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Database: UniProt
Entry: A1CI82_ASPCL
LinkDB: A1CI82_ASPCL
Original site: A1CI82_ASPCL 
ID   A1CI82_ASPCL            Unreviewed;       375 AA.
AC   A1CI82;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=Mannose-1-phosphate guanyltransferase {ECO:0000256|ARBA:ARBA00018601};
DE            EC=2.7.7.13 {ECO:0000256|ARBA:ARBA00012387};
DE   AltName: Full=GDP-mannose pyrophosphorylase {ECO:0000256|ARBA:ARBA00031190};
DE   AltName: Full=GTP-mannose-1-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00030179};
GN   ORFNames=ACLA_050590 {ECO:0000313|EMBL:EAW10587.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW10587.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW10587.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-
CC         alpha-D-mannose; Xref=Rhea:RHEA:15229, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57527,
CC         ChEBI:CHEBI:58409; EC=2.7.7.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00001083};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC       biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP
CC       route): step 1/1. {ECO:0000256|ARBA:ARBA00004823}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000256|ARBA:ARBA00007274}.
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DR   EMBL; DS027054; EAW10587.1; -; Genomic_DNA.
DR   RefSeq; XP_001272013.1; XM_001272012.1.
DR   AlphaFoldDB; A1CI82; -.
DR   STRING; 344612.A1CI82; -.
DR   EnsemblFungi; EAW10587; EAW10587; ACLA_050590.
DR   GeneID; 4703793; -.
DR   KEGG; act:ACLA_050590; -.
DR   VEuPathDB; FungiDB:ACLA_050590; -.
DR   eggNOG; KOG1322; Eukaryota.
DR   HOGENOM; CLU_029499_0_0_1; -.
DR   OMA; GPNCWIC; -.
DR   OrthoDB; 5486038at2759; -.
DR   UniPathway; UPA00126; UER00930.
DR   Proteomes; UP000006701; 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:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006486; P:protein glycosylation; IEA:EnsemblFungi.
DR   GO; GO:0043934; P:sporulation; IEA:UniProt.
DR   CDD; cd05824; LbH_M1P_guanylylT_C; 1.
DR   CDD; cd06425; M1P_guanylylT_B_like_N; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   InterPro; IPR045233; GMPPB_N.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR018357; Hexapep_transf_CS.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR22572:SF15; MANNOSE-1-PHOSPHATE GUANYLTRANSFERASE BETA; 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   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 2.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:EAW10587.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..233
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   375 AA;  41419 MW;  7077000DC616A86F CRC64;
     MKALILVGGF GTRLRPLTLT LPKPLVEFGN RPMILHQVES LAAAGVTDIV LAVNYRPDVM
     VAALKKYEEQ YNVRIEFSVE SEPLGTAGPL KLAEKILGKD DSPFFVLNSD IICDYPFKQL
     AEFHKKHGDE GTIVVTKVDE PSKYGVVVHK PNHPSRIDRF VEKPVEFVGN RINAGIYILN
     PSVLKRIDLR PTSIEQETFP AICGDGQLHS YDLEGFWMDV GQPKDFLTGT CLYLTSLAKR
     NSKLLAPNSE PYVHGGNVMV DPSAKIGKNC RIGPNVVIGP NVVVGDGVRL QRCVVLENSK
     IKDHAWIKST IVGWNSSVGK WARLENVTVL GDDVTIADEV YVNGGSILPH KSIKQNVDGK
     FIFFPPLRAP CRNKN
//
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