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Database: UniProt
Entry: H3CYF1_TETNG
LinkDB: H3CYF1_TETNG
Original site: H3CYF1_TETNG 
ID   H3CYF1_TETNG            Unreviewed;      1816 AA.
AC   H3CYF1;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Myosin VB {ECO:0000313|Ensembl:ENSTNIP00000013286.1};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000013286.1, ECO:0000313|Proteomes:UP000007303};
RN   [1] {ECO:0000313|Proteomes:UP000007303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|Ensembl:ENSTNIP00000013286.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC       ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   Ensembl; ENSTNIT00000013478.1; ENSTNIP00000013286.1; ENSTNIG00000010379.1.
DR   GeneTree; ENSGT00940000155402; -.
DR   HOGENOM; CLU_000192_9_1_1; -.
DR   Proteomes; UP000007303; Unassembled WGS sequence.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   CDD; cd01380; MYSc_Myo5; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 3.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.30.70.1590; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   InterPro; IPR002710; Dilute_dom.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
DR   InterPro; IPR036103; MYSc_Myo5.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF289; UNCONVENTIONAL MYOSIN-XIX; 1.
DR   Pfam; PF01843; DIL; 1.
DR   Pfam; PF00612; IQ; 4.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM01132; DIL; 1.
DR   SMART; SM00015; IQ; 6.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51126; DILUTE; 1.
DR   PROSITE; PS50096; IQ; 5.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000007303}.
FT   DOMAIN          8..65
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          69..756
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1491..1771
FT                   /note="Dilute"
FT                   /evidence="ECO:0000259|PROSITE:PS51126"
FT   REGION          600..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          635..657
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1083..1117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1163..1189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1193..1258
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1315..1404
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1092..1117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         163..170
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1816 AA;  209456 MW;  3F584C91EE740BD1 CRC64;
     LYSEELEEQF TRVWIPDPEE VWKAAEITRD YKEGETVLHL KLEDETPLEY AVGAKGKPLP
     FLRNPDILVG ENDLTALSYL HEPAVLHNLR VRFLESNHIY TYCGIVLVAI NPYEQLQIYG
     EEVITAYSGQ NMGDMDPHIF AVAEEAYKQM ARDERNQSII VSGESGAGKT VSAKYAMRFF
     ATVGGSANDT NVEEKVLASS PIMEAIGNAK TTRNDNSSRF GKYIQIGFSR RYHIIGANMR
     TYLLEKSRVV FQAEDERNYH IFYQLCASAS LPEFKDLALT SAEEFTYTSY GENIFIEGVN
     DAEDFVKTRE GFVFFLGIKD STQNNVFKII ASILHLGNIE ICSERDEDSC HISRDDIHLK
     HFCRLLGVEL QQMEHWLCHR KLVTSAETYV KNMTSKQANN ARAALAKHIY ARMFDWIVDH
     INMALQTSSK QHSFIGVLDI YGFETFEVNS FEQFCINYAN EKLQQQFNSH VFKLEQEEYM
     KEEIPWTMIE YYDNQPCIDL IEARLGVLDL LDEECKVPKG TDQNWAQKLY KQHSSSAHFQ
     KPRMSNISFI IIHFADEVEY QCEGFLEKNR DRVYEEQINI LKASQFQLVA DLFHEKEDAG
     PSKSARVNVR PAKSIPKASN KDHKKTVGHQ FRSSLHLLMD TLNATTPHYV RCIKPNDFKE
     AFTFDSGRAV QQLRACGVLE TIRISAAGYP SRWTYSDFFN RYRVLMTKSD MMSTDKKLVC
     KNLLKTLIKE PDMFQFGKTK IFFRAGQVAY LEKLRADKFR AACIKIQKTV RGWLQRVRYR
     KIYRAAVTLQ RYGRGYLARR YAEYLRLSRA VVICQKQYRM VRERRAYLRV RQAVITIQAY
     TRGMYTRRIY WVFLQHHRAM IIQKYVRGWL QRRKFNRARA AAITIQCAYR RTLAKRQLKQ
     LKIEARSAEH LKKLNTGMEN KIVQMQRKMD EQSKDFKAQN EQLLLVNTTL GSEVNKLQKQ
     LDQVRSKQDG EHLTSLQDEL EMLREQLQEA SADKKELEKE HSSEKMKLEK RVEELEKENA
     LLKSEKEEMN QIILQQSLSS AGGGSIVSQS EASLQKELDQ ERQRYQNLVK EFSRLEQRYD
     NLKEEFHPGH RRTTSNQSSI GSDSNYPSFS TSEVGDTEDA IQQVEEMGLE KAAMDISLFM
     KLQKRVRELE QERRRLQASV EKMEEINRRK GSESRNTISE QESADQAYDS LKRQELETEN
     KNLKNDLNEL RKTIADHASQ NNSSNELQDG YNLLLSQLKA ANEELDARKE EVLILKSQIV
     STAQLLDKND NLPESNGVPE MTNGTEPMDK EEAVKAYNGL CESKKLLEAQ LQTQSKHHKD
     ELEALHTQIE LLRDDIEKKQ EMLNYTASLS PEAKVEYSVQ QEITRLTNEN LDLKELVEKL
     EKNEKKLKKQ LRIYMKKVQE LEASQAAAAQ NSRSKPELSR QVTVQRKEKD FEGMLEYSKE
     EEAHLLKALI MDMRPSTVSA TVPCLPAYIL FMCIRHADYI NDDQKVESLL TSTINSVKKV
     LKKNSDDFEM TSFWLANTSR LLHCLKQYSG DEAFMKQNTG KQNEHCLKNF DLTEYRQVLS
     DLSIQIYQQL IKVAEGIIQP MIVSAMLESE SIPSLAGVKP MGYRNRSSSM DTDAGGPSSY
     TLEALIRQLG QFLGIMQDHG MDPEIVGQVV RQLFHCINAV TLNNLLLRKD VCSWSNGMQL
     RYNTTQMEEW LRANNLYSSN AAATLEPIIQ AAQLLQVKKK TIQDAEAICS LCSSLTTQQI
     VKILNLYTPL NEFEERVTVS FIRNIQNGLQ ERNDPPQLLV DTKHVFPVLF PYTPSALSLE
     TLHIPASLGL EFLVRV
//
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