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Entry version 122 (12 Aug 2020)
Sequence version 1 (01 Nov 1996)
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Protein

pH-response transcription factor pacC/RIM101

Gene

pacC

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
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

Transcription factor that mediates regulation of both acid- and alkaline-expressed genes in response to ambient pH. At alkaline ambient pH, activates transcription of alkaline-expressed genes (including pacC itself) and represses transcription of acid-expressed genes. Specifically recognizes and binds the consensus sequence 5'-GCCARG-3'. Required for virulence in invasive pulmonary aspergillosis (IPA).3 Publications

Caution

Met-5 is the major initiator, but Met-1 may also be used.Curated

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 fingeri76 – 101C2H2-type 1PROSITE-ProRule annotationAdd BLAST26
Zinc fingeri112 – 136C2H2-type 2PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri142 – 164C2H2-type 3PROSITE-ProRule annotationAdd BLAST23

<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 functionActivator, DNA-binding, Repressor
Biological processTranscription, Transcription regulation
LigandMetal-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%5Fand%5Ftaxonomy%5Fsection">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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:pacC
ORF Names:AN2855
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillusAspergillus subgen. Nidulantes
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 VI
  • 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

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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi259L → R: Prevents intramolecular interactions, resulting in the 'open' conformation protein committed to processing independent on ambient pH. 1 Publication1
Mutagenesisi266L → F: Prevents intramolecular interactions, resulting in the 'open' conformation protein committed to processing independent on ambient pH. 1 Publication1
Mutagenesisi340L → S: Prevents intramolecular interactions, resulting in the 'open' conformation protein committed to processing independent on ambient pH. 2 Publications1
Mutagenesisi455Y → D: Abolishes interaction with palA. Severely reduces proteolytic processing of the full-length translation product by signaling protease, causing a stringent loss-of-function, acidity-mimicking phenotype. 1 Publication1
Mutagenesisi498L → F: Partially reduces proteolytic cleavage of the full-length translation product by signaling protease. 1 Publication1
Mutagenesisi498L → S: Completely prevents proteolytic cleavage of the full-length translation product by signaling protease. 1 Publication1
Mutagenesisi573R → W: Prevents intramolecular interactions, resulting in the 'open' conformation protein committed to processing independent on ambient pH. 1 Publication1
Mutagenesisi579R → G or T: Prevents intramolecular interactions, resulting in the 'open' conformation protein committed to processing independent on ambient pH. 1 Publication1
Mutagenesisi662Y → N: Abolishes interaction with palA. Partially reduces proteolytic processing of the full-length translation product by signaling protease, causing a weak loss-of-function phenotype. 1 Publication1

Miscellaneous databases

Pathogen-Host Interaction database

More...
PHI-basei
PHI:398

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000468321 – 678pH-response transcription factor pacC/RIM101 closed formAdd BLAST678
ChainiPRO_00003125901 – ?493pH-response transcription factor pacC/RIM101 open form 2Add BLAST493
ChainiPRO_00003125891 – ?252pH-response transcription factor pacC/RIM101 open form 1Add BLAST252
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000312591?253 – ?493Removed in open form 1; by processing proteaseAdd BLAST241
PropeptideiPRO_0000312592?494 – 678Removed in open form 2; by signaling proteaseAdd BLAST185

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Activated by C-terminal proteolytic cleavage. At neutral to alkaline ambient pH, the signaling protease (probably palB) cleaves pacC within the conserved 24-residue signaling protease box, removing the C-terminal interacting region C and producing a 53 kDa 'open' conformation intermediate protein, which is committed to further processing. In an ambient pH-independent reaction, the processing protease (probably the proteasome) removes additional C-terminal residues to yield the 27 kDa functional form.2 Publications

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By alkaline conditions.1 Publication

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Binds to DNA.

Interacts with palA, which binds to the two YPX[LI] motifs and is required for proteolytic processing.

1 Publication

Protein-protein interaction databases

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
Q00202

STRING: functional protein association networks

More...
STRINGi
162425.CADANIAP00010235

<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
Q00202

Database of comparative protein structure models

More...
ModBasei
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>Regioni169 – 301Interacting region AAdd BLAST133
Regioni252 – 254Processing protease cleavage3
Regioni334 – 410Interacting region BAdd BLAST77
Regioni479 – 502Signaling protease boxAdd BLAST24
Regioni493 – 500Signaling protease cleavage8
Regioni529 – 592Interacting region CAdd BLAST64

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>Motifi158 – 164Nuclear localization signal7
Motifi455 – 458YPX[LI] motif 14
Motifi662 – 665YPX[LI] motif 24

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi41 – 51Poly-AlaAdd BLAST11
Compositional biasi593 – 618Asp/Gln/Glu-rich (acidic)Add BLAST26

<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

Only zinc fingers 2 and 3 contact DNA. Zinc finger 1 interacts with zinc finger 2.1 Publication
Interacting regions A, B and C form intramolecular interactions in the full-length translation product at acidic ambient pH, keeping the protein in a 'closed' conformation preventing proteolytic cleavage by the processing protease.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 pacC/RIM101 family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri76 – 101C2H2-type 1PROSITE-ProRule annotationAdd BLAST26
Zinc fingeri112 – 136C2H2-type 2PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri142 – 164C2H2-type 3PROSITE-ProRule annotationAdd BLAST23

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1721, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_012842_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q00202

Database of Orthologous Groups

More...
OrthoDBi
507875at2759

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036236, Znf_C2H2_sf
IPR013087, Znf_C2H2_type

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00096, zf-C2H2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00355, ZnF_C2H2, 3 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF57667, SSF57667, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00028, ZINC_FINGER_C2H2_1, 2 hits
PS50157, ZINC_FINGER_C2H2_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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q00202-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLGAMAEEAV APVAVPTTQE QPTSQPAAAQ VTTVTSPSVT ATAAAATAAV
60 70 80 90 100
ASPQANGNAA SPVAPASSTS RPAEELTCMW QGCSEKLPTP ESLYEHVCER
110 120 130 140 150
HVGRKSTNNL NLTCQWGSCR TTTVKRDHIT SHIRVHVPLK PHKCDFCGKA
160 170 180 190 200
FKRPQDLKKH VKTHADDSVL VRSPEPGSRN PDMMFGGNGK GYAAAHYFEP
210 220 230 240 250
ALNPVPSQGY AHGPPQYYQA HHAPQPSNPS YGNVYYALNT GPEPHQASYE
260 270 280 290 300
SKKRGYDALN EFFGDLKRRQ FDPNSYAAVG QRLLSLQNLS LPVLTAAPLP
310 320 330 340 350
EYQAMPAPVA VASGPYGGGP HPAPAYHLPP MSNVRTKNDL INIDQFLQQM
360 370 380 390 400
QDTIYENDDN VAAAGVAQPG AHYIHNGISY RTTHSPPTQL PSAHATTQTT
410 420 430 440 450
AGPIISNTSA HSPSSSTPAL TPPSSAQSYT SGRSPISLPS AHRVSPPHES
460 470 480 490 500
GSSMYPRLPS ATDGMTSGYT AASSAAPPST LGGIFDNDER RRYTGGTLQR
510 520 530 540 550
ARPASRAASE SMDLSSDDKE SGERTPKQIS ASLIDPALHS GSPGEDDVTR
560 570 580 590 600
TAKAATEVAE RSDVQSEWVE KVRLIEYLRN YIANRLERGE FSDDSEQEQD
610 620 630 640 650
QEQEQDQEQE QDQEQGQDRV SRSPVSKADV DMEGVERDSL PRSPRTVPIK
660 670
TDGESAEDSV MYPTLRGLDE DGDSKMPS
Length:678
Mass (Da):72,939
Last modified:November 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:i7B626632C8366342
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti189G → F in EAA63426 (PubMed:16372000).Curated1
Sequence conflicti189G → F in CBF83867 (PubMed:16372000).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Z47081 Genomic DNA Translation: CAA87390.1
AACD01000051 Genomic DNA Translation: EAA63426.1
BN001306 Genomic DNA Translation: CBF83867.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S54308

NCBI Reference Sequences

More...
RefSeqi
XP_660459.1, XM_655367.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
EAA63426; EAA63426; AN2855.2

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2873843

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ani:AN2855.2

<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
Z47081 Genomic DNA Translation: CAA87390.1
AACD01000051 Genomic DNA Translation: EAA63426.1
BN001306 Genomic DNA Translation: CBF83867.1
PIRiS54308
RefSeqiXP_660459.1, XM_655367.1

3D structure databases

SMRiQ00202
ModBaseiSearch...

Protein-protein interaction databases

ELMiQ00202
STRINGi162425.CADANIAP00010235

Genome annotation databases

EnsemblFungiiEAA63426; EAA63426; AN2855.2
GeneIDi2873843
KEGGiani:AN2855.2

Phylogenomic databases

eggNOGiKOG1721, Eukaryota
HOGENOMiCLU_012842_1_0_1
InParanoidiQ00202
OrthoDBi507875at2759

Miscellaneous databases

PHI-baseiPHI:398

Family and domain databases

InterProiView protein in InterPro
IPR036236, Znf_C2H2_sf
IPR013087, Znf_C2H2_type
PfamiView protein in Pfam
PF00096, zf-C2H2, 1 hit
SMARTiView protein in SMART
SM00355, ZnF_C2H2, 3 hits
SUPFAMiSSF57667, SSF57667, 2 hits
PROSITEiView protein in PROSITE
PS00028, ZINC_FINGER_C2H2_1, 2 hits
PS50157, ZINC_FINGER_C2H2_2, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiPACC_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: Q00202
Secondary accession number(s): C8VJC9, Q5B9C5
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: November 1, 1996
Last modified: August 12, 2020
This is version 122 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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