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Protein

Alpha-ketoglutarate-dependent dioxygenase abh1

Gene

abh1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Putative dioxygenase that may repair alkylated DNA or RNA by oxidative demethylation. Requires molecular oxygen, alpha-ketoglutarate and iron (By similarity).By similarity

Cofactori

Fe2+Note: Binds 1 Fe2+ ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei142 – 1421SubstrateBy similarity
Metal bindingi205 – 2051Iron; catalyticPROSITE-ProRule annotation
Metal bindingi207 – 2071Iron; catalyticPROSITE-ProRule annotation
Binding sitei235 – 2351SubstrateBy similarity
Metal bindingi261 – 2611Iron; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-ketoglutarate-dependent dioxygenase abh1 (EC:1.14.11.-)
Alternative name(s):
Alkylated DNA repair protein alkB homolog
Gene namesi
Name:abh1
ORF Names:SPBC13G1.04c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC13G1.04c.
PomBaseiSPBC13G1.04c. abh1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 302302Alpha-ketoglutarate-dependent dioxygenase abh1PRO_0000066669Add
BLAST

Proteomic databases

MaxQBiO60066.

Interactioni

Protein-protein interaction databases

BioGridi276479. 8 interactions.
MINTiMINT-4676892.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini187 – 299113Fe2OG dioxygenasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni149 – 1513Substrate bindingBy similarity
Regioni194 – 1963Alpha-ketoglutarate bindingBy similarity
Regioni290 – 2967Alpha-ketoglutarate bindingBy similarity

Sequence similaritiesi

Belongs to the alkB family.Curated
Contains 1 Fe2OG dioxygenase domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000215431.
InParanoidiO60066.
OMAiMLESIFT.
OrthoDBiEOG75F4PF.

Family and domain databases

Gene3Di2.60.120.590. 1 hit.
InterProiIPR004574. Alkb.
IPR027450. AlkB-like.
IPR005123. Oxoglu/Fe-dep_dioxygenase.
[Graphical view]
PANTHERiPTHR16557. PTHR16557. 1 hit.
PfamiPF13532. 2OG-FeII_Oxy_2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00568. alkb. 1 hit.
PROSITEiPS51471. FE2OG_OXY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O60066-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLAGNMEQAN VFRLEEKRYK CRADTIPDMS EVLDPNDPQS FGFEALVEIK
60 70 80 90 100
PRVFSFQKAP GLLILKNYVS SELQMQLLKS IMFTQIQDPE NKTNLSPFYQ
110 120 130 140 150
LPLGNDSIWR RYYNGDGESI IDGLGETKPL TVDRLVHKKL RWVTLGEQYD
160 170 180 190 200
WTTKEYPDPS KSPGFPKDLG DFVEKVVKES TDFLHWKAEA AIVNFYSPGD
210 220 230 240 250
TLSAHIDESE EDLTLPLISL SMGLDCIYLI GTESRSEKPS ALRLHSGDVV
260 270 280 290 300
IMTGTSRKAF HAVPKIIPNS TPNYLLTGNK AWDGWISRKR VNFNVRQVRP

SR
Length:302
Mass (Da):34,348
Last modified:October 3, 2012 - v3
Checksum:iB4FD6B9D7618276C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA18657.3.
AB548892 mRNA. Translation: BAI81891.1.
PIRiT39405.
RefSeqiNP_596553.3. NM_001022474.3.

Genome annotation databases

GeneIDi2539935.
KEGGispo:SPBC13G1.04c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA18657.3.
AB548892 mRNA. Translation: BAI81891.1.
PIRiT39405.
RefSeqiNP_596553.3. NM_001022474.3.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276479. 8 interactions.
MINTiMINT-4676892.

Proteomic databases

MaxQBiO60066.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2539935.
KEGGispo:SPBC13G1.04c.

Organism-specific databases

EuPathDBiFungiDB:SPBC13G1.04c.
PomBaseiSPBC13G1.04c. abh1.

Phylogenomic databases

HOGENOMiHOG000215431.
InParanoidiO60066.
OMAiMLESIFT.
OrthoDBiEOG75F4PF.

Miscellaneous databases

PROiO60066.

Family and domain databases

Gene3Di2.60.120.590. 1 hit.
InterProiIPR004574. Alkb.
IPR027450. AlkB-like.
IPR005123. Oxoglu/Fe-dep_dioxygenase.
[Graphical view]
PANTHERiPTHR16557. PTHR16557. 1 hit.
PfamiPF13532. 2OG-FeII_Oxy_2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00568. alkb. 1 hit.
PROSITEiPS51471. FE2OG_OXY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Comparative functional genomics of the fission yeasts."
    Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.
    , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
    Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVISION OF GENE MODEL.
  3. "cDNA cloning of an AlkB homolog from Schizosaccharomyces pombe."
    Inatani S., Kanamitsu K., Ikeda S.
    Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-302.

Entry informationi

Entry nameiALKBH_SCHPO
AccessioniPrimary (citable) accession number: O60066
Secondary accession number(s): D3KZ45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 3, 2012
Last modified: June 8, 2016
This is version 96 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.