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Database: UniProt
Entry: U3KBL5_FICAL
LinkDB: U3KBL5_FICAL
Original site: U3KBL5_FICAL 
ID   U3KBL5_FICAL            Unreviewed;      1695 AA.
AC   U3KBL5;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Myosin VA {ECO:0000313|Ensembl:ENSFALP00000012419.2};
GN   Name=MYO5A {ECO:0000313|Ensembl:ENSFALP00000012419.2};
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:ENSFALP00000012419.2, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000012419.2, 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:ENSFALP00000012419.2}
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.ENSFALP00000012419; -.
DR   Ensembl; ENSFALT00000012469.2; ENSFALP00000012419.2; ENSFALG00000011894.2.
DR   eggNOG; KOG0160; Eukaryota.
DR   GeneTree; ENSGT00940000155347; -.
DR   HOGENOM; CLU_000192_9_2_1; -.
DR   Proteomes; UP000016665; Chromosome 10.
DR   GO; GO:0005884; C:actin filament; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0032433; C:filopodium tip; IEA:Ensembl.
DR   GO; GO:0005770; C:late endosome; IEA:Ensembl.
DR   GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR   GO; GO:0042470; C:melanosome; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:Ensembl.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0005777; C:peroxisome; IEA:Ensembl.
DR   GO; GO:0055037; C:recycling endosome; IEA:Ensembl.
DR   GO; GO:0001726; C:ruffle; IEA:Ensembl.
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:0031267; F:small GTPase binding; IEA:Ensembl.
DR   GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IEA:Ensembl.
DR   GO; GO:0030050; P:vesicle transport along actin filament; IEA:Ensembl.
DR   CDD; cd15478; Myo5a_CBD; 1.
DR   CDD; cd01380; MYSc_Myo5; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 3.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.30.70.1590; -; 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   InterPro; IPR002710; Dilute_dom.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR037988; Myo5a_CBD.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR036103; MYSc_Myo5.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF273; UNCONVENTIONAL MYOSIN-VA; 1.
DR   Pfam; PF01843; DIL; 1.
DR   Pfam; PF00612; IQ; 5.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM01132; DIL; 1.
DR   SMART; SM00015; IQ; 6.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR   PROSITE; PS51126; DILUTE; 1.
DR   PROSITE; PS50096; IQ; 6.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW   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}; Reference proteome {ECO:0000313|Proteomes:UP000016665}.
FT   DOMAIN          1..632
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1374..1650
FT                   /note="Dilute"
FT                   /evidence="ECO:0000259|PROSITE:PS51126"
FT   REGION          469..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          512..534
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          975..999
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1039..1070
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          784..967
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1190..1279
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         32..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1695 AA;  196975 MW;  3E27297D7F9A0BD9 CRC64;
     MGDMDPHIFA VAEEAYKQMA RDERNQSIIV SGESGAGKTV SAKYAMRYFA TVSGSASEAN
     VEEKVLASNP IMESIGNAKT TRNDNSSRFG KYIEIGFDKR YRIIGANMRT YLLEKSRVVF
     QAEEERNYHI FYQLCASAAL PEFKTLRLGN ANYFHYTKQG GSPVIDGVDD AKEMVNTRQA
     CTLLGISDSY QMGIFRILAG ILHLGNVEFA SRDSDSCTVP PKHEPLTIFC DLMGVEYEEM
     AHWLCHRKLA TATETYIKPI SKLHAINARD ALAKHIYANL FNWIVDHVNK ALHATVKQHS
     FIGVLDIYGF ETFEINSFEQ FCINYANEKL QQQFNMHVFK LEQEEYMKEQ IPWTLIDFYD
     NQPCINLIEA KMGVLDLLDE ECKMPKGSDD SWAQKLYNTH LNKCALFEKP RMSNKAFIIK
     HFADKVEYQC EGFLEKNKDT VYEEQIKVLK SSKFKLLLEL FQDEEKVLSP TSATPSGRVP
     LSRTPIKPAK ARPGQASKEH KKTVGHQFRN SLHLLMETLN ATTPHYVRCI KPNDFKFPFT
     FDEKRAVQQL RACGVLETIR ISAAGFPSRW TYQEFFSRYR VLMKQKDVLG DRKQTCKNVL
     EKLIQDKDKY QFGKTKIFFR AGQVAYLEKI RADKLRAACI RIQKTIRGWL MRKKYMRMRK
     AAITIQRHVR GYQARCYATF LRRTRAATTI QKFQRMYVVR KRYQRMREAT IALQALLRGY
     MVRNKYQMML REHKCVVLQK HVRGWLARRR YRRTLRAVVY LQCCYRRMMA KRELKKLKIE
     ARSVERYKKL HIGLENKIMQ LQRKIDEQNK EYKSLLEKMS SLELTYSTET EKLRSDVERL
     RTSEEEARSA TSRVLSLQEE IAKLRRELQH TQAEKRSIEE RADKYKHETE QLVSELKEQN
     SLLKTEKEEL NRRIHDQAKE ITESMEKKLV EETKQLELDL NDERLRYQNL LNEFSRLEER
     YDDLKDEMNL MVSIPKPGHK RTDSTHSSNE SEYTFSSEIT EAEDLPLRME QEPSEKKAAL
     DMSLFLKLQK RVSELEQEKQ SLQDELDRKE EQALRAKAKE EERPPIRGAE LEYESLKRQE
     LESENKKLKN ELNELQKALT ETRAPEVTAP GAPAYRVLLD QLTSVSEELE VRKEEVLILR
     SQLVSQKEAI QPKHTMTDAT ILLEDVQKMK DKGEIAQAYI GLKETNRLLE SQLQSQKKSH
     ENELESLRGE IQSLKEENNR QQQLLAQNLQ LPPEARIEAS LQHEITRLTN ENLDLMEQLE
     KQDKTVRKLK KQLKVFAKKI GELEVGQMEN ISPGQIIDEP IRPVNIPRKE KDFQGMLEYK
     KEDEQKLVKN LILELKPRGV AVNLIPGLPA YILFMCVRHA DYLNDDQKVR SLLTSTINGI
     KKVLKKRGDD FETVSFWLSN TCRFLHCLKQ YSGEEGFMKH NTPRQNEHCL TNFDLAEYRQ
     VLSDLAIQIY QQLVRVLENI LQPMIVSGML EHETIQGVSG VKPTGLRKRT SSIADEGTYT
     LDSIIRQLNS FHSVMCQHGM DPELIKQVVK QMFYIIGAIT LNNLLLRKDM CSWSKGMQIR
     YNVSQLEEWL RDKNLMNSGA KETLEPLIQA AQLLQVKKKT DEDAEAICSM CNALTTAQIV
     KVLNLYTPVN EFEERVLVSF IRTIQVRLRD RKDSPQLLMD AKHIFPVTFP FNPSSLALET
     IQIPASLGLG FISRV
//
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