ID A0A2Y9NQQ1_DELLE Unreviewed; 1852 AA.
AC A0A2Y9NQQ1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Unconventional myosin-Va isoform X6 {ECO:0000313|RefSeq:XP_022435226.1};
GN Name=MYO5A {ECO:0000313|RefSeq:XP_022435226.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022435226.1};
RN [1] {ECO:0000313|RefSeq:XP_022435226.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022435226.1};
RG RefSeq;
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 RefSeq; XP_022435226.1; XM_022579518.2.
DR Proteomes; UP000248483; 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 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; IPR004009; Myosin_N.
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; 6.
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; 6.
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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, 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:UP000248483}.
FT DOMAIN 8..60
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 69..763
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1531..1807
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 598..634
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 1106..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 915..1105
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1155..1231
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1336..1436
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 598..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 163..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1852 AA; 214874 MW; 07F225EDF7BF4DBA CRC64;
MAASELYTKF ARVWIPDPEE VWKSAELLKD YKPGDKVLLL HLEDGRDLEY RLDPKTKELP
HLRNPDILVG ENDLTALSYL HEPAVLHNLR VRFIDSKLIY TYCGIVLVAI NPYEQLPIYG
EDIINAYSGQ NMGDMDPHIF AVAEEAYKQM ARDERNQSII VSGESGAGKT VSAKYAMRYF
ATVSGSASEA NVEEKVLASN PIMESIGNAK TTRNDNSSRF GKYIEIGFDK RHRIIGANMR
TYLLEKSRVV FQAEEERNYH IFYQLCASAK LPEFKMLRLG DANNFHYTKQ GGSPVIEGVD
DAKEMAQTRQ ACTLLGISES YQMGIFRILA GILHLGNVGF MSRDSDSCTI PPKHEPLSIF
CDLMAVDFEE MCHWLCHRKL ATAAETYIKP ISKLQATNAR DALAKHIYAK LFNWIVDHVN
QVLHSAVKQH SFIGVLDIYG FETFEINSFE QFCINYANEK LQQQFNMHVF KLEQEEYMKE
QIPWTLIDFY DNQPCINLIE SKLGILDLLD EECKMPKGTD DTWAQKLYNT HLNKCALFEK
PRLSNKAFII QHFADKVEYQ CEGFLEKNKD TVFEEQIKVL KSSKFKMLPE LFQDDEKAIS
PSSATSSGRT LLTRTPAKPT KGRPGQAAKE HKKTVGHQFR NSLHLLMETL NATTPHYVRC
IKPNDFKFPF TFDEKRAVQQ LRACGVLETI RISAAGFPSR WTYQEFFSRY RVLMKQKDVL
SERKQTCKNV LEKLIEDKDK YQFGKTKIFF RAGQVAYLEK LRADKLRAAC IRIQKTIRGW
LLRKKFLRMR KAAITVQRYV RGHQARCYAK FLRRTKAATI IQKYWRMYVI RQRYKIWRTA
TIVLQSYLRG YLARNRYRKI LREHKAVIIQ KWVRGWLART YYKRSMHAII YLQCCFRRMM
AKRELKKLKI EARSVERYKK LHIGMENKIM QLQRKVDEQN KDYKCLMEKL TNLEGIYNSE
TEKLRSDLER LQLSEEEAKI ATGRVLSLQE EIAKLRKDLE QTQCEKKSIE ECADRYKQET
EQLVSNLKEE NTLLKQEKEA LNHLIVEQAK EMTETMEKKL IEETKQLELD LNDERLRYQN
LLNEFSRLEE RYDDLKEEMT LMVNVPKPGH RRTDSTHSSN ESEYTFSSEI AETEDIPSRT
EEPSEKKVPL DMSLFLKLQK RVTELEQEKQ VMQDELDRKE EQVLRSKAKE EERPQIRGAE
LEYESLKRQE LESENKKLKN ELNELRKALS EKSAPEVTAP GAPAYRVLME QLTSVSEELD
VRKEEVLILR SQLVSQKEAI QPKNTMTDST ILLEDVQKMK DKGEIAQAYI GLKETNRSSA
MDGHELNEDG ELLLVYEGLK QANRLLESQL QSQKRSHENE AEALRGEIQS LKEENNRQQQ
LLAQNLQLPP EARIEASLQH EITRLTNENL DLMEQLEKQD KTVRKLKKQL KVFAKKIGEL
EVGQMENISP GQIIDEPIRP VNIPRKEKDF QGMLEYKKED EQKLVKNLIL ELKPRGVAVN
LIPGLPAYIL FMCVRHADYL NDDQKVRSLL TSTINSIKKV LKKRGDDFET VSFWLSNTCR
FLHCLKQYSG EEGFMKHNTS RQNEHCLTNF DLAEYRQVLS DLAIQIYQQL VRVLENILQP
MIVSGMLEHE TIQGVSGVKP TGLRKRTSSI ADEGTYTLDS ILRQLNSFHS VMCQHGMDPE
LIKQVVKQMF YIVGAVTLNN LLLRKDMCSW SKGMQIRYNV SQLEEWLRDK NLMNSGAKET
LEPLIQAAQL LQVKKKTDDD AEAICSMCNA LTTAQIVKVL NLYTPVNEFE ERVSVSFIRT
IQMRLRDRKD SPQLLMDAKH IFPVTFPFNP SSLALETIQI PASLGLGFIS RV
//
