RIR1_ASFM2
ID RIR1_ASFM2 Reviewed; 779 AA.
AC P26685;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Ribonucleoside-diphosphate reductase large subunit;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase large subunit;
GN OrderedLocusNames=Mal-053;
OS African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=10500;
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 [GENOMIC DNA].
RX PubMed=1871976; DOI=10.1016/0042-6822(91)90860-e;
RA Boursnell M., Shaw K., Yanez R.J., Vinuela E., Dixon L.;
RT "The sequences of the ribonucleotide reductase genes from African swine
RT fever virus show considerable homology with those of the orthopoxvirus,
RT vaccinia virus.";
RL Virology 184:411-416(1991).
RN [2]
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; M64728; AAA42732.1; -; Genomic_DNA.
DR PIR; A40568; WMVZAL.
DR SMR; P26685; -.
DR UniPathway; UPA00326; -.
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_0000187228"
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; 87388 MW; 88A3D0C8D5D10819 CRC64;
MENFFIVKKL ASATYGKALN VDLNKLLQAL NHHSLQGLIS YCSALTILHY DYSTLAARLS
VYLLHQSTAS SFSKAVSLQA AQSCSRLSSH FVDVVYKYKA IFDSYIDYSR DYKLSLLGIE
TMKNSYLLKN KDGVIMERPQ DAYMRVAIMI HGMGRVVNMK MILLTYDLLS RHVITHASPT
MFNAGTKKPQ LSSCFLLNVN DNLENLYDMV KTAGIISGGG GGIGLCLSGI RAKNSFISGS
GLRSNGIQNY IVLQNASQCY ANQGGLRPGA YAVYLELWHQ DIFTFLQMPR LKGQMAEQRL
NAPNLKYGLW VPDLFMEILE DQIHNRGDGT WYLFSPDQAP NLHKVFDLER SQHENAHREF
KKLYYQYVAE KRYTGVTTAK EIIKEWFKTV VQVGNPYIGF KDAINRKSNL SHVGTITNSN
LCIEITIPCW EGNEAEQGVC NLAAVNLAAF IRESSYDYRG LIEAAGNVTE NLDNIIDNGY
YPTEATRRSN MRHRPIGIGV FGLADVFASL KMKFGSPEAI AIDEAIHAAL YYGAMRRSIE
LAKEKGSHPS FPGSAASKGL LQPDLWVRCG DLIPSWENRV AQTTQGVLTP KKWWQLRLAA
IQGVRNGYLT ALMPTATSSN STGKNECFEP FTSNLYTRRT LSGEFIILNK YLMDDLEEIN
LWSEDIQQQL LNAGGSIQHI LDIPAEIRER YKTSREMNQK ILTKHAAARN PFVSQSMSLN
YYFYEPELSQ VLTVLVLGWK KGLTTGSYYC HFSPGAGTQK KIIRNSEKAC NADCEACLL
