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UniProtKB/Swiss-Prot entry Q2HG02


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

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Entry information
Entry name MCR1_CHAGB
Primary accession number Q2HG02
Secondary accession numbers None
Integrated into Swiss-Prot on April 29, 2008
Sequence was last modified on March 21, 2006 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 18)
Name and origin of the protein
Protein name NADH-cytochrome b5 reductase 2
Synonyms EC 1.6.2.2
Mitochondrial cytochrome b reductase
Gene name
Name: MCR1
ORFNames: CHGG_00852
From
Chaetomium globosum (Soil fungus) [TaxID: 38033] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / IFO 6347 / NRRL 1970;
Birren B.W., Lander E.S., Galagan J.E., Devon K., Nusbaum C., Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C., Kodira C.D., Yandava C., Zeng Q., Alvarado L., Oleary S., Untereiner W.;
"Annotation of the Chaetomium globosum CBS 148.51 genome.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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
CH408029; EAQ92617.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq XP_001220073.1; -.
3D structure databases
ModBase Q2HG02.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005741; Cellular component: mitochondrial outer membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0004128; Molecular function: cytochrome-b5 reductase activity (inferred from electronic annotation from EC).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001834; Cyt_B5_reductase.
IPR001709; FPN_cyt_redctse.
IPR008333; OxRdtase_FAD-bd.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.
Pfam PF00970; FAD_binding_6; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00406; CYTB5RDTASE.
PR00371; FPNCR.
PROSITE PS51384; FAD_FR; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q2HG02.
Genome annotation databases
GeneID 4388100; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane; NAD; Oxidoreductase; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   348  348     NADH-cytochrome b5 reductase 2. PRO_0000330178
TRANSMEM   41    61  21     Potential. 
DOMAIN   97   202  106     FAD-binding FR-type. 
NP_BIND   205   240  36     FAD (By similarity). 
Sequence information
Length: 348 AA [This is the length of the unprocessed precursor] Molecular weight: 38131 Da [This is the MW of the unprocessed precursor] CRC64: 812F98E27939A0E7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSLFVASRSA FRAAAPLKRQ FQIRRYATEP PSADAKKGNN TLLYGAAAAA VAGAGYYFLG 

        70         80         90        100        110        120 
GTPAAKKAEE KVKDASSAAA GKLSTSEVKQ ALTGGEQGWV SLKLEEVEIV NHNSKRLRFR 

       130        140        150        160        170        180 
LPEDDMVSGV HVASAILTKF KPVDAEKPVI RPYTPTNDED ARGYLDLLVK KYPNGPMSTH 

       190        200        210        220        230        240 
LHDMVPGQRL DVKGPLPKYP WTANKHGHIA LVAGGTGITP MFQLCRAIFN NPDDQTKVTL 

       250        260        270        280        290        300 
VFGNVREDDI LLKKELAALE NNNPRRFRAF YVLDDPPKHW TGGKGFITKD LLKTVLPEPK 

       310        320        330        340 
DENIKVFVCG PPGMMDAISG NKKSPKDQGE LKGILKELGY SPEQVYKF 

Q2HG02 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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