ID F4HE39_GALAU Unreviewed; 726 AA.
AC F4HE39;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Anaerobic ribonucleoside triphosphate reductase {ECO:0000313|EMBL:AEC18000.1};
GN OrderedLocusNames=UMN179_01987 {ECO:0000313|EMBL:AEC18000.1};
OS Gallibacterium anatis (strain UMN179) (Pasteurella anatis).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Gallibacterium.
OX NCBI_TaxID=1005058 {ECO:0000313|EMBL:AEC18000.1, ECO:0000313|Proteomes:UP000006908};
RN [1] {ECO:0000313|EMBL:AEC18000.1, ECO:0000313|Proteomes:UP000006908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN179 {ECO:0000313|EMBL:AEC18000.1,
RC ECO:0000313|Proteomes:UP000006908};
RX PubMed=21602325; DOI=10.1128/JB.05177-11;
RA Johnson T.J., Fernandez-Alarcon C., Bojesen A.M., Nolan L.K., Trampel D.W.,
RA Seemann T.;
RT "Complete genome sequence of Gallibacterium anatis strain UMN179, isolated
RT from a laying hen with peritonitis.";
RL J. Bacteriol. 193:3676-3677(2011).
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DR EMBL; CP002667; AEC18000.1; -; Genomic_DNA.
DR AlphaFoldDB; F4HE39; -.
DR STRING; 1005058.UMN179_01987; -.
DR KEGG; gan:UMN179_01987; -.
DR eggNOG; COG1327; Bacteria.
DR eggNOG; COG1328; Bacteria.
DR HOGENOM; CLU_002707_2_0_6; -.
DR Proteomes; UP000006908; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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 22..113
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 603..726
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT COILED 102..129
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 701
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 726 AA; 82372 MW; F83CCC7BB1373BA6 CRC64;
MFTYSSQQQL NSVNYQDLSV LPIVIKRDGS KAQFDAQFIL NAMKKAAQAV NIEDDGYFEQ
LSQEISFEIL NGVNQQIDIA DIQQVVENHL MQSRYPQVAR AYIEYRHDRD KEREKRSQLT
QEIEGLIEQN NVLLMNENAN KDAKVIPTQR DLLAGIVARH YAKSYLLPKE VVQAHERGEI
HYHDLDYSPF FPMFNCMLVD LQGMLTNGFK MGNAEIEPPK SITTATAVTA QIIAQVASHI
YGGTTIDRLD EVLAPYVEKS YQKHLHNAEV WHIPNREGYA KALIEKECFD AFQSLEYEVN
TLHTANGQTP FVTFGFGLGT SWQSKLIQRS ILQNRIVGLG KNHKTAVFPK LVFTIKRGLN
QQPQDPNYDI KQLALECASK RMYPDILNYD QVVKVTGSFK APMGCRSFLG RYVENGKEIH
AGRNNLGVVS INLPRIALEA QHDEQRFYHI LDQRLAIAKQ ALLTRIARLE QTKARVAPIL
YMEGACGVRL KADDNVADIF KQGRASISLG YIGIHETINA LYGQGHIFDS DKLRGKGVAI
VRYLSEATKK WQAETGYAFS LYSTPSESLC DRFCRLDSKQ FGVVEGVTDK GYYTNSFHLD
VEKKVNPYDK LDFEMVYPPL ASGGFICYGE YPNLQHNLKA LEDVWDYSYD RVPYYGTNTP
IDECYQCGFT GEFECTSKGF VCPKCGNHDS AKVSVIRRVC GYLGSPDARP FNHGKQEEVK
RRVKHL
//
