ID A0A316YPE5_9BASI Unreviewed; 1669 AA.
AC A0A316YPE5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Glycosyltransferase family 24 protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=FA10DRAFT_302202 {ECO:0000313|EMBL:PWN91022.1};
OS Acaromyces ingoldii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Cryptobasidiaceae; Acaromyces.
OX NCBI_TaxID=215250 {ECO:0000313|EMBL:PWN91022.1, ECO:0000313|Proteomes:UP000245768};
RN [1] {ECO:0000313|EMBL:PWN91022.1, ECO:0000313|Proteomes:UP000245768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4198 {ECO:0000313|EMBL:PWN91022.1,
RC ECO:0000313|Proteomes:UP000245768};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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; KZ819636; PWN91022.1; -; Genomic_DNA.
DR STRING; 215250.A0A316YPE5; -.
DR InParanoid; A0A316YPE5; -.
DR OrthoDB; 1734at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000245768; 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:UP000245768};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1669
FT /note="Glycosyltransferase family 24 protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016440792"
FT DOMAIN 49..270
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 365..494
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 506..769
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 821..1002
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1379..1645
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 310..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1269..1295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1669 AA; 182417 MW; 4666B163216E6D58 CRC64;
MFALTSVLLL LLRPLLPLLL LLLASAAGEA RAQEASPPVH VSLRSGWPAS PFVVELLEAA
HQEAPSSFFD IVAIVAGPWF FNDTDDGTHD LASATPQQVF KGAKRAFDRY GVLPGEATRR
RWEAALALRA QSSKVAAFTH LYRTSGLEQR WEEAMAARDS SDECRSWVDW DGKVLCSRDE
LQRHLDETGS TAVTKSPYPG PVAFDHVLAH PLDETDGEQE QEAATAVLYG DPASSNFFGL
HAALSEYALG ARAEVPFRYI LRWRPPPQSS TGGAATKEEE EERDYLAGFG ASLDVKKVDY
LVIDDRAVAA SGSEDGGGDS NDGDGSTATR RGAATEREAA RAQLDDRRWL DAQLGGPPSD
EAEEEEGGDA GLRAAYIVAK SSEPLRALRQ LSHDFPLHAG ALARSSAARP SRRFLDEMLG
LHQMYLQQAT TDVWLNGRSL SATSDEAGAA SALTLLPLVR DERRLLDSLI ALNLSAEAAV
SLLTYAPLQQ QQQQPQSQQQ VHDAYFDASD RPEGGAVVSW WNDVEADEAY VRFQPELRGL
LRPLYPGSFP TVRRNLFNVV LLMDLRRAET CRFLAESVSL ATKRLALHWG FVPTGLVEPG
DESSQLARLY WLAMERGGST LAAEYLARLA NAMQTHVTVA QARAQLQAVL LAAAHVDGSD
EEEEAAAVEQ AIEAALAPAS EWTEREAKAR RYAKRLGAVV ADKDHRGDVF VNGRHVPFTA
ALIQHVHQLI AAQVQALAPL VYYGTLTDEA DVSTHFYDLN TTFAARSPLA FPPPQASNIS
ADAVDLTQVA AQLDDSTLLR RFFLPRQATT ATTATTTPID TTLWLVGDLD SDEGTSLLRE
TIKAQQALPQ AFRLGLVHAA PSQSSLGTVS RAIYDQLQRD DGAASEALLE VLNSSVSRGD
DNKNEEPARR FWRGQARLAR LFGVAKSKSP FAIVINGRIV AGFDAAKVES IDVESLVAVE
RQRRIAPLVE GLQTPAIAQH DAALAELARD ADAITTLTSI IARAGFVDAA SEGLFARAST
ARSTAIDDVP TTNGLTSFEL GADRAHARLR LTLMVDPLSK EAQRWADLVE HVLQLDDAIW
VRVLLNPAGA SRAGAATDEA EAAEAATTLR RFYRASSPAR LAFDGDGQLR RPRASFYGMP
ADAVLTMAIE APPAWVTMAS VAVHDLDNIR LSDVARASAG TRAVVAATFD VKHVLIEGHA
RDTAARSVPR GLELVLETLD GSLVDDTIVM ANLAYLQLRA PSPGLYTLRI RGAGSKSAEL
YEMESVGSAG WNSPPVGGGG GGGGESSSSD DVVTVDSPAG LTIYPRVRKR KGREHDRLVF
DSEGEGEEAH AMGAGRSPAA AQGLVPFAWS LVADAARRIQ TSFSAATATA TSRRKAETIN
VFTVASGHLY ERMASLMILS VLRHTQTPCK FWFIENFLSP SFKDFVPHLA REYGFEYEMV
TYAWPHWLRA QSEKQRQIWG YKVLFLDVLF PLDVSRIIFV DADQIVRADL LELVQLDMGG
KPYGFPPMGN DSYDMDNYRF WETGYWKKFL RGLPYPISAL YVVDLDRFRL LAAGDRLRGH
YQALSADKGS LSNLDQDLVA SLIHQVPIYG LAREWLWCET WCSWDWQAQA KSIDLCSNPK
TKEPKLDRAR RQIPEWTAYD DEVARFAERV RAQQATQKTT QGTVQHDEL
//
