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Protein

5'-3' exoribonuclease 2

Gene

dhp1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Required for the processing of nuclear mRNA and rRNA precursors. May promote the termination of transcription by RNA polymerase II (By similarity). Essential for vegetative cell growth and chromosome segregation. Possesses 5'->3' exoribonuclease activity.By similarity

Catalytic activityi

Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 5'-phosphates.

GO - Molecular functioni

  • 5'-3' exoribonuclease activity Source: PomBase
  • nucleic acid binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

mRNA processing, rRNA processing, Transcription, Transcription regulation, Transcription termination

Enzyme and pathway databases

ReactomeiR-SPO-6791226. Major pathway of rRNA processing in the nucleolus and cytosol.

Names & Taxonomyi

Protein namesi
Recommended name:
5'-3' exoribonuclease 2 (EC:3.1.13.-)
Alternative name(s):
Protein dhp1
Gene namesi
Name:dhp1
ORF Names:SPAC26A3.12c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC26A3.12c.
PomBaseiSPAC26A3.12c. dhp1.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000713981 – 9915'-3' exoribonuclease 2Add BLAST991

Proteomic databases

MaxQBiP40848.
PRIDEiP40848.

Interactioni

Protein-protein interaction databases

BioGridi279127. 18 interactors.
DIPiDIP-59743N.
MINTiMINT-4689803.

Structurei

Secondary structure

1991
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 13Combined sources11
Helixi15 – 17Combined sources3
Beta strandi18 – 20Combined sources3
Beta strandi49 – 55Combined sources7
Helixi57 – 64Combined sources8
Beta strandi67 – 69Combined sources3
Helixi75 – 93Combined sources19
Beta strandi95 – 102Combined sources8
Helixi109 – 143Combined sources35
Helixi149 – 152Combined sources4
Helixi159 – 161Combined sources3
Helixi167 – 184Combined sources18
Helixi188 – 190Combined sources3
Beta strandi194 – 198Combined sources5
Helixi206 – 218Combined sources13
Beta strandi229 – 232Combined sources4
Helixi238 – 244Combined sources7
Beta strandi248 – 255Combined sources8
Turni269 – 273Combined sources5
Beta strandi292 – 296Combined sources5
Helixi297 – 308Combined sources12
Helixi319 – 329Combined sources11
Helixi330 – 333Combined sources4
Beta strandi336 – 338Combined sources3
Helixi346 – 348Combined sources3
Helixi350 – 365Combined sources16
Beta strandi369 – 371Combined sources3
Helixi377 – 388Combined sources12
Helixi391 – 402Combined sources12
Turni403 – 405Combined sources3
Helixi591 – 598Combined sources8
Helixi608 – 629Combined sources22
Helixi647 – 649Combined sources3
Helixi668 – 675Combined sources8
Helixi678 – 683Combined sources6
Helixi686 – 693Combined sources8
Helixi700 – 702Combined sources3
Beta strandi712 – 715Combined sources4
Beta strandi719 – 722Combined sources4
Helixi729 – 737Combined sources9
Helixi740 – 742Combined sources3
Helixi745 – 749Combined sources5
Beta strandi757 – 761Combined sources5
Helixi767 – 774Combined sources8
Beta strandi776 – 778Combined sources3
Beta strandi780 – 782Combined sources3
Helixi788 – 791Combined sources4
Beta strandi796 – 800Combined sources5
Helixi819 – 824Combined sources6
Beta strandi828 – 830Combined sources3
Beta strandi833 – 839Combined sources7
Helixi864 – 873Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FQDX-ray2.20A1-885[»]
SMRiP40848.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi264 – 268Nuclear localization signalSequence analysis5

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000205514.
InParanoidiP40848.
KOiK12619.
OMAiISKPFEQ.
OrthoDBiEOG092C068M.
PhylomeDBiP40848.

Family and domain databases

InterProiIPR027073. 5_3_exoribonuclease.
IPR017151. 5_3_exoribonuclease_2/3.
IPR004859. Put_53exo.
[Graphical view]
PANTHERiPTHR12341. PTHR12341. 2 hits.
PfamiPF03159. XRN_N. 1 hit.
[Graphical view]
PIRSFiPIRSF037239. Exonuclease_Xrn2. 1 hit.

Sequencei

Sequence statusi: Complete.

P40848-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVPALFRLL SRKFAKVITP VIEAPTEKLP DGTEIEPDLS LPNPNGVECD
60 70 80 90 100
NLYLDMNGIV HPCSHPEDRP APETEDEMMV AVFEYTDRIL AMVRPRQLLF
110 120 130 140 150
IAIDGVAPRA KMNQQRSRRF RSSREAALKE EELQAFIEEA KQQGIPIDEN
160 170 180 190 200
ATKKKSWDSN CITPGTPFMD TLAKSLRYYI INKLNSDPCW RNVRFILSDA
210 220 230 240 250
SVPGEGEHKI MEFIRSQRVK PEYDPNTHHV VYGLDADLIM LGLATHEPHF
260 270 280 290 300
RVLREDVFFQ QGSTKKTKEE RLGIKRLDDV SETNKVPVKK PFIWLNVSIL
310 320 330 340 350
REYLEVELYV PNLPFPFDLE RAIDDWVFFI FFVGNDFLPH LPSLDIRDGA
360 370 380 390 400
VERLTEIWRA SLPHMGGYLT LDGSVNLARA EVILSAVGNQ EDDIFKRLKQ
410 420 430 440 450
QEDRRNENYR RRQQRESNQE SESYVDNVVI QRSVETQSTE VVTSSKSTSV
460 470 480 490 500
DTKPPKKTQK IDAPAPVDLV NLSEKTSNRS LGATNRELIN NRAANRLGLS
510 520 530 540 550
REAAAVSSVN KLAASALKAQ LVSNETLQNV PLEDSIASSS AYEDTDSIES
560 570 580 590 600
STPVVHPIDT KVSNVGQKRK APDSTEENEN TDTVRLYEPG YRERYYEQKF
610 620 630 640 650
HISPDEPEKI REAVKHYVHG LCWVLLYYYQ GCPSWTWYYP YHYAPFAADF
660 670 680 690 700
KDLASIDVKF ELNQPFKPYE QLLGVLPAAS KNNLPEKLQT LMTDENSEII
710 720 730 740 750
DFYPENFTID LNGKKFEWQG VALLPFIDEN RLLNAVSKIY PQLTEEESKR
760 770 780 790 800
NEDGSTLLFI SEHHPMFSEL VKQLYSKKRQ GKPLKLSGKM AHGLFGKVNT
810 820 830 840 850
NDSVIPNVSV QCPIDVTSAD ALQKYGSIDD NQSISLVFEV PKSHFVHKSM
860 870 880 890 900
LLRGVKMPNR VLTPEDINQV RAERSFSSRR NNGNSYRGGH QSYGVRRSYQ
910 920 930 940 950
SQSYSSRQSY TGVTNGFANG GVQPPWSGNG NFPRSNASYN SRGGHEGYGG
960 970 980 990
RSRGGGYSNG PPAGNHYSSN RGKGYGYQRE SYNNNNRNGY Y
Length:991
Mass (Da):112,368
Last modified:February 1, 1995 - v1
Checksum:i83FA34D93DADAD00
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D17752 Genomic DNA. Translation: BAA04601.1.
CU329670 Genomic DNA. Translation: CAA93235.1.
PIRiS43891.
RefSeqiNP_594155.1. NM_001019579.2.

Genome annotation databases

EnsemblFungiiSPAC26A3.12c.1; SPAC26A3.12c.1:pep; SPAC26A3.12c.
GeneIDi2542674.
KEGGispo:SPAC26A3.12c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D17752 Genomic DNA. Translation: BAA04601.1.
CU329670 Genomic DNA. Translation: CAA93235.1.
PIRiS43891.
RefSeqiNP_594155.1. NM_001019579.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FQDX-ray2.20A1-885[»]
SMRiP40848.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279127. 18 interactors.
DIPiDIP-59743N.
MINTiMINT-4689803.

Proteomic databases

MaxQBiP40848.
PRIDEiP40848.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC26A3.12c.1; SPAC26A3.12c.1:pep; SPAC26A3.12c.
GeneIDi2542674.
KEGGispo:SPAC26A3.12c.

Organism-specific databases

EuPathDBiFungiDB:SPAC26A3.12c.
PomBaseiSPAC26A3.12c. dhp1.

Phylogenomic databases

HOGENOMiHOG000205514.
InParanoidiP40848.
KOiK12619.
OMAiISKPFEQ.
OrthoDBiEOG092C068M.
PhylomeDBiP40848.

Enzyme and pathway databases

ReactomeiR-SPO-6791226. Major pathway of rRNA processing in the nucleolus and cytosol.

Miscellaneous databases

PROiP40848.

Family and domain databases

InterProiIPR027073. 5_3_exoribonuclease.
IPR017151. 5_3_exoribonuclease_2/3.
IPR004859. Put_53exo.
[Graphical view]
PANTHERiPTHR12341. PTHR12341. 2 hits.
PfamiPF03159. XRN_N. 1 hit.
[Graphical view]
PIRSFiPIRSF037239. Exonuclease_Xrn2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiXRN2_SCHPO
AccessioniPrimary (citable) accession number: P40848
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 30, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. 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.