ID A0A3Q1BNW3_AMPOC Unreviewed; 1850 AA.
AC A0A3Q1BNW3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Myosin VA {ECO:0000313|Ensembl:ENSAOCP00000010681.1};
GN Name=MYO5A {ECO:0000313|Ensembl:ENSAOCP00000010681.1};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000010681.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000010681.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; 80972.ENSAOCP00000010681; -.
DR Ensembl; ENSAOCT00000017852.1; ENSAOCP00000010681.1; ENSAOCG00000015070.1.
DR GeneTree; ENSGT00940000155347; -.
DR Proteomes; UP000257160; 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:SF860; DILUTE CLASS UNCONVENTIONAL MYOSIN, ISOFORM C; 1.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 4.
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}; Reference proteome {ECO:0000313|Proteomes:UP000257160}.
FT DOMAIN 10..62
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 71..763
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1529..1805
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 599..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..665
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1101..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1152..1267
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1333..1433
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 617..631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 165..172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1850 AA; 213978 MW; 591E9BE406B57BEA CRC64;
MNRELEYMFV QCARVWIPDA EEVWKSAELT KDYKNGDASL HLMLEDGTNI DHKLDPKTKN
LPYLRNPDIL VGENDLTALS YLHEPAVLHN LKVRFIDSKL IYTYCGIVLV AINPYETLPI
YGTDIINAYS GQNMGDMDPH IFAVAEEAYK QMARDERNQS IIVSGESGAG KTVSAKYAMR
YFATVSGSAS EANVEDKVLA SNPIMEAIGN AKTTRNDNSS RFGKYIEIGF DTRYRIIGAN
MRTYLLEKSR VVFQADEERN YHIFYQLCAS AHLPEFKNLR LSSANDFLYT RQGRSPVIDG
VDDTKELCTT RNAFTLLGIN ESYQMGLFQV LAAILHLGNV EIKDRDSDSS LIPPNNRHLT
AFCELVGVTY QDMAQWLCHR KLKTATETYV KPLPRLQATN ARDALSKHIY AKLFNWIVEH
VNKALITNVK QHSFIGVLDI YGFETFEINS FEQFCINYAN EKLQQQFNMH VFKLEQEEYM
KEQIPWTLID FYDNQPCINL IEAKMGILDL LDEECKMPKG SDDSWAQKLY NTHLKTCSLF
EKPRMSNRAF IIQHFADKVE YQCDGFLEKN KDTVNEEQIN VMKASKFDLL VELFQDEEKA
TSPTGQVPGT GGRTRLSIKP DKGRDTKSKE HKKTVGCQFR NSLQMLMETL NATTPHYVRC
IKPNDFKLAF SFDPKRAVQQ LRACGVLETI RISAAGFPSR WTYQEFFSRY RVLMKQKDVL
PDKKLTCRNV LEKLVQDQDK YQFGKTKIFF RAGQVAYLEK LRADKLRAAC IRIQKTIRCW
LARKKYLRKR CAAITIQRFT RGYQARCLAK FMRRTQAATI IQKYQRMYVE KRRYRQKQAA
ALAMQTILRA YMARQKYQAL LREAKAVIIQ KRIRGWLARC WYKRCLHSIV YLQCCIRRMR
AKRELKKLKI EARSVEHFKK LNKGMENKIM QLQRKIDEQS KENRTINDRL VGLESSYTAE
SERMRGELGR LRGVEEDAKN KANQVSSLLE ELERLKKELS ATQQEKKTIE DWAQKYRDEM
EKMVSELKDQ NGLLKKEKDD LNRSIQEQSQ QMTEKMTRAI AQETQQLETD LNEERSRYQN
LLTEHLRLEE KYDDLKEEMA LSSNVSKPGH KRTDSTHSSN ESEYTYNSEY AELEDGSRAR
EDVTRGIDTS LTLKLQKRLT ELEQEKQSLR NELENKEEQF QRARARDDEE FKKARGAELE
YESLKRQELE SENKKLKHDL AEMRQSLLGN AATGAGAPGS PAYKVLLDQL NASCEELEVR
KEEVLILRSQ LVSQKEAMHH KETMTEPSVY AADVSKLKDA EVKQAYVGLK DTNRSAAPDF
HKLNEDGELW LVNQGLKETI RLLEQQLQTQ RRTYDNEVEA LRGELQNVKE ENNRQQQLLA
QNLQLPPEAR IEASLQHEIT RLTNENLDLM EQLEKQDRTI RKLKKQLKVY SKRIGEMGAG
QTEGQTSPGQ MVDEPIHPVN IPRREKDFQG MLEYKKEDEL KLVKNLILEL KPRGVAVNLI
PGLPAYILFM CLRHADYVND DQKVRTLLTS TINSIKKILK KRGDDFETVS FWLANTCRFL
HCLKQYSGDE QFMKHNTSRQ NEHCLSNFDL AEYRQVISDL AIQIYQQLIK CMENILQPMI
VSGMLEHETI QGVSGVKPTG LRKRTSSIAD EGTYTLDSIL RQLSAFHSTM CQHGTDPELI
KQVVKQQFYI IGAVTLNNLL LRKDMCSWSK GMQIRYNVSQ LEEWLRDKGL MTCGAKETLE
PLIQAAQLLQ VKKKTDEDAE AICSMCLALT TAQIVKVLNL YTPVNEFEER VSVAFIRTIQ
TRLRDRCESP QLLMDTKMIY PVTFPFNPSS LALETIQIPG SLNLAFLTRV
//
