ID D2TH00_CITRI Unreviewed; 398 AA.
AC D2TH00;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=CinA-like protein {ECO:0000256|HAMAP-Rule:MF_00226};
GN OrderedLocusNames=ROD_26621 {ECO:0000313|EMBL:CBG89405.1};
OS Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG89405.1, ECO:0000313|Proteomes:UP000001889};
RN [1] {ECO:0000313|EMBL:CBG89405.1, ECO:0000313|Proteomes:UP000001889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC168 {ECO:0000313|EMBL:CBG89405.1,
RC ECO:0000313|Proteomes:UP000001889};
RX PubMed=19897651; DOI=10.1128/JB.01144-09;
RA Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT "The Citrobacter rodentium genome sequence reveals convergent evolution
RT with human pathogenic Escherichia coli.";
RL J. Bacteriol. 192:525-538(2010).
CC -!- SIMILARITY: Belongs to the CinA family. {ECO:0000256|HAMAP-
CC Rule:MF_00226}.
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DR EMBL; FN543502; CBG89405.1; -; Genomic_DNA.
DR RefSeq; WP_012906826.1; NC_013716.1.
DR AlphaFoldDB; D2TH00; -.
DR STRING; 637910.ROD_26621; -.
DR KEGG; cro:ROD_26621; -.
DR eggNOG; COG1058; Bacteria.
DR HOGENOM; CLU_030805_9_1_6; -.
DR OrthoDB; 9801454at2; -.
DR Proteomes; UP000001889; Chromosome.
DR CDD; cd00885; cinA; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR HAMAP; MF_00226_B; CinA_B; 1.
DR InterPro; IPR036653; CinA-like_C.
DR InterPro; IPR008135; Competence-induced_CinA.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR NCBIfam; TIGR00200; cinA_nterm; 1.
DR NCBIfam; TIGR00177; molyb_syn; 1.
DR PANTHER; PTHR13939; NICOTINAMIDE-NUCLEOTIDE AMIDOHYDROLASE PNCC; 1.
DR PANTHER; PTHR13939:SF6; NMN AMIDOHYDROLASE-LIKE PROTEIN YFAY; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR PIRSF; PIRSF006728; CinA; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF142433; CinA-like; 1.
DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
PE 3: Inferred from homology;
FT DOMAIN 5..172
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 398 AA; 44020 MW; 4043ADD6C2B55FD0 CRC64;
MLKVEMLSTG DEVLHGQIVD TNAAWLADFF FNQGLPLTRR NTVGDNLDDL VAVLRERSQQ
ADVLIVNGGL GPTSDDLSAL AAATAKGEGL VLHEPWLAEM ERFFRERGRV MAPSNRKQAE
LPASAEFINN PVGTACGFAV QLNRCLMFFT PGVPSEFKVM VEHEILPRLR ERFSLTEAPL
CLRLTTFGRS ESDLAQSLDA LTLPAGVTLG YRSSMPIIEL KLTGPYAQRD AMHTLWQEVK
RVAGQSMIFE GTEGLPVQIA RELQNRQLSL TLSEQYTAGL LALQLSRAGA PLLASEVVPS
QEETLAQTAH WTNERRGNHY AGLALAVSGL ENEHLNFALA TPDGTFALRV HFSVTRHSLQ
IRQEVCAMMA LNMLRRWLNH QDIATEHGWI EVVESLTL
//
