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Q6FP42 (RNY1_CANGA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribonuclease T2-like
Short name=RNase T2-like
EC=3.1.27.1
Gene names
Name:RNY1
Ordered Locus Names:CAGL0J06820g
OrganismCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]
Taxonomic identifier284593 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces ›

Protein attributes

Sequence length433 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Rnase which modulates cell survival under stress conditions. Released from the vacuole to the cytoplasm during stress to promote tRNA and rRNA cleavage and to activate separately a downstream pathway that promotes cell death. Involved in cell size, vacuolar morphology and growth at high temperatures and high salt concentration By similarity.

Catalytic activity

Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.

Subcellular location

Vacuole lumen. Cytoplasm. Note: Is released from the vacuole to the cytoplasm during stress conditions like oxidative stress or stationary phase stress By similarity.

Sequence similarities

Belongs to the RNase T2 family.

Ontologies

Keywords
   Cellular componentCytoplasm
Vacuole
   DomainSignal
   Molecular functionEndonuclease
Hydrolase
Nuclease
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processnucleic acid phosphodiester bond hydrolysis

Inferred from electronic annotation. Source: GOC

   Cellular_componentvacuolar lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: InterPro

ribonuclease T2 activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – ? Potential
Chain? – 433Ribonuclease T2-likePRO_0000043253

Sites

Active site881 By similarity
Active site1561 By similarity
Active site1601 By similarity

Amino acid modifications

Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation711N-linked (GlcNAc...) Potential
Glycosylation2211N-linked (GlcNAc...) Potential
Glycosylation2631N-linked (GlcNAc...) Potential
Disulfide bond28 ↔ 47 By similarity
Disulfide bond36 ↔ 95 By similarity
Disulfide bond46 ↔ 171 By similarity
Disulfide bond103 ↔ 163 By similarity
Disulfide bond247 ↔ 283 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6FP42 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 0D9C24B324520463

FASTA43349,674
        10         20         30         40         50         60 
MILASVLKAF QGLQTGLQHS YQDGSPSCPI NLPLSCGNET AISDLCCFEY PGGILLMTQF 

        70         80         90        100        110        120 
WNYAPSKPNL NRTELEEELG PVDSFTIHGL WPDDCMGGYP QFCKRDLFID DVDYLLKSDA 

       130        140        150        160        170        180 
FNNDDTLPIQ GEELLNNLNK YWKSNNGNHE SLWIHEYNKH GTCLSTLQPQ CYSRWNPTTS 

       190        200        210        220        230        240 
QKGPKYYKKK AVYDYFRISY DLFQKLNTYE MLAKHNITPS NDTSYTKSEI LSALSSEFQG 

       250        260        270        280        290        300 
TQAHINCNSQ NALTEVWYYH QLNGSILNED FIPLDPLRSM SRCKDQGIKY YPKGYQRRDN 

       310        320        330        340        350        360 
RGPNKKPISR GTIRISQYGG FLIKTGRWMK RGTPANFELI ESKYGNYLLK SRMGYCTVHN 

       370        380        390        400        410        420 
DKSQLDCSSR SPDYATQFDY NEEKGILGYS GSFEWGAESA PKNGRTSRSV VFAVSNEKNS 

       430 
NLKYKFQLKF NRK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR380956 Genomic DNA. Translation: CAG60953.1.
RefSeqXP_448002.1. XM_448002.1.

3D structure databases

ProteinModelPortalQ6FP42.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2889620.
KEGGcgr:CAGL0J06820g.

Phylogenomic databases

HOGENOMHOG000197570.
KOK01166.
OMAVYDYFRI.
OrthoDBEOG42C1J1.

Family and domain databases

Gene3D3.90.730.10. 1 hit.
InterProIPR001568. RNase_T2-like.
IPR018188. RNase_T2_AS.
[Graphical view]
PANTHERPTHR11240. PTHR11240. 1 hit.
PfamPF00445. Ribonuclease_T2. 1 hit.
[Graphical view]
SUPFAMSSF55895. RNase_T2. 1 hit.
PROSITEPS00530. RNASE_T2_1. 1 hit.
PS00531. RNASE_T2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRNY1_CANGA
AccessionPrimary (citable) accession number: Q6FP42
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: July 19, 2004
Last modified: May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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