ID G2ZA59_LISIP Unreviewed; 716 AA.
AC G2ZA59;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Putative anaerobic ribonucleoside-triphosphate reductase {ECO:0000313|EMBL:CBW84735.1};
GN OrderedLocusNames=LIV_0256 {ECO:0000313|EMBL:CBW84735.1};
OS Listeria ivanovii (strain ATCC BAA-678 / PAM 55).
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=881621 {ECO:0000313|EMBL:CBW84735.1, ECO:0000313|Proteomes:UP000001286};
RN [1] {ECO:0000313|EMBL:CBW84735.1, ECO:0000313|Proteomes:UP000001286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-678 / PAM 55 {ECO:0000313|Proteomes:UP000001286};
RX PubMed=22072644; DOI=10.1128/JB.06120-11;
RA Buchrieser C., Rusniok C., Garrido P., Hain T., Scortti M., Lampidis R.,
RA Karst U., Chakraborty T., Cossart P., Kreft J., Vazquez-Boland J.A.,
RA Goebel W., Glaser P.;
RT "Complete genome sequence of the animal pathogen Listeria ivanovii, which
RT provides insights into host specificities and evolution of the genus
RT Listeria.";
RL J. Bacteriol. 193:6787-6788(2011).
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; FR687253; CBW84735.1; -; Genomic_DNA.
DR RefSeq; WP_014091798.1; NZ_CVPH01000001.1.
DR AlphaFoldDB; G2ZA59; -.
DR GeneID; 57075266; -.
DR KEGG; liv:LIV_0256; -.
DR eggNOG; COG1328; Bacteria.
DR HOGENOM; CLU_002707_2_0_9; -.
DR OrthoDB; 9804622at2; -.
DR Proteomes; UP000001286; Chromosome.
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}.
FT DOMAIN 9..98
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 588..713
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT MOD_RES 686
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 716 AA; 82011 MW; 6DE0789D7A5FAFB2 CRC64;
MYVEQLNEQM VIKRDGRKAS FDLIKIRNAI EASMKAINLE DEPFLEEVLL EVVSELPNKA
DMTIDEIQNS VENTLMKSTY PDVARAYIEY RHDRDHEREN ITDMHKSVEK LLQKDKTVVN
ENANKDATVF NTQRDLTAGA VAKSYALKYM LPKHVSNAHL KGEIHFHDLD YSPYHAMTNC
CLIDIESMLS KGFTIGNANV ESPKSIQTAT AQIAQIIANV ASSQYGGCSV DRIDEVLSVY
ARLNFEKHQK DAAEWVVLEK QEGYAEEKTR KDIYDAMQSL EYEINTLYTS NGQTPFVTLG
FGLGKDWFAR EIQKAILKVR IGGVGKDKHT AIFPKLVFSI RRGTNLNAAD PNYDIKQLAL
ECSSKRMYPD VLNYDSLVRL TGDFKVPMGC RSFLPAWTNE NGEHVNAGRN NLGVVTLNIP
RIAIQSGGDK DRFWEIFHDR MKTVKDALLF RLNRVRQARP ENAPILYKYG AFGKRLQDGE
EVDQLFNKER STISIGYIGL YEAATVFYGG EWEGDAEAKD FTLAILKELK AYADNWKDEY
GYWFSVYSTP SESLTDRFNR LDKEKYGVIK DITDKDYYQN SFHYDVRKKI TPFEKIDFEK
DYPEFCSGGF IHYCEYPKMV HNTKALEAVW DYSYDRVAYL GTNTPIDKCY ECDFEGEFVP
TEEGFKCPSC GNTDPEKADV VKRTCGYLGN PMKRPMVHGR HVEISNRVKH MENLGE
//
