Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C0.1: RNA Pol CTD Phosphatase Like

  ⌊ FunctionalDomain C0.1: RNA Pol CTD Phosphatase Like (ID 273198)

Superfamily Assignment Evidence Code(s) ISS
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Schizosaccharomyces pombe Taxon ID: 4896 215794709

Uniprot

Protein NameAccessionEC Number Identifier
RNA polymerase II subunit A C-terminal domain phosphatase Q9P376 3.1.3.16 FCP1_SCHPO (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 372 | Length of Functional Domain: 277

1       10        20        30        40        50        60

SLSRLESENVKRLRQEKRLSLIVDLDQTIIHATVDPTVGEWMSDPGNVNYDVLRDVRSFN
LQEGPSGYTSCYYIKFRPGLAQFLQKISELYELHIYTMGTKAYAKEVAKIIDPTGKLFQD
RVLSRDDSGSLAQKSLRRLFPCDTSMVVVIDDRGDVWDWNPNLIKVVPYEFFVGIGDINS
NFLSGNREALEEQNKERVTALELQKSERPLAKQQNALLEDEGKPTPSHTLLHNRDHELER
LEKVLKDIHAVYYEEENDISSRSGNHKHANVGLIIPKMKQKVLKGCRLLFSGVIPLGVDV
LSSDIAKWAMSFGAEVVLDFSVPPTHLIAAKIRTEKVKKAVSMGNIKVVKLNWLTESLSQ
WKRLPESDYLLY
This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. The Superfamily domain, when present, is shown using underlining. In many cases the functional domain is the full-length sequence.
Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues

Subgroup CAR This EFD conserves 6/6 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
24 Asp (D) side chain Mg2+ ligand; nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:19026779
26 Asp (D) side chain general acid (donates proton to leaving group), general base (activates water), Mg2+ ligand metal ligand -- binding ICS PubMed:19026779
97 Thr (T) side chain binds phosphate and stabilizes transition state substrate binding -- binding,
transition state stabiliser -- binding 		ICS PubMed:19026779
134 Lys (K) side chain binds phosphate and stabilizes transition state substrate binding -- binding,
transition state stabiliser -- binding 		ICS PubMed:19026779
151 Asp (D) side chain Mg2+ ligand (via water) metal ligand -- binding ICS PubMed:19026779
152 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:19026779

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
3EF0 The Structure Of Fcp1, An Essential Rna Polymerase Ii Ctd Phosphatase Rna Polymerase Ii Subunit A C-Terminal Domain Phosphatase 1 2.1 Tetrafluoroaluminate Ion • Magnesium Ion CSA • PDB • PDBSum
4XPZ Structure Of Fission Yeast Rna Polymerase Ii Ctd Phosphatase Fcp1-R271A Bound To Aluminum Fluoride Rna Polymerase Ii Subunit A C-Terminal Domain Phosphatase 1 1.45 Aluminum Fluoride
(2 more ⇓) 		CSA • PDB • PDBSum
4XQ0 Structure Of Fission Yeast Rna Polymerase Ii Ctd Phosphatase Fcp1-R271A Bound To Beryllium Fluoride Rna Polymerase Ii Subunit A C-Terminal Domain Phosphatase 1 1.85 Aspartate Beryllium Trifluoride
(2 more ⇓) 		CSA • PDB • PDBSum
Percent identity and alignment length from the BLAST match of the Functional Domain sequence to the PDB sequence.
"Yes" indicates that a GI associated with this Functional Domain was mapped to the PDB ID via UniProtKB.

Curation History
Time Change Annotation Old Value New Value
April 30, 2014, 5:25 a.m. update curation agent sbrown setDomainBoundaries.py
update domain end position 276 280
update domain start position 1 4
EC number assigned by UniProtKB accession ID.