RIR1_ASFK5
ID RIR1_ASFK5 Reviewed; 779 AA.
AC P0C8H7;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Ribonucleoside-diphosphate reductase large subunit;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase large subunit;
GN OrderedLocusNames=Ken-057;
OS African swine fever virus (isolate Pig/Kenya/KEN-50/1950) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=561445;
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; AY261360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0C8H7; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000861; 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..779
FT /note="Ribonucleoside-diphosphate reductase large subunit"
FT /id="PRO_0000355219"
FT ACT_SITE 420
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 422
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 424
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 193..194
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 420..424
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 614..618
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 194
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 201
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 231
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 440
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 748
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 749
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 774
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT SITE 777
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT DISULFID 194..440
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 779 AA; 87767 MW; 7FF7134ECDC5C861 CRC64;
MENFFIVKKL ASDTYGKALN VDLDRLLQAQ NKYTLQELIS YCSALTILHY DYSTLAARLS
VYLLHQSTAS SFSEAVSLQA AQSCSRLSPQ FVDVVYKYKA IFDSYIDYSR DYKLTLLGIE
TMKNSYLLKN KDGVIMERPQ DAYMRVAIMI YGMGRVVNMK MILLTYDLLS RHVITHASPT
MFNAGTKKPQ LSSCFLLNVN DNLENLYDMV KTAGIISGGG GGIGLCLSGI RAKNSFISGS
GLRSNGIQNY IVLQNASQCY ANQGGLRPGA YAVYLELWHQ DIFTFLQMPR LKGQMAEQRL
NAPNLKYGLW VPDLFMEILE DQIHDRGDGT WYLFSPDQAP NLHKVFDLER SRHKNAHREF
RKLYYQYVAE KRYTGVTTAK EIIKEWFKTV IQVGNPYIGF KDAINRKSNL SHVGTITNSN
LCIEITIPCW EGSEAEQGVC NLAAVNLAAF IRENSYDYRG LIEAAGNVTE NLDNIIDNGY
YPTEATRRSN MRHRPIGIGV FGLADVFASF KMKFGSPEAI AMDEAIHAAL YYGAMRRSVE
LAKEKGSHPS FPGSAASKGL LQPDLWVRCD DLVFSWEERV AQTTQGVLTP KKWWQLRLAA
MQGVRNGYLT ALMPTATSSN STGKNECFEP FTSNLYTRRT LSGEFIVLNK YLIDDLKEIN
LWTEAIQQQL LNAGGSIQHI LDIPAEIRER YKTSREMNQK ILTKHAAARN PFVSQSMSLN
YYFYEPELSQ VLTVLVLGWK KGLTTGSYYC HFSPGAGTQK KIIRNSEKAC SADCEACLL
