ID F4RHJ0_MELLP Unreviewed; 1483 AA.
AC F4RHJ0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Family 24 glycosyltransferase {ECO:0000313|EMBL:EGG08350.1};
DE Flags: Fragment;
GN ORFNames=MELLADRAFT_22334 {ECO:0000313|EMBL:EGG08350.1};
OS Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf
OS rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX NCBI_TaxID=747676 {ECO:0000313|Proteomes:UP000001072};
RN [1] {ECO:0000313|Proteomes:UP000001072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072};
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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; GL883101; EGG08350.1; -; Genomic_DNA.
DR RefSeq; XP_007408548.1; XM_007408486.1.
DR STRING; 747676.F4RHJ0; -.
DR EnsemblFungi; EGG08350; EGG08350; MELLADRAFT_22334.
DR GeneID; 18926889; -.
DR KEGG; mlr:MELLADRAFT_22334; -.
DR VEuPathDB; FungiDB:MELLADRAFT_22334; -.
DR eggNOG; KOG1879; Eukaryota.
DR HOGENOM; CLU_002668_1_0_1; -.
DR InParanoid; F4RHJ0; -.
DR OrthoDB; 1734at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001072; 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; 2.
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:UP000001072};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGG08350.1}.
FT DOMAIN 14..102
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 103..172
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 233..367
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 389..634
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 730..877
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1218..1482
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 199..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGG08350.1"
FT NON_TER 1483
FT /evidence="ECO:0000313|EMBL:EGG08350.1"
SQ SEQUENCE 1483 AA; 166364 MW; CCD2004E04F7B154 CRC64;
SPPISVSIQA TWPEPPLLIQ IIESAAIERS DSFFPILTAV SKHWRTIDSL SLTPQQIYNQ
TLNQITLNGL LNDQGEIESL ETSIALKEAS PKIEAFRAWY RDRPAPRILS FDHICPPGSH
IPPPSVPVVI LYASNDPRSF GPFHDVLHQA SSSSPIRATY IFRWQVSSDD SQSSSIGPSH
LSGWATRLDI KKSDYLTVDD RPVETNSRES RDSESESTKE NTKEDAPETS TVIIPLQADE
FSTIGLKATQ HILTSPNPLS ALRVLSEDFP RHAYNLVKNW VPGEINADLD RELKENAAEG
VVKPGQSAIW INGLDISSVL PVANINFFKL IQLMRDERRW IKSLTSLGLS VSEIRKLVTD
EQLNSALSGE GGARSDDLEI DPSILGERFD ASDRLEHGEM ILWLNDLEKD TRYAAWPKSL
RDFLRPTYPG QLHAVARNTI TVVLALNVTH TANLRILTES VETFITRSVP IRWGLVPLDD
PNASGSSEAL KGIFPIYSSG TSTGSTSSDM VDALDFKQRA DAYRAAHPES DSDDQKDTAS
FGEGDFNSWS EKTQSYIRRL ALCSGSGEVP GCMFVNGKFF VLDDDFRMNL QQTAMLHIQF
LQHQIYYGLI QGSVDVSHYL YDLPGVYPAR NEFVFPSPGR PVRVVNLVQA FVAAKLGSCA
VEADHETNEP PISAIWVIGN LDSKSGAASV LALLELMVNT DMCFPLLEQC GDMLHLTFTL
QAFPSDQTRG SVFVGFVHAS SQQTDAHIDP RLSDSLGQLI HSPEHPGILI KNVTDQFAHF
GLQPSKPFPE SFSLSKMPSE WRRSTEDGED VWAGAQSLIT ELDITEGHVA VVINGRVLDV
PHSQVLQASD LRMLIDYEIQ KRTNPLQVAL RSVLGPERFT TIKSMVPYIA SVISSVLVSS
DDEAGSKTRG RAVSNALTER KHSSISYGDH DAAVIQFRVI LNPASELAQS WSALLETLSG
RKDVAIKVWF NPMQHVEELP IKRFLRTSFH SRIQFDQDGS SVSPSVVFKH MPTDVLLTLS
IEAPPAWLAL PLESVHDLDN IMLSKIGSTE RERGVEGVFQ LEHIIIAGHA SELPSEVPPR
GLQVVLTNLL TSASVDTIIM ANLGYFQFKA EPGMFVMKIR PGRSSELYTL ERVDLKTGKD
RLSTDKNKTD EDHQFSLTTF DGLLLFPRFR KRPGKEKEKL IQPVAAMSES EDAHTSTTQK
LIGHKPSDVI PGKKRNVINV FTVASGLLYE RMAYLMCVSV MRHTKSDVKF WFISNFLSPS
FKRFIPHLAR KYEFEYELVT YRWPPWLRAQ KEKQRVIWGY KILFLDVLFP LELDRVIFVD
SDQIVRTDLQ ELVDLDLRGA PYAYTPMCND REETKGFRFW DTGYWKDSLR GRPYHISALY
VVDLRVFRAV AAGDQLRQHY QALSADPNSL ANLDQDLPNN MQEVLPIYSL DQKWLWCETW
CSDDGLKTAK TIDLCNNPLT HEPKLTRARR LIPEWDVYDK EVA
//
