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UniProtKB/Swiss-Prot entry Q9C169


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CAT3_NEUCR
Primary accession number Q9C169
Secondary accession number Q7RV04
Integrated into Swiss-Prot on May 9, 2003
Sequence was last modified on June 1, 2001 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 56)
Name and origin of the protein
Protein name Catalase-3 [Precursor]
Synonym EC 1.11.1.6
Gene name
Name: cat-3
ORFNames: NCU00355
From
Neurospora crassa [TaxID: 5141] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-58 AND 638-656, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, AND INDUCTION.
STRAIN=74-ORS23-1A;
TISSUE=Mycelium;
DOI=10.1016/S0891-5849(02)00909-7; PubMed=12160934 [NCBI, ExPASy, EBI, Israel, Japan]
Michan S., Lledias F., Baldwin J.D., Natvig D.O., Hansberg W.;
"Regulation and oxidation of two large monofunctional catalases.";
Free Radic. Biol. Med. 33:521-532(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
DOI=10.1038/nature01554; PubMed=12712197 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The genome sequence of the filamentous fungus Neurospora crassa.";
Nature 422:859-868(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AY027544; AAK15807.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AABX02000001; EAA28590.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq XP_957826.1; -.
3D structure databases
HSSP P21179; 1CF9. [HSSP ENTRY / PDB]
ModBase Q9C169.
Protein family/group databases
PeroxiBase 5416; NcKat03.
Enzyme and pathway databases
BioCyc NCRA-XX3-01:NCRA-XX3-01-004065-MON; -.
Ontologies
GO
GO:0004096; Molecular function: catalase activity (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0042744; Biological process: hydrogen peroxide catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002226; Catalase.
IPR010582; Catalase-rel.
IPR011614; Catalase_N.
Graphical view of domain structure.
Gene3D G3DSA:2.40.180.10; Catalase_N; 1.
PANTHER PTHR11465; Catalase; 1.
Pfam PF00199; Catalase; 1.
PF06628; Catalase-rel; 1.
Pfam graphical view of domain structure.
PRINTS PR00067; CATALASE.
ProDom PD000510; Catalase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00437; CATALASE_1; FALSE_NEG.
PS00438; CATALASE_2; 1.
PS51402; CATALASE_3; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 3873876; -.
KEGG ncr:NCU00355; -.
NMPDR fig|5141.1.peg.374; -.
Other
ProtoNet Q9C169.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    18  18     Potential. 
PROPEP   19    30  12      PRO_0000004687
CHAIN   31   719  689     Catalase-3. PRO_0000004688
ACT_SITE   102   102        By similarity. 
ACT_SITE   175   175        By similarity. 
METAL   389   389        Iron (heme axial ligand) (By similarity). 
Sequence information
Length: 719 AA [This is the length of the unprocessed precursor] Molecular weight: 79228 Da [This is the MW of the unprocessed precursor] CRC64: 72790DE3310B64D0 [This is a checksum on the sequence]
        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 

Q9C169 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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