ID V2X2E7_MONRO Unreviewed; 335 AA.
AC V2X2E7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 13-SEP-2023, entry version 37.
DE SubName: Full=Glucokinase regulator family {ECO:0000313|EMBL:ESK86951.1};
GN ORFNames=Moror_3348 {ECO:0000313|EMBL:ESK86951.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK86951.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK86951.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK86951.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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:ESK86951.1}.
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DR EMBL; AWSO01000858; ESK86951.1; -; Genomic_DNA.
DR RefSeq; XP_007853734.1; XM_007855543.1.
DR AlphaFoldDB; V2X2E7; -.
DR STRING; 1381753.V2X2E7; -.
DR KEGG; mrr:Moror_3348; -.
DR HOGENOM; CLU_049049_1_0_1; -.
DR OrthoDB; 7403at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0016835; F:carbon-oxygen lyase activity; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046348; P:amino sugar catabolic process; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05007; SIS_Etherase; 1.
DR Gene3D; 1.10.8.1080; -; 1.
DR HAMAP; MF_00068; MurQ; 1.
DR InterPro; IPR005488; Etherase_MurQ.
DR InterPro; IPR005486; Glucokinase_regulatory_CS.
DR InterPro; IPR040190; MURQ/GCKR.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR NCBIfam; TIGR00274; N-acetylmuramic acid 6-phosphate etherase; 1.
DR PANTHER; PTHR10088; GLUCOKINASE REGULATORY PROTEIN; 1.
DR PANTHER; PTHR10088:SF4; GLUCOKINASE REGULATORY PROTEIN; 1.
DR Pfam; PF13580; SIS_2; 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS01272; GCKR; 1.
DR PROSITE; PS51464; SIS; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Kinase {ECO:0000313|EMBL:ESK86951.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Transferase {ECO:0000313|EMBL:ESK86951.1}.
FT DOMAIN 67..232
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 335 AA; 35980 MW; CA842306F9281E15 CRC64;
MDSFFGLHRT PPPPLSSLST EGRNPASTTI DEADTEHICR IINTEDSQVP KAVEEVVPKI
AEAIDAIVER VQLGGRLLYM GAGTSGRLGV LDAAELPPTY TADPMQYIAL IAGGDRALRT
ASEGVEDSRD AGMADLNALL VTPNDTLIGI AASGRTPYVL GALECARMHG LLTIGLVCVR
PSEVELEGNC HIVIDPVTGP EVITGSTRMK AGTATKMVLN MLSTGLQIKL GKTYGNLMID
VKATNAKLVD RARRIIRTVA SEFPLPPTYS AILRDDEQLD AVVRRCEGSV KLALVVIISG
WGIGLCKDAL ERRHGVLKAV LEDVRYETVV RVFNR
//
