ID A0A1I0I4R9_9FIRM Unreviewed; 831 AA.
AC A0A1I0I4R9;
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:SET91566.1};
GN ORFNames=SAMN04487771_10682 {ECO:0000313|EMBL:SET91566.1};
OS [Clostridium] aminophilum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1526 {ECO:0000313|EMBL:SET91566.1, ECO:0000313|Proteomes:UP000199820};
RN [1] {ECO:0000313|EMBL:SET91566.1, ECO:0000313|Proteomes:UP000199820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH1P1 {ECO:0000313|EMBL:SET91566.1,
RC ECO:0000313|Proteomes:UP000199820};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOIL01000068; SET91566.1; -; Genomic_DNA.
DR RefSeq; WP_074650486.1; NZ_FOIL01000068.1.
DR AlphaFoldDB; A0A1I0I4R9; -.
DR STRING; 1526.SAMN02910262_01336; -.
DR eggNOG; COG1328; Bacteria.
DR OrthoDB; 9804622at2; -.
DR Proteomes; UP000199820; 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 CDD; cd02947; TRX_family; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR005144; ATP-cone_dom.
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; PF13597; NRDD; 1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 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}; Reference proteome {ECO:0000313|Proteomes:UP000199820}.
FT DOMAIN 4..97
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 831 AA; 93737 MW; ED218D8ABB7E2EAA CRC64;
MRERQVIKRS GSKVDFDSAR ITAALSKAIL ASRDRDYAVM APKLCADMEM ELGGRYPEGV
YSVEDIQDLA EKALMSHGLY DAAKSFIRYR AVHENVRNIR SAEDFCEQTI TGYTGEPDAG
VFLTPGMEGA DTSREKNWHV KQNASVSYSI GAMILNNSER ISKAHWLTKF YDRDIVDAYR
SGAIHIHDLG MLSGYCAGWD LRKLIREGLG GVAGKISSAP AKHLNALCIQ MVNFLGILQN
EWAGAQAFSS FDTYLAPFVK ADHLSYDEVK QSIQSFVYGV NMPSRWGTQA PFSNITLDWN
CPADLKNVPA IVGGKDQDFT YGDCQEEMAM INKAFIEIMV EGDCDGRGFA YPIPTYSITS
DFDWSDTENN RLLFEMAAKY GTPYFSNYIN SDMKPSDVRS MCCRLRLDLR ELRKQNGGNF
GAGENTGSIG VVTVNMPRIA YLAKDEEDFF DRLERMMDIA ARSLDIKRKV ICKYLDMGLY
PYTKRYLPQG FKNHFSTIGL VGMNEACLNA KWIGKDLSHP ESSAWTAKVL DFMREKLSDY
QEKYGDLFNL EATPAESTAY RLARHDRELY PDIITAGKPG EVPYYTNSSH LPVGFTSDVF
EALDIQDNLQ TKYTSGTVFH CFLGEKLPDY RAAMRLVKTV AENYRLPYFT LSPVYSVCEA
HGYLAGEQKI CPVCGKRTEV YSRITGYYRP VSNWNDGKMQ EYLDRKAYRI DSAYHRDSGE
DLQKTEKNVT AGNVTDKTLT DENPLAMQWT EPGERDEVLF FTTPTCPNCK MIKAKGILSG
YREIDAAAPE NREYVDRFDI RTAPTLVVIH GGRAEKYENA SQILGYAQGR R
//