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Database: UniProt
Entry: A0A3B4BYQ1_PYGNA
LinkDB: A0A3B4BYQ1_PYGNA
Original site: A0A3B4BYQ1_PYGNA 
ID   A0A3B4BYQ1_PYGNA        Unreviewed;      1623 AA.
AC   A0A3B4BYQ1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Unconventional myosin-IXb-like {ECO:0000313|Ensembl:ENSPNAP00000004713.1};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000004713.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000004713.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   STRING; 42514.ENSPNAP00000004713; -.
DR   Ensembl; ENSPNAT00000006550.1; ENSPNAP00000004713.1; ENSPNAG00000011162.1.
DR   GeneTree; ENSGT00940000156845; -.
DR   OMA; HAMLNKR; -.
DR   Proteomes; UP000261440; Unplaced.
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:0048513; P:animal organ development; IEA:UniProt.
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; -; 3.
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; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR046349; C1-like_sf.
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; PF00063; Myosin_head; 3.
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; 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}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          15..106
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          134..899
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1286..1334
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          1352..1535
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          780..802
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          957..1085
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        986..1003
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1006..1026
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1035..1065
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         227..234
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1623 AA;  186562 MW;  FDD58D2AEA779A4D CRC64;
     MSFPESRKSA YLDEATYVLQ IYPRLSLKTA QCCTLNVHKE ATAAWVIQIA AVTLGLDKSK
     PYQLVEVRET GGEEWVLQAS DRPVERLLLW PRKVQDQHLQ IHGYYFALQS GVPDGPSQSE
     RVLYVRSFLK PQSEDCNDLC SLPVLTEKNI LEALRRRFLK NQIYTYANNI LIAVNPFKFL
     PIYNPKYVEM YENHTLGRLN PHVFAIADAA FRAMLNKRLN QCIVISGESG SGKTQSTNFL
     IHCLTAFSRK GCTSGVERTI LGAGPVLELQ AFGNAKTAYN NNSSRFGKFI QVNFLEGGVV
     RATIEKYLLE KCRLVSRKSC ENYHVFYYLL VGASDEEREE FKLQEPEDYH YLRQQDNPHL
     EDQAEIQYEF KRLHQAMEMV GFLPATKKIF SVLSAILYLG NLTYEAKADG EGLTVGPADV
     LSTLSDLLKV KKEPLVEALT KRRAMTANDV LILPYTLSEL QAITARDSMA KSLYSSLFDW
     IVLRINHALL NKRDMEESVP CLSIGVLDIF GFEDFRTNSF EQFCINYANE QLQHYCNQHI
     FRLEQFPHAT DNTLLEKFKQ QHQENLFFVP TPVMEPAFVI LHYAGKVKYQ IKLQDFRAKN
     TDHMRPDMVA LLRSSERGYL RQLIGSDPVA VFRWGILRAV VRTVATFKEA GRRWVTEHPQ
     SLIDFSFDRS EENPLEVFED IFATFESKEL HAKVLCTIKR LGGEVPQKLR LSTISVRKSR
     QFFKSRTNRH KQLIPKNLID SRALKLIVDL NLHNRDTRSL LHLHKKKKPP SISAQFQTSL
     VRLLDTLKKA EPFFVRCIRS NAEKREMQFD EDLVLKQLRY TGMLETVRIK RSGYGAKYTF
     KQEFTDEFRV LLPKNPSTPQ KDITNLLRRT GLDDSSFQIG KTKVFLKEVD RQKLQETLHR
     EVMHRILLLQ RWFRACLTRK HFLMKRKAII TLQQRSWRGY HESTCFRAAS VIQAAWRQSH
     RKENESPSPA PTRPGTLDLS SGPKLAQPVQ DDSSNTAPLQ RYSKPSTMKE KVEKWKERRS
     EILPPDRSSL KDQQLENQKL KSLSRGISMS LDNLSKFSSS ESDSSPPTKN EKRSRRRLRH
     KRRLARPRSS LMLKGMEDAD PDYWSFPLPP LSPSEPFRTK RLTPQDGSVT MARTLAERDA
     GRNPTIRISR GTRVQDQFDA FLDRQITDSD ELRHLDEYLG NQMNDLHSQA KVRSETEEIF
     LKATTQFRDT IKSMYSVSNP QVSYKGLLQG YKSKVTNLAG QKKKDEVPMV VNLFQSVLDN
     FIRAEIKKAS LERASSDPAK PDSPLDHCFS TYQVNIYQSC DLCSSYIWGM EKACMCSCKM
     VCHKKCLSKI VLFCSKHIES GKSTAHFGVH VSSLTSNQTP VPVVMEMMLS YVELHGLYTE
     GIYRKSGSAC KAKELHQLLE TDPKSECLNN YPIHTVTGLI KCWLRELPEP LMTFSLYNDF
     LYAALPEKSE RLRAIYRKVE DLPAPNYNTL ERLIFHLVRV AKEEAHNRMS ANSLAIVFAP
     CVLRCPDVSD PLLSMKDLPR TTCLEILIME QTRRYEEKMK EIQQLEHAEA LAIKQLTLQR
     KNTSPMDSLG TEVEKTLRER IKSIKLVLPE LDQDASDNET LDTESMISLE CSLDDHFVSS
     VSE
//
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