ID A0A2B7ZSE6_9EURO Unreviewed; 1935 AA.
AC A0A2B7ZSE6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=UDP-glucose:glycoprotein glucosyltransferase {ECO:0000313|EMBL:PGH36109.1};
GN ORFNames=GX50_01121 {ECO:0000313|EMBL:PGH36109.1};
OS Emmonsia crescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=73230 {ECO:0000313|EMBL:PGH36109.1, ECO:0000313|Proteomes:UP000226031};
RN [1] {ECO:0000313|EMBL:PGH36109.1, ECO:0000313|Proteomes:UP000226031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH4076 {ECO:0000313|EMBL:PGH36109.1,
RC ECO:0000313|Proteomes:UP000226031};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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 acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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:PGH36109.1}.
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DR EMBL; PDND01000012; PGH36109.1; -; Genomic_DNA.
DR STRING; 73230.A0A2B7ZSE6; -.
DR VEuPathDB; FungiDB:EMCG_04539; -.
DR VEuPathDB; FungiDB:EMCG_04540; -.
DR OrthoDB; 1734at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000226031; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
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 Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
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; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 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; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000226031};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PGH36109.1}.
FT DOMAIN 29..152
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 244..400
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 481..666
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 721..850
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 856..1099
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 1112..1313
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1631..1897
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 702..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1902..1935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1935 AA; 216346 MW; 4992336980C1F720 CRC64;
MDPGKQFGSA LPWAEPAWYS GRPSPYYNES HFKLRDAVRK WTEENVLDKT DEWRAAGQVP
DEVYQKCARD GLLLPIAFGK SIPEEFAHYP IIGGIKASEW NGFHDLVLWD ELYRGGAISS
IFVGLTVGAP PIRQFASPWL QKKILPEILS GQKRICLAVT EPSCGSDVRN LTTKAEKSAC
GKFYITAVRT GGPGAEGISF LLVPRSEGIR TRKIEIGADG LSATTYVIFE DVKVPIEYLV
GSEGQGFRYV MSNFNHERLW IAFQTLRNAR TCLQDAMAWA MKREAFGIKL IDQPVVRHKF
GSMAKEVEAL QAWTEQIVYE LDHLSYQDGN RQLGGVTALL KVKGGQMNKF VADNCVQIMG
GLGLTKTGQG SRIEAISRGT HSLIVPGGSE DVLIDLSVRE ALKVAAIKKI WLRDIKNYHI
STVPTIFTVA ERWPDRSQNG KIINILHNIA HMAYDNKRSN LYGRRYMPPS VNVALSASFN
AAPYLVELLE TAAEENSTSY FPLLDRIAEG TFAEITTERD LYERFTQLLQ DDGHLANPES
ISSFKFALSI RSTAPRIEAH YQYYNTSVES SLMVAQDAVC TVWAHYDGDQ YCSPSLEYAQ
QSVSGDQHDR VLPFDRVLGD SSLPPLVLYA DVASPLFGGF HQELIQKARD GQFSYRIRYR
PSGPETSRPL FVNGYGVELA LKRTDYIVID DRDAEQRVLK DTDAAKPTLT PVEDLEEEPP
ADLKPLSASE VSTLGMNAAS FVMSSDDPFA TLLRLTQDFP RHSSAIASRN ATPEFTKEFE
ENRAALLPVG YNLMWINGVQ MDPRAIDAFS LLDHFRRERK LINGLRDFGL SARQAVDLLS
DPAIAKIQAA DDSPRYDYRD ELEGGGVIIW LNDLEKDHRY DGWPSDLRSL LKPTYHGQLP
TVRRDIHNAV IPVDLTSPVD VGIVVESLQM LVRRKVPVRF GIVPLVHNQN ALEQAKVVHH
LFDTYGIGAS IAYLRASLST EKVASPDQAS FTAALENRIV REDRTPLAFE NVLKSENYDP
ILSGTKSYLK RLAVEGEATP FFVNGVSFIR DGGFLQYIVA TVSKDLEDIQ RRVYERTLEE
DIWVPSHFLQ GALQSRNPLL IPEDPSKIRT VDLNEIYAKH NDIFDTILRI PATAESDHPL
LDWSSIILIA DLNSDAGAKQ LGYLLELHEK HPGVEVLLLH NGDGSSTSKD LSTRLYSARN
GRDLDPAVAI AALASGIDEP ASDSAGASAY WNTVQSLVKE IGIGNNENGM VVNSRMLGPV
PSATVFDAQD LEQLRTYEHS KGIGVFARKA FELGLESKIP DPLSLAKLQA LISLSAASDI
PEAIYDSGPR LRTNQFEKWS STHSAISVSN SDDPSIYIVA TIDPTTEIAQ RWVPILKVLS
ELSGVSLKLF LNPREQIKEL PIKRFYRHVL EAAPSFNEDG SIAKPQAIFH GIPREALLNL
GMDVPHAWLV APKESIHDLD NLKLSSLKEG TNVDAIYELE HILIEGHSQD VTLNAPPKGV
QLLLGTEKNP HFADTIIMAN LGYFQFKAQP GCWKITLKPG QSERIFHLDS VGGQGYAPTP
GDENNDVALL SFQGKTLFPR LSRRPGHETD DVLDAGHKPA SAKDYLSKGL NFASNVLHSL
TGPAKETHAD INIFSVASGH LYERMLNIMM VSVMKHTKHS VKFWFIEQFL SPSFKSFLPH
LAAEYGFSYE MVTYKWPHWL RAQTEKQRII WGYKILFLDV LFPLSLDKVI FVDADQIVRT
DMYELVTLDL EGAPYGFTPM CDSRTSMEGF RFWKQGYWEK FLRGLPYHIS ALYVVDLNRF
RAIAAGDRLR GQYHSLSADP GSLSNLDQDL PNNMQRVLPI KSLPQDWLWC ETWCSDEALE
TAKTIDLCNN PLTKEPKLER ARRQVPEWTV YDEEIAAVQR RVLEEEGNIK AEDEEGDDGR
GKGKGNKKEL RKDEL
//
