ID Q2BZB3_9GAMM Unreviewed; 708 AA.
AC Q2BZB3;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 08-NOV-2023, entry version 63.
DE SubName: Full=Anaerobic ribonucleoside triphosphate reductase {ECO:0000313|EMBL:EAR54158.1};
DE EC=1.17.4.2 {ECO:0000313|EMBL:EAR54158.1};
GN ORFNames=SKA34_10358 {ECO:0000313|EMBL:EAR54158.1};
OS Photobacterium sp. SKA34.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=121723 {ECO:0000313|EMBL:EAR54158.1, ECO:0000313|Proteomes:UP000005284};
RN [1] {ECO:0000313|EMBL:EAR54158.1, ECO:0000313|Proteomes:UP000005284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKA34 {ECO:0000313|EMBL:EAR54158.1,
RC ECO:0000313|Proteomes:UP000005284};
RA Hagstrom A.J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) 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:EAR54158.1}.
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DR EMBL; AAOU01000035; EAR54158.1; -; Genomic_DNA.
DR RefSeq; WP_006644971.1; NZ_CH724141.1.
DR AlphaFoldDB; Q2BZB3; -.
DR HOGENOM; CLU_002707_2_0_6; -.
DR OrthoDB; 9804622at2; -.
DR Proteomes; UP000005284; 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}; 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}; Oxidoreductase {ECO:0000313|EMBL:EAR54158.1}.
FT DOMAIN 3..94
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 585..708
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT COILED 83..110
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 683
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 708 AA; 79532 MW; DC5325D2F18759DF CRC64;
MKLVVIKRDG CRVPFEMQRI KEAVMGAAQS INDMDMSEVD AMSVAEATLA QFQHAEEVDI
HAIQDAVENQ LMVGPHKTVA RAYIEYRHDR DIAREKKSRL NNEIRGLIEQ SNASLLNENA
NKDSKVIPTQ RDLLAGIVAK HYATQHLLPR DIVKAHECGD IHFHDLDYSP FFPMFNCMLI
DLNGMLTHGF KMGNAEIDTP KSISTATAVT AQIIAQVASH IYGGTTINRI DEVLAPYVTV
SYEKHLEVAK EWSIEDPIAF ANARTEKECY DAFQSLEYEV NTLHTANGQT PFVTFGFGLG
TSWESRMIQE SILKNRIAGL GKNHKTAVFP KLVFAIKDGL NHKQGDANYD IKQLALECAS
KRMYPDILNY DKLVEVTGSF KTPMGCRSFL GPYEEKGELI HEGRNNLGVV SINLPRIALE
AKGDEARFFA LLDERLALSR RALDARISRL DGVKARVAPI LYMEGACGVR LKEDDDVSEI
FKNGRASISL GYIGIHETVN ALYGNDMHVY DSEELRQKAV AIVQRLRDAT DSWKKETGYG
FSLYSTPSEN LCSRFCAIDT KEFGVVAGVT DKGYYTNSFH LDVEKKVNPY DKIDFEMAYP
DIANGGFICY GEYPNIQHNL EALENVWDYS YSRVPYYGTN TPIDECYECG FTGEFDCTSK
GFTCPKCGNH EPSKVSVTRR VCGYLGSPDA RPFNFGKQEE VKRRVKHM
//
