NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1717042355|ref|XP_030055682|]
View 

GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1 [Microcaecilia unicolor]

Protein Classification

ART domain-containing protein( domain architecture ID 10471557)

ART domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ART pfam01129
NAD:arginine ADP-ribosyltransferase;
41-261 5.74e-105

NAD:arginine ADP-ribosyltransferase;


:

Pssm-ID: 279473  Cd Length: 222  Bit Score: 305.53  E-value: 5.74e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717042355  41 LDIALTSFDDQYVGCTDVMEAELAWLNQTEYTTNRDYAEAWEAARSNWEGRKKNVPLPRGFKDEHAIAILAYTTNGPLHK 120
Cdd:pfam01129   1 LDMAPNAFDDQYLGCVDRMEAKAPLLLKEEFAMNQALAVSWEQAKKRWQERKALLSLPMGFKDDHGIALLAYTSSSPLYR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717042355 121 VFNEAVREAGRSRGYYLKNFKFKTLHFLLTKALQILdKETTPKCHRVYRGIRGIRFKSEEK-KAIRFGQFASSSLSNANA 199
Cdd:pfam01129  81 LFNEAVREAGRSREDYIGNFHFKALHFYLTRALQLL-RQSYQPCHQVYRGVKGTRFTYTGPgKSVRFGQFTSSSLHKQVA 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717042355 200 QQFGNDTLFNIETCYGVNIKNFSFFPLEQEVLIPPFEMFKVTNFTKVQDKTVINLHSWNTSS 261
Cdd:pfam01129 160 EFFGQDTLFIIKTCLGVPIKPFSFFPSEDEVLIPPFEVFQVTGFSRTQGYNHIDLDSIGKTS 221
 
Name Accession Description Interval E-value
ART pfam01129
NAD:arginine ADP-ribosyltransferase;
41-261 5.74e-105

NAD:arginine ADP-ribosyltransferase;


Pssm-ID: 279473  Cd Length: 222  Bit Score: 305.53  E-value: 5.74e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717042355  41 LDIALTSFDDQYVGCTDVMEAELAWLNQTEYTTNRDYAEAWEAARSNWEGRKKNVPLPRGFKDEHAIAILAYTTNGPLHK 120
Cdd:pfam01129   1 LDMAPNAFDDQYLGCVDRMEAKAPLLLKEEFAMNQALAVSWEQAKKRWQERKALLSLPMGFKDDHGIALLAYTSSSPLYR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717042355 121 VFNEAVREAGRSRGYYLKNFKFKTLHFLLTKALQILdKETTPKCHRVYRGIRGIRFKSEEK-KAIRFGQFASSSLSNANA 199
Cdd:pfam01129  81 LFNEAVREAGRSREDYIGNFHFKALHFYLTRALQLL-RQSYQPCHQVYRGVKGTRFTYTGPgKSVRFGQFTSSSLHKQVA 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717042355 200 QQFGNDTLFNIETCYGVNIKNFSFFPLEQEVLIPPFEMFKVTNFTKVQDKTVINLHSWNTSS 261
Cdd:pfam01129 160 EFFGQDTLFIIKTCLGVPIKPFSFFPSEDEVLIPPFEVFQVTGFSRTQGYNHIDLDSIGKTS 221
 
Name Accession Description Interval E-value
ART pfam01129
NAD:arginine ADP-ribosyltransferase;
41-261 5.74e-105

NAD:arginine ADP-ribosyltransferase;


Pssm-ID: 279473  Cd Length: 222  Bit Score: 305.53  E-value: 5.74e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717042355  41 LDIALTSFDDQYVGCTDVMEAELAWLNQTEYTTNRDYAEAWEAARSNWEGRKKNVPLPRGFKDEHAIAILAYTTNGPLHK 120
Cdd:pfam01129   1 LDMAPNAFDDQYLGCVDRMEAKAPLLLKEEFAMNQALAVSWEQAKKRWQERKALLSLPMGFKDDHGIALLAYTSSSPLYR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717042355 121 VFNEAVREAGRSRGYYLKNFKFKTLHFLLTKALQILdKETTPKCHRVYRGIRGIRFKSEEK-KAIRFGQFASSSLSNANA 199
Cdd:pfam01129  81 LFNEAVREAGRSREDYIGNFHFKALHFYLTRALQLL-RQSYQPCHQVYRGVKGTRFTYTGPgKSVRFGQFTSSSLHKQVA 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717042355 200 QQFGNDTLFNIETCYGVNIKNFSFFPLEQEVLIPPFEMFKVTNFTKVQDKTVINLHSWNTSS 261
Cdd:pfam01129 160 EFFGQDTLFIIKTCLGVPIKPFSFFPSEDEVLIPPFEVFQVTGFSRTQGYNHIDLDSIGKTS 221
ADPrib_exo_Tox pfam03496
ADP-ribosyltransferase exoenzyme; This is a family of bacterial and viral bi-glutamic acid ...
148-254 6.79e-04

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: 40.04  E-value: 6.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717042355 148 LLTKALQildKETTPKCHRVYRGIRGIRFKSE-----------------------EKKAIRFGQFASSSLSNANAQQFGN 204
Cdd:pfam03496  60 NIDSAFS---KSPIPENIIVYRRVGEDYFGLDgglplnnngtineelvsafkekfEGKVKTEYGYMSTSLVSDVAASFGG 136
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1717042355 205 D-TLFNIETCYGVN---IKNFSFFPLEQEVLIPPFEMFKVTNFTKVQDKTVINL 254
Cdd:pfam03496 137 RpIILRITVPKGTKgayISPLSGYPGEQEVLLPRGSTYKINKITIVESKGHTKL 190
 
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