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Database: UniProt
Entry: D9QR51_ACEAZ
LinkDB: D9QR51_ACEAZ
Original site: D9QR51_ACEAZ 
ID   D9QR51_ACEAZ            Unreviewed;       416 AA.
AC   D9QR51;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 53.
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=Acear_1482 {ECO:0000313|EMBL:ADL12992.1};
OS   Acetohalobium arabaticum (strain ATCC 49924 / DSM 5501 / Z-7288).
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC   Acetohalobium.
OX   NCBI_TaxID=574087 {ECO:0000313|EMBL:ADL12992.1, ECO:0000313|Proteomes:UP000001661};
RN   [1] {ECO:0000313|EMBL:ADL12992.1, ECO:0000313|Proteomes:UP000001661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49924 / DSM 5501 / Z-7288
RC   {ECO:0000313|Proteomes:UP000001661};
RX   PubMed=21304692;
RA   Sikorski J., Lapidus A., Chertkov O., Lucas S., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Brambilla E.,
RA   Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA   Bruce D., Detter C., Tapia R., Goodwin L., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M.,
RA   Spring S., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Acetohalobium arabaticum type strain (Z-
RT   7288).";
RL   Stand. Genomic Sci. 3:57-65(2010).
CC   -!- SIMILARITY: Belongs to the CinA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00226}.
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DR   EMBL; CP002105; ADL12992.1; -; Genomic_DNA.
DR   RefSeq; WP_013278437.1; NC_014378.1.
DR   AlphaFoldDB; D9QR51; -.
DR   STRING; 574087.Acear_1482; -.
DR   KEGG; aar:Acear_1482; -.
DR   eggNOG; COG1058; Bacteria.
DR   eggNOG; COG1546; Bacteria.
DR   HOGENOM; CLU_030805_9_3_9; -.
DR   OrthoDB; 9801454at2; -.
DR   Proteomes; UP000001661; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001661}.
FT   DOMAIN          4..170
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   416 AA;  45534 MW;  3176620D61312E6C CRC64;
     MRAEIVSIGT ELLLGQIVDA NSAYIAEKLA DLGIDLYYQM TVGDNQERLQ KVLKRSLEHS
     DIVITTGGLG PTDDDLTREA VAEVMGVDLI KDEKLEEQIR GFFAELEREM TVNNLSQAYL
     PAGAEPIINS RGTAPGIIIE RNGKTVISMP GVPPEMKQMM NKKVIPYLHD KAGSKELIKS
     KVLRVCGYGE SSLETEIKDI LDSQTNPTVA LLSDKAEVHL RLTAKAGNQK MADNLINQVE
     AELRERLGDD IFGIDDETME KVVGDRLREE VLTLAVAESC TGGLIGHRIT NVSGSSDYFK
     QGVVVYSNQA KKDLVQVKEE TLSEYGAVSR ETACEMAEGV KELADTDLGI AVTGIAGPTG
     GSEEKPVGLV YMGLADDKKV GSFKFKFHGS RKQIKYLTSQ YTLDKLRRYL EGSIVL
//
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