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Conserved domains on  [gi|1785000356|ref|NP_001364102|]
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ecto-ADP-ribosyltransferase 3 isoform d precursor [Homo sapiens]

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;
29-252 1.10e-109

NAD:arginine ADP-ribosyltransferase;


:

Pssm-ID: 279473  Cd Length: 222  Bit Score: 320.93  E-value: 1.10e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785000356  29 LDMADNAFDDEYLKCTDRMEIKyVPQLLKEEKASHQQLDTVWENAKAKWAARKTQIFLPMNFKDNHGIALMAYISEAqeq 108
Cdd:pfam01129   1 LDMAPNAFDDQYLGCVDRMEAK-APLLLKEEFAMNQALAVSWEQAKKRWQERKALLSLPMGFKDDHGIALLAYTSSS--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785000356 109 tPFYHLFSEAVKMAGQSREDYIYGFQFKAFHFYLTRALQLLRK---PCEAssktvVYRTSQGTSFTFGGLN-QARFGHFT 184
Cdd:pfam01129  77 -PLYRLFNEAVREAGRSREDYIGNFHFKALHFYLTRALQLLRQsyqPCHQ-----VYRGVKGTRFTYTGPGkSVRFGQFT 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785000356 185 LAYSAKPQAA-NDQLTVLSIYTCLGVDIENFLDKESERITLIPLNEVFQV---SQEGAGNNLILQSINKTCS 252
Cdd:pfam01129 151 SSSLHKQVAEfFGQDTLFIIKTCLGVPIKPFSFFPSEDEVLIPPFEVFQVtgfSRTQGYNHIDLDSIGKTSS 222
 
Name Accession Description Interval E-value
ART pfam01129
NAD:arginine ADP-ribosyltransferase;
29-252 1.10e-109

NAD:arginine ADP-ribosyltransferase;


Pssm-ID: 279473  Cd Length: 222  Bit Score: 320.93  E-value: 1.10e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785000356  29 LDMADNAFDDEYLKCTDRMEIKyVPQLLKEEKASHQQLDTVWENAKAKWAARKTQIFLPMNFKDNHGIALMAYISEAqeq 108
Cdd:pfam01129   1 LDMAPNAFDDQYLGCVDRMEAK-APLLLKEEFAMNQALAVSWEQAKKRWQERKALLSLPMGFKDDHGIALLAYTSSS--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785000356 109 tPFYHLFSEAVKMAGQSREDYIYGFQFKAFHFYLTRALQLLRK---PCEAssktvVYRTSQGTSFTFGGLN-QARFGHFT 184
Cdd:pfam01129  77 -PLYRLFNEAVREAGRSREDYIGNFHFKALHFYLTRALQLLRQsyqPCHQ-----VYRGVKGTRFTYTGPGkSVRFGQFT 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785000356 185 LAYSAKPQAA-NDQLTVLSIYTCLGVDIENFLDKESERITLIPLNEVFQV---SQEGAGNNLILQSINKTCS 252
Cdd:pfam01129 151 SSSLHKQVAEfFGQDTLFIIKTCLGVPIKPFSFFPSEDEVLIPPFEVFQVtgfSRTQGYNHIDLDSIGKTSS 222
 
Name Accession Description Interval E-value
ART pfam01129
NAD:arginine ADP-ribosyltransferase;
29-252 1.10e-109

NAD:arginine ADP-ribosyltransferase;


Pssm-ID: 279473  Cd Length: 222  Bit Score: 320.93  E-value: 1.10e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785000356  29 LDMADNAFDDEYLKCTDRMEIKyVPQLLKEEKASHQQLDTVWENAKAKWAARKTQIFLPMNFKDNHGIALMAYISEAqeq 108
Cdd:pfam01129   1 LDMAPNAFDDQYLGCVDRMEAK-APLLLKEEFAMNQALAVSWEQAKKRWQERKALLSLPMGFKDDHGIALLAYTSSS--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785000356 109 tPFYHLFSEAVKMAGQSREDYIYGFQFKAFHFYLTRALQLLRK---PCEAssktvVYRTSQGTSFTFGGLN-QARFGHFT 184
Cdd:pfam01129  77 -PLYRLFNEAVREAGRSREDYIGNFHFKALHFYLTRALQLLRQsyqPCHQ-----VYRGVKGTRFTYTGPGkSVRFGQFT 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785000356 185 LAYSAKPQAA-NDQLTVLSIYTCLGVDIENFLDKESERITLIPLNEVFQV---SQEGAGNNLILQSINKTCS 252
Cdd:pfam01129 151 SSSLHKQVAEfFGQDTLFIIKTCLGVPIKPFSFFPSEDEVLIPPFEVFQVtgfSRTQGYNHIDLDSIGKTSS 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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