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Database: UniProt
Entry: A0A117LWR4_9FIRM
LinkDB: A0A117LWR4_9FIRM
Original site: A0A117LWR4_9FIRM 
ID   A0A117LWR4_9FIRM        Unreviewed;       687 AA.
AC   A0A117LWR4;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Anaerobic ribonucleoside-triphosphate reductase {ECO:0000313|EMBL:KUK71692.1};
GN   ORFNames=XD91_1768 {ECO:0000313|EMBL:KUK71692.1};
OS   Clostridiales bacterium 38_11.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales.
OX   NCBI_TaxID=1641393 {ECO:0000313|EMBL:KUK71692.1, ECO:0000313|Proteomes:UP000053314};
RN   [1] {ECO:0000313|Proteomes:UP000053314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(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:KUK71692.1}.
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DR   EMBL; LGGM01000122; KUK71692.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117LWR4; -.
DR   PATRIC; fig|1641393.3.peg.1233; -.
DR   Proteomes; UP000053314; 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          3..91
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   687 AA;  78545 MW;  A4FA4AA74F9FDC6F CRC64;
     MITHVIKREG QIEDYKSSKI SGAMGKAFKE TGIELKHNMT QLVEQTTDKL DKDTIHIEEI
     QDAVEQTLME NGYYEVAKAY ILYREEHAKK RLGIDHYINK IDEYMDKIDW RVTENSNAHY
     SYGALNKYIS EMQSRDYWLH RVYPSKIANG YKSGDFHIHD LGSLTVYCCG YSLIEIVQKG
     VRGISNIPCS KPAKHFGSLL AQVANLTTIF QNEIAGAVAF SSFDTLTAPF VKEDNLTYNE
     VKQIMQSFVF QINSNSRGGS EPAFSNLTFD LMVPIDMQVK PVIVAGKTLN YKYSDCQDEM
     DMINRAFYEV MLEGDSNGSV LSYPIPTYNI HKAFNWDRDN DKLLWEMTGK YGIPYFANFI
     NSDMKPEDAR SMCCRLRLDK RELVKRNGGL FGSGEKTGSI GVVTLNLPRY AYEANNKEMF
     YKRLDHNLSL AKESLVIKRK FLTQQLERGL LPAFTEYIGT LQNHFSTIGY VGANEMCENL
     LGQDITSEEG YAFTYEVLEY MRSRIQDFQE ETGDLFNLEA TPAESTAYKL ASRDKKIYKE
     IITQGDKIPY YTNSCHIPVK LVTDIHSLYE HQHKLQALHT GGTVIHNYLE TSISGEKAKT
     IVKYVTENFK APYTSLSPVY SICKTHGFIH GRHTTCPYCG GLVESYQRVT GYIRPVSRFN
     NGKKEEFKDR NQINDFNLNN PIKTKGV
//
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