ID A0A3B5B7J8_9TELE Unreviewed; 1848 AA.
AC A0A3B5B7J8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Unconventional myosin-Va-like {ECO:0000313|Ensembl:ENSSPAP00000029055.1};
GN Name=MYO5A {ECO:0000313|Ensembl:ENSSPAP00000029055.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000029055.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000029055.1}
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}.
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DR STRING; 144197.ENSSPAP00000029055; -.
DR Ensembl; ENSSPAT00000029523.1; ENSSPAP00000029055.1; ENSSPAG00000021833.1.
DR GeneTree; ENSGT00940000155347; -.
DR Proteomes; UP000261400; Unplaced.
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; 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; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR036103; MYSc_Myo5.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF752; MYOSIN-M HEAVY CHAIN; 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; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 5.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 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}.
FT DOMAIN 32..84
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 93..785
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1527..1803
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 622..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..687
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1125..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 937..1120
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1174..1289
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1342..1431
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 639..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 187..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1848 AA; 213268 MW; 27AA9C3690E50032 CRC64;
MDVPGLKQCA QHCSSAVAAV CPSSNFAFYS VSQCARVWIP DTEEVWKSAE LTKDYKNGDA
SLQLMLEDGS NIDHKLDPKT KNLPYLRNPD ILVGENDLTA LSYLHEPAVL HNLKVRFIDS
KLIYTYCGIV LVAINPYETL PIYGTDIINA YSGQNMGDMD PHIFAVAEEA YKQMARDERN
QSIIVSGESG AGKTVSAKYA MRYFATVSGS ASEANVEDKV LASNPIMEAI GNAKTTRNDN
SSRFGKYIEI GFDTRYRIIG ANMRTYLLEK SRVVFQADEE RNYHVFYQLC ASAHLPEFKN
LRLSNANDFL YTRQGRSPVI DGVDDTKELC TTRNAFTLLG INESYQMGLF QVLAAILHLG
NVEIKDRDSD SSVIPPNNRH LTAFCELVGV TYQDMSQWLC HRKLKTATET YIKTLPRLQA
TNARDALSKH IYAKLFNWIV EHVNKALITN VKQHSFIGVL DIYGFETFEI NSFEQFCINY
ANEKLQQQFN MHVFKLEQEE YMKEQIPWTL IDFYDNQPCI NLIEAKMGIL DLLDEECKMP
KGSDDSWAQK LYNTHLKTCS LFEKPRMSNR AFIIQHFADK VEYQCDGFLE KNKDTVNEEQ
INVLKASKFD LLVELFQDEE KATSPTGQVQ GTGGRTRLSI KPDKGREKSS KEHKKTVGCQ
FRNSLQMLME TLNATTPHYV RCIKPNDFKM AFSFDPKRAV QQLRACGVLE TIRISAAGFP
SRWTYQEFFS RYRVLMKQKD VLPDKKLTCR NVLEKLVQDQ DKYQFGKTKI FFRAGQVAYL
EKLRADKLRA ACIRIQKTIR CWLARKKYLR KRCAAITIQR FTRGYQARCL VKFMRRTQAA
IIIQKYQKMY VEKKRYRQKQ AAALAMQTIL RAYMARQKYQ GLLRQASAVI IQKHIRGWLA
RCWYKRCLVS IVYLQCCIRR MKARRELKKL KIEARSVEHF KKLNKGMENK IMQLQRKIDE
QHKENRVVNE RLVGLETSYT AESERMRGEL SRLRGVEEDA KNKANQVSSL LEELERLRKE
LSATQQEKKT IEDWAQTYRD EMEKMVSELK DQNGLLKKEK DDLNRSIQEQ SQQMTEKMTR
AIAQETQQLE TDLNEERSRY QNLLTEHLRL EEKYDDLKEE MVLSSNVSKP GHRRTDSTHS
SNESEYTYNS EYAELEDGSR VREDVTRGID TSLTLKLQKR LTELEQEKQS LRNELENKEE
QFQRARARDD EEFKKARGAE LEYESLKRQE LESENKKLKH DLAEMRQSLL GNAATGAGAP
GSPAYKVLLD QLNASCEELE VRKEEVLILR SQLVSQKEAM HHKVGCETMT EPSVYADDVT
KLKDAEVKQA YVGLKDTNRL LEQQLQSQRR TYDSEVEALR GELQNVKEEN NRQQQLLAQN
LQLPPEARIE ASLQHEITRL TNENLDLMEQ LEKQDRTIRK LKKQLKVYSK RIGEMGAGQA
EGQTSPGQMV DEPIHPVNIP RREKDFQGML EYKKEDELKL VKNLILELKP RGVAVNLIPG
LPAYILFMCL RHADYVNDDQ KVRTLLTSTI NSIKKILKKR GDDFETVSFW LANTCRFLHC
LKQYSGDEQF MKHNTSRQNE HSLSNFDLAE YRQVISDLAI QIYQQLIKCM ENILQPMIVS
GMLEHETIQG VSGVKPTGLR KRTSSIADEG TYTLDSILRQ LSAFHSTMCQ HGTDPELIKQ
VVKQQFYIIG AVTLNNLLLR KDMCSWSKGM QIRYNVSQLE EWLRDKGLMT CGAKETLEPL
IQAAQLLQVK KKTDEDAEAI CSMCLALTTA QIVKVLNLYT PVNEFEERVS VAFIRTIQTR
LRDRCESPQL LMDTKMIYPV TFPFNPSSLA LETIQIPSSL NLAFLTRV
//
