ID A9JKY7_ASFPB Unreviewed; 778 AA.
AC A9JKY7;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN Name=F778R {ECO:0000313|EMBL:CAN10144.1};
OS African swine fever virus (isolate Pig/Benin/Ben 97-1/1997) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus; African swine fever virus.
OX NCBI_TaxID=443876 {ECO:0000313|EMBL:CAN10144.1, ECO:0000313|Proteomes:UP000130745};
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1] {ECO:0000313|EMBL:CAN10144.1, ECO:0000313|Proteomes:UP000130745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Benin 97/1 {ECO:0000313|EMBL:CAN10144.1};
RX PubMed=18198370; DOI=10.1099/vir.0.83343-0;
RA Chapman D.A.G., Tcherepanov V., Upton C., Dixon L.K.;
RT "Comparison of the genome sequences of non-pathogenic and pathogenic
RT African swine fever virus isolates.";
RL J. Gen. Virol. 89:397-408(2008).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC Evidence={ECO:0000256|RuleBase:RU003410};
CC -!- SUBUNIT: Heterotetramer composed of a homodimer of the large subunit
CC (R1) and a homodimer of the small subunit (R2). Larger multisubunit
CC protein complex are also active, composed of (R1)n(R2)n.
CC {ECO:0000256|ARBA:ARBA00025859}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406,
CC ECO:0000256|RuleBase:RU003410}.
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DR EMBL; AM712239; CAN10144.1; -; Genomic_DNA.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000130745; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Deoxyribonucleotide synthesis {ECO:0000256|RuleBase:RU003410};
KW Early protein {ECO:0000256|ARBA:ARBA00022518};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410}.
FT DOMAIN 592..613
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 778 AA; 87504 MW; 38522386CF946561 CRC64;
METFFIETLA SDVYGKALNV DLDRLSQAQV KYTLQELISY CSALTILHYD YSTLAARLSV
YQLHQSTASS FSKAVRLQAA QSCSRLSPQF VDVVYKYKAI FDSYIDYNRD YKLSLLGIET
MKNSYLLKNK DGVIMERPQD AYMRVAIMIY GMGKVVNIKM ILLTYDLLSR HVITHASPTM
FNAGTKKPQL SSCFLLNVND NLENLYDMVK TAGIISGGGG GIGLCLSGIR AKNSFISGSG
LRSNGIQNYI MLQNASQCYA NQGGLRPGAY AVYLELWHQD IFTFLQMPRL KGQMAEQRLN
APNLKYGLWV PDLFMEILED QIHNRGDGTW YLFSPDQAPN LHKVFDLERS QHENAHREFK
KLYYQYVAEK RYTGVTTAKE IIKEWFKTVI QVGNPYIGFK DAINRKSNLS HVGTITNSNL
CIEVIIPCWE GDKAEQGVCN LAAVNLAAFI RENGYDYRGL IEASGNVTEN LDNIIDNGYY
PTEATRRSNM RHRPIGIGVF GLADVFASLK MKFGSPEAIA MDEAIHAALY YGAMRRSIEL
AKEKGSHPSF PGSAASKGLL QPDLWVRCGD LSSSWEERVA QTTQGVLTRK SWWQLRLAAM
QGVRNGYLTA LMPTATSSNS TGKNECFEPF TSNLYTRRTL SGEFIVLNKY LIDDLKEIDL
WTEAIQQQLL NAGGSIQHIL DIPAEIRDRY KTSREMNQKI LTKHAAARNP FVSQSMSLNY
YFYEPELSQV LTVLVLGWKK GLTTGSYYCH FSPGAGTQKK IIRNSEKACN ADCEACLL
//
