Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P26685

- RIR1_ASFM2

UniProt

P26685 - RIR1_ASFM2

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

Mal-053

Organism
African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity).By similarity

Catalytic activityi

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.

Enzyme regulationi

Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction (By similarity).By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei178 – 1781SubstrateBy similarity
Sitei194 – 1941Important for hydrogen atom transferBy similarity
Sitei201 – 2011Allosteric effector bindingBy similarity
Binding sitei222 – 2221Substrate; via amide nitrogenBy similarity
Sitei231 – 2311Allosteric effector bindingBy similarity
Active sitei420 – 4201Proton acceptorBy similarity
Active sitei422 – 4221Cysteine radical intermediateBy similarity
Active sitei424 – 4241Proton acceptorBy similarity
Sitei440 – 4401Important for hydrogen atom transferBy similarity
Sitei748 – 7481Important for electron transferBy similarity
Sitei749 – 7491Important for electron transferBy similarity
Sitei774 – 7741Interacts with thioredoxin/glutaredoxinBy similarity
Sitei777 – 7771Interacts with thioredoxin/glutaredoxinBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: UniProtKB-EC

GO - Biological processi

  1. DNA replication Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00326.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonucleoside-diphosphate reductase large subunit (EC:1.17.4.1)
Alternative name(s):
Ribonucleotide reductase large subunit
Gene namesi
Ordered Locus Names:Mal-053
OrganismiAfrican swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV)
Taxonomic identifieri10500 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageAsfarviridaeAsfivirus
Virus hostiOrnithodoros (relapsing fever ticks) [TaxID: 6937]
Phacochoerus aethiopicus (Warthog) [TaxID: 85517]
Phacochoerus africanus (Warthog) [TaxID: 41426]
Potamochoerus larvatus (Bushpig) [TaxID: 273792]
Sus scrofa (Pig) [TaxID: 9823]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 779779Ribonucleoside-diphosphate reductase large subunitPRO_0000187228Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi194 ↔ 440Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Expressioni

Keywords - Developmental stagei

Early protein

Interactioni

Subunit structurei

Heterotetramer composed of a homodimer of the large subunit (R1) and a homodimer of the small subunit (R2). Larger multisubunit protein complex are also active, composed of (R1)n(R2)n (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliP26685.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni193 – 1942Substrate bindingBy similarity
Regioni420 – 4245Substrate bindingBy similarity
Regioni614 – 6185Substrate bindingBy similarity

Sequence similaritiesi

Family and domain databases

InterProiIPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamiPF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSiPR01183. RIBORDTASEM1.
SUPFAMiSSF48168. SSF48168. 1 hit.
TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
PROSITEiPS00089. RIBORED_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P26685-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MENFFIVKKL ASATYGKALN VDLNKLLQAL NHHSLQGLIS YCSALTILHY
60 70 80 90 100
DYSTLAARLS VYLLHQSTAS SFSKAVSLQA AQSCSRLSSH FVDVVYKYKA
110 120 130 140 150
IFDSYIDYSR DYKLSLLGIE TMKNSYLLKN KDGVIMERPQ DAYMRVAIMI
160 170 180 190 200
HGMGRVVNMK MILLTYDLLS RHVITHASPT MFNAGTKKPQ LSSCFLLNVN
210 220 230 240 250
DNLENLYDMV KTAGIISGGG GGIGLCLSGI RAKNSFISGS GLRSNGIQNY
260 270 280 290 300
IVLQNASQCY ANQGGLRPGA YAVYLELWHQ DIFTFLQMPR LKGQMAEQRL
310 320 330 340 350
NAPNLKYGLW VPDLFMEILE DQIHNRGDGT WYLFSPDQAP NLHKVFDLER
360 370 380 390 400
SQHENAHREF KKLYYQYVAE KRYTGVTTAK EIIKEWFKTV VQVGNPYIGF
410 420 430 440 450
KDAINRKSNL SHVGTITNSN LCIEITIPCW EGNEAEQGVC NLAAVNLAAF
460 470 480 490 500
IRESSYDYRG LIEAAGNVTE NLDNIIDNGY YPTEATRRSN MRHRPIGIGV
510 520 530 540 550
FGLADVFASL KMKFGSPEAI AIDEAIHAAL YYGAMRRSIE LAKEKGSHPS
560 570 580 590 600
FPGSAASKGL LQPDLWVRCG DLIPSWENRV AQTTQGVLTP KKWWQLRLAA
610 620 630 640 650
IQGVRNGYLT ALMPTATSSN STGKNECFEP FTSNLYTRRT LSGEFIILNK
660 670 680 690 700
YLMDDLEEIN LWSEDIQQQL LNAGGSIQHI LDIPAEIRER YKTSREMNQK
710 720 730 740 750
ILTKHAAARN PFVSQSMSLN YYFYEPELSQ VLTVLVLGWK KGLTTGSYYC
760 770
HFSPGAGTQK KIIRNSEKAC NADCEACLL
Length:779
Mass (Da):87,388
Last modified:August 1, 1992 - v1
Checksum:i88A3D0C8D5D10819
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64728 Genomic DNA. Translation: AAA42732.1.
PIRiA40568. WMVZAL.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64728 Genomic DNA. Translation: AAA42732.1 .
PIRi A40568. WMVZAL.

3D structure databases

ProteinModelPortali P26685.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00326 .

Family and domain databases

InterProi IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view ]
Pfami PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view ]
PRINTSi PR01183. RIBORDTASEM1.
SUPFAMi SSF48168. SSF48168. 1 hit.
TIGRFAMsi TIGR02506. NrdE_NrdA. 1 hit.
PROSITEi PS00089. RIBORED_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The sequences of the ribonucleotide reductase genes from African swine fever virus show considerable homology with those of the orthopoxvirus, vaccinia virus."
    Boursnell M., Shaw K., Yanez R.J., Vinuela E., Dixon L.
    Virology 184:411-416(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "African swine fever virus genomes."
    Kutish G.F., Rock D.L.
    Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiRIR1_ASFM2
AccessioniPrimary (citable) accession number: P26685
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: October 29, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3