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Conserved domains on  [gi|40254800|ref|NP_942030|]
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T-cell ecto-ADP-ribosyltransferase 2 precursor [Rattus norvegicus]

Protein Classification

ADP-ribosyltransferase family protein; tetratricopeptide repeat protein( domain architecture ID 10471557)

ADP-ribosyltransferase family protein similar to mono (ADP-ribosyl) transferases, which exist in vertebrates and transfer ADP-ribose to arginine| tetratricopeptide repeat (TPR) protein may adopt a right-handed helical structure with an amphipathic channel and may function as an interaction scaffold in the formation of multi-protein complexes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ART pfam01129
NAD:arginine ADP-ribosyltransferase;
27-239 6.62e-116

NAD:arginine ADP-ribosyltransferase;


:

Pssm-ID: 279473  Cd Length: 222  Bit Score: 331.72  E-value: 6.62e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254800    27 LDTAPNAFDDQYEGCVNKMEEKAPLLLQEDFNMNAKLKVAWEEAKKRWNNIKPSRSYPKGFNDFHGTALVAYTGS--IAV 104
Cdd:pfam01129   1 LDMAPNAFDDQYLGCVDRMEAKAPLLLKEEFAMNQALAVSWEQAKKRWQERKALLSLPMGFKDDHGIALLAYTSSspLYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254800   105 DFNRAVRE----FKENPGQFHYKAFHYYLTRALQLLSN--GDCHSVYRGTK-TRFHYTGAG-SVRFGQFTSSSLSKKVAQ 176
Cdd:pfam01129  81 LFNEAVREagrsREDYIGNFHFKALHFYLTRALQLLRQsyQPCHQVYRGVKgTRFTYTGPGkSVRFGQFTSSSLHKQVAE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40254800   177 sqefFSDHGTLFIIKTCLGVYIKEFSFRPDQEEVLIPGYEVYQKV---RTQGYNEIFLDSPKRKKS 239
Cdd:pfam01129 161 ----FFGQDTLFIIKTCLGVPIKPFSFFPSEDEVLIPPFEVFQVTgfsRTQGYNHIDLDSIGKTSS 222
 
Name Accession Description Interval E-value
ART pfam01129
NAD:arginine ADP-ribosyltransferase;
27-239 6.62e-116

NAD:arginine ADP-ribosyltransferase;


Pssm-ID: 279473  Cd Length: 222  Bit Score: 331.72  E-value: 6.62e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254800    27 LDTAPNAFDDQYEGCVNKMEEKAPLLLQEDFNMNAKLKVAWEEAKKRWNNIKPSRSYPKGFNDFHGTALVAYTGS--IAV 104
Cdd:pfam01129   1 LDMAPNAFDDQYLGCVDRMEAKAPLLLKEEFAMNQALAVSWEQAKKRWQERKALLSLPMGFKDDHGIALLAYTSSspLYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254800   105 DFNRAVRE----FKENPGQFHYKAFHYYLTRALQLLSN--GDCHSVYRGTK-TRFHYTGAG-SVRFGQFTSSSLSKKVAQ 176
Cdd:pfam01129  81 LFNEAVREagrsREDYIGNFHFKALHFYLTRALQLLRQsyQPCHQVYRGVKgTRFTYTGPGkSVRFGQFTSSSLHKQVAE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40254800   177 sqefFSDHGTLFIIKTCLGVYIKEFSFRPDQEEVLIPGYEVYQKV---RTQGYNEIFLDSPKRKKS 239
Cdd:pfam01129 161 ----FFGQDTLFIIKTCLGVPIKPFSFFPSEDEVLIPPFEVFQVTgfsRTQGYNHIDLDSIGKTSS 222
 
Name Accession Description Interval E-value
ART pfam01129
NAD:arginine ADP-ribosyltransferase;
27-239 6.62e-116

NAD:arginine ADP-ribosyltransferase;


Pssm-ID: 279473  Cd Length: 222  Bit Score: 331.72  E-value: 6.62e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254800    27 LDTAPNAFDDQYEGCVNKMEEKAPLLLQEDFNMNAKLKVAWEEAKKRWNNIKPSRSYPKGFNDFHGTALVAYTGS--IAV 104
Cdd:pfam01129   1 LDMAPNAFDDQYLGCVDRMEAKAPLLLKEEFAMNQALAVSWEQAKKRWQERKALLSLPMGFKDDHGIALLAYTSSspLYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254800   105 DFNRAVRE----FKENPGQFHYKAFHYYLTRALQLLSN--GDCHSVYRGTK-TRFHYTGAG-SVRFGQFTSSSLSKKVAQ 176
Cdd:pfam01129  81 LFNEAVREagrsREDYIGNFHFKALHFYLTRALQLLRQsyQPCHQVYRGVKgTRFTYTGPGkSVRFGQFTSSSLHKQVAE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40254800   177 sqefFSDHGTLFIIKTCLGVYIKEFSFRPDQEEVLIPGYEVYQKV---RTQGYNEIFLDSPKRKKS 239
Cdd:pfam01129 161 ----FFGQDTLFIIKTCLGVPIKPFSFFPSEDEVLIPPFEVFQVTgfsRTQGYNHIDLDSIGKTSS 222
 
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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