ID A0A1I2PLS0_9FIRM Unreviewed; 727 AA.
AC A0A1I2PLS0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Ribonucleoside-triphosphate reductase class III catalytic subunit {ECO:0000313|EMBL:SFG14937.1};
GN ORFNames=SAMN04487761_1062 {ECO:0000313|EMBL:SFG14937.1};
OS Lachnospiraceae bacterium C7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1792306 {ECO:0000313|EMBL:SFG14937.1, ECO:0000313|Proteomes:UP000198643};
RN [1] {ECO:0000313|EMBL:SFG14937.1, ECO:0000313|Proteomes:UP000198643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7 {ECO:0000313|EMBL:SFG14937.1,
RC ECO:0000313|Proteomes:UP000198643};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FOPE01000006; SFG14937.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2PLS0; -.
DR STRING; 1792306.SAMN04487761_1062; -.
DR OrthoDB; 9804622at2; -.
DR Proteomes; UP000198643; 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 Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR001150; Gly_radical.
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.
DR PROSITE; PS51149; GLY_RADICAL_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};
KW Organic radical {ECO:0000256|ARBA:ARBA00022818, ECO:0000256|PROSITE-
KW ProRule:PRU00493}; Reference proteome {ECO:0000313|Proteomes:UP000198643}.
FT DOMAIN 1..94
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 601..727
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT MOD_RES 705
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 727 AA; 82997 MW; 949E7AE3C7987F57 CRC64;
MKIIKRSGSE EMFDASKIVA AVSKANESVI DYEKVDEEQI KKIAQSVEVA CENMKRSASV
EEIQDMVENQ LMNQRAFNVA RNYITYRYKR ALVRKSNSTD ERILSLIECN NEEVKQENSN
KNPTVSSVQR DYMAGEVSKD ITKRFLLPED IVEAHEKGII HFHDSDYFAQ HMHNCCLVNL
EDMLQNGTAI SETMIEKPKS FSTACNIATQ AIAQIASSQY GGQSISLAHL APFVEVSRQK
FRRRVREEFE SAGLELDDEK INKIVELRVK EEINRGVQMI QYQVITLMTT NGQAPFVTVF
MYLDEAPEGQ TRDDLAAITE EMLRQRIKGV KNENGVYITP AFPKLIYVLE EDNIHEDSKY
WYLTQLAAEC TAKRMVPDYI SEKKMKELKV DKNGNGNCYT CMGCRSFLTP YVDPETNKPK
YYGRFNQGVV TINLVDVACS SEGDEEKFWK ILDERLQLCY RALMCRHKRL IGTPSDVAPI
LWQNGALSRL KPGEPIDKLL FGGYSTISLG YAGLCECTRY MKGVSHTDPQ GTPFALKVMH
KLNDACAEWK AKENIDFSLY GTPLESTTYK FAKCLQKRFG VIEGVTDKNY ITNSYHVHVT
EEINAFDKLK FESQFQELSP GGAISYVEVP NMQDNIEAVI SVMQYIYENI MYAELNTKSD
FCQKCGYTGE IQIVEEENSG KLVWECPNCG NRDQSKMNVA RRTCGYIGTQ FWNQGRTQEI
KERVLHL
//