Summary: Ham1 family
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Ham1 family Provide feedback
This family consists of the HAM1 protein P47119 and hypothetical archaeal bacterial and C. elegans proteins. HAM1 controls 6-N-hydroxylaminopurine (HAP) sensitivity and mutagenesis in S. cerevisiae P47119 . The HAM1 protein protects the cell from HAP, either on the level of deoxynucleoside triphosphate or the DNA level by a yet unidentified set of reactions .
Noskov VN, Staak K, Shcherbakova PV, Kozmin SG, Negishi K, Ono BC, Hayatsu H, Pavlov YI; , Yeast 1996;12:17-29.: HAM1, the gene controlling 6-N-hydroxylaminopurine sensitivity and mutagenesis in the yeast Saccharomyces cerevisiae. PUBMED:8789257 EPMC:8789257
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002637
This family contains the Saccharomyces cerevisiae (Baker's yeast) HAM1 protein SWISSPROT and other hypothetical archaeal, bacterial and Caenorhabditis elegans proteins. S. cerevisiae HAM1 protects against the mutagenic effects of the base analog 6-N-hydroxylaminopurine (HAP) which can be a natural product of monooxygenase activity on adenine. HAM1 protein protects the cell from HAP, either on the level of deoxynucleoside triphosphate or the DNA level by a yet unidentified set of reactions [PUBMED:8789257].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||hydrolase activity (GO:0016787)|
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We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_2030 (release 4.1)|
|Author:||Bashton M, Bateman A|
|Number in seed:||1300|
|Number in full:||2223|
|Average length of the domain:||183.70 aa|
|Average identity of full alignment:||34 %|
|Average coverage of the sequence by the domain:||89.31 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||13|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Ham1p_like domain has been found. There are 39 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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