ID I6NDD3_ERECY Unreviewed; 615 AA.
AC I6NDD3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Alpha-1,2-mannosyltransferase MNN2 {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=Ecym_5314 {ECO:0000313|EMBL:AET40075.1};
OS Eremothecium cymbalariae (strain CBS 270.75 / DBVPG 7215 / KCTC 17166 /
OS NRRL Y-17582) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=931890 {ECO:0000313|EMBL:AET40075.1, ECO:0000313|Proteomes:UP000006790};
RN [1] {ECO:0000313|EMBL:AET40075.1, ECO:0000313|Proteomes:UP000006790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 270.75 / DBVPG 7215 / KCTC 17166 / NRRL Y-17582
RC {ECO:0000313|Proteomes:UP000006790};
RX PubMed=22384365;
RA Wendland J., Walther A.;
RT "Genome evolution in the Eremothecium clade of the Saccharomyces complex
RT revealed by comparative genomics.";
RL G3 (Bethesda) 1:539-548(2011).
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SIMILARITY: Belongs to the MNN1/MNT family.
CC {ECO:0000256|ARBA:ARBA00009105}.
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DR EMBL; CP002501; AET40075.1; -; Genomic_DNA.
DR RefSeq; XP_003646892.1; XM_003646844.1.
DR AlphaFoldDB; I6NDD3; -.
DR STRING; 931890.I6NDD3; -.
DR GeneID; 11471959; -.
DR KEGG; erc:Ecym_5314; -.
DR eggNOG; ENOG502QQ16; Eukaryota.
DR HOGENOM; CLU_013298_1_1_1; -.
DR InParanoid; I6NDD3; -.
DR OMA; KGYQYKA; -.
DR OrthoDB; 1985716at2759; -.
DR Proteomes; UP000006790; Chromosome 5.
DR GO; GO:0000030; F:mannosyltransferase activity; IEA:UniProt.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR InterPro; IPR022751; Alpha_mannosyltransferase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR31646; ALPHA-1,2-MANNOSYLTRANSFERASE MNN2; 1.
DR PANTHER; PTHR31646:SF1; ALPHA-1,2-MANNOSYLTRANSFERASE MNN2-RELATED; 1.
DR Pfam; PF11051; Mannosyl_trans3; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006790}.
FT REGION 69..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 615 AA; 70051 MW; D205D14EFF4108AB CRC64;
MLTRRFSKTL RLTVLTLIVC SLFLISNRTI TGELSQSIHA YLEDWIVLNG GDGKDRQILQ
EVIDAINGED ETHRESASRS DNAEKSIPDK LLSHSTPTAE EESRQAKLRG FYEKVFNMLS
KHAPSGSSSK IRGENCQLTK DIGGRLEDQK WWYKLSYEHL SKCLQVSRKD RKMLKKKHSD
YVADLASLVL PLDSYTGNGI VTVGGGKFSV LAFLMITTLR NVGTTLPVEV LIPPNEESEH
EFCNNVLPEF NAKCIYLSDV LPKSVLTSFE VKGYQLKSFA IIASSFQNLL LLDADNLPIK
NLDDIFESKP YKSTGLVLWP DFWRRTTSPI YYEVAGIPIN YNKRVRNSID DVTPASVYTS
NPYSLSTVPM HDLEGAIPDM STESGQLMIS KRTHLGTALL SLYYNVNGPT WYYPLFSQGA
SGEGDKETFI AAASFYQLPF YQVRTVTGVD GYHRSSGYRG VAMLQHDFRQ DYERYTHSKE
DTEAKYAAGS AAYESSYNVN DFYNTYFGTY NSQEPLDVMF VHSNLPKLEP LSLSTDLMED
GQHIRSYSNL KRLHGYDIEL RSFQTFNEYL CDKRVKFKYY EKTLIDEESW TSMCDYIKGR
LSFLERTHDE ALNKN
//