ID A0A179U6Y3_BLAGS Unreviewed; 1505 AA.
AC A0A179U6Y3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=UGGG2_UDP-glucose:glycoprotein glucosyltransferase 2 {ECO:0000313|EMBL:OAT03766.1};
GN ORFNames=BDBG_00453 {ECO:0000313|EMBL:OAT03766.1};
OS Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=559298 {ECO:0000313|EMBL:OAT03766.1, ECO:0000313|Proteomes:UP000002038};
RN [1] {ECO:0000313|Proteomes:UP000002038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SLH14081 {ECO:0000313|Proteomes:UP000002038};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(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}.
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DR EMBL; GG657448; OAT03766.1; -; Genomic_DNA.
DR RefSeq; XP_002629207.1; XM_002629161.1.
DR STRING; 559298.A0A179U6Y3; -.
DR GeneID; 8508041; -.
DR KEGG; bgh:BDBG_00453; -.
DR VEuPathDB; FungiDB:BDBG_00453; -.
DR OrthoDB; 1734at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002038; 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:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0043934; P:sporulation; IEA:UniProt.
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:UP000002038};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 44..226
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 284..412
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 419..662
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 675..874
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1194..1460
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 261..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1467..1505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1483..1505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1505 AA; 167945 MW; 58E9880F93B366B3 CRC64;
MTFRYHPFPW RLGGLALFGA SLLFTSNAIA GPSVNVALTT SFNAAPYLVE LLETAAEENS
TCYFPLLDRI AEGTFAEITT DQGLYERFTQ LLQEDGHLTH PEAISLFKFA LSLRSTAPRI
EAHYQYYNTS VEPSLMAAQD AVCTVWAHYD GDQYCSPSLE YAQQSVSGDQ HDRILPFDRV
LGDSSLPPLI LYADITSPLF GGFHQELIEK ARDGQFSYRI RYRPSGSEVP RPLFVNGYGV
ELALKRTDYI VIDDRDAKQR VLQDNDAEKP TLAPAEDLEE EPPADLKPLS ASEVSTLGMN
AASFVMSSDD PFATLLRLSQ DFPTHSATIA SGKASSKFTK ELKQNRAALL PEGHNVMWVN
GLQIDPRTID AFSLLNHFRR EGKLINGFRK FGLSGQQGVN LLSNPVLAKS HAAGDPLRYD
YRDEFEGGGV IIWLNDLEKD HRYNGWPSDL KSLLRITLQG QLPPVRRDIH NVVIPVDLTS
PEDVRIVAET LLILVKRMVP IRFGIVPLVH NKNTLGQAKI AHHLLDAYGI GALISYLQAS
LSADKVASPD RASFTSALEN RKLREDRTPL AFEDALESDN YDPILSNTKS YLERLAVKGE
VLPFFVNGVA FMRDESFLQY MLASLSKDLE DIQRRVYEGT IDEDVWVPSH FLQGALQGRN
PLLIPENPTE ILTVDLDEMY MNHKDIFDTT LRIPAAAESE HPLLDWSSII LVADLDSDAG
AKQLTYLLEL HKKHPGVEIL LLHNGESSST SQALSTRLYS IRNGRDLDPT VITAALGSEN
EEPSDSAAAS AYWKTVQPLV KEIGFGTSEI GMVVNSRVIG PMPSSTTLDI QDLEQLHMYE
QSKRVGVLSR AAFELGLEAN ISDPLGLARL QALASLSATS NVPEGIYGSG QTARTDIFEK
WNGVHSAISV SNSDDPSIHI VAAIDPTTEI AQRWVPILKV LSELNGVSLK LFLNPREEIK
ELPIKRFYRQ VLESAPSFNA DGSIAKPQAI FRGIPGEALL NLGMDVPPSW LVAPKESIHD
LDNLKLSTLK EGTNVDVIYE LEHILIEGHS RDVTRGVPPK GVQLLLGTEK NPHFADTIVM
ANLGYFQFKA RPGCWKITLK PGQSERIFRI DSVGGHGYIP TPGDENNDVA LLSFQGKTLF
PRLSRKPGHE RDDVLDADHK PASAAKHFLS KGLNFASNIL HSITGPAQET HADINIFSVA
SGHLYERMLN IMMVSVMKHT KHSVKFWFIE QFLSPSFKSF LPHLAAEYGF SYEMVTYKWP
HWLRAQTEKQ RIIWGYKILF LDVLFPLSLD KVIFVDADQI VRADMYELVT LDLEGAPYGF
TPMCDSRTSM EGFRFWKQGY WEKFLRGLPY HISALYVVDL NRFRAIAAGD KLRGQYHTLS
ADPASLSNLD QDLPNNMQQV LPIKSLPQDW LWCETWCSDE SLATAKTIDL CNNPLTKEPK
LERARRQVPE WTVYDEEIAA VQRRVLEEER EAKGGTKGGD QNVPRDDGGD DGKGKSEKGT
RKDEL
//
