ID A0A096MC06_POEFO Unreviewed; 2059 AA.
AC A0A096MC06;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Myosin X, like 1 {ECO:0008006|Google:ProtNLM};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000028947.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000028947.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000256|ARBA:ARBA00004544}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; AYCK01013440; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSPFOT00000031288.1; ENSPFOP00000028947.1; ENSPFOG00000005639.2.
DR GeneTree; ENSGT00940000164909; -.
DR OMA; FHADDEM; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13202; FERM_C_MyoX; 1.
DR CDD; cd17206; FERM_F1_Myosin-X; 1.
DR CDD; cd14873; MYSc_Myo10; 1.
DR CDD; cd13296; PH2_MyoX; 1.
DR CDD; cd13297; PH3_MyoX-like; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.5.190; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 1.25.40.530; MyTH4 domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 4.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR031971; MYO10_CC.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR041797; MyoX_FERM_C.
DR InterPro; IPR040640; MyoX_N_SH3.
DR InterPro; IPR036124; MYSc_Myo10.
DR InterPro; IPR000857; MyTH4_dom.
DR InterPro; IPR038185; MyTH4_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000159; RA_dom.
DR PANTHER; PTHR46049; AGAP003327-PA; 1.
DR PANTHER; PTHR46049:SF4; UNCONVENTIONAL MYOSIN-X ISOFORM X1; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF16735; MYO10_CC; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00784; MyTH4; 1.
DR Pfam; PF00169; PH; 2.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF18597; SH3_19; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00295; B41; 1.
DR SMART; SM00015; IQ; 3.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00139; MyTH4; 1.
DR SMART; SM00233; PH; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 4.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51016; MYTH4; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS50200; RA; 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};
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:UP000028760};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 66..740
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1210..1308
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1390..1495
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1533..1693
FT /note="MyTH4"
FT /evidence="ECO:0000259|PROSITE:PS51016"
FT DOMAIN 1698..2044
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 1702..1751
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REGION 620..642
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 992..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1043
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 160..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2059 AA; 235588 MW; 2734B0C5002DF451 CRC64;
MLICFVFQGA RVWLRHKEQL LPSTVSSSDD LSLVLTSDYG KVKFATFQIE ELNRDTVYPM
HPSSINGVED MSTLAELHEA AIMHNLFLRY QKDNIYTNIG SILAAVNPYQ QIAGLYDSTA
VDLYSKHQMG ELPPHIFAVA NECYRCLWKR HDSQCVLISG ESGAGKTEST KLLLKFLSVM
SQNSSGTPLS ERTTRVEQAL VQSSSPIMEA FGNAKTVYNN NSSRFGKFIQ LHFSQNGNIQ
GGCIIDYLLE KNRVVRQNPG ERNYHIFYAL LAGADRDHRD MYLLSEGPES YHYLSQAGCV
QDSSLDDKQL FNSVMEALKV MEFSEEEIRD VFKLLSAVLQ MGNIEFMTAG GAQITSNGVV
SNVSELLGLD SFQLSEVLTQ RSMILRGEEI CSPLTVEQAV DSRDSVAMAL YSQCFSWIIM
RINQKIKGKD NFKSIGILDI FGFENFEVNR FEQFNINYAN EKLQEYFNKH IFSLEQLEYN
REGIQWEAID WMDNAECLDL IEKKLGMLAL INEESRFPKG TDYTLLEKLH SRHATNPYYV
KPRVTDHQFG IKHYAGEVLY DVRGILEKNR DTFRDDILFI LKDSRLDFIY DLGSRSGDET
LKMGTARRKP TVSSQFRDSL HSLMATLSAS NPFFVRCIKP NMDKKANRFD PDVVLNQLRY
SGMLETVKIR KAGFPVRRTF KDFFSRYKMI HKNKTASAEE KSCCLEVLTL HDNTKKEWQL
GKTKVFLKEA LEQRLEKERE EVRRRAGMVI RAHILRFVYR KQYKRVLYSV VTIQKNYRAH
FWRRAFVRLR LAAVILQKHR RGQLARSVCH KLMKEKEEQQ KLAAKGDTTR NSLVNGACPK
VTQFHLPLLK WLNFLNRSGQ QQDLTQTPSY NHTSEEESRQ MEEILRLERE IERLQKQQED
GVSLLGDVSR EELRQMRDAE IYRLEKEASR VATEFLELLD FGGLEPSLSS EENLHEVNES
AAPLAEEEVD EGFPAEDECV PLPDFPPPAA VPLDTDVFQS IPPPPPAFAE GVTVSSSSGP
HSGPEKLPPA TTNGLNHTPI VTDSQTRPPP PSPLIVTNGE RQPCQTTTRT LDFVPLNDVP
SQSNLPDAES DYDQEEFEEA HGSSGASIND GHITDEEVLR ESSCTQNSLD SFRGSSDSVS
SKFIDSDEEN DGYVDTDEEI SNGRVSLLNG TGPPYFHGYL YMKGGLMIPW RRRWCVLKDE
TFMWFRAKQD SLKSGWLYKK GGGMSTLSRR NWKMRWFVLR EAKLMYFEND SEEKLKGTID
IRAAKEIVDN HEKENALNIV TEERTYQIYA ESPEDASGWF NVLSRVHSAS PEQLLEMHHE
QANPKNAVGT LDVGLIDSVC ASDNPDRPNS FVIITANRVI HCNTDTPEEM HHWIGLLQKS
KGDTKVDGQE FLVRGWLHKE MKSGAKSTSL KLKKRWFVLT TNSLDYYKSS ERNTTKLGTL
VLNSLCSVVQ PDEKVFKDSG YWNIIVYGRK HSYRLYTKML NEAMRWANAI QGVIDNKVPI
ETPTQQLIRD IKESSLNVEA VEQTYWRNPI LRYTQHPLHS PLLPLPYGDV SVHLQKEKGY
TSLQDEAVKI FNSLQEMEAV SDPVPIIQGI LQTCQDLRPL RDEVYCQLIK QTNHVPHPNS
PANRAHWHLL TCMSCTFLPS RGILRYLKFH LKRIKELFPG TEIEMFAHFI GESLKKTKMR
EFVPSQEEIV ALLTRQEMTT TVYCHGGGSC KISINSNTTA GEVVEKLIRG LAMEDSRNMF
ALFEHNNTVD KAVESRVLVA DVLAKFERLA GSEEARDEGQ WRLYFKLYCF LDVESMPKEG
VEFAFMFEQA HESLTRGHFP AREETLQHLA ALRLQFLFGD KTRIAWNLEN VYPVGRLRNR
ILQFTKAGGA SGSGQTLERR RTSFLDGTLR RGLKTGSMKK QRMEEEQMLE MWIKEEMSAT
RASIVEKWSH LKGLDQHQAM LKYMSIIKEW PGYGSTLFDV ECKEGGFPHD LWLSVSAENV
SVYKRGEPKP LETFPYEHIV FFGAPQPCTY KITVDEREMF FETPEVGEIT KIMKAYINMI
VKKRCSVKSV SSYGTNWIR
//
