ID A0A0B2JZR0_9FIRM Unreviewed; 760 AA.
AC A0A0B2JZR0;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Ribonucleoside-triphosphate reductase {ECO:0000313|EMBL:KHM51442.1};
GN ORFNames=NZ47_10450 {ECO:0000313|EMBL:KHM51442.1};
OS Anaerovibrio lipolyticus.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Anaerovibrio.
OX NCBI_TaxID=82374 {ECO:0000313|EMBL:KHM51442.1, ECO:0000313|Proteomes:UP000030993};
RN [1] {ECO:0000313|EMBL:KHM51442.1, ECO:0000313|Proteomes:UP000030993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5S {ECO:0000313|EMBL:KHM51442.1,
RC ECO:0000313|Proteomes:UP000030993};
RX PubMed=23950883;
RA Prive F., Kaderbhai N.N., Girdwood S., Worgan H.J., Pinloche E.,
RA Scollan N.D., Huws S.A., Newbold C.J.;
RT "Identification and characterization of three novel lipases belonging to
RT families II and V from Anaerovibrio lipolyticus 5ST.";
RL PLoS ONE 8:E69076-E69076(2013).
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:KHM51442.1}.
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DR EMBL; JSCE01000197; KHM51442.1; -; Genomic_DNA.
DR RefSeq; WP_039210327.1; NZ_JSCE01000197.1.
DR AlphaFoldDB; A0A0B2JZR0; -.
DR STRING; 82374.NZ47_10450; -.
DR eggNOG; COG1328; Bacteria.
DR Proteomes; UP000030993; 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:UP000030993}.
FT DOMAIN 6..97
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 760 AA; 85627 MW; EA95189B8CC1EBBB CRC64;
MASYIQNIRK RNGDIVPFIA QKITDAIRKA NLESIDDTFT AKELERLTNE VTEAISAQDI
PTVEFIQDTV EKVLIRNNFA STAKAYIIYR AEHTKIREAQ GNLMDIYNEL TFKKSADADI
KRENANIDAD TAMGTMLKYG SEGSKYYIDN YILPKDIAAA HIDGDIHIHD KDFYMLTETC
CQIDLLKLFK DGFSTGHGYL REPNGIRSYA ALGCIAIQAN QNEMHGGQSI PNFDYSMAPG
VAKTFAKEYF KALAAFFIAV LSMNSNDAKL LSKEIRRCIP MDIRLGNTDE YLHHLVDFLP
YHQQSHNYQA ISPNQTERAH NYAVATAVDA TEDATYQAME AFIHNLNTMN SRAGAQVPFS
SINYGTDTSP EARMVIRNLL KATTAGLGNG ETPIFPVQIF KVKEGINYNK HDPNFDLFQQ
AIRTSAKRLF PNFSFLDAPF NLQFYKEGDY NSEVAYMGCR TRVMGNVHDK NRQVTCGRGN
LSFTSINLPR LALKSKGNKK IFFNELDSII ELVFRQLLHR FKIQCSKTVR NYPFLMGQGV
WIDSEKLKTD DSVAEVLKHG TLSMGFIGLA ETLIALTGKH HGESEEAQQL GLEIVEHMRK
RMDEKSQQTG LNFTLLATPA EGLSGRFVRL DRKEYGEIPG VTDKDYYTNS FHVPVYHKIA
AAKKLELEGP YHALTNAGHI SYVEMDGDPS KNLKAFEAII RCMHDNGIGY GSVNHPVDRD
PVCGYNGIIY DVCPQCGRSE AAHKMRRIVR RPQYDSNTRV
//
