ID T0M007_COLGC Unreviewed; 712 AA.
AC T0M007;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=NAD(+) diphosphatase {ECO:0000256|ARBA:ARBA00012381};
DE EC=3.6.1.22 {ECO:0000256|ARBA:ARBA00012381};
GN ORFNames=CGLO_02792 {ECO:0000313|EMBL:EQB57116.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB57116.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in mRNA + H2O = a 5'-
CC end phospho-adenosine-phospho-ribonucleoside in mRNA + beta-
CC nicotinamide D-ribonucleotide + 2 H(+); Xref=Rhea:RHEA:60876,
CC Rhea:RHEA-COMP:15698, Rhea:RHEA-COMP:15719, ChEBI:CHEBI:14649,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:144029,
CC ChEBI:CHEBI:144051; Evidence={ECO:0000256|ARBA:ARBA00023679};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60877;
CC Evidence={ECO:0000256|ARBA:ARBA00023679};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudC subfamily.
CC {ECO:0000256|ARBA:ARBA00009595}.
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:EQB57116.1}.
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DR EMBL; AMYD01000571; EQB57116.1; -; Genomic_DNA.
DR AlphaFoldDB; T0M007; -.
DR STRING; 1237896.T0M007; -.
DR eggNOG; KOG3084; Eukaryota.
DR HOGENOM; CLU_023860_0_0_1; -.
DR OMA; VEWSSTM; -.
DR OrthoDB; 3024612at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd03429; NADH_pyrophosphatase; 1.
DR Gene3D; 3.90.79.20; -; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR015375; NADH_PPase-like_N.
DR InterPro; IPR049734; NudC-like_C.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR PANTHER; PTHR42904:SF6; NAD-CAPPED RNA HYDROLASE NUDT12; 1.
DR PANTHER; PTHR42904; NUDIX HYDROLASE, NUDC SUBFAMILY; 1.
DR Pfam; PF00025; Arf; 1.
DR Pfam; PF00293; NUDIX; 1.
DR Pfam; PF09296; NUDIX-like; 1.
DR SMART; SM00177; ARF; 1.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51417; ARF; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530}.
FT DOMAIN 245..373
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 712 AA; 78030 MW; 42585B88C0C3DD4D CRC64;
MGSQIPNLPA PVDHPDSMLS RKFGRETVNY FAGSALNRVG WLRTDHTFIR SAFQAKETNF
MLLKDLSPLT SAPSKLAFVS FDDVKSVTSE DPFGPSEEDL IKNYDSSVSR PLIIFLGLEE
GAKVPFEYKG LQGRPWFAVD VTPKGPYAEA ANQLIEAQSA KGNTFLQGTR HITLEPDAAG
IYAQARSLAD WNSRNKFCAG CGQTTLSGNT GYKRLCPPTD LAGTKAALDR PECPTRGGVS
NISFPRTDPT MIAAVVSADG QKVLLGRQKR WPPHWYSTLA GFIEPGESIE ESVRREVLEE
SGVRVGRVVI HSSQPWPYPA SLMIGAIAQA LPDGETIDLG NDPELEDAQW FPFETVREAL
KTGVSGLGEA APEGYKEGSL RLPPPTAIAN RLMTAVIEGY ATTIPKMAEE PPTQSPLKPL
HCPHRWRYGQ RVSAGGQHQA PAPAPVPSSI HLTSIVPIPP CAANEASVAD NLPRRPARPR
PRDELVRKPP LPIMYHLAKG LYLLATSKEE YSVILLGLDN AGKTTFHEQV KSFFLPSHPD
PKLKTVPTVG QNVSTITLPD MYLKIWDVGG QHSLRRLWQS YYASAHAIVF IIDSTDIGDG
NLEHDSSGRL EECRLVLEDV LQHSETEGVP VLVLANKQDR EDCVEVVRIK EGLVKKVFEG
EKASSIRDSR VLPVSALTGT GVKEAVEWSG VSGVWPQEED EYPREKMFTT KV
//
