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Q9C169 (CAT3_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length719 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide By similarity.

Catalytic activity

2 H2O2 = O2 + 2 H2O. Ref.1

Cofactor

Heme group.

Developmental stage

Activity is predominant during late exponential growth and at the start of the conidiation process. Ref.1

Induction

Induced under stress conditions, such as H2O2, paraquat, cadmium, heat shock, uric acid and nitrate treatment. Ref.1

Sequence similarities

Belongs to the catalase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 3012
PRO_0000004687
Chain31 – 719689Catalase-3
PRO_0000004688

Sites

Active site1021 By similarity
Active site1751 By similarity
Metal binding3891Iron (heme axial ligand) By similarity

Secondary structure

............................................................................................................................ 719
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9C169 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 72790DE3310B64D0

FASTA71979,228
        10         20         30         40         50         60 
MRVNALLPLS GLIGTALAAC PFADPSALGR RAEGGEVDAR QRLKEVEVDD NGQFMTTDFG 

        70         80         90        100        110        120 
GNIEEQFSLK AGGRGSTLLE DFIFRQKLQH FDHERIPERV VHARGAGAHG IFTSYGDWSN 

       130        140        150        160        170        180 
ITAASFLGAK DKQTPVFVRF STVAGSRGSA DTARDVHGFA TRFYTDEGNF DIVGNNIPVF 

       190        200        210        220        230        240 
FIQDAIRFPD LIHSVKPSPD NEVPQAATAH DSAWDFFSSQ PSALHTLFWA MSGNGIPRSY 

       250        260        270        280        290        300 
RHMDGFGIHT FRLVTEDGKS KLVKWHWKTK QGKAALVWEE AQVLAGKNAD FHRQDLWDAI 

       310        320        330        340        350        360 
ESGNAPSWEL AVQLIDEDKA QAYGFDLLDP TKFLPEEFAP LQVLGEMTLN RNPMNYFAET 

       370        380        390        400        410        420 
EQISFQPGHI VRGVDFTEDP LLQGRLYSYL DTQLNRHRGP NFEQLPINRP VSGVHNNHRD 

       430        440        450        460        470        480 
GQGQAWIHKN IHHYSPSYLN KGYPAQANQT VGRGFFTTPG RTASGVLNRE LSATFDDHYT 

       490        500        510        520        530        540 
QPRLFFNSLT PVEQQFVINA IRFEASHVTN EQVKKNVLEQ LNKISNDVAK RVAVALGLEA 

       550        560        570        580        590        600 
PQPDPTYYHN NVTRGVSIFN ESLPTIATLR VGVLSTTKGG SLDKAKALKE QLEKDGLKVT 

       610        620        630        640        650        660 
VIAEYLASGV DQTYSAADAT AFDAVVVAEG AERVFSGKGA MSPLFPAGRP SQILTDGYRW 

       670        680        690        700        710 
GKPVAAVGSA KKALQSIGVE EKEAGVYAGA QDEVIKGVEE GLKVFKFLER FAVDGDDEE 

« Hide

References

« Hide 'large scale' references
[1]"Regulation and oxidation of two large monofunctional catalases."
Michan S., Lledias F., Baldwin J.D., Natvig D.O., Hansberg W.
Free Radic. Biol. Med. 33:521-532(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-58 AND 638-656, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, INDUCTION.
Strain: 74-ORS23-1A.
Tissue: Mycelium.
[2]"The genome sequence of the filamentous fungus Neurospora crassa."
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. expand/collapse author list , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY027544 Genomic DNA. Translation: AAK15807.1.
CM002238 Genomic DNA. Translation: EAA28590.1.
RefSeqXP_957826.1. XM_952733.2.
UniGeneNcr.16984.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EJ6X-ray2.30A/B/C/D32-719[»]
3ZJ4X-ray3.10A/B/C/D1-719[»]
3ZJ5X-ray1.95A/B/C/D1-719[»]
4AJ9X-ray1.85A/B/C/D38-719[»]
4BIMX-ray2.95A/B/C/D1-719[»]
ProteinModelPortalQ9C169.
SMRQ9C169. Positions 40-714.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9C169. 1 interaction.
MINTMINT-2515988.
STRING5141.NCU00355.1.

Protein family/group databases

PeroxiBase5416. NcKat03.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEFNCRT00000000465; EFNCRP00000000465; EFNCRG00000000465.
GeneID3873876.
KEGGncr:NCU00355.

Phylogenomic databases

eggNOGCOG0753.
HOGENOMHOG000087851.
KOK03781.
OrthoDBEOG7K9KBN.

Family and domain databases

Gene3D2.40.180.10. 1 hit.
3.40.50.880. 1 hit.
InterProIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024712. Catalase_clade2.
IPR011614. Catalase_core.
IPR010582. Catalase_immune_responsive.
IPR029062. Class_I_gatase-like.
[Graphical view]
PANTHERPTHR11465. PTHR11465. 1 hit.
PfamPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFPIRSF038927. Catalase_clade2. 1 hit.
PRINTSPR00067. CATALASE.
SMARTSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMSSF56634. SSF56634. 1 hit.
PROSITEPS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9C169.

Entry information

Entry nameCAT3_NEUCR
AccessionPrimary (citable) accession number: Q9C169
Secondary accession number(s): Q7RV04
Entry history
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: June 1, 2001
Last modified: June 11, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references