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Database: UniProt
Entry: A0A074LUE3_9BACL
LinkDB: A0A074LUE3_9BACL
Original site: A0A074LUE3_9BACL 
ID   A0A074LUE3_9BACL        Unreviewed;       416 AA.
AC   A0A074LUE3;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=EL26_05390 {ECO:0000313|EMBL:KEO84200.1};
OS   Tumebacillus flagellatus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Tumebacillus.
OX   NCBI_TaxID=1157490 {ECO:0000313|EMBL:KEO84200.1, ECO:0000313|Proteomes:UP000027931};
RN   [1] {ECO:0000313|EMBL:KEO84200.1, ECO:0000313|Proteomes:UP000027931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GST4 {ECO:0000313|EMBL:KEO84200.1,
RC   ECO:0000313|Proteomes:UP000027931};
RX   PubMed=23435245; DOI=10.1099/ijs.0.045351-0;
RA   Wang Q., Xie N., Qin Y., Shen N., Zhu J., Mi H., Huang R.;
RT   "Tumebacillus flagellatus sp. nov., an alpha-amylase/pullulanase-producing
RT   bacterium isolated from cassava wastewater.";
RL   Int. J. Syst. Evol. Microbiol. 63:3138-3142(2013).
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:KEO84200.1}.
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DR   EMBL; JMIR01000005; KEO84200.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A074LUE3; -.
DR   STRING; 1157490.EL26_05390; -.
DR   eggNOG; COG1058; Bacteria.
DR   eggNOG; COG1546; Bacteria.
DR   OrthoDB; 9801454at2; -.
DR   Proteomes; UP000027931; 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:UP000027931}.
FT   DOMAIN          4..171
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   416 AA;  44843 MW;  334D0E17B263688B CRC64;
     MNAELIAVGT ELLMGQISNT NAQYLSQRMA EIGIAVYHHA VVGDNLERAQ KVLGIAKQRG
     ADVIILCGGL GPTEDDLTRQ VVASFLGKNL ILSDEIVEHI RSFYTYRGRE MPENNKQQAL
     VIEGATVLDN PRGTAPGQYI EADGVHYFLL PGPPAELKGM YQEQVLPILQ RVQGEAKQVF
     ASRYLHTFNI GESALVLKIK DIIDAQSNPT VAPYASEAGC TIRLTASSAN EAEARALIAP
     VESAIRERIG HYVYGVDDET LPVKPGLLLR ERGERMVTAE SCTGGLIGQL LTDIPNCSDY
     FYGSIVAYDN TIKEKVLGVD SQVLREHGAV SAQTAKQMAE GARKVMGVEW AISVTGIAGP
     GGGTAEKPVG LVYIGVAGPG GTTVGEHRLF GDRSQVRLRA ARTALHSLIE RIQNER
//
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