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Database: UniProt
Entry: H3D1T7_TETNG
LinkDB: H3D1T7_TETNG
Original site: H3D1T7_TETNG 
ID   H3D1T7_TETNG            Unreviewed;      1633 AA.
AC   H3D1T7;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
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:ENSTNIP00000014475.1, 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:ENSTNIP00000014475.1}
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   Ensembl; ENSTNIT00000014674.1; ENSTNIP00000014475.1; ENSTNIG00000011525.1.
DR   GeneTree; ENSGT00940000163461; -.
DR   HOGENOM; CLU_000192_8_1_1; -.
DR   Proteomes; UP000007303; Unassembled WGS sequence.
DR   GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
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   Gene3D; 1.20.5.340; -; 4.
DR   Gene3D; 1.20.5.370; -; 5.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR   Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
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; IPR008989; Myosin_S1_N.
DR   InterPro; IPR002928; Myosin_tail.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014751; XRCC4-like_C.
DR   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   PANTHER; PTHR45615:SF44; MYOSIN-13; 1.
DR   Pfam; PF00063; Myosin_head; 2.
DR   Pfam; PF02736; Myosin_N; 1.
DR   Pfam; PF01576; Myosin_tail_1; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 4.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 2.
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};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, 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          33..82
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          86..293
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          323..481
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          358..380
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1579..1633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          543..593
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          727..852
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          889..930
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          966..1528
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1579..1626
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         180..187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1633 AA;  187714 MW;  6AE0651AB1C27D4C CRC64;
     MSSDSEMAVF GQAAPYLRRP ERERIEAQNR PFDAKTAVFV VDPKELFVKG TLLSKDGGKA
     TVKTCKGQVV TGREDVIFLR TQCNIVKVNL SCIKTNGENC CVKSYLKPVI YSDILQTYSG
     LFCVTVNPYK WLPVYNQEVV WAYRGKKRQE APPHIFSISD NAYQFMLTVD RENQSILITG
     ESGAGKTVNT KRVIQFFATI AGLGDRKKEP ISSGKLHGNL EDQIISANPL LEAFGNAKTV
     RNDNSSRFGK FIRIHFGTTG KLSSADIETY LLEKSRVTFQ LSAERSYHIF YQITSNKKPE
     LIGNIKHNKL NNPMTPRCFF FFLFPIXDAS GGAGAGKKGA KKRGSSFQTV SALFRENLGK
     LMTNLRSTHP HFVRCLIPNE TKTPGIMEHH LVIHQLRCNG VLEGIRICRK GFPSRILYGD
     FKQRYKVLNA SVIPEGQFID NKKAAEKLLG SIDVDHTQYR FGHTKVFFKA GLLGLLEEMR
     DEKLASLITI TQALCRGFLK RREFQKMMER RESIYIVQYN VRSFMNVKHW PWMKLYFKIK
     PLLRSAETEK EMANVKVEFA KCKEDLAKAE SKRKEMEAKM VTLLQEKNDL CLQIQTVSKI
     LADECNNRLA SLSKGRIYMS KNFEKLKDNE KFYQRVINAF VRKEQMKKKL LSNIEKHDLC
     VNLIVMTTVP HQPQTILGVT DTFAPISVYC DKVWTELKGQ GSRQDVMDDA SQPSSMQHSV
     LVEVIEMDHL EGSLEQEKKN RLDVERAKRK LEGDLKLAQE SIMDLENDKQ QMEERLKKKD
     FELSQFLAKI EDEQSVAAQS QKKIKELQAR TEELEEEIEV ERVAKSKVEK QRSDLSRELE
     EISQRLEEAG GAIVAQGELN KRREAEFQKL RRDLEESTLH HEALNTALRK KHADSVAELG
     EQIDNLQRVK QKLEKEKSEY KMEIDDLSGN VEVTVKSKIN FEKLCHSLED QLSDFKTKHD
     ENTHLINEIN TQKAKLQNEN GEVSRLLEEK EAVLSQALRA KVAFSQQVEE LKRQIEEEAK
     AKSALAHALQ SARHDCDLLR EQFEEEQEAK AELQRAMSKA NSEVAQWRVK YETDAIQRNE
     ELEEAKKKLV QRLQEAEEAV KAMNAKCSSL EKTKQRLQGE VEDLMSDVER ANSQAASLDK
     KQKSFDKVLS EWKQKYEEAQ AELDGSQKEL RSLNTELFKI KNSYEEALEH LEILKRENKN
     LQQEISDFTE QLGENNKTLH ELEKMKKQAE SEKSELQTAL EEAEASLEHE ESKFLRVQLD
     LCQVKGEVDR RLAEKDEEME QMKRNHQRVA ETLQSALDAE TRSKNDGVRI RKKMETDLNE
     MEIQLSHANR QAAESQKQLK NIQAHLKEQT LNLDEALRSQ EEQREQAATM ERRSCLMQAE
     VEELRAALEQ SERSRKLAEQ ELADACERAG LLHSQNTSLL NTKKKLDADM TRLQAEVEEA
     VQEARNAEEK TKKAINDAAM MAEELKKEQD TSSHLERMKK NLEGSVKDLQ LRLDEAESLA
     LKGGKKQLQK LEARVRELEG EVESEQKRAA DAVKGMRKYE RRAKELTYQS EEDKKSMARL
     QDLADKLQLK VKAYKRQMEE AEEEASTHLA KLRKEQHELE EAQERADLAE TQVNKLRTKS
     REFGKHTENI TIP
//
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