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Database: UniProt
Entry: H6QP65_PUCGT
LinkDB: H6QP65_PUCGT
Original site: H6QP65_PUCGT 
ID   H6QP65_PUCGT            Unreviewed;       479 AA.
AC   H6QP65;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Mannosyltransferase {ECO:0000256|RuleBase:RU363075};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU363075};
GN   ORFNames=PGTG_01857 {ECO:0000313|EMBL:EHS63195.1};
OS   Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS   (Black stem rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=418459 {ECO:0000313|EMBL:EHS63195.1, ECO:0000313|Proteomes:UP000008783};
RN   [1] {ECO:0000313|Proteomes:UP000008783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRL 75-36-700-3 / race SCCL
RC   {ECO:0000313|Proteomes:UP000008783};
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA   Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA   Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA   Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA   Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA   Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA   Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA   Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU363075}.
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DR   EMBL; DS178263; EHS63195.1; -; Genomic_DNA.
DR   RefSeq; XP_003890750.1; XM_003890701.1.
DR   AlphaFoldDB; H6QP65; -.
DR   EnsemblFungi; EHS63195; EHS63195; PGTG_01857.
DR   GeneID; 10542638; -.
DR   VEuPathDB; FungiDB:PGTG_01857; -.
DR   OrthoDB; 37262at2759; -.
DR   Proteomes; UP000008783; Unassembled WGS sequence.
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; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000008783};
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   TRANSMEM        58..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        95..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        145..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   REGION          345..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..362
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   479 AA;  54096 MW;  6F26C5E37600C8DA CRC64;
     MRLLRQLACS LTSLFNAYAG IRTFSNSLET ALTASALAYW PWNPAQISSS WANLSFSILL
     IALSVIIRPS SILFWSLLGY TLLQKSNGET RMDVMAIVAV MGVISALACF LIDSSFYGVA
     TFTPLNFVRQ NLLNDISSFY GVNRLHFYFT QAFTFVNFSM FPTVILGMNM LATPQNDHES
     RGQLDRLRSA RVAVLGTMLG LSVLRHKEFR FIEPLLPLFN CFAARAMVNN YIKDRLARPA
     TSPADVSPLE RILSARPLGF ILRSSISLLA AVYLLGFHYR AQVSVIDYLR EVPDLQLKSV
     GFLTPCHSTP WQSHLHKPHL APNGTQERLW MLNCEPPLVS FQNSSLSEAD STANTTTYQN
     ATESDEDSER KRETIATTKQ MNETREYEDE ASEFYGDPTG FLRARFPGTV DRGYPATDKS
     LQSYQWPSHL VLFEALWNHT SVRELLQTLG YQVVWNQTNG WWHDDPQRRA GSVIVLRSV
//
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