RIR1_MIMIV
ID RIR1_MIMIV Reviewed; 881 AA.
AC Q7T6Y8;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Ribonucleoside-diphosphate reductase large subunit;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase large subunit;
GN Name=RNR1; OrderedLocusNames=MIMI_R313;
OS Acanthamoeba polyphaga mimivirus (APMV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Imitervirales; Mimiviridae; Mimivirus.
OX NCBI_TaxID=212035;
OH NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rowbotham-Bradford;
RX PubMed=15486256; DOI=10.1126/science.1101485;
RA Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA La Scola B., Susan M., Claverie J.-M.;
RT "The 1.2-megabase genome sequence of Mimivirus.";
RL Science 306:1344-1350(2004).
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 -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000305}.
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DR EMBL; AY653733; AAQ09572.2; -; Genomic_DNA.
DR RefSeq; YP_003986816.1; NC_014649.1.
DR SMR; Q7T6Y8; -.
DR PRIDE; Q7T6Y8; -.
DR GeneID; 9924930; -.
DR KEGG; vg:9924930; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000001134; 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; IPR005144; ATP-cone_dom.
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; PS51161; ATP_CONE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; ATP-binding; Deoxyribonucleotide synthesis;
KW Disulfide bond; Early protein; Nucleotide-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..881
FT /note="Ribonucleoside-diphosphate reductase large subunit"
FT /id="PRO_0000187229"
FT DOMAIN 69..160
FT /note="ATP-cone"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492"
FT ACT_SITE 493
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 495
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 497
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 286..287
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 493..497
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 675..679
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 287
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 294
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 324
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 510
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 809
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 810
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 876
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT SITE 879
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT DISULFID 287..510
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 881 AA; 101472 MW; BC4A893F2212E068 CRC64;
MNSKNSIILD NLADVSDIID YEQNSIDYQR SIKNIEQLKS TEATEITNKL AINKAKKSSN
ILLEVPKETI YLDHNGSIQV ITSEIIRTYV EKIFEKMEVT HLDIDKMTKN IFPKLKSINT
IKDIDNQIIS TASEMVTDHY DYPKIAVWIL MTNLHDNTSD DFLETAEKLY NNKSESNKNA
PIISENIYNF IKKHIKEINR VIRYDRDYNL TIFGFRTLEK SYLKRINKKI VERPQHLFMR
VAITLHYRKN DLDRIFETYK YLSKGYFTHA TPTLFNAGTT HEQLSSCFLL GIGDSLEEIS
ECWKECALIS KHAGGIGIHM TNIRVEGAYI ASTQGEAGGL RVLTIFNDIS RYANQGGKRP
GSFAIFIEPW HGDIFFFLDL KKNTGAETER ARDLFLGLMI NDIFMERVYK DDVWSLMCPS
QCPNLLNKYG DEFTKEYLKY ESEGIYLKQI RAIDLWFKIM ESQIETGVPY VMFKDAINDK
SNQINIGVVN GSNLCCEIVE VSDKNNFSVC NLSSICLPRF VKIIDEVPTF NYQKLFKISR
ILTRNLNNII DINFYPLDKT RITNLRDRPI GIGVQGLADV FAMFKTPFDS EIARDLNRKI
FETIYYGALT ESNKLAREFG TYQTYQGSPI SQGKFQFDLW NFDKSQLSGM WDWELLRQEI
LNHGVRNSLV TTCMPTASTS QIMGWNECIE PYTENIYSRS TMAGEYFVIN KHLIKDLIEL
GVWNSEMVDL IKYYKGSVAN IPNIPDNIKA IYRTVWEIPQ KSIIEMAADR APFVDQTQSM
NLYIDKPSFA RLNSCLFYAW RKGLKTGMYY LRSKPASSAN QFGIDIDKIK EIESKNGIKK
QEDTFDLTDL TNTINQQVSG MVCRFVPAHL RKPGECLSCD G
