Consensus sequences of arylsulfatases and phosphonate monoester hydrolases (doi:10.18419/darus-1838)

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Part 2: Study Description
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Document Description

Citation

Title:

Consensus sequences of arylsulfatases and phosphonate monoester hydrolases

Identification Number:

doi:10.18419/darus-1838

Distributor:

DaRUS

Date of Distribution:

2021-05-12

Version:

1

Bibliographic Citation:

Buchholz, Patrick C. F., 2021, "Consensus sequences of arylsulfatases and phosphonate monoester hydrolases", https://doi.org/10.18419/darus-1838, DaRUS, V1

Study Description

Citation

Title:

Consensus sequences of arylsulfatases and phosphonate monoester hydrolases

Identification Number:

doi:10.18419/darus-1838

Authoring Entity:

Buchholz, Patrick C. F. (Universität Stuttgart)

Distributor:

DaRUS

Access Authority:

Pleiss, Jürgen

Depositor:

Buchholz, Patrick C. F.

Date of Deposit:

2021-05-07

Holdings Information:

https://doi.org/10.18419/darus-1838

Study Scope

Keywords:

Medicine, Health and Life Sciences, amino acid sequence, protein sequence

Abstract:

A multiple sequence alignment was constructed by Clustal Omega for the 95 protein sequences annotated as homologues of arylsulfatases and the 85 protein sequences annotated as homologues of phosphonate monoester hydrolases, respectively. The HMMER software suite was used to derive a profile hidden Markov model from a multiple sequence alignment via the command hmmbuild, and to derive a consensus sequence from a profile hidden Markov model via the command hmmemit.

Methodology and Processing

Sources Statement

Data Sources:

van Loo B, Schober M, Valkov E, Heberlein M, Bornberg-Bauer E, Faber K, et al. Structural and Mechanistic Analysis of the Choline Sulfatase from Sinorhizobium melliloti: A Class I Sulfatase Specific for an Alkyl Sulfate Ester. J Mol Biol. 2018;430: 1004-1023. <a href="https://doi.org/10.1016/j.jmb.2018.02.010">doi:10.1016/j.jmb.2018.02.010</a>

van Loo B, Bayer CD, Fischer G, Jonas S, Valkov E, Mohamed MF, et al. Balancing Specificity and Promiscuity in Enzyme Evolution: Multidimensional Activity Transitions in the Alkaline Phosphatase Superfamily. J Am Chem Soc. 2019;141: 370-387. <a href="https://doi.org/10.1021/jacs.8b10290">doi:10.1021/jacs.8b10290</a>

Data Access

Other Study Description Materials

Related Studies

<a href="https://doi.org/10.18419/darus-1801">https://doi.org/10.18419/darus-1801</a>

Related Publications

Citation

Title:

Patrick C. F. Buchholz, Bert van Loo, Bernard D. G. Eenink, Erich Bornberg-Bauer, Jürgen Pleiss: "Ancestral sequences of a large promiscuous enzyme family correspond to bridges in sequence space in a network representation" (submitted)

Bibliographic Citation:

Patrick C. F. Buchholz, Bert van Loo, Bernard D. G. Eenink, Erich Bornberg-Bauer, Jürgen Pleiss: "Ancestral sequences of a large promiscuous enzyme family correspond to bridges in sequence space in a network representation" (submitted)

Other Study-Related Materials

Label:

AS-consensus.fasta

Text:

FASTA file containing the consensus protein sequence of arylsulfatases based on the profile hidden Markov model in AS.hmm

Notes:

application/octet-stream

Other Study-Related Materials

Label:

AS.aln

Text:

Multiple sequence alignment in Clustal format for 95 homologues of arylsulfatases

Notes:

application/octet-stream

Other Study-Related Materials

Label:

AS.hmm

Text:

Profile hidden Markov model in HMMER3 format based on the multiple sequence alignment in AS.aln

Notes:

application/octet-stream

Other Study-Related Materials

Label:

PMH-consensus.fasta

Text:

FASTA file containing the consensus protein sequence of phosphonate monoester hydrolases based on the profile hidden Markov model in PMH.hmm

Notes:

application/octet-stream

Other Study-Related Materials

Label:

PMH.aln

Text:

Multiple sequence alignment in Clustal format for 85 homologues of phosphonate monoester hydrolases

Notes:

application/octet-stream

Other Study-Related Materials

Label:

PMH.hmm

Text:

Profile hidden Markov model in HMMER3 format based on the multiple sequence alignment in PMH.aln

Notes:

application/octet-stream