ID A0A165KDF1_EXIGL Unreviewed; 555 AA.
AC A0A165KDF1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Mannosyltransferase {ECO:0000256|RuleBase:RU363075};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU363075};
GN ORFNames=EXIGLDRAFT_833800 {ECO:0000313|EMBL:KZV96167.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV96167.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV96167.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV96167.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV425946; KZV96167.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165KDF1; -.
DR STRING; 1314781.A0A165KDF1; -.
DR InParanoid; A0A165KDF1; -.
DR OrthoDB; 37262at2759; -.
DR Proteomes; UP000077266; 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:UP000077266};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KZV96167.1};
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..555
FT /note="Mannosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007860748"
FT TRANSMEM 78..100
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 177..203
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 215..238
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 265..288
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 300..318
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
SQ SEQUENCE 555 AA; 63817 MW; ACDE59C7F60F67B8 CRC64;
MGRRWTSVAL RVFLAVLTRT FFQPDEFFQA LEVAHHAVFG YGHLTWEWLA QVPIRSPSFP
MIYAPIYWLL KITRLDNTFL LVLLPKVLTG CLASITDVAV YDLANLVLGP RYADVAIFLS
WTSFFHSLSL VRSLSNSVET SLTTLALCHW LKYSDSASQV LQDEDIALRS SELVTALLYA
GLATMFRPTN AVVWIFMLGC LIWQIRSRYS LFARTMVVTV WFGNLVGGIL FCVDSMYYGK
VTISPLNFLI TNLSSVSSFY GSNPWHYYLT QALPILCTTS LPFVLHGFYT SWRSPAHPHL
RTLAMLVLWT TAVYSMTAHK EWRFIHPLLP ILHVFAAKSL VDLYTQHVKD DNRPDEGRSL
AVRQRHRTLL LLSVPASLYV MLLHGRAQVS VVTHLRKRAD VRSVGFLMPC HSTPWQSHLH
RQDLEGHMWA LGCEPPLRGE DITTYRDQTR VFFDAPAAYL RDRFPRRVNT TFPPAPRATT
PPGQAPIVWQ HTWPSHLVFF GALLDEDGVE ALLTEKGYRP TRRFRNGWEE DEKRRGDVRL
WEWNELEFQK RFVNA
//
