NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|489047786|ref|WP_002958006|]
View 

MULTISPECIES: hypothetical protein [Pseudoalteromonas]

Protein Classification

site-specific integrase( domain architecture ID 332)

tyrosine based site-specific recombinase (integrase) is involved in cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct

CATH:  1.10.443.10
Gene Ontology:  GO:0015074|GO:0003677|GO:0006310
SCOP:  4002347

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
DNA_BRE_C super family cl00213
DNA breaking-rejoining enzymes, C-terminal catalytic domain; The DNA breaking-rejoining enzyme ...
10-169 1.77e-24

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.


The actual alignment was detected with superfamily member cd01184:

Pssm-ID: 469662 [Multi-domain]  Cd Length: 180  Bit Score: 95.45  E-value: 1.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489047786  10 FSAMELHTLYNGYIYGDFKVAREqpkhWHFWLPLIAYYSGAYSDEIGYLTLDDLSLEKDVLCFNFHTHGKIK-------P 82
Cdd:cd01184    1 FTPEELAKIFSSPLYTGCKKKDP----ALYWLPLIGLYTGARLNEICQLRVDDIKEEDGIWCIDINDDAEGRrlktkasR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489047786  83 RLVPVHQALIDAGFNEYLAFIKSQNQQRLMFDLPAKTGRYSEKVRIWFSgegeraGYLQKCDIPNVDQLGMktavSSLRL 162
Cdd:cd01184   77 RLVPIHPRLIELGFLDYVEALRADGKLFLFPEKRDKDGKYSKAASKWFN------RLLRKLGIKDDERKSF----HSFRH 146

                 ....*..
gi 489047786 163 NFEQQVR 169
Cdd:cd01184  147 TFITALK 153
 
Name Accession Description Interval E-value
INT_C_like_1 cd01184
Uncharacterized site-specific tyrosine recombinase, C-terminal catalytic domain; Tyrosine ...
10-169 1.77e-24

Uncharacterized site-specific tyrosine recombinase, C-terminal catalytic domain; Tyrosine recombinase (integrase) belongs to a DNA breaking-rejoining enzyme superfamily. The catalytic domain containing 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.


Pssm-ID: 271184 [Multi-domain]  Cd Length: 180  Bit Score: 95.45  E-value: 1.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489047786  10 FSAMELHTLYNGYIYGDFKVAREqpkhWHFWLPLIAYYSGAYSDEIGYLTLDDLSLEKDVLCFNFHTHGKIK-------P 82
Cdd:cd01184    1 FTPEELAKIFSSPLYTGCKKKDP----ALYWLPLIGLYTGARLNEICQLRVDDIKEEDGIWCIDINDDAEGRrlktkasR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489047786  83 RLVPVHQALIDAGFNEYLAFIKSQNQQRLMFDLPAKTGRYSEKVRIWFSgegeraGYLQKCDIPNVDQLGMktavSSLRL 162
Cdd:cd01184   77 RLVPIHPRLIELGFLDYVEALRADGKLFLFPEKRDKDGKYSKAASKWFN------RLLRKLGIKDDERKSF----HSFRH 146

                 ....*..
gi 489047786 163 NFEQQVR 169
Cdd:cd01184  147 TFITALK 153
 
Name Accession Description Interval E-value
INT_C_like_1 cd01184
Uncharacterized site-specific tyrosine recombinase, C-terminal catalytic domain; Tyrosine ...
10-169 1.77e-24

Uncharacterized site-specific tyrosine recombinase, C-terminal catalytic domain; Tyrosine recombinase (integrase) belongs to a DNA breaking-rejoining enzyme superfamily. The catalytic domain containing 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.


Pssm-ID: 271184 [Multi-domain]  Cd Length: 180  Bit Score: 95.45  E-value: 1.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489047786  10 FSAMELHTLYNGYIYGDFKVAREqpkhWHFWLPLIAYYSGAYSDEIGYLTLDDLSLEKDVLCFNFHTHGKIK-------P 82
Cdd:cd01184    1 FTPEELAKIFSSPLYTGCKKKDP----ALYWLPLIGLYTGARLNEICQLRVDDIKEEDGIWCIDINDDAEGRrlktkasR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489047786  83 RLVPVHQALIDAGFNEYLAFIKSQNQQRLMFDLPAKTGRYSEKVRIWFSgegeraGYLQKCDIPNVDQLGMktavSSLRL 162
Cdd:cd01184   77 RLVPIHPRLIELGFLDYVEALRADGKLFLFPEKRDKDGKYSKAASKWFN------RLLRKLGIKDDERKSF----HSFRH 146

                 ....*..
gi 489047786 163 NFEQQVR 169
Cdd:cd01184  147 TFITALK 153
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH