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Database: UniProt
Entry: D6XU30_BACIE
LinkDB: D6XU30_BACIE
Original site: D6XU30_BACIE 
ID   D6XU30_BACIE            Unreviewed;       412 AA.
AC   D6XU30;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Putative competence-damage inducible protein {ECO:0000256|HAMAP-Rule:MF_00226};
GN   Name=cinA {ECO:0000256|HAMAP-Rule:MF_00226};
GN   OrderedLocusNames=Bsel_1809 {ECO:0000313|EMBL:ADH99316.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Salisediminibacterium.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH99316.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH99316.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the CinA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00226}.
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DR   EMBL; CP001791; ADH99316.1; -; Genomic_DNA.
DR   RefSeq; WP_013172740.1; NC_014219.1.
DR   AlphaFoldDB; D6XU30; -.
DR   STRING; 439292.Bsel_1809; -.
DR   KEGG; bse:Bsel_1809; -.
DR   eggNOG; COG1058; Bacteria.
DR   eggNOG; COG1546; Bacteria.
DR   HOGENOM; CLU_030805_9_3_9; -.
DR   OrthoDB; 9801454at2; -.
DR   Proteomes; UP000000271; Chromosome.
DR   CDD; cd00885; cinA; 1.
DR   Gene3D; 3.30.70.2860; -; 1.
DR   Gene3D; 3.90.950.20; CinA-like; 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; IPR008136; CinA_C.
DR   InterPro; IPR041424; CinA_KH.
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   NCBIfam; TIGR00199; PncC_domain; 1.
DR   PANTHER; PTHR13939; NICOTINAMIDE-NUCLEOTIDE AMIDOHYDROLASE PNCC; 1.
DR   PANTHER; PTHR13939:SF0; NICOTINAMIDE-NUCLEOTIDE AMIDOHYDROLASE PNCC; 1.
DR   Pfam; PF02464; CinA; 1.
DR   Pfam; PF18146; CinA_KH; 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          4..170
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   412 AA;  45372 MW;  C2228650BE752115 CRC64;
     MNAEIVAIGS ELLLGQIVNS NASHISKELS YLGIDVYHHV AVGDNPDRLR DVLKQAAARS
     DLVICTGGLG PTKDDLTKEI LAGLTGRDLV YDEETEQNII DYYQKWNRVM PENNRKQAMV
     IKGSEILPNH HGLSCGMVVP VGKSQVMLLP GPPNELIPMF RDFALPYLKT MLNVTEEIES
     RVLRFFDIGE SMLAEKLDDL FEAQTNPTMA PLASMGEVML RLTVKGEDTE KNRAALDELQ
     DTILDRIGDY FIGIGETPLV RQVVELLQSR KKTVTAAESL TGGLFSSALT SVQGVSSVFP
     GSIVCYSNQV KETVLSVPEE LIQSEGVVSE ACARKLAENS RRLFNTDIAI SFTGVAGPDE
     LEGHPPGTVF ISITDGKRDE VHRLQLAGSR ENIQDRTVKY GCFYLRTFLL NE
//
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