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Database: UniProt
Entry: H3DBQ4_TETNG
LinkDB: H3DBQ4_TETNG
Original site: H3DBQ4_TETNG 
ID   H3DBQ4_TETNG            Unreviewed;      1914 AA.
AC   H3DBQ4;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Myosin IXb {ECO:0000313|Ensembl:ENSTNIP00000017947.1};
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:ENSTNIP00000017947.1, 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:ENSTNIP00000017947.1}
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; ENSTNIT00000018171.1; ENSTNIP00000017947.1; ENSTNIG00000014903.1.
DR   GeneTree; ENSGT00940000156845; -.
DR   HOGENOM; CLU_000192_2_2_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:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000146; F:microfilament motor activity; IEA:InterPro.
DR   GO; GO:0048468; P:cell development; IEA:UniProt.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 1.
DR   Gene3D; 1.20.58.530; -; 2.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 6.20.240.20; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 2.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR046987; Myo9.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR000159; RA_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR46184:SF2; UNCONVENTIONAL MYOSIN-IXB; 1.
DR   PANTHER; PTHR46184; UNCONVENTIONAL MYOSIN-IXB-LIKE PROTEIN; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00612; IQ; 1.
DR   Pfam; PF00063; Myosin_head; 2.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00242; MYSc; 1.
DR   SMART; SM00314; RA; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          31..113
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          116..913
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1534..1583
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          1605..1790
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          796..818
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          996..1090
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1205..1227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1881..1914
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        996..1018
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1058..1090
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1893..1907
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         210..217
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1914 AA;  219622 MW;  69081F64BB3C0FCE CRC64;
     MSRHTGGKTA SFLPYLGFMK IHPRVSPSTP AYCPLQIGSQ DTARTVIHNA LVALGLDLSG
     RYHLLEVRES GQEERPLELE DRLLERVLLW PPETQRWHPE TQGYYFILQQ TDSGADDYDD
     LCGLQAVSQE SILEVLCQRF HRLKIYTYAR NVLVAINPNK FLPLYYNPKY IQMYEKQPLG
     RLSPHIFAVA DAAFRAMQVG RVNQCIVMHG DSGSGKTESS SYLVHYLTAL SEKTCSVGLK
     RTILGAVPVL QAFGNARTSE NNNSSRFGKF IQLNYLESGV IRGAVIEKYL LEKSRLVSRD
     KTERNYHVFY YLLMGATRDE QEEFHLLKPQ DYYYLNQGDL QLDDDANFGQ EYKKLKQAME
     MVGFLASTKK HVFSVLSAIL LLGNVTYTLS EDAQVLEVGP AEVLSTLSDL LNVKVDLLVK
     TLTRRKVVIT NTLVESPYIL EEASRVRDSM AKSLYGALFD WIIVHVNHAM FNRRDMEESV
     SCLSIGILDM FGFENLKKNT FEQLCINYSN EKLQYYINQH IFRFKQEDYI SEGITWQNIA
     FADNSGCIQL IDEKPSGLFD LLDQENKLPQ ATDKTLLDKL KQLHQDNPFF ITSSDADLTF
     VIQHFAGAVK YHAEDFPREN NEHMRPEVVS LLRSSKQSFF HHLVASSPEA LFRWGVLRAT
     IRILAVFKSL GRKRAEESLL FKCFFLPPII HSNSLTLDFS FDRSDELPLD VFEDIFTNYE
     NRNCIVKLHK LSLWSFFPRR SRSGRQKQII PKNLMDYVSL QHVVGLTAHD RTSKLIYHPH
     RTAKVPTFSA QVQASLNKLL ERIEKAEPFF IFCIRSNDQK KELHFDRELV LQQIKHMGIT
     QMVHIHRSGY GAYTFKEFVE KFRLLLPKGA SETPEYITEL FERMGIDKSS YQIGKTKVFL
     KEKERQLLLD TLTKEVMRRA IILQRWFRSC LIRLHFLQKR DATMIIQRSW REFYEKKNLA
     ATVIQSAWRS SLHMSSLNLG VIKWISCHSL TKKGLQRQRQ VEVSPNRIQQ TDPSGSRAAH
     GDSSREAPEG RGSPPPLNRP LSLPLDPKVC IGDQSGRLIR SSKEKQSDDS SPEMQRRAVS
     RKEEFSVRFR KQPKRKRRLA YARSGSNRHV EETLSILCMH NLHVQNRRSG WSGNSSFCFA
     IQDKRNEGWL LQAFPELESV LKLVAELSEI TQKCIATTKL DLKVNLSILI PSFFSPQKHD
     GARLSLPGRT AEEGLGQHSS NPSQLTSPER LNTSFTIFLG WFVAFFFQIK TILLIVRKVF
     VCGDTLWTTQ ALRIWFLSRF LKKKAPKYSP VNSPSVHADK SAVPRGKLDT AAAFYDPFEP
     GHCLFSSCTV FRHICQLYKL NSRMDPNGTS HCQNVAAETF SRYTPQSYHS PHSDSERVKR
     NPTIRISRAT RVMESNASLD REITDPKELQ NLDEFLGSQA YELRTRIKEL SPTESIYLNA
     TMQFRETIKE MYSLQHQKPK IGYKDLLKGF HQKVSTLAGS KNKTEVSLVI NLFQSVLDGF
     IRGEIKRMES EPTKLTKTTK KRKKKDKCLS SPLDHRFSTY QVSIMQSCDL CGSYIWGMEK
     AYMCSACKLI CHKKCLGKII TDCSTRQARQ DDGTPGSLHF GVQVYMLTST ANPVPKVIEM
     LLIHVEINGL YTEGLYRKSG SACRAKELHQ ILETDPESAC LDSYVIHTIT GMVKRWLREL
     PDPLMTFDLY TDFLHAAELP DKAEKIRAVY QKIDELPPAN YSTLERLIFH LVRVAKEEKH
     NKMSPSALAI VFAPCILRSP DVDNPFLSMN DVPKSTACVE ILISEQFRRY KEKMQNIQEL
     EYAEAIAVHQ LKLRRQNTRC PLSLFYSADS ETMYRFDMLQ IVEKPPELDV PQEIPSDEIE
     KTLIERIRSI KEEKEDLTCR LPNLEHENSD NEILDSASSM SSESLEDRLG SVDS
//
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