RIR1_ASFP4
ID RIR1_ASFP4 Reviewed; 778 AA.
AC P0C8H8;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Ribonucleoside-diphosphate reductase large subunit;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase large subunit;
GN OrderedLocusNames=Pret-057;
OS African swine fever virus (isolate Tick/South Africa/Pretoriuskop Pr4/1996)
OS (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=561443;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kutish G.F., Rock D.L.;
RT "African swine fever virus genomes.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ribonucleoside-diphosphate reductase holoenzyme provides the
CC precursors necessary for viral DNA synthesis. Allows virus growth in
CC non-dividing cells. Catalyzes the biosynthesis of deoxyribonucleotides
CC from the corresponding ribonucleotides (By similarity). {ECO:0000250}.
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 -!- ACTIVITY REGULATION: Under complex allosteric control mediated by
CC deoxynucleoside triphosphates and ATP binding. The type of nucleotide
CC bound at the specificity site determines substrate preference. It seems
CC probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP
CC reduction and dTTP favors GDP reduction (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Genetic information processing; DNA replication.
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 (By
CC similarity). {ECO:0000250}.
CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000305}.
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DR EMBL; AY261363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0C8H8; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000859; 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:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR InterPro; IPR013346; NrdE_NrdA.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR PANTHER; PTHR11573; PTHR11573; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF48168; SSF48168; 1.
DR TIGRFAMs; TIGR02506; NrdE_NrdA; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; ATP-binding; Deoxyribonucleotide synthesis;
KW Disulfide bond; Early protein; Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..778
FT /note="Ribonucleoside-diphosphate reductase large subunit"
FT /id="PRO_0000355220"
FT ACT_SITE 419
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 421
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 423
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 192..193
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 419..423
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 613..617
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 193
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 200
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 230
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 439
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 747
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 748
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 773
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT SITE 776
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT DISULFID 193..439
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 778 AA; 87445 MW; 9C57F84C0F3E8AE3 CRC64;
METFFIETLA SDVYGKALNV DLDRLSQAQI KYTLQELISY CSALTILHYD YSTLAARLSV
YQLHQSTASS FSKAVRLQAA QSCSRLSPQF VDVVYKYKAI FDSYIDYSRD YKLSLLGIET
MKNSYLLKNK DGVIMERPQD AYMRVAIMIY GMGKVVNIKM ILLTYDLLSR HIITHASPTM
FNAGTKKPQL SSCFLLNVND NLENLYDMVK TAGIISGGGG GIGLCLSGIR AKNSFISGSG
LRSNGIQNYI MLQNASQCYA NQGGLRPGAY AVYLELWHQD IFTFLEMPRL KGQMAEQRLN
APNLKYGLWV PDLFMEILED QIHNRGDGRW YLFSPDQAPN LHKVFDLERS QHENAHREFK
KLYYQYVAEK RYTGVTTAKE IIKAWFKTVI QVGNPYIGFK DAINRKSNLS HVGTITNSNL
CIEVTIPCWE GDKAEQGVCN LAAVNLAAFI RENGYDYRGL IEASGNVTEN LDNIIDNGYY
PTEATRRSNM RHRPIGIGVF GLADVFASLK IKFGSPEAIA MDEAIHAALY YGAMRRSIEL
AKEKGSHPSF PGSAASKGLL QPDLWVRCGD LIPSWEERVA QTTQGVLTRK SWRQLRLAAI
QGVRNGYLTA LMPTATSSNS TGKNECFEPF TSNLYTRRTL SGEFIVLNKY LIDDLKEINL
WTEAIQLQLL NAGGSIQHIL DIPAEIRDRY KTSREMNQKI LTKHAAARNP FVSQSMSLNY
YFYEPELSQV LTVLVLGWKK GLTTGSYYCH FSPGAGTQKK IIRNSEKACN ADCEACLL
