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
//