ID L0F9K7_DESDL Unreviewed; 415 AA.
AC L0F9K7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=Desdi_2177 {ECO:0000313|EMBL:AGA69618.1};
OS Desulfitobacterium dichloroeliminans (strain LMG P-21439 / DCA1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=871963 {ECO:0000313|EMBL:AGA69618.1, ECO:0000313|Proteomes:UP000010797};
RN [1] {ECO:0000313|Proteomes:UP000010797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG P-21439 / DCA1 {ECO:0000313|Proteomes:UP000010797};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Kruse T.,
RA de Vos W.M., Boon N., Smidt H., Woyke T.;
RT "Complete sequence of Desulfitobacterium dichloroeliminans LMG P-21439.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in the biosynthesis of molybdopterin.
CC {ECO:0000256|ARBA:ARBA00003487}.
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005046}.
CC -!- SIMILARITY: Belongs to the CinA family. {ECO:0000256|HAMAP-
CC Rule:MF_00226}.
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DR EMBL; CP003344; AGA69618.1; -; Genomic_DNA.
DR RefSeq; WP_015262597.1; NC_019903.1.
DR AlphaFoldDB; L0F9K7; -.
DR STRING; 871963.Desdi_2177; -.
DR KEGG; ddl:Desdi_2177; -.
DR eggNOG; COG1058; Bacteria.
DR eggNOG; COG1546; Bacteria.
DR HOGENOM; CLU_030805_9_3_9; -.
DR OMA; PGVPYEM; -.
DR OrthoDB; 9801454at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000010797; Chromosome.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
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 InterPro; IPR008284; MoCF_biosynth_CS.
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; PROTEIN YDEJ; 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.
DR PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
PE 3: Inferred from homology;
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150};
KW Reference proteome {ECO:0000313|Proteomes:UP000010797}.
FT DOMAIN 4..170
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 415 AA; 45205 MW; 03C3C3FAF94007FF CRC64;
MKAEIVATGT EILLGQTLNT SAHYLTGKLS ELGIEVDYHT TVGDNKERLG KVIIQGIERS
DLLLITGGTG PTEDDLSKEL IAQVFSLKML LDPTSLERIQ EFFVLRGTEM PETERKQAYF
PEGSQVLPNH QGTAPGVILQ KSNKTVILLP GPPTEMEPMF KEYVWPFLEQ KAQGDMARMY
VRTIKVVGLG ESDLEESLQD FVGRKNPSIT LLCKPTEMHI RIVVRGNATE SLEVLDQAEF
AIRERLGGRV FGTDEDTMLR LVSESLKKKQ LTLSTAESCT GGTLGALLTE QPGSSDFYLG
GVISYSNAMK ENFLGVSAQT LAQFGAVSAE TAREMAAGVR ERTKTDLGIS ITGIAGPGGG
SQEKPVGLVY IGLATSEGIK ANKFQFHGGR NSIRQLSVQA ALDWIRCYLL KSERG
//