ID A0A1G4SA35_9FIRM Unreviewed; 796 AA.
AC A0A1G4SA35;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Ribonucleoside-triphosphate reductase class III catalytic subunit {ECO:0000313|EMBL:SCW65926.1};
GN ORFNames=SAMN02910456_02438 {ECO:0000313|EMBL:SCW65926.1};
OS Ruminococcaceae bacterium YRB3002.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae.
OX NCBI_TaxID=1520819 {ECO:0000313|EMBL:SCW65926.1, ECO:0000313|Proteomes:UP000199293};
RN [1] {ECO:0000313|EMBL:SCW65926.1, ECO:0000313|Proteomes:UP000199293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YRB3002 {ECO:0000313|EMBL:SCW65926.1,
RC ECO:0000313|Proteomes:UP000199293};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FMTG01000027; SCW65926.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4SA35; -.
DR STRING; 1520819.SAMN02910456_02438; -.
DR OrthoDB; 9804622at2; -.
DR Proteomes; UP000199293; 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; cd02976; NrdH; 1.
DR CDD; cd01675; RNR_III; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR012833; NrdD.
DR InterPro; IPR036249; Thioredoxin-like_sf.
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; PF00462; Glutaredoxin; 1.
DR Pfam; PF13597; NRDD; 1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 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}; Reference proteome {ECO:0000313|Proteomes:UP000199293}.
FT DOMAIN 2..95
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 796 AA; 90377 MW; 2F54B289E424E0AB CRC64;
MYQVVKRDEK VVDFNITKIS DAIKKAFDAT KVEYNDDVID LLALKVTADY APKIKDGKIT
VEEIQDSVES VLQRTGYEDV AKAYILYRKN REKIRAMKSA ALNYKDLVNS YVRIDDWRVK
ENSTVTYSVG GLILSNSGAI TANYWLSEIY DQEIADAHRH ADLHIHDLSM LTGYCAGWSL
KQLIQQGLGG ITGKITSAPP KHLATLCNQM VNFLGIMQNE WAGAQAFSSF DTYLAAFVKA
DNLDYDTVKK CIESFIYGVN TPSRWGTQAP FSNITLDWTV PNDLAELNCI VGGKEMDFKY
KDCQKEMDMV NKAFIEIMIE GDANGRGFQY PIPTYSITRD FDWSETENNK LLFEMTSKYG
TPYFSNYINS DMEPSDVRSM CCRLRLDLRE LRKKSGGFFG SGESTGSIGV VTINLPRIAY
LAKDEEDFFK RLNKMMDIAA RSLKVKRETI TKLLEVGLYP YTKHYLGTFN NHFSTIGLVG
MNEVGLNANW LKKDLTHAET QEFAKKVLNH MRERLSDYQE QYGDLYNLEA TPAESTSYRL
AKHDKKHYPD IITANDASGV YYYTNSSHLP VGFSSDIYDA LDIQDQLQTL YTSGTVFHAF
LGEKLPDWKS AATLVRKIAE NYSLPYYTLS PTYSICQAHG YLTGQVEECP ICGKKTETYS
RITGYYRPVQ NWNDGKTQEF KDRKLYKIET SVLKHAGPVA HKETTYSEAE EETIGNKIML
FTTKTCPNCK MAKQFLSDAG IEYEVIDAEE MVDMSNKYNI MQAPTLVVVQ DGECQTIPNL
SNIRRYIMDV TAASKQ
//
