Protein Family Models for Protein (Select 495525597) - Protein Family Models

Select item 4240241.

This domain is found at the C-terminus of a wide variety of helicase enzymes. This domain has a AAA-like structural fold. (from Pfam)

GO Terms:

Molecular Function:: ATP binding (GO:0005524)

Molecular Function:: hydrolase activity (GO:0016787)

Date:: 2024-08-14

Family Accession:: NF024754.5
Method:: HMM

Select item 4221642.

AAA family ATPase

Date:: 2024-08-14

Family Accession:: NF024642.5
Method:: HMM

Select item 4206663.

PD-(D/E)XK nuclease family protein

Members of this family belong to the PD-(D/E)XK nuclease superfamily [1]. 15972856. Identification of novel restriction endonuclease-like fold. families among hypothetical proteins.. Kinch LN, Ginalski K, Rychlewski L, Grishin NV;. Nucleic Acids Res. 2005;33:3598-3605. (from Pfam)

Date:: 2024-08-14

Family Accession:: NF024117.5
Method:: HMM

Select item 4168394.

ImmA/IrrE family metallo-endopeptidase

This entry includes the catalytic domain of the protein ImmA, which is a metallopeptidase containing an HEXXH zinc-binding motif from peptidase family M78. ImmA is encoded on a conjugative transposon. Conjugating bacteria are able to transfer conjugative transposons that can, for example, confer resistance to antibiotics. The transposon is integrated into the chromosome, but during conjugation excises itself and then moves to the recipient bacterium and re-integrate into its chromosome. Typically a conjugative tranposon encodes only the proteins required for this activity and the proteins that regulate it. During exponential growth, the ICEBs1 transposon of Bacillus subtilis is inactivated by the immunity repressor protein ImmR, which is encoded by the transposon and represses the genes for excision and transfer. Cleavage of ImmR relaxes repression and allows transfer of the transposon. ImmA has been shown to be essential for the cleavage of ImmR [2]. This domain is also found in in metalloprotease IrrE, a central regulator of DNA damage repair in Deinococcaceae [1], HTH-type transcriptional regulators RamB [3] and PrpC [4]. [1]. 19150362. Crystal structure of the IrrE protein, a central regulator of. DNA damage repair in deinococcaceae.. Vujicic-Zagar A, Dulermo R, Le Gorrec M, Vannier F, Servant P,. Sommer S, de Groot A, Serre L;. J Mol Biol. 2009;386:704-716.. [2]. 18761623. A conserved anti-repressor controls horizontal gene transfer by. proteolysis.. Bose B, Auchtung JM, Lee CA, Grossman AD;. Mol Microbiol. 2008;70:570-582.. [3]. 15090522. RamB, a novel transcriptional regulator of genes involved in. ac. TRUNCATED at 1650 bytes (from Pfam)

Date:: 2024-08-14

Family Accession:: NF017885.5
Method:: HMM

Select item 4112215.

UvrD-helicase domain-containing protein

The Rep family helicases are composed of four structural domains. The Rep family function as dimers. REP helicases catalyse ATP dependent unwinding of double stranded DNA to single stranded DNA. Swiss:P23478, Swiss:P08394 have large insertions near to the carboxy-terminus relative to other members of the family. Structure of Swiss:P09980. [1]. 9288744. Major domain swiveling revealed by the crystal structures of. complexes of E. coli Rep helicase bound to single-stranded DNA. and ADP.. Korolev S, Hsieh J, Gauss GH, Lohman TM, Waksman G;. Cell 1997;90:635-647. (from Pfam)

GO Terms:

Molecular Function:: ATP binding (GO:0005524)

Date:: 2024-08-14

Family Accession:: NF012789.5
Method:: HMM

Select item 4012466.