MYO2B_NAUCC
ID MYO2B_NAUCC Reviewed; 1419 AA.
AC Q875X4; G0VGN7; Q875X5;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Myosin-2B;
DE AltName: Full=Class V unconventional myosin MYO2B;
DE AltName: Full=Type V myosin heavy chain MYO2B;
DE Short=Myosin V MYO2B;
GN Name=MYO2B; OrderedLocusNames=NCAS_0F01740;
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 1-361 AND 373-1419.
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; AACF01000111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; HE576757; CCC70658.1; -; Genomic_DNA.
DR EMBL; AY144941; AAO32504.1; -; Genomic_DNA.
DR EMBL; AY144940; AAO32503.1; -; Genomic_DNA.
DR RefSeq; XP_003677013.1; XM_003676965.1.
DR AlphaFoldDB; Q875X4; -.
DR SMR; Q875X4; -.
DR STRING; 1064592.Q875X4; -.
DR EnsemblFungi; CCC70658; CCC70658; NCAS_0F01740.
DR GeneID; 11527573; -.
DR KEGG; ncs:NCAS_0F01740; -.
DR eggNOG; KOG0160; Eukaryota.
DR HOGENOM; CLU_000192_9_0_1; -.
DR InParanoid; Q875X4; -.
DR OMA; FEHFEQN; -.
DR OrthoDB; 311886at2759; -.
DR Proteomes; UP000001640; Chromosome 6.
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; 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; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51126; DILUTE; 1.
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..1419
FT /note="Myosin-2B"
FT /id="PRO_0000123487"
FT DOMAIN 4..57
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 75..780
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 783..805
FT /note="IQ 1"
FT DOMAIN 806..830
FT /note="IQ 2"
FT DOMAIN 831..854
FT /note="IQ 3"
FT DOMAIN 855..878
FT /note="IQ 4"
FT DOMAIN 879..901
FT /note="IQ 5"
FT DOMAIN 902..931
FT /note="IQ 6"
FT DOMAIN 1143..1357
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 451..531
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 1061..1419
FT /note="Non alpha-helical, tail domain"
FT COILED 909..940
FT /evidence="ECO:0000255"
FT BINDING 169..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1419 AA; 162600 MW; F2ADF7D72A0845FC CRC64;
MSFEVGTRCW YPNSEAGWIG CEVTKNDFQD GTYHIELTSE TGLVIPIETK HLESNNAMEN
NHEFLPVLRN PPILEATHDL TTLSYLNEPA VLHAIKERYN QRNIYTYSGI VLIATNPFDK
VEELYSSEMI QAYARKNRDE MAPHIFAIAE EAYREMINND QNQTIIVSGE SGAGKTVSAK
YIMRFFASVE EEHFNKEGDS KHQEEMSDIE VKILATNPVM EAFGNAKTTR NDNSSRFGKY
LQILFDSNKN IIGSSIKTYL LERSRLVFQP TSERNYHIFY QMLSGLSSDM KKQLYLTNAE
DFFYLNQGGE STINGIDDSL EYSTTIESLS TVGIDTEVQL QIFKILAALL HIGNIEIKKT
RTDATLSSTD PSLQKACELL GLDPLTFSKW ITKKQINTRS EKIISNLSFN QALVARDSVA
KFIYSSLFDW LVGNINNVLC TSQVSETINS FIGVLDIYGF EHFEQNSFEQ FCINYANEKL
QQEFNHHVFK LEQEEYVKEE IEWSFIEFSD NQPCIDLIEN KLGILSLLDE ESRLPAGSDE
SWTTKLYQTF NKPPSNTVFG KPRFGQNKFI ISHYAVDVTY EVDGFIEKNK DTISESQLEV
LKATTNPTLA TIFEFSEAEN KTNITEQAGT IQRKTINRKP TLGSIFKRSL VELMETINST
NVHYIRCIKP NTEKEAWKFD NLMVLSQLRA CGVLETIKIS CAGFPSRWAF EEFIQRYYLL
APTDQWGRVT ADMEMSLEDM VAFCDLILSE KIDSKDKYQI GKTKIFFKAG VLAYLEKIRS
DKVTELAVLI QKHIRAKYYR SLYLQAMLSI KNCQSLIRGV QSRQRVDFEM KTDAATLLQT
LHRSTRVRSQ VFETLKNILE VQTAIRRVLV SNFIQREFES RSAIMIQSKI RANSPKHRYQ
TLKTGTILIQ ALVRRKQSQE KLKQLKIQAE SAASLKNSAA GIQKELIGFI EELISNIKEN
DAKTTEYKSL LKHTSLPVVT GTNERTAAYI STKNQVEEDK VTIRTILTKY ETLKDLCRKE
LKSLESLEKG VNDEKFASSL QSSLELIKRD ISDLRINAIE KDNERTSTSS ELKDGTDCTD
NAVVQILTKR QGDLINDLVN VVFLEFQIPQ RGRTKDCEHF YPVKLLISIV NLMNKFGLRK
SSHSILKQTV QDLIGKISSM DAKKCVTFGL YWIISLHKLS SLPQEPAVLN KLQDKFYKTW
LKQCFNQMKT VDSILILFDT ISEFTLFFQG TTELLTNIIT ALLQHINAKW FNDLLIKQNT
LSWTHGLEKD SEIKKVLDWC NSHKIRNSTE YLRNVNQACK LLQLRISNIS DFQLVCEFCY
DLSSLQMHAL LTKYRPTQFE KPIPVDVLNH LSNTARRERT TMKRELTLDA GTETYSVENL
FQGHPIEASD EHDDINQLIN QLPSDKDFPV IKELGSLLA
