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Database: UniProt
Entry: J9VMG6_CRYNH
LinkDB: J9VMG6_CRYNH
Original site: J9VMG6_CRYNH 
ID   J9VMG6_CRYNH            Unreviewed;       658 AA.
AC   J9VMG6;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 2.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Mannosyltransferase {ECO:0000256|RuleBase:RU363075};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU363075};
GN   ORFNames=CNAG_02892 {ECO:0000313|EMBL:AFR93799.2};
OS   Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS   CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=235443 {ECO:0000313|EMBL:AFR93799.2, ECO:0000313|Proteomes:UP000010091};
RN   [1] {ECO:0000313|EMBL:AFR93799.2, ECO:0000313|Proteomes:UP000010091}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487
RC   {ECO:0000313|Proteomes:UP000010091};
RX   PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA   Janbon G., Ormerod K.L., Paulet D., Byrnes E.J.III., Yadav V.,
RA   Chatterjee G., Mullapudi N., Hon C.C., Billmyre R.B., Brunel F., Bahn Y.S.,
RA   Chen W., Chen Y., Chow E.W., Coppee J.Y., Floyd-Averette A., Gaillardin C.,
RA   Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S., Hamlin J.L.,
RA   Hsueh Y.P., Ianiri G., Jones S., Kodira C.D., Kozubowski L., Lam W.,
RA   Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K., Proux C.,
RA   Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A., Zeng Q.,
RA   Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA   Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA   Cuomo C.A., Dietrich F.S.;
RT   "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT   grubii reveals complex RNA expression and microevolution leading to
RT   virulence attenuation.";
RL   PLoS Genet. 10:E1004261-E1004261(2014).
CC   -!- FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC       anchor biosynthesis. Transfers the third mannose to Man2-GlcN-acyl-PI
CC       during GPI precursor assembly. {ECO:0000256|ARBA:ARBA00024708}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU363075}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU363075}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 22 family. PIGB
CC       subfamily. {ECO:0000256|ARBA:ARBA00006065}.
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DR   EMBL; CP003822; AFR93799.2; -; Genomic_DNA.
DR   RefSeq; XP_012047859.1; XM_012192469.1.
DR   AlphaFoldDB; J9VMG6; -.
DR   GeneID; 23886442; -.
DR   KEGG; cng:CNAG_02892; -.
DR   VEuPathDB; FungiDB:CNAG_02892; -.
DR   HOGENOM; CLU_012353_2_0_1; -.
DR   OrthoDB; 37262at2759; -.
DR   Proteomes; UP000010091; Chromosome 3.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005599; GPI_mannosylTrfase.
DR   PANTHER; PTHR22760; GLYCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR22760:SF4; GPI MANNOSYLTRANSFERASE 3; 1.
DR   Pfam; PF03901; Glyco_transf_22; 2.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|RuleBase:RU363075};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU363075};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363075};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU363075};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU363075}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..658
FT                   /note="Mannosyltransferase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003829208"
FT   TRANSMEM        255..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        291..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        325..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        398..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        428..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        463..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
SQ   SEQUENCE   658 AA;  73926 MW;  0CC5499F9DADE7E1 CRC64;
     MACLAFLTPL VVRALLTLLL PHTYFQPDEF YQALEPAHYY VFGYGYLSWE WRDLPLAETL
     VSTGTSEFHG KLWNKLVEVA AGGRMRGWAW PGIFVVIYEV LKGLKLDRGL FLTMSPRAVG
     VIVAVLTDYY TYCLSSKLLG HGSAPTALFL SLTSLFNAHL LPRSLSTSPE TLLTLMALYY
     FPFPAPGVPQ VNGLHNVTNL KLIRASKGET GEGEKELIGV KDSDKRFYGV NDLDYVVIDR
     TPPFVVKTPQ HKDKLALSVC LATIALCIRP TMVSLWAFLG VNLLWRRFQT SGLPSLISTT
     ALAISSIFCT VAGSAAIDYL MTGRLYVPLL TFIYQNVIAN ISSFYGSTNH LYHLVQSLPI
     MLFPLWIWWA KGFIACMLPT GLLPAQLNKF DKPEGLRILA KAITFTVAAL SLSPHSEWRF
     LHPLLPPLLL YAIPSFSISY TPTVLGAYYP VRSFRQYLRM DKVPFYVILF SGIVPFIYLN
     VFHGAAQVEV MNVLRRGDLG NVTSLAVLAP CHSTPWMSHL HKDIEGWFLT CEPPVGVDAK
     MHRTQQDWFY SNPVQYLSAV FPYPPSQLHD IPYASFSKTY PSHIILFGEL LSRHGVVSET
     ILEADESQPV MVTTREGDVV GELESLGYQE VWNGWNGFDW AQDEEERKGG VRVWRRLT
//
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