ID C8Z3J7_YEAS8 Unreviewed; 1471 AA.
AC C8Z3J7;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Myo4p {ECO:0000313|EMBL:CAY77621.1};
GN ORFNames=EC1118_1A20_0507g {ECO:0000313|EMBL:CAY77621.1};
OS Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=643680 {ECO:0000313|EMBL:CAY77621.1, ECO:0000313|Proteomes:UP000000286};
RN [1] {ECO:0000313|EMBL:CAY77621.1, ECO:0000313|Proteomes:UP000000286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lalvin EC1118 / Prise de mousse
RC {ECO:0000313|Proteomes:UP000000286};
RX PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambot B.,
RA Legras J.L., Wincker P., Casaregola S., Dequin S.;
RT "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FN393058; CAY77621.1; -; Genomic_DNA.
DR HOGENOM; CLU_000192_9_0_1; -.
DR Proteomes; UP000000286; Chromosome I, Scaffold EC1118_1A20.
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:0051641; P:cellular localization; IEA:UniProt.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR CDD; cd15479; fMyo4p_CBD; 1.
DR CDD; cd01380; MYSc_Myo5; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 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; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 4.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 2.
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 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}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 4..57
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 71..777
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1164..1419
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 647..669
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT BINDING 165..172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1471 AA; 169194 MW; 6F4138853C8EA3AA CRC64;
MSFEVGTKCW YPHKEQGWIG GEVTKNDFFE GTFHLELKLE DGETVSIETN SFENDDDHPT
LPVLRNPPIL ESTDDLTTLS YLNEPAVLHA IKKRYMNGQI YTYSGIVLIA ANPFDKVDHL
YSREMIQNYS SKRKDELEPH LFAIAEEAYR FMVHEKANQT VVVSGESGAG KTVSAKYIMR
YFASVQESNN REGEVEMSQI ESQILATNPI MEAFGNAKTT RNDNSSRFGK YLQILFDENT
TIRGSKIRTY LLEKSRLVYQ PETERNYHIF YQILEGLPEP VKQELHLSSP KDYHYTNQGG
QPNIAGIDEA REYKITTDAL SLVGINHETQ LGIFKILAGL LHIGNIEMKM TRNDASLSSE
EQNLQIACEL LGIDPFNFAK WIVKKQIVTR SEKIVTNLNY NQALIARDSV AKFIYSTLFD
WLVDNINKTL YDPELDQQDH VFSFIGILDI YGFEHFEKNS FEQFCINYAN EKLQQEFNQH
VFKLEQEEYV KEEIEWSFIE FSDNQPCIDL IENKLGILSL LDEESRLPSG SDESWASKLY
SAFNKPPSNE VFSKPRFGQT KFIVSHYAVD VEYEVEGFIE KNRDSVSLGH LDVFKATTNP
IFKQILDNRE LRSDDAPEEQ NTEKKIMIPA RLSQKKPTLG SMFKKSLGEL MAIINSTNVH
YIRCIKPNSE KKPWEFDNLM VLSQLRACGV LETIRISCAG FPSRWTFDEF VQRYFLLTDY
SLWSGILYNP DLPKEEIVNF CQSILDATIS DSAKYQIGNT KIFFKAGMLA FLEKLRTNKM
NEICIIIQKK IRARYYRLQY LQTMESIKKC QSQIRSLLVR TRVDHELKTR AAILLQTNIR
ALWKREYYRA AIGQIVKLQC TCKSKLILDS VNRKFMLMAA VIIQSYIRSY GHKTDYRTLK
RSSVLVQSAM RMQLARRRYI VLQKEAEERN IRASYGIGLL EEAIEFKNSF ILNLEMLNDS
YTRLTQLLQG DLSNIPSKQR QEYETIVNGY NDKISKLKTL QGEIMNTLNK KNALKERKKK
QSSLIQSHMQ SLAAIKGNKP SRLSDEVKSM KQELAFIENV IAQDFTTTYS TNKNDKVKGL
GIAGQQVKPK LVNVIRRESG NPDLLELLMD LNCYTLEVTE GYLKKVNVTE VNGDNVLGPI
HVITTVVSSL VRNGLLIQSS KFISKVLLTV ESIVMSLPKD ETMLGGIFWL SNLSRLPAFA
ANQKTLYEGN GGDEKDKLTL IYLNDLENET LKVFDKIYST WLVKFMKHAS AHIEIFDMVL
NEKLFKNSGD EKFAKLFTFL NEFDAVLCKF QVGDSMHTKI FNDTLKYLNV MLFNDLITKC
PALNWKYGYE VDRNIERLVS WFEPRIEDVR PNLIQIIQAV KILQLNISNL NEFKLLFDFW
YALNPAQIQA ILLKYKPANK GEAGVPNEIL NYLANVIKRE NLSLPGKMEI MLSAQFDSAK
NHLRYDTSAI TQNSNTEGLA TVSKIIKLDR K
//
