ID A0A3P8TXG4_AMPPE Unreviewed; 1792 AA.
AC A0A3P8TXG4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Myosin IXb {ECO:0000313|Ensembl:ENSAPEP00000030895.1};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000030895.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000030895.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000030895.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 161767.ENSAPEP00000030895; -.
DR Ensembl; ENSAPET00000031717.1; ENSAPEP00000030895.1; ENSAPEG00000021943.1.
DR GeneTree; ENSGT00940000156845; -.
DR OMA; HAMLNKR; -.
DR Proteomes; UP000265080; Chromosome 10.
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; 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}; 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:UP000265080};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 15..113
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 125..921
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1432..1481
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1500..1688
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 803..825
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 978..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1208..1239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1255..1284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1757..1792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..1014
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1040
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1074
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1219..1239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1757..1782
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 1792 AA; 204151 MW; 72FECFA26AED43A5 CRC64;
MSTTDGTGVS EQDGEVHVVQ IYPRLSQDTT AYCPVQVSAG DTASAVIHNA VVTLGLDSSL
TYCLLEARES GGEERLLEAG DCPLDRVLLW PPETQKWHPP SHGYYFILQE QQANSAGKRV
ENIKEEYDDL CNLPTVTEES VLEALRQRFY KHKIYTYTSN ILIAINPNKF LPVYYNPKYI
KMYENQPLGK LSPHIFAIAD VAFRAMLNRQ VNQCIVISGE SGSGKTESSS FLIHCLTGLS
QKTYSSGLER TILGAGPVIE AFGNAKTAEN NNSSRFGKFI QLNYLESGVI RGAVIEKYLL
EKSRLVSRDK SERNYHVFYY LLMGASKDEK EEFHLFKPQD YLYLNQGDVH LDDDEDLGQQ
YKRLHQAMEM VGFLSSTKKQ LCSIFSILSA VLLLGNVTFT LSEDTQVLDA GPAEVLSTLS
DLLKVKNELL VTALTKRRVV TANCTAVSQY TLQEASTMRD SMAKSLYGAL FDWIILHINH
ALLNRRDMEE SISCLSIGVL DMFGFENLQT NSFEQLCINY SHETLQYYIN QNIFKLEQND
YVSEGISWQN IDFTDNRGCI QLISSESVGL FDLLDQECSL PQATDETFMD KLKQQIQDNP
LFVPSQNTEP TFVIQHFAGR VKYHIKDFRK KNTEHMRPEV VSLLRSSGRS FLHHLVASSP
EALFRWGVLR ATIRILTVFK SMACQRAELI AERRSSRKSL KDMKQCSSPM GKLSSKSEPL
DFSFDRSDEH PIDIFEDIFV SYEKRKKSRG GRQKQLIPKN LMNLRSLQHI VGVTAHDRTS
KSIFHPHRTS KLQTVNAQFQ ASLKKLMKTV EKAEPFFIFC VRSNAEKKEL QFDNELVLNQ
IKYTGILQMI HIQKSGYSAK YTFKEFVKKF RMLLPKGATA TPEHITELFE RMELDKSTYQ
IGKTKVFLKE KERQLLQDTL NKEVMRHIII LQRWFRTCLI RLHFLEKRDA SVIIQRCWRE
FYVQQNRAAT VIQTAWRSSL KKSKNPHEED EDKSKARPGR DSLAKKELKR QQKVELSPSR
TQQPDPGRSR SKDKREGRGS PPPLNRPLSL PLDSKVSTDD FSSSPKSSSL QRYQDVGGIK
DKAIRWRERQ SEGEPTDESS PEIQRRRDKK KDDFYRKAKS MSADELSKVS SSGSDSSPST
TEVRVRPRKQ NQRRRRLAYA RSGLVINFAA SKESEYWSFP LPPISPLVPT LKSSASSIDV
RALKSQVKLP AEPDGSRFSL PPRTSNESSG QQRSSQSQLT TPERIWFLGK FLKKRTPKLP
PSSDSPTSKT ANQNSGRASR NPTIRISRAT RALQWDASLD REITNPKELR NLDEFLGNQV
NELRTRIKEL SATESIFLTA TMEFRETIKG MYSVQKPQIG YKDLMKGFHN KVNSLAGPKE
KGEVSLVVNL FQSVLDGFIR GEIKRVESEP AKATKTTKKR RKKKQCPDSP LDHLFSTYQV
NIMQSCDLCG SYIWGMEKAY MCSACKLICH KKCLKQIITD CSTRCAMKDD NVPGSLHFGV
QVCVLTSKAN PVPKVVELLL MHVELNGLYT EGIYRKSGSA CRARELHQIL ETNPEGACLD
NYPIHTISGL VKRWLRDLPD PLMTFSLYSD FLHAVELPEK PEKIRAVYKL IEELPPANYN
TLERLIFHLV RVAKEEDHNK MSPSSLAIVF APCILRSPDA SDPFLGMKDV SKTTLCVEIL
ISEQFRRYKE KMQNIQELEY AEALAVNQLK LRRQNTVVEK PSQLDVLQQT HFDETDKLIE
RIKSIKQEKV DLACTLPNLE QENSDNDNLD SSSSMSTESL EDRLGSLESE GQ
//
