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Entry version 154 (13 Feb 2019)
Sequence version 1 (01 Feb 1996)
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Protein

Protein Dicer

Gene

dcr1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
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

Required for G1 arrest and mating in response to nitrogen starvation. Ago1 regulation of cytokinesis and cell cycle checkpoints occurs downstream of dcr1. Required, indirectly, for regulated hyperphosphorylation of cdc2.
Has a role in the RNA interference (RNAi) pathway which is important for heterochromatin formation, accurate chromosome segregation, centromere cohesion and telomere function during mitosis and meiosis. Digests double-stranded RNA (dsRNA) producing 21 to 23 bp dsRNAs, so-called interfering RNAs (siRNA). Required for both post-transcriptional and transcriptional gene silencing. Required for silencing at the centromeres and for initiation of transcriptionally silent heterochromatin at the mating type locus. Promotes histone H3 'Lys-10' methylation necessary for centromere function. Required for recruitment of swi6 and cohesin to an ectopic dg repeat.6 Publications

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+By similarity, Mn2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi1123Magnesium or manganeseBy similarity1
<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>Sitei1215Important for activityBy similarity1
Metal bindingi1219Magnesium or manganeseBy similarity1
Metal bindingi1222Magnesium or manganeseBy similarity1
Metal bindingi1275ZincCombined sources1 Publication1
Metal bindingi1312Zinc; via tele nitrogenCombined sources1 Publication1
Metal bindingi1350ZincCombined sources1 Publication1
Metal bindingi1352ZincCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi32 – 39ATPPROSITE-ProRule annotation8

<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 - Molecular functioni

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

Molecular functionEndonuclease, Helicase, Hydrolase, Nuclease
Biological processCell cycle, Chromosome partition, RNA-mediated gene silencing
LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding, Zinc

<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_and_taxonomy_section">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:
Protein Dicer
Alternative name(s):
Cell cycle control protein dcr1
RNA interference pathway protein dcr1
Including the following 2 domains:
Endoribonuclease dcr1 (EC:3.1.26.-)
ATP-dependent helicase dcr1 (EC:3.6.4.-)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:dcr1
ORF Names:SPCC188.13c, SPCC584.10c
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri284812 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000002485 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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: Chromosome III

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:SPCC188.13c

Schizosaccharomyces pombe database

More...
PomBasei
SPCC188.13c dcr1

<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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<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_and_biotech_section">'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>Mutagenesisi1265K → A: Abolishes binding to dsRNA and dsDNA. No effect on retention in the nucleus, nor on function in RNAi-dependent heterochromatin assembly. 1 Publication1
Mutagenesisi1275C → S: Abolishes retention in the nucleus and function in RNAi-dependent heterochromatin assembly; when associated with S-1350 and S-1352. 1 Publication1
Mutagenesisi1287 – 1302Missing : Abolishes binding to dsRNA and dsDNA. No effect on retention in the nucleus, nor on function in RNAi-dependent heterochromatin assembly. 1 PublicationAdd BLAST16
Mutagenesisi1322R → A: Abolishes binding to dsRNA and dsDNA. No effect on retention in the nucleus, nor on function in RNAi-dependent heterochromatin assembly. 1 Publication1
Mutagenesisi1334R → A: No effect on retention in the nucleus. 1 Publication1
Mutagenesisi1344N → A: Decreases location in the nucleus. Abolishes retention in the nucleus; when associated with A-1348 and A-1349. 1 Publication1
Mutagenesisi1348Y → A: Decreases location in the nucleus. Abolishes retention in the nucleus; when associated with A-1344 and A-1349. 1 Publication1
Mutagenesisi1349S → A: Decreases location in the nucleus. Abolishes retention in the nucleus; when associated with A-1344 and A-1348. 1 Publication1
Mutagenesisi1350C → S: Abolishes retention in the nucleus and function in RNAi-dependent heterochromatin assembly; when associated with S-1275 and S-1352. 1 Publication1
Mutagenesisi1352C → S: Abolishes retention in the nucleus and function in RNAi-dependent heterochromatin assembly; when associated with S-1275 and S-1350. 1 Publication1

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001021941 – 1374Protein DicerAdd BLAST1374

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q09884

PRoteomics IDEntifications database

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PRIDEi
Q09884

PTM databases

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q09884

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
275506, 188 interactors

STRING: functional protein association networks

More...
STRINGi
4896.SPCC188.13c.1

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11374
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2L6MNMR-A1259-1358[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q09884

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q09884

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini19 – 206Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST188
Domaini340 – 517Helicase C-terminalPROSITE-ProRule annotationAdd BLAST178
Domaini537 – 628Dicer dsRNA-binding foldPROSITE-ProRule annotationAdd BLAST92
Domaini916 – 1038RNase III 1PROSITE-ProRule annotationAdd BLAST123
Domaini1083 – 1233RNase III 2PROSITE-ProRule annotationAdd BLAST151

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1263 – 1355C-terminal dsRNA-binding fold1 PublicationAdd BLAST93

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>Motifi145 – 148DECH boxCurated4

<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 C-terminal dsRNA-binding fold contains a bound zinc ion and is important for normal nuclear retention and function in RNAi-dependent heterochromatin assembly. It binds double-stranded DNA and RNA (in vitro).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 helicase family. Dicer subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q09884

KEGG Orthology (KO)

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KOi
K11592

Identification of Orthologs from Complete Genome Data

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OMAi
SFVDYYH

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q09884

Family and domain databases

Conserved Domains Database

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CDDi
cd00079 HELICc, 1 hit
cd00593 RIBOc, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1520.10, 2 hits
3.30.160.380, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR038248 Dicer_dimer_sf
IPR005034 Dicer_dimerisation_dom
IPR006935 Helicase/UvrB_N
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR027417 P-loop_NTPase
IPR000999 RNase_III_dom
IPR036389 RNase_III_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03368 Dicer_dimer, 1 hit
PF00271 Helicase_C, 1 hit
PF04851 ResIII, 1 hit
PF00636 Ribonuclease_3, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit
SM00535 RIBOc, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 1 hit
SSF69065 SSF69065, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51327 DICER_DSRBF, 1 hit
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit
PS00517 RNASE_3_1, 1 hit
PS50142 RNASE_3_2, 2 hits

<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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

Q09884-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDISSFLLPQ LLRKYQQDVY NIASKQNTLL VMRTGAGKTL LAVKLIKQKL
60 70 80 90 100
EEQILIQESN LEHKKISVFL VNKVPLVFQQ AEYIRSQLPA KVGMFYGELS
110 120 130 140 150
IEMSEQLLTN IILKYNVIVI TADLFYLFLA RGFLSINDLN LIIFDECHHA
160 170 180 190 200
IGNDAYARIM NDFYHRAKAV LSKKHFTLPR IFGMTASPFT GKKGNLYHRL
210 220 230 240 250
YQWEQLFDSK AHVVSENELA DYFCLPEESY VMYSNKLVVP PSDSIIKKCE
260 270 280 290 300
ETLQGCKLIS RAVKTALAET IDMGLWFGEQ VWLYLVDFVE TKRLKKKALG
310 320 330 340 350
KQLSDDEELA IDRLKIFVED WKNNKYSDNG PRIPVFDSTD VTDKVFKLLE
360 370 380 390 400
LLKATYRKSD SVRTVIFVER KATAFTLSLF MKTLNLPNIR AHSFIGHGPS
410 420 430 440 450
DQGEFSMTFR RQKDTLHKFK TGKYNVLIAT AVAEEGIDVP SCNLVIRFNI
460 470 480 490 500
CRTVTQYVQS RGRARAMASK FLIFLNTEEL LIHERILHEE KNLKFALSEL
510 520 530 540 550
SNSNIFDSLV CEERERVTDD IVYEVGETGA LLTGLYAVSL LYNFCNTLSR
560 570 580 590 600
DVYTRYYPTF TAQPCLSGWY CFEVELPKAC KVPAAQGSPA KSIRKAKQNA
610 620 630 640 650
AFIMCLDLIR MGLIDKHLKP LDFRRKIADL ETLEEDELKD EGYIETYERY
660 670 680 690 700
VPKSWMKVPE DITRCFVSLL YTDANEGDNH IFHPLVFVQA HSFPKIDSFI
710 720 730 740 750
LNSTVGPRVK IVLETIEDSF KIDSHLLELL KKSTRYLLQF GLSTSLEQQI
760 770 780 790 800
PTPYWLAPLN LSCTDYRFLE NLIDVDTIQN FFKLPEPVQN VTDLQSDTVL
810 820 830 840 850
LVNPQSIYEQ YAFEGFVNSE FMIPAKKKDK APSALCKKLP LRLNYSLWGN
860 870 880 890 900
RAKSIPKSQQ VRSFYINDLY ILPVSRHLKN SALLIPSILY HIENLLVASS
910 920 930 940 950
FIEHFRLDCK IDTACQALTS AESQLNFDYD RLEFYGDCFL KLGASITVFL
960 970 980 990 1000
KFPDTQEYQL HFNRKKIISN CNLYKVAIDC ELPKYALSTP LEIRHWCPYG
1010 1020 1030 1040 1050
FQKSTSDKCR YAVLQKLSVK RIADMVEASI GACLLDSGLD SALKICKSLS
1060 1070 1080 1090 1100
VGLLDISNWD EWNNYFDLNT YADSLRNVQF PYSSYIEETI GYSFKNKKLL
1110 1120 1130 1140 1150
HLAFIHPSMM SQQGIYENYQ QLEFLGDAVL DYIIVQYLYK KYPNATSGEL
1160 1170 1180 1190 1200
TDYKSFYVCN KSLSYIGFVL NLHKYIQHES AAMCDAIFEY QELIEAFRET
1210 1220 1230 1240 1250
ASENPWFWFE IDSPKFISDT LEAMICAIFL DSGFSLQSLQ FVLPLFLNSL
1260 1270 1280 1290 1300
GDATHTKAKG DIEHKVYQLL KDQGCEDFGT KCVIEEVKSS HKTLLNTELH
1310 1320 1330 1340 1350
LTKYYGFSFF RHGNIVAYGK SRKVANAKYI MKQRLLKLLE DKSNLLLYSC
1360 1370
NCKFSKKKPS DEQIKGDGKV KSLT
Length:1,374
Mass (Da):158,040
Last modified:February 1, 1996 - 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:i89AE9EF8DE7966C6
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
CU329672 Genomic DNA Translation: CAB41233.1

Protein sequence database of the Protein Information Resource

More...
PIRi
T39130 S62524

NCBI Reference Sequences

More...
RefSeqi
NP_588215.2, NM_001023205.2

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
SPCC188.13c.1; SPCC188.13c.1:pep; SPCC188.13c

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2538930

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
spo:SPCC188.13c

<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
CU329672 Genomic DNA Translation: CAB41233.1
PIRiT39130 S62524
RefSeqiNP_588215.2, NM_001023205.2

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2L6MNMR-A1259-1358[»]
ProteinModelPortaliQ09884
SMRiQ09884
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275506, 188 interactors
STRINGi4896.SPCC188.13c.1

PTM databases

SwissPalmiQ09884

Proteomic databases

PaxDbiQ09884
PRIDEiQ09884

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC188.13c.1; SPCC188.13c.1:pep; SPCC188.13c
GeneIDi2538930
KEGGispo:SPCC188.13c

Organism-specific databases

EuPathDBiFungiDB:SPCC188.13c
PomBaseiSPCC188.13c dcr1

Phylogenomic databases

InParanoidiQ09884
KOiK11592
OMAiSFVDYYH
PhylomeDBiQ09884

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q09884

Family and domain databases

CDDicd00079 HELICc, 1 hit
cd00593 RIBOc, 2 hits
Gene3Di1.10.1520.10, 2 hits
3.30.160.380, 1 hit
InterProiView protein in InterPro
IPR038248 Dicer_dimer_sf
IPR005034 Dicer_dimerisation_dom
IPR006935 Helicase/UvrB_N
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR027417 P-loop_NTPase
IPR000999 RNase_III_dom
IPR036389 RNase_III_sf
PfamiView protein in Pfam
PF03368 Dicer_dimer, 1 hit
PF00271 Helicase_C, 1 hit
PF04851 ResIII, 1 hit
PF00636 Ribonuclease_3, 2 hits
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit
SM00535 RIBOc, 2 hits
SUPFAMiSSF52540 SSF52540, 1 hit
SSF69065 SSF69065, 2 hits
PROSITEiView protein in PROSITE
PS51327 DICER_DSRBF, 1 hit
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit
PS00517 RNASE_3_1, 1 hit
PS50142 RNASE_3_2, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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 nameiDCR1_SCHPO
<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: Q09884
Secondary accession number(s): Q9UUN1
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: February 13, 2019
This is version 154 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 programFungal 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

3D-structure, Complete proteome, Reference proteome

Documents

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