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Database: UniProt
Entry: A0A1B6BHF7_9FIRM
LinkDB: A0A1B6BHF7_9FIRM
Original site: A0A1B6BHF7_9FIRM 
ID   A0A1B6BHF7_9FIRM        Unreviewed;       420 AA.
AC   A0A1B6BHF7;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=F3D3_3734 {ECO:0000313|EMBL:GAU79096.1};
OS   Fusibacter sp. 3D3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Eubacteriales Family XII. Incertae Sedis; Fusibacter.
OX   NCBI_TaxID=1048380 {ECO:0000313|EMBL:GAU79096.1, ECO:0000313|Proteomes:UP000095197};
RN   [1] {ECO:0000313|EMBL:GAU79096.1, ECO:0000313|Proteomes:UP000095197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3D3 {ECO:0000313|EMBL:GAU79096.1,
RC   ECO:0000313|Proteomes:UP000095197};
RA   Serrano A.E., Escudero L.V., Encalada O., Tebes C.J., Fernandez S.,
RA   Demergasso C.S.;
RT   "Draft genome sequence of Fusibacter ascotence 3D3 isolated from the high
RT   arsenic level Ascotan salt flat in northern Chile.";
RL   Submitted (SEP-2016) 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:GAU79096.1}.
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DR   EMBL; BDHH01000018; GAU79096.1; -; Genomic_DNA.
DR   RefSeq; WP_069875860.1; NZ_BDHH01000018.1.
DR   AlphaFoldDB; A0A1B6BHF7; -.
DR   STRING; 1048380.F3D3_3734; -.
DR   OrthoDB; 9801454at2; -.
DR   Proteomes; UP000095197; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000095197}.
FT   DOMAIN          11..179
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   420 AA;  46262 MW;  0FEF77783C4982E2 CRC64;
     MTESSRYLKA GILAIGTELL MGQTVNTNAT FLSQKLNEIG IGVYYHMTVG DNPMRIENIL
     KLLIDECDII FTTGGLGPTQ DDITKDIIAK ALGLEMVFDP HSMERIEKRF RAFNRVMTEN
     NKRQAYFPEN AQILDNDMGT APACIMKLEA LNKHIVVLPG PPKEMKWLYD EYIQNYLLAL
     NPNKMFSKYL SVYDLGESST EDALLDLIND QTDPTIATYA GDGKVLVRVT SFGHSNEKCQ
     QSVNSMVSEI KKRIGSYIIS EEGKDINEVV ASMLLEKNLS IAFVESCTGG KLVESIVKFS
     GVSKVVDRGI VTYSNKAKTD EVGVSEQTLL THGAVSHETC FEMVKGLCEK TGSTIGVSIT
     GVAGPTGGTV EKPVGLVYIG LKIGHKIMTF ENHFSGDRLT VQNRAVNKAL KMLYDELSKL
//
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