Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

  ⌊ FunctionalDomain uncharacterized haloacid dehalogenase superfamily sequence (ID 469953)

Superfamily Assignment Evidence Code(s) IEA
This entry was last updated onFeb. 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Anolis carolinensis Taxon ID: 28377 327267539 XP_003218558.1 (RefSeq) PRP URP

Sequence

Length of Enzyme (full-length): 565 | Length of Functional Domain: 565

1       10        20        30        40        50        60

MSTSWSDRLQNAADLPANMDGHAMKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVY
KSPEYESLGFDLTVERLVSIGYPQELLNFVYDPTFPTRGLVFDSLYGNLLKVDAYGNILV
CAHGFNFMRGPDIREQYPNKFIQRDDTDRFYILNTLFNLPETYLLACLVDFFTNCARYSS
CETGFKDGDLFMSFRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMN
EVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGNSHRPWQSYFDLILVDARKPLFFGEGT
VLRQVDTVTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKS
KKRQGWRTFLVIPELAQELHVWTDKSCLFEELQSLDIFLAELYKHLDSSSNERPDISSIQ
RRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAA
HVLMPHESTVEHTHVDINETESPMATRNRTSGDFKDSDKRHQLTRSVSEIKPPNLFPQTP
QEITHCHDEDDDEEEEEEEEEEEEE
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.

Structures

PDB ID Title Molecule Name Number of
EFDs
Resolution (Å) Mutant? Het group Links
5CR7 Human Cytosolic 5'-Nucleotidase Ii In Complex With N-(9H-Purin-6-Yl)-3-(3-Pyrrol-1-Ylphenyl)Benzamide Cytosolic Purine 5'-Nucleotidase 9 2.9 ~{N}-(7~{H}-Purin-6-Yl)-3-(3-Pyrrol-1-Ylphenyl) Benzamide
(4 more ⇓)
CSA • PDB • PDBSum
2JC9 Crystal Structure Of Human Cytosolic 5'-Nucleotidase Ii In Complex With Adenosine Cytosolic Purine 5'-Nucleotidase 19 1.5 Magnesium Ion
(3 more ⇓)
CSA • PDB • PDBSum
2J2C Crystal Structure Of Human Cytosolic 5'-Nucleotidase Ii (Nt5C2, Cn-Ii) Cytosolic Purine 5'-Nucleotidase 19 2.2 Sulfate Ion
(2 more ⇓)
CSA • PDB • PDBSum
4H4B Human Cytosolic 5'-Nucleotidase Ii In Complex With Anthraquinone-2,6-Disulfonic Acid Cytosolic Purine 5'-Nucleotidase 19 2.9 9,10-Dioxo-9,10-Dihydroanthracene-2,6-Disulfonic Acid
(3 more ⇓)
CSA • PDB • PDBSum
5CQZ Human Cytosolic 5'-Nucleotidase Ii In Complex With 3-(3-Imidazol-1-Ylphenyl)-N-(9H-Purin-6-Yl)Benzamide Cytosolic Purine 5'-Nucleotidase 9 2.9 Glycerol
(3 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
Aug. 1, 2014, 2:57 p.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.