ID   A0A1I5VI14_9FIRM        Unreviewed;       697 AA.
AC   A0A1I5VI14;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Ribonucleoside-triphosphate reductase class III catalytic subunit {ECO:0000313|EMBL:SFQ07145.1};
GN   ORFNames=SAMN05444406_11134 {ECO:0000313|EMBL:SFQ07145.1};
OS   Caldicoprobacter faecalis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Caldicoprobacteraceae;
OC   Caldicoprobacter.
OX   NCBI_TaxID=937334 {ECO:0000313|EMBL:SFQ07145.1, ECO:0000313|Proteomes:UP000198577};
RN   [1] {ECO:0000313|EMBL:SFQ07145.1, ECO:0000313|Proteomes:UP000198577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20678 {ECO:0000313|EMBL:SFQ07145.1,
RC   ECO:0000313|Proteomes:UP000198577};
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; FOXR01000011; SFQ07145.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5VI14; -.
DR   STRING; 937334.SAMN05444406_11134; -.
DR   OrthoDB; 9804622at2; -.
DR   Proteomes; UP000198577; 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:UP000198577}.
FT   DOMAIN          3..95
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   697 AA;  79818 MW;  8B7949FBDC204A34 CRC64;
     MITQIRKRDG RIEKFQPEKI TWAIFKAAMA CGGNDFNRAE ELCRQVVDIA NLKFGDRIPD
     VEAIQDIVEK VLIENGHAQT AKAYILYREK RRNARNLNAL IGATIEMFSN YLGDKDWQIK
     ENANTHKSVN GLNNYVREVF TKNYWLHEIY PQEVREAHES GDCHIHDLGF FGPYCAGWDL
     RQLLLEGFGG VPGKVESKPA KHLRSFLGQI VNSTFTTQGE TAGAQAWSSI DTYCAPFIRY
     DKMTYSQVRQ CIQEFIFNIN VPTRVGFQCP FSNLTFDIKV PATLRDQPVI IGGQMMDETY
     GEFQEEMDMF NRAFCDVMLE GDAKGRVFTF PIPTINVTPD FDWDSPVVED FMKITCKYGI
     PYFANYINSD LSPEDAVSMC CRLRLDITEL RKRGGGLFGS NPMTGSIGVV TINLPRIGYL
     SSSEREFKSR LWRQVQIAKT ALEIKRKVIE QQSENGLYPY STHYLRHIKE RTGQYWYNHF
     STIGIVGMNE ALLNFMGKDI TTPEGQAFAI EVMHYLRDLL IELQKETGHF YNLEATPAEA
     TAYRLAKLDK SRYPDIITAG DDETPYYTNS TQLPVGYTDD IFEVVALQDE LQSLYTGGTV
     LHLYLGEQIE DTAVAKKLIQ KIFTQSKIPY ISITPTFSIC NQHGYIKGEH FKCPQCGAEA
     EVWSRVTGYL RPVQNYNPGK KREYFDRKKF KIREETL
//