ID   A0A2U9R050_PICKU        Unreviewed;       585 AA.
AC   A0A2U9R050;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Alpha-1,2-mannosyltransferase MNN2 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=C5L36_0A12490 {ECO:0000313|EMBL:AWU74673.1};
OS   Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Pichia.
OX   NCBI_TaxID=4909 {ECO:0000313|EMBL:AWU74673.1, ECO:0000313|Proteomes:UP000249293};
RN   [1] {ECO:0000313|EMBL:AWU74673.1, ECO:0000313|Proteomes:UP000249293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS573 {ECO:0000313|EMBL:AWU74673.1,
RC   ECO:0000313|Proteomes:UP000249293};
RA   Douglass A.P., Offei B., Braun-Galleani S., Coughlan A.Y., Martos A.,
RA   Ortiz-Merino R.A., Byrne K.P., Wolfe K.H.;
RT   "Population genomics shows no distinction between pathogenic Candida krusei
RT   and environmental Pichia kudriavzevii: One species, four names.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SIMILARITY: Belongs to the MNN1/MNT family.
CC       {ECO:0000256|ARBA:ARBA00009105}.
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; CP028773; AWU74673.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U9R050; -.
DR   STRING; 4909.A0A2U9R050; -.
DR   VEuPathDB; FungiDB:C5L36_0A12490; -.
DR   OrthoDB; 1985716at2759; -.
DR   Proteomes; UP000249293; Chromosome 1.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:InterPro.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249293};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   585 AA;  67646 MW;  B8650B1BA86BF121 CRC64;
     MLFLRKSVVV KISVFGIISL LLLALFSYHT EKIQTSYGTI KESVTNLKPK IGSMKENIGS
     YVSNDKAYND AVESELTHEL DEENGNLLED NGDEVIKYIN TLALEDDKLV RRSQYFHKIF
     KLISKFKPIL EPLDTYLSDK ISVQSVDGFD EPAFTKEQLE KYLVVNRKDV DDLQENLNFY
     ISNMTEIGEY PENIYEKGTN GIVYVGGEKY SWLTLMSIMN IREVGSELPI EVLIPNREEY
     EFGFCKDILP KYNAKCIYLP KLVGLNVFNE YHFKGYQFKS LAIALSSFEN ILLLDADNSP
     LVNPDYLFTS KVFQDNGLVL WPDFWKRTTH PAFYEIAGFD IDLTRRRDFG YKEYGEHVKK
     LCKDDEVLFH QLEGTLPDPS TESGQVLFSK SKHFKTILLS LYLNSYGPDY YYPLLSQGAG
     GEGDKETFIA AAHILEEHYY TVKKHVIALG RFRDGEFKGS AMGQFNAVED YDIFERYQGS
     NEEVDEEPGL LFVHANFPKL DPWELYQNDV IIDKSKNERN RLFGVEFIDR VGYDFELKTW
     ENMKQLLCDE TLEFATFKNH DVTTKQVCDE VLLQLEYLRS TSKNV
//