ID A0A2G8S8H9_9APHY Unreviewed; 1585 AA.
AC A0A2G8S8H9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Glycosyltransferase family 24 protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=GSI_07656 {ECO:0000313|EMBL:PIL30079.1};
OS Ganoderma sinense ZZ0214-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Ganoderma.
OX NCBI_TaxID=1077348 {ECO:0000313|EMBL:PIL30079.1, ECO:0000313|Proteomes:UP000230002};
RN [1] {ECO:0000313|EMBL:PIL30079.1, ECO:0000313|Proteomes:UP000230002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZZ0214-1 {ECO:0000313|EMBL:PIL30079.1,
RC ECO:0000313|Proteomes:UP000230002};
RX PubMed=26046933; DOI=10.1038/srep11087;
RA Zhu Y., Xu J., Sun C., Zhou S., Xu H., Nelson D.R., Qian J., Song J.,
RA Luo H., Xiang L., Li Y., Xu Z., Ji A., Wang L., Lu S., Hayward A., Sun W.,
RA Li X., Schwartz D.C., Wang Y., Chen S.;
RT "Chromosome-level genome map provides insights into diverse defense
RT mechanisms in the medicinal fungus Ganoderma sinense.";
RL Sci. Rep. 5:11087-11087(2015).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family.
CC {ECO:0000256|ARBA:ARBA00006351}.
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:PIL30079.1}.
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DR EMBL; AYKW01000016; PIL30079.1; -; Genomic_DNA.
DR STRING; 1077348.A0A2G8S8H9; -.
DR OrthoDB; 1734at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000230002; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003980; F:UDP-glucose:glycoprotein glucosyltransferase activity; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR CDD; cd06432; GT8_HUGT1_C_like; 1.
DR InterPro; IPR040497; Glyco_transf_24.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR009448; UDP-g_GGtrans.
DR InterPro; IPR040693; UGGT_TRXL_1.
DR InterPro; IPR040694; UGGT_TRXL_2.
DR InterPro; IPR040692; UGGT_TRXL_3.
DR InterPro; IPR040525; UGGT_TRXL_4.
DR PANTHER; PTHR11226; UDP-GLUCOSE GLYCOPROTEIN:GLUCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11226:SF0; UDP-GLUCOSE:GLYCOPROTEIN GLUCOSYLTRANSFERASE; 1.
DR Pfam; PF18404; Glyco_transf_24; 1.
DR Pfam; PF18400; Thioredoxin_12; 1.
DR Pfam; PF18401; Thioredoxin_13; 1.
DR Pfam; PF18402; Thioredoxin_14; 1.
DR Pfam; PF18403; Thioredoxin_15; 1.
DR Pfam; PF06427; UDP-g_GGTase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000230002};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1585
FT /note="Glycosyltransferase family 24 protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013701454"
FT DOMAIN 33..247
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 315..447
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 456..718
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 753..960
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1293..1558
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 275..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1563..1585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1585 AA; 176478 MW; 562C53C55452B1E6 CRC64;
MLGALIPLLA WPILCASAGK PPVNVELRTS WQATPILLES LESVAIEEPS SFFHLLDGVT
DPSVFPLSKD KSTPKHAHKH VFDIALAMDH LAAPGAYVAA EMHVALHSAS PKLEAFYQYY
NDHHAARKRA FGKRGEECES WVDWYGSIVC DAKTLARLVE METLDPAEGD TKATCSTAPP
APKLLPFDHV LSDPARLLDL PPKTAVLYGT LDSPNFRELH SYLYAAARAP SPHLTYVFRP
IPPPPSASSE RTYLSGYGVA LDLKKMDYLA VDDRLQSGSG GSHEEDSGTA VQDDEEVDPI
VTLLQQYPID ESVDVALPLT EEELHEIDFQ AAQLIYDAED KHKLRTLKHL AQNFPRYAGA
LARRVAVFPA LLAELAENQP RARGGVTMAW LNGVALDERD MTPSALLRLV RRERGVMAGL
MGGRLGMSSK EGIEVLTHRA VARAQSEGGG PMDGLFDASD RAEGGGVVGY FNDFEKDERY
DRWGRNLKII LRQMYPGQFP TLKLNLFNVV LAVDLSQLSS VDFIATTVQM LISRGLPFRW
GVAPIVETED GSRMARLFYF LMENFGGDET LAFFLNISQR DEPMESLKPT VDWALVRSAF
KSLLERKAED LAEDLGLETD LDKILEGTAG DLEKQRAYAL RLGTSLASAP QGHAFFNGKH
FDLDDDFLRY LQTESAEHLQ HVQLKVYKGE LTDEEHADGM ATYFYDLPTT AKRRNAYVHP
SAKAGAGDLR IFGLPDLIEA NGLKSSPGAF VYPAESQQVP LTTYVVADFD SEEGAKFLKE
ALASVTPDSL SRLSFIHNLA SSSTRGKSDA LESPSRSIAQ LIVSDTLSKV APERLLEALQ
PKELEESTGE GKQAPFSLSL DELADAEGRV LTAVEHEQYL NACRLVLRQL ELKPGEHAVI
VNGRVVGPIK PGEFVAGDFE TLAAYEHHRR VQPVVDALLE VHGASAEATR EDFAELVSVA
SSIVSSIQQP DPSEAGLFNA PQRPRLRNYQ RLSSTYTGFS IGDNSTAIYH FGLLLDPLSE
VAQKYTALFE WLQEMPGVYI EFHINPTRFE ELPLKRFYRY NIAPRLTFDD NGNEIHATTQ
FTQLPVEPIY TLAMDAPQSW LIRPKEALYD LDNIQLSKLS GKDRVSGLKA IFDLDYLVVE
GHARESVSSA PPRGLQMQLV TSDSTPIADT LVMANLGYLQ FKTKPGVYKL EIRPGRGREI
FEMESVGNEG WNSPTVGEAG DEVTVTSFEG VTLYPRLATL PGKEGEDVLL ATGAHAEEAS
VVENLMAKVT SLFGSKHKGE TAVVPVGDGQ AEINIFTVAS GHLYERFASI MILSVLRHTK
SSVKFWFIEN FLSPDFLEFL PHFASEYGFQ YELITYKWPS WLRAQTEKQR IIWAYKILFL
DVLFPMDLKK VIFVDADQIV RTDLKELVEL DLHGAPYGYT PMGDDNPDTE GFRFWKTGYW
KDFLRGLPYH ISALYVIDLV RFREIAAGDM LRGHYQQLSA DPNSLANLDQ DLPNNLQREV
PIFSLPEDWL WCETWCSKDR LHRAKTIDLC QNPLTKEPKL DRARQIPEWE VYDGEIAAFA
RRLQSNQTSG SEDESAANPV KHVEL
//
