MYO2A_NAUCC
ID MYO2A_NAUCC Reviewed; 1567 AA.
AC Q875X3; G0VJK1; Q875X2;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Myosin-2A;
DE AltName: Full=Class V unconventional myosin MYO2A;
DE AltName: Full=Type V myosin heavy chain MYO2A;
DE Short=Myosin V MYO2A;
GN Name=MYO2A; OrderedLocusNames=NCAS_0I00130;
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630;
RX PubMed=12775844; DOI=10.1126/science.1084337;
RA Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J.,
RA Waterston R., Cohen B.A., Johnston M.;
RT "Finding functional features in Saccharomyces genomes by phylogenetic
RT footprinting.";
RL Science 301:71-76(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-252 AND 263-782.
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630;
RX PubMed=12594514; DOI=10.1038/nature01419;
RA Langkjaer R.B., Cliften P.F., Johnston M., Piskur J.;
RT "Yeast genome duplication was followed by asynchronous differentiation of
RT duplicated genes.";
RL Nature 421:848-852(2003).
CC -!- FUNCTION: Myosin heavy chain that is required for the cell cycle-
CC regulated transport of various organelles and proteins for their
CC segregation. Functions by binding with its tail domain to receptor
CC proteins on organelles and exerting force with its N-terminal motor
CC domain against actin filaments, thereby transporting its cargo along
CC polarized actin cables (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with calmodulin (CMD1) and the myosin
CC light chain MLC1 through its IQ repeats (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; AACF01000056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; HE576760; CCC71681.1; -; Genomic_DNA.
DR EMBL; AY144942; AAO32505.1; -; Genomic_DNA.
DR EMBL; AY144943; AAO32506.1; -; Genomic_DNA.
DR RefSeq; XP_003678027.1; XM_003677979.1.
DR AlphaFoldDB; Q875X3; -.
DR SMR; Q875X3; -.
DR STRING; 1064592.Q875X3; -.
DR PRIDE; Q875X3; -.
DR EnsemblFungi; CCC71681; CCC71681; NCAS_0I00130.
DR GeneID; 11525428; -.
DR KEGG; ncs:NCAS_0I00130; -.
DR eggNOG; KOG0160; Eukaryota.
DR HOGENOM; CLU_000192_3_1_1; -.
DR InParanoid; Q875X3; -.
DR OMA; WRGHRAF; -.
DR OrthoDB; 311886at2759; -.
DR Proteomes; UP000001640; Chromosome 9.
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-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd01380; MYSc_Myo5; 1.
DR Gene3D; 3.40.850.10; -; 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 Pfam; PF01843; DIL; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 5.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 3: Inferred from homology;
KW Actin-binding; ATP-binding; Cell cycle; Coiled coil; Motor protein; Myosin;
KW Nucleotide-binding; Protein transport; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..1567
FT /note="Myosin-2A"
FT /id="PRO_0000123486"
FT DOMAIN 4..57
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 70..786
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 789..818
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 812..836
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 837..859
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 860..884
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 885..907
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 908..937
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1230..1505
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 446..526
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 619..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1567
FT /note="Non alpha-helical, tail domain"
FT COILED 947..1091
FT /evidence="ECO:0000255"
FT BINDING 164..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 240..252
FT /note="FDKETAIIGAKMR -> LLKEFHHMEFSAE (in Ref. 3;
FT AAO32505)"
FT /evidence="ECO:0000305"
FT CONFLICT 263..276
FT /note="YQPKTERNYHIFYQ -> SSAELHVVEFYFLS (in Ref. 3;
FT AAO32506)"
FT /evidence="ECO:0000305"
FT CONFLICT 781..782
FT /note="FE -> LK (in Ref. 3; AAO32506)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1567 AA; 179490 MW; 86A37BC40BDBE3BE CRC64;
MSFEVGTRCW YPSKEQGWIG AEVTKNDLKD GTYFMELTLE DNEVVNVETK DLTNEKDPSL
PLLRNPPILE STEDLTTLSY LNEPAVLHAI KQRYSQLNIY TYSGIVLIAT NPFDRMDQLY
SQDMIQAYSG KRRGEIEPHL FAIAEEAYRL MKNDKQNQTI VVSGESGAGK TVSAKYIMRY
FASCDEENSS NMGNLQHTAE MSETEERILA TNPIMEAFGN AKTTRNDNSS RFGKYLEILF
DKETAIIGAK MRTYLLERSR LVYQPKTERN YHIFYQILAG LPEDVKQELH LTKADDYFYM
NQGGEPEIAG IDDVSEYGIT IKALTLVGVA PETQQHIFKI LAALLHIGNI EIKKTRNDSS
LSSDEPNLKI ACELLGVDPS NFAKWITKKQ IVTRSEKIVS NLNYSQALVA RDSVAKFIYS
ALFDWLVTNI NTVLCNPAVL DQIHSFIGVL DIYGFEHFEK NSFEQFCINY ANEKLQQEFN
QHVFKLEQEE YIKEEIEWSF IEFNDNQPCI DLIENKLGIL SLLDEESRLP AGSDESWTQK
LYQTLDKPPT NKVFSKPRFG QTKFVVSHYA LDVAYDVEGF IEKNRDTVSD GHLEVLKATT
NDTLSTILES VEESARKVEE AKKNAASQDQ KQLKKPTPIR QVQRKPTLGS MFKLSLIELM
QTINSTNVHY IRCIKPNGEK EAWKFDNLMV LSQLRACGVL ETIRISCAGF PSRWTFNEFI
LRYYILIPPV EWAPIFQKND LTEQDVINLC KKILAATVQD KEKYQIGNTK IFFKAGMLAY
FEKLRSTKMN SAIVLIQKHI RSKYYRKQYM LMKASLSLLG AYSKGTVIRQ RVEYELEQHA
ATLIQTMYRG YSKRSYISGV ISSIVKLQSR IREELEQREM QSKYESNAAI SIQSRIRAFV
PRKAYESKRR DTIVVQSLIR RRIAQRDFKK LKADAKSVHH LKEVSYKLEN KVIQLTQNLA
AKVKENRQLS KRLEELQATM VTVSELQDQL EAQKMENQKA LADQKDGFVL DSKSLKDQLI
KANKDVESVK FELATLTAKY TEMEAESKNQ LDELERTKTL LTESKTQNSD LYSEIKSLKE
ELAHLQTSIA LGTVTTNTNI VPHTPSRENR MPSGHMRAAE ENISPNQLKS IPSDTAADHV
SVNGYGMDDD IINTNTLTQI NEELYRLLEG TDVLNNEITE GLLKGFQVPD AGVAIQLSRR
DVVYPARILI IVLSEMWRFG LTKQSESFLA QVLTTIQKVV TTLKGIDLIP SGAFWLANVR
ELYSFVVFAQ HSILTEESFK KGMNDEEYNE YVSLVTELKE DFESLSYNIY NIWLKKLQKD
LQKKAINAVV VSESLPGFNA SESNGFLNKI FNSGEEYTMD DILTFFNNIF WCMKSFHIEN
EVFRTVIITL LNYVDTICFN DLIMKRNFLS WKRGLQLNYN VTRLEEWCKT HGLPDGAQYL
QHLIQTAKLL QLRKYTIEDI DMVRGICSSL SPAQLQKLIS QYHVADYESP IPQDILKYVA
DIVKKESTSA HNDIFLHPET GPFNDPFVAV KTRKFDQVEA YIPSWLVLPV TKRIVDLVAQ
QVTVPDA
