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Conserved domains on  [gi|2092143962|ref|XP_043382800|]
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GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1 isoform X1 [Chelonia mydas]

Protein Classification

ART domain-containing protein( domain architecture ID 10471557)

ART domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ART pfam01129
NAD:arginine ADP-ribosyltransferase;
81-306 4.46e-97

NAD:arginine ADP-ribosyltransferase;


:

Pssm-ID: 279473  Cd Length: 222  Bit Score: 287.42  E-value: 4.46e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092143962  81 LDMALSSFDDQYKDCASMMQAELGELNRTELANNRNYAETWLEAASNWKEMKDKSYMPRDFKPEYAIAILAYTSQGPLYK 160
Cdd:pfam01129   1 LDMAPNAFDDQYLGCVDRMEAKAPLLLKEEFAMNQALAVSWEQAKKRWQERKALLSLPMGFKDDHGIALLAYTSSSPLYR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092143962 161 qplhqEFNAAVREAGRTRDFYLNNFNFKTLHFLLTRALQVLKASEPtKCHQVYRGVRGIRFK-AESRKPVRFGHFTSTSL 239
Cdd:pfam01129  81 -----LFNEAVREAGRSREDYIGNFHFKALHFYLTRALQLLRQSYQ-PCHQVYRGVKGTRFTyTGPGKSVRFGQFTSSSL 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2092143962 240 KNESALQFGQDTFFSIKTCYGVNIKNFSFFPGEDEVLIPPFEKFKVTNFTRAQDRTLIQLLSLDSSS 306
Cdd:pfam01129 155 HKQVAEFFGQDTLFIIKTCLGVPIKPFSFFPSEDEVLIPPFEVFQVTGFSRTQGYNHIDLDSIGKTS 221
 
Name Accession Description Interval E-value
ART pfam01129
NAD:arginine ADP-ribosyltransferase;
81-306 4.46e-97

NAD:arginine ADP-ribosyltransferase;


Pssm-ID: 279473  Cd Length: 222  Bit Score: 287.42  E-value: 4.46e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092143962  81 LDMALSSFDDQYKDCASMMQAELGELNRTELANNRNYAETWLEAASNWKEMKDKSYMPRDFKPEYAIAILAYTSQGPLYK 160
Cdd:pfam01129   1 LDMAPNAFDDQYLGCVDRMEAKAPLLLKEEFAMNQALAVSWEQAKKRWQERKALLSLPMGFKDDHGIALLAYTSSSPLYR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092143962 161 qplhqEFNAAVREAGRTRDFYLNNFNFKTLHFLLTRALQVLKASEPtKCHQVYRGVRGIRFK-AESRKPVRFGHFTSTSL 239
Cdd:pfam01129  81 -----LFNEAVREAGRSREDYIGNFHFKALHFYLTRALQLLRQSYQ-PCHQVYRGVKGTRFTyTGPGKSVRFGQFTSSSL 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2092143962 240 KNESALQFGQDTFFSIKTCYGVNIKNFSFFPGEDEVLIPPFEKFKVTNFTRAQDRTLIQLLSLDSSS 306
Cdd:pfam01129 155 HKQVAEFFGQDTLFIIKTCLGVPIKPFSFFPSEDEVLIPPFEVFQVTGFSRTQGYNHIDLDSIGKTS 221
 
Name Accession Description Interval E-value
ART pfam01129
NAD:arginine ADP-ribosyltransferase;
81-306 4.46e-97

NAD:arginine ADP-ribosyltransferase;


Pssm-ID: 279473  Cd Length: 222  Bit Score: 287.42  E-value: 4.46e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092143962  81 LDMALSSFDDQYKDCASMMQAELGELNRTELANNRNYAETWLEAASNWKEMKDKSYMPRDFKPEYAIAILAYTSQGPLYK 160
Cdd:pfam01129   1 LDMAPNAFDDQYLGCVDRMEAKAPLLLKEEFAMNQALAVSWEQAKKRWQERKALLSLPMGFKDDHGIALLAYTSSSPLYR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092143962 161 qplhqEFNAAVREAGRTRDFYLNNFNFKTLHFLLTRALQVLKASEPtKCHQVYRGVRGIRFK-AESRKPVRFGHFTSTSL 239
Cdd:pfam01129  81 -----LFNEAVREAGRSREDYIGNFHFKALHFYLTRALQLLRQSYQ-PCHQVYRGVKGTRFTyTGPGKSVRFGQFTSSSL 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2092143962 240 KNESALQFGQDTFFSIKTCYGVNIKNFSFFPGEDEVLIPPFEKFKVTNFTRAQDRTLIQLLSLDSSS 306
Cdd:pfam01129 155 HKQVAEFFGQDTLFIIKTCLGVPIKPFSFFPSEDEVLIPPFEVFQVTGFSRTQGYNHIDLDSIGKTS 221
ADPrib_exo_Tox pfam03496
ADP-ribosyltransferase exoenzyme; This is a family of bacterial and viral bi-glutamic acid ...
193-300 1.79e-05

ADP-ribosyltransferase exoenzyme; This is a family of bacterial and viral bi-glutamic acid ADP-ribosyltransferases, where, in Swiss:Q93Q17, E403 is the catalytic residue and E401 contributes to the transfer of ADP-ribose to the target protein. In clostridial species it is actin that is being ADP-ribosylated; this result is lethal and dermonecrotic in infected mammals.


Pssm-ID: 427336 [Multi-domain]  Cd Length: 199  Bit Score: 45.05  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092143962 193 LLTRALQVLKASEPTKchqVYRGVRGIRFKAESRKPVR-----------------------FGHFTSTSLKNESALQFGQ 249
Cdd:pfam03496  60 NIDSAFSKSPIPENII---VYRRVGEDYFGLDGGLPLNnngtineelvsafkekfegkvktEYGYMSTSLVSDVAASFGG 136
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2092143962 250 DTF---FSI-KTCYGVNIKNFSFFPGEDEVLIPPFEKFKVTNFTRAQDRTLIQLL 300
Cdd:pfam03496 137 RPIilrITVpKGTKGAYISPLSGYPGEQEVLLPRGSTYKINKITIVESKGHTKLI 191
 
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.
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