ID W0EC55_9FIRM Unreviewed; 418 AA.
AC W0EC55;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=DESME_05945 {ECO:0000313|EMBL:AHF06646.1};
OS Desulfitobacterium metallireducens DSM 15288.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=871968 {ECO:0000313|EMBL:AHF06646.1, ECO:0000313|Proteomes:UP000010847};
RN [1] {ECO:0000313|EMBL:AHF06646.1, ECO:0000313|Proteomes:UP000010847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15288 {ECO:0000313|Proteomes:UP000010847};
RG DOE Joint Genome Institute;
RA Smidt H., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) 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; CP007032; AHF06646.1; -; Genomic_DNA.
DR RefSeq; WP_006715686.1; NZ_CP007032.1.
DR AlphaFoldDB; W0EC55; -.
DR STRING; 871968.DESME_05945; -.
DR KEGG; dmt:DESME_05945; -.
DR eggNOG; COG1058; Bacteria.
DR eggNOG; COG1546; Bacteria.
DR HOGENOM; CLU_030805_9_3_9; -.
DR OrthoDB; 9801454at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000010847; 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; 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.
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:UP000010847}.
FT DOMAIN 4..170
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 418 AA; 45460 MW; E7994062D5CED30D CRC64;
MKAEIIATGT EILLGQTLNT SAHYLTGKLS ELGIEVDYHT TVGDNRERVE QVLKRAINRS
ELLVTTGGTG PTVDDMTKEL VAKVLGLNLQ LDSGSLERIQ HFFSSRGSVM PKTEEKEAYF
PEGSKILTNN HGTAPGAIIQ HKGRTIVILP GPPAEMKPMF DDSVFPFLEK LVVNNMERMY
SRVIKIFGLG ESEIEQSLQD LMGNDQLGMT LLAKHSEMHV RLVIRSESEP KAIALFDKTE
RIIRERLEAR VFGTNDETML GIVNEILKSR QFTISTAESC TGGLLGATLT QEPGSSEIYL
GGVVSYSNSL KEKFLGVNPQ TLQAYGAVSP ETACEMAAGV KERSGSDLAV GITGIAGPGG
GNDVKPVGLV YIGLATPEGV QASKFQFHGQ RESIRQLSVM AALDMVRQYM LKVERSTL
//
