ID A0A0C2Q610_9CYAN Unreviewed; 419 AA.
AC A0A0C2Q610;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 29.
DE RecName: Full=CinA-like protein {ECO:0000256|HAMAP-Rule:MF_00226};
GN ORFNames=SD81_30920 {ECO:0000313|EMBL:KIJ73820.1};
OS Tolypothrix campylonemoides VB511288.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ73820.1};
RN [1] {ECO:0000313|EMBL:KIJ73820.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VB511288 {ECO:0000313|EMBL:KIJ73820.1};
RA Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.;
RT "Draft whole genome shotgun sequence of Tolypothrix campylonemoides
RT VB511288.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KIJ73820.1}.
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DR EMBL; JXCB01000012; KIJ73820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2Q610; -.
DR OrthoDB; 9801454at2; -.
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; 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.
PE 3: Inferred from homology;
FT DOMAIN 4..172
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 419 AA; 44892 MW; A00B9EE990A044A5 CRC64;
MSAEIICVGT ELLLGDILNS NAQYLAQQLA KLGIPHYYQT VVGDNPGRLK QVIEIASQRA
QILIFTGGLG PTPDDLTCET IADFFGAALV ERPDIIEDIT RKYAGRDRVM TPSNRKQALI
PQGAEILPNP TGTAPGIIWQ PRPDLTIFTF PGVPSEMHRM WEETAVPFLK SQGWGKEIIY
SRMLKFWGVA ESALAEKVAS YLNLPNPTVA PYSSRGEVKL RVSAKAASEA QAQDLIAPVE
KQIKEIAGLD YYGADDDTLA SVVGELLRAK GQTLSVAESC TGGGLGQMLT EISGSSDYFW
GGVISYDNSV KERLLGVNSE DLAKFGAVSS IVAEQMAAGV RSRLSTSWGV SITGIAGPGG
GTETKPVGLV YIGLAGPNGE VESFEYRFGA LRGRSLIRHV SACTALDNLR RKLVKGIGD
//