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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-Experimental evidence at protein leveli

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri76 – 10126C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri112 – 13625C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri142 – 16423C2H2-type 3PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Gene namesi
Name:pacC
ORF Names:AN2855
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000000560 Componenti: Chromosome VI
  • UP000005890 Componenti: Partially assembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi259 – 2591L → R: Prevents intramolecular interactions, resulting in the 'open' conformation protein committed to processing independent on ambient pH. 1 Publication
Mutagenesisi266 – 2661L → F: Prevents intramolecular interactions, resulting in the 'open' conformation protein committed to processing independent on ambient pH. 1 Publication
Mutagenesisi340 – 3401L → S: Prevents intramolecular interactions, resulting in the 'open' conformation protein committed to processing independent on ambient pH. 2 Publications
Mutagenesisi455 – 4551Y → 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 Publication
Mutagenesisi498 – 4981L → F: Partially reduces proteolytic cleavage of the full-length translation product by signaling protease. 1 Publication
Mutagenesisi498 – 4981L → S: Completely prevents proteolytic cleavage of the full-length translation product by signaling protease. 1 Publication
Mutagenesisi573 – 5731R → W: Prevents intramolecular interactions, resulting in the 'open' conformation protein committed to processing independent on ambient pH. 1 Publication
Mutagenesisi579 – 5791R → G or T: Prevents intramolecular interactions, resulting in the 'open' conformation protein committed to processing independent on ambient pH. 1 Publication
Mutagenesisi662 – 6621Y → 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 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 678678pH-response transcription factor pacC/RIM101 closed formPRO_0000046832Add
BLAST
Chaini1 – ?493493pH-response transcription factor pacC/RIM101 open form 2PRO_0000312590Add
BLAST
Chaini1 – ?252252pH-response transcription factor pacC/RIM101 open form 1PRO_0000312589Add
BLAST
Propeptidei?253 – ?493241Removed in open form 1; by processing proteasePRO_0000312591Add
BLAST
Propeptidei?494 – 678185Removed in open form 2; by signaling proteasePRO_0000312592Add
BLAST

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

Expressioni

Inductioni

By alkaline conditions.1 Publication

Interactioni

Subunit structurei

Binds to DNA. Interacts with palA, which binds to the two YPX[LI] motifs and is required for proteolytic processing.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ00202.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni169 – 301133Interacting region AAdd
BLAST
Regioni252 – 2543Processing protease cleavage
Regioni334 – 41077Interacting region BAdd
BLAST
Regioni479 – 50224Signaling protease boxAdd
BLAST
Regioni493 – 5008Signaling protease cleavage
Regioni529 – 59264Interacting region CAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi158 – 1647Nuclear localization signal
Motifi455 – 4584YPX[LI] motif 1
Motifi662 – 6654YPX[LI] motif 2

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi41 – 5111Poly-AlaAdd
BLAST
Compositional biasi593 – 61826Asp/Gln/Glu-rich (acidic)Add
BLAST

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

Sequence similaritiesi

Belongs to the pacC/RIM101 family.Curated
Contains 3 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri76 – 10126C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri112 – 13625C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri142 – 16423C2H2-type 3PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

HOGENOMiHOG000198116.
InParanoidiQ00202.
OrthoDBiEOG092C1EDI.

Family and domain databases

Gene3Di3.30.160.60. 2 hits.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 3 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 2 hits.
PS50157. ZINC_FINGER_C2H2_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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
Checksum:i7B626632C8366342
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti189 – 1891G → F in EAA63426 (PubMed:16372000).Curated
Sequence conflicti189 – 1891G → F in CBF83867 (PubMed:16372000).Curated

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.

Genome annotation databases

EnsemblFungiiCADANIAT00010235; CADANIAP00010235; CADANIAG00010235.
EAA63426; EAA63426; AN2855.2.
GeneIDi2873843.
KEGGiani:AN2855.2.

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

ProteinModelPortaliQ00202.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00010235; CADANIAP00010235; CADANIAG00010235.
EAA63426; EAA63426; AN2855.2.
GeneIDi2873843.
KEGGiani:AN2855.2.

Phylogenomic databases

HOGENOMiHOG000198116.
InParanoidiQ00202.
OrthoDBiEOG092C1EDI.

Family and domain databases

Gene3Di3.30.160.60. 2 hits.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 3 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 2 hits.
PS50157. ZINC_FINGER_C2H2_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPACC_EMENI
AccessioniPrimary (citable) accession number: Q00202
Secondary accession number(s): C8VJC9, Q5B9C5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: November 1, 1996
Last modified: September 7, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.