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Reviewed, UniProtKB/Swiss-Prot P37193 (ADXH_DROME)

Last modified November 24, 2009. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Adrenodoxin-like protein, mitochondrial
Gene names
Name: Fdxh
ORF Names: CG4205
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length172 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Cofactor

Binds 1 2Fe-2S cluster By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the adrenodoxin/putidaredoxin family.

Contains 1 2Fe-2S ferredoxin-type domain.

Sequence caution

The sequence CAB55551.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processElectron transport
Transport
   Cellular componentMitochondrion
   DomainTransit peptide
   Ligand2Fe-2S
Iron
Iron-sulfur
Metal-binding
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processelectron transport chain

Inferred from electronic annotation. Source: UniProtKB-KW

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function2 iron, 2 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

electron carrier activity

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion
Chain? – 172Adrenodoxin-like protein, mitochondrialPRO_0000000993

Regions

Domain57 – 1591032Fe-2S ferredoxin-type

Sites

Metal binding941Iron-sulfur (2Fe-2S) By similarity
Metal binding1001Iron-sulfur (2Fe-2S) By similarity
Metal binding1031Iron-sulfur (2Fe-2S) By similarity
Metal binding1401Iron-sulfur (2Fe-2S) By similarity

Experimental info

Sequence conflict159 – 17214TRNFY…KPKPH → PGTSTSMGTSPSHINIIVIS RIINNI Ref.1
Sequence conflict1611N → D in AAM29625. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P37193-1 [UniParc].

Last modified August 15, 2003. Version 3.
Checksum: 9D70F51572562E2F

FASTA17219,734
        10         20         30         40         50         60 
MFCLLLRRSA VHNSCKLISK QIAKPAFYTP HNALHTTIPR RHGEFEWQDP KSTDEIVNIT 

        70         80         90        100        110        120 
YVDKDGKRTK VQGKVGDNVL YLAHRHGIEM EGACEASLAC TTCHVYVQHD YLQKLKEAEE 

       130        140        150        160        170 
QEDDLLDMAP FLRENSRLGC QILLDKSMEG MELELPKATR NFYVDGHKPK PH 

« Hide

References

« Hide 'large scale' references
[1]"A Drosophila heat shock gene from locus 67B is expressed during embryogenesis and pupation."
Pauli D., Tonka C.H.
J. Mol. Biol. 198:235-240(1987) [PubMed: 3123699] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The genome sequence of Drosophila melanogaster."
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. expand/collapse author list , 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.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
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. expand/collapse author list , 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.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[4]"A Drosophila full-length cDNA resource."
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.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Head.
[5]Rudd K.E.
Unpublished observations (JUL-1994)
Cited for: IDENTIFICATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

X06542 Genomic DNA. Translation: CAB55551.1. Sequence problems.
AE014296 Genomic DNA. Translation: AAF50293.2.
AY113620 mRNA. Translation: AAM29625.1.
RefSeqNP_523993.1.
UniGeneDm.31181

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGP37193.

Genome annotation databases

EnsemblFBtr0076498; FBpp0076226; FBgn0011769; Drosophila melanogaster. [Genome view]
GeneID39070.
KEGGdme:Dmel_CG4205.
NMPDRfig|7227.3.peg.9034.
UCSCCG4205-RA. d. melanogaster.

Organism-specific databases

CTD39070.
FlyBaseFBgn0011769. Fdxh.

Phylogenomic databases

HOGENOMP37193.
OMADMAPALK
OrthoDBEOG95DWW6

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-015930-MON.

Gene expression databases

BgeeP37193.
GermOnlineCG4205. Drosophila melanogaster.

Family and domain databases

InterProIPR001055. Adrenodoxin.
IPR018298. Adrenodoxin_Fe-S_BS.
IPR012675. b-grasp_ferredoxin-like.
IPR001041. Ferredoxin.
[Graphical view]
Gene3DG3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
PfamPF00111. Fer2. 1 hit.
[Graphical view]
PRINTSPR00355. ADRENODOXIN.
PROSITEPS51085. 2FE2S_FER_2. 1 hit.
PS00814. ADX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio811775.

Entry information

Entry nameADXH_DROME
AccessionPrimary (citable) accession number: P37193
Secondary accession number(s): Q8MYT2, Q9VSW8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: August 15, 2003
Last modified: November 24, 2009
This is version 86 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents