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Entry version 95 (08 May 2019)
Sequence version 3 (16 Nov 2011)
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Protein

PAN2-PAN3 deadenylation complex subunit pan3

Gene

pan3

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score:

Annotation score:4 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>
-Protein inferred from homologyi <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

Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein pab1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails. pan3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit pan2 to mRNA via its interaction with RNA and with pab1.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei315ATPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri26 – 55C3H1-typeUniRule annotationAdd BLAST30
<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 bindingi364 – 371ATPUniRule annotation8
Nucleotide bindingi424 – 425ATPUniRule annotation2

<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

Biological processmRNA processing
LigandATP-binding, 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:
PAN2-PAN3 deadenylation complex subunit pan3UniRule annotation
Alternative name(s):
PAB1P-dependent poly(A)-specific ribonucleaseUniRule annotation
Poly(A)-nuclease deadenylation complex subunit 3UniRule annotation
Short name:
PAN deadenylation complex subunit 3UniRule annotation
<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:pan3UniRule annotation
ORF Names:AN0769, AN10121/AN10119
<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>OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
<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 identifieri227321 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
<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
  • UP000000560 <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 VIII
  • UP000005890 Componenti: Unassembled WGS sequence

<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

Cytoplasm

<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_00002953681 – 661PAN2-PAN3 deadenylation complex subunit pan3Add BLAST661

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer. Forms a heterotrimer with a catalytic subunit pan2 to form the poly(a)-nuclease (PAN) deadenylation complex. Interacts (via PAM-2 motif) with poly(A)-binding protein pab1 (via PABC domain), conferring substrate specificity of the enzyme complex.UniRule annotation

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
162425.CADANIAP00001896

<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

3D structure databases

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

More...
SMRi
Q5BFB1

Database of comparative protein structure models

More...
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

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>Regioni263 – 524Pseudokinase domainUniRule annotationAdd BLAST262
Regioni564 – 661Knob domainUniRule annotationAdd BLAST98

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili525 – 563UniRule annotationAdd BLAST39

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>Motifi63 – 83PABPC-interacting motif-2 (PAM-2)CuratedAdd BLAST21

<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 zinc finger binds to poly(A) RNA.UniRule annotation
Contains a pseudokinase domain. The protein kinase domain is predicted to be catalytically inactive because some of the residues important for catalytic activity are substituted and it lacks the equivalent of the binding site for a peptide substrate. However, it has retained an ATP-binding site and ATP-binding is required for mRNA degradation, stimulating the activity of the pan2 nuclease in vitro. The nucleotide-binding site is juxtaposed to the RNase active site of pan2 in the complex and may actually bind nucleosides of a poly(A) RNA rather than ATP, feeding the poly(A)-tail to the active site of the deadenylase and thus increasing the efficiency with which this distributive enzyme degrades oligo(A) RNAs.UniRule annotation
The pseudokinase domain, the coiled-coil (CC), and C-terminal knob domain (CK) form a structural unit (PKC) that forms an extensive high-affinity interaction surface for pan2.UniRule annotation

<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 protein kinase superfamily. PAN3 family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri26 – 55C3H1-typeUniRule annotationAdd BLAST30

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000007619

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q5BFB1

KEGG Orthology (KO)

More...
KOi
K12572

Database of Orthologous Groups

More...
OrthoDBi
1515085at2759

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_03181 PAN3, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR030844 PAN3
IPR041332 Pan3_PK
IPR000719 Prot_kinase_dom
IPR000571 Znf_CCCH

The PANTHER Classification System

More...
PANTHERi
PTHR12272 PTHR12272, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF18101 Pan3_PK, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS50103 ZF_C3H1, 1 hit

<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.

Q5BFB1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASVGKPSLE DARRGTGSPK MKARENAKDT LCRNVTIYGR CRYEDKGCAF
60 70 80 90 100
NHDPHKNSNQ SDNASKKRFN VDSPSFTPSL LPSNGSSPTS SSSSLKKSST
110 120 130 140 150
ISPKAANAAP FQPRTAASRS NTSTPGVRQD AVAPDWSVAE AQEFIPQGFD
160 170 180 190 200
PTHMSPLHGN GNPGVASANA FDPFVSTPNP LAAPGAVGPV QANPFSHDAA
210 220 230 240 250
AATLGGAYYA NQAGFQQPVQ YHLYAPIGPH NQNALAYQRN VHDLFLPNDF
260 270 280 290 300
REELQKKAAA TLQTLPNTQL PAQVDYFHSL VPLDLNHQKN AAIFGYPSWV
310 320 330 340 350
YKAQSTKDGS YYALRRLEGF RLTNEKAIRS VQAWKRIASG SMVTIHDAFT
360 370 380 390 400
SRSFQDSSLI FVTDYHPLSK TLAEQHLSAG GPRFQARHNA HVPEQILWGY
410 420 430 440 450
ITQIANALKC IHSAGLAARI IDPSKILLTG RNRIRLNACA IMDVVQYDAQ
460 470 480 490 500
RSVADLQRQD LVNFGQLILT LGANQPNVIH NPSKAMEHFT RAYSPQLKNT
510 520 530 540 550
VMWLLGGMQK DQERNIDILI NGISSQLMST FDSALHLDDQ LTSDLGRELE
560 570 580 590 600
NGRLVRLLTK LNFINERPEH EHDRQWSENG ERFYLKIFRD YVFHQVDASG
610 620 630 640 650
DPVVDLGHVL TCLNKLDAGT DERITLVSRD EQTCFVVSYK ELKKGLESSF
660
QALLRPSRRP H
Length:661
Mass (Da):73,162
Last modified:November 16, 2011 - v3
<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:i117DB622830E046E
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CBF88820 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CBF88822 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence EAA65411 differs from that shown. Reason: Erroneous gene model prediction.Curated

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AACD01000012 Genomic DNA Translation: EAA65411.1 Sequence problems.
BN001308 Genomic DNA Translation: CBF88822.1 Sequence problems.
BN001308 Genomic DNA Translation: CBF88820.1 Sequence problems.

NCBI Reference Sequences

More...
RefSeqi
XP_658373.1, XM_653281.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
EAA65411; EAA65411; AN0769.2

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2876545

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ani:AN0769.2

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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
AACD01000012 Genomic DNA Translation: EAA65411.1 Sequence problems.
BN001308 Genomic DNA Translation: CBF88822.1 Sequence problems.
BN001308 Genomic DNA Translation: CBF88820.1 Sequence problems.
RefSeqiXP_658373.1, XM_653281.1

3D structure databases

SMRiQ5BFB1
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi162425.CADANIAP00001896

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAA65411; EAA65411; AN0769.2
GeneIDi2876545
KEGGiani:AN0769.2

Phylogenomic databases

HOGENOMiHOG000007619
InParanoidiQ5BFB1
KOiK12572
OrthoDBi1515085at2759

Family and domain databases

HAMAPiMF_03181 PAN3, 1 hit
InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR030844 PAN3
IPR041332 Pan3_PK
IPR000719 Prot_kinase_dom
IPR000571 Znf_CCCH
PANTHERiPTHR12272 PTHR12272, 1 hit
PfamiView protein in Pfam
PF18101 Pan3_PK, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS50103 ZF_C3H1, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
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 nameiPAN3_EMENI
<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: Q5BFB1
Secondary accession number(s): C8VQW3, C8VQW4
<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: July 24, 2007
Last sequence update: November 16, 2011
Last modified: May 8, 2019
This is version 95 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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