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Database: UniProt
Entry: E4LBS8_9FIRM
LinkDB: E4LBS8_9FIRM
Original site: E4LBS8_9FIRM 
ID   E4LBS8_9FIRM            Unreviewed;       415 AA.
AC   E4LBS8;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Putative competence-damage inducible protein {ECO:0000256|HAMAP-Rule:MF_00226};
GN   Name=cinA {ECO:0000256|HAMAP-Rule:MF_00226};
GN   ORFNames=HMPREF9199_1239 {ECO:0000313|EMBL:EFR60919.1};
OS   Veillonella sp. oral taxon 158 str. F0412.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Veillonella.
OX   NCBI_TaxID=879309 {ECO:0000313|EMBL:EFR60919.1, ECO:0000313|Proteomes:UP000003565};
RN   [1] {ECO:0000313|EMBL:EFR60919.1, ECO:0000313|Proteomes:UP000003565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0412 {ECO:0000313|EMBL:EFR60919.1,
RC   ECO:0000313|Proteomes:UP000003565};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the CinA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00226}.
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:EFR60919.1}.
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DR   EMBL; AENU01000007; EFR60919.1; -; Genomic_DNA.
DR   RefSeq; WP_009351235.1; NZ_AENU01000007.1.
DR   AlphaFoldDB; E4LBS8; -.
DR   STRING; 879309.HMPREF9199_1239; -.
DR   eggNOG; COG1058; Bacteria.
DR   eggNOG; COG1546; Bacteria.
DR   OrthoDB; 9801454at2; -.
DR   Proteomes; UP000003565; Unassembled WGS sequence.
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..171
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   415 AA;  44708 MW;  192D427E97FC3FCB CRC64;
     MIVELISTGS ELLLGDTVNT NVSWLAQELN KLGYTIAHQS VVGDNPKRMA EVFQLASTRA
     DIVISTGGLG PTQGDITRNV LADSIGRPIV FNQEAMDEVK RFFESVKRTV PDASRREAEL
     PEGANVLHNP VGVAPGVVVE DGDTTYILLP GPPGEMKEMF QEGVVPYLDN RFGSQGVVAS
     YRYGVYDIRE IDLENTLMDL IKNQSNPTIA LLIKKGYIEV RITAKADTLE AAQALLNPWD
     SIIRERLGSR VGRDLTVSIE ETLGRALLEE HSTISTAESC TSGLVGKLLT NVSGSSEYYM
     GGVISYSNDI KHRVLSVPQD MLDTYGAVSE QVAKAMAEGA RAIGQTTYAV STTGIAGPGG
     GSPEKPVGLV WFGVTGPHGT VAHKANLIGN RDDIRQSAAE LALYYVYTYI TEKGK
//
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