ID A0A1E4I1V4_9PSEU Unreviewed; 428 AA.
AC A0A1E4I1V4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=CinA-like protein {ECO:0000256|HAMAP-Rule:MF_00226};
GN ORFNames=ABS81_15155 {ECO:0000313|EMBL:ODU03177.1};
OS Pseudonocardia sp. SCN 72-86.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1660131 {ECO:0000313|EMBL:ODU03177.1, ECO:0000313|Proteomes:UP000094542};
RN [1] {ECO:0000313|EMBL:ODU03177.1, ECO:0000313|Proteomes:UP000094542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
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:ODU03177.1}.
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DR EMBL; MEFA01000086; ODU03177.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4I1V4; -.
DR Proteomes; UP000094542; Unassembled WGS sequence.
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; IPR008135; Competence-induced_CinA.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
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; 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 11..186
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 428 AA; 43891 MW; DB269CC08806978B CRC64;
MGEGVDRPRA GIVVTGSELL TGAISDANGP WIARRLADLG FEVVHVVSAG DRPDDLVRAL
EFLAGAGVSL VVTSGGLGPT ADDMTAEVVA GFAGVELEPD EAMRARIEEI LADWGARTGF
AGPALDEATR KQALVPRGAT ALPPVGTAPG LVVDRPGGPL VVVLPGPPRE LQGMWPAALA
APAVEKLLST VPPANARLLR FFGLPESEIA ATLREVPFDV SGVEVGTCLR RSELEVDLRP
RPGAEAVAEE LAGLIVERHA RNLVSAEGAT VDELVAQALL GKEFMVATGE SCTGGLLAGR
LVDRAGSSAY VSGGVVAYSN EAKTALLGVP AEMIAAHGAV SPEVARALAD GARERFGADV
GVGITGVAGP GGGTEAKPVG YVCFCVTTSD GTVLARDPRL RGSRADIRER SVDTAMHLIL
RAVAPRRG
//
