Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 55 (07 Apr 2021)
Sequence version 1 (31 Oct 2006)
Previous versions | rss
Add a publicationFeedback
Protein

Ribonucleoside-diphosphate reductase large subunit-like protein

Gene

RIR1

Organism
Murid herpesvirus 1 (strain Smith) (MuHV-1) (Mouse cytomegalovirus)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Provides optimal viral replication conditions by promoting host cell survival and avoiding the host inflammatory response linked to NF-kappa-B activation. Blocks RIPK1 ubiquitination, thereby preventing NF-kappa-B activation and virally induced inflammatory response. Prevents host necroptosis by targeting RIPK3 thereby preventing the formation of necroptotic RIPK1-RIPK3 complexes. Also inhibits ZBP1-induced necroptosis. Does not have ribonucleotide reductase activity. Betaherpesviruses probably use another strategy to expand the dNTP pool in a quiescent host cell.7 Publications

Caution

Lacks the conserved sequence Asn-x-Cys-x-Glu essential for ribonucleotide reductase activity.UniRule annotation

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processHost-virus interaction, Inhibition of host NF-kappa-B by virus

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Ribonucleoside-diphosphate reductase large subunit-like proteinUniRule annotation
Alternative name(s):
Viral inhibitor of RIP activation
Cleaved into the following 2 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RIR1UniRule annotation
Synonyms:M45, m45.1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMurid herpesvirus 1 (strain Smith) (MuHV-1) (Mouse cytomegalovirus)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10367 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiVirusesDuplodnaviriaHeunggongviraePeploviricotaHerviviricetesHerpesviralesHerpesviridaeBetaherpesvirinaeMuromegalovirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiMus musculus (Mouse) [TaxID: 10090]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000008774 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome
  • UP000180711 Componenti: Genome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Host cytoplasm, Virion

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi61 – 64IQIG → AAAA in M45mut(RHIM); abolished ability to prevent necroptosis in infected cells. 2 Publications4

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004121111 – 1174Ribonucleoside-diphosphate reductase large subunit-like proteinAdd BLAST1174
ChainiPRO_00004121121 – 277N-terminal peptideAdd BLAST277
ChainiPRO_0000412113278 – 1174116 kDa peptideAdd BLAST897

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Undergoes proteolytic cleavage, generating two peptides, a N-terminal and a 116 kDa. The N-terminal peptide retains RIPK1- and RIPK3-binding activity as well as cell death suppression activity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei277 – 278Cleavage2

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Keywords - Developmental stagei

Late protein

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Self-assembles into homo-oligomeric amyloid fibrils.

Interacts with host RIPK1 (via RIP homotypic interaction motif); this interaction inhibits RIPK1 ubiquitination thereby preventing effective activation of host NF-kappa-B.

Interacts with host RIPK3 (via RIP homotypic interaction motif); this interaction disrupts RIPK3-RIPK1 interactions characteristic of TNF-alpha induced necroptosis, thereby suppressing this death pathway.

Interacts (via RIP homotypic interaction motif) with host ZBP1 (via RIP homotypic interaction motif); this interaction inhibits recruitment of RIPK1 and RIPK3 to ZBP1 and prevents ZBP1-induced NF-kappa-B activation.

5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-29743N

Protein interaction database and analysis system

More...
IntActi
Q06A28, 4 interactors

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi50 – 72RIP homotypic interaction motif (RHIM)2 PublicationsAdd BLAST23

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi82 – 85Poly-Arg4
Compositional biasi91 – 315Ala-richAdd BLAST225
Compositional biasi257 – 263Poly-Gln7

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminal region drives rapid self-assembly into homo-oligomeric amyloid fibrils and interacts with the RHIMs of host kinases RIPK1 and RIPK3, and ZBP1 to form heteromeric amyloid fibrils.1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the ribonucleoside diphosphate reductase large chain family.UniRule annotation

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_04027, HSV_RIR1_betahv, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR034716, HSV_RIR1_betahv
IPR025735, RHIM_dom
IPR000788, RNR_lg_C
IPR039718, Rrm1

The PANTHER Classification System

More...
PANTHERi
PTHR11573, PTHR11573, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12721, RHIM, 1 hit
PF02867, Ribonuc_red_lgC, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01183, RIBORDTASEM1

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q06A28-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDRQPKVYSD PDNGFFFLDV PMPDDGQGGQ QTATTAAGGA FGVGGGHSVP
60 70 80 90 100
YVRIMNGVSG IQIGNHNAMS IASCWSPSYT DRRRRSYPKT ATNAAADRVA
110 120 130 140 150
AAVSAANAAV NAAAAAAAAG GGGGANLLAA AVTCANQRGC CGGNGGHSLP
160 170 180 190 200
PTRMPKTNAT AAAAPAVAGA SNAKSDNNHA NATSGAGSAA ATPAATTPAA
210 220 230 240 250
TAVENRRPSP SPSTASTAPC DEGSSPRHHR PSHVSVGTQA TPSTPIPIPA
260 270 280 290 300
PRCSTGQQQQ QPQAKKLKPA KADPLLYAAT MPPPASVTTA AAAAVAPESE
310 320 330 340 350
SSPAASAPPA AAAMATGGDD EDQSSFSFVS DDVLGEFEDL RIAGLPVRDE
360 370 380 390 400
MRPPTPTMTV IPVSRPFRAG RDSGRDALFD DAVESVRCYC HGILGNSRFC
410 420 430 440 450
ALVNEKCSEP AKERMARIRR YAADVTRCGP LALYTAIVSS ANRLIQTDPS
460 470 480 490 500
CDLDLAECYV ETASKRNAVP LSAFYRDCDR LRDAVAAFFK TYGMVVDAMA
510 520 530 540 550
QRITERVGPA LGRGLYSTVV MMDRCGNSFQ GREETPISVF ARVAAALAVE
560 570 580 590 600
CEVDGGVSYK ILSSKPVDAA QAFDAFLSAL CSFAIIPSPR VLAYAGFGGS
610 620 630 640 650
NPIFDAVSYR AQFYSAESTI NGTLHDICDM VTNGLSVSVS AADLGGDIVA
660 670 680 690 700
SLHILGQQCK ALRPYARFKT VLRIYFDIWS VDALKIFSFI LDVGREYEGL
710 720 730 740 750
MAFAVNTPRI FWDRYLDSSG DKMWLMFARR EAAALCGLDL KSFRNVYEKM
760 770 780 790 800
ERDGRSAITV SPWWAVCQLD ACVARGNTAV VFPHNVKSMI PENIGRPAVC
810 820 830 840 850
GPGVSVVSGG FVGCTPIHEL CINLENCVLE GAAVESSVDV VLGLGCRFSF
860 870 880 890 900
KALESLVRDA VVLGNLLIDM TVRTNAYGAG KLLTLYRDLH IGVVGFHAVM
910 920 930 940 950
NRLGQKFADM ESYDLNQRIA EFIYYTAVRA SVDLCMAGAD PFPKFPKSLY
960 970 980 990 1000
AAGRFYPDLF DDDERGPRRM TKEFLEKLRE DVVKHGIRNA SFITGCSADE
1010 1020 1030 1040 1050
AANLAGTTPG FWPRRDNVFL EQTPLMMTPT KDQMLDECVR SVKIEPHRLH
1060 1070 1080 1090 1100
EEDLSCLGEN RPVELPVLNS RLRQISKESA TVAVRRGRSA PFYDDSDDED
1110 1120 1130 1140 1150
EVACSETGWT VSTDAVIKMC VDRQPFVDHA QSLPVAIGFG GSSVELARHL
1160 1170
RRGNALGLSV GVYKCSMPPS VNYR
Length:1,174
Mass (Da):125,215
Last modified:October 31, 2006 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iBDDC93B8E71E40C7
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U68299 Genomic DNA No translation available.
DQ978788 Genomic DNA Translation: ABI94733.1
GU305914 Genomic DNA Translation: ADD10427.1

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U68299 Genomic DNA No translation available.
DQ978788 Genomic DNA Translation: ABI94733.1
GU305914 Genomic DNA Translation: ADD10427.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

DIPiDIP-29743N
IntActiQ06A28, 4 interactors

Family and domain databases

HAMAPiMF_04027, HSV_RIR1_betahv, 1 hit
InterProiView protein in InterPro
IPR034716, HSV_RIR1_betahv
IPR025735, RHIM_dom
IPR000788, RNR_lg_C
IPR039718, Rrm1
PANTHERiPTHR11573, PTHR11573, 1 hit
PfamiView protein in Pfam
PF12721, RHIM, 1 hit
PF02867, Ribonuc_red_lgC, 1 hit
PRINTSiPR01183, RIBORDTASEM1

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRIR1_MUHVS
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q06A28
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: October 31, 2006
Last modified: April 7, 2021
This is version 55 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again