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Database: UniProt
Entry: A0A0A2L2B5_PENEN
LinkDB: A0A0A2L2B5_PENEN
Original site: A0A0A2L2B5_PENEN 
ID   A0A0A2L2B5_PENEN        Unreviewed;       496 AA.
AC   A0A0A2L2B5;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Alpha-mannosyltransferase {ECO:0000313|EMBL:KGO56565.1};
GN   ORFNames=PEX2_097230 {ECO:0000313|EMBL:KGO56565.1};
OS   Penicillium expansum (Blue mold rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO56565.1, ECO:0000313|Proteomes:UP000030143};
RN   [1] {ECO:0000313|EMBL:KGO56565.1, ECO:0000313|Proteomes:UP000030143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-8 {ECO:0000313|EMBL:KGO56565.1,
RC   ECO:0000313|Proteomes:UP000030143};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
CC   -!- SIMILARITY: Belongs to the MNN1/MNT family.
CC       {ECO:0000256|ARBA:ARBA00009105}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGO56565.1}.
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DR   EMBL; JQFZ01000166; KGO56565.1; -; Genomic_DNA.
DR   RefSeq; XP_016598292.1; XM_016746993.1.
DR   AlphaFoldDB; A0A0A2L2B5; -.
DR   STRING; 27334.A0A0A2L2B5; -.
DR   GeneID; 27682413; -.
DR   HOGENOM; CLU_013298_0_1_1; -.
DR   OrthoDB; 1985716at2759; -.
DR   Proteomes; UP000030143; Unassembled WGS sequence.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR   GO; GO:0043934; P:sporulation; IEA:UniProt.
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; 2.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000313|EMBL:KGO56565.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW   Transferase {ECO:0000313|EMBL:KGO56565.1}.
FT   REGION          69..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   496 AA;  55703 MW;  B294CF138007DF39 CRC64;
     MSAFRPGRAK ALVLAMLAVI LVCTVYFYRS PITASSTVPL VPNTAFEVPL TERQKDFWKV
     LRPIIERHKP SCPSPEKRGD VAAQHFDPTK EAPRPDLTGL SEEDVRKMEE AHAAFIEDIK
     KSDKELKPIH TPGKRGLVST AGSTYLPVFV SSLRMLRRAG STLPVELYMK DATEHEKHVC
     NEVLPKLDAR CLVLADVVGK NIIEHYQLKI FAVLFSSFEE IVWMDADCFP LGKPEDLLDS
     EPFKTNGLVT WPDFWASSAS PLYYRISRQQ APSMAARQSS ETGAFLVSKK THSLALLLAA
     YYNFYGPSHY FRLLSQGGPG EGDKETFIQA ASAVGAPFYT VSERVQAIGH ANADGLSGSA
     MAQSDPREDF ALIQQDKWRI KDESVAPAPH IFFIHANYPK FNPGDRIFGM GWETTPTLKE
     DGSDGRAWTA PPDTIRRFGY DVEKAYWEEI KWVSCTLETA FKTWENKVDL CKRVEEYWGH
     VFAEPHDDDP KFTLDG
//
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