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Protein

RING finger protein Z

Gene

Z

Organism
Sabia mammarenavirus (isolate Human/Brasil/SPH114202/1990) (SABV) (Sabi mammarenavirus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z (By similarity).By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri43 – 79RING-type; atypicalAdd BLAST37

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host RIG-I by virus, Inhibition of host RLR pathway by virus, Viral budding, Viral budding via the host ESCRT complexes, Viral immunoevasion, Virus exit from host cell

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
RING finger protein Z
Short name:
Protein Z
Alternative name(s):
Zinc-binding protein
Gene namesi
Name:Z
OrganismiSabia mammarenavirus (isolate Human/Brasil/SPH114202/1990) (SABV) (Sabi mammarenavirus)
Taxonomic identifieri45709 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesArenaviridaeMammarenavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000009267 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host cytoplasm, Host membrane, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostBy similarity
ChainiPRO_00003610402 – 100RING finger protein ZAdd BLAST99

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by hostBy similarity1

Keywords - PTMi

Lipoprotein, Myristate

Interactioni

Subunit structurei

Interacts with protein N; this interaction probably directs the encapsidated genome to budding sites. Interacts (via RING domain) with polymerase L; this interaction inhibits viral transcription and replication. Interacts with the glycoprotein complex; this interaction plays a role in virion budding.

Binary interactionsi

WithEntry#Exp.IntActNotes
DDX58O957862EBI-3647496,EBI-995350From a different organism.

Protein-protein interaction databases

IntActiQ6UY62. 1 interactor.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi93 – 96PTAP/PSAP motif4

Domaini

The RING finger domain is essential for the inhibitory activity of protein Z in transcription and RNA replication.By similarity
Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. Ring-finger protein Z contains one L domain: a PSAP motif that may be sufficient to mediate budding (By similarity).By similarity

Sequence similaritiesi

Belongs to the arenaviridae Z protein family.Curated
Contains 1 RING-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri43 – 79RING-type; atypicalAdd BLAST37

Keywords - Domaini

Zinc-finger

Family and domain databases

InterProiIPR024183. RING_finger_Z_arenaviridae.
IPR003224. Znf_P11.
[Graphical view]
PfamiPF03854. zf-P11. 1 hit.
[Graphical view]
PIRSFiPIRSF004030. Z_ArenaV. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6UY62-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNSKSKSKL SANQYEQQTV NSTKQVAILK RQAEPSLYGR HNCRCCWFAN
60 70 80 90 100
TNLIKCSDHY ICLKCLNIML GKSSFCDICG EELPTSIVVP IEPSAPPPED
Length:100
Mass (Da):11,123
Last modified:July 5, 2004 - v1
Checksum:i544CCC8FDDD891AD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY358026 Genomic RNA. Translation: AAQ55262.1.
AY216506 Genomic RNA. Translation: ABY59837.1.
RefSeqiYP_089659.1. NC_006313.1.

Genome annotation databases

GeneIDi3077249.
KEGGivg:3077249.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY358026 Genomic RNA. Translation: AAQ55262.1.
AY216506 Genomic RNA. Translation: ABY59837.1.
RefSeqiYP_089659.1. NC_006313.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ6UY62. 1 interactor.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3077249.
KEGGivg:3077249.

Family and domain databases

InterProiIPR024183. RING_finger_Z_arenaviridae.
IPR003224. Znf_P11.
[Graphical view]
PfamiPF03854. zf-P11. 1 hit.
[Graphical view]
PIRSFiPIRSF004030. Z_ArenaV. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiZ_SABVB
AccessioniPrimary (citable) accession number: Q6UY62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: July 5, 2004
Last modified: September 16, 2015
This is version 50 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

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.