ID   A0A1G9U3V9_9FIRM        Unreviewed;       781 AA.
AC   A0A1G9U3V9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Ribonucleoside-triphosphate reductase class III catalytic subunit {ECO:0000313|EMBL:SDM54572.1};
GN   ORFNames=SAMN05192585_10166 {ECO:0000313|EMBL:SDM54572.1};
OS   Acetanaerobacterium elongatum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetanaerobacterium.
OX   NCBI_TaxID=258515 {ECO:0000313|EMBL:SDM54572.1, ECO:0000313|Proteomes:UP000199182};
RN   [1] {ECO:0000313|EMBL:SDM54572.1, ECO:0000313|Proteomes:UP000199182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.5012 {ECO:0000313|EMBL:SDM54572.1,
RC   ECO:0000313|Proteomes:UP000199182};
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; FNID01000001; SDM54572.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9U3V9; -.
DR   STRING; 258515.SAMN05192585_10166; -.
DR   OrthoDB; 9804622at2; -.
DR   Proteomes; UP000199182; 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}; Reference proteome {ECO:0000313|Proteomes:UP000199182}.
FT   DOMAIN          7..98
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   781 AA;  87346 MW;  20C79870D1358BCE CRC64;
     MIRTLTDTIK KRSGEVVPFN SIKIRTAISK ANQSVDGELM SDAALDALTA QVVAALPDGQ
     VPTVEQIQDR VEEVLISSGF AKTAKSYILY RAAHAKIRQT EADLMDIYKE LTFAYAKDAD
     IKRENANIDA DTAMGTMLKY GSEGAKYFID NYILPKEIAA AHINGDIHIH DKDFYMLTET
     CCQIDLIKLF RGGFSTGHGN LREPNDIQSY SALACIAIQA NQNEMHGGQS VPNFDYAMAM
     GVAKTFKRNY YKAVRDYAKV RFGISGEEGD ALVQGLKENI SETVTLHSDE ACGKALAEYL
     MGSPFKSLME GLDAAEAEKL HRYAFDTAQN ETQRTTYQAM EAFVHNLNTM NSRAGAQVPF
     SSVNYGTDTS PEGRMVIMNL LLATEAGLGE GETPIFPVQI FKVKEGVNYN EGDPNYDLFK
     LAIHCSAKRL FPNFSFLDAP FNLPYYKEGD YNSEVAYMGC RTRVLGNSHD KSREVTCGRG
     NLSFTSINLP RIGIEAHGDM TRFYEILDRR IDLVIQQLLH RFKIQCTKKG RNYPFLMGQG
     VWIDSEKLGP DDSVEEVLKH GTLSMGFIGL AETLVALTGK HHGESKESQK LGLEIIGYMR
     KRMDEESEKT GLNFTLLATP AEGLSGRFLR IDRQQYGVLP GITDRDYYTN SFHVPVYYPI
     RAFDKIRIEA PYHALTNAGH ISYVEMDGDT SKNLEAFETV IRFMKEQGIG YGSVNHPVDR
     DPVCGYNGII DNECPKCHRK EGDGAPDFER IRRITGYLVG TIDRWNNAKR AEEKDRVKHG
     I
//