ID A0A0G1A8Q5_9BACT Unreviewed; 695 AA.
AC A0A0G1A8Q5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Ribonucleoside-triphosphate reductase class III catalytic subunit {ECO:0000313|EMBL:KKS57422.1};
GN ORFNames=UV20_C0001G0062 {ECO:0000313|EMBL:KKS57422.1};
OS Candidatus Magasanikbacteria bacterium GW2011_GWA2_42_32.
OC Bacteria; Candidatus Magasanikbacteria.
OX NCBI_TaxID=1619039 {ECO:0000313|EMBL:KKS57422.1, ECO:0000313|Proteomes:UP000034837};
RN [1] {ECO:0000313|EMBL:KKS57422.1, ECO:0000313|Proteomes:UP000034837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKS57422.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LCDO01000001; KKS57422.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1A8Q5; -.
DR PATRIC; fig|1619039.3.peg.63; -.
DR Proteomes; UP000034837; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd01675; RNR_III; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR012833; NrdD.
DR NCBIfam; TIGR02487; NrdD; 1.
DR PANTHER; PTHR21075; ANAEROBIC RIBONUCLEOSIDE-TRIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR21075:SF0; ANAEROBIC RIBONUCLEOSIDE-TRIPHOSPHATE REDUCTASE; 1.
DR Pfam; PF03477; ATP-cone; 1.
DR Pfam; PF13597; NRDD; 1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492}.
FT DOMAIN 10..108
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 695 AA; 79191 MW; 966234AA3BEBBEBD CRC64;
MTAAKVNKIT QIRKRDDRIV PFEEGKLVKA ILLSLEATQE IESPKKRIKI AGKVAEEILN
TLNKRFHARS IPAVEEVQDI VEEELGKAKL FKTAKAYILY RDQRAKVRDM QTLINSDELI
DGYLNQLDWR VKENSNMSYS LQGLNNHVAS AVSSHYWLNR IYPQEVRDTH SSGDLHLHDL
QLLSAYCCGW DLKELLIQGF GGVSGKIESK PPKHFRTALG QLVNFFYTLQ GETAGAQAVS
SFDTLLAPFI RFDKLSYDDV KQGLQEFLFN MNVPTRVGFQ TPFTNITMDL LPGKYMADEA
VIIGGVPQKE TYKDFQPEID TLNRAFAEIM LEGDAKGRVF TFPIPTYNIT KDFNWENPVL
EPVWLMTAKY GIPYFSNFIN SDMKPEDARS MCCRLRLDNR ELRKKGGGLF GANPLTGSIG
VVTINLPRIG YLSKSKEELF NRLSRLMDIA KTSLEIKRQA IEKFTEQGLY PYSKHYLGGI
KERFGQYWKN HFNTIGINGM NEMALNFLGE DKNLITVEGQ EFAKEVLDFM RQRMGTYQEE
TNNLYNLEAT PAEGTAYRFA RKDKELYPGI LCANEEAYRK GKADPYYTNS SHLPVGFTDD
IFEALRLQDP LQTRYTGGTV LHGFIGEMLP SAEATKQLVK KIAENFHLPY YTITPTFSVC
PKHGYLAGEH QFCPRCDEEI GYTDYVSKKQ PALIN
//