ID B2ABC1_PODAN Unreviewed; 1238 AA.
AC B2ABC1;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE SubName: Full=Glycosyltransferase Family 1 {ECO:0000313|EMBL:CDP23023.1};
DE SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 1, supercontig 1 {ECO:0000313|EMBL:CAP60383.1};
GN ORFNames=PODANS_1_6820 {ECO:0000313|EMBL:CAP60383.1};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP60383.1};
RN [1] {ECO:0000313|EMBL:CAP60383.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC {ECO:0000313|EMBL:CAP60383.1};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|EMBL:CAP60383.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP60383.1};
RA Genoscope - CEA;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
RN [4] {ECO:0000313|EMBL:CDP23023.1}
RP NUCLEOTIDE SEQUENCE.
RA Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CU633438; CAP60383.1; -; Genomic_DNA.
DR EMBL; FO904936; CDP23023.1; -; Genomic_DNA.
DR RefSeq; XP_001912901.1; XM_001912866.1.
DR AlphaFoldDB; B2ABC1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GeneID; 6197507; -.
DR KEGG; pan:PODANSg09950; -.
DR VEuPathDB; FungiDB:PODANS_1_6820; -.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_000537_1_0_1; -.
DR OrthoDB; 76239at2759; -.
DR Proteomes; UP000001197; Chromosome 1.
DR GO; GO:0016906; F:sterol 3-beta-glucosyltransferase activity; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0030259; P:lipid glycosylation; IEA:InterPro.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR010610; EryCIII-like_C.
DR InterPro; IPR004276; GlycoTrans_28_N.
DR InterPro; IPR002213; UDP_glucos_trans.
DR InterPro; IPR003903; UIM_dom.
DR PANTHER; PTHR48050; STEROL 3-BETA-GLUCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR48050:SF13; UDP-GLUCURONOSYLTRANSFERASE; 1.
DR Pfam; PF06722; EryCIII-like_C; 1.
DR Pfam; PF03033; Glyco_transf_28; 1.
DR SMART; SM00726; UIM; 4.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS50330; UIM; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 68..217
FT /note="Glycosyltransferase family 28 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03033"
FT DOMAIN 376..473
FT /note="Erythromycin biosynthesis protein CIII-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF06722"
FT REGION 28..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..47
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1238 AA; 135597 MW; 66EBA09636738B53 CRC64;
MTVEATGRVS IHLLEKNRRL STLLAPAIAK RSKPPPLPPL PSGPLPPPYI PPNLGGLPGQ
TPPPKLNVVI QIVGSRGDVQ PFIALGLVLR DTYGHRVRIA THGTFKKFVE ENGLEFFDIG
GDPAELMAFM VKHPGLMPGF EALRQGEIRR RRKGVEEMLE GCWRSCITQG GEGDRPFVAD
AIIANPPSFA HVHIAEKLGV PVHVMFTMPW TPTRAFPHPL ADIIATNADD VLTNYVSYTL
VEMMTWQGLG DVINRFRTNV LDLESLSLLW APGLISRMRI PTTYCWSPAL IPKPADWGEE
VSVSGFFFLN LESGYEPDPT LKAFLDAGPP PVYIGFGSIV VDDPDALTKT IFDAVKRTGV
RALVSKGWGG IGGDALSLPD NVFMLGNCPH DWLFKKVAAV VHHGGAGTTA AGINAGKPTV
VVPFFGDQIF WGNMIARSGA GPAPIPFKTL TAENLAAAIE KCLEPGTQTK AKELGQKIRA
EKGADVGGKT FHQFLNTDNM RCSLAPSRVA VWRVRRTHVR LSALAAAVLV REGWLKYTDL
KLHRSVEHDT DEQPWDPVSA ATAALVGDFS ALTLAVADFP REVFKGAKEN KKAKEKSSNS
EASSSRSTIV GDRNSVLVDD AASISASTIS PSSSHQRTTS HAADAASISS NSTTPTAFTR
IDTGTGTDTS SKLSPPPTRA SGSSSPTREP FNLDLAVGAG KGAMRILGVG AKVHTNFCLG
VARGFRNAPK LYHDETVRPV EKVTGFSSGV RVAGKEFSLG VYDGVSGLFT QPWKGAQKEG
PVGLVKGFGK GVGGFFLKNS AALWSIPAYF SQGVQVQMRK SYFSKTEVMG YIIASRAKQG
EEDLEFSTEE ERRDILARWR EMRQDGHDLK GLYSRYKDIK NEDRELSGEG NSNNKEEEPK
TGWLRTRGLS IDKRKELHRQ KEEWRRTHQG GAASPMSPGD VTPPERGMSR GSASSSTNNM
LMALDDHEAI EAAIRESVQR TSNGNPEEDA AIEQLVRASV MGMRRQAAER ALAAAEKQAV
DNRGASGQNT PPERPPQFDA GWPVDFKGNY ISDEEFTNIT DEEYQALIEE AVRQSLMEEQ
ADQQGQSYQP YYADEKAALR NLQRKPVPSP RDEAFELPGN SGGTPPQRNS NDRDDEEEQL
RRALEESEKE FRKDKEKLQR QMTEEEIVLE YVKKQSLQEE EFKRATRQSG SREGKGKDVS
ESWEVLNEYS DEDDEDLKRA LEESLRMANK GRDGGPSA
//
