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Database: UniProt
Entry: S7QF63_GLOTA
LinkDB: S7QF63_GLOTA
Original site: S7QF63_GLOTA 
ID   S7QF63_GLOTA            Unreviewed;       541 AA.
AC   S7QF63;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, 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=GLOTRDRAFT_114546 {ECO:0000313|EMBL:EPQ57997.1};
OS   Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS   rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX   NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ57997.1, ECO:0000313|Proteomes:UP000030669};
RN   [1] {ECO:0000313|EMBL:EPQ57997.1, ECO:0000313|Proteomes:UP000030669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ57997.1,
RC   ECO:0000313|Proteomes:UP000030669};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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; KB469298; EPQ57997.1; -; Genomic_DNA.
DR   RefSeq; XP_007863296.1; XM_007865105.1.
DR   AlphaFoldDB; S7QF63; -.
DR   STRING; 670483.S7QF63; -.
DR   GeneID; 19299900; -.
DR   KEGG; gtr:GLOTRDRAFT_114546; -.
DR   eggNOG; KOG1771; Eukaryota.
DR   HOGENOM; CLU_012353_0_1_1; -.
DR   OMA; HEWPDYL; -.
DR   OrthoDB; 37262at2759; -.
DR   Proteomes; UP000030669; 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:UP000030669};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EPQ57997.1};
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..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..541
FT                   /note="Mannosyltransferase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004556282"
FT   TRANSMEM        171..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        204..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        262..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        347..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
SQ   SEQUENCE   541 AA;  61636 MW;  3B1B4408FACD79E0 CRC64;
     MARCMRTCAL VAILLRVFIA LSTRTFFQPD EYFQALEVAH QLVFGYGHLT WEWRASRPIR
     SIIYPLLNAP VYWLAKIARL DDTVFLIAGP KVLHGVLGAC TDIWVAELAQ KVLGERYVTT
     AVFLSLTSFF HALSLTRSMS NSLETSLATI ALSYFPWDPE RLFDRRGIRK AFVFAALACS
     IRATNAVIWV YMLAVLIWRL RTQIWLVLIV VLDVVGIGLV ILDSIYYGQV TFTPLNFLLT
     NLSSVSLFYG SSDWHYYLSQ GLPLLCTTSL PFVLHGAWLA LGPTGTPASR TMLGLVTWTL
     TIYSLAGHKE WRFLHPLLPL LHILASKSLV DLYYASERTA PLQRPLLPIR FTHLCMLLIT
     VPAAIYVLYF HGEPQISVMH YLRNVPPGEL ESLGFLMPCH STPWQAYLHK SELADPGRMW
     ALGCEPPLSN DKDVTSSYRD QTDIFYQSPT GYLKERFPYR VDPTFPPSPF PSSIPGVTRL
     DDKSWRHEWP KYLVMFGALS EESEVRTLLL DRGYREVWAR NTGWEGDSRR RGGVRVWKFK
     G
//
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