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Database: UniProt
Entry: A5DLV2_PICGU
LinkDB: A5DLV2_PICGU
Original site: A5DLV2_PICGU 
ID   A5DLV2_PICGU            Unreviewed;       718 AA.
AC   A5DLV2;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 2.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDK40155.2};
GN   ORFNames=PGUG_04253 {ECO:0000313|EMBL:EDK40155.2};
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK40155.2, ECO:0000313|Proteomes:UP000001997};
RN   [1] {ECO:0000313|EMBL:EDK40155.2, ECO:0000313|Proteomes:UP000001997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC   Y-324 {ECO:0000313|Proteomes:UP000001997};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004323}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the MNN1/MNT family.
CC       {ECO:0000256|ARBA:ARBA00009105}.
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DR   EMBL; CH408159; EDK40155.2; -; Genomic_DNA.
DR   RefSeq; XP_001483524.1; XM_001483474.1.
DR   AlphaFoldDB; A5DLV2; -.
DR   STRING; 294746.A5DLV2; -.
DR   GeneID; 5125171; -.
DR   KEGG; pgu:PGUG_04253; -.
DR   VEuPathDB; FungiDB:PGUG_04253; -.
DR   eggNOG; ENOG502RZ48; Eukaryota.
DR   HOGENOM; CLU_015387_0_0_1; -.
DR   InParanoid; A5DLV2; -.
DR   OMA; IWGDKEM; -.
DR   OrthoDB; 2005743at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046354; P:mannan biosynthetic process; IEA:UniProt.
DR   GO; GO:0035268; P:protein mannosylation; IEA:UniProt.
DR   InterPro; IPR022751; Alpha_mannosyltransferase.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR31392; ALPHA-1,3-MANNOSYLTRANSFERASE MNN1-RELATED; 1.
DR   PANTHER; PTHR31392:SF1; ALPHA-1,3-MANNOSYLTRANSFERASE MNN1-RELATED; 1.
DR   Pfam; PF11051; Mannosyl_trans3; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001997};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ   SEQUENCE   718 AA;  83448 MW;  F37FE37D0ECD3534 CRC64;
     MRYSIRRGFL VALVALAMVC MMVMYLRYDY AMGAVRGIPQ HTRFEESDSL LSKHVHVSNY
     KYGDYDRLAA KFNMEQFKQL PQEERCVKFF RDLLENDPDW ELRPFDKNVD LFERRILDKQ
     RYFRESIRDL RDDNDDRKKL DVPGSTYENA TVERNFQQAI KKTMETEQKM ADFIATTRIY
     QKCFVEEWVP PSTETELYDK MTNKVLPFLT NTLPEFTFNN STITNGFPLA DNFDVYHEYK
     GSNLVEFIKT KSNGKGIVLS ASSKHGRDIV KLIRLLRALD NTLPIQIIHR DDFSKRNREF
     VEFAATADKK ELLEPPGTYS WKKVWPEIDL LANGTAYGIN YTPQNVTFVN IKPAIKSEFR
     TKFPGFANKL LALFFTSFKE VVLLDADAIP LVRPNHFFLS QEYRETGTYF FKDRTLRDTN
     EYIETNFFAK LFPSANEKTL EDIFGISSAT YVSLGNTYMA GYRHYQEAGV VAIDKVAHLS
     GVMMMFPLSL WKEPVGSAVW GEKEMYWLGL SMAGDENYRF NYYPAASVGQ LTTAKQYSYY
     PDAESNEVCS THPGHIDKYG NVLWMNSGFS FCKKNSQSRD KQHFPLSEMN QMEVLGPLYA
     EPLVVTHAII PPTEPELRGI HNSYDKSRQM KKMDGWKLQK EIDEVDRSKQ PFFKDRNPSK
     GWMKNPICSG YYYCAYDKIT TFDKTTDNGV LVKIDNTLVE YYRYLGKAWL SGSSRLRN
//
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