Cdd:COG5022   841 SLK--AEVLIQKFGRSLKAKKRFSLLkketiYLQSAQRVELAERQLQELKIDVKSISSLKLVnleleseiielkkslssd 918
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755522197  926 EEAERKHQ-ERLAQLAREDAEREL-----KEKEEARRKKELLEQMEKARHEPINHSDMVDKM 981
Cdd:COG5022   919 LIENLEFKtELIARLKKLLNNIDLeegpsIEYVKLPELNKLHEVESKLKETSEEYEDLLKKS 980
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
110-764 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: 770.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  110 ILRNLLIRY-RDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQC 188
Cdd:cd01380     3 VLHNLKVRFcQRNAIYT------YCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  189 CIISGESGAGKTESTKLILQFLAAISGQHSW---IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGA 265
Cdd:cd01380    77 IIVSGESGAGKTVSAKYAMRYFATVGGSSSGetqVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  266 KIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMF 345
Cdd:cd01380   157 NMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  346 TDTENWEISKLLAAILHMGNLQYEARtfENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQ 425
Cdd:cd01380   237 SEEEQMEIFRILAAILHLGNVEIKAT--RNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQ 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  426 ALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPPLEVKNsrrSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHVF 505
Cdd:cd01380   315 AIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQHS---FIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVF 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  506 KLEQEEYDLESIDWLHIEFTDNQEALDMIANRpMNVISLIDEESKFPKGTDATMLHKLNSQH--KLNANYVPPKNShETQ 583
Cdd:cd01380   392 KLEQEEYVKEEIEWSFIDFYDNQPCIDLIEGK-LGILDLLDEECRLPKGSDENWAQKLYNQHlkKPNKHFKKPRFS-NTA 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  584 FGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNkfikqifqadvamgaetrkRSPTLSSQFKRSLELLMRTLGAC 663
Cdd:cd01380   470 FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKN-------------------RKKTVGSQFRDSLILLMETLNST 530
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  664 QPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPGVKPayKQGDLRGTCQRM 743
Cdd:cd01380   531 TPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEW--LRDDKKKTCENI 608
                         650       660
                  ....*....|....*....|.
gi 755522197  744 AEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd01380   609 LENLILDPDKYQFGKTKIFFR 629
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
110-764 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: 743.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  110 ILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQCC 189
Cdd:cd01378     3 INENLKKRFENDEIYT------YIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  190 IISGESGAGKTESTKLILQFLAAISGQHSW----IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGA 265
Cdd:cd01378    77 IISGESGAGKTEASKRIMQYIAAVSGGSESeverVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  266 KIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMF 345
Cdd:cd01378   157 HITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGF 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  346 TDTENWEISKLLAAILHMGNLQYEartfENLDACEVLFSPS-LATAASLLEVNPPDLMSCLTSRTLITRGE---TVSTPL 421
Cdd:cd01378   237 TEEEQDSIFRILAAILHLGNIQFA----EDEEGNAAISDTSvLDFVAYLLGVDPDQLEKALTHRTIETGGGgrsVYEVPL 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  422 SREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPPlevkNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFV 501
Cdd:cd01378   313 NVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSG----GKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFI 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  502 RHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFP-KGTDATMLHKLNSQHKLNANYVPPKNSH 580
Cdd:cd01378   389 ELTLKAEQEEYVREGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGHF 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  581 E---TQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAmgAETRKRSPTLSSQFKRSLELLM 657
Cdd:cd01378   469 ElrrGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD--LDSKKRPPTAGTKFKNSANALV 546
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  658 RTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPGVKPAYkqgdlR 737
Cdd:cd01378   547 ETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAW-----D 621
                         650       660       670
                  ....*....|....*....|....*....|.
gi 755522197  738 GTCQRMAEAVLGTH----DDWQIGKTKIFLK 764
Cdd:cd01378   622 GTWQGGVESILKDLnippEEYQMGKTKIFIR 652
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
108-764 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: 734.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLS-IYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRD 186
Cdd:cd14873     1 GSIMYNLFQRYKRNQIYT------YIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  187 QCCIISGESGAGKTESTKLILQFLAAISGQ---------HSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFN 257
Cdd:cd14873    75 QCILISGESGAGKTESTKLILKFLSVISQQslelslkekTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNIC 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  258 KRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCEGRVDSQEYANIR 337
Cdd:cd14873   155 QKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVI 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  338 SAMKVLMFTDTENWEISKLLAAILHMGNLQyeartFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETV 417
Cdd:cd14873   235 TAMEVMQFSKEEVREVSRLLAGILHLGNIE-----FITAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEI 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  418 STPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKppplevKNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQ 497
Cdd:cd14873   310 LTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKG------KEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQ 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  498 QFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIaNRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANYVPPK 577
Cdd:cd14873   384 EYFNKHIFSLEQLEYSREGLVWEDIDWIDNGECLDLI-EKKLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPR 462
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  578 NShETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVA------MGAETRKRSPTLSSQFKR 651
Cdd:cd14873   463 VA-VNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSrnnqdtLKCGSKHRRPTVSSQFKD 541
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  652 SLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPGVKPAY 731
Cdd:cd14873   542 SLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPE 621
                         650       660       670
                  ....*....|....*....|....*....|...
gi 755522197  732 kqgDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd14873   622 ---DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
108-764 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: 719.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQ 187
Cdd:cd01387     1 TTVLWNLKTRYERNLIYT------YIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  188 CCIISGESGAGKTESTKLILQFLAAIS-GQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFnKRGAIEGAK 266
Cdd:cd01387    75 CVVISGESGSGKTEATKLIMQYLAAVNqRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  267 IEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFT 346
Cdd:cd01387   154 TSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  347 DTENWEISKLLAAILHMGNLQYEARTFEN-LDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQ 425
Cdd:cd01387   234 SEEQDSIFRILASVLHLGNVYFHKRQLRHgQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQ 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  426 ALDVRDAFVKGIYGRLFVWIVEKINAAIYKPpplevKNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHVF 505
Cdd:cd01387   314 ALDARDAIAKALYALLFSWLVTRVNAIVYSG-----TQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVF 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  506 KLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANYVPPKNShETQFG 585
Cdd:cd01387   389 KLEQEEYIREQIDWTEIAFADNQPVINLISKKPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRMP-LPEFT 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  586 INHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIF-----QADVAM--GAE----TRK-RSPTLSSQFKRSL 653
Cdd:cd01387   468 IKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFsshraQTDKAPprLGKgrfvTMKpRTPTVAARFQDSL 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  654 ELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPGVKPAYKQ 733
Cdd:cd01387   548 LQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPRPAP 627
                         650       660       670
                  ....*....|....*....|....*....|..
gi 755522197  734 GDLRGTC-QRMAEAVlgTHDDWQIGKTKIFLK 764
Cdd:cd01387   628 GDMCVSLlSRLCTVT--PKDMYRLGATKVFLR 657
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
108-764 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: 709.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQ 187
Cdd:cd01377     1 ASVLHNLRERYYSDLIYT------YSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  188 CCIISGESGAGKTESTKLILQFLAAISGQHSW----------IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFN 257
Cdd:cd01377    75 SILITGESGAGKTENTKKVIQYLASVAASSKKkkesgkkkgtLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  258 KRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCEGRVDSQEYANIR 337
Cdd:cd01377   155 STGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTD 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  338 SAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTfeNLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETV 417
Cdd:cd01377   235 EAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRR--REEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWV 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  418 STPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAiykpppLEVKNSRRS-IGLLDIFGFENFTVNSFEQLCINFANEHL 496
Cdd:cd01377   313 TKGQNKEQVVFSVGALAKALYERLFLWLVKRINKT------LDTKSKRQYfIGVLDIAGFEIFEFNSFEQLCINYTNEKL 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  497 QQFFVRHVFKLEQEEYDLESIDWLHIEF-TDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQH--KLNANY 573
Cdd:cd01377   387 QQFFNHHMFVLEQEEYKKEGIEWTFIDFgLDLQPTIDLIEKPNMGILSILDEECVFPKATDKTFVEKLYSNHlgKSKNFK 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  574 VPPKNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAM---GAETRKRSP---TLSS 647
Cdd:cd01377   467 KPKPKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESgggGGKKKKKGGsfrTVSQ 546
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  648 QFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPGV 727
Cdd:cd01377   547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
                         650       660       670
                  ....*....|....*....|....*....|....*..
gi 755522197  728 KPAYkQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd01377   627 IPKG-FDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
110-764 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: 709.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  110 ILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQCC 189
Cdd:cd01385     3 LLENLRARFKHGKIYT------YVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  190 IISGESGAGKTESTKLILQFLAAIS--GQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKI 267
Cdd:cd01385    77 VISGESGSGKTESTNFLLHHLTALSqkGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  268 EQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTD 347
Cdd:cd01385   157 EKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLP 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  348 TENWEISKLLAAILHMGNLQYEARTFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQAL 427
Cdd:cd01385   237 ETQRQIFSVLSAVLHLGNIEYKKKAYHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAI 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  428 DVRDAFVKGIYGRLFVWIVEKINAAIYKPPPLEvKNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHVFKL 507
Cdd:cd01385   317 ATRDAMAKCLYSALFDWIVLRINHALLNKKDLE-EAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKL 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  508 EQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANY-VPPKNshETQFGI 586
Cdd:cd01385   396 EQEEYKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYeKPQVM--EPAFII 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  587 NHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQAD-VAM-------------------GAETR------- 639
Cdd:cd01385   474 AHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDpVAVfrwavlrafframaafreaGRRRAqrtaghs 553
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  640 -----------------KRSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRI 702
Cdd:cd01385   554 ltlhdrttksllhlhkkKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRI 633
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755522197  703 RHAGYPIRYSFVEFVERYRVLLPGVKPAYKQgdlrgTCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd01385   634 RRSGYSVRYTFQEFITQFQVLLPKGLISSKE-----DIKDFLEKLNLDRDNYQIGKTKVFLK 690
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
108-764 0e+00

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


Pssm-ID: 276835  Cd Length: 647  Bit Score: 697.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLS-IYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRD 186
Cdd:cd01384     1 PGVLHNLKVRYELDEIYT------YTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  187 QCCIISGESGAGKTESTKLILQFLAAISGQHSW----IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAI 262
Cdd:cd01384    75 QSILVSGESGAGKTETTKMLMQYLAYMGGRAVTegrsVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  263 EGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCEGRVDSQEYANIRSAMKV 342
Cdd:cd01384   155 SGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDV 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  343 LMFTDTENWEISKLLAAILHMGNLQYEARtfENLDACEVLFSPS---LATAASLLEVNPPDLMSCLTSRTLITRGETVST 419
Cdd:cd01384   235 VGISEEEQDAIFRVVAAILHLGNIEFSKG--EEDDSSVPKDEKSefhLKAAAELLMCDEKALEDALCKRVIVTPDGIITK 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  420 PLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPplevkNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQF 499
Cdd:cd01384   313 PLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDP-----NSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQH 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  500 FVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANYVPPKNS 579
Cdd:cd01384   388 FNQHVFKMEQEEYTKEEIDWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPKLS 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  580 hETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAETRKRSPTLSSQFKRSLELLMRT 659
Cdd:cd01384   468 -RTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREGTSSSSKFSSIGSRFKQQLQELMET 546
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  660 LGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPGVKPAY--KQGDLR 737
Cdd:cd01384   547 LNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVLKGSddEKAACK 626
                         650       660
                  ....*....|....*....|....*..
gi 755522197  738 GTCQRMAEavlgthDDWQIGKTKIFLK 764
Cdd:cd01384   627 KILEKAGL------KGYQIGKTKVFLR 647
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
110-764 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: 694.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  110 ILRNLLIRYRDHLIYTScggrtyTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGemPPHIFAIADNCYFNMKRNNRDQCC 189
Cdd:cd01383     3 VLHNLEYRYSQDIIYTK------AGPVLIAVNPFKDVPLYGNEFITAYRQKLLD--SPHVYAVADTAYREMMRDEINQSI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  190 IISGESGAGKTESTKLILQFLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQ 269
Cdd:cd01383    75 IISGESGAGKTETAKIAMQYLAALGGGSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  270 YLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTDTE 349
Cdd:cd01383   155 YLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKED 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  350 NWEISKLLAAILHMGNLqyearTFENLDAC---EVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQA 426
Cdd:cd01383   235 QEHIFQMLAAVLWLGNI-----SFQVIDNEnhvEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQA 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  427 LDVRDAFVKGIYGRLFVWIVEKINAAiykpppLEVKNSR--RSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHV 504
Cdd:cd01383   310 IDARDALAKAIYASLFDWLVEQINKS------LEVGKRRtgRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  505 FKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANYvppKNSHETQF 584
Cdd:cd01383   384 FKLEQEEYELDGIDWTKVDFEDNQECLDLIEKKPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCF---KGERGGAF 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  585 GINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNK----FIKQIFQADVAMGAETRKRSP-----TLSSQFKRSLEL 655
Cdd:cd01383   461 TIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQlpqlFASKMLDASRKALPLTKASGSdsqkqSVATKFKGQLFK 540
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  656 LMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPgvKPAYKQGD 735
Cdd:cd01383   541 LMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLP--EDVSASQD 618
                         650       660       670
                  ....*....|....*....|....*....|...
gi 755522197  736 LRGTCQrmaeAVLGTHDD----WQIGKTKIFLK 764
Cdd:cd01383   619 PLSTSV----AILQQFNIlpemYQVGYTKLFFR 647
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
110-764 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: 686.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  110 ILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQCC 189
Cdd:cd01379     3 IVSQLQKRYSRDQIYT------YIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  190 IISGESGAGKTESTKLILQFLAAIS-GQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIE 268
Cdd:cd01379    77 VISGESGAGKTESANLLVQQLTVLGkANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARIS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  269 QYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEK-KKLGLGQAADYNYLAMGNCITCEGRVDS---QEYANIRSAMKVLM 344
Cdd:cd01379   157 EYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDIVNNSgnrEKFEEIEQCFKVIG 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  345 FTDTENWEISKLLAAILHMGNLQYE--ARTFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLS 422
Cdd:cd01379   237 FTKEEVDSVYSILAAILHIGDIEFTevESNHQTDKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNT 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  423 REQALDVRDAFVKGIYGRLFVWIVEKINAAIyKPPPlEVKNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVR 502
Cdd:cd01379   317 VEEATDARDAMAKALYGRLFSWIVNRINSLL-KPDR-SASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQ 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  503 HVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKL--NSQHKlnaNYVPPKnSH 580
Cdd:cd01379   395 HIFAWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKPMGLLALLDEESRFPKATDQTLVEKFhnNIKSK---YYWRPK-SN 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  581 ETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQifqadvamgaetrkrspTLSSQFKRSLELLMRTL 660
Cdd:cd01379   471 ALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ-----------------TVATYFRYSLMDLLSKM 533
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  661 GACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLlpgvkpAYKQGDL---- 736
Cdd:cd01379   534 VVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFL------AFKWNEEvvan 607
                         650       660
                  ....*....|....*....|....*...
gi 755522197  737 RGTCQRMAEAvLGThDDWQIGKTKIFLK 764
Cdd:cd01379   608 RENCRLILER-LKL-DNWALGKTKVFLK 633
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
108-761 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: 642.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTScggrtyTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQ 187
Cdd:cd14872     1 AMIVHNLRKRFKNDQIYTN------VGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  188 CCIISGESGAGKTESTKLILQFLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKI 267
Cdd:cd14872    75 SILISGESGAGKTEATKQCLSFFAEVAGSTNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGAST 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  268 EQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLgqAADYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTD 347
Cdd:cd14872   155 ENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGS--SAAYGYLSLSGCIEVEGVDDVADFEEVVLAMEQLGFDD 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  348 TENWEISKLLAAILHMGNLQYEARTFENL-DACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRG-ETVSTPLSREQ 425
Cdd:cd14872   233 ADINNVMSLIAAILKLGNIEFASGGGKSLvSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIKGcDPTRIPLTPAQ 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  426 ALDVRDAFVKGIYGRLFVWIVEKINAAIyKPPPLEVKnsrRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHVF 505
Cdd:cd14872   313 ATDACDALAKAAYSRLFDWLVKKINESM-RPQKGAKT---TFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTF 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  506 KLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANYVP-PKNSHETQF 584
Cdd:cd14872   389 KLEEALYQSEGVKFEHIDFIDNQPVLDLIEKKQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYaEVRTSRTEF 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  585 GINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQadVAMGAETRKRsPTLSSQFKRSLELLMRTLGACQ 664
Cdd:cd14872   469 IVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFP--PSEGDQKTSK-VTLGGQFRKQLSALMTALNATE 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  665 PFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPGVKPAYKQgDLRGTCQRMA 744
Cdd:cd14872   546 PHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVKTIAKRVGP-DDRQRCDLLL 624
                         650
                  ....*....|....*..
gi 755522197  745 EAVLGTHDDWQIGKTKI 761
Cdd:cd14872   625 KSLKQDFSKVQVGKTRV 641
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
108-764 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: 619.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQ-LLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKR---- 182
Cdd:cd14890     1 ASLLHTLRLRYERDEIYT------YVGPILISINPYKsIPDLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvl 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  183 NNRDQCCIISGESGAGKTESTKLILQFLAAISGQHSWI-------------------EQQVLEATPILEAFGNAKTIRND 243
Cdd:cd14890    75 DPSNQSIIISGESGAGKTEATKIIMQYLARITSGFAQGasgegeaaseaieqtlgslEDRVLSSNPLLESFGNAKTLRND 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  244 NSSRFGKYIDIHFNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLaMGNCIT 323
Cdd:cd14890   155 NSSRFGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYL-RGECSS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  324 CEGRVDSQEYANIRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFENLDACEVLFsPSLATAASLLEVNPPDLMS 403
Cdd:cd14890   234 IPSCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTL-QSLKLAAELLGVNEDALEK 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  404 CLTSRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPpplevknSRR--SIGLLDIFGFENFTV 481
Cdd:cd14890   313 ALLTRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSP-------DDKwgFIGVLDIYGFEKFEW 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  482 NSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRP---MNVISLIDEESKFpKGTDA- 557
Cdd:cd14890   386 NTFEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVngkPGIFITLDDCWRF-KGEEAn 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  558 ----TMLHKL-------------NSQHklnANYVPPKNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSR 620
Cdd:cd14890   465 kkfvSQLHASfgrksgsggtrrgSSQH---PHFVHPKFDADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR 541
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  621 NKFikqifqadvamgaetrkRSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETI 700
Cdd:cd14890   542 RSI-----------------REVSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAI 604
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755522197  701 RIRHAGYPIRYSFVEFVERYRVLLPgvkpaykqgDLRGTCQRMAE--AVLG-THDDWQIGKTKIFLK 764
Cdd:cd14890   605 QIRQQGFALREEHDSFFYDFQVLLP---------TAENIEQLVAVlsKMLGlGKADWQIGSSKIFLK 662
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
108-764 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: 616.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPY-QLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRD 186
Cdd:cd01382     1 ATLLNNIRVRYSKDKIYT------YVANILIAVNPYfDIPKLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  187 QCCIISGESGAGKTESTKLILQFLAAISGQHSW-IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGA 265
Cdd:cd01382    75 QSIIVSGESGAGKTESTKYILRYLTESWGSGAGpIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  266 KIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADynylamgncitcegrvDSQEYANIRSAMKVLMF 345
Cdd:cd01382   155 FVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPLLD----------------DVGDFIRMDKAMKKIGL 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  346 TDTENWEISKLLAAILHMGNLQYEARTFENLDACEVLFS--PSLATAASLLEVNPPDLMSCLTSR-TLITRGETVST--- 419
Cdd:cd01382   219 SDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGGCNVKPKseQSLEYAAELLGLDQDELRVSLTTRvMQTTRGGAKGTvik 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  420 -PLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIykppPLEvkNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQ 498
Cdd:cd01382   299 vPLKVEEANNARDALAKAIYSKLFDHIVNRINQCI----PFE--TSSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQ 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  499 FFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANYVPPKN 578
Cdd:cd01382   373 FFNERILKEEQELYEKEGLGVKEVEYVDNQDCIDLIEAKLVGILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSIPRK 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  579 S----HET-----QFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAETRKRSPTLS--- 646
Cdd:cd01382   453 SklkiHRNlrddeGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNKDSKQKAGKLSfis 532
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  647 --SQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLL 724
Cdd:cd01382   533 vgNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYL 612
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|
gi 755522197  725 PgvkPAYKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd01382   613 P---PKLARLDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
110-764 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: 612.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  110 ILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEM-PPHIFAIADNCYFNMKRNNRDQC 188
Cdd:cd14897     3 IVQTLKSRYNKDKFYT------YIGDILVAVNPCKPLPIFDKKHHEEYSNLSVRSQrPPHLFWIADQAYRRLLETGRNQC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  189 CIISGESGAGKTESTKLILQFLAAISG-QHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKI 267
Cdd:cd14897    77 ILVSGESGAGKTESTKYMIKHLMKLSPsDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  268 EQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNcITCEGRVDSQEYANIRSA-------M 340
Cdd:cd14897   157 DDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDN-RNRPVFNDSEELEYYRQMfhdltniM 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  341 KVLMFTDTENWEISKLLAAILHMGNLQYEartfENLDACEVLFSPS--LATAASLLEVNPPDLMSCLTSRTLITRGETVS 418
Cdd:cd14897   236 KLIGFSEEDISVIFTILAAILHLTNIVFI----PDEDTDGVTVADEypLHAVAKLLGIDEVELTEALISNVNTIRGERIQ 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  419 TPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPPLEVKNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQ 498
Cdd:cd14897   312 SWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQ 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  499 FFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANYVPPKN 578
Cdd:cd14897   392 YFNDYVFPRERSEYEIEGIEWRDIEYHDNDDVLELFFKKPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVASPG 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  579 SHeTQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFqadvamgaetrkrsptlSSQFKRSLELLMR 658
Cdd:cd14897   472 NR-VAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF-----------------TSYFKRSLSDLMT 533
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  659 TLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPGVKPAY--KQGDL 736
Cdd:cd14897   534 KLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFSNKVRsdDLGKC 613
                         650       660
                  ....*....|....*....|....*....
gi 755522197  737 RGTCQ-RMAEavlgthdDWQIGKTKIFLK 764
Cdd:cd14897   614 QKILKtAGIK-------GYQFGKTKVFLK 635
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
108-764 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: 595.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLL-SIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRD 186
Cdd:cd14903     1 AAILYNVKKRFLRKLPYT------YTGDICIAVNPYQWLpELYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  187 QCCIISGESGAGKTESTKLILQFLAAI-SGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGA 265
Cdd:cd14903    75 QSILVSGESGAGKTETTKILMNHLATIaGGLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  266 KIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEkkKLGLGQAADYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMF 345
Cdd:cd14903   155 KCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEE--RLFLDSANECAYTGANKTIKIEGMSDRKHFARTKEALSLIGV 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  346 TDTENWEISKLLAAILHMGNLQYEARTFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQ 425
Cdd:cd14903   233 SEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQ 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  426 ALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPplevkNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHVF 505
Cdd:cd14903   313 AEDCRDALAKAIYSNVFDWLVATINASLGNDA-----KMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVF 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  506 KLEQEEYDLESIDWLHIEFTDNQEALDMIANRpMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANYVP-PKNShETQF 584
Cdd:cd14903   388 KTVQIEYEEEGIRWAHIDFADNQDVLAVIEDR-LGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEfPRTS-RTQF 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  585 GINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAET---------RKRSPTLS-----SQFK 650
Cdd:cd14903   466 TIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAAstslargarRRRGGALTtttvgTQFK 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  651 RSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPG---- 726
Cdd:cd14903   546 DSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEgrnt 625
                         650       660       670
                  ....*....|....*....|....*....|....*....
gi 755522197  727 -VKPAYKQGDLrgtcqrMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd14903   626 dVPVAERCEAL------MKKLKLESPEQYQMGLTRIYFQ 658
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
108-764 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: 593.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLL-SIYSPEHIRQYTnKKIGEMPPHIFAIADNCYFNMKRNNRD 186
Cdd:cd14888     1 ASILHSLNLRFDIDEIYT------FTGPILIAVNPFKTIpGLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  187 QCCIISGESGAGKTESTKLILQFLA-AISG---QHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNK---- 258
Cdd:cd14888    74 QTILISGESGAGKTESTKYVMKFLAcAGSEdikKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKlksk 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  259 -----RGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCML---------EGMNEEEKKKLGLGQAAD------------ 312
Cdd:cd14888   154 rmsgdRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCaaareakntGLSYEENDEKLAKGADAKpisidmssfeph 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  313 --YNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTDTENWEISKLLAAILHMGNLQyeartFENLDAC------EVLFS 384
Cdd:cd14888   234 lkFRYLTKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNIL-----FENNEACsegavvSASCT 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  385 PSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAI-YKPpplevKN 463
Cdd:cd14888   309 DDLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIgYSK-----DN 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  464 SRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVIS 543
Cdd:cd14888   384 SLLFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKPLGIFC 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  544 LIDEESKFPKGTDATMLHKLNSQHKLNANYVPPKnSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKF 623
Cdd:cd14888   464 MLDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVK-TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPF 542
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  624 IKQIFQADVAMGAE---TRKRSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETI 700
Cdd:cd14888   543 ISNLFSAYLRRGTDgntKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAV 622
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755522197  701 RIRHAGYPIRYSFVEFVERYRVLLPgvkpayKQGDLrgtcqrmaeavlgTHDDWQIGKTKIFLK 764
Cdd:cd14888   623 QVSRAGYPVRLSHAEFYNDYRILLN------GEGKK-------------QLSIWAVGKTLCFFK 667
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
110-764 0e+00

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


Pssm-ID: 276854  Cd Length: 659  Bit Score: 591.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  110 ILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNM----KRNNR 185
Cdd:cd14889     3 LLEVLKVRFMQSNIYT------YVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMlgrlARGPK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  186 DQCCIISGESGAGKTESTKLILQFLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFnKRGAIEGA 265
Cdd:cd14889    77 NQCIVISGESGAGKTESTKLLLRQIMELCRGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  266 KIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGncITCEGRVDS--QEYANIRSAMKVL 343
Cdd:cd14889   156 KINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNG--AGCKREVQYwkKKYDEVCNAMDMV 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  344 MFTDTENWEISKLLAAILHMGNLQYEARTFENLDACEVLFSPsLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSR 423
Cdd:cd14889   234 GFTEQEEVDMFTILAGILSLGNITFEMDDDEALKVENDSNGW-LKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTK 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  424 EQALDVRDAFVKGIYGRLFVWIVEKINAAIykPPPLEVKNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRH 503
Cdd:cd14889   313 QQAEDARDSIAKVAYGRVFGWIVSKINQLL--APKDDSSVELREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHH 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  504 VFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANYVPPKNsHETQ 583
Cdd:cd14889   391 IFLMEQKEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYYGKSRS-KSPK 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  584 FGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAM---------------GAETRKRSPTLSSQ 648
Cdd:cd14889   470 FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRtgtlmpraklpqagsDNFNSTRKQSVGAQ 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  649 FKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLpgVK 728
Cdd:cd14889   550 FKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILL--CE 627
                         650       660       670
                  ....*....|....*....|....*....|....*...
gi 755522197  729 PaykqgDLRGTCQRMAeAVLGTHD--DWQIGKTKIFLK 764
Cdd:cd14889   628 P-----ALPGTKQSCL-RILKATKlvGWKCGKTRLFFK 659
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
108-764 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: 579.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQllSI---YS-PEHIRQYTNKKIGEM-PPHIFAIADNCYFNMKR 182
Cdd:cd14892     1 APLLDVLRRRYERDAIYT------FTADILISINPYK--SIpllYDvPGFDSQRKEEATASSpPPHVFSIAERAYRAMKG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  183 ----NNRDQCCIISGESGAGKTESTKLILQFLAAIS-------------GQHSWIEQQVLEATPILEAFGNAKTIRNDNS 245
Cdd:cd14892    73 vgkgQGTPQSIVVSGESGAGKTEASKYIMKYLATASklakgastskgaaNAHESIEECVLLSNLILEAFGNAKTIRNDNS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  246 SRFGKYIDIHFNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCE 325
Cdd:cd14892   153 SRFGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVD 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  326 GRVDSQEYANIRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFENLDACEVLFSPSLATAASLLEVNPPDLMSCL 405
Cdd:cd14892   233 GVDDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNVAKAAGLLGVDAAELMFKL 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  406 TSRTLIT-RGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAA-----IYKPPPLEVKNSRRSIGLLDIFGFENF 479
Cdd:cd14892   313 VTQTTSTaRGSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINAChkqqtSGVTGGAASPTFSPFIGILDIFGFEIM 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  480 TVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFP-KGTDAT 558
Cdd:cd14892   393 PTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKPLGLLPLLEEQMLLKrKTTDKQ 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  559 MLHKLNSQH-KLNANYVPPKNSHEtQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRnkfikqifqadvamgae 637
Cdd:cd14892   473 LLTIYHQTHlDKHPHYAKPRFECD-EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS----------------- 534
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  638 trkrsptlssQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFV 717
Cdd:cd14892   535 ----------KFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFY 604
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755522197  718 ERYRVLL-PGVKPAYKQGDLRGTCQR-MAEAVLGTH---DDWQIGKTKIFLK 764
Cdd:cd14892   605 EKFWPLArNKAGVAASPDACDATTARkKCEEIVARAlerENFQLGRTKVFLR 656
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
108-763 1.95e-179

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: 563.26  E-value: 1.95e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTScggrtyTGSILVAVNPYQLLSIYSPEHIRQY----TNKKIG--EMPPHIFAIADNCYFNMK 181
Cdd:cd14901     1 PSILHVLRRRFAHGLIYTS------TGAILVAINPFRRLPLYDDETKEAYyehgERRAAGerKLPPHVYAVADKAFRAML 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  182 RNNR----DQCCIISGESGAGKTESTKLILQFLAAIS---------GQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRF 248
Cdd:cd14901    75 FASRgqkcDQSILVSGESGAGKTETTKIIMNYLASVSsatthgqnaTERENVRDRVLESNPILEAFGNARTNRNNNSSRF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  249 GKYIDIHFNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNC-ITCEGR 327
Cdd:cd14901   155 GKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCyDRRDGV 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  328 VDSQEYANIRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFENlDACEVLFSPSLATAASLLEVNPPDLMSCLTS 407
Cdd:cd14901   235 DDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEG-GTFSMSSLANVRAACDLLGLDMDVLEKTLCT 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  408 RTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAI-YKPPplevKNSRRSIGLLDIFGFENFTVNSFEQ 486
Cdd:cd14901   314 REIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIaYSES----TGASRFIGIVDIFGFEIFATNSLEQ 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  487 LCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQ 566
Cdd:cd14901   390 LCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARPTGLFSLLDEQCLLPRGNDEKLANKYYDL 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  567 HKLNANYVPPK-NSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIkqifqadvamgaetrkrSPTL 645
Cdd:cd14901   470 LAKHASFSVSKlQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFL-----------------SSTV 532
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  646 SSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLP 725
Cdd:cd14901   533 VAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAP 612
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....
gi 755522197  726 GVkpAYKQGDLRGTCQRMA------EAVLGTHDDWQIGKTKIFL 763
Cdd:cd14901   613 DG--ASDTWKVNELAERLMsqlqhsELNIEHLPPFQVGKTKVFL 654
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
108-764 8.45e-179

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: 561.96  E-value: 8.45e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLS-IYSPEHIRQYTNK--------KIGEMPPHIFAIADNCYF 178
Cdd:cd14907     1 AELLINLKKRYQQDKIFT------YVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  179 NMKRNNRDQCCIISGESGAGKTESTKLILQFLAAISGQHSW--------------------IEQQVLEATPILEAFGNAK 238
Cdd:cd14907    75 QLFENNKKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNseevltltssiratskstksIEQKILSCNPILEAFGNAK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  239 TIRNDNSSRFGKYIDIHFNKR-GAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGL---GQAADYN 314
Cdd:cd14907   155 TVRNDNSSRFGKYVSILVDKKkRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLknqLSGDRYD 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  315 YLAMGNCITCEGRVDSQEYANIRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFENLDACEVLFSPSLATAASLL 394
Cdd:cd14907   235 YLKKSNCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSPCCVKNKETLQIIAKLL 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  395 EVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYkpPPLEVK-----NSRRSIG 469
Cdd:cd14907   315 GIDEEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIM--PKDEKDqqlfqNKYLSIG 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  470 LLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESI-DWL-HIEFTDNQEALDMIANRPMNVISLIDE 547
Cdd:cd14907   393 LLDIFGFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLeDYLnQLSYTDNQDVIDLLDKPPIGIFNLLDD 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  548 ESKFPKGTDATMLHKLNSQHKLNANYVPPKNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQI 627
Cdd:cd14907   473 SCKLATGTDEKLLNKIKKQHKNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSI 552
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  628 FQAD-------VAMGAETRKRSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETI 700
Cdd:cd14907   553 FSGEdgsqqqnQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESI 632
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755522197  701 RIRHAGYPIRYSFVEFVERYRVLLpgvkpaykqgdlrgtcqrmaEAVLgthddwqIGKTKIFLK 764
Cdd:cd14907   633 RVRKQGYPYRKSYEDFYKQYSLLK--------------------KNVL-------FGKTKIFMK 669
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
110-764 2.47e-167

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: 529.35  E-value: 2.47e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  110 ILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQCC 189
Cdd:cd14896     3 VLLCLKKRFHLGRIYT------FGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  190 IISGESGAGKTESTKLILQFLAAI-SGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFnKRGAIEGAKIE 268
Cdd:cd14896    77 LLSGHSGSGKTEAAKKIVQFLSSLyQDQTEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  269 QYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTDT 348
Cdd:cd14896   156 HYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  349 ENWEISKLLAAILHMGNLQYEARTFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALD 428
Cdd:cd14896   236 ELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAID 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  429 VRDAFVKGIYGRLFVWIVEKINAAIYKPPPLEvknSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHVFKLE 508
Cdd:cd14896   316 ARDALAKTLYSRLFTWLLKRINAWLAPPGEAE---SDATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQE 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  509 QEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANYVPPKNSHETqFGINH 588
Cdd:cd14896   393 EEECQRELLPWVPIPQPPRESCLDLLVDQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQLPLPV-FTVRH 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  589 FAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ-ADVAMGAETRKrsPTLSSQFKRSLELLMRTLGACQPFF 667
Cdd:cd14896   472 YAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQeAEPQYGLGQGK--PTLASRFQQSLGDLTARLGRSHVYF 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  668 VRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPGVKPAYkqgDLRGTCQRMAEAV 747
Cdd:cd14896   550 IHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEAL---SDRERCGAILSQV 626
                         650
                  ....*....|....*...
gi 755522197  748 LGTHDD-WQIGKTKIFLK 764
Cdd:cd14896   627 LGAESPlYHLGATKVLLK 644
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
108-764 1.17e-159

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: 508.33  E-value: 1.17e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLL-SIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRD 186
Cdd:cd14904     1 PSILFNLKKRFAASKPYT------YTNDIVIALNPYKWIdNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  187 QCCIISGESGAGKTESTKLILQFLAAISG--QHSWIEQqVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEG 264
Cdd:cd14904    75 QSILVSGESGAGKTETTKIVMNHLASVAGgrKDKTIAK-VIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  265 AKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMG-NCITCEGRVDSQEYANIRSAMKVL 343
Cdd:cd14904   154 AKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSlAQMQIPGLDDAKLFASTQKSLSLI 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  344 MFTDTENWEISKLLAAILHMGNLQY-----EARTFENLDACEVLfSPSLATAASLLEvnppdlmSCLTSRTLITRGETVS 418
Cdd:cd14904   234 GLDNDAQRTLFKILSGVLHLGEVMFdksdeNGSRISNGSQLSQV-AKMLGLPTTRIE-------EALCNRSVVTRNESVT 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  419 TPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIykppplEVKNSRRS--IGLLDIFGFENFTVNSFEQLCINFANEHL 496
Cdd:cd14904   306 VPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAI------STDDDRIKgqIGVLDIFGFEDFAHNGFEQFCINYANEKL 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  497 QQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRpMNVISLIDEESKFPKGTDATMLHKL--NSQHKLNANYV 574
Cdd:cd14904   380 QQKFTTDVFKTVEEEYIREGLQWDHIEYQDNQGIVEVIDGK-MGIIALMNDHLRQPRGTEEALVNKIrtNHQTKKDNESI 458
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  575 PPKNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ-----ADVAMGAETRKRS--PTLSS 647
Cdd:cd14904   459 DFPKVKRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGsseapSETKEGKSGKGTKapKSLGS 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  648 QFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPgv 727
Cdd:cd14904   539 QFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFP-- 616
                         650       660       670
                  ....*....|....*....|....*....|....*....
gi 755522197  728 kPAYKQGDLRGTCQRMAEAVlGTHD--DWQIGKTKIFLK 764
Cdd:cd14904   617 -PSMHSKDVRRTCSVFMTAI-GRKSplEYQIGKSLIYFK 653
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
108-764 9.01e-156

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: 497.26  E-value: 9.01e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRdhliytSCGGRTYT--GSILVAVNPyqLLSIYSPeHIRQYTNKKIGEMPPHIFAIADNCYFNM---KR 182
Cdd:cd14891     1 AGILHNLEERSK------LDNQRPYTfmANVLIAVNP--LRRLPEP-DKSDYINTPLDPCPPHPYAIAEMAYQQMclgSG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  183 NNRDQCCIISGESGAGKTESTKLILQFL-------AAISGQHSW------------IEQQVLEATPILEAFGNAKTIRND 243
Cdd:cd14891    72 RMQNQSIVISGESGAGKTETSKIILRFLttravggKKASGQDIEqsskkrklsvtsLDERLMDTNPILESFGNAKTLRNH 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  244 NSSRFGKYIDIHFNKRG-AIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCI 322
Cdd:cd14891   152 NSSRFGKFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCV 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  323 TCEGRVDSQEYANIRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFENLDACEVLFS--PSLATAASLLEVNPPD 400
Cdd:cd14891   232 SDDNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAEIASESdkEALATAAELLGVDEEA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  401 LMSCLTSRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAI-YKPPPLEVknsrrsIGLLDIFGFENF 479
Cdd:cd14891   312 LEKVITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLgHDPDPLPY------IGVLDIFGFESF 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  480 -TVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDAT 558
Cdd:cd14891   386 eTKNDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPNGILPLLDNEARNPNPSDAK 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  559 MLHKLNSQHKLNANYVPP--KNSHETqFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSrNKFIKQifqadvamga 636
Cdd:cd14891   466 LNETLHKTHKRHPCFPRPhpKDMREM-FIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS-AKFSDQ---------- 533
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  637 etrkrsptlssqfkrsLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEF 716
Cdd:cd14891   534 ----------------MQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAEL 597
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755522197  717 VERYRVLLP-GVKPAYKQGDlrgtcQRMAEAVLGTH----DDWQIGKTKIFLK 764
Cdd:cd14891   598 VDVYKPVLPpSVTRLFAEND-----RTLTQAILWAFrvpsDAYRLGRTRVFFR 645
MYSc_Myh7b cd14927
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...
108-764 9.14e-156

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: 498.32  E-value: 9.14e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQ 187
Cdd:cd14927     1 ASVLHNLRRRYSRWMIYT------YSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  188 CCIISGESGAGKTESTKLILQFLAAISG---------------QHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYI 252
Cdd:cd14927    75 SMLITGESGAGKTVNTKRVIQYFAIVAAlgdgpgkkaqflatkTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  253 DIHFNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLG-QAADYNYLAMGnCITCEGRVDSQ 331
Cdd:cd14927   155 RIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSmNPYDYHFCSQG-VTTVDNMDDGE 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  332 EYANIRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFEnlDACEVLFSPSLATAASLLEVNPPDLMSCL------ 405
Cdd:cd14927   234 ELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQRE--EQAEADGTESADKAAYLMGVSSADLLKGLlhprvk 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  406 TSRTLITRGETVstplsrEQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPPLEVknsrrSIGLLDIFGFENFTVNSFE 485
Cdd:cd14927   312 VGNEYVTKGQSV------EQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQF-----FIGVLDIAGFEIFEFNSFE 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  486 QLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEF-TDNQEALDMIaNRPMNVISLIDEESKFPKGTDATMLHKLN 564
Cdd:cd14927   381 QLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFIDFgLDLQACIDLI-EKPLGILSILEEECMFPKASDASFKAKLY 459
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  565 SQH-KLNANYVPP----KNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ--------AD 631
Cdd:cd14927   460 DNHlGKSPNFQKPrpdkKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYEnyvgsdstED 539
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  632 VAMGAETRKRSP----TLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGY 707
Cdd:cd14927   540 PKSGVKEKRKKAasfqTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGF 619
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755522197  708 PIRYSFVEFVERYRVLLPGVKPAYKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd14927   620 PNRILYADFKQRYRILNPSAIPDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
108-764 1.71e-155

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: 497.61  E-value: 1.71e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQ 187
Cdd:cd14920     1 ASVLHNLKDRYYSGLIYT------YSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  188 CCIISGESGAGKTESTKLILQFLAAISGQHSW---------IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNK 258
Cdd:cd14920    75 SILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  259 RGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNcITCEGRVDSQEYANIRS 338
Cdd:cd14920   155 TGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGY-IPIPGQQDKDNFQETME 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  339 AMKVLMFTDTENWEISKLLAAILHMGNLQYeaRTFENLDACEVLFSPSLATAASLLEVNPPDLM-SCLTSRTLITRgETV 417
Cdd:cd14920   234 AMHIMGFSHEEILSMLKVVSSVLQFGNISF--KKERNTDQASMPENTVAQKLCHLLGMNVMEFTrAILTPRIKVGR-DYV 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  418 STPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPplevKNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQ 497
Cdd:cd14920   311 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTK----RQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQ 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  498 QFFVRHVFKLEQEEYDLESIDWLHIEF-TDNQEALDMIaNRPMN---VISLIDEESKFPKGTDATMLHKLNSQHKLNANY 573
Cdd:cd14920   387 QLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLI-ERPANppgVLALLDEECWFPKATDKTFVEKLVQEQGSHSKF 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  574 VPPKNSH-ETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADV----------------AMGA 636
Cdd:cd14920   466 QKPRQLKdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgldqvtgmtetafGSAY 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  637 ETRK-RSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVE 715
Cdd:cd14920   546 KTKKgMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 625
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|
gi 755522197  716 FVERYRVLLPGVKP-AYKQGdlRGTCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd14920   626 FRQRYEILTPNAIPkGFMDG--KQACERMIRALELDPNLYRIGQSKIFFR 673
MYSc_Myh15_mammals cd14929
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...
108-764 5.81e-155

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: 495.65  E-value: 5.81e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQ 187
Cdd:cd14929     1 ASVLHTLRRRYDHWMIYT------YSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  188 CCIISGESGAGKTESTKLILQFLAAISG------QHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGA 261
Cdd:cd14929    75 SILFTGESGAGKTVNTKHIIQYFATIAAmieskkKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGM 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  262 IEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGnCITCEGRVDSQEYANIRSAMK 341
Cdd:cd14929   155 LSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCG-AVAVESLDDAEELLATEQAMD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  342 VLMFTDTENWEISKLLAAILHMGNLQYEARTFEnlDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPL 421
Cdd:cd14929   234 ILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPRE--EQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQ 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  422 SREQALDVRDAFVKGIYGRLFVWIVEKINAAiykpppLEVKNSRR-SIGLLDIFGFENFTVNSFEQLCINFANEHLQQFF 500
Cdd:cd14929   312 NIEQVTYAVGALSKSIYERMFKWLVARINRV------LDAKLSRQfFIGILDITGFEILDYNSLEQLCINFTNEKLQQFF 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  501 VRHVFKLEQEEYDLESIDWLHIEF-TDNQEALDMIaNRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANYV----P 575
Cdd:cd14929   386 NQHMFVLEQEEYRKEGIDWVSIDFgLDLQACIDLI-EKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFqkpkP 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  576 PKNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVA------MGAETRKRSP---TLS 646
Cdd:cd14929   465 DKKKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYIStdsaiqFGEKKRKKGAsfqTVA 544
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  647 SQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPG 726
Cdd:cd14929   545 SLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPR 624
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 755522197  727 VKPAYKQGDLRgtcqRMAEAVLGT----HDDWQIGKTKIFLK 764
Cdd:cd14929   625 TFPKSKFVSSR----KAAEELLGSleidHTQYRFGITKVFFK 662
MYSc_Myh1_insects_crustaceans cd14909
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
108-764 2.80e-154

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: 493.97  E-value: 2.80e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQ 187
Cdd:cd14909     1 ASVLHNLRQRYYAKLIYT------YSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  188 CCIISGESGAGKTESTKLILQFLAAI---------SGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNK 258
Cdd:cd14909    75 SMLITGESGAGKTENTKKVIAYFATVgaskktdeaAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  259 RGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQ-AADYNYLAMGNcITCEGRVDSQEYANIR 337
Cdd:cd14909   155 TGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDnIYDYYIVSQGK-VTVPNVDDGEEFSLTD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  338 SAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFEnlDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETV 417
Cdd:cd14909   234 QAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGRE--EQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFV 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  418 STPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAiykpppLEVKNSRRS-IGLLDIFGFENFTVNSFEQLCINFANEHL 496
Cdd:cd14909   312 TQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNET------LDTQQKRQHfIGVLDIAGFEIFEYNGFEQLCINFTNEKL 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  497 QQFFVRHVFKLEQEEYDLESIDWLHIEF-TDNQEALDMIaNRPMNVISLIDEESKFPKGTDATMLHKLNSQH-KLNANYV 574
Cdd:cd14909   386 QQFFNHHMFVLEQEEYKREGIDWAFIDFgMDLLACIDLI-EKPMGILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQ 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  575 PPK----NSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIF-----QADVAMGAETRKRS--- 642
Cdd:cd14909   465 KPKppkpGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFadhagQSGGGEQAKGGRGKkgg 544
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  643 --PTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERY 720
Cdd:cd14909   545 gfATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRY 624
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....
gi 755522197  721 RVLLPgvKPAYKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd14909   625 KILNP--AGIQGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
108-764 5.13e-153

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: 490.65  E-value: 5.13e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQ 187
Cdd:cd14911     1 ASVLHNIKDRYYSGLIYT------YSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  188 CCIISGESGAGKTESTKLILQFLAAISGQHS------------------WIEQQVLEATPILEAFGNAKTIRNDNSSRFG 249
Cdd:cd14911    75 SILCTGESGAGKTENTKKVIQFLAYVAASKPkgsgavphpavnpavligELEQQLLQANPILEAFGNAKTVKNDNSSRFG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  250 KYIDIHFNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNcITCEGRVD 329
Cdd:cd14911   155 KFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGS-LPVPGVDD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  330 SQEYANIRSAMKVLMFTDTENWEISKLLAAILHMGNLQYeaRTFENLDACEVLFSPSLATAASLLEVNPPDLMSC-LTSR 408
Cdd:cd14911   234 YAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKF--RQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAfLTPR 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  409 TLITRgETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPplevKNSRRSIGLLDIFGFENFTVNSFEQLC 488
Cdd:cd14911   312 IKVGR-DFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTK----RQGASFIGILDMAGFEIFELNSFEQLC 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  489 INFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEF-TDNQEALDMIaNRPMNVISLIDEESKFPKGTDATMLHKLNSQH 567
Cdd:cd14911   387 INYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLI-DKPGGIMALLDEECWFPKATDKTFVDKLVSAH 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  568 KLNANYVPPKNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ------------ADVAMG 635
Cdd:cd14911   466 SMHPKFMKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKdaeivgmaqqalTDTQFG 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  636 AETRK-RSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFV 714
Cdd:cd14911   546 ARTRKgMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 625
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755522197  715 EFVERYRVLLPGVKPaykQG--DLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd14911   626 EFRQRYELLTPNVIP---KGfmDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
PTZ00014 PTZ00014
myosin-A; Provisional
102-816 7.74e-153

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 495.70  E-value: 7.74e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  102 LGDL---NEAGILRNLLIRYRDHLIYTScggrtyTGSILVAVNPYQLLSIYSPEHIRQY-TNKKIGEMPPHIFAIADNCY 177
Cdd:PTZ00014  101 IGLLphtNIPCVLDFLKHRYLKNQIYTT------ADPLLVAINPFKDLGNTTNDWIRRYrDAKDSDKLPPHVFTTARRAL 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  178 FNMKRNNRDQCCIISGESGAGKTESTKLILQFLAAISGQH--SWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIH 255
Cdd:PTZ00014  175 ENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNmdLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQ 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  256 FNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAmGNCITCEGRVDSQEYAN 335
Cdd:PTZ00014  255 LGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYIN-PKCLDVPGIDDVKDFEE 333
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  336 IRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFENLDACEVLFSPSLAT---AASLLEVNPPDLMSCLTSRTLIT 412
Cdd:PTZ00014  334 VMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDAAAISDESLEVfneACELLFLDYESLKKELTVKVTYA 413
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  413 RGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPPLEVknsrrSIGLLDIFGFENFTVNSFEQLCINFA 492
Cdd:PTZ00014  414 GNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-----FIGMLDIFGFEVFKNNSLEQLFINIT 488
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  493 NEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNAN 572
Cdd:PTZ00014  489 NEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPK 568
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  573 YVPPKNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAETRKRSpTLSSQFKRS 652
Cdd:PTZ00014  569 YKPAKVDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKGKLAKGQ-LIGSQFLNQ 647
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  653 LELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVL-LPGVKPay 731
Cdd:PTZ00014  648 LDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLdLAVSND-- 725
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  732 KQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK-DHHDMLLEVERDK--------AITDRVILLQKVIRGFKDRSNFLrl 802
Cdd:PTZ00014  726 SSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkDAAKELTQIQREKlaaweplvSVLEALILKIKKKRKVRKNIKSL-- 803
                         730
                  ....*....|....
gi 755522197  803 ksaaTLIQRHWRGH 816
Cdd:PTZ00014  804 ----VRIQAHLRRH 813
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
108-764 1.82e-152

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: 489.42  E-value: 1.82e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTN------------KKIGempPHIFAIADN 175
Cdd:cd14908     1 PAILHSLSRRFFRGIIYT------WTGPVLIAVNPFQRLPLYGKEILESYRQegllrsqgiespQALG---PHVFAIADR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  176 CYFNM-KRNNRDQCCIISGESGAGKTESTKLILQFLAAI------------SGQHSWIEQQVLEATPILEAFGNAKTIRN 242
Cdd:cd14908    72 SYRQMmSEIRASQSILISGESGAGKTESTKIVMLYLTTLgngeegapnegeELGKLSIMDRVLQSNPILEAFGNARTLRN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  243 DNSSRFGKYIDIHFNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKK--------LGLGQAADYN 314
Cdd:cd14908   152 DNSSRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKyefhdgitGGLQLPNEFH 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  315 YLAMGNCITCEGRVDSQEYANIRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFENL-DACEVLFSPSLATAASL 393
Cdd:cd14908   232 YTGQGGAPDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAaEIAEEGNEKCLARVAKL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  394 LEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPPLEVknsRRSIGLLDI 473
Cdd:cd14908   312 LGVDVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDI---RSSVGVLDI 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  474 FGFENFTVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFP- 552
Cdd:cd14908   389 FGFECFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAKKKGILTMLDDECRLGi 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  553 KGTDAtmlhklNSQHKLNANYVPPKNSHETQ---------------FGINHFAGVVYYESQ-GFLEKNRDTLhgdiiqlv 616
Cdd:cd14908   469 RGSDA------NYASRLYETYLPEKNQTHSEntrfeatsiqktkliFAVRHFAGQVQYTVEtTFCEKNKDEI-------- 534
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  617 hssrNKFIKQIFQAdvamgaetrkrsptlSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGM 696
Cdd:cd14908   535 ----PLTADSLFES---------------GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGV 595
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  697 METIRIRHAGYPIRYSFVEFVERYRVLLPG----VKPAYKQG-DLRGTCQRMAEAVLGTH--------------DDWQIG 757
Cdd:cd14908   596 LEAVRVARSGYPVRLPHKDFFKRYRMLLPLipevVLSWSMERlDPQKLCVKKMCKDLVKGvlspamvsmknipeDTMQLG 675

                  ....*..
gi 755522197  758 KTKIFLK 764
Cdd:cd14908   676 KSKVFMR 682
MYSc_Myh3 cd14913
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...
109-764 1.82e-150

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: 483.40  E-value: 1.82e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  109 GILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQC 188
Cdd:cd14913     2 AVLYNLKDRYTSWMIYT------YSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  189 CIISGESGAGKTESTKLILQFLAAI-----------SGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFN 257
Cdd:cd14913    76 ILITGESGAGKTVNTKRVIQYFATIaatgdlakkkdSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  258 KRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLG-QAADYNYLAMGNcITCEGRVDSQEYANI 336
Cdd:cd14913   156 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITtNPYDYPFISQGE-ILVASIDDAEELLAT 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  337 RSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFENL---DACEVLfspslATAASLLEVNPPDLMSCL------TS 407
Cdd:cd14913   235 DSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQaepDGTEVA-----DKTAYLMGLNSSDLLKALcfprvkVG 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  408 RTLITRGETVstplsrEQALDVRDAFVKGIYGRLFVWIVEKINAAiykpppLEVKNSRRS-IGLLDIFGFENFTVNSFEQ 486
Cdd:cd14913   310 NEYVTKGQTV------DQVHHAVNALSKSVYEKLFLWMVTRINQQ------LDTKLPRQHfIGVLDIAGFEIFEYNSLEQ 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  487 LCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQ 566
Cdd:cd14913   378 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQ 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  567 H-KLNANYVPPKNSH---ETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIF------QADVAMGA 636
Cdd:cd14913   458 HlGKSNNFQKPKVVKgraEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYatfataDADSGKKK 537
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  637 ETRKRSP---TLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSF 713
Cdd:cd14913   538 VAKKKGSsfqTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILY 617
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755522197  714 VEFVERYRVLLPGVKPAYKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd14913   618 GDFKQRYRVLNASAIPEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
110-735 3.73e-150

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: 480.96  E-value: 3.73e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  110 ILRNLLIRYRDHLIYTScggrtyTGSILVAVNPYQLL-SIYSPEHIRQY-----------TNKKIGEMPPHIFAIADNCY 177
Cdd:cd14900     3 ILSALETRFYAQKIYTN------TGAILLAVNPFQKLpGLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  178 FNMKR--NNR--DQCCIISGESGAGKTESTKLILQFLA-----------AISGQHSWIEQQVLEATPILEAFGNAKTIRN 242
Cdd:cd14900    77 KAMMLglNGVmsDQSILVSGESGSGKTESTKFLMEYLAqagdnnlaasvSMGKSTSGIAAKVLQTNILLESFGNARTLRN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  243 DNSSRFGKYIDIHFNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKklglgqaadynylamgnci 322
Cdd:cd14900   157 DNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK------------------- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  323 tcegrvdSQEYANIRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFENLDACEVL-FSPS----LATAASLLEVN 397
Cdd:cd14900   218 -------RDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSdLAPSsiwsRDAAATLLSVD 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  398 PPDLMSCLTSRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPPLEVKNSRRSIGLLDIFGFE 477
Cdd:cd14900   291 ATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKSHGGLHFIGILDIFGFE 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  478 NFTVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDA 557
Cdd:cd14900   371 VFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRPTGILSLIDEECVMPKGSDT 450
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  558 TMLHKL----NSQHKLNANYVppkNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLvhssrnkfikqiFQAdva 633
Cdd:cd14900   451 TLASKLyracGSHPRFSASRI---QRARGLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDL------------FVY--- 512
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  634 mgaetrkrsptlSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSF 713
Cdd:cd14900   513 ------------GLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLH 580
                         650       660
                  ....*....|....*....|....
gi 755522197  714 VEFVERYRVLLPGVKP--AYKQGD 735
Cdd:cd14900   581 DEFVARYFSLARAKNRllAKKQGT 604
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
108-748 1.41e-149

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: 482.47  E-value: 1.41e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQ-LLSIYSPEHIRQY--------TNKKIGEMPPHIFAIADNCYF 178
Cdd:cd14902     1 AALLQALSERFEHDQIYT------SIGDILVALNPLKpLPDLYSESQLNAYkasmtstsPVSQLSELPPHVFAIGGKAFG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  179 NMKRNNR-DQCCIISGESGAGKTESTKLILQFLAAISGQHSWIEQ----------QVLEATPILEAFGNAKTIRNDNSSR 247
Cdd:cd14902    75 GLLKPERrNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQegsdaveigkRILQTNPILESFGNAQTIRNDNSSR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  248 FGKYIDIHFNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCEGR 327
Cdd:cd14902   155 FGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSYGPSFARKR 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  328 VDSQEYANiRSAMKVLMFTDT-----ENWEISKLLAAILHMGNLQYEArTFENLDACEVLFSPS--LATAASLLEVNPPD 400
Cdd:cd14902   235 AVADKYAQ-LYVETVRAFEDTgvgelERLDIFKILAALLHLGNVNFTA-ENGQEDATAVTAASRfhLAKCAELMGVDVDK 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  401 LMSCLTSRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEK----INAAIYKPPPLEVKNSRRSIGLLDIFGF 476
Cdd:cd14902   313 LETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRlsdeINYFDSAVSISDEDEELATIGILDIFGF 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  477 ENFTVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTD 556
Cdd:cd14902   393 ESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSNGLFSLLDQECLMPKGSN 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  557 ATMLHKLNSQHklnanyvppknSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQAD--VAM 634
Cdd:cd14902   473 QALSTKFYRYH-----------GGLGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADEnrDSP 541
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  635 GAETRK---------RSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHA 705
Cdd:cd14902   542 GADNGAagrrrysmlRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARH 621
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|
gi 755522197  706 GYPIRYSFVEFVERYRVLLP-------GVKPAYKQGDLRGTCQRMAEAVL 748
Cdd:cd14902   622 GYSVRLAHASFIELFSGFKCflstrdrAAKMNNHDLAQALVTVLMDRVLL 671
MYSc_Myh16 cd14934
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...
108-764 1.04e-145

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: 469.51  E-value: 1.04e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQ 187
Cdd:cd14934     1 ASVLDNLRQRYTNMRIYT------YSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  188 CCIISGESGAGKTESTKLILQFLAAIS--------GQHSwIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKR 259
Cdd:cd14934    75 SMLITGESGAGKTENTKKVIQYFANIGgtgkqssdGKGS-LEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  260 GAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGL-GQAADYNYLAMGnCITCEGRVDSQEYANIRS 338
Cdd:cd14934   154 GKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvPNPKEYHWVSQG-VTVVDNMDDGEELQITDV 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  339 AMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFE---NLDACEVLfspslATAASLLEVNPPDLMSCLTSRTLITRGE 415
Cdd:cd14934   233 AFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREeqaEVDTTEVA-----DKVAHLMGLNSGELQKGITRPRVKVGNE 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  416 TVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAiykpppLEVKNSRRS-IGLLDIFGFENFTVNSFEQLCINFANE 494
Cdd:cd14934   308 FVQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKT------LDTKMQRQFfIGVLDIAGFEIFEFNSFEQLCINFTNE 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  495 HLQQFFVRHVFKLEQEEYDLESIDWLHIEF-TDNQEALDMIaNRPMNVISLIDEESKFPKGTDATMLHKLNSQH-KLNAN 572
Cdd:cd14934   382 KLQQFFNHHMFVLEQEEYKREGIEWVFIDFgLDLQACIDLL-EKPMGIFSILEEQCVFPKATDATFKAALYDNHlGKSSN 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  573 YVPPKNSH----ETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAM-GAETRKRSP---T 644
Cdd:cd14934   461 FLKPKGGKgkgpEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPaGSKKQKRGSsfmT 540
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  645 LSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLL 724
Cdd:cd14934   541 VSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLN 620
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....
gi 755522197  725 PGVKPaykQGDLRGtcQRMAEAVLGTHD----DWQIGKTKIFLK 764
Cdd:cd14934   621 PNVIP---QGFVDN--KKASELLLGSIDldvnEYKIGHTKVFFR 659
MYSc_Myo14 cd14876
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...
117-764 3.91e-144

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: 464.46  E-value: 3.91e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  117 RYRDHLIYTScggrtyTGSILVAVNPYQLLSIYSPEHIRQYTN-KKIGEMPPHIFAIADNCYFNMKRNNRDQCCIISGES 195
Cdd:cd14876    10 RYLKNQIYTT------ADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVSGES 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  196 GAGKTESTKLILQFLAAISGQH--SWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYLLE 273
Cdd:cd14876    84 GAGKTEATKQIMRYFASAKSGNmdLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVAFLLE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  274 KSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAmGNCITCEGRVDSQEYANIRSAMKVLMFTDTENWEI 353
Cdd:cd14876   164 KSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLN-PKCLDVPGIDDVADFEEVLESLKSMGLTEEQIDTV 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  354 SKLLAAILHMGNLQYEARTFENLDACEVLFSPSLA---TAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVR 430
Cdd:cd14876   243 FSIVSGVLLLGNVKITGKTEQGVDDAAAISNESLEvfkEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDDAEMLK 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  431 DAFVKGIYGRLFVWIVEKINAAIyKPPplevKNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHVFKLEQE 510
Cdd:cd14876   323 LSLAKAMYDKLFLWIIRNLNSTI-EPP----GGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERESK 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  511 EYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANYVPPKNSHETQFGINHFA 590
Cdd:cd14876   398 LYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKVDSNINFIVVHTI 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  591 GVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFqADVAMGAETRKRSPTLSSQFKRSLELLMRTLGACQPFFVRC 670
Cdd:cd14876   478 GDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALF-EGVVVEKGKIAKGSLIGSQFLKQLESLMGLINSTEPHFIRC 556
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  671 IKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPGVKPAyKQGDLRGTCQRMAEAVLGT 750
Cdd:cd14876   557 IKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLGIAND-KSLDPKVAALKLLESSGLS 635
                         650
                  ....*....|....
gi 755522197  751 HDDWQIGKTKIFLK 764
Cdd:cd14876   636 EDEYAIGKTMVFLK 649
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
108-764 8.46e-144

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: 464.89  E-value: 8.46e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQ 187
Cdd:cd14932     1 ASVLHNLKERYYSGLIYT------YSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  188 CCIISGESGAGKTESTKLILQFLAAISGQ-------------HSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDI 254
Cdd:cd14932    75 SILCTGESGAGKTENTKKVIQYLAYVASSfktkkdqssialsHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  255 HFNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNcITCEGRVDSQEYA 334
Cdd:cd14932   155 NFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGN-VTIPGQQDKELFA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  335 NIRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARtfENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRG 414
Cdd:cd14932   234 ETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKE--RNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGR 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  415 ETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPplevKNSRRSIGLLDIFGFENFTVNSFEQLCINFANE 494
Cdd:cd14932   312 DYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTK----RQGASFIGILDIAGFEIFELNSFEQLCINYTNE 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  495 HLQQFFVRHVFKLEQEEYDLESIDWLHIEF-TDNQEALDMI--ANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNA 571
Cdd:cd14932   388 KLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIELIekPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNP 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  572 NYVPPKN-SHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ--------------ADVAMGA 636
Cdd:cd14932   468 KFQKPKKlKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKdvdrivgldkvagmGESLHGA 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  637 -ETRK-RSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFV 714
Cdd:cd14932   548 fKTRKgMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 627
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755522197  715 EFVERYRVLLPGVKPaykQG--DLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd14932   628 EFRQRYEILTPNAIP---KGfmDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
133-764 1.35e-143

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


Pssm-ID: 276860 [Multi-domain]  Cd Length: 704  Bit Score: 465.20  E-value: 1.35e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  133 TGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNN-------RDQCCIISGESGAGKTESTKL 205
Cdd:cd14895    20 SGAVLIAVNPFKHIPGLYDLHKYREEMPGWTALPPHVFSIAEGAYRSLRRRLhepgaskKNQTILVSGESGAGKTETTKF 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  206 ILQFLAAIS----------GQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHF-----NKRGAIEGAKIEQY 270
Cdd:cd14895   100 IMNYLAESSkhttatssskRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFVRMFFeghelDTSLRMIGTSVETY 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  271 LLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLG--QAADYNYLAMGNCITCEGRV-DSQEYANIRSAMKVLMFTD 347
Cdd:cd14895   180 LLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLEllSAQEFQYISGGQCYQRNDGVrDDKQFQLVLQSMKVLGFTD 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  348 TENWEISKLLAAILHMGNLQYEART-----FENLDACEVLF----SPS-------LATAASLLEVNPPDLMSCLTSRTLI 411
Cdd:cd14895   260 VEQAAIWKILSALLHLGNVLFVASSedegeEDNGAASAPCRlasaSPSsltvqqhLDIVSKLFAVDQDELVSALTTRKIS 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  412 TRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAI------YKPPPLEVKNSRRSIGLLDIFGFENFTVNSFE 485
Cdd:cd14895   340 VGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASpqrqfaLNPNKAANKDTTPCIAVLDIFGFEEFEVNQFE 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  486 QLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNS 565
Cdd:cd14895   420 QFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRPSGIFSLLDEECVVPKGSDAGFARKLYQ 499
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  566 QHKLNANYVPPKNSH-ETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ-ADVAMGAE------ 637
Cdd:cd14895   500 RLQEHSNFSASRTDQaDVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGKTSDAHLRELFEfFKASESAElslgqp 579
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  638 -TRKRSPTLS-----SQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRY 711
Cdd:cd14895   580 kLRRRSSVLSsvgigSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRM 659
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755522197  712 SFVEFVERYRVLLpgvkPAYKQGDLRGTCQRMAEAVLGThddwQIGKTKIFLK 764
Cdd:cd14895   660 KHADFVKQYRLLV----AAKNASDATASALIETLKVDHA----ELGKTRVFLR 704
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
105-763 1.37e-140

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: 454.32  E-value: 1.37e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  105 LNEAGILRNLLIRYRDHLIYTSCGGrtytgSILVAVNPYQLLSIYSPEHIRQY-------TNKKIGEMPPHIFAIADNCY 177
Cdd:cd14879     1 PSDDAITSHLASRFRSDLPYTRLGS-----SALVAVNPYKYLSSNSDASLGEYgseyydtTSGSKEPLPPHAYDLAARAY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  178 FNMKRNNRDQCCIISGESGAGKTESTKLILQ---FLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDI 254
Cdd:cd14879    76 LRMRRRSEDQAVVFLGETGSGKSESRRLLLRqllRLSSHSKKGTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTEL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  255 HFNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCEGRV---DSQ 331
Cdd:cd14879   156 QFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYGCHPLPLGPgsdDAE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  332 EYANIRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLI 411
Cdd:cd14879   236 GFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHEGGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTYKTKL 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  412 TRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPPlEVKNsrrSIGLLDIFGFENFT---VNSFEQLC 488
Cdd:cd14879   316 VRKELCTVFLDPEGAAAQRDELARTLYSLLFAWVVETINQKLCAPED-DFAT---FISLLDFPGFQNRSstgGNSLDQFC 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  489 INFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESK-FPKGTDATMLHKLNSQH 567
Cdd:cd14879   392 VNFANERLHNYVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKPGGLLGILDDQTRrMPKKTDEQMLEALRKRF 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  568 KLNANYV----PPKNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVhssrnkfikqifqadvamgaetrkRSP 643
Cdd:cd14879   472 GNHSSFIavgnFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLL------------------------RGA 527
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  644 TlssQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVL 723
Cdd:cd14879   528 T---QLNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKST 604
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|
gi 755522197  724 LPGvkpaykqGDLRGTCQRMAEAVLGTHDDWQIGKTKIFL 763
Cdd:cd14879   605 LRG-------SAAERIRQCARANGWWEGRDYVLGNTKVFL 637
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
108-763 2.50e-140

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: 456.36  E-value: 2.50e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQ-LLSIYSPEHIRQYTN-KKIGEMPPHIFAIADNCYFNMKRNNR 185
Cdd:cd14906     1 AIILNNLGKRYKSDSIYT------YIGNVLISINPYKdISSIYSNLILNEYKDiNQNKSPIPHIYAVALRAYQSMVSEKK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  186 DQCCIISGESGAGKTESTKLILQFLAAISGQHSW-----------IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDI 254
Cdd:cd14906    75 NQSIIISGESGSGKTEASKTILQYLINTSSSNQQqnnnnnnnnnsIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  255 HFNKR-GAIEGAKIEQYLLEKSRVCRQaPDERN--YHVFYCMLEGMNEEEKKKLGL-GQAADYNYL-------------A 317
Cdd:cd14906   155 EFRSSdGKIDGASIETYLLEKSRISHR-PDNINlsYHIFYYLVYGASKDERSKWGLnNDPSKYRYLdarddvissfksqS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  318 MGNCITCEGRVDSQE-YANIRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEA-RTFENLDACEVLFSPSLATAASLLE 395
Cdd:cd14906   234 SNKNSNHNNKTESIEsFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEdSDFSKYAYQKDKVTASLESVSKLLG 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  396 VNPPDLMSCLTSRTLIT--RGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYK---PPPLEVKNSRRS--- 467
Cdd:cd14906   314 YIESVFKQALLNRNLKAggRGSVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqSNDLAGGSNKKNnlf 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  468 IGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDE 547
Cdd:cd14906   394 IGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKSDGILSLLDD 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  548 ESKFPKGTDATMLHKLNSQHKlNANYVPPKNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQI 627
Cdd:cd14906   474 ECIMPKGSEQSLLEKYNKQYH-NTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSL 552
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  628 FQADVAMGAETRKR---SPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRH 704
Cdd:cd14906   553 FQQQITSTTNTTKKqtqSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRK 632
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  705 AGYPIRYSFVEFVERYRVLLPGVKPAYKQGDLRGT--CQRMAEAVLGTHDD---------------------WQIGKTKI 761
Cdd:cd14906   633 MGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASqlILQNIQSKLKTMGIsnnkkknnsnsnsnttndkplFQIGKTKI 712

                  ..
gi 755522197  762 FL 763
Cdd:cd14906   713 FI 714
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
134-764 3.75e-140

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: 453.88  E-value: 3.75e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  134 GSILVAVNPYQLLSIYSPEHIRQYTNKKIGEM-PPHIFAIADNCYFNMK-RNNRDQCCIISGESGAGKTESTKLILQFLA 211
Cdd:cd14875    22 GEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFNAIFvQGLGNQSVVISGESGSGKTENAKMLIAYLG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  212 AISGQHS------WIEQQVLE----ATPILEAFGNAKTIRNDNSSRFGKYIDIHFNK-RGAIEGAKIEQYLLEKSRVCRQ 280
Cdd:cd14875   102 QLSYMHSsntsqrSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPtSGVMVGGQTVTYLLEKSRIIMQ 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  281 APDERNYHVFYCMLEGMNEEEKKKLG-LGQAADYNYLAMGNCIT---CEGRV--DSQEYANIRSAMKVLMFTDTENWEIS 354
Cdd:cd14875   182 SPGERNYHIFYEMLAGLSPEEKKELGgLKTAQDYKCLNGGNTFVrrgVDGKTldDAHEFQNVRHALSMIGVELETQNSIF 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  355 KLLAAILHMGNLQYEArtfENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTlitRGETVSTPLSREQALDVRDAFV 434
Cdd:cd14875   262 RVLASILHLMEVEFES---DQNDKAQIADETPFLTACRLLQLDPAKLRECFLVKS---KTSLVTILANKTEAEGFRNAFC 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  435 KGIYGRLFVWIVEKINAAIYkpPPLEVkNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDL 514
Cdd:cd14875   336 KAIYVGLFDRLVEFVNASIT--PQGDC-SGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQNHYNKYTFINDEEECRR 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  515 ESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANY-VPPKNSHETQFGINHFAGVV 593
Cdd:cd14875   413 EGIQIPKIEFPDNSECVNMFDQKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPYfVLPKSTIPNQFGVNHYAAFV 492
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  594 YYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGaetrKRSPTLSSQFKRSLELLMRTLGACQPFFVRCIKP 673
Cdd:cd14875   493 NYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLA----RRKQTVAIRFQRQLTDLRTELESTETQFIRCIKP 568
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  674 NEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLP-GVKPAYKQGDLRGTCQRMAEAVLGTHd 752
Cdd:cd14875   569 NMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPrSTASLFKQEKYSEAAKDFLAYYQRLY- 647
                         650
                  ....*....|....*..
gi 755522197  753 DWQ-----IGKTKIFLK 764
Cdd:cd14875   648 GWAkpnyaVGKTKVFLR 664
MYSc_Myh7 cd14917
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...
109-764 3.93e-140

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: 454.18  E-value: 3.93e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  109 GILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQC 188
Cdd:cd14917     2 AVLYNLKERYASWMIYT------YSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  189 CIISGESGAGKTESTKLILQFLAAIS--GQHS---------WIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFN 257
Cdd:cd14917    76 ILITGESGAGKTVNTKRVIQYFAVIAaiGDRSkkdqtpgkgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  258 KRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGL-GQAADYNYLAMGNcITCEGRVDSQEYANI 336
Cdd:cd14917   156 ATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGE-TTVASIDDAEELMAT 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  337 RSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFEnlDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGET 416
Cdd:cd14917   235 DNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQRE--EQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEY 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  417 VSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAiykpppLEVKNSRRS-IGLLDIFGFENFTVNSFEQLCINFANEH 495
Cdd:cd14917   313 VTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINAT------LETKQPRQYfIGVLDIAGFEIFDFNSFEQLCINFTNEK 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  496 LQQFFVRHVFKLEQEEYDLESIDWLHIEF-TDNQEALDMIaNRPMNVISLIDEESKFPKGTDATMLHKLNSQH-KLNANY 573
Cdd:cd14917   387 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNF 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  574 VPPKN---SHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIF------QADVAMGAETRKRSP- 643
Cdd:cd14917   466 QKPRNikgKPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFanyagaDAPIEKGKGKAKKGSs 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  644 --TLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYR 721
Cdd:cd14917   546 fqTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 625
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|...
gi 755522197  722 VLLPGVKPAYKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd14917   626 ILNPAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
108-764 5.80e-139

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: 451.01  E-value: 5.80e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQ 187
Cdd:cd14921     1 ASVLHNLRERYFSGLIYT------YSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  188 CCIISGESGAGKTESTKLILQFLAAISGQHSW---------IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNK 258
Cdd:cd14921    75 SILCTGESGAGKTENTKKVIQYLAVVASSHKGkkdtsitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  259 RGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNcITCEGRVDSQEYANIRS 338
Cdd:cd14921   155 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGF-VPIPAAQDDEMFQETLE 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  339 AMKVLMFTDTENWEISKLLAAILHMGNLQYEARtfENLDACEVLFSPSLATAASLLEVNPPDLMSC-LTSRTLITRgETV 417
Cdd:cd14921   234 AMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKE--RNTDQASMPDNTAAQKVCHLMGINVTDFTRSiLTPRIKVGR-DVV 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  418 STPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPplevKNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQ 497
Cdd:cd14921   311 QKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTH----RQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQ 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  498 QFFVRHVFKLEQEEYDLESIDWLHIEF-TDNQEALDMI--ANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANYV 574
Cdd:cd14921   387 QLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIerPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQ 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  575 PPKN-SHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQaDV-------AMGAETRKRSPTLS 646
Cdd:cd14921   467 KPKQlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWK-DVdrivgldQMAKMTESSLPSAS 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  647 SQ-----------FKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVE 715
Cdd:cd14921   546 KTkkgmfrtvgqlYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQE 625
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755522197  716 FVERYRVLLPGVKPaykQG--DLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd14921   626 FRQRYEILAANAIP---KGfmDGKQACILMIKALELDPNLYRIGQSKIFFR 673
MYSc_Myh2_mammals cd14912
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
109-764 1.99e-137

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: 446.49  E-value: 1.99e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  109 GILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQC 188
Cdd:cd14912     2 AVLYNLKERYAAWMIYT------YSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  189 CIISGESGAGKTESTKLILQFLA--AISGQ-----------HSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIH 255
Cdd:cd14912    76 ILITGESGAGKTVNTKRVIQYFAtiAVTGEkkkeeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  256 FNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLG-QAADYNYLAMGNcITCEGRVDSQEYA 334
Cdd:cd14912   156 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITtNPYDYPFVSQGE-ISVASIDDQEELM 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  335 NIRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFENL---DACEVLfspslATAASLLEVNPPDLMSCLTSRTLI 411
Cdd:cd14912   235 ATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQaepDGTEVA-----DKAAYLQSLNSADLLKALCYPRVK 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  412 TRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAiykpppLEVKNSRRS-IGLLDIFGFENFTVNSFEQLCIN 490
Cdd:cd14912   310 VGNEYVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQ------LDTKQPRQYfIGVLDIAGFEIFDFNSLEQLCIN 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  491 FANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQH-KL 569
Cdd:cd14912   384 FTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGK 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  570 NANYVPP---KNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ-ADVAMG---------A 636
Cdd:cd14912   464 SANFQKPkvvKGKAEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSgAQTAEGasagggakkG 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  637 ETRKRSP--TLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFV 714
Cdd:cd14912   544 GKKKGSSfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYA 623
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|
gi 755522197  715 EFVERYRVLLPGVKPAYKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd14912   624 DFKQRYKVLNASAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
MYSc_Myh8 cd14918
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...
109-764 2.49e-136

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: 443.41  E-value: 2.49e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  109 GILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQC 188
Cdd:cd14918     2 GVLYNLKERYAAWMIYT------YSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  189 CIISGESGAGKTESTKLILQFLA--AISGQ---------HSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFN 257
Cdd:cd14918    76 ILITGESGAGKTVNTKRVIQYFAtiAVTGEkkkeesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  258 KRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLG-QAADYNYLAMGNcITCEGRVDSQEYANI 336
Cdd:cd14918   156 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITtNPYDYAFVSQGE-ITVPSIDDQEELMAT 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  337 RSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFENL---DACEVLfspslATAASLLEVNPPDLMSCLTSRTLITR 413
Cdd:cd14918   235 DSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQaepDGTEVA-----DKAAYLQSLNSADLLKALCYPRVKVG 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  414 GETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAiykpppLEVKNSRRS-IGLLDIFGFENFTVNSFEQLCINFA 492
Cdd:cd14918   310 NEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQ------LDTKQPRQYfIGVLDIAGFEIFDFNSLEQLCINFT 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  493 NEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQH-KLNA 571
Cdd:cd14918   384 NEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHlGKSA 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  572 NYVPP---KNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIF------QADVAMGAETRKRS 642
Cdd:cd14918   464 NFQKPkvvKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFstyasaEADSGAKKGAKKKG 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  643 P---TLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVER 719
Cdd:cd14918   544 SsfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQR 623
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*
gi 755522197  720 YRVLLPGVKPAYKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd14918   624 YKVLNASAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
108-763 4.01e-136

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: 442.37  E-value: 4.01e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTScggrtyTGSILVAVNPYQLLS-IYSPEHIRQY-TNKKIGEMPPHIFAIADNCYFNMK--RN 183
Cdd:cd14880     1 ETVLRCLQARYTADTFYTN------AGCTLVALNPFKPVPqLYSPELMREYhAAPQPQKLKPHIFTVGEQTYRNVKslIE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  184 NRDQCCIISGESGAGKTESTKLILQFLAAISGQH-SW--------IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDI 254
Cdd:cd14880    75 PVNQSIVVSGESGAGKTWTSRCLMKFYAVVAASPtSWeshkiaerIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  255 HFNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAmgnciTCEGRVDSQEYA 334
Cdd:cd14880   155 QLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLP-----NPERNLEEDCFE 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  335 NIRSAMKVL-MFTDTENwEISKLLAAILHMGNLQY-----EARTFENLDACEVlfspSLATAASLLEVNPPDLMSCLTSR 408
Cdd:cd14880   230 VTREAMLHLgIDTPTQN-NIFKVLAGLLHLGNIQFadsedEAQPCQPMDDTKE----SVRTSALLLKLPEDHLLETLQIR 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  409 TlITRG---ETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPplevKNSRRSIGLLDIFGFENFTVNSFE 485
Cdd:cd14880   305 T-IRAGkqqQVFKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADT----DSWTTFIGLLDVYGFESFPENSLE 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  486 QLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHK--- 562
Cdd:cd14880   380 QLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSPISICSLINEECRLNRPSSAAQLQTrie 459
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  563 --LNSQHKLNANyvppKNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAE--- 637
Cdd:cd14880   460 saLAGNPCLGHN----KLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQeep 535
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  638 -TRKRSP--TLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFV 714
Cdd:cd14880   536 sGQSRAPvlTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQ 615
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*....
gi 755522197  715 EFVERYRVLLPgVKPAYKqgdlrgTCQRMAEAVLGTHDDWQIGKTKIFL 763
Cdd:cd14880   616 NFVERYKLLRR-LRPHTS------SGPHSPYPAKGLSEPVHCGRTKVFM 657
MYSc_Myh6 cd14916
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...
109-764 5.38e-136

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: 442.19  E-value: 5.38e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  109 GILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQC 188
Cdd:cd14916     2 AVLYNLKERYAAWMIYT------YSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  189 CIISGESGAGKTESTKLILQFLAAISG------------QHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHF 256
Cdd:cd14916    76 ILITGESGAGKTVNTKRVIQYFASIAAigdrskkenpnaNKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  257 NKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGL-GQAADYNYLAMGNcITCEGRVDSQEYAN 335
Cdd:cd14916   156 GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtNNPYDYAFVSQGE-VSVASIDDSEELLA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  336 IRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFEnlDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGE 415
Cdd:cd14916   235 TDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQRE--EQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNE 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  416 TVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAiykpppLEVKNSRRS-IGLLDIFGFENFTVNSFEQLCINFANE 494
Cdd:cd14916   313 YVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINAT------LETKQPRQYfIGVLDIAGFEIFDFNSFEQLCINFTNE 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  495 HLQQFFVRHVFKLEQEEYDLESIDWLHIEF-TDNQEALDMIaNRPMNVISLIDEESKFPKGTDATMLHKLNSQH-KLNAN 572
Cdd:cd14916   387 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKASDMTFKAKLYDNHlGKSNN 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  573 YVPPKN---SHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ-------ADVAMGAETRKRS 642
Cdd:cd14916   466 FQKPRNvkgKQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFStyasadtGDSGKGKGGKKKG 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  643 P---TLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVER 719
Cdd:cd14916   546 SsfqTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQR 625
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*
gi 755522197  720 YRVLLPGVKPAYKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd14916   626 YRILNPAAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
MYSc_Myh9 cd14919
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...
108-764 7.97e-136

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: 441.84  E-value: 7.97e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQ 187
Cdd:cd14919     1 ASVLHNLKERYYSGLIYT------YSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  188 CCIISGESGAGKTESTKLILQFLAAISGQHSW------IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGA 261
Cdd:cd14919    75 SILCTGESGAGKTENTKKVIQYLAHVASSHKSkkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  262 IEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNcITCEGRVDSQEYANIRSAMK 341
Cdd:cd14919   155 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH-VTIPGQQDKDMFQETMEAMR 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  342 VLMFTDTENWEISKLLAAILHMGNLQYEARtfENLDACEVLFSPSLATAASLLEVNPPDLM-SCLTSRTLITRgETVSTP 420
Cdd:cd14919   234 IMGIPEEEQMGLLRVISGVLQLGNIVFKKE--RNTDQASMPDNTAAQKVSHLLGINVTDFTrGILTPRIKVGR-DYVQKA 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  421 LSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPplevKNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFF 500
Cdd:cd14919   311 QTKEQADFAIEALAKATYERMFRWLVLRINKALDKTK----RQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLF 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  501 VRHVFKLEQEEYDLESIDWLHIEF-TDNQEALDMIANR--PMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANYVPPK 577
Cdd:cd14919   387 NHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPK 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  578 N-SHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ--------------ADVAMGAETRKRS 642
Cdd:cd14919   467 QlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKdvdriigldqvagmSETALPGAFKTRK 546
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  643 ---PTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVER 719
Cdd:cd14919   547 gmfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQR 626
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*..
gi 755522197  720 YRVLLPGVKPaykQGDLRG--TCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd14919   627 YEILTPNSIP---KGFMDGkqACVLMIKALELDSNLYRIGQSKVFFR 670
MYSc_Myh1_mammals cd14910
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
109-764 1.64e-135

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: 441.09  E-value: 1.64e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  109 GILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQC 188
Cdd:cd14910     2 AVLYNLKERYAAWMIYT------YSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  189 CIISGESGAGKTESTKLILQFLAAI------------SGQ-HSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIH 255
Cdd:cd14910    76 ILITGESGAGKTVNTKRVIQYFATIavtgekkkeeatSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  256 FNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLG-QAADYNYLAMGNcITCEGRVDSQEYA 334
Cdd:cd14910   156 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITtNPYDYAFVSQGE-ITVPSIDDQEELM 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  335 NIRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFENL---DACEVLfspslATAASLLEVNPPDLMSCL------ 405
Cdd:cd14910   235 ATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQaepDGTEVA-----DKAAYLQNLNSADLLKALcyprvk 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  406 TSRTLITRGETVstplsrEQALDVRDAFVKGIYGRLFVWIVEKINAAiykpppLEVKNSRRS-IGLLDIFGFENFTVNSF 484
Cdd:cd14910   310 VGNEYVTKGQTV------QQVYNAVGALAKAVYDKMFLWMVTRINQQ------LDTKQPRQYfIGVLDIAGFEIFDFNSL 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  485 EQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLN 564
Cdd:cd14910   378 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLY 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  565 SQHKLNANYV----PPKNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAET-- 638
Cdd:cd14910   458 EQHLGKSNNFqkpkPAKGKVEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEgg 537
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  639 -----RKRSP---TLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIR 710
Cdd:cd14910   538 gkkggKKKGSsfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSR 617
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....
gi 755522197  711 YSFVEFVERYRVLLPGVKPAYKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd14910   618 ILYADFKQRYKVLNASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh4 cd14915
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...
109-764 1.81e-134

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: 438.01  E-value: 1.81e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  109 GILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQC 188
Cdd:cd14915     2 AVLYNLKERYAAWMIYT------YSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  189 CIISGESGAGKTESTKLILQFLAAI------------SGQ-HSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIH 255
Cdd:cd14915    76 ILITGESGAGKTVNTKRVIQYFATIavtgekkkeeaaSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  256 FNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLG-QAADYNYLAMGNcITCEGRVDSQEYA 334
Cdd:cd14915   156 FGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITtNPYDFAFVSQGE-ITVPSIDDQEELM 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  335 NIRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFENL---DACEVLfspslATAASLLEVNPPDLMSCLTSRTLI 411
Cdd:cd14915   235 ATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQaepDGTEVA-----DKAAYLTSLNSADLLKALCYPRVK 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  412 TRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAiykpppLEVKNSRRS-IGLLDIFGFENFTVNSFEQLCIN 490
Cdd:cd14915   310 VGNEYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQ------LDTKQPRQYfIGVLDIAGFEIFDFNSLEQLCIN 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  491 FANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLN 570
Cdd:cd14915   384 FTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGK 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  571 ANYV----PPKNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAE--------T 638
Cdd:cd14915   464 SNNFqkpkPAKGKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEggggkkggK 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  639 RKRSP--TLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEF 716
Cdd:cd14915   544 KKGSSfqTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADF 623
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*...
gi 755522197  717 VERYRVLLPGVKPAYKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd14915   624 KQRYKVLNASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh13 cd14923
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...
109-764 6.16e-134

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: 436.42  E-value: 6.16e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  109 GILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQC 188
Cdd:cd14923     2 AVLYNLKERYAAWMIYT------YSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  189 CIISGESGAGKTESTKLILQFLAAI------------SGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHF 256
Cdd:cd14923    76 ILITGESGAGKTVNTKRVIQYFATIavtgdkkkeqqpGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  257 NKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLG-QAADYNYLAMGNcITCEGRVDSQEYAN 335
Cdd:cd14923   156 GATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIStNPFDFPFVSQGE-VTVASIDDSEELLA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  336 IRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFENL---DACEVLfspslATAASLLEVNPPDLMSCLTSRTLIT 412
Cdd:cd14923   235 TDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQaepDGTEVA-----DKAGYLMGLNSAEMLKGLCCPRVKV 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  413 RGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAiykpppLEVKNSRRS-IGLLDIFGFENFTVNSFEQLCINF 491
Cdd:cd14923   310 GNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQ------LDTKQPRQYfIGVLDIAGFEIFDFNSLEQLCINF 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  492 ANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNA 571
Cdd:cd14923   384 TNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKS 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  572 NYV----PPKNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ----ADVAMGAETRKRSP 643
Cdd:cd14923   464 NNFqkpkPAKGKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSnyagAEAGDSGGSKKGGK 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  644 -------TLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEF 716
Cdd:cd14923   544 kkgssfqTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADF 623
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*...
gi 755522197  717 VERYRVLLPGVKPAYKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd14923   624 KQRYRILNASAIPEGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
MYSc_Myh19 cd15896
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...
108-764 7.08e-133

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: 433.72  E-value: 7.08e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQ 187
Cdd:cd15896     1 ASVLHNLKERYYSGLIYT------YSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  188 CCIISGESGAGKTESTKLILQFLAAISGQHSW-------------IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDI 254
Cdd:cd15896    75 SILCTGESGAGKTENTKKVIQYLAHVASSHKTkkdqnslalshgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  255 HFNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNcITCEGRVDSQEYA 334
Cdd:cd15896   155 NFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGN-VTIPGQQDKDLFT 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  335 NIRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARtfENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRG 414
Cdd:cd15896   234 ETMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKE--RHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGR 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  415 ETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPplevKNSRRSIGLLDIFGFENFTVNSFEQLCINFANE 494
Cdd:cd15896   312 DYVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTK----RQGASFIGILDIAGFEIFELNSFEQLCINYTNE 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  495 HLQQFFVRHVFKLEQEEYDLESIDWLHIEF-TDNQEALDMIAN--RPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNA 571
Cdd:cd15896   388 KLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIEKpaSPPGILALLDEECWFPKATDKSFVEKVLQEQGTHP 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  572 NYVPPKN-SHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ--------------ADVAMGA 636
Cdd:cd15896   468 KFFKPKKlKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKdvdrivgldkvsgmSEMPGAF 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  637 ETRK-RSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVE 715
Cdd:cd15896   548 KTRKgMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 627
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755522197  716 FVERYRVLLPGVKPaykQG--DLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd15896   628 FRQRYEILTPNAIP---KGfmDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
MYSc_Myo25 cd14886
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...
110-764 4.40e-130

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: 424.68  E-value: 4.40e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  110 ILRNlliRYRDHLIYTscggrtYTGSILVAVNPYQLLS-IYSPEHIRQY--TNKKIG---EMPPHIFAIADNCYFNMKRN 183
Cdd:cd14886     6 ILRD---RFAKDKIYT------YAGKLLVALNPFKQIRnLYGTEVIGRYrqADTSRGfpsDLPPHSYAVAQSALNGLISD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  184 NRDQCCIISGESGAGKTESTKLILQFLAAISGQHS-WIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAI 262
Cdd:cd14886    77 GISQSCIVSGESGAGKTETAKQLMNFFAYGHSTSStDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  263 EGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCEGRVDSQEYANIRSAMKV 342
Cdd:cd14886   157 KGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  343 lMFTDTENWEISKLLAAILHMGNLQYEARTFENLD-ACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPL 421
Cdd:cd14886   237 -LFSKNEIDSFYKCISGILLAGNIEFSEEGDMGVInAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPV 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  422 SREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPpplevKNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFV 501
Cdd:cd14886   316 TQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFD-----ADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFI 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  502 RHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKlNANYVPPKNShE 581
Cdd:cd14886   391 NQVFKSEIQEYEIEGIDHSMITFTDNSNVLAVFDKPNLSIFSFLEEQCLIQTGSSEKFTSSCKSKIK-NNSFIPGKGS-Q 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  582 TQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAETRKRspTLSSQFKRSLELLMRTLG 661
Cdd:cd14886   469 CNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNMKGK--FLGSTFQLSIDQLMKTLS 546
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  662 ACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPGVKPAYKQG-DLRGTC 740
Cdd:cd14886   547 ATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILISHNSSSQNAGeDLVEAV 626
                         650       660
                  ....*....|....*....|....
gi 755522197  741 QRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd14886   627 KSILENLGIPCSDYRIGKTKVFLR 650
MYSc_Myh14_mammals cd14930
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...
108-764 4.06e-125

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: 411.03  E-value: 4.06e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQ 187
Cdd:cd14930     1 ASVLHNLRERYYSGLIYT------YSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  188 CCIISGESGAGKTESTKLILQFLAAIS---------GQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNK 258
Cdd:cd14930    75 SILCTGESGAGKTENTKKVIQYLAHVAsspkgrkepGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  259 RGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCiTCEGRvDSQEYANIRS 338
Cdd:cd14930   155 AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPS-SSPGQ-ERELFQETLE 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  339 AMKVLMFTDTENWEISKLLAAILHMGNLQYEARtfENLDACEVLFSPSLATAASLLEVNPPDL-MSCLTSRTLITRgETV 417
Cdd:cd14930   233 SLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRE--RNTDQATMPDNTAAQKLCRLLGLGVTDFsRALLTPRIKVGR-DYV 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  418 STPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPplevKNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQ 497
Cdd:cd14930   310 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSP----RQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQ 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  498 QFFVRHVFKLEQEEYDLESIDWLHIEF-TDNQEALDMIaNRPMN---VISLIDEESKFPKGTDATMLHKLNSQHKLNANY 573
Cdd:cd14930   386 QLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLI-ERPANppgLLALLDEECWFPKATDKSFVEKVAQEQGGHPKF 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  574 VPPKN-SHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ--------------ADVAMGAET 638
Cdd:cd14930   465 QRPRHlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdvegivgleqvsslGDGPPGGRP 544
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  639 RK-RSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFV 717
Cdd:cd14930   545 RRgMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFR 624
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*....
gi 755522197  718 ERYRVLLPGVKPaykQG--DLRGTCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd14930   625 QRYEILTPNAIP---KGfmDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
117-764 4.82e-117

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: 387.25  E-value: 4.82e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  117 RYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQY---TNKKIGEMPPHIFAIADNCYFNMKRNNRDQCCIISG 193
Cdd:cd14878    10 RFGNNQIYT------FIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFILSG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  194 ESGAGKTESTKLILQFLAAISG-QHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHF-NKRGAIEGAKIEQYL 271
Cdd:cd14878    84 ERGSGKTEASKQIMKHLTCRASsSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARIYTYM 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  272 LEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYL---AMGNCITCEGRVDSQEYANIRSAMKVLMFTdt 348
Cdd:cd14878   164 LEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLnqtMREDVSTAERSLNREKLAVLKQALNVVGFS-- 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  349 eNWEISKL---LAAILHMGNLQYEARTfenlDACEVLFS--PSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSR 423
Cdd:cd14878   242 -SLEVENLfviLSAILHLGDIRFTALT----EADSAFVSdlQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTI 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  424 EQALDVRDAFVKGIYGRLFVWIVEKINAAIYK------PPPLEvknsrrsIGLLDIFGFENFTVNSFEQLCINFANEHLQ 497
Cdd:cd14878   317 QIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSqdeqksMQTLD-------IGILDIFGFEEFQKNEFEQLCVNMTNEKMH 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  498 QFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEA-LDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQ---HKLNANY 573
Cdd:cd14878   390 HYINEVLFLQEQTECVQEGVTMETAYSPGNQTGvLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLlesSNTNAVY 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  574 VPPKN--------SHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAmgaetrkrspTL 645
Cdd:cd14878   470 SPMKDgngnvalkDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLV----------TI 539
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  646 SSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYR---- 721
Cdd:cd14878   540 ASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKplad 619
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|...
gi 755522197  722 VLLPGVKPAYKQGDLRGTCQRMaeavlgTHDDWQIGKTKIFLK 764
Cdd:cd14878   620 TLLGEKKKQSAEERCRLVLQQC------KLQGWQMGVRKVFLK 656
MYSc_Myo38 cd14899
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...
108-735 1.14e-114

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: 382.52  E-value: 1.14e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQ---------LLSIYSPEHIRQYTNKKIGEMP--PHIFAIADNC 176
Cdd:cd14899     1 ASILNALRLRYERHAIYT------HIGDILISINPFQdlpqlygdeILRGYAYDHNSQFGDRVTSTDPrePHLFAVARAA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  177 YFNMKRNNRDQCCIISGESGAGKTESTKLILQFLAAISG------------------QHSWIEQQVLEATPILEAFGNAK 238
Cdd:cd14899    75 YIDIVQNGRSQSILISGESGAGKTEATKIIMTYFAVHCGtgnnnltnsesisppaspSRTTIEEQVLQSNPILEAFGNAR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  239 TIRNDNSSRFGKYIDIHF-NKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEG----MNEEEKKKLGL-GQAAD 312
Cdd:cd14899   155 TVRNDNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALsGGPQS 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  313 YNYLAMGNCITC-EGRVDSQEYANIRSAMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFEN-----LDACEVLFSPS 386
Cdd:cd14899   235 FRLLNQSLCSKRrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKGddtvfADEARVMSSTT 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  387 -----LATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYK--PPPL 459
Cdd:cd14899   315 gafdhFTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRqaSAPW 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  460 EV--------KNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEAL 531
Cdd:cd14899   395 GAdesdvddeEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACL 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  532 DMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANY----VPPKNSHETQFGINHFAGVVYYESQGFLEKNRDT 607
Cdd:cd14899   475 ELFEHRPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHphfrSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDS 554
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  608 LHGDIIQLVHSSRNKFIKQIFQADV-----------AMGAETRKRSPT------LSSQFKRSLELLMRTLGACQPFFVRC 670
Cdd:cd14899   555 FCESAAQLLAGSSNPLIQALAAGSNdedangdseldGFGGRTRRRAKSaiaavsVGTQFKIQLNELLSTVRATTPRYVRC 634
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755522197  671 IKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPGVkpaYKQGD 735
Cdd:cd14899   635 IKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYRRVLLSL---YKWGD 696
MYSc_Myo12 cd14874
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...
108-764 2.61e-110

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: 366.89  E-value: 2.61e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDhliytscgGRTYT--GSILVAVNPYQLLSIYSPEHIRQYtnkkigemppHIFAIADNCYFNMKRN-N 184
Cdd:cd14874     1 AGIAQNLHERFKK--------GQTYTkaSNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMsS 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  185 RDQCCIISGESGAGKTESTKLILQFLAAiSGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFnKRGAIEG 264
Cdd:cd14874    63 NAESIVFGGESGSGKSYNAFQVFKYLTS-QPKSKVTTKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLTG 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  265 AKIEQYL-LEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCEgRVDSQEYANIRSAMKVL 343
Cdd:cd14874   141 LNLKYTVpLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENI-QSDVNHFKHLEDALHVL 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  344 MFTDTENWEISKLLAAILHMGNLQYEARTFENL--DACEVLFSPSLATAASLLEVNPPDLMSCLTSRTlitrgeTVSTPL 421
Cdd:cd14874   220 GFSDDHCISIYKIISTILHIGNIYFRTKRNPNVeqDVVEIGNMSEVKWVAFLLEVDFDQLVNFLLPKS------EDGTTI 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  422 SREQALDVRDAFVKGIYGRLFVWIVEKINAAiYKPPplevkNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFV 501
Cdd:cd14874   294 DLNAALDNRDSFAMLIYEELFKWVLNRIGLH-LKCP-----LHTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLFV 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  502 RHVFKLEQEEYDLE--SIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANYVPPKNS 579
Cdd:cd14874   368 KHSFHDQLVDYAKDgiSVDYKVPNSIENGKTVELLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARNK 447
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  580 HETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQadvAMGAETRKRSPTLSSQFKRSLELLMRT 659
Cdd:cd14874   448 ERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE---SYSSNTSDMIVSQAQFILRGAQEIADK 524
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  660 LGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPgvkpaykqGDLrGT 739
Cdd:cd14874   525 INGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLP--------GDI-AM 595
                         650       660       670
                  ....*....|....*....|....*....|...
gi 755522197  740 CQRMAEAV--------LGTHDDWQIGKTKIFLK 764
Cdd:cd14874   596 CQNEKEIIqdilqgqgVKYENDFKIGTEYVFLR 628
MYSc_Myo37 cd14898
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...
110-725 1.79e-103

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: 344.96  E-value: 1.79e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  110 ILRNLLIRYRDHLIYTSCGgrtytgSILVAVNPYQllSIYSPEHIRQYTnKKIGEMPPHIFAIADNCYFNMKRNNrDQCC 189
Cdd:cd14898     3 TLEILEKRYASGKIYTKSG------LVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVHG-NQTI 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  190 IISGESGAGKTESTKLILQFLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNkrGAIEGAKIEQ 269
Cdd:cd14898    73 VISGESGSGKTENAKLVIKYLVERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFET 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  270 YLLEKSRVCRQAPDERNYHVFY--CMLEGMNEEEkkklglgQAADYNYLAmGNcitCEGRVD-SQEYANIRSAMKVLMFT 346
Cdd:cd14898   151 YLLEKSRVTHHEKGERNFHIFYqfCASKRLNIKN-------DFIDTSSTA-GN---KESIVQlSEKYKMTCSAMKSLGIA 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  347 DTEnwEISKLLAAILHMGNLQYeartfeNLDACEVLFS-PSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQ 425
Cdd:cd14898   220 NFK--SIEDCLLGILYLGSIQF------VNDGILKLQRnESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQ 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  426 ALDVRDAFVKGIYGRLFVWIVEKINAAIYkppplevKNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHVF 505
Cdd:cd14898   292 ARTIRNSMARLLYSNVFNYITASINNCLE-------GSGERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMF 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  506 KLEQEEYDLESIDWLHIEFTDNQEALDMIaNRPMNVISLIDEESKFPKGTDATMLHKLnsqHKLNANYVppKNSHETQFG 585
Cdd:cd14898   365 RAKQGMYKEEGIEWPDVEFFDNNQCIRDF-EKPCGLMDLISEESFNAWGNVKNLLVKI---KKYLNGFI--NTKARDKIK 438
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  586 INHFAGVVYYESQGFLEKNRDTLHGDIIQlvhssrnkfikqifqaDVAMGAETRKRSptLSSQFKRSLELLMRTLGACQP 665
Cdd:cd14898   439 VSHYAGDVEYDLRDFLDKNREKGQLLIFK----------------NLLINDEGSKED--LVKYFKDSMNKLLNSINETQA 500
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  666 FFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLP 725
Cdd:cd14898   501 KYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGI 560
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
127-763 1.66e-101

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: 341.32  E-value: 1.66e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  127 CGGRTYT--GSILVAVNPYQLLSiySPEHIRQYTNKKIGempPHIFAIADNCYFNMKRNNRDQCCIISGESGAGKTESTK 204
Cdd:cd14881    12 YAKEFFTnvGPILLSVNPYRDVG--NPLTLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSGTSGSGKTYASM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  205 LILQFLAAISGQHSWIE--QQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKrGAIEGAKIEQYLLEKSRVCRQAP 282
Cdd:cd14881    87 LLLRQLFDVAGGGPETDafKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-GALYRTKIHCYFLDQTRVIRPLP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  283 DERNYHVFYCMLEGMNEEEKKKLGLG--QAADYNYLAMGNcITCEGRVDSQEYANIRSAMKVL--MFTDtenweISKLLA 358
Cdd:cd14881   166 GEKNYHIFYQMLAGLSQEERVKLHLDgySPANLRYLSHGD-TRQNEAEDAARFQAWKACLGILgiPFLD-----VVRVLA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  359 AILHMGNLQYEARTFENLDaceVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRDAFVKGIY 438
Cdd:cd14881   240 AVLLLGNVQFIDGGGLEVD---VKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKSVCDANMSNMTRDALAKALY 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  439 GRLFVWIVEKINAAIYKPPPLEVKNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESID 518
Cdd:cd14881   317 CRTVATIVRRANSLKRLGSTLGTHATDGFIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQ 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  519 W-LHIEFTDNQEALDMIANRPMNVISLIDEESKfPKGTDATMLHKLNSQHKLNANYVPPKNSHETQFGINHFAGVVYYES 597
Cdd:cd14881   397 CeVEVDYVDNVPCIDLISSLRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLFEAKPQDDRMFGIRHFAGRVVYDA 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  598 QGFLEKNRDTLHGDIIQLvhssrnkFIKQIFQADVAmgaetrkrspTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFK 677
Cdd:cd14881   476 SDFLDTNRDVVPDDLVAV-------FYKQNCNFGFA----------THTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTE 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  678 KPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPgVKPAYKQGDLRGTCQRMAEAVLGTHDD---- 753
Cdd:cd14881   539 TPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAP-FRLLRRVEEKALEDCALILQFLEAQPPskls 617
                         650
                  ....*....|....*
gi 755522197  754 -----WQIGKTKIFL 763
Cdd:cd14881   618 svstsWALGKRHIFL 632
MYSc_Myo24A cd14937
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
108-764 5.15e-101

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: 340.07  E-value: 5.15e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIyspeHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQ 187
Cdd:cd14937     1 AEVLNMLALRYKKNYIYT------IAEPMLISINPYQVIDV----DINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQ 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  188 CCIISGESGAGKTESTKLILQFLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKI 267
Cdd:cd14937    71 SIIISGESGSGKTEASKLVIKYYLSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  268 EQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCEGRvDSQEYANIRSAMKVLMFTD 347
Cdd:cd14937   151 EIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEID-DAKDFGNLMISFDKMNMHD 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  348 TENwEISKLLAAILHMGNLQYEARTFENLDACEVLFSPSLAT---AASLLEVNPPDLMSCLTSRTLITRGETVSTPLSRE 424
Cdd:cd14937   230 MKD-DLFLTLSGLLLLGNVEYQEIEKGGKTNCSELDKNNLELvneISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVE 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  425 QALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPPLEvknsrRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHV 504
Cdd:cd14937   309 ESVSICKSISKDLYNKIFSYITKRINNFLNNNKELN-----NYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIV 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  505 FKLEQEEYDLESIDWLHIEFTDNQEALDMIANRpMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANYVPPKNSHETQF 584
Cdd:cd14937   384 YEKETELYKAEDILIESVKYTTNESIIDLLRGK-TSIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINKNF 462
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  585 GINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQaDVAMgAETRKRSPTLSSQFKRSLELLMRTLGACQ 664
Cdd:cd14937   463 VIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYE-DVEV-SESLGRKNLITFKYLKNLNNIISYLKSTN 540
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  665 PFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAgYPIRYSFVEFVERYRVLLPGVKPAYKQGDlRGTCQRMA 744
Cdd:cd14937   541 IYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNISFF-FQYKYTFDVFLSYFEYLDYSTSKDSSLTD-KEKVSMIL 618
                         650       660
                  ....*....|....*....|
gi 755522197  745 EAVLGThDDWQIGKTKIFLK 764
Cdd:cd14937   619 QNTVDP-DLYKVGKTMVFLK 637
MYSc_Myo26 cd14887
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...
108-764 1.00e-99

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: 339.32  E-value: 1.00e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDhlIYTSCGGR----TYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRN 183
Cdd:cd14887     1 PNLLENLYQRYNK--AYINKENRnciyTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  184 NRDQCCIISGESGAGKTESTKLILQFLAAISG-QH----SWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNK 258
Cdd:cd14887    79 RRSQSILISGESGAGKTETSKHVLTYLAAVSDrRHgadsQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  259 RGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFY--CMLEGMNEEEKKKLGLGqaadYNYLAMGNCITcegrvdsqeyani 336
Cdd:cd14887   159 RGKLTRASVATYLLANERVVRIPSDEFSFHIFYalCNAAVAAATQKSSAGEG----DPESTDLRRIT------------- 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  337 rSAMKVLMFTDTENWEISKLLAAILHMGNLQY--------------EARTFENLDACEVLFSPS---------------- 386
Cdd:cd14887   222 -AAMKTVGIGGGEQADIFKLLAAILHLGNVEFttdqepetskkrklTSVSVGCEETAADRSHSSevkclssglkvteasr 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  387 --LATAASLLEVNPPD-----LMSCLTSRTLitrGETVSTpLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYK---- 455
Cdd:cd14887   301 khLKTVARLLGLPPGVegeemLRLALVSRSV---RETRSF-FDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRsakp 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  456 -----PPPLEVKNSRRSIGLLDIFGFENF---TVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDN 527
Cdd:cd14887   377 sesdsDEDTPSTTGTQTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAFP 456
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  528 QE--ALDMIANRPMNVISLI-------------------------DEESKFP---KGTDATML--HKLNSQHKLNANY-- 573
Cdd:cd14887   457 FSfpLASTLTSSPSSTSPFSptpsfrsssafatspslpsslsslsSSLSSSPpvwEGRDNSDLfyEKLNKNIINSAKYkn 536
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  574 -VPPKNSHETQFGINHFAGVVYYESQGFLEKNRDTLHGDI----------IQLVHSSRNKFIKQIfqadvamgaetRKRS 642
Cdd:cd14887   537 iTPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELerlflacstyTRLVGSKKNSGVRAI-----------SSRR 605
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  643 PTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRV 722
Cdd:cd14887   606 STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYET 685
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|...
gi 755522197  723 LLP-GVKPAYKQGDLrgtCQRMAEAVLGTHDDWQIGKTKIFLK 764
Cdd:cd14887   686 KLPmALREALTPKMF---CKIVLMFLEINSNSYTFGKTKIFFR 725
MYSc_Myo18 cd01386
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...
108-764 3.72e-93

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: 318.87  E-value: 3.72e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQ 187
Cdd:cd01386     1 SSVLHTLRQRYGANLIHT------YAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  188 CCIISGESGAGKTESTKLILQFLAAISGQHSW-IEQQVLEAT-PILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGA 265
Cdd:cd01386    75 SIVLLGRSGSGKTTNCRHILEYLVTAAGSVGGvLSVEKLNAAlTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  266 KIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCEGRVD-SQEYANIRSAMKVLM 344
Cdd:cd01386   155 SIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKQKaAAAFSKLQAAMKTLG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  345 FTDTENWEISKLLAAILHMGNlqyeARTFENLDACEVLFS-PSLAT-AASLLEVNPPDLMSCLTSRTLITRGETVSTPLS 422
Cdd:cd01386   235 ISEEEQRAIWSILAAIYHLGA----AGATKAASAGRKQFArPEWAQrAAYLLGCTLEELSSAIFKHHLSGGPQQSTTSSG 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  423 REQ------------ALDVRDAFVKGIYGRLFVWIVEKINAAIykppplevKNSRR---SIGLLDIFGFEN------FTV 481
Cdd:cd01386   311 QESparsssggpkltGVEALEGFAAGLYSELFAAVVSLINRSL--------SSSHHstsSITIVDTPGFQNpahsgsQRG 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  482 NSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDwLHIEFTDN--QEALDMIANRPMNVIS--------------LI 545
Cdd:cd01386   383 ATFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVE-VDFDLPELspGALVALIDQAPQQALVrsdlrdedrrgllwLL 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  546 DEESKFPKGTDATMLHKLNSQH----KLNANYVPPKNSHETQFGINHFAGV--VYYESQGFLEKNRDTL-HGDIIQLVHS 618
Cdd:cd01386   462 DEEALYPGSSDDTFLERLFSHYgdkeGGKGHSLLRRSEGPLQFVLGHLLGTnpVEYDVSGWLKAAKENPsAQNATQLLQE 541
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  619 SRNKFikqifqadvamgAETRKRSPTLssQFKRSLELLMRTLGACQPFFVRCIKPN------------EFKKPMLFDRHL 686
Cdd:cd01386   542 SQKET------------AAVKRKSPCL--QIKFQVDALIDTLRRTGLHFVHCLLPQhnagkderstssPAAGDELLDVPL 607
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  687 CVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLPGVKPAYKQGDLRGTCQRMAEAVLGTHD----DWQIGKTKIF 762
Cdd:cd01386   608 LRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGLNSEVADERKAVEELLEELDleksSYRIGLSQVF 687

                  ..
gi 755522197  763 LK 764
Cdd:cd01386   688 FR 689
MYSc_Myo23 cd14884
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ...
108-721 4.22e-93

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: 318.39  E-value: 4.22e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  108 AGILRNLLIRYRDHLIYTscggrtYTGSILVAVNPY-QLLSIYSPEHIRQYTNKKIGE-------MPPHIFAIADNCYFN 179
Cdd:cd14884     1 PNVLQNLKNRYLKNKIYT------FHASLLLALNPYkPLKELYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  180 MKRNNRDQCCIISGESGAGKTESTKLILQFLAAISGQHSWIE--QQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFN 257
Cdd:cd14884    75 MRGKLKRQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTEriDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  258 KR---------GAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQ-----------AADYNYLA 317
Cdd:cd14884   155 EVentqknmfnGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRncgvygllnpdESHQKRSV 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  318 MGNCITCEGRVD------SQEYANIRSAMKVLMFTDTENWEISK---LLAAILHMGNLQYEArtfenldacevlfspsla 388
Cdd:cd14884   235 KGTLRLGSDSLDpseeekAKDEKNFVALLHGLHYIKYDERQINEffdIIAGILHLGNRAYKA------------------ 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  389 tAASLLEVNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPPLEVKNSRRS- 467
Cdd:cd14884   297 -AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDESDNEDIy 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  468 ------IGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIAnrpmNV 541
Cdd:cd14884   376 sineaiISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIA----KI 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  542 ISLIDEESKFP----KGTDA------------TMLHKLNSQHKLN---ANYVPPKNS-HETQFGINHFAGVVYYESQGFL 601
Cdd:cd14884   452 FRRLDDITKLKnqgqKKTDDhffryllnnerqQQLEGKVSYGFVLnhdADGTAKKQNiKKNIFFIRHYAGLVTYRINNWI 531
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  602 EKNRDTLHGDIIQLVHSSRNKFIKQifqadvAMGAETRKRSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPML 681
Cdd:cd14884   532 DKNSDKIETSIETLISCSSNRFLRE------ANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNT 605
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|
gi 755522197  682 FDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYR 721
Cdd:cd14884   606 FKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKETAAALK 645
MYSc_Myo44 cd14905
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...
117-764 6.01e-87

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: 300.09  E-value: 6.01e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  117 RYRDHLIYTscggrtYTGSILVAVNPYQLLS-IYSPEHIRQYTNKKigEMPPHIFAIADNCYFNMKRNNRDQCCIISGES 195
Cdd:cd14905    10 RYKKEIIYT------YIGPILVSVNPLRYLPfLHSQELVRNYNQRR--GLPPHLFALAAKAISDMQDFRRDQLIFIGGES 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  196 GAGKTESTKLILQFLAAISGQHS-WIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYLLEK 274
Cdd:cd14905    82 GSGKSENTKIIIQYLLTTDLSRSkYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  275 SRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTDTENWEIS 354
Cdd:cd14905   162 NRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIF 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  355 KLLAAILHMGNLQYeartFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTlitrgetvSTPLSreQALDVRDAFV 434
Cdd:cd14905   242 KTLSFIIILGNVTF----FQKNGKTEVKDRTLIESLSHNITFDSTKLENILISDR--------SMPVN--EAVENRDSLA 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  435 KGIYGRLFVWIVEKINAAIyKPpplevKNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDL 514
Cdd:cd14905   308 RSLYSALFHWIIDFLNSKL-KP-----TQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQT 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  515 ESIDWLH-IEFTDNQEALDMIAnrpmNVISLIDEESKFPKGTDATMLHKLnsQHKLNANYVPPKNSHetQFGINHFAGVV 593
Cdd:cd14905   382 ERIPWMTpISFKDNEESVEMME----KIINLLDQESKNINSSDQIFLEKL--QNFLSRHHLFGKKPN--KFGIEHYFGQF 453
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  594 YYESQGFLEKNRDtlhgDIIQLVHS-SRNKFIKQIFQAD-----VAMGAETRKRSPTLSSQFKRSLELLMRTLGA----- 662
Cdd:cd14905   454 YYDVRGFIIKNRD----EILQRTNVlHKNSITKYLFSRDgvfniNATVAELNQMFDAKNTAKKSPLSIVKVLLSCgsnnp 529
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  663 --------------------------------------------CQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMME 698
Cdd:cd14905   530 nnvnnpnnnsgggggggnsgggsgsggstyttysstnkainnsnCDFHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLE 609
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  699 TIRIRHAGYPIRYSFVEFVERYRVLLPgvkpayKQGDLRGTCQRMAEAVLGTHD----DWQIGKTKIFLK 764
Cdd:cd14905   610 TTRIQRFGYTIHYNNKIFFDRFSFFFQ------NQRNFQNLFEKLKENDINIDSilppPIQVGNTKIFLR 673
MYSc_Myo21 cd14882
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...
110-764 7.71e-83

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: 287.02  E-value: 7.71e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  110 ILRNLLIRYRDhliytscgGRTYT--GSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQ 187
Cdd:cd14882     3 ILEELRHRYLM--------GESYTfiGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  188 CCIISGESGAGKTESTKLILQFLAAISGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKI 267
Cdd:cd14882    75 HIILSGESYSGKTTNARLLIKHLCYLGDGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  268 EQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEK-KKLGLGQAADYNYLAMGNCITCEG----RVDSQE----YANIRS 338
Cdd:cd14882   155 WMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNRlKEYNLKAGRNYRYLRIPPEVPPSKlkyrRDDPEGnverYKEFEE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  339 AMKVLMFTDTENWEISKLLAAILHMGNLQY-EARTFENLDACEVlfspsLATAASLLEVNPPDLMSCLTSRTLITRGETV 417
Cdd:cd14882   235 ILKDLDFNEEQLETVRKVLAAILNLGEIRFrQNGGYAELENTEI-----ASRVAELLRLDEKKFMWALTNYCLIKGGSAE 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  418 STPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPplEVKNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQ 497
Cdd:cd14882   310 RRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR--AVFGDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQMQ 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  498 QFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEESKfpKGTDATMLhkLNSQHKLNANYVPPK 577
Cdd:cd14882   388 YHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDASR--SCQDQNYI--MDRIKEKHSQFVKKH 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  578 NSHEtqFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQadvamGAETRKRSpTLSSQFK-RSLELL 656
Cdd:cd14882   464 SAHE--FSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFT-----NSQVRNMR-TLAATFRaTSLELL 535
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  657 mRTL----GACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLlpgvkpAYK 732
Cdd:cd14882   536 -KMLsigaNSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFL------AFD 608
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....
gi 755522197  733 qgdlrgtcqrMAEAVLGTHDD------------WQIGKTKIFLK 764
Cdd:cd14882   609 ----------FDETVEMTKDNcrlllirlkmegWAIGKTKVFLK 642
MYSc_Myo32 cd14893
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...
111-763 6.44e-80

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: 281.47  E-value: 6.44e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  111 LRNLLIRYRDHLIYTscggrtYTGSILVAVNPYQLLSIYSPEHIRQYTNKK----------IGEMPPHIFAIADNCYFNM 180
Cdd:cd14893     4 LYTLRARYRMEQVYT------WVDRVLVGVNPVTPLPIYTPDHMQAYNKSReqtplyekdtVNDAPPHVFALAQNALRCM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  181 KRNNRDQCCIISGESGAGKTESTKLILQFLAAI-------------SGQHSWIEQQVLEATPILEAFGNAKTIRNDNSSR 247
Cdd:cd14893    78 QDAGEDQAVILLGGMGAGKSEAAKLIVQYLCEIgdeteprpdsegaSGVLHPIGQQILHAFTILEAFGNAATRQNRNSSR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  248 FGKYIDIHFNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEE--KKKLGLGQAA-DYNYLAMGNCITC 324
Cdd:cd14893   158 FAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDPtlRDSLEMNKCVnEFVMLKQADPLAT 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  325 EGRVDSQEYANIRSAMKVLMFTDTENWEISKLLAAILHMGNLQY-------------EARTFENLDACEVLFSPSLATAA 391
Cdd:cd14893   238 NFALDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggksvggaNSTTVSDAQSCALKDPAQILLAA 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  392 SLLEVNPPDLMSCLTSRTLITR--GETVST--PLSREQALDVRDAFVKGIYGRLFVWIVEKINAAI------YKPPPLeV 461
Cdd:cd14893   318 KLLEVEPVVLDNYFRTRQFFSKdgNKTVSSlkVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdrYEKSNI-V 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  462 KNSrRSIGLLDIFGFENFT--VNSFEQLCINFANEHLQQFFVRHVFK-----LEQEEYDLES--IDWLHIEFTDNQE-AL 531
Cdd:cd14893   397 INS-QGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrlTVNSNVDITSEQEkCL 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  532 DMIANRPMNVISLI----------DEE--SKFPKGTDAT-MLHKLNSQHKLNANYVPPKNSHETQFGINHFAGVVYYESQ 598
Cdd:cd14893   476 QLFEDKPFGIFDLLtenckvrlpnDEDfvNKLFSGNEAVgGLSRPNMGADTTNEYLAPSKDWRLLFIVQHHCGKVTYNGK 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  599 GFLEKNRDTLHGDIIQLVHSSRNKFI-----KQIFQADVAMGAETRKRSPTLSSQFKRSL-------------------- 653
Cdd:cd14893   556 GLSSKNMLSISSTCAAIMQSSKNAVLhavgaAQMAAASSEKAAKQTEERGSTSSKFRKSAssaresknitdsaatdvynq 635
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  654 -ELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVLLpgvkpayk 732
Cdd:cd14893   636 aDALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYKNVC-------- 707
                         730       740       750
                  ....*....|....*....|....*....|....*
gi 755522197  733 qgDLRGTCQRMAEAV--LGTHDD--WQIGKTKIFL 763
Cdd:cd14893   708 --GHRGTLESLLRSLsaIGVLEEekFVVGKTKVYL 740
FERM_C2_MyoVII cd13199
FERM domain C-lobe, repeat 2, of Myosin VII (MyoVII, Myo7); MyoVII, a MyTH-FERM myosin, is an ...
2146-2241 1.94e-66

FERM domain C-lobe, repeat 2, of Myosin VII (MyoVII, Myo7); MyoVII, a MyTH-FERM myosin, is an actin-based motor protein essential for a variety of biological processes in the actin cytoskeleton function. Mutations in MyoVII leads to problems in sensory perception: deafness and blindness in humans (Usher Syndrome), retinal defects and deafness in mice (shaker 1), and aberrant auditory and vestibular function in zebrafish. Myosin VIIAs have plus (barbed) end-directed motor activity on actin filaments and a characteristic actin-activated ATPase activity. MyoVII consists of a conserved spectrin-like, SH3 subdomain N-terminal region, a motor/head region, a neck made of 4-5 IQ motifs, and a tail consisting of a coiled-coil domain, followed by a tandem repeat of myosin tail homology 4 (MyTH4) domains and partial FERM domains that are separated by an SH3 subdomain and are thought to mediate dimerization and binding to other proteins or cargo. Members include: MyoVIIa, MyoVIIb, and MyoVII members that do not have distinct myosin VIIA and myosin VIIB genes. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270020  Cd Length: 96  Bit Score: 219.44  E-value: 1.94e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 2146 GSAFFEVKQTTEPNFPEILLIAINKYGVSLIDPRTKDILTTHPFTKISNWSSGNTYFHITIGNLVRGSKLLCETSLGYKM 2225
Cdd:cd13199     1 GSAFFEVKQTTDPSLPEILLIAINKNGVSLIDPKTKEILATHPFSKISNWSSGNTYFHMTIGNLVRGSKLLCETSLGYKM 80
                          90
                  ....*....|....*.
gi 755522197 2226 DDLLTSYISQMLTAMS 2241
Cdd:cd13199    81 DDLLTSYISLLLSNMK 96
FERM1_F1_Myosin-VII cd17092
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, ...
1292-1390 8.23e-66

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of the myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in the MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the first FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340612  Cd Length: 99  Bit Score: 217.51  E-value: 8.23e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 1292 PIMLPVTFMDGTTKTLLTDSATTARELCNALADKISLKDRFGFSLYIALFDKVSSLGSGSDHVMDAISQCEQYAKEQGAQ 1371
Cdd:cd17092     1 PIMLPVTFMDGSTKTVEVDSATTARELCRQLAEKLGLKDTFGFSLYIALFDKVSSLGSGTDHVMDAISQCEQYAKEKGAQ 80
                          90
                  ....*....|....*....
gi 755522197 1372 ERNAPWRLFFRKEVFTPWH 1390
Cdd:cd17092    81 EREAPWRLYFRKEIFAPWH 99
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
1782-1931 6.44e-64

Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 214535  Cd Length: 152  Bit Score: 214.53  E-value: 6.44e-64
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   1782 HTREPLKQALLKKIlgSEELSQEACMAFVAVLKYMGDYPSKRMRSVNELTDQIFEWALKAEPLKDEAYVQILKQLTDNHI 1861
Cdd:smart00139    1 YTKDPIKTSLLKLE--SDELQKEAVKIFKAILKFMGDIPLPRPDSHLDLVQFILQKGLDHPELRDEIYCQLIKQLTDNPS 78
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755522197   1862 RYSEERGWELLWLCTGLFPPSNILLPHVQRFLQSRKHC----PLAIDCLQRLQKALRNGSRKYPPHLVEVEAIQ 1931
Cdd:smart00139   79 RQSEERGWQLLYLCTSLFPPSERLLPYLLQFLSRRADPgseqGLAKYCLYRLERTLKNGARKQPPSRLELEAIL 152
FERM2_F1_Myosin-VII cd17093
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, ...
1936-2033 1.59e-63

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the second FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340613  Cd Length: 98  Bit Score: 210.94  E-value: 1.59e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 1936 QIFHKVYFPDDTDEAFEVESSTKAKDFCQNIASRLLLKSSEGFSLFVKIADKVISVPENDFFFDFVRHLTDWIKKARPIK 2015
Cdd:cd17093     1 QIFHKVYFPDDTDEAFEVDSSTRARDLCQNIASRLGLKSSEGFSLFVKIADKVISLPEGDFFFDFIRHLTDWIKKARPTK 80
                          90
                  ....*....|....*...
gi 755522197 2016 DGIVPSLTYQVFFMKKLW 2033
Cdd:cd17093    81 DGPKPSLTYQVFFMRKLW 98
MyTH4 smart00139
Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 ...
1052-1288 2.20e-55

Domain in Myosin and Kinesin Tails; Domain present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 214535  Cd Length: 152  Bit Score: 189.88  E-value: 2.20e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   1052 YTRRPLKQPLLYHDDEGDQLAALAVWITILRFMGDLPEPkyhtamsdgsekipvmtkiyetlgkktykrelqalqgeget 1131
Cdd:smart00139    1 YTKDPIKTSLLKLESDELQKEAVKIFKAILKFMGDIPLP----------------------------------------- 39
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   1132 qlpegqkktsvrhklvhltlkkksklteevtkrlndgestvqgnsmledRPTSNLEKLHFIIGNGILRPALRDEIYCQIS 1211
Cdd:smart00139   40 -------------------------------------------------RPDSHLDLVQFILQKGLDHPELRDEIYCQLI 70
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   1212 KQLTHNPSKSSYARGWILVSLCVGCFAPSEKFVKYLRNFIHGGPP-----GYAPYCEERLRRTFVNGTRTQPPSWLELQA 1286
Cdd:smart00139   71 KQLTDNPSRQSEERGWQLLYLCTSLFPPSERLLPYLLQFLSRRADpgseqGLAKYCLYRLERTLKNGARKQPPSRLELEA 150

                    ..
gi 755522197   1287 TK 1288
Cdd:smart00139  151 IL 152
FERM_C1_MyoVII cd13198
FERM domain C-lobe, repeat 1, of Myosin VII (MyoVII/Myo7); MyoVII, a MyTH-FERM myosin, is an ...
1503-1639 4.56e-52

FERM domain C-lobe, repeat 1, of Myosin VII (MyoVII/Myo7); MyoVII, a MyTH-FERM myosin, is an actin-based motor protein essential for a variety of biological processes in the actin cytoskeleton function. Mutations in MyoVII leads to problems in sensory perception: deafness and blindness in humans (Usher Syndrome), retinal defects and deafness in mice (shaker 1), and aberrant auditory and vestibular function in zebrafish. Myosin VIIAs have plus (barbed) end-directed motor activity on actin filaments and a characteristic actin-activated ATPase activity. MyoVII consists of a conserved spectrin-like, SH3 subdomain N-terminal region, a motor/head region, a neck made of 4-5 IQ motifs, and a tail consisting of a coiled-coil domain, followed by a tandem repeat of myosin tail homology 4 (MyTH4) domains and partial FERM domains that are separated by an SH3 subdomain and are thought to mediate dimerization and binding to other proteins or cargo. Members include: MyoVIIa, MyoVIIb, and MyoVII members that do not have distinct myosin VIIA and myosin VIIB genes. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270019  Cd Length: 99  Bit Score: 178.18  E-value: 4.56e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 1503 LLFSRFYEAYKFSGPPLPKSDVIVAVNWTGVYFVDEQEQVLLELSFPEIMAVSSSrecrvllslgcsdlgcatcqsgrag 1582
Cdd:cd13198     1 LLFSRFFEATKFSGPSLPKSEVIIAVNWTGIYFVDEQEQVLLELSFPEITGVSSS------------------------- 55
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755522197 1583 ltpagpcspcwscRGTKMMAPSFTLATIKGDEYTFTSSNAEDIRDLVVTFLEGLRKR 1639
Cdd:cd13198    56 -------------RGKRDGGQSFTLTTIQGEEFVFQSPNAEDIAELVNYFLEGLRKR 99
MYSc_Myo24B cd14938
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
110-763 8.51e-50

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: 190.82  E-value: 8.51e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  110 ILRNLLIRYRDHLIYTScggrtyTGSILVAVNPYQLLSIYSPEHIRQYT-NKKIGEMPPHIFAIADNCYFNMKRNNRDQC 188
Cdd:cd14938     3 VLYHLKERFKNNKFYTK------MGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  189 CIISGESGAGKTESTKLILQFLA----------AISGQHSWIEQQVLEATP--------------ILEAFGNAKTIRNDN 244
Cdd:cd14938    77 IIISGESGSGKSEIAKNIINFIAyqvkgsrrlpTNLNDQEEDNIHNEENTDyqfnmsemlkhvnvVMEAFGNAKTVKNNN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  245 SSRFGKYIDIHFNKRgAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITC 324
Cdd:cd14938   157 SSRFSKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  325 EGRvDSQEYANIRSAMKVLMFTDTENWEISKLLAAILHMGNLQ-----YEARTFENLDACEVLFS--------------- 384
Cdd:cd14938   236 FSD-YSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEivkafRKKSLLMGKNQCGQNINyetilselensedig 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  385 -----PSLATAASLLEVNPPDLMSCLTSRTLITrgETVSTPLSREQALDVR-DAFVKGIYGRLFVWIVEKINAaiyKPPP 458
Cdd:cd14938   315 ldenvKNLLLACKLLSFDIETFVKYFTTNYIFN--DSILIKVHNETKIQKKlENFIKTCYEELFNWIIYKINE---KCTQ 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  459 LEVKNSRRS-IGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDW-LHIEFTDNQEALDMIAN 536
Cdd:cd14938   390 LQNININTNyINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCeYNSENIDNEPLYNLLVG 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  537 RPMNVISLIDEESKFPKGTDATMLHKL-NSQHKLNANYVPPKNSHETQ--FGINHFAGVVYYESQGFLEKNRDTLHGDII 613
Cdd:cd14938   470 PTEGSLFSLLENVSTKTIFDKSNLHSSiIRKFSRNSKYIKKDDITGNKktFVITHSCGDIIYNAENFVEKNIDILTNRFI 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  614 QLVHSSRNKFIKQI---FQADVAMGAETRKRSPTLSSQFK------------------RSLELLMRTLGACQPFFVRCIK 672
Cdd:cd14938   550 DMVKQSENEYMRQFcmfYNYDNSGNIVEEKRRYSIQSALKlfkrrydtknqmavsllrNNLTELEKLQETTFCHFIVCMK 629
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  673 PNEFKKPM-LFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVERYRVllpgvkpayKQGDLRGTCQRMAEAVLGTH 751
Cdd:cd14938   630 PNESKRELcSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDI---------KNEDLKEKVEALIKSYQISN 700
                         730
                  ....*....|..
gi 755522197  752 DDWQIGKTKIFL 763
Cdd:cd14938   701 YEWMIGNNMIFL 712
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
1938-2150 1.91e-46

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 166.32  E-value: 1.91e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   1938 FHKVYFPDDTDEAFEVESSTKAKDFCQNIASRLLLKSSEGFSLFVKIADKVISvpendfffdfvrhltDWIKKARPIKDG 2017
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLR---------------HWLDPAKTLLDQ 65
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   2018 IVPSLTYQVFFMKKLWTTTV--PGKDPMADsIFHYYQELPKYLRGYHKCTREEVLQLGALIYRVKFEEDKSYFPSIPK-- 2093
Cdd:smart00295   66 DVKSEPLTLYFRVKFYPPDPnqLKEDPTRL-NLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHDLRGel 144
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 755522197   2094 LLRELVPQDLIRQVSPDDWKRSIVAYFNKHAGKSKEEAKLAFLKLIFKWPTFGSAFF 2150
Cdd:smart00295  145 SLKRFLPKQLLDSRKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
MyTH4 pfam00784
MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also ...
1189-1286 8.43e-42

MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 459939  Cd Length: 105  Bit Score: 149.27  E-value: 8.43e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  1189 LHFIIGNGILRPALRDEIYCQISKQLTHNPSKSSYARGWILVSLCVGCFAPSEKFVKYLRNFIH-------GGPPGYAPY 1261
Cdd:pfam00784    1 AQNILQKGLKRPELRDEIYCQLIKQTTNNPKPESLLRGWQLLALCLGTFPPSKKLLKYLLKFLKrhaddpsREVGKYAQF 80
                           90       100
                   ....*....|....*....|....*
gi 755522197  1262 CEERLRRTFVNGTRTQPPSWLELQA 1286
Cdd:pfam00784   81 CLKRLKRTLKNGGRKYPPSREEIEA 105
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
136-254 1.53e-39

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: 145.18  E-value: 1.53e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  136 ILVAVNPYQLLSIYSPEH-IRQYTNKKIGEMPPHIFAIADNCYFNMKRNNRDQCCIISGESGAGKTESTKLILQFLAAIS 214
Cdd:cd01363     1 VLVRVNPFKELPIYRDSKiIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 755522197  215 GQH-------SW---------IEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDI 254
Cdd:cd01363    81 FNGinkgeteGWvylteitvtLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
1294-1509 2.52e-38

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 143.20  E-value: 2.52e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   1294 MLPVTFMDGTTKTLLTDSATTARELCNALADKISLKDRFGFSLYIALFDKVsslgsgsdhvmdaISQCEQYAKEQGAQER 1373
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDED-------------LRHWLDPAKTLLDQDV 67
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   1374 N-APWRLFFRKEVFTPWHN-PSEDNVATNLIYQQVVRGVKFGEYRCEKEdDLAELASQQYFVDYG---SEMILERLLSLV 1448
Cdd:smart00295   68 KsEPLTLYFRVKFYPPDPNqLKEDPTRLNLLYLQVRNDILEGRLPCPEE-EALLLAALALQAEFGdydEELHDLRGELSL 146
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755522197   1449 PTYIPDREITPLKnLEKWAQLAIAAHKKGIYaQRRTDSqKVKedVVNYARfKWPLLFSRFY 1509
Cdd:smart00295  147 KRFLPKQLLDSRK-LKEWRERIVELHKELIG-LSPEEA-KLK--YLELAR-KLPTYGVELF 201
MyTH4 pfam00784
MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also ...
1831-1929 2.78e-37

MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also present in 3 other myosins.


Pssm-ID: 459939  Cd Length: 105  Bit Score: 136.17  E-value: 2.78e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  1831 TDQIFEWALKAEPLKDEAYVQILKQLTDNHIRYSEERGWELLWLCTGLFPPSNILLPHVQRFLQ------SRKHCPLAID 1904
Cdd:pfam00784    1 AQNILQKGLKRPELRDEIYCQLIKQTTNNPKPESLLRGWQLLALCLGTFPPSKKLLKYLLKFLKrhaddpSREVGKYAQF 80
                           90       100
                   ....*....|....*....|....*
gi 755522197  1905 CLQRLQKALRNGSRKYPPHLVEVEA 1929
Cdd:pfam00784   81 CLKRLKRTLKNGGRKYPPSREEIEA 105
SH3_MYO7A cd11881
Src Homology 3 domain of Myosin VIIa and similar proteins; Myo7A is an uncoventional myosin ...
1640-1704 4.50e-36

Src Homology 3 domain of Myosin VIIa and similar proteins; Myo7A is an uncoventional myosin that is involved in organelle transport. It is required for sensory function in both Drosophila and mammals. Mutations in the Myo7A gene cause both syndromic deaf-blindness [Usher syndrome I (USH1)] and nonsyndromic (DFNB2 and DFNA11) deafness in humans. It contains an N-terminal motor domain, light chain-binding IQ motifs, a coiled-coil region for heavy chain dimerization, and a tail consisting of a pair of MyTH4-FERM tandems separated by a SH3 domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212814  Cd Length: 64  Bit Score: 131.48  E-value: 4.50e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755522197 1640 SKYVVALQDNPNPAGEeSGFLSFAKGDLIILDHDTGEQVMNSGWANGINERTKQRGDFPTDCVYV 1704
Cdd:cd11881     1 SKYVVALQDYPNPSDG-SSFLSFAKGDLIILDQDTGEQVMNSGWCNGRNDRTGQRGDFPADCVYV 64
MYSc_Myo33 cd14894
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...
224-724 2.25e-29

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: 127.94  E-value: 2.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  224 VLEATPILEAFGNAKTIRNDNSSRFGKY--IDIHFNKRG---AIEGAKIEQYLLEKSRVC----RQAPD--ERNYHVFYC 292
Cdd:cd14894   249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTsergRESGDqnELNFHILYA 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  293 MLEGMNEEEKKKL--------GLGQAAdYNYLA-----MGNCITCEG--RVDSQEYANIRSAMKVLMFTDTENWEISKLL 357
Cdd:cd14894   329 MVAGVNAFPFMRLlakelhldGIDCSA-LTYLGrsdhkLAGFVSKEDtwKKDVERWQQVIDGLDELNVSPDEQKTIFKVL 407
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  358 AAILHMGNLQYEARTFEN---LDACEVLFSPSlaTAASLLE---VNPPDLMSCLTSRTLITRGETVSTPLSREQALDVRD 431
Cdd:cd14894   408 SAVLWLGNIELDYREVSGklvMSSTGALNAPQ--KVVELLElgsVEKLERMLMTKSVSLQSTSETFEVTLEKGQVNHVRD 485
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  432 AFVKGIYGRLFVWIVEKINAAIyKPPPLEVKNSRRS-------------IGLLDIFGFENFTVNSFEQLCINFANEHLqq 498
Cdd:cd14894   486 TLARLLYQLAFNYVVFVMNEAT-KMSALSTDGNKHQmdsnasapeavslLKIVDVFGFEDLTHNSLDQLCINYLSEKL-- 562
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  499 ffvrhvFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRPMNVISLIDEeskfpkgtdATMLHK---LNSQHKLNANYVP 575
Cdd:cd14894   563 ------YAREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEE---------LTILHQsenMNAQQEEKRNKLF 627
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  576 PKNSHETQ--------------------------FGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQ 629
Cdd:cd14894   628 VRNIYDRNssrlpepprvlsnakrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLN 707
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  630 ADVAMG------------AETR-KRSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGM 696
Cdd:cd14894   708 ESSQLGwspntnrsmlgsAESRlSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRL 787
                         570       580       590
                  ....*....|....*....|....*....|..
gi 755522197  697 ---METIRIRHAGY-PIRYSFVEFVERYRVLL 724
Cdd:cd14894   788 irqMEICRNSSSSYsAIDISKSTLLTRYGSLL 819
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
2048-2150 3.42e-20

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 88.10  E-value: 3.42e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  2048 FHYYQELPKYLRGYHKCTREEVLQLGALIYRVKF--EEDKSYFPSIPKLLReLVPQDLIRQVSPDDWKRSIVAYFNKHAG 2125
Cdd:pfam00373   14 LLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFgdYQPSSHTSEYLSLES-FLPKQLLRKMKSKELEKRVLEAHKNLRG 92
                           90       100
                   ....*....|....*....|....*
gi 755522197  2126 KSKEEAKLAFLKLIFKWPTFGSAFF 2150
Cdd:pfam00373   93 LSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
2048-2142 1.23e-18

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 83.06  E-value: 1.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 2048 FHYYQELPKYLRGYHKCTREEVLQLGALIYRVKF-EEDKSYFPSIPKLLRELVPQDLIRQVSPDDWKRSIVAYFNKHAGK 2126
Cdd:cd14473     4 LLYLQVKRDILEGRLPCSEETAALLAALALQAEYgDYDPSEHKPKYLSLKRFLPKQLLKQRKPEEWEKRIVELHKKLRGL 83
                          90
                  ....*....|....*.
gi 755522197 2127 SKEEAKLAFLKLIFKW 2142
Cdd:cd14473    84 SPAEAKLKYLKIARKL 99
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
2146-2237 3.33e-16

FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 275389  Cd Length: 93  Bit Score: 75.87  E-value: 3.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 2146 GSAFFEVKQTTEpnFPEILLIAINKYGVSLIDPRTKDILTTHPFTKISNWS-SGNTYFHITIGNLVRGSKLLCETS--LG 2222
Cdd:cd00836     1 GVEFFPVKDKSK--KGSPIILGVNPEGISVYDELTGQPLVLFPWPNIKKISfSGAKKFTIVVADEDKQSKLLFQTPsrQA 78
                          90
                  ....*....|....*
gi 755522197 2223 YKMDDLLTSYISQML 2237
Cdd:cd00836    79 KEIWKLIVGYHRFLL 93
FERM_F1_DdMyo7_like cd17208
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Dictyostelium ...
1291-1386 1.39e-12

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Dictyostelium discoideum Myosin-VIIa (DdMyo7) and similar proteins; DdMyo7, also termed Myosin-I heavy chain, or class VII unconventional myosin, or M7, plays a role in adhesion in Dictyostelium where it is a component of a complex of proteins that serve to link membrane receptors to the underlying actin cytoskeleton. It interacts with talinA, an actin-binding protein with a known role in cell-substrate adhesion. DdMyo7 is required for phagocytosis. It is also essential for the extension of filopodia, plasma membrane protrusions filled with parallel bundles of F-actin. Members in this family contain a myosin motor domain, two MyTH4 domains, two FERM (Band 4.1, ezrin, radixin, moesin) domains, and two Pleckstrin homology (PH) domains. Some family members contain an extra SH3 domain. Each FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340728  Cd Length: 98  Bit Score: 65.74  E-value: 1.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 1291 KPIMLPVTFMDGTTKTLLTDSATTARELCNALADKISLKDR-FGFSLYIALFDKVSSLGSgSDHVMDAISQCEQYAKEQG 1369
Cdd:cd17208     2 RPIVARFYFLDGQFKALEFDSAATAAEVLEQLKQKIGLRSTaDGFALYEVFGGIERAILP-EEKVADVLSKWEKLQRTMA 80
                          90
                  ....*....|....*..
gi 755522197 1370 AQERNAPWRLFFRKEVF 1386
Cdd:cd17208    81 SCAAQQAVKFVFKKRLF 97
FERM2_F1_Myosin-VII cd17093
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, ...
1292-1383 4.93e-12

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the second FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340613  Cd Length: 98  Bit Score: 64.18  E-value: 4.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 1292 PIMLPVTFMDGTTKTLLTDSATTARELCNALADKISLKDRFGFSLYIALFDKVSSLGSGsDHVMDAISQCEQY-AKEQGA 1370
Cdd:cd17093     1 QIFHKVYFPDDTDEAFEVDSSTRARDLCQNIASRLGLKSSEGFSLFVKIADKVISLPEG-DFFFDFIRHLTDWiKKARPT 79
                          90
                  ....*....|....*..
gi 755522197 1371 QERNAP---WRLFF-RK 1383
Cdd:cd17093    80 KDGPKPsltYQVFFmRK 96
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
1398-1498 6.28e-11

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 61.11  E-value: 6.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 1398 ATNLIYQQVVRGVKFGEYRCeKEDDLAELASQQYFVDYG--SEMILERLLSLVPTYIPDREITPLKNlEKWAQLAIAAHK 1475
Cdd:cd14473     1 TRYLLYLQVKRDILEGRLPC-SEETAALLAALALQAEYGdyDPSEHKPKYLSLKRFLPKQLLKQRKP-EEWEKRIVELHK 78
                          90       100
                  ....*....|....*....|...
gi 755522197 1476 KgiyaQRRTDSQKVKEDVVNYAR 1498
Cdd:cd14473    79 K----LRGLSPAEAKLKYLKIAR 97
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
892-970 2.21e-10

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 61.21  E-value: 2.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   892 RRLRVEYQRRLEAERM-RLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKKELLEQME-KARH 969
Cdd:pfam05672   33 ERLEKEEEERLRKEELrRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEaKARE 112

                   .
gi 755522197   970 E 970
Cdd:pfam05672  113 E 113
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
1937-2031 2.29e-09

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found in FERM (Four.1/Ezrin/Radixin/Moesin) family proteins; FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain is present at the N-terminus of a large and diverse group of proteins that mediate linkage of the cytoskeleton to the plasma membrane. FERM-containing proteins are ubiquitous components of the cytocortex and are involved in cell transport, cell structure and signaling functions. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N), which is structurally similar to ubiquitin.


Pssm-ID: 340464  Cd Length: 80  Bit Score: 55.67  E-value: 2.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 1937 IFHKVYFPDDTDEAFEVESSTKAKDFCQNIASRLLLKSSEGFSLFVKIADKvisvpeNDFFFDFVRHLTDWIKKARPikd 2016
Cdd:cd01765     1 ISCRVRLLDGTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFYEDNDG------QKHWLDLDKKISKQLKRSGP--- 71
                          90
                  ....*....|....*
gi 755522197 2017 givpsltYQVFFMKK 2031
Cdd:cd01765    72 -------YQFYFRVK 79
FERM1_F1_Myosin-VII cd17092
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, ...
1941-2001 7.83e-09

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of the myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in the MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the first FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340612  Cd Length: 99  Bit Score: 54.95  E-value: 7.83e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755522197 1941 VYFPDDTDEAFEVESSTKAKDFCQNIASRLLLKSSEGFSLFVKIADKVISV-PENDFFFDFV 2001
Cdd:cd17092     6 VTFMDGSTKTVEVDSATTARELCRQLAEKLGLKDTFGFSLYIALFDKVSSLgSGTDHVMDAI 67
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
1293-1383 8.07e-09

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found in FERM (Four.1/Ezrin/Radixin/Moesin) family proteins; FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain is present at the N-terminus of a large and diverse group of proteins that mediate linkage of the cytoskeleton to the plasma membrane. FERM-containing proteins are ubiquitous components of the cytocortex and are involved in cell transport, cell structure and signaling functions. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N), which is structurally similar to ubiquitin.


Pssm-ID: 340464  Cd Length: 80  Bit Score: 54.13  E-value: 8.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 1293 IMLPVTFMDGTTKTLLTDSATTARELCNALADKISLKDRFGFSLYIALFDKVS-SLGSgSDHVMDAISqceqyakeqgaq 1371
Cdd:cd01765     1 ISCRVRLLDGTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFYEDNDGQKhWLDL-DKKISKQLK------------ 67
                          90
                  ....*....|..
gi 755522197 1372 eRNAPWRLFFRK 1383
Cdd:cd01765    68 -RSGPYQFYFRV 78
FERM_C2_myosin_like cd13204
FERM domain C-lobe, repeat 2, of Myosin-like proteins; These myosin-like proteins are ...
2146-2232 1.22e-08

FERM domain C-lobe, repeat 2, of Myosin-like proteins; These myosin-like proteins are unidentified though they are sequence similar to myosin 1/myo1, myosin 7/myoVII, and myosin 10/myoX. These myosin-like proteins contain an N-terminal motor/head region and a C-terminal tail consisting of two myosin tail homology 4 (MyTH4) and twos FERM domains. In myoX the FERM domain forms a supramodule with its MyTH4 domain which binds to the negatively charged E-hook region in the tails of alpha- and beta-tubulin forming a proposed motorized link between actin filaments and microtubules and a similar thing might happen in these myosins. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The second FERM_N repeat is present in this hierarchy. The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270025  Cd Length: 93  Bit Score: 54.36  E-value: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 2146 GSAFFEVKQTTEPNFPEILLIAINKYGVSLIDPRTKDILTTHPFTKISNWSSGNTYFHITIGNLVRGSKLLCETSLGYKM 2225
Cdd:cd13204     1 GSTVFDVTQSYTSNLPKTLWLAIDQSGVHLLERRTKEPLCSYDYSSIVSYSPSLNSLMIVTGSLTKGSKFIFNTNQAFQI 80

                  ....*..
gi 755522197 2226 DDLLTSY 2232
Cdd:cd13204    81 ANLIRDY 87
FERM_F1_Myo10_like cd17110
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in unconventional ...
1291-1386 1.66e-08

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in unconventional myosin-X and similar proteins; Myosin-X, also termed myosin-10 (Myo10), is an untraditional member of myosin superfamily. It is an actin-based motor protein that plays a critical role in diverse cellular motile events, such as filopodia formation/extension, phagocytosis, cell migration, and mitotic spindle maintenance, as well as a number of disease states including cancer metastasis and pathogen infection. Myosin-X functions as an important regulator of cytoskeleton that modulates cell motilities in many different cellular contexts. It regulates neuronal radial migration through interacting with N-cadherin. Like other unconventional myosins, Myosin-X is composed of a conserved motor head, a neck region and a variable tail. The neck region consists of three IQ motifs (light chain-binding sites), and a predicted stalk of coiled coil. The tail contains three PEST regions, three PH domains, a MyTH4 domain, and a FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Amoebozoan Dictyostelium discoideum myosin VII (DdMyo7) and uncharacterized pleckstrin homology domain-containing family H member 3 (PLEKHH3) are also included in this family. Like metazoan Myo10, DdMyo7 is essential for the extension of filopodia, plasma membrane protrusions filled with parallel bundles of F-actin.


Pssm-ID: 340630  Cd Length: 97  Bit Score: 53.93  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 1291 KPIMLPVTFMDGTTKTLLTDSATTARELCNALADKISLKD-RFGFSLYiALFDKVSSLGSGSDHVMDAISQCEQYAKEqG 1369
Cdd:cd17110     2 QELTVTVTCQGGRTCKVAIDSWTTCGEVSKDLARRLGLERsRNGFALF-ETSGDIERALEAKTRVVDVLSKWEKLAAT-G 79
                          90
                  ....*....|....*..
gi 755522197 1370 AQERNAPWRLFFRKEVF 1386
Cdd:cd17110    80 SSPGDDGWKLLFKLYLF 96
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
878-970 1.70e-08

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 55.44  E-value: 1.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   878 VQAYARGMIARRLHRR---LRVEYQRRLEA-----ERMRLAEEEKLRK-EMSAKKAKEEAERKHQERLAQLARED----- 943
Cdd:pfam15346   16 VEEAVAKRVEEELEKRkdeIEAEVERRVEEarkimEKQVLEELEREREaELEEERRKEEEERKKREELERILEENnrkie 95
                           90       100       110
                   ....*....|....*....|....*....|...
gi 755522197   944 ------AERELKEKEEARRKKELLEQMEKARHE 970
Cdd:pfam15346   96 eaqrkeAEERLAMLEEQRRMKEERQRREKEEEE 128
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
899-974 3.40e-08

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 58.01  E-value: 3.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   899 QRRLEAERMRLAEE-EKLRKEMSAKKAKEEAERKHQERL-AQLAREDAERE--LKEKEEARRKKELLEQMEKARHEPINH 974
Cdd:pfam13868  168 EEEREAEREEIEEEkEREIARLRAQQEKAQDEKAERDELrAKLYQEEQERKerQKEREEAEKKARQRQELQQAREEQIEL 247
PTZ00121 PTZ00121
MAEBL; Provisional
838-1010 4.89e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 4.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  838 SRKLHKQYRLARQRIIEfQARcRAYLVRKAFRHRlwaviTVQAYARGMIARRLHRRLRVEYQRRLE----AERMRLAEE- 912
Cdd:PTZ00121 1115 RKAEEAKKKAEDARKAE-EAR-KAEDARKAEEAR-----KAEDAKRVEIARKAEDARKAEEARKAEdakkAEAARKAEEv 1187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  913 ---EKLRKEMSAKKAkEEAERKHQERLAQLAR--EDAER--ELKEKEEARRKKELLEQMEKARHEPINHSDMVDKMFGFL 985
Cdd:PTZ00121 1188 rkaEELRKAEDARKA-EAARKAEEERKAEEARkaEDAKKaeAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFA 1266
                         170       180
                  ....*....|....*....|....*
gi 755522197  986 GTSGSLPGQEGQAPSGFEDLERGRR 1010
Cdd:PTZ00121 1267 RRQAAIKAEEARKADELKKAEEKKK 1291
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
887-968 1.67e-07

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 52.74  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   887 ARRL--HRRLRVEYQRRL---EAERMRLAEEEKLR-----KEMSAKKAKEEAERKHQERLAQLAREDAERELkekeearR 956
Cdd:pfam05672   63 ARRLeeERRREEEERQRKaeeEAEEREQREQEEQErlqkqKEEAEAKAREEAERQRQEREKIMQQEEQERLE-------R 135
                           90
                   ....*....|..
gi 755522197   957 KKELLEQMEKAR 968
Cdd:pfam05672  136 KKRIEEIMKRTR 147
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
809-966 1.91e-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: 56.67  E-value: 1.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   809 IQRHWRGHHCRKNYELIRLgfLRLQALHRSRKLHKQYRLARQrIIEFQARCRAYLVRKAFRHRlwavitvqayargmiAR 888
Cdd:pfam17380  385 MERQQKNERVRQELEAARK--VKILEEERQRKIQQQKVEMEQ-IRAEQEEARQREVRRLEEER---------------AR 446
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755522197   889 RLHRRLRVEYQRRLEAERMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKKELLEQMEK 966
Cdd:pfam17380  447 EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEE 524
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
887-970 2.04e-07

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 51.46  E-value: 2.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   887 ARRLHRRLRV--EYQRRLEAERMRlAEEEKLRKEMSAKKAKEEaerkhQERLAQLAREdAERELKEKEEARRKKE----- 959
Cdd:pfam20492   36 AEELEEERRQaeEEAERLEQKRQE-AEEEKERLEESAEMEAEE-----KEQLEAELAE-AQEEIARLEEEVERKEeearr 108
                           90
                   ....*....|.
gi 755522197   960 LLEQMEKARHE 970
Cdd:pfam20492  109 LQEELEEAREE 119
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
892-968 2.21e-07

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 56.11  E-value: 2.21e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755522197   892 RRLRVEYQRRLEAERMRLAEEEKLRkemsAKKAKEEAERKHQERLAQ--LAREDAERELKEKEEARRKKELLEQMEKAR 968
Cdd:pfam15709  346 RRLEVERKRREQEEQRRLQQEQLER----AEKMREELELEQQRRFEEirLRKQRLEEERQRQEEEERKQRLQLQAAQER 420
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
900-971 2.82e-07

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 51.97  E-value: 2.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   900 RRLEAERMRLA-------EEEKLRKEMSAKKAKEEAERKHQERLAQL---AREDAERELKEKEEARRKKElLEQMEKARH 969
Cdd:pfam05672   13 ARILAEKRRQAreqrereEQERLEKEEEERLRKEELRRRAEEERARReeeARRLEEERRREEEERQRKAE-EEAEEREQR 91

                   ..
gi 755522197   970 EP 971
Cdd:pfam05672   92 EQ 93
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
895-959 2.91e-07

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 54.85  E-value: 2.91e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   895 RVEYQRRLEAERMRLAEEEKLRKEMSAKKAKEE-----AERKHQERLAQLAREDAERELKEKEEARRKKE 959
Cdd:TIGR02794   84 RAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEkqkqaEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE 153
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
897-967 3.38e-07

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 54.85  E-value: 3.38e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755522197   897 EYQRRLEAERMRLAEEEKLRKEMSAKKAKE-EAERKHQERLAQLAREDAEreLKEKEEARRKKELLEQMEKA 967
Cdd:TIGR02794  108 EQAAKQAEEKQKQAEEAKAKQAAEAKAKAEaEAERKAKEEAAKQAEEEAK--AKAAAEAKKKAEEAKKKAEA 177
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
892-971 3.45e-07

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 51.97  E-value: 3.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   892 RRLRVEYQRRLEAERmRLAEEEKLRKEMSAKKAKEEAERKHQERLaQLAREDAERelKEKEEARRKK----ELLEQMEKA 967
Cdd:pfam05672   56 RARREEEARRLEEER-RREEEERQRKAEEEAEEREQREQEEQERL-QKQKEEAEA--KAREEAERQRqereKIMQQEEQE 131

                   ....
gi 755522197   968 RHEP 971
Cdd:pfam05672  132 RLER 135
PTZ00121 PTZ00121
MAEBL; Provisional
860-970 4.10e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.92  E-value: 4.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  860 RAYLVRKAFRHRLWAVITVQAYARGMIARRLhrrlRVEYQRRLEAERMRLAEEEKLRKEMSAKKAKEE---AE--RKHQE 934
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEA----KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEkkkAEelKKAEE 1657
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 755522197  935 ----RLAQLAREDAE-----RELKEKEEARRKKEllEQMEKARHE 970
Cdd:PTZ00121 1658 enkiKAAEEAKKAEEdkkkaEEAKKAEEDEKKAA--EALKKEAEE 1700
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
888-970 6.12e-07

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 51.19  E-value: 6.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   888 RRLHR--RLRVEYQRRLEAERMRLAEEEKLRKEMSAK-KAKEEAERKHQERLAQLAREDAERELKEKEEARRKKELLEQM 964
Cdd:pfam05672   20 RRQAReqREREEQERLEKEEEERLRKEELRRRAEEERaRREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERL 99

                   ....*.
gi 755522197   965 EKARHE 970
Cdd:pfam05672  100 QKQKEE 105
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
819-968 6.56e-07

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 54.57  E-value: 6.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   819 RKNYELIRLgflRLQALHRSRkLHKQYRLARQRIIEFQARCRAYLVRKAFRHRLwavitvqayargmiaRRLHRRLRVEY 898
Cdd:pfam15709  383 QRRFEEIRL---RKQRLEEER-QRQEEEERKQRLQLQAAQERARQQQEEFRRKL---------------QELQRKKQQEE 443
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755522197   899 QRRLEAER-------MRLAEEEKLRKEMsAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKKEllEQMEKAR 968
Cdd:pfam15709  444 AERAEAEKqrqkeleMQLAEEQKRLMEM-AEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALE--EAMKQAQ 517
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
881-967 8.08e-07

Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 50.95  E-value: 8.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   881 YARGM--------IARRLHRRLR-VEYQRRL-----EAERMRLAEEEKLRKEmsakkAKEEAERKHQERLAQLAR-EDAE 945
Cdd:pfam15236   31 FLRGQnalldpaqLEERERKRQKaLEHQNAIkkqleEKERQKKLEEERRRQE-----EQEEEERLRREREEEQKQfEEER 105
                           90       100
                   ....*....|....*....|....
gi 755522197   946 RELKEKEEARRKK--ELLEQMEKA 967
Cdd:pfam15236  106 RKQKEKEEAMTRKtqALLQAMQKA 129
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
898-967 8.09e-07

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 53.70  E-value: 8.09e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755522197   898 YQRRLEAERMRLAEEEKLRKEMSAKKAKEEAERKHQE---RLAQLAREDAERELKEKEEARRKKELLEQMEKA 967
Cdd:TIGR02794  126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAeakKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKA 198
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
831-981 8.15e-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: 54.36  E-value: 8.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   831 RLQALHRSRKLHKQYRlARQRIIEFQARCRAYLVRKAF-RHRLWAVITVQAYARGMiARRLHRRLRVEYQRRLEAERMRL 909
Cdd:pfam17380  308 KAREVERRRKLEEAEK-ARQAEMDRQAAIYAEQERMAMeRERELERIRQEERKREL-ERIRQEEIAMEISRMRELERLQM 385
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   910 AEE---EKLRKEM-SAKKAK---EEAERKHQERLAQLAREDAERELKEKEEARR-KKELLEQMEKARHEPINHSDMVDKM 981
Cdd:pfam17380  386 ERQqknERVRQELeAARKVKileEERQRKIQQQKVEMEQIRAEQEEARQREVRRlEEERAREMERVRLEEQERQQQVERL 465
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
909-968 1.22e-06

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 47.65  E-value: 1.22e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  909 LAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKKELLEQMEKAR 968
Cdd:cd22249     1 LSKPGEIREEYEAQLKKLEEERRKEREEEEKASEELIRKLQEEEERQRKREREEQLKQDE 60
FERM_C_MyoXV cd13201
FERM domain C-lobe of Myosin XV (MyoXV/Myo15); MyoXV, a MyTH-FERM myosin, are actin-based ...
2146-2244 1.22e-06

FERM domain C-lobe of Myosin XV (MyoXV/Myo15); MyoXV, a MyTH-FERM myosin, are actin-based motor proteins essential for a variety of biological processes in actin cytoskeleton function. Specifically MyoXV functions in the actin organization in hair cells of the organ of Corti. Mutations in Human MyoXVa causes non-syndromic deafness, DFNB3 and the mouse shaker-2 mutation. MyoXV consists of a N-terminal motor/head region, a neck made of 1-3 IQ motifs, and a tail that consists of either a myosin tail homology 4 (MyTH4) domains, followed by an SH3 domain, and a MyTH-FERM domains as in rat Myo15 or two MyTH-FERM domains separated by a SH3 domain as in human Myo15A. The MyTH-FERM domains are thought to mediate dimerization and binding to other proteins or cargo. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270022  Cd Length: 101  Bit Score: 48.76  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 2146 GSAFFEVKQTTEPNFPEILLIAINKYGVSLIDPRTKDILTTHPFT------KISNWSSGNTYFHITIGNLVRGSKLLCET 2219
Cdd:cd13201     1 GSNFFYVQRVSDPRLPGPCLLALNREGLHFLDPKTHETLLRIPLKevqstrKLRPLEDGTPFLDIKYGNLMQQRTIRLET 80
                          90       100
                  ....*....|....*....|....*
gi 755522197 2220 SLGYkmddLLTSYISQMLTAMSKQR 2244
Cdd:cd13201    81 DQAH----EISRLIAQYIEEASENR 101
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
886-960 1.22e-06

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 52.96  E-value: 1.22e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755522197   886 IARRLHrrLRVEYQRRLEAerMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQ----LAREDAErELKEKEEARRKKEL 960
Cdd:pfam07946  248 LAKRAK--LRPEALKKAKK--TREEEIEKIKKAAEEERAEEAQEKKEEAKKKEreekLAKLSPE-EQRKYEEKERKKEQ 321
PTZ00121 PTZ00121
MAEBL; Provisional
819-980 2.18e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 2.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  819 RKNYELIRLGFLRLQALHRSRKLHKQYRL-----ARQRIIEFQARCRAYLVRKAFRHRlwavitvqayargmiaRRLHRR 893
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEekkmkAEEAKKAEEAKIKAEELKKAEEEK----------------KKVEQL 1638
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  894 LRVEYQRRLEAERMRLAEEE-KLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKkelLEQMEKARHEPI 972
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEEnKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK---AEELKKKEAEEK 1715

                  ....*...
gi 755522197  973 NHSDMVDK 980
Cdd:PTZ00121 1716 KKAEELKK 1723
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
844-964 6.62e-06

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 51.11  E-value: 6.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   844 QYRLARQRIIEFQARCRAYLVRKAFRH-----RLWAvitvQAYARgmiARRLHRRLRVEYQRRLEAERMRLA--EEEKLR 916
Cdd:pfam15709  330 QEKASRDRLRAERAEMRRLEVERKRREqeeqrRLQQ----EQLER---AEKMREELELEQQRRFEEIRLRKQrlEEERQR 402
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 755522197   917 KEMSAKK-------AKEEAERKHQE---RLAQLAREDAERELKEKE-EARRKKELLEQM 964
Cdd:pfam15709  403 QEEEERKqrlqlqaAQERARQQQEEfrrKLQELQRKKQQEEAERAEaEKQRQKELEMQL 461
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
879-1041 1.02e-05

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 48.91  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   879 QAYARGM-IARRLHRRLRVEYQR--RLEaERMRLA---EEEKLRKEMSAKKAKEE--AERKHQER-LAQLAREDAERELK 949
Cdd:pfam04012   43 QALAQTIaRQKQLERRLEQQTEQakKLE-EKAQAAltkGNEELAREALAEKKSLEkqAEALETQLaQQRSAVEQLRKQLA 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   950 EKE----EARRKKELLeqmeKARHEPINHSDMVDKMFGFLGTSGslpgqegqAPSGFEDLERGRREMvEEDVDAALPLPD 1025
Cdd:pfam04012  122 ALEtkiqQLKAKKNLL----KARLKAAKAQEAVQTSLGSLSTSS--------ATDSFERIEEKIEER-EARADAAAELAS 188
                          170
                   ....*....|....*.
gi 755522197  1026 EDEEDlseykfAKFAA 1041
Cdd:pfam04012  189 AVDLD------AKLEQ 198
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
832-970 1.31e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 49.53  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   832 LQALHRSRKLHKQYR-LARQRIIEFQARCRAYLVRKAFRHRLW-AVITVQAYARGMIARRLHRRLRVEYQRRLEAERMR- 908
Cdd:pfam13868  129 REEIDEFNEEQAEWKeLEKEEEREEDERILEYLKEKAEREEEReAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRa 208
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755522197   909 -LAEEEKLRKEmsAKKAKEEAERKHQERLA-QLARED--AERELKEKEEARRKKELLEQMEKARHE 970
Cdd:pfam13868  209 kLYQEEQERKE--RQKEREEAEKKARQRQElQQAREEqiELKERRLAEEAEREEEEFERMLRKQAE 272
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
834-967 1.32e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  834 ALHRSRKLHKQYRLARQRIIEFQARCRAYLVRKAFRHRLWAVITVQAYArgmIARRLHRRLRVEYQ--RRLEAERMRLAE 911
Cdd:COG1196   230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE---LELELEEAQAEEYEllAELARLEQDIAR 306
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 755522197  912 EEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKKELLEQMEKA 967
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
897-970 1.57e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 49.80  E-value: 1.57e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755522197  897 EYQRRLEAERMRLAEEEKlRKEMSAKKAKEEAERKHQERLAQLAREDAER----ELKEKEEARRKKEL-LEQMEKARHE 970
Cdd:PRK09510  121 EEAAKQAALKQKQAEEAA-AKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKkaeaEAAKKAAAEAKKKAeAEAAAKAAAE 198
PTZ00121 PTZ00121
MAEBL; Provisional
838-980 1.63e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  838 SRKLHKQYRLARQRIIEfQARcRAYLVRKAFRHRlwavitvqayaRGMIARRLHRRLRVEYQRRleAERMRLAEEEK--- 914
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAE-AAR-KAEEVRKAEELR-----------KAEDARKAEAARKAEEERK--AEEARKAEDAKkae 1227
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755522197  915 -LRKEMSAKKAKEEAERKHQERLAQLAREDAERELK---------EKEEARRKKELLEQMEKARHEPINHSDMVDK 980
Cdd:PTZ00121 1228 aVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAhfarrqaaiKAEEARKADELKKAEEKKKADEAKKAEEKKK 1303
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
897-970 1.81e-05

Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.


Pssm-ID: 462259 [Multi-domain]  Cd Length: 353  Bit Score: 49.22  E-value: 1.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   897 EYQRRL----EAERMRLAEEEKLRKEMSAKKAK------EEAERK-HQERLAQLAREDAERELKEKEEARRKKELLEQME 965
Cdd:pfam07767  196 DHQELLqkavEAEKKRLKEEEKLERVLEKIAESaataeaREEKRKtKAQRNKEKRRKEEEREAKEEKALKKKLAQLERLK 275

                   ....*
gi 755522197   966 KARHE 970
Cdd:pfam07767  276 EIAKE 280
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
888-965 2.11e-05

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 50.12  E-value: 2.11e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755522197  888 RRLHRRLRVEYQRrLEAERMRLAEEEKLRKEmSAKKAKEEAERKHQERLAQLAREDAERELKEK-EEARRKKELLEQME 965
Cdd:PTZ00266  458 KRIERLEREERER-LERERMERIERERLERE-RLERERLERDRLERDRLDRLERERVDRLERDRlEKARRNSYFLKGME 534
PTZ00121 PTZ00121
MAEBL; Provisional
839-968 2.16e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  839 RKLHKQYRLARQRIIEfQARCRAYLVRKAFRHRLWAVITVQAYARGMIARRLHRRLRVEYQRRLE----AERMRLAEE-- 912
Cdd:PTZ00121 1218 RKAEDAKKAEAVKKAE-EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADelkkAEEKKKADEak 1296
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  913 --EKLRKEMSAKKAKEEAeRKHQE--RLAQLAREDAERELKEKEEARRKKELLEQMEKAR 968
Cdd:PTZ00121 1297 kaEEKKKADEAKKKAEEA-KKADEakKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAA 1355
Caldesmon pfam02029
Caldesmon;
899-971 2.45e-05

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 49.48  E-value: 2.45e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755522197   899 QRRLEAErMRLAEEEKLRKEmsAKKAKEEAERKHQErlaqlarEDAERELKEKEEARRKKElleQMEKARHEP 971
Cdd:pfam02029  270 QKQQEAE-LELEELKKKREE--RRKLLEEEEQRRKQ-------EEAERKLREEEEKRRMKE---EIERRRAEA 329
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
888-972 3.34e-05

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 46.22  E-value: 3.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   888 RRLHR-RLRVEYQRRLEAERmrlAEEEKLRKEMSA--KKAKEEAERKHQERLAQLAREDAERELKEKEEARRKKELLEQM 964
Cdd:pfam11600   16 QRLEKdKERLRRQLKLEAEK---EEKERLKEEAKAekERAKEEARRKKEEEKELKEKERREKKEKDEKEKAEKLRLKEEK 92

                   ....*...
gi 755522197   965 EKARHEPI 972
Cdd:pfam11600   93 RKEKQEAL 100
FERM_C_Talin cd10569
FERM domain C-lobe/F3 of Talin; Talin (also called filopodin) plays an important role in ...
2146-2233 3.80e-05

FERM domain C-lobe/F3 of Talin; Talin (also called filopodin) plays an important role in initiating actin filament growth in motile cell protrusions. It is responsible for linking the cytoplasmic domains of integrins to the actin-based cytoskeleton, and is involved in vinculin, integrin and actin interactions. At the leading edge of motile cells, talin colocalises with the hyaluronan receptor layilin in transient adhesions, some of which become more stable focal adhesions (FA). During this maturation process, layilin is replaced with integrins, where localized production of PI(4,5)P(2) by type 1 phosphatidyl inositol phosphate kinase type 1gamma (PIPK1gamma) is thought to play a role in FA assembly. Talins are composed of a N-terminal region FERM domain which us made up of 3 subdomains (N, alpha-, and C-lobe; or- A-lobe, B-lobe, and C-lobe; or F1, F2, and F3) connected by short linkers, a talin rod which binds vinculin, and a conserved C-terminal region with actin- and integrin-binding sites. There are 2 additional actin-binding domains, one in the talin rod and the other in the FERM domain. Both the F2 and F3 FERM subdomains contribute to F-actin binding. Subdomain F3 of the FERM domain contains overlapping binding sites for integrin cytoplasmic domains and for the type 1 gamma isoform of PIP-kinase (phosphatidylinositol 4-phosphate 5-kinase). The FERM domain has a cloverleaf tripart structure . F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 269973  Cd Length: 92  Bit Score: 44.25  E-value: 3.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 2146 GSAFFEVKQTTE-PNFPEILLIAINKYGVSLIDPRTKDILTTHPFTKISNWSSGNTYFHITIGNLvRGSKLLCETSLGYK 2224
Cdd:cd10569     1 GVTFFLVKEKMKgKNKLVPRLLGITKESVLRLDEETKEVLKVWPLTTIKRWAASPKSFTLDFGDY-SENYYSVQTTEGEQ 79

                  ....*....
gi 755522197 2225 MDDLLTSYI 2233
Cdd:cd10569    80 ISQLISGYI 88
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
903-970 3.94e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 48.30  E-value: 3.94e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755522197   903 EAERMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKKELLEQMEKARHE 970
Cdd:TIGR02794   79 EAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKE 146
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
895-970 4.21e-05

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 48.50  E-value: 4.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  895 RVEYQRRLEAERMRLAEEEKLRKEMSAKKAKEEAERK-------HQERLAQLAREDAERELK-EKEEARRKKELLEQMEK 966
Cdd:COG3064    20 QAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEareakaeAEQRAAELAAEAAKKLAEaEKAAAEAEKKAAAEKAK 99

                  ....
gi 755522197  967 ARHE 970
Cdd:COG3064   100 AAKE 103
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
892-970 4.77e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 47.99  E-value: 4.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   892 RRLRVEYQRRLEAERMRLAEE-----EKLRKEM--------SAKKAKEEAERKHQERLAQLAREDAERELK---EKEEAR 955
Cdd:pfam13868  100 REQMDEIVERIQEEDQAEAEEklekqRQLREEIdefneeqaEWKELEKEEEREEDERILEYLKEKAEREEEreaEREEIE 179
                           90       100
                   ....*....|....*....|
gi 755522197   956 RKKE-----LLEQMEKARHE 970
Cdd:pfam13868  180 EEKEreiarLRAQQEKAQDE 199
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
833-970 5.06e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 5.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  833 QALHRSRKLHKQYRLARQRIIEFQARC-RAYLVRKAFRHRLWAVITVQAYARGMIARRLHRRLRVEYQRRLEAERMRLAE 911
Cdd:COG4717    78 EELKEAEEKEEEYAELQEELEELEEELeELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEE 157
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 755522197  912 EEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKeeARRKKELLEQMEKARHE 970
Cdd:COG4717   158 LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL--AEELEELQQRLAELEEE 214
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
922-1222 6.53e-05

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 47.94  E-value: 6.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  922 KKAKEEAERKHQERLaQLAREDAERELKEKEEARRKKELLEQMEKARH-EPINHSDMVDkmfgflgtsgslpgQEGQaps 1000
Cdd:PLN03086    6 RRAREKLEREQRERK-QRAKLKLERERKAKEEAAKQREAIEAAQRSRRlDAIEAQIKAD--------------QQMQ--- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 1001 gfEDLERGRREMVEEDVDAA--------LPLPDEDEEDLSEYKFAKFAATYFQGTTTHsytrrplkqpllyHDDEGDQLA 1072
Cdd:PLN03086   68 --ESLQAGRGIVFSRIFEAVsfqgngdkIKLPPSCFTELSDQGAFDKGPLYFRLSVVH-------------QEGSGEMKD 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 1073 ALAVWIT---ILRFMGD-----LPEPKYHTAMSDGSEKIPVMTKIYETLGKKTYKReLQAlQGEGETQLPEgqkktsvrH 1144
Cdd:PLN03086  133 TDSQKTThsgVLEFTAEegsvgLPPHVWSNLFPSDPPDVPLVEVRYIWLPKGTYAK-LQP-DGVGFSDLPN--------H 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 1145 KLV-HLTLKKKSKLTEEVTKRLNDGESTVQgNSMLEDRPTSNLEKLHFIIGNGILRP-ALRDEIYCQISKQLTHNPSKSS 1222
Cdd:PLN03086  203 KAVlETALRQHATLSEDDVLVVNYGQLTYK-LKVLELKPASSVSVLETDIEVDIVGPdSVSNEENQHVLKPLEFGKSESG 281
HAUS5 pfam14817
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ...
861-969 7.48e-05

HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.


Pssm-ID: 464332 [Multi-domain]  Cd Length: 643  Bit Score: 48.12  E-value: 7.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   861 AYLVRKAFRHRLWAVI--TVQAYARGMIARRLHRRlRVEYQRRLEAERmrlaEEEKLRKEMSAKKAKEEAerkhqeRLAQ 938
Cdd:pfam14817   38 KYLIQHVKSERNVRKIrgNLLWYGGLQDKGKAESR-QSAAARRLELQK----EIERLRAEISRLDKQLEA------RELE 106
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 755522197   939 LAREDAERE--LKEKEEARRKKELLE----QMEKARH 969
Cdd:pfam14817  107 LSREEAEREraLDEISDSRHRQLLLEaydqQCEEARK 143
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
801-822 1.02e-04

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 41.16  E-value: 1.02e-04
                            10        20
                    ....*....|....*....|..
gi 755522197    801 RLKSAATLIQRHWRGHHCRKNY 822
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRY 22
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
823-970 1.02e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  823 ELIRLGFLRLQAlhRSRKLHKQYRLARQRIIEFQARCRAYLVRKAFRHRlwaviTVQAYARGMIARRLHRRLRVEYQRRL 902
Cdd:COG1196   270 EELRLELEELEL--ELEEAQAEEYELLAELARLEQDIARLEERRRELEE-----RLEELEEELAELEEELEELEEELEEL 342
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755522197  903 EAERMRLAEEEKLRKEM--SAKKAKEEAERKHQERLAQL--AREDAERELKEKEEARRKKELLEQMEKARHE 970
Cdd:COG1196   343 EEELEEAEEELEEAEAElaEAEEALLEAEAELAEAEEELeeLAEELLEALRAAAELAAQLEELEEAEEALLE 414
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
888-970 1.22e-04

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 44.68  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   888 RRLHRRLRVEYQRRLEAERMRLAEEEKLR----KEMSAKKAKEEAERKHQERlaqlaREDAERELKEKEEARRKKELLEQ 963
Cdd:pfam11600   20 KDKERLRRQLKLEAEKEEKERLKEEAKAEkeraKEEARRKKEEEKELKEKER-----REKKEKDEKEKAEKLRLKEEKRK 94

                   ....*..
gi 755522197   964 MEKARHE 970
Cdd:pfam11600   95 EKQEALE 101
UDM1_RNF168 cd22265
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ...
894-968 1.26e-04

UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; RING finger protein 168 (RNF168) is an E3 ubiquitin-protein ligase that promotes noncanonical K27 ubiquitination to signal DNA damage. Together with RNF8, RNF168 functions as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. This model corresponds to the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) domain of RNF168, which comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409018 [Multi-domain]  Cd Length: 73  Bit Score: 42.16  E-value: 1.26e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755522197  894 LRVEYqrrlEAERMRLAEEeklrkemsaKKAKEEAERKHQERLAQ--LAREDAERELKEKEEARRKKELLEQMEKAR 968
Cdd:cd22265     7 LRQEY----EEEISKLEAE---------RRALEEEENRASEEYIQklLAEEEEEEKLAEERRRAEEEQLKEDEELAR 70
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
899-970 1.28e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 46.96  E-value: 1.28e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755522197  899 QRRLEA---ERMRLAEEEKLRKEMSAKKAKEEAErkhQERLAQL-AREDAERELKEK--EEARRKKELLEQMEKARHE 970
Cdd:COG3064     7 EKAAEAaaqERLEQAEAEKRAAAEAEQKAKEEAE---EERLAELeAKRQAEEEAREAkaEAEQRAAELAAEAAKKLAE 81
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
831-978 1.59e-04

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 46.57  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   831 RLQALHRSRKLHKQYRLARQriiefQARCRAYLVR-KAFRHRLWAVI-TVQAYARGMIARRlhRRLRVEYQRRL------ 902
Cdd:pfam15558   16 RHKEEQRMRELQQQAALAWE-----ELRRRDQKRQeTLERERRLLLQqSQEQWQAEKEQRK--ARLGREERRRAdrrekq 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   903 ----EAERMRLAEE-EKLRKEMSAKKAKEEAERKH--------QERLAQLAREDAERELKEK-EEARRKKELLEQMEKAR 968
Cdd:pfam15558   89 viekESRWREQAEDqENQRQEKLERARQEAEQRKQcqeqrlkeKEEELQALREQNSLQLQERlEEACHKRQLKEREEQKK 168
                          170
                   ....*....|
gi 755522197   969 HEPINHSDMV 978
Cdd:pfam15558  169 VQENNLSELL 178
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
877-970 1.66e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  877 TVQAYARGMIARRLHRRLRVEYQRRLEAERMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAR--EDAERELKEKEEA 954
Cdd:COG4717    38 TLLAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEelEELEAELEELREE 117
                          90       100
                  ....*....|....*....|...
gi 755522197  955 RRKKE-------LLEQMEKARHE 970
Cdd:COG4717   118 LEKLEkllqllpLYQELEALEAE 140
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
892-970 1.70e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 46.57  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  892 RRLRVEYQRR---LEAERMRLAEEEKLRKEMSAKKAKEEAER--KHQERLAQLAREDAERELKEKEEARRKKElleqmEK 966
Cdd:COG3064    58 REAKAEAEQRaaeLAAEAAKKLAEAEKAAAEAEKKAAAEKAKaaKEAEAAAAAEKAAAAAEKEKAEEAKRKAE-----EE 132

                  ....
gi 755522197  967 ARHE 970
Cdd:COG3064   133 AKRK 136
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
1642-1701 1.83e-04

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.


Pssm-ID: 212690 [Multi-domain]  Cd Length: 51  Bit Score: 40.91  E-value: 1.83e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 1642 YVVALQDNpnpAGEESGFLSFAKGDLIILDHDTgeqvmNSGWANGINERtKQRGDFPTDC 1701
Cdd:cd00174     1 YARALYDY---EAQDDDELSFKKGDIITVLEKD-----DDGWWEGELNG-GREGLFPANY 51
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
887-959 1.85e-04

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 44.29  E-value: 1.85e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755522197   887 ARRLHRRLRVEYQR-RLEAERMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKKE 959
Cdd:pfam11600   38 KERLKEEAKAEKERaKEEARRKKEEEKELKEKERREKKEKDEKEKAEKLRLKEEKRKEKQEALEAKLEEKRKKE 111
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
617-673 1.94e-04

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: 44.26  E-value: 1.94e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 755522197  617 HSSR-NKFIKQIFqaDVAmGAETrkrsptlssqFKRSLELLMRTLGACQPFFVRCIKP 673
Cdd:cd01363   126 NSSRfGKFIEILL--DIA-GFEI----------INESLNTLMNVLRATRPHFVRCISP 170
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
888-965 2.18e-04

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 43.32  E-value: 2.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   888 RRLHRRLRVEYQRRLEAERMRL--------AEEEKLRK-----EMSAKKAKEEAERKHQERLAQLAR-EDAERELKEKEE 953
Cdd:pfam12474   50 RRLPKRIRAEQKKRLKMFRESLkqekkelkQEVEKLPKfqrkeAKRQRKEELELEQKHEELEFLQAQsEALERELQQLQN 129
                           90
                   ....*....|..
gi 755522197   954 ArrKKELLEQME 965
Cdd:pfam12474  130 E--KRKELAEHE 139
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
899-959 2.46e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 46.19  E-value: 2.46e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755522197  899 QRRLEAERMRLAEEEKLRKEmsAKKAKEEAERK-HQERLAQLAREDAERELKEK--EEARRKKE 959
Cdd:COG3064    77 KKLAEAEKAAAEAEKKAAAE--KAKAAKEAEAAaAAEKAAAAAEKEKAEEAKRKaeEEAKRKAE 138
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
879-968 2.51e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 45.68  E-value: 2.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   879 QAYARGMIARRLHRRLRVEyQRRLEAERMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKK 958
Cdd:pfam13868  239 QAREEQIELKERRLAEEAE-REEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEG 317
                           90
                   ....*....|
gi 755522197   959 ELLEQMEKAR 968
Cdd:pfam13868  318 ERLREEEAER 327
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
892-970 2.81e-04

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 43.52  E-value: 2.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   892 RRLRVEYQRRLEAERMRLaEEEKLRKEmsaKKAKEEAERKHQERLAQLAREDAERElkeKEEARRKK-ELLEQMEKARHE 970
Cdd:pfam11600    1 RRSQKSVQSQEEKEKQRL-EKDKERLR---RQLKLEAEKEEKERLKEEAKAEKERA---KEEARRKKeEEKELKEKERRE 73
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
1639-1702 3.23e-04

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 40.60  E-value: 3.23e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755522197   1639 RSKYVVALQDNPnpaGEESGFLSFAKGDLIILDHDTgeqvmNSGWANGINERtKQRGDFPTDCV 1702
Cdd:smart00326    1 EGPQVRALYDYT---AQDPDELSFKKGDIITVLEKS-----DDGWWKGRLGR-GKEGLFPSNYV 55
PTZ00121 PTZ00121
MAEBL; Provisional
903-980 3.52e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 3.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  903 EAERMRLAEE-----EKLRKEMSAKKAKEEAERKHQE-RLAQLAREDAErELKEKEEARRKKELLEQMEKARHEPINHSD 976
Cdd:PTZ00121 1465 KAEEAKKADEakkkaEEAKKADEAKKKAEEAKKKADEaKKAAEAKKKAD-EAKKAEEAKKADEAKKAEEAKKADEAKKAE 1543

                  ....
gi 755522197  977 MVDK 980
Cdd:PTZ00121 1544 EKKK 1547
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
899-966 3.59e-04

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 42.42  E-value: 3.59e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755522197  899 QRRLEAERMRLAEEEKL---RKEMSA--KKAKEEAERKHQERLAQlAREDAERELKEKEE--ARRKKELLEQMEK 966
Cdd:cd06503    44 KAKEEAEELLAEYEEKLaeaRAEAQEiiEEARKEAEKIKEEILAE-AKEEAERILEQAKAeiEQEKEKALAELRK 117
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
896-1001 3.88e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 45.18  E-value: 3.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  896 VEYQRRLEAERMRLAEEEKLRKEMSAKKAKEEAERKhqERLAQLAREDAERELKEKEE--ARRKKELLEQMEKA----RH 969
Cdd:PRK09510  173 AEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAK--KKAAAEAKKKAAAEAKAAAAkaAAEAKAAAEKAAAAkaaeKA 250
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 755522197  970 EPINHSDMVDKMFGFLGTSGSLPGQ------EGQAPSG 1001
Cdd:PRK09510  251 AAAKAAAEVDDLFGGLDSGKNAPKTgggakgNGAQGAG 288
PTZ00121 PTZ00121
MAEBL; Provisional
903-968 4.06e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 4.06e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755522197  903 EAERMRLAEEEKLRKEMSAKKAKE----EAERKHQERLAQLARE--DAERELKEKEEARRKKELLEQMEKAR 968
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADElkkaAAAKKKADEAKKKAEEkkKADEAKKKAEEAKKADEAKKKAEEAK 1457
SH3_PI3K_p85beta cd11909
Src Homology 3 domain of the p85beta regulatory subunit of Class IA Phosphatidylinositol ...
1660-1706 4.27e-04

Src Homology 3 domain of the p85beta regulatory subunit of Class IA Phosphatidylinositol 3-kinases; Class I PI3Ks convert PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. They are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. Class IA PI3Ks associate with the p85 regulatory subunit family, which contains SH3, RhoGAP, and SH2 domains. The p85 subunits recruit the PI3K p110 catalytic subunit to the membrane, where p110 phosphorylates inositol lipids. Vertebrates harbor two p85 isoforms, called alpha and beta. In addition to regulating the p110 subunit, p85beta binds CD28 and may be involved in the activation and differentiation of antigen-stimulated T cells. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212842  Cd Length: 74  Bit Score: 40.97  E-value: 4.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 755522197 1660 LSFAKGDLIILD-HDTGEQVMNS-GWANGINERTKQRGDFPTDCV-YVMP 1706
Cdd:cd11909    25 LTVSRAALQALGvKEGGEQCPQSiGWILGLNERTKQRGDFPGTYVeFLGP 74
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
839-970 5.05e-04

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 45.33  E-value: 5.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   839 RKLHKQYRLARQRIIEFQARcRAYLVRKafRHRLWAVitVQAYARGMiARRLHRRLRvEYQRRLEAERMRLAEEEKLR-K 917
Cdd:pfam15709  383 QRRFEEIRLRKQRLEEERQR-QEEEERK--QRLQLQA--AQERARQQ-QEEFRRKLQ-ELQRKKQQEEAERAEAEKQRqK 455
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 755522197   918 EMSAKKAKEeaerkhQERLAQLAREDAERELKEKEEArRKKELLEQMEKARHE 970
Cdd:pfam15709  456 ELEMQLAEE------QKRLMEMAEEERLEYQRQKQEA-EEKARLEAEERRQKE 501
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
887-1091 5.27e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 45.03  E-value: 5.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  887 ARRLHR--RLRVEYQRRLEAERMRLAE--EEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKKELLE 962
Cdd:COG3064    76 AKKLAEaeKAAAEAEKKAAAEKAKAAKeaEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAE 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  963 QMEKARHEPINHSDMVDKMFGFLGTSGSLPGQEGQAPSGFEDLERGRREMVEEDVDAALPLPDEDEEDLSEYKFAKFAAT 1042
Cdd:COG3064   156 AARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALA 235
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 755522197 1043 YFQGTTTHSYTRRPLKQPLLYHDDEGDQLAALAVWITILRFMGDLPEPK 1091
Cdd:COG3064   236 AVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAA 284
FERM_F1_PLEKHH2 cd17179
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in pleckstrin ...
1292-1386 5.54e-04

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in pleckstrin homology domain-containing family H member 2 (PLEKHH2); PLEKHH2 is a novel podocyte protein downregulated in human focal segmental glomerulosclerosis. It is highly enriched in renal glomerular podocytes, and acts as a novel, important component of the podocyte foot processes. PLEKHH2 contains a putative alpha-helical coiled-coil segment within the N-terminal half, and two Pleckstrin homology (PH) domains, a MyTH4 domain, and a FERM (Band 4.1, ezrin, radixin, moesin) domain within the C-terminal half. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PLEKHH2 is involved in matrix adhesion and actin dynamics. It directly interacts through its FERM domain with the focal adhesion protein Hic-5 and actin.


Pssm-ID: 340699  Cd Length: 103  Bit Score: 41.50  E-value: 5.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 1292 PIMLPVTFMDGTTKTLLTDSATTARELCNALADKISLKD--RFGFSLYIalfDKVSslGSGSDHVM-------DAISQCE 1362
Cdd:cd17179     1 PFSIPVHFMNGTYQVVGFDASTTVEEFLNTLNQDTGMRKpgQSGFALFT---DDPS--GKDLEHCLqgnikicDIISKWE 75
                          90       100
                  ....*....|....*....|....*.
gi 755522197 1363 QYAKEQ--GAQERNAPWRLFFRKEVF 1386
Cdd:cd17179    76 QASKEQhpGKCEGTRTVRLTYKNRLY 101
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
888-972 6.04e-04

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: 45.11  E-value: 6.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   888 RRLHRRLRVEYQRRLEAERMRLAEEEKLRkEMSAKKAKEEAERKHQ---ERLAQLARE------DAERELKEKEEARRKK 958
Cdd:pfam17380  282 KAVSERQQQEKFEKMEQERLRQEKEEKAR-EVERRRKLEEAEKARQaemDRQAAIYAEqermamERERELERIRQEERKR 360
                           90
                   ....*....|....
gi 755522197   959 ElleqMEKARHEPI 972
Cdd:pfam17380  361 E----LERIRQEEI 370
Efg1 pfam10153
rRNA-processing protein Efg1; Efg1 is involved in rRNA processing.
886-968 6.42e-04

rRNA-processing protein Efg1; Efg1 is involved in rRNA processing.


Pssm-ID: 462968 [Multi-domain]  Cd Length: 114  Bit Score: 41.34  E-value: 6.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   886 IARRLHRR------LRVEYQRRLEAERMRLAEEEKLRKE--MSAK--KAKeEAERKHQERlaQLARedAERELKEKEEAR 955
Cdd:pfam10153    8 IERLLAKKkdlpadVRVEKERELEALKSELEEAERKKKEkkMAKKyhMVR-FFERKKATR--KLKQ--LKKQLEEAEDEE 82
                           90
                   ....*....|...
gi 755522197   956 RKKELLEQMEKAR 968
Cdd:pfam10153   83 ERAKLEKQLHKAE 95
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
896-967 6.43e-04

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 44.94  E-value: 6.43e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755522197  896 VEYQRRLEAErMRLAEEEKlrkemsaKKAkEEAERKHQERLAQLAREDAERELKEKEEARRKKELLEQMEKA 967
Cdd:PRK05035  428 VQYYRQAKAE-IRAIEQEK-------KKA-EEAKARFEARQARLEREKAAREARHKKAAEARAAKDKDAVAA 490
PTZ00121 PTZ00121
MAEBL; Provisional
903-980 6.96e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 6.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  903 EAERMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAER----ELKEKEEARRKKELLEQMEKARHEPINHSDMV 978
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAkkadEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557

                  ..
gi 755522197  979 DK 980
Cdd:PTZ00121 1558 KK 1559
PRK12704 PRK12704
phosphodiesterase; Provisional
881-966 6.99e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.77  E-value: 6.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  881 YARGMIARRLHRRLRVEYQRRLEAERMRlAEEEKLRKEMSAK----KAKEEAERKHQERLAQLARedAERELKEKEEA-R 955
Cdd:PRK12704   23 FVRKKIAEAKIKEAEEEAKRILEEAKKE-AEAIKKEALLEAKeeihKLRNEFEKELRERRNELQK--LEKRLLQKEENlD 99
                          90
                  ....*....|.
gi 755522197  956 RKKELLEQMEK 966
Cdd:PRK12704  100 RKLELLEKREE 110
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
903-970 7.35e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 44.65  E-value: 7.35e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755522197  903 EAERMRlAEEEKLRKEMSAKKAKE--EAERKHQERLAQLAREDAERELKEKEEARRKKELL----EQMEKARHE 970
Cdd:COG3064    56 EAREAK-AEAEQRAAELAAEAAKKlaEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAaaekEKAEEAKRK 128
SH3_PI3K_p85alpha cd11910
Src Homology 3 domain of the p85alpha regulatory subunit of Class IA Phosphatidylinositol ...
1660-1698 7.39e-04

Src Homology 3 domain of the p85alpha regulatory subunit of Class IA Phosphatidylinositol 3-kinases; Class I PI3Ks convert PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. They are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. Class IA PI3Ks associate with the p85 regulatory subunit family, which contains SH3, RhoGAP, and SH2 domains. The p85 subunits recruit the PI3K p110 catalytic subunit to the membrane, where p110 phosphorylates inositol lipids. Vertebrates harbor two p85 isoforms, called alpha and beta. In addition to regulating the p110 subunit, p85alpha interacts with activated FGFR3. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212843  Cd Length: 75  Bit Score: 40.27  E-value: 7.39e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 755522197 1660 LSFAKGDLIILDHDTGEQVMNS--GWANGINERTKQRGDFP 1698
Cdd:cd11910    26 LTVNKGSLLALGFSEGQEARPEeiGWLNGYNETTGERGDFP 66
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
1506-1567 7.40e-04

FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 275389  Cd Length: 93  Bit Score: 40.82  E-value: 7.40e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755522197 1506 SRFYEAYKFSGPPlpkSDVIVAVNWTGVYFVDEQE-QVLLELSFPEIMAVSSSRECRVLLSLG 1567
Cdd:cd00836     2 VEFFPVKDKSKKG---SPIILGVNPEGISVYDELTgQPLVLFPWPNIKKISFSGAKKFTIVVA 61
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
901-970 7.48e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 41.44  E-value: 7.48e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755522197   901 RLEAERMRLAEEEKLRK-EMSAKKAKEEAERKHQ--ERLAQLAREdAERELKEKEEARRkkELLEQMEKARHE 970
Cdd:pfam20492    1 REEAEREKQELEERLKQyEEETKKAQEELEESEEtaEELEEERRQ-AEEEAERLEQKRQ--EAEEEKERLEES 70
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
892-962 7.50e-04

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 42.72  E-value: 7.50e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755522197   892 RRLRVEYQRRLEAERMRLAEEEKLRKEMSAKKAKEEAERkhQERLAQLAREDAERELKEKEEARRKKELLE 962
Cdd:pfam09756    9 AKLELKEAKRQQREAEEEEREEREKLEEKREEEYKEREE--REEEAEKEKEEEERKQEEEQERKEQEEYEK 77
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
841-970 7.95e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 7.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  841 LHKQY-RLARQRII-----EFQARCRAYLVRKAFRHRLWAVITVQAYARGMIARRLHRRLRVEYQRRLEAERMRLAEE-E 913
Cdd:COG1196   198 LERQLePLERQAEKaeryrELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLElE 277
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755522197  914 KLRKEMSAKKAkeeAERKHQERLAQLAREDAERELKEKEEARRKKELLEQMEKARHE 970
Cdd:COG1196   278 ELELELEEAQA---EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
912-970 8.04e-04

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 41.65  E-value: 8.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755522197  912 EEKLRKEM-SAKKAKEEAERKHQERLAQL--AREDAERELKE-KEEARRKKEllEQMEKARHE 970
Cdd:cd06503    32 EEKIAESLeEAEKAKEEAEELLAEYEEKLaeARAEAQEIIEEaRKEAEKIKE--EILAEAKEE 92
PTZ00121 PTZ00121
MAEBL; Provisional
903-968 8.88e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 8.88e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755522197  903 EAERMRLAEEEKlRKEMSAKKAKEEAERKHQERLAQLAREDAER------ELKEKEEARRKKELLEQMEKAR 968
Cdd:PTZ00121 1452 KAEEAKKAEEAK-KKAEEAKKADEAKKKAEEAKKADEAKKKAEEakkkadEAKKAAEAKKKADEAKKAEEAK 1522
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
831-975 9.11e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 9.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  831 RLQALH-RSRKLHKQYRLARQRIIEFQ---ARCRAYLVRKAFRHRLWAVITVQAYARGMIARRLHRRLRVEYQRRLEAER 906
Cdd:COG4913   700 ELEELEeELDELKGEIGRLEKELEQAEeelDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALR 779
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  907 MRLA-EEEKLRKEMSAKKAK-----------EEAERKHQERLAQLAREDAER------ELKEKEEARRKKELLEQMEKAR 968
Cdd:COG4913   780 ARLNrAEEELERAMRAFNREwpaetadldadLESLPEYLALLDRLEEDGLPEyeerfkELLNENSIEFVADLLSKLRRAI 859
                         170
                  ....*....|...
gi 755522197  969 HE------PINHS 975
Cdd:COG4913   860 REikeridPLNDS 872
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
881-970 1.06e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 41.70  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  881 YARGMIARRLHRRlrveyQRRLEAErmrLAEEEKLRKEmsAKKAKEEAERKHQErlaqlAREDAERELKE-KEEARRKKE 959
Cdd:COG0711    20 FAWPPILKALDER-----QEKIADG---LAEAERAKEE--AEAALAEYEEKLAE-----ARAEAAEIIAEaRKEAEAIAE 84
                          90
                  ....*....|.
gi 755522197  960 llEQMEKARHE 970
Cdd:COG0711    85 --EAKAEAEAE 93
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
897-966 1.12e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 43.71  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  897 EYQRRLEAERMRLAEEEK-LRKEMSAKKAKEEAERKHQERLAQLAR-----------EDAERE----LKEKEEARRKKEL 960
Cdd:COG2268   227 ELEQEREIETARIAEAEAeLAKKKAEERREAETARAEAEAAYEIAEanaerevqrqlEIAEREreieLQEKEAEREEAEL 306

                  ....*.
gi 755522197  961 LEQMEK 966
Cdd:COG2268   307 EADVRK 312
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
899-971 1.13e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 43.68  E-value: 1.13e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755522197   899 QRRLEAERMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKKELLEQME----KARHEP 971
Cdd:TIGR02794   54 RIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQaeeaKAKQAA 130
PTZ00121 PTZ00121
MAEBL; Provisional
895-1033 1.16e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  895 RVEYQRRLEAERMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKKelLEQMEKARHEPINH 974
Cdd:PTZ00121 1668 KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIK--AEEAKKEAEEDKKK 1745
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 755522197  975 SDMVDKMFGFLGTSGSLPGQEGQAPsgfEDLERGRREMVEEDVDaalplpDEDEEDLSE 1033
Cdd:PTZ00121 1746 AEEAKKDEEEKKKIAHLKKEEEKKA---EEIRKEKEAVIEEELD------EEDEKRRME 1795
DUF6481 pfam20089
Family of unknown function (DUF6481); This family of proteins is functionally uncharacterized. ...
893-968 1.18e-03

Family of unknown function (DUF6481); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are approximately 120 amino acids in length.


Pssm-ID: 437921 [Multi-domain]  Cd Length: 119  Bit Score: 40.86  E-value: 1.18e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755522197   893 RLRVEYQRRLEAERMRLA---EEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKKELLEQMEKAR 968
Cdd:pfam20089   40 ERAAERAAELAAVRAAREaerAAARRAAAEAEEAAREAAAAAAAEALDAKRAERKERKAALKAEQKAARDARYAARKAR 118
SH3_BAIAP2L1 cd11913
Src Homology 3 domain of Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 1, ...
1650-1699 1.35e-03

Src Homology 3 domain of Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 1, also called Insulin Receptor Tyrosine Kinase Substrate (IRTKS); BAIAP2L1 or IRTKS is widely expressed, serves as a substrate for the insulin receptor, and binds the small GTPase Rac. It plays a role in regulating the actin cytoskeleton and colocalizes with F-actin, cortactin, VASP, and vinculin. BAIAP2L1 expression leads to the formation of short actin bundles, distinct from filopodia-like protrusions induced by the expression of the related protein IRSp53. IRTKS mediates the recruitment of effector proteins Tir and EspFu, which regulate host cell actin reorganization, to bacterial attachment sites. It contains an N-terminal IMD or Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. The SH3 domain of IRTKS has been shown to bind the proline-rich C-terminus of EspFu. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212846  Cd Length: 58  Bit Score: 38.74  E-value: 1.35e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 755522197 1650 PNPAGEESGFLSFAKGDLIIL----DHDtgeqvmnsGWANGINERTKQRGDFPT 1699
Cdd:cd11913     8 PHTAGNNKTLLSFAQGDVITLlipeEKD--------GWLYGEHDTTKARGWFPS 53
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
1394-1476 1.41e-03

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 40.72  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  1394 EDNVATNLIYQQVVRGVKFGEYRCEkEDDLAELASQQYFVDYGS------EMILERLLSLVPtyipdREITPLKNLEKWA 1467
Cdd:pfam00373    7 QDEVTRHLLYLQAKDDILEGRLPCS-EEEALLLAALQLQAEFGDyqpsshTSEYLSLESFLP-----KQLLRKMKSKELE 80

                   ....*....
gi 755522197  1468 QLAIAAHKK 1476
Cdd:pfam00373   81 KRVLEAHKN 89
FERM_F1_PLEKHH1 cd17178
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in pleckstrin ...
1292-1386 1.42e-03

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in pleckstrin homology domain-containing family H member 1 (PLEKHH1); PLEKHH1 is a homolog of Caenorhabditis elegans MAX-1 that has been implicated in motor neuron axon guidance. PLEKHH1 is critical in vascular patterning in vertebrate species through acting upstream of the ephrin pathway. PLEKHH1 contains a putative alpha-helical coiled-coil segment within the N-terminal half, and two Pleckstrin homology (PH) domains, a MyTH4 domain, and a FERM (Band 4.1, ezrin, radixin, moesin) domain within the C-terminal half. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340698  Cd Length: 106  Bit Score: 40.33  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197 1292 PIMLPVTFMDGTTKTLLTDSATTARELCNALADKISLK--DRFGFSLYIalfDKVSSLG-----SGSDHVMDAISQCEQY 1364
Cdd:cd17178     1 PFSIPVHFMNGTYQVVGFDGSTTVDEFLQTLNQETGMRkpSHSGFALFT---DDPSGKDlehclQGSVKICDVISKWEQA 77
                          90       100
                  ....*....|....*....|....
gi 755522197 1365 AKE--QGAQERNAPWRLFFRKEVF 1386
Cdd:cd17178    78 LKElhPGKYEGTRTVRLTYKSRLY 101
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
892-965 1.46e-03

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 41.96  E-value: 1.46e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755522197   892 RRLRVEYQRRL--EAERMRLAEEEKLRKEMSAKKAKEEAERKHQerlaqlaREDAERELKEKEEA--RRKKELLEQME 965
Cdd:pfam15927    1 ARLREEEEERLraEEEEAERLEEERREEEEEERLAAEQDRRAEE-------LEELKHLLEERKEAleKLRAEAREEAE 71
PLC-beta_C pfam08703
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ...
896-980 1.50e-03

PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of phospholipase C beta.


Pssm-ID: 462571 [Multi-domain]  Cd Length: 176  Bit Score: 41.59  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   896 VEYQRRLEAERMRLAEEEKLRKemsaKKAKEEAERKHQERLAQLAREDAERELKEKEEA--RRKKELLEQMEKARHEPIN 973
Cdd:pfam08703    4 RELKERLEQELLELREEQYEQE----KKRKEQHLTEQIQKLKELAREKQAAELKALKESseSEKKEMKKKLERKRLESIQ 79

                   ....*..
gi 755522197   974 HSDMVDK 980
Cdd:pfam08703   80 EAKKRTS 86
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
904-970 1.53e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 43.32  E-value: 1.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755522197  904 AERMRLAEEEKLRKEM---SAKKAKEEAE---RKHQERL-AQLAREDAERELKEkEEARRKKELLEQMEKARHE 970
Cdd:COG2268   217 AQANREAEEAELEQEReieTARIAEAEAElakKKAEERReAETARAEAEAAYEI-AEANAEREVQRQLEIAERE 289
growth_prot_Scy NF041483
polarized growth protein Scy;
901-970 1.55e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 44.05  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  901 RLEAERMR-----LAEEEKLRKEMSAKKAKEEAERKHQERLAQLARE------DAERELKEKEEA---------RRKKEL 960
Cdd:NF041483  530 RAEAERLRaeaeeQAEEVRAAAERAARELREETERAIAARQAEAAEEltrlhtEAEERLTAAEEAladaraeaeRIRREA 609
                          90
                  ....*....|
gi 755522197  961 LEQMEKARHE 970
Cdd:NF041483  610 AEETERLRTE 619
growth_prot_Scy NF041483
polarized growth protein Scy;
903-976 1.59e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 44.05  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  903 EAERMRlAEE-----------EKLRKEmsAKKAKEEAERKhQERLAQLAREDAERELKE--KEEARRKKELLEQMEKARH 969
Cdd:NF041483  969 EAERLR-AEAaetvgsaqqhaERIRTE--AERVKAEAAAE-AERLRTEAREEADRTLDEarKDANKRRSEAAEQADTLIT 1044

                  ....*..
gi 755522197  970 EPINHSD 976
Cdd:NF041483 1045 EAAAEAD 1051
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
917-978 1.62e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 43.04  E-value: 1.62e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755522197   917 KEMSAKKAKEEAERKHQERLAQLAREDAER-ELKEKEEARRKKELLEQMEKARHEPINHSDMV 978
Cdd:pfam02841  204 KAIEAERAKAEAAEAEQELLREKQKEEEQMmEAQERSYQEHVKQLIEKMEAEREQLLAEQERM 266
NtpH COG2811
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ...
917-970 1.64e-03

Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit H is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 442060 [Multi-domain]  Cd Length: 108  Bit Score: 40.28  E-value: 1.64e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755522197  917 KEMSAKKAKEEAERKHQERLAQlAREDAERELKE-KEEARRKKEllEQMEKARHE 970
Cdd:COG2811    13 AEEEADEIIEEAKEEREERIAE-AREEAEEIIEQaEEEAEEEAQ--ERLEEAREE 64
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
885-980 1.96e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  885 MIARRLHRRLRVEyQRRLEAERMrLAEEEKLRKEMSAKKAKEEAERkhqERLAQLAREDAERELKE-KEEARRKKELLEQ 963
Cdd:PRK00409  521 LIASLEELERELE-QKAEEAEAL-LKEAEKLKEELEEKKEKLQEEE---DKLLEEAEKEAQQAIKEaKKEADEIIKELRQ 595
                          90
                  ....*....|....*..
gi 755522197  964 MEKARHEPINHSDMVDK 980
Cdd:PRK00409  596 LQKGGYASVKAHELIEA 612
COG3899 COG3899
Predicted ATPase [General function prediction only];
795-956 2.05e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 43.69  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  795 DRSNFLRLKSAATLIQ---RHWRGHHcRKNYELIRLGF-----------LRLQALHRSRKLHKQYRLARQRIIEFQARCR 860
Cdd:COG3899   821 ERLGDRRLEARALFNLgfiLHWLGPL-REALELLREALeagletgdaalALLALAAAAAAAAAAAALAAAAAAAARLLAA 899
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  861 AYLVRKAFRHRLWAVITVQAYARGMIARRLHRRLRVEYQRRLEAERMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLA 940
Cdd:COG3899   900 AAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAA 979
                         170
                  ....*....|....*.
gi 755522197  941 REDAERELKEKEEARR 956
Cdd:COG3899   980 AAAAAAAAAAALEAAA 995
V-ATPase_G_2 pfam16999
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ...
897-971 2.11e-03

Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from several bacterial and archaeal species. Subunit G is a component of the peripheral stalk of the ATPase complex


Pssm-ID: 339878 [Multi-domain]  Cd Length: 104  Bit Score: 39.73  E-value: 2.11e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755522197   897 EYQRRLEAERmRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKKELLEQMEKARHEP 971
Cdd:pfam16999   16 ALDQQIEAAR-KEAEREVEAAEAEAARILREAEAKAKALQAEYRQELAAETARIREEARARAEAEAQAVRTRAEG 89
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
829-970 2.22e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.60  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   829 FLRLQALHRSRKLHKQYRLARQRIIEFQ---ARCRAYLVRKAFRHRLWAVITVQAYARgmiarRLHRRLRVEYQRRLEAE 905
Cdd:pfam13868  160 YLKEKAEREEEREAEREEIEEEKEREIArlrAQQEKAQDEKAERDELRAKLYQEEQER-----KERQKEREEAEKKARQR 234
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   906 R-MRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRK----KELLEQMEKARHE 970
Cdd:pfam13868  235 QeLQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKrlehRRELEKQIEEREE 304
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
887-966 2.38e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.60  E-value: 2.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   887 ARRLHRRLRvEYQRRLEAERMRLAEEEKLRKEMSA-KKAKEEAER------------------KHQERLAQLAREDAERE 947
Cdd:pfam13868  240 AREEQIELK-ERRLAEEAEREEEEFERMLRKQAEDeEIEQEEAEKrrmkrlehrrelekqieeREEQRAAEREEELEEGE 318
                           90
                   ....*....|....*....
gi 755522197   948 LKEKEEARRKKELLEQMEK 966
Cdd:pfam13868  319 RLREEEAERRERIEEERQK 337
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
832-971 2.70e-03

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 41.61  E-value: 2.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   832 LQALHRSRKLHKQYRLARQRIIE--FQARCRaylvRKAfrhrlwavitvqayargmiarRLHRRLRVEYQRRLEAER--M 907
Cdd:pfam13904   72 LQAQKEEREKEEQEAELRKRLAKekYQEWLQ----RKA---------------------RQQTKKREESHKQKAAESasK 126
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755522197   908 RLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKKELLEQ-----MEKARHEP 971
Cdd:pfam13904  127 SLAKPERKVSQEEAKEVLQEWERKKLEQQQRKREEEQREQLKKEEEEQERKQLAEKawqkwMKNVKNKP 195
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
831-965 2.82e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  831 RLQALHRSRKLHKQYRLARQRIIEFQARcraylvrkafRHRLWAVITVQAYARgmiARRLHRRLRVEyQRRLEAERMRLA 910
Cdd:COG4913   250 QIELLEPIRELAERYAAARERLAELEYL----------RAALRLWFAQRRLEL---LEAELEELRAE-LARLEAELERLE 315
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755522197  911 EEEKLrkemsAKKAKEEAERKHQE----RLAQLARE--DAERELKEKEEARRK-KELLEQME 965
Cdd:COG4913   316 ARLDA-----LREELDELEAQIRGnggdRLEQLEREieRLERELEERERRRARlEALLAALG 372
SH3_Irsp53 cd11915
Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53; IRSp53 is also known ...
1653-1698 2.89e-03

Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53; IRSp53 is also known as BAIAP2 (Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2). It is a scaffolding protein that takes part in many signaling pathways including Cdc42-induced filopodia formation, Rac-mediated lamellipodia extension, and spine morphogenesis. IRSp53 exists as multiple splicing variants that differ mainly at the C-termini. One variant (T-form) is expressed exclusively in human breast cancer cells. The gene encoding IRSp53 is a putative susceptibility gene for Gilles de la Tourette syndrome. IRSp53 can also mediate the recruitment of effector proteins Tir and EspFu, which regulate host cell actin reorganization, to bacterial attachment sites. It contains an N-terminal IMD, a CRIB (Cdc42 and Rac interactive binding motif), an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. The SH3 domain of IRSp53 has been shown to bind the proline-rich C-terminus of EspFu. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212848  Cd Length: 59  Bit Score: 38.07  E-value: 2.89e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 755522197 1653 AGEESGFLSFAKGDLIILDHDTGEqvmnSGWANGINERTKQRGDFP 1698
Cdd:cd11915    11 AGDNSTLLSFKEGDYITLLVPEAR----DGWHYGECEKTKMRGWFP 52
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
909-970 2.91e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 40.11  E-value: 2.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755522197  909 LAEEEKLRKEMSAKKAK-----EEAERKHQERLAQlAREDAERELKE-KEEARRKKELLeqMEKARHE 970
Cdd:cd06503    39 LEEAEKAKEEAEELLAEyeeklAEARAEAQEIIEE-ARKEAEKIKEEiLAEAKEEAERI--LEQAKAE 103
SH3_Amphiphysin cd11790
Src Homology 3 domain of Amphiphysin and related domains; Amphiphysins function primarily in ...
1654-1698 2.92e-03

Src Homology 3 domain of Amphiphysin and related domains; Amphiphysins function primarily in endocytosis and other membrane remodeling events. They exist in several isoforms and mammals possess two amphiphysin proteins from distinct genes. Amphiphysin I proteins, enriched in the brain and nervous system, contain domains that bind clathrin, Adaptor Protein complex 2 (AP2), dynamin, and synaptojanin. They function in synaptic vesicle endocytosis. Human autoantibodies to amphiphysin I hinder GABAergic signaling and contribute to the pathogenesis of paraneoplastic stiff-person syndrome. Some amphiphysin II isoforms, also called Bridging integrator 1 (Bin1), are localized in many different tissues and may function in intracellular vesicle trafficking. In skeletal muscle, Bin1 plays a role in the organization and maintenance of the T-tubule network. Mutations in Bin1 are associated with autosomal recessive centronuclear myopathy. Amphiphysins contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. The SH3 domain of amphiphysins bind proline-rich motifs present in binding partners such as dynamin, synaptojanin, and nsP3. It also belongs to a subset of SH3 domains that bind ubiquitin in a site that overlaps with the peptide binding site. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212724 [Multi-domain]  Cd Length: 64  Bit Score: 38.08  E-value: 2.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 755522197 1654 GEESGFLSFAKGDLI-ILDHDTGEQvMNSGWANGINERTKQRGDFP 1698
Cdd:cd11790    13 AEDTDELTFEKGDVIlVIPFDDPEE-QDEGWLMGVKESTGCRGVFP 57
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
803-822 2.99e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 36.91  E-value: 2.99e-03
                           10        20
                   ....*....|....*....|
gi 755522197   803 KSAATLIQRHWRGHHCRKNY 822
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRY 20
SH3_PI3K_p85 cd11776
Src Homology 3 domain of the p85 regulatory subunit of Class IA Phosphatidylinositol 3-kinases; ...
1682-1698 3.01e-03

Src Homology 3 domain of the p85 regulatory subunit of Class IA Phosphatidylinositol 3-kinases; Class I PI3Ks convert PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. They are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. Class IA PI3Ks associate with the p85 regulatory subunit family, which contains SH3, RhoGAP, and SH2 domains. The p85 subunits recruit the PI3K p110 catalytic subunit to the membrane, where p110 phosphorylates inositol lipids. Vertebrates harbor two p85 isoforms, called alpha and beta. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212710  Cd Length: 72  Bit Score: 38.26  E-value: 3.01e-03
                          10
                  ....*....|....*..
gi 755522197 1682 GWANGINERTKQRGDFP 1698
Cdd:cd11776    49 GWLEGKNERTGERGDFP 65
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
900-972 3.28e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 42.55  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  900 RRLEAERMRLAEEEKLRKEMSAKKAKEEAERK--------HQERLAQLAREDAERELKEKEEARRK-----KELLEQMEK 966
Cdd:COG2268   247 AKKKAEERREAETARAEAEAAYEIAEANAEREvqrqleiaEREREIELQEKEAEREEAELEADVRKpaeaeKQAAEAEAE 326

                  ....*.
gi 755522197  967 ARHEPI 972
Cdd:COG2268   327 AEAEAI 332
Stathmin pfam00836
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ...
897-970 3.46e-03

Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.


Pssm-ID: 459956 [Multi-domain]  Cd Length: 136  Bit Score: 40.02  E-value: 3.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   897 EYQRRLE-AERMRLAEEEKLRKEMSAKKAKE-EAERKHQERLAQLAREdAEREL-------KEKEEAR------RKKELL 961
Cdd:pfam00836   46 EIQKKLEaAEERRKSLEAQKLKQLAEKREKEeEALQKADEENNNFSKM-AEEKLkqkmeayKENREAQiaalkeKLKEKE 124

                   ....*....
gi 755522197   962 EQMEKARHE 970
Cdd:pfam00836  125 KHVEEVRKN 133
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
902-970 3.54e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 42.17  E-value: 3.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755522197  902 LEAERMRLAEEekLRKEmsAKKAKEEAER------KHQERLAQLAREDAERELKEKEEARRKKELLEQMEKARHE 970
Cdd:COG2268   186 LDALGRRKIAE--IIRD--ARIAEAEAEReteiaiAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERRE 256
SH3_MYO15 cd11884
Src Homology 3 domain of Myosin XV; This subfamily is composed of proteins with similarity to ...
1642-1702 3.59e-03

Src Homology 3 domain of Myosin XV; This subfamily is composed of proteins with similarity to Myosin XVa. Myosin XVa is an unconventional myosin that is critical for the normal growth of mechanosensory stereocilia of inner ear hair cells. Mutations in the myosin XVa gene are associated with nonsyndromic hearing loss. Myosin XVa contains a unique N-terminal extension followed by a motor domain, light chain-binding IQ motifs, and a tail consisting of a pair of MyTH4-FERM tandems separated by a SH3 domain, and a PDZ domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212817 [Multi-domain]  Cd Length: 56  Bit Score: 37.69  E-value: 3.59e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755522197 1642 YVVALQDNpnpAGEESGFLSFAKGDLIILDHDtgEQVMNSGWANG-INERTkqrGDFPTDCV 1702
Cdd:cd11884     1 YVVAVRAY---ITRDQTLLSFHKGDVIKLLPK--EGPLDPGWLFGtLDGRS---GAFPKEYV 54
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
892-970 3.68e-03

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 41.23  E-value: 3.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   892 RRLRVEYQRRLEAERMRLAEEEKLRKEMSA--------KKAKEEAERK-----------HQERLAQLAREDAERELKEK- 951
Cdd:pfam13904   65 QRQRQKELQAQKEEREKEEQEAELRKRLAKekyqewlqRKARQQTKKReeshkqkaaesASKSLAKPERKVSQEEAKEVl 144
                           90       100
                   ....*....|....*....|....*....
gi 755522197   952 ----------EEARRKKELLEQMEKARHE 970
Cdd:pfam13904  145 qewerkkleqQQRKREEEQREQLKKEEEE 173
SH3_Irsp53_BAIAP2L cd11779
Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53, Brain-specific ...
1660-1698 3.88e-03

Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53, Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2 (BAIAP2)-Like proteins, and similar proteins; Proteins in this family include IRSp53, BAIAP2L1, BAIAP2L2, and similar proteins. They all contain an Inverse-Bin/Amphiphysin/Rvs (I-BAR) or IMD domain in addition to the SH3 domain. IRSp53, also known as BAIAP2, is a scaffolding protein that takes part in many signaling pathways including Cdc42-induced filopodia formation, Rac-mediated lamellipodia extension, and spine morphogenesis. IRSp53 exists as multiple splicing variants that differ mainly at the C-termini. BAIAP2L1, also called IRTKS (Insulin Receptor Tyrosine Kinase Substrate), serves as a substrate for the insulin receptor and binds the small GTPase Rac. It plays a role in regulating the actin cytoskeleton and colocalizes with F-actin, cortactin, VASP, and vinculin. IRSp53 and IRTKS also mediate the recruitment of effector proteins Tir and EspFu, which regulate host cell actin reorganization, to bacterial attachment sites. BAIAP2L2 co-localizes with clathrin plaques but its function has not been determined. The SH3 domains of IRSp53 and IRTKS have been shown to bind the proline-rich C-terminus of EspFu. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212713 [Multi-domain]  Cd Length: 57  Bit Score: 37.69  E-value: 3.88e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 755522197 1660 LSFAKGDLIILdhdTGEQVMNsGWANGINERTKQRGDFP 1698
Cdd:cd11779    17 LSFEEGDVITL---LGPEPRD-GWHYGENERSGRRGWFP 51
PRK00247 PRK00247
putative inner membrane protein translocase component YidC; Validated
854-1001 3.90e-03

putative inner membrane protein translocase component YidC; Validated


Pssm-ID: 178945 [Multi-domain]  Cd Length: 429  Bit Score: 42.15  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  854 EFQARCRA-YLVRK-AFRHRLWAVitvqAYARGMIARRLHR--RLRVEyQRRLEAERMRLAEEEKLRKEMSAKKaKEEAE 929
Cdd:PRK00247  285 EHHAEQRAqYREKQkEKKAFLWTL----RRNRLRMIITPWRapELHAE-NAEIKKTRTAEKNEAKARKKEIAQK-RRAAE 358
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755522197  930 RKHQERLAQLAREDAERELKEKEEARRKKELLEQMEKARHEPINHSDmvdkmfgflgTSGSLPGQEGQAPSG 1001
Cdd:PRK00247  359 REINREARQERAAAMARARARRAAVKAKKKGLIDASPNEDTPSENEE----------SKGSPPQVEATTTAE 420
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
888-970 5.02e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.44  E-value: 5.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   888 RRLHRRLRVEYQRrleAERMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKKELLEQMEKA 967
Cdd:pfam13868    9 RELNSKLLAAKCN---KERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEER 85

                   ...
gi 755522197   968 RHE 970
Cdd:pfam13868   86 EQK 88
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
818-970 5.53e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 41.56  E-value: 5.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   818 CRKNYELIRLGFLRLQALHRSRKLHKQyrlARQRIIEFQARCRAYLVRKAFRHRLWAVITVqaYARGMIARrlHRRLRVE 897
Cdd:pfam15558  155 CHKRQLKEREEQKKVQENNLSELLNHQ---ARKVLVDCQAKAEELLRRLSLEQSLQRSQEN--YEQLVEER--HRELREK 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   898 YQRrleaermrlaEEEKLRKemsAKKAKEEAERKHQER---LAQL-------AREDAERELKEKeeARRKKELLEQMEKA 967
Cdd:pfam15558  228 AQK----------EEEQFQR---AKWRAEEKEEERQEHkeaLAELadrkiqqARQVAHKTVQDK--AQRARELNLEREKN 292

                   ...
gi 755522197   968 RHE 970
Cdd:pfam15558  293 HHI 295
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
894-945 5.89e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 37.25  E-value: 5.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755522197  894 LRVEYQ---RRLEAERMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAE 945
Cdd:cd22249     7 IREEYEaqlKKLEEERRKEREEEEKASEELIRKLQEEEERQRKREREEQLKQDEE 61
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
887-968 6.72e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 6.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  887 ARRLHRRLRvEYQRRLEAERMRLAEEE--KLRKEMSAKKAKEEAERKHQERLAQLArEDAERELKEKEEARRKkelLEQM 964
Cdd:PRK03918  642 LEELRKELE-ELEKKYSEEEYEELREEylELSRELAGLRAELEELEKRREEIKKTL-EKLKEELEEREKAKKE---LEKL 716

                  ....
gi 755522197  965 EKAR 968
Cdd:PRK03918  717 EKAL 720
TAF4 pfam05236
Transcription initiation factor TFIID component TAF4 family; This region of similarity is ...
921-969 6.89e-03

Transcription initiation factor TFIID component TAF4 family; This region of similarity is found in Transcription initiation factor TFIID component TAF4.


Pssm-ID: 461598 [Multi-domain]  Cd Length: 264  Bit Score: 40.72  E-value: 6.89e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 755522197   921 AKKAKEEAERKHQERLAQLAREDAERELKEK-EEARRKKELLEQ----MEKARH 969
Cdd:pfam05236  120 AQKDKEEEERRVAEEREGLLKAAKSRSNQEDpEQLKLKQEAKEMqkeeDEKMRH 173
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
891-963 7.37e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.64  E-value: 7.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755522197  891 HRRLRVEYQRRLEAERMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEEARRKKeLLEQ 963
Cdd:cd16269   197 EKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESK-LKEQ 268
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
917-970 7.76e-03

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 39.64  E-value: 7.76e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   917 KEMSAKKAKEEAERkhQERLAQLAREDAERELKEKEEARR------KKELLEQMEKARHE 970
Cdd:pfam09756    1 KKLGAKKRAKLELK--EAKRQQREAEEEEREEREKLEEKReeeykeREEREEEAEKEKEE 58
CCDC50_N pfam15295
Coiled-coil domain-containing protein 50 N-terminus;
859-968 8.59e-03

Coiled-coil domain-containing protein 50 N-terminus;


Pssm-ID: 464621 [Multi-domain]  Cd Length: 126  Bit Score: 38.55  E-value: 8.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197   859 CRAYLVRK--AFRHRLWAVITVQAYARGMIARRLHRR-LRVEYQRRLEAERMRLAEEEKLRKEMsaKKAKEEAERKHQER 935
Cdd:pfam15295   15 CQEFAVLEdgALAHNLQEQEIEHHYATNIQRNQLVQNdIRVAKQLQEEEELQAQTLFQRRLAQL--EEQDEEIAKEIQEE 92
                           90       100       110
                   ....*....|....*....|....*....|...
gi 755522197   936 LAQLAREDAERELKEKEEARRKKELLEQMEKAR 968
Cdd:pfam15295   93 LQREAEERRRREEEDEEIARQLQERERERERRR 125
PRK12704 PRK12704
phosphodiesterase; Provisional
899-970 8.68e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 8.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  899 QRRLEAERMRLAEEEK--LRKEMSAKKAKEEAERKHQ------ERLAQLAREDAerelkekeearrKKELLEQME-KARH 969
Cdd:PRK12704  102 LELLEKREEELEKKEKelEQKQQELEKKEEELEELIEeqlqelERISGLTAEEA------------KEILLEKVEeEARH 169

                  .
gi 755522197  970 E 970
Cdd:PRK12704  170 E 170
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
887-968 8.78e-03

Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441000 [Multi-domain]  Cd Length: 196  Bit Score: 39.54  E-value: 8.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755522197  887 ARRLHRRLRVEYQRrlEAERMRLAEEEKLRKEMSA--KKAKEEAERKHQERLAQlaredAERELKeKEEARRKKELLEQ- 963
Cdd:COG1390    15 AEAEAEEILEEAEE--EAEKILEEAEEEAEEIKEEilEKAEREAEREKRRIISS-----AELEAR-KELLEAKEELIEEv 86

                  ....*
gi 755522197  964 MEKAR 968
Cdd:COG1390    87 FEEAL 91
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
899-966 9.60e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 39.00  E-value: 9.60e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755522197  899 QRRLEAERMRLAEEEKL---RKEMSA--KKAKEEAERKHQERLAQlAREDAERELKEKEE--ARRKKELLEQMEK 966
Cdd:COG0711    45 RAKEEAEAALAEYEEKLaeaRAEAAEiiAEARKEAEAIAEEAKAE-AEAEAERIIAQAEAeiEQERAKALAELRA 118
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
901-961 9.93e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 36.48  E-value: 9.93e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755522197  901 RLEAERMRLAEEEKLRKEmsakkaKEEAERKHQERLAQLAREDAERELKEKEEARRKKELL 961
Cdd:cd22249     8 REEYEAQLKKLEEERRKE------REEEEKASEELIRKLQEEEERQRKREREEQLKQDEEL 62
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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