ID A0A3B3WS78_9TELE Unreviewed; 2027 AA.
AC A0A3B3WS78;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Myosin X {ECO:0008006|Google:ProtNLM};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000005612.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000005612.1}
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 STRING; 48701.ENSPMEP00000005612; -.
DR Ensembl; ENSPMET00000007220.1; ENSPMEP00000005612.1; ENSPMEG00000007108.1.
DR Proteomes; UP000261480; Unplaced.
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: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 PANTHER; PTHR46049; AGAP003327-PA; 1.
DR PANTHER; PTHR46049:SF2; UNCONVENTIONAL MYOSIN-X; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF00612; IQ; 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; 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; 2.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51016; MYTH4; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
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|SAM:Coils};
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}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 59..741
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1190..1288
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1370..1474
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1512..1670
FT /note="MyTH4"
FT /evidence="ECO:0000259|PROSITE:PS51016"
FT DOMAIN 1675..2010
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 621..643
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 940..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 865..904
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 940..963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 153..160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2027 AA; 232424 MW; 299A340D4A7267CC CRC64;
MDSGDRVWLR EEDQFLPGSV SSCSGGVVVF ATDYGQVYTY KQNALTRQKV QPMHHSSVRG
VEDMATLEDL HDGAIMHNLY QRYQQRQIYT YIGSILAAVN PYQPLPGLYD RPTIELYSRH
HLGEISPHIF AVASDCYRSL WRRQQNQCVL ISGESGAGKT ESTKLILRFL SAMSQHSLEV
SCRDKTSHVE EALLESSPIM EAFGNAKTVY NNNSSRFGKF VQLHFNQKGN IQGGRIVDCI
LSNSNRVVRQ NPGERNYHIF YAILAGANNQ QREAFGLTRP ESYHYLRQSS CTEDKTINDS
STFQDVLSAM QTMQFTEENI REVLRLLAGI LHAGNIEFMT AGGAQVASKS ALSWTSELLG
LNSEQLAEVL THRSMILRGE EISTPLTVEQ AVDSRDSMAM ALYSQCFNWI IHKLNHRIRG
KEDFKSISIL DIFGFENFEV NRFEQFNINY ANEKLQEYFN KHIFSLEQLE YNKEGLVWVD
INWMDNAECL DLIEKKLGLL ALMNEESHFP KATDDTLLEK LHSQHSKNPF YVKPRVAVHL
FGVRHYAGEV VYDVRGMLEK NRDTFRDDIL NMLRESRSVG WMLDFVYDLF EHVLSRNKQD
TLKSSTKHRR PTVSSQFKDS LHSLMATLST SNPYFIRCIK PNTHKMPDQF DQTVVLNQLR
YSGMLETVKI RRSGFPVRRS FQDFCSRYKV LMRGVLTPDD HRGRCKQLLH LYDSSSADWQ
LGKTKVFLRE SLEQRLEKQR EVEVLKAAMI IQAHVLGYMA RKQYRRLLQC IVVIQKNYRA
FYWRRKFLLL RWAALTFQKR LRGRLARRAV GRLLDERRKR EEEEQRQRLR LEAERPAAAF
PETPEELESV FEEPGEEEEA IRPQEASQVE EILRLEREIQ ALQRQKEQQE LSLTEASLHR
LQRLRDQELQ RLEDEACKAA QQFLDSLNFD EIDECVRNIE SSLGVGEEEE KENGGRRGNE
EEEVDEGFGA DDEAFKDSPN PSEHGHSDGQ RTSGIRTSDD SSEEDPYAND VPIPAMPLTT
LLHMPLPPLP PAALSVSSSG DSTFCRPQSS SEAPSDDLVE LIPPDEDSDY DQDDYDEGAI
VSSGSVAFSN PRSGQWSPDY RGSVGTYNSS GAYRFSSEGA QSSFEDSEDD FDRFDTDDEL
SYRRDSVYSC VTLPYFHSFL FIKGGLMNTW KRRWCVLKDE TFLWFRAKQE ALKQGWLHKK
GGGSSTLSRR NWKRRWFVLR QSRLMYFEND SEEKMKGVLD MHNAKEIVDN TGKENGIDIV
MPERTYHLIA ESAEDASQWF SVLSQVHGAT EQEISEMHDE QANPQNAVGT LDVGMIDSVC
ASDNPERPNS FVIITAERVL HCNADTPEEM HHWITLLQRS KGDARVDGQE FIIRGWLHKE
MKNSTKASLK LKKRWFLLTH NSLDYYKSSE RNALKLGTLV LNSLCSVVQP DEKLYKETGY
WNVIVYGRKH SYRLYCKLLN EATRWASSIQ NVIDTKAPID TPTQQLIQDI RENCLNSEVV
EQIYKRNPIL RYSHHPLHSP LLPLPYGDIQ LSGDRSYTTL QDEALRVFSS LQHLDGVADP
VAIIQGILQT GQELKPLRDE LYCQLIKQTA RPPQPGGPGN LCSWKILACM CCTFMPSRSI
LRYLKFHLKR TRELFPASEM DRYAAFAFES LKKTRARENV PSQEEIRSIV ARQEMSTTVH
CHGGGSCKIT INSHTTAGEV VEKLIRGLAM EDSRNMFALF EHNDASEKAI EMRTSESNTG
WKLYFKLYCF LDTDGVPKDS VEFAFMFEQA HEAVIQGHYP APEETLQFLA ALRLQYLLGD
QNPQSTVPEM SQVFPMARLR TRVQNSAKTF SGTGSVAERS GTAERKRSSF LEGTLRRSFR
SGSLSRQRLE EENSLEAWLR EEAAAVRTSV LDKWRKLQGM SQEQAMVKYM ALVKEWQGYG
STLFNVESRD GAFPAELWLG VSRESISVYK RGEPWPLEVF PYELILSFGA PLPNAYKIAV
EGRELVFETQ MVMDIAKLMK AYISMIVKKR YSNSQSVSSH ESKCSAW
//
