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Database: UniProt
Entry: I3YX35_AEQSU
LinkDB: I3YX35_AEQSU
Original site: I3YX35_AEQSU 
ID   I3YX35_AEQSU            Unreviewed;       415 AA.
AC   I3YX35;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=CinA-like protein {ECO:0000256|HAMAP-Rule:MF_00226};
GN   OrderedLocusNames=Aeqsu_2090 {ECO:0000313|EMBL:AFL81553.1};
OS   Aequorivita sublithincola (strain DSM 14238 / LMG 21431 / ACAM 643 / 9-3).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Aequorivita.
OX   NCBI_TaxID=746697 {ECO:0000313|EMBL:AFL81553.1, ECO:0000313|Proteomes:UP000006049};
RN   [1] {ECO:0000313|EMBL:AFL81553.1, ECO:0000313|Proteomes:UP000006049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14238 / LMG 21431 / ACAM 643 / 9-3
RC   {ECO:0000313|Proteomes:UP000006049};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA   Munk A.C.C., Kyrpides N., Mavromatis K., Pagani I., Ivanova N.,
RA   Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA   Faehnrich R., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Aequorivita sublithincola DSM 14238.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the CinA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00226}.
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DR   EMBL; CP003280; AFL81553.1; -; Genomic_DNA.
DR   RefSeq; WP_014782806.1; NC_018013.1.
DR   AlphaFoldDB; I3YX35; -.
DR   STRING; 746697.Aeqsu_2090; -.
DR   KEGG; asl:Aeqsu_2090; -.
DR   PATRIC; fig|746697.3.peg.2126; -.
DR   eggNOG; COG1058; Bacteria.
DR   eggNOG; COG1546; Bacteria.
DR   HOGENOM; CLU_030805_9_2_10; -.
DR   OrthoDB; 9801454at2; -.
DR   Proteomes; UP000006049; Chromosome.
DR   CDD; cd00885; cinA; 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;
FT   DOMAIN          4..172
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   415 AA;  45815 MW;  4B212D3916D43776 CRC64;
     MLAEIITIGD EILIGQIIDT NSAFISKELN KIGVKIYQIT SIQDDRDHIL QAFKDAKKHA
     DLVIVTGGLG PTKDDITKQT FCDFFEDTLI EDQSVVENVT QLFKKYQLNK PLPANFLQAM
     VPSKATILTN QYGTAPGMWM EKDETVFVSL PGVPYEMKHL VLEEVLPSVI KRFNRPYIYH
     KTLLTYGLGE SAVAERIADW ENSLPKTIKL AYLPSLGKVR LRLSSSGEDE VFLKESIDSR
     MEVLSEMLSD IAIGFEDETS IVGRIAHILN EKKQTLSLAE SCTGGAIAER ITAEAGASSF
     FMGSIVPYKT ELKTQILGVP SSLIEEYSVV SIEVAESMAV NSCKLFNTDY AIATTGIAGP
     TKGDGKDEVG TVCIAIASPR GIVSEKFNFG NDRYRVIEKT INKAFEMILK EISKN
//
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