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Database: UniProt
Entry: J3EQ59_9LACO
LinkDB: J3EQ59_9LACO
Original site: J3EQ59_9LACO 
ID   J3EQ59_9LACO            Unreviewed;       686 AA.
AC   J3EQ59;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Anaerobic ribonucleoside-triphosphate reductase {ECO:0000313|EMBL:EJN55440.1};
GN   ORFNames=A11Y_119067 {ECO:0000313|EMBL:EJN55440.1};
OS   Loigolactobacillus coryniformis subsp. coryniformis CECT 5711.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Loigolactobacillus.
OX   NCBI_TaxID=1185325 {ECO:0000313|EMBL:EJN55440.1, ECO:0000313|Proteomes:UP000007271};
RN   [1] {ECO:0000313|EMBL:EJN55440.1, ECO:0000313|Proteomes:UP000007271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT5711 {ECO:0000313|Proteomes:UP000007271};
RA   Rodriguez J.M.;
RT   "Complete Genome Sequence of Lactobacillus coryniformis CECT5711.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJN55440.1}.
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DR   EMBL; AKFP01000052; EJN55440.1; -; Genomic_DNA.
DR   AlphaFoldDB; J3EQ59; -.
DR   STRING; 1185325.A11Y_119067; -.
DR   PATRIC; fig|1185325.3.peg.1934; -.
DR   Proteomes; UP000007271; 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; IPR019777; Form_AcTrfase_GR_CS.
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; PS00850; GLY_RADICAL_1; 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:UP000007271}.
FT   DOMAIN          1..61
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
FT   DOMAIN          551..676
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000259|PROSITE:PS51149"
FT   MOD_RES         649
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00493"
SQ   SEQUENCE   686 AA;  77902 MW;  C500CC3DC5F929C3 CRC64;
     MTNHKIETVT NKVVAEVQER FTDAVKIYEI QNIVEHILLG EHQYDLAQEY INYRTHRDFA
     RNQATDINFT IQKLMQKDAT VVHENANKDS KVFNTQRDLT AGTVAKAMGL KLLPPHVANA
     HLKGDIHWHD LDYQPYSPMT NCCLIDFKEM LTNGFKIGNA EVESPHSIQT ATAQMAQIIA
     NVASSQYGGC SADRVDELLA PFAQLNYDKH LSDAADWIDG TEKQHAFAKM KTKKDIYDAM
     QALEYEINTL YSSQGQTPFT TLGFGLGTSW IEREIQRSIL QIRIQGLGKE QRTAIFPKLV
     FSIKRGLNLN PDEPNYDIKQ LAIECASKRM YPDVLMYDKL VELTGSFKAP MGCRSFLQGW
     QDEHGQEVNS GRMNLGVVTL NLPRIALEAA GDQDKFWTIL KERLQICKDA LVFKVERAKQ
     AEPENAPILY EHGAFGKRLK PEDSVDELFK NNRATVSLGY IGLYEVGAVF YGHAWEKNPA
     AKDFTLAIVK ELAANCEAWE KEYGYHFSVY GTPAESLTNT FCQADLKKFG KVKDVTDKDY
     YTNSFHYDVR KAPTPFEKLD FEKDYPKYSA GGFIHYCEYP NLKQNPKALE AVWDYAYDRV
     AYLGTNTPID QCFECGFKGD FKPTERGFEC PQCGNHNPQT CDVVKRTCGY LGNPLQRPMV
     HGRHKEISAR VKHLVLGNDQ TTQARQ
//
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