ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9VWP4


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name SUOX_DROME
Primary accession number Q9VWP4
Secondary accession numbers None
Integrated into Swiss-Prot on November 15, 2002
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 64)
Name and origin of the protein
Protein name Probable sulfite oxidase, mitochondrial [Precursor]
Synonym EC 1.8.3.1
Gene name
ORFNames: CG7280
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2]
GENOME REANNOTATION.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
TISSUE=Embryo;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
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
AE014298; AAF48894.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY069352; AAL39497.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_573331.1; -.
UniGene Dm.213
3D structure databases
HSSP P07850; 1SOX. [HSSP ENTRY / PDB]
ModBase Q9VWP4.
Enzyme and pathway databases
BioCyc DMEL-XXX-02:DMEL-XXX-02-002532-MON; -.
Organism-specific databases
FlyBase FBgn0030966; CG7280.
Gene expression databases
ArrayExpress Q9VWP4; -.
GermOnline CG7280; Drosophila melanogaster.
Ontologies
GO
GO:0005758; Cellular component: mitochondrial intermembrane space (non-traceable author statement from UniProtKB).
GO:0008482; Molecular function: sulfite oxidase activity (non-traceable author statement from UniProtKB).
GO:0030163; Biological process: protein catabolic process (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001199; Cyt_B5.
IPR005066; MoCF_OxRdtse_dimer.
IPR008335; Mopterin_OxRdtase_euk.
IPR000572; OxRdtase_Mopterin-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.10.120.10; Cyt_B5; 1.
G3DSA:2.60.40.650; MoCF_oxrdtse_dimer; 1.
G3DSA:3.90.420.10; Oxred_molyb_bd; 1.
Pfam PF00173; Cyt-b5; 1.
PF03404; Mo-co_dimer; 1.
PF00174; Oxidored_molyb; 1.
Pfam graphical view of domain structure.
PRINTS PR00363; CYTOCHROMEB5.
PR00407; EUMOPTERIN.
ProDom PD000612; Cyt_B5; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00191; CYTOCHROME_B5_1; 1.
PS50255; CYTOCHROME_B5_2; 1.
PS00559; MOLYBDOPTERIN_EUK; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9VWP4.
Genome annotation databases
Ensembl CG7280; Drosophila melanogaster. [Contig view]
GeneID 32878; -.
KEGG dme:Dmel_CG7280; -.
NMPDR fig|7227.3.peg.18553; -.
Phylogenomic databases
HOGENOM Q9VWP4; -.
Other
ProtoNet Q9VWP4.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Heme; Iron; Metal-binding; Mitochondrion; Molybdenum; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1     ?        Mitochondrion. 
CHAIN   ?   573        Probable sulfite oxidase, mitochondrial. PRO_0000006485
DOMAIN   108   186  79     Cytochrome b5 heme-binding. 
REGION   187   206  20     Hinge (By similarity). 
REGION   207   573  367     Molybdenum-pterin domain (By similarity). 
REGION   240   244  5     Molybdenum-pterin-binding (By similarity). 
REGION   342   344  3     Molybdenum-pterin-binding (By similarity). 
REGION   388   401  14     Molybdenum-pterin-binding (By similarity). 
METAL   144   144        Iron (heme axial ligand) (By similarity). 
METAL   168   168        Iron (heme axial ligand) (By similarity). 
METAL   287   287        Molybdenum-pterin (By similarity). 
Sequence information
Length: 573 AA [This is the length of the unprocessed precursor] Molecular weight: 64346 Da [This is the MW of the unprocessed precursor] CRC64: 71AB1D2B3465D811 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRLLRPSWAG LLRGRHHQHQ RHHRRLLLTT SRGSNGEREE QQHSQWSSPG SRSEQLFYAA 

        70         80         90        100        110        120 
FWAGGLTLGY HWLTDKKNHV LLEGQKVASE EELEATARLW HVTNRRELPT YRAEEVEQHN 

       130        140        150        160        170        180 
SVEKRIWVTY GLGVYDVTDF VENHPGGDKI LMAAGSAIDP FWGIYQQHNT LEVLELLEGF 

       190        200        210        220        230        240 
RIGNLEGLVV TNVDDELGSP WSQEPQRHAL LKPASKRPFN AEPPIGLLAE QFYTPNELFY 

       250        260        270        280        290        300 
VRNHLPVPVI NPEDYELEIE GGAKDKTLTL DGIKALPKHS VTAAIMCGGN RRSEMTKVKA 

       310        320        330        340        350        360 
VKGLSWGAGA VGNAKWSGAR LCDILREQGV QPDETKHVIF EGADLDPTSH PYGASIPLAK 

       370        380        390        400        410        420 
ALDPRGDVIL AYEMNDEPLS RDHGFPIRVI VPGTVGARNV KWLTRIVVAD KESDSHWQQN 

       430        440        450        460        470        480 
DYKGFSPSTD WDTVDFSKSD AIQAMPVTSA ICTPQPGARV KVDDDEGHIT VRGYAWSGGG 

       490        500        510        520        530        540 
RKIVRVDLTN DEGVSWHVAE LEQEEMPDGR HYGWSLWTAR LPVSEAQRRA GDVEIWAKAV 

       550        560        570 
DSAYNVQPEK FEHIWNLRGV LANAYHKVKV KII 

Q9VWP4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
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

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by kr flag YPRC Korea Mirror sites: Australia  Brazil  Canada  China  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!