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Database: UniProt
Entry: A0A3Q1CDT6_AMPOC
LinkDB: A0A3Q1CDT6_AMPOC
Original site: A0A3Q1CDT6_AMPOC 
ID   A0A3Q1CDT6_AMPOC        Unreviewed;      1643 AA.
AC   A0A3Q1CDT6;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Unconventional myosin-IXb-like {ECO:0000313|Ensembl:ENSAOCP00000018006.1};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000018006.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000018006.1}
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; 80972.ENSAOCP00000018006; -.
DR   Ensembl; ENSAOCT00000032941.1; ENSAOCP00000018006.1; ENSAOCG00000023212.1.
DR   GeneTree; ENSGT00940000156845; -.
DR   OMA; HAMLNKR; -.
DR   Proteomes; UP000257160; 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: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; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 2.
DR   Gene3D; 3.30.60.20; -; 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; PF00130; C1_1; 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}; 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:UP000257160};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          15..113
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          125..850
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1237..1286
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          1302..1490
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          653..673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          732..754
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          908..1012
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1607..1643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        923..937
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        953..971
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        975..1005
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1607..1627
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         219..226
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1643 AA;  187246 MW;  6BB12BA3282D05E7 CRC64;
     MSTTDGTGVS EQDGEVHVVQ IYPRLSQDTT AYCPVQVSAG DTASAIIHNA VVTLGLDSSL
     TYCLLEARES GGEERLLEAG DCPLDRVLLW PPETQKWHPP SHGYYFILQE QQANSAGKRV
     ETIKEDYDDL CNLPTVTEES VLEALRQRFY KHKIYTYTSN ILIAINPNKF LPVYYNPKYI
     KMYENQPLGK LSPHIFAIAD VAFRAMLNRQ VNQCIVISGE SGSGKTESSS FLIHCLTGLS
     QKTYSSGLER TILGAGPVIE AFGNSKTAEN NNSSPIMLYF SHQLPVLVKN YHVFYYLLMG
     ASKDEKEEFH LFKPQDYLYL NQVPLQYKRL HQAMEMVGFL SSTKKHIFSI LSAVLLLGNV
     TFTLSEDTQV LEAGPAEVLS TLSDLLKVKN ELLVTALTKR RVVTANCTVV SQYTLQEAST
     MRDSMAKSLY GALFDWIILH INHALLNRRD MEESISCLSI GVLDMFGFEN LQTNSFEQLC
     INYSHETLQY YINQNIFKLE QNDYVSEGIS WQNIDFTDNR GCIQLISSES VGLFDLLDQE
     CSLPQATDET FMDKLKQQIQ DNPLFVPSQN TEPTFVIQHF AGRVKYHIKD FRKKNTEHMR
     PEVVSLLRSS GRSFLHHLVA SSPEALFRWG VLRATIRILT VFKSMARQRA ELTERRSSGK
     SLKDMKQCSS PMGKLKSEPL DFSFDRSDEH PIDIFEDIFV SYEKRKKSRG GRQKQLIPKV
     NLLYAYISQA SLKKLMKTIE KAEPFFIFCV RSNAEKKELQ FDNELVLNQI KYTGILQMIH
     IQKSGYSAKY TFKEFVKKFR MLLPKGATAT PEHITELFER MELDKSTYQI GKTKVFLKEK
     ERQLLQDTLN KEVMRHIIIL QRWFRACLIR LHFLEKRDAS VIIQVQFFCY GCDCFLLNSL
     AKKELKRQHK VELSPSRTQQ PDPGRSRSKD KREGRGSPPP LNRPLSLPLD PKVSTDDFSS
     SPKSSSLQRY QDVGGIKDKA IRWRERQSEG EPTDESSPEI QVRPRKQNQR RRRLAYARSG
     LVINFAASKE SEYWSFPLPP ISPLVPTLKS SASSIDVRAL KSQVKVLTKG IYTPPPYHTA
     NQNSGRASRN PTIRISRATR ALQWDASLDR EITNPKELRN LDEFLGNQVN ELRTRIKELS
     ATESIFLTAT MEFRETIKGM YSVQKPQIGY KDLMKGFHNK VNSLAGSKEK GEVSLVVNLF
     QSVLDGFIRG EIKRVESEPA KVNFRRKKKQ CPDSPLDHLF STYQVNIMQS CDLCGSYIWG
     MEKAYMCSAC KLICHKKCLK QIITDCSTRC DDNVPGSLHF GVQVCVLTSK ANPVPKVVEL
     LLMHVELNGL YTEGIYRKSG SACRARELHQ ILETNPEGAC LDNYPIHTIS GLVKRWLRDL
     PDPLMTFSLY SDFLHAVELP EKPEKIRAVY KLIEELPPAN YNTLERLIFH LVRVAKEEDH
     NKMSPSSLAI VFAPCILRSP DASDPFLGMK DVSKTTLCVE ILISEQFRRY KEKMQNIQEL
     EYAEALAVNQ LKLRRQNTVT SQTKTCSWRS MGLFATKCVP SMFINVMFLL AGKEKVQLKT
     QRPNCPQKPP DLAQRVRKLM ALSDNEQTEL TSGQNTDVMQ SMCFLPNQDT PVPASKPQDT
     NKTLNGSFDD LDIPYIDEDE DPS
//
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