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Links from Protein

Items: 12

1.

HAD hydrolase family protein

This family contains haloacid dehalogenase-like hydrolase enzymes. (from Pfam)

Date:
2024-08-14
Family Accession:
NF019887.5
Method:
HMM
2.

HAD family hydrolase

This family consists of Sucrose-6F-phosphate phosphohydrolase proteins found in plants and cyanobacteria. Sucrose-6(F)-phosphate phosphohydrolase catalyses the final step in the pathway of sucrose biosynthesis [1]. [1]. 11050182. Purification, molecular cloning, and sequence analysis of. sucrose-6F-phosphate phosphohydrolase from plants.. Lunn JE, Ashton AR, Hatch MD, Heldt HW;. Proc Natl Acad Sci U S A 2000;97:12914-12919. (from Pfam)

Date:
2024-08-14
Family Accession:
NF016972.5
Method:
HMM
3.

helicase HerA domain-containing protein

This entry represents the central domain found in archaeal proteins such as DNA double-strand break repair helicase HerA (EC:3.6.4.12). HerA is a helicase which is able to utilise either 3' or 5' single-stranded DNA extensions for loading and subsequent DNA duplex unwinding [1]. It forms a complex with NurA nuclease, this complex has the 5'-3' DNA end resection activity and is essential for cell viability in the crenarchaeon Sulfolobus islandicus [2]. This domain includes the the central RecA-like catalytic core and a flanking four-helix bundle [3]. The function of this prokaryotic domain is unknown. It contains several conserved aspartates and histidines that could be metal ligands. [1]. 14990749. A bipolar DNA helicase gene, herA, clusters with rad50, mre11. and nurA genes in thermophilic archaea.. Constantinesco F, Forterre P, Koonin EV, Aravind L, Elie C;. Nucleic Acids Res. 2004;32:1439-1447.. [2]. 25880130. Efficient 5'-3' DNA end resection by HerA and NurA is essential. for cell viability in the crenarchaeon Sulfolobus islandicus.. Huang Q, Liu L, Liu J, Ni J, She Q, Shen Y;. BMC Mol Biol. 2015;16:2.. [3]. 25420454. Structure of the hexameric HerA ATPase reveals a mechanism of. translocation-coupled DNA-end processing in archaea.. Rzechorzek NJ, Blackwood JK, Bray SM, Maman JD, Pellegrini L,. Robinson NP;. Nat Commun. 2014;5:5506. (from Pfam)

Date:
2024-08-14
Family Accession:
NF014044.5
Method:
HMM
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
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6.
new record, indexing in progress
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7.
new record, indexing in progress
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8.
new record, indexing in progress
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9.
new record, indexing in progress
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10.
new record, indexing in progress
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11.

HAD family hydrolase

haloacid dehalogenase (HAD) family hydrolase uses a nucleophilic aspartate in the phosphoryl transfer reaction; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

Date:
2024-05-15
Family Accession:
11426169
Method:
Sparcle
12.

HAD-IIB family hydrolase

This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (PF03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear.

GO Terms:
Biological Process:
metabolic process (GO:0008152)
Molecular Function:
hydrolase activity (GO:0016787)
Date:
2021-04-27
Family Accession:
TIGR01484.1
Method:
HMM
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