Uncharacterized site-specific tyrosine recombinase, C-terminal catalytic domain; Tyrosine recombinase (integrase) belongs to a DNA breaking-rejoining enzyme superfamily. The catalytic domain contains six conserved active site residues. The recombination reaction involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA. Many DNA breaking-rejoining enzymes also have N-terminal domains, which show little sequence or structure similarity.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2511838199  55 PEEARQLLDSIPADTLMGQRDRALIGLMTYTFARIGAAIGMRSG 98
Cdd:cd01196     2 APEARRLLESIDSTHPVGLRDRALIALMVYSFARIGAVLAMRVE 45

Phage integrase family; Members of this family cleave DNA substrates by a series of staggered cuts, during which the protein becomes covalently linked to the DNA through a catalytic tyrosine residue at the carboxy end of the alignment. The catalytic site residues in CRE recombinase are Arg-173, His-289, Arg-292 and Tyr-324.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2511838199  52 RFPPEEARQLLDSIPADTLmGQRDRALIGLMTYTFARIGAAIGMR 96
Cdd:pfam00589   1 RLTEDEVERLLDAAETGPL-SIRDKALLELLYATGLRISELCSLR 44

Uncharacterized site-specific tyrosine recombinase, C-terminal catalytic domain; Tyrosine recombinase (integrase) belongs to a DNA breaking-rejoining enzyme superfamily. The catalytic domain contains six conserved active site residues. The recombination reaction involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA. Many DNA breaking-rejoining enzymes also have N-terminal domains, which show little sequence or structure similarity.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2511838199  55 PEEARQLLDSIPADTLMGQRDRALIGLMTYTFARIGAAIGMRSG 98
Cdd:cd01196     2 APEARRLLESIDSTHPVGLRDRALIALMVYSFARIGAVLAMRVE 45

site-specific tyrosine recombinase XerC; Reviewed

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2511838199   5 HAAPTVNQRPAAVRHLFDWLVTGQVMTVNPAHSVRAPSFRANAARPLRfpPEEARQLLDSIPADTLMGQRDRALIGLM 82
Cdd:PRK00236   70 LSARSLARRLSALRSFYRWLVRRGLLKANPAAGLRAPKIPKRLPKPLD--VDQAKRLLDAIDEDDPLALRDRAILELL 145

DNA breaking-rejoining enzymes, C-terminal catalytic domain; The DNA breaking-rejoining enzyme superfamily includes type IB topoisomerases and tyrosine based site-specific recombinases (integrases) that share the same fold in their catalytic domain containing conserved active site residues. The best-studied members of this diverse superfamily include Human topoisomerase I, the bacteriophage lambda integrase, the bacteriophage P1 Cre recombinase, the yeast Flp recombinase, and the bacterial XerD/C recombinases. Their overall reaction mechanism is essentially identical and involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA. The enzymes differ in that topoisomerases cleave and then rejoin the same 5' and 3' termini, whereas a site-specific recombinase transfers a 5' hydroxyl generated by recombinase cleavage to a new 3' phosphate partner located in a different duplex region. Many DNA breaking-rejoining enzymes also have N-terminal domains, which show little sequence or structure similarity.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2511838199  57 EARQLLDSIPADTLMGQRDRALIGLMTYTFARIGAAIGMR 96
Cdd:cd00397     1 ELEKLLDAIDEDKKIDLRDRAILLLLLETGLRISELLALK 40

Uncharacterized site-specific tyrosine recombinase, C-terminal catalytic domain; Tyrosine recombinase (integrase) belongs to a DNA breaking-rejoining enzyme superfamily. The catalytic domain contains six conserved active site residues. The recombination reaction involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA. Many DNA breaking-rejoining enzymes also have N-terminal domains, which show little sequence or structure similarity.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2511838199  55 PEEARQLLDSIPADTLMGQRDRALIGLMTYTFARIGAAIGMR 96
Cdd:cd01195     2 REEARQRLDAADRHTAKGKRDEALVRLLLDNALRRSEAVALD 43

Phage integrase family; Members of this family cleave DNA substrates by a series of staggered cuts, during which the protein becomes covalently linked to the DNA through a catalytic tyrosine residue at the carboxy end of the alignment. The catalytic site residues in CRE recombinase are Arg-173, His-289, Arg-292 and Tyr-324.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2511838199  52 RFPPEEARQLLDSIPADTLmGQRDRALIGLMTYTFARIGAAIGMR 96
Cdd:pfam00589   1 RLTEDEVERLLDAAETGPL-SIRDKALLELLYATGLRISELCSLR 44