ID U3JP31_FICAL Unreviewed; 1977 AA.
AC U3JP31;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 24-JAN-2024, entry version 74.
DE RecName: Full=Myosin X {ECO:0008006|Google:ProtNLM};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000004535.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000004535.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000004535.2}
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|PROSITE-ProRule:PRU00782}.
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DR STRING; 59894.ENSFALP00000004535; -.
DR Ensembl; ENSFALT00000004559.2; ENSFALP00000004535.2; ENSFALG00000004359.2.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000155469; -.
DR HOGENOM; CLU_001626_1_0_1; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000016665; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; 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 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; 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:SF4; MYOSIN X,-LIKE 1; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF16735; MYO10_CC; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00784; MyTH4; 1.
DR Pfam; PF00169; PH; 2.
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; 5.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
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|PROSITE-ProRule:PRU00782};
KW Reference proteome {ECO:0000313|Proteomes:UP000016665}.
FT DOMAIN 13..690
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1127..1225
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1307..1412
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1450..1610
FT /note="MyTH4"
FT /evidence="ECO:0000259|PROSITE:PS51016"
FT DOMAIN 1615..1959
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 570..592
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 893..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 756..846
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 901..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107..114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1977 AA; 226121 MW; BE3B580C93200B46 CRC64;
MKKVLPMHQT SVDGVEDMSM LGDLHEAAIL LNLHQRYQQG NIYTNIGSIL ASVNPYKAIP
GLYSVDAIEL YRQHRLGELP PHIFATANEC YCCLWKRHDS QCVLISGESG AGKTESTKLL
LKFLSAMSQT SLGAPVCEKS THVEEAILES SPILEAFGNA KTVYNNNSSR FGKFIQLHFS
QHGHIQGGRV TDCILLCSNR VVHQNPGERN YHIFYALLAG VSGEQKESLS LCEPEAYHYL
NQSGCVTDEN LNDVEMFSKV MTAMKVVDFS TEEIRDIFKL LSGTLHLGNV EFMTAGGAQV
TTKAVLNVAS DLLGLDAFQL SEVLTQRSMI LRGEEISSPL TVEQAADSRD SLSMALYSQC
FSWLISKINT KIKGKENFKS VGILDIFGFE NFQVNRFEQF NINYANEKLQ EYFNKHIFSL
EQLEYNREGI NWEAIDWMDN AECLDLIEKK LGLLALVNEE SRFPKGTDNT LLEKLHSQHM
SNPYYVKPRV TDHQFGIRHY AGEVLYDVRG FLEKNRDTFR DDILNMLKDS RLDFIYDLFE
RVCSRCSEET LKMGTQRRRP TVSSQFRDSL HSLMATLSTS NPFFIRCIKP NTEKAPNLFN
PDVVLNQLRY SGMLETVKVR RAGFPVRRLF QDFLSRYKML VKGPSPSDNS KAVCAGFLQT
YDSSKKEWQL GKTKVFLKEA LEQKLEKDRE EELRKAAIVI RAHVLGYMAR KKYQKVLSSV
VVIQKNYRAY LWKRSLLRLK ASAVTLQKHW RGRLARGRYQ QLLRELRRRR EEEEEINTEE
VDIPLQEEER RQMEEILRLE KEIEKLQQQK EDHMSVISED TRNEICRQRE EEIQRLEKEA
SRVAQEFLEL LDFGNLDESV QNLERSLSSE GTLNIDCSLV APLAEEEVDE GFHADDEGRP
ASSLVSNQHG TRNSGNYSKE VTNTKLLHLQ REVGEVAHAP GLLVERTTSP KEQGALSDPA
ESIYSTVSDT QRSNSGGAGE PIYTCPPDVE SDYDHESNSG GAGEPIDTCP PDVESDYDHE
EFDGCGDAGN ASAEPLNDEE GLRHSHGTSL DSNRGSLDSF LESEEEVDVY IDTDEEFCNG
RVTIFNGSGP PYFHSYLYMK GGLMNPWRRR WCVLKNEAFM WFRTKQEALK SGWLYKKGGG
MSTLSRRNWK RRWFVLRESK LMYFENDSEE KLKGTIDIRR AKEIVDIHEK ENALDIVTED
RVYHIVAESP EDASGWFNVL SRVHSATAQQ LREMQDEQAN PKNAVGTLDV GLIDSVCASD
NPDRPNSFVI ITANRVIHCN SDTPEEMHHW ISLLQKPKGE SKVDGQEFLV RGWLHKEVQS
SNKMSSLKMK KRWFVLTNTA LDYYKSSERT AAKLGTLVLN SLCSVVQPDE RVFKDTGYWN
IIVHGRKHSY RLYTKLLNEA MRWASAIQGV IDSKVPIETP TQQLIRDIRE NSTNFEVVEQ
TYRRNPILRY TQHPLHSPLL PLPYGDVSVN LQQEKGYSSL QDEAVKIFNS LQEIETVSDP
IPIIQGILQT CHDLKPLRDE VYCQLIKQTN HMPHPNSTGN LHHWQLMTCM SCTFLPSRGI
LRYLKFHLRR VKDLFPDSEI DRYAQFISDS LKRTKTREFV PSQEEIQALL TREEMTTTVY
CHGGGSCKIT INSHTSAGEV VEKLIRGLAM EDSRNMFALF EHNQQVDRAV ESRVIVADIL
AKFERLAGSE EDEEEGQWQL YFKLYCFLDI ENVPKDGVEF AFMFEQAHES LIAGHFPGPE
DTLQRLAALR LQYLHGDYSK ISWTLDGIYP VNRLKSKILH STKSSSSTSH TLERRRTSFL
EGTLKRSFKT GSVKKQKVEE EQMMEMWVKE ELSAARASIA QKWTKLQGLS QHQAMVKYMS
IVKEWPGYGS TLFDVECKEG GFPNDLWLGV STENVSVYKR GDPKPLETFQ YEHIVFFGAP
QPNTFKITVD EREMFFETSQ VGEIIKIMKA YINMIVKKRC SVKSATSVDS HASIWTR
//