Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Alkyltransferase-like protein 1

Gene

atl1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in DNA damage recognition. Binds DNA containing O(6)-methylguanine and larger O(6)-alkylguanine adducts. The DNA is bent, the damaged base is rotated out of the DNA duplex into a hydrophobic binding pocket (nucleotide flipping), with Arg-39 donating a hydrogen bond to the orphaned cytosine to stabilize the extrahelical DNA conformation. This structural change in DNA presents the lesion to the nucleotide excision repair (NER) pathway (PubMed:16679453, PubMed:19516334, PubMed:23112169). The affinity for O(6)-alkylguanine adducts increases with the size of the alkyl group. Low affinity small O(6)-alkylguanines are directed to the global genome repair pathway of NER via rhp7-rhp16 and rhp41-rhp23, while strong binding to bulky O(6)-alkylguanines stalls the transcription machinery and diverts the damage to the transcription-coupled repair pathway of NER via rhp26 (PubMed:22658721).4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei25 – 251Required for phosphate rotation/nucleotide flipping1 Publication
Sitei39 – 391Arg finger, required for nucleotide flipping1 Publication
Sitei69 – 691Critical for recognition of O(6)-alkylguanines, probes the electrostatic potential of the flipped base to distinguish between O(6)-alkylguanine and guanine1 Publication

GO - Molecular functioni

  • catalytic activity Source: InterPro
  • damaged DNA binding Source: PomBase
  • O6-alkylguanine-DNA binding Source: PomBase

GO - Biological processi

  • DNA dealkylation involved in DNA repair Source: PomBase
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Alkyltransferase-like protein 11 Publication
Gene namesi
Name:atl11 Publication
ORF Names:SPAC1250.04cImported
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1250.04c.
PomBaseiSPAC1250.04c. atl1.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi69 – 691R → A or F: Reduces discrimination of modified bases 10-100-fold and increases sensitivity toward alkylating agents. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 108108Alkyltransferase-like protein 1PRO_0000249237Add
BLAST

Proteomic databases

MaxQBiQ9UTN9.

Interactioni

Protein-protein interaction databases

BioGridi278199. 18 interactions.
DIPiDIP-60450N.
MINTiMINT-4710996.

Structurei

Secondary structure

1
108
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1412Combined sources
Beta strandi22 – 243Combined sources
Helixi25 – 317Combined sources
Helixi35 – 373Combined sources
Helixi38 – 469Combined sources
Helixi56 – 583Combined sources
Turni62 – 643Combined sources
Beta strandi70 – 723Combined sources
Helixi73 – 8412Combined sources
Beta strandi90 – 923Combined sources
Beta strandi93 – 953Combined sources
Helixi101 – 1044Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GVAX-ray2.00A/B1-108[»]
3GX4X-ray2.70X1-108[»]
3GYHX-ray2.80X1-108[»]
4ENJX-ray3.10A1-108[»]
4ENKX-ray3.04A1-108[»]
4ENMX-ray2.84A1-108[»]
4ENNX-ray2.84A/B1-108[»]
4HDUX-ray2.85A1-108[»]
4HDVX-ray2.70A1-108[»]
ProteinModelPortaliQ9UTN9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UTN9.

Family & Domainsi

Sequence similaritiesi

Belongs to the MGMT family. ATL subfamily.Curated

Phylogenomic databases

HOGENOMiHOG000244138.
InParanoidiQ9UTN9.
KOiK07443.
OMAiTTEGINI.
OrthoDBiEOG7966V1.
PhylomeDBiQ9UTN9.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR014048. MethylDNA_cys_MeTrfase_DNA-bd.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01035. DNA_binding_1. 1 hit.
[Graphical view]
SUPFAMiSSF46767. SSF46767. 1 hit.
TIGRFAMsiTIGR00589. ogt. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9UTN9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRMDEFYTKV YDAVCEIPYG KVSTYGEIAR YVGMPSYARQ VGQAMKHLHP
60 70 80 90 100
ETHVPWHRVI NSRGTISKRD ISAGEQRQKD RLEEEGVEIY QTSLGEYKLN

LPEYMWKP
Length:108
Mass (Da):12,670
Last modified:May 1, 2000 - v1
Checksum:i7F8B3BA12CED07F1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB54827.1.
PIRiT37558.
RefSeqiNP_594858.1. NM_001020287.2.

Genome annotation databases

EnsemblFungiiSPAC1250.04c.1; SPAC1250.04c.1:pep; SPAC1250.04c.
GeneIDi2541704.
KEGGispo:SPAC1250.04c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB54827.1.
PIRiT37558.
RefSeqiNP_594858.1. NM_001020287.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GVAX-ray2.00A/B1-108[»]
3GX4X-ray2.70X1-108[»]
3GYHX-ray2.80X1-108[»]
4ENJX-ray3.10A1-108[»]
4ENKX-ray3.04A1-108[»]
4ENMX-ray2.84A1-108[»]
4ENNX-ray2.84A/B1-108[»]
4HDUX-ray2.85A1-108[»]
4HDVX-ray2.70A1-108[»]
ProteinModelPortaliQ9UTN9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278199. 18 interactions.
DIPiDIP-60450N.
MINTiMINT-4710996.

Proteomic databases

MaxQBiQ9UTN9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1250.04c.1; SPAC1250.04c.1:pep; SPAC1250.04c.
GeneIDi2541704.
KEGGispo:SPAC1250.04c.

Organism-specific databases

EuPathDBiFungiDB:SPAC1250.04c.
PomBaseiSPAC1250.04c. atl1.

Phylogenomic databases

HOGENOMiHOG000244138.
InParanoidiQ9UTN9.
KOiK07443.
OMAiTTEGINI.
OrthoDBiEOG7966V1.
PhylomeDBiQ9UTN9.

Miscellaneous databases

EvolutionaryTraceiQ9UTN9.
PROiQ9UTN9.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR014048. MethylDNA_cys_MeTrfase_DNA-bd.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01035. DNA_binding_1. 1 hit.
[Graphical view]
SUPFAMiSSF46767. SSF46767. 1 hit.
TIGRFAMsiTIGR00589. ogt. 1 hit.
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. Cited for: FUNCTION.
  3. Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH SUBSTRATE DNA, FUNCTION.
  4. Cited for: X-RAY CRYSTALLOGRAPHY (2.84 ANGSTROMS), FUNCTION.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), FUNCTION, MUTAGENESIS OF ARG-69.

Entry informationi

Entry nameiATL1_SCHPO
AccessioniPrimary (citable) accession number: Q9UTN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Does not have alkyltransferase activity. A tryptophan residue replaces the cysteine at the known active site of MGMT.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. 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.