ID A0A087DGL4_9BIFI Unreviewed; 798 AA.
AC A0A087DGL4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Anaerobic ribonucleoside-triphosphate reductase {ECO:0000313|EMBL:KFI94664.1};
DE EC=1.17.4.2 {ECO:0000313|EMBL:KFI94664.1};
GN ORFNames=BSCA_0715 {ECO:0000313|EMBL:KFI94664.1};
OS Bifidobacterium scardovii.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=158787 {ECO:0000313|EMBL:KFI94664.1, ECO:0000313|Proteomes:UP000029033};
RN [1] {ECO:0000313|EMBL:KFI94664.1, ECO:0000313|Proteomes:UP000029033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21589 {ECO:0000313|EMBL:KFI94664.1,
RC ECO:0000313|Proteomes:UP000029033};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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:KFI94664.1}.
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DR EMBL; JGZO01000006; KFI94664.1; -; Genomic_DNA.
DR RefSeq; WP_033517268.1; NZ_JULC01000027.1.
DR AlphaFoldDB; A0A087DGL4; -.
DR STRING; 158787.BSCA_0715; -.
DR GeneID; 85166472; -.
DR eggNOG; COG1328; Bacteria.
DR Proteomes; UP000029033; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IEA:UniProtKB-EC.
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}; Oxidoreductase {ECO:0000313|EMBL:KFI94664.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029033}.
FT DOMAIN 20..115
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 652..778
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT REGION 289..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 751
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 798 AA; 90063 MW; 4BD2DF27EE7A207A CRC64;
MEAQVMTAVE TNARPGTGAV LVEKRDGRVV DFDPINIISA VKSAFADLDK EVGPEEEKLV
RGFADQVEGE IKERYNGPAK IEDIQNLVEH ALIDAHLYDV ARAYTNYRLD KDIQRAKATD
VNEAVSRFIN QDPTLIHENA NKDANVYATQ RDLLAGAVSK AAAFNMLPPA VANAHMKGDI
HFHDADYSPF TAQSNCSLPN FWDMLANGFT LGNAPMASPK SIAIAATQIT QIMKDVASSQ
YGGQTANRAD EHLATYAKKD YEKFLEEARE TIPDGMPVEF ARRQVENAKK NEPSKLHFGS
REPLPMDTPF HDDVDELEQE REILAKIRTR KSIYDAMQTM EYQINSNRVS NGQTPFVTIG
FGLGTDWFAR EVQRAILLNR IRGLGKDHHT AIFPKLVFTI RHGVNADPGD PNYDLKQLAL
ECATKRMYPD VVFYENIVKI TGSFKAPMGC RSFLQGWINP ATGKDEEDGR MNLGVVSVNV
PRIALESHGD KARFWKLFNE RMETAHQALQ FRIMRCKQAT PVNAPTLFRF GAFGRLGAND
NVDALFKNER ATVSLGYIGL AEATAVFYGK NWIRDHGWDP QGKEFALSIV KRMNELCKQW
SRMEGYHYSV YSTPAESLTD RFNRMDREKF GRVEGVTDHD FYTNSFHYPV WLQPTPMEKL
NYEKDFPYYA SGGFINYCEY PCLQDNPKAL EAVWDYAYNI GIGYLGTNTP IDHCFVCGFQ
GDFEPTEEGF KCPECGNADP DKCNVTKRTC GYLGNPVQRP MVHGRHEEIS HRVKHMSGET
GHVTLSDGTE REWFEEAK
//