ID A0A0F4GDW8_9PEZI Unreviewed; 444 AA.
AC A0A0F4GDW8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Mannose-1-phosphate guanyltransferase {ECO:0000256|ARBA:ARBA00018601};
DE AltName: Full=GDP-mannose pyrophosphorylase {ECO:0000256|ARBA:ARBA00031190};
DE AltName: Full=GTP-mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00030179};
GN ORFNames=TI39_contig4101g00021 {ECO:0000313|EMBL:KJX95603.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX95603.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJX95603.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJX95603.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in cell wall synthesis where it is required for
CC glycosylation. Involved in cell cycle progression through cell-size
CC checkpoint. {ECO:0000256|ARBA:ARBA00024813}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000256|ARBA:ARBA00007274}.
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:KJX95603.1}.
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DR EMBL; LAFY01004061; KJX95603.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4GDW8; -.
DR STRING; 1047168.A0A0F4GDW8; -.
DR OrthoDB; 5486038at2759; -.
DR Proteomes; UP000033647; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase (GTP) activity; IEA:UniProtKB-EC.
DR GO; GO:0044271; P:cellular nitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd06428; M1P_guanylylT_A_like_N; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR22572:SF104; MANNOSE-1-PHOSPHATE GUANYLTRANSFERASE ALPHA; 1.
DR PANTHER; PTHR22572; SUGAR-1-PHOSPHATE GUANYL TRANSFERASE; 1.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000033647};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KJX95603.1}.
FT DOMAIN 19..212
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT REGION 226..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 49182 MW; 33A7E01E05677983 CRC64;
MATLQIPTRG KTGGGSVTKA VILVGGPSRG TRFRPLSLDL PKPLFEVAGH PIIEHCFAAI
TRVPEIREVF IVGYYDESVF RDFIKDCSRT HPHISIKYLR EYQALGTAGG LYHFRDAILK
GRPDRFFVLN ADVCCSFPLE QMLRLFEEKD AEAIILGTRV SNDAATNFGC IVSDAHTKRV
LHYVEKPESH ISNLINCGVY LFSTESIFPS IKSAIKRRAD RPRLLSYPSS DNLDAQYTPA
TGDDDDDNTK NEVIRLEQDI LSDLADSRQF YVLETKDFWR QIKTAGSAVP ANALYLMKAF
QQQSDELAKP SANILPPVFI HPSAQVDPTA KLGPNVSVGP RAVIGAGVRI KESIVLEDAE
IRHDACVLYS IIGWNSRVGA WARVEGTPTP VREHSTSVVK NGVKVQSITI LGKECAVADE
VRVQNCVCLP YKELKRDVAN EVIM
//
