ID B3LTA9_YEAS1 Unreviewed; 918 AA.
AC B3LTA9;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Vacuolar membrane protein {ECO:0000313|EMBL:EDV09444.1};
GN ORFNames=SCRG_05127 {ECO:0000313|EMBL:EDV09444.1};
OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=285006 {ECO:0000313|EMBL:EDV09444.1, ECO:0000313|Proteomes:UP000008335};
RN [1] {ECO:0000313|Proteomes:UP000008335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM11-1a {ECO:0000313|Proteomes:UP000008335};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA Kruglyak L.;
RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004287};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the VPS18 family.
CC {ECO:0000256|ARBA:ARBA00010454}.
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DR EMBL; CH408054; EDV09444.1; -; Genomic_DNA.
DR AlphaFoldDB; B3LTA9; -.
DR SMR; B3LTA9; -.
DR HOGENOM; CLU_003488_0_0_1; -.
DR Proteomes; UP000008335; Unassembled WGS sequence.
DR GO; GO:0098588; C:bounding membrane of organelle; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd16462; RING-H2_Pep3p-like; 1.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR007810; Pep3_Vps18.
DR PANTHER; PTHR23323; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR23323:SF26; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 18 HOMOLOG; 1.
DR Pfam; PF05131; Pep3_Vps18; 1.
DR SMART; SM00299; CLH; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50236; CHCR; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 4..378
FT /note="Pep3/Vps18/deep orange beta-propeller"
FT /evidence="ECO:0000259|Pfam:PF05131"
SQ SEQUENCE 918 AA; 107398 MW; 37AE3C34AE0470B8 CRC64;
MIKTRIEEVQ LQFLTGNTEL THLKVSNDQL IVTTQRTIYR INLQDPAIVN HFDCPLSKEL
ETIMNVHVSP MGSVILIRTN FGRYMLLKDG EFTQLNKIKN LDLSSLHWIN ETTFLMGIKK
TPKLYRVELT GKDITTKLWY ENKKLSGGID GIAYWEGSLL LTIKDNILYW RDVTNMKFPL
VLPDESEQFE RLKHHAIKKF DSYNGLFAWV TSNGIVFGDL KEKQMEKDPA SNNFGKFLSS
SKVLLNFELP DYQNDKDHLI KDIVLTAFHI LLLRKNTVTM VSQLNNDVVF HETIPRHQLT
GSNTDSNEKF LGLVRDSVKE TFWCFSNINV FEIIIENEPN SVWNLLVRDN KFDKALSLKG
LTVREIESVK LSKAMYLFHT AKDFHSAAQT LGSMKDLSHF GEIALNFLQI KDYNDLNVIL
IKQLDNVPWK STQVVLSSWI IWNFMKQLND IELKINTTKP ASTDEDNLLN WNLNLKEKSN
ELTKFLESHL EKLDNETVYQ IMSKQNRQNE LLIFASLIND MKFLLSFWID QGNWYESLKI
LLTINNHDLV YKYSLILLLN SPEATVSTWM KIKDLDPNKL IPTILKFFTN WQNNSKLITN
ISEYPENYSL TYLKWCVREV PKMCNPIVYN SILYMMITDP RNDMILENDI IKFMKSNENK
YDLNFQLRLS LKFKKTKTSI FLLTRLNLFE DAIDLALKNN LIDDCKVIVN DEILIEDYKL
RKRLWLKIAK HLLLSMKDID IKQLIRTILN DSNEILTIKD LLPFFNEYTT IANLKEELIK
FLENHNMKMN EISEDIINSK NLKVEINTEI SKFNEIYRIL EPGKSCDECG KFLQIKKFIV
FPCGHCFHWN CIIRVILNSN DYNLRQKTEN FLKAKSKHNL NDLENIIVEK CGLCSDININ
KIDQPISIDE TELAKWNE
//