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Conserved domains on  [gi|226293511|gb|EEH48931|]
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hypothetical protein PADG_05010 [Paracoccidioides brasiliensis Pb18]

Protein Classification

arrestin C-terminal domain-containing protein( domain architecture ID 10659953)

arrestin C-terminal domain-containing protein similar to Saccharomyces cerevisiae arrestin-related trafficking adapter 6 that may regulate endocytosis by recruiting RSP5 ubiquitin ligase activity to specific plasma membrane proteins in response to extracellular stimuli

CATH:  2.60.40.840
Gene Ontology:  GO:0005515
PubMed:  7720881|7833798|35563378
SCOP:  4007521

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 185-339 1.66e-06

Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports duplication with N-terminal domain. Arrestins comprise a family of closely-related proteins that includes beta-arrestin-1 and -2, which regulate the function of beta-adrenergic receptors by binding to their phosphorylated forms, impairing their capacity to activate G(S) proteins; Cone photoreceptors C-arrestin (arrestin-X). which could bind to phosphorylated red/green opsins; and Drosophila phosrestins I and II, which undergo light-induced phosphorylation, and probably play a role in photoreceptor transduction.


:

Pssm-ID: 214976 [Multi-domain]  Cd Length: 142  Bit Score: 47.34  E-value: 1.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226293511   185 TDHLVRLGISLPRWSYGPLDPISVYVKLSPNPDWINKARRVTIQKISISIDEEIIYNHEGDEPQRKTKTLTKRTENVNlk 264
Cdd:smart01017   1 WSGPLSLEVSLPKKGYVPGETIPVTIKITNLSKKTVKKIKVSLVQTVTYVSSDGPVKRSLAEKSKEKKADRKTLVKEL-- 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226293511   265 lpeagyiSNLGLVFPSRDLRDSEGILPRGKPAfpmyavsgfTTTASLYRIEYYLTVKAHLTS-ARDIVLRQPIVVC 339
Cdd:smart01017  79 -------DGGPVLPGNKDKFEGQLKVPPLPPT---------SRTCRLIKVEYKLKVKLRLSGkHSELRLELPITIG 138
 
Name Accession Description Interval E-value
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 185-339 1.66e-06

Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports duplication with N-terminal domain. Arrestins comprise a family of closely-related proteins that includes beta-arrestin-1 and -2, which regulate the function of beta-adrenergic receptors by binding to their phosphorylated forms, impairing their capacity to activate G(S) proteins; Cone photoreceptors C-arrestin (arrestin-X). which could bind to phosphorylated red/green opsins; and Drosophila phosrestins I and II, which undergo light-induced phosphorylation, and probably play a role in photoreceptor transduction.


Pssm-ID: 214976 [Multi-domain]  Cd Length: 142  Bit Score: 47.34  E-value: 1.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226293511   185 TDHLVRLGISLPRWSYGPLDPISVYVKLSPNPDWINKARRVTIQKISISIDEEIIYNHEGDEPQRKTKTLTKRTENVNlk 264
Cdd:smart01017   1 WSGPLSLEVSLPKKGYVPGETIPVTIKITNLSKKTVKKIKVSLVQTVTYVSSDGPVKRSLAEKSKEKKADRKTLVKEL-- 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226293511   265 lpeagyiSNLGLVFPSRDLRDSEGILPRGKPAfpmyavsgfTTTASLYRIEYYLTVKAHLTS-ARDIVLRQPIVVC 339
Cdd:smart01017  79 -------DGGPVLPGNKDKFEGQLKVPPLPPT---------SRTCRLIKVEYKLKVKLRLSGkHSELRLELPITIG 138
Arrestin_C pfam02752
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 185-338 1.45e-03

Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports duplication with N-terminal domain.


Pssm-ID: 460676  Cd Length: 135  Bit Score: 38.46  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226293511  185 TDHLVRLGISLPRWSYGPLDPISVYVKLSPNPDwiNKARRVTIQkisISIDEEIIYNHEGDEPQRKTKTLTKRTENVNLK 264
Cdd:pfam02752   1 WSGKVSYSVSLPKKGYVPGETIPVTIEIDNQSK--KKIKKIKIS---LVQQLTYKAKTPLGESKREERVVAKEKNPGVAP 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226293511  265 LPEAGYISNLGLVFPsrdlrdsegilprgKPAFPMyavsgfTTTASLYRIEYYLTVKAHL-TSARDIVLRQPIVV 338
Cdd:pfam02752  76 GSKDKWEKELQLQIP--------------TDLPPS------STKCKIIKVEYKLKVTVDLsGSASELRLELPITI 130
 
Name Accession Description Interval E-value
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 185-339 1.66e-06

Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports duplication with N-terminal domain. Arrestins comprise a family of closely-related proteins that includes beta-arrestin-1 and -2, which regulate the function of beta-adrenergic receptors by binding to their phosphorylated forms, impairing their capacity to activate G(S) proteins; Cone photoreceptors C-arrestin (arrestin-X). which could bind to phosphorylated red/green opsins; and Drosophila phosrestins I and II, which undergo light-induced phosphorylation, and probably play a role in photoreceptor transduction.


Pssm-ID: 214976 [Multi-domain]  Cd Length: 142  Bit Score: 47.34  E-value: 1.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226293511   185 TDHLVRLGISLPRWSYGPLDPISVYVKLSPNPDWINKARRVTIQKISISIDEEIIYNHEGDEPQRKTKTLTKRTENVNlk 264
Cdd:smart01017   1 WSGPLSLEVSLPKKGYVPGETIPVTIKITNLSKKTVKKIKVSLVQTVTYVSSDGPVKRSLAEKSKEKKADRKTLVKEL-- 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226293511   265 lpeagyiSNLGLVFPSRDLRDSEGILPRGKPAfpmyavsgfTTTASLYRIEYYLTVKAHLTS-ARDIVLRQPIVVC 339
Cdd:smart01017  79 -------DGGPVLPGNKDKFEGQLKVPPLPPT---------SRTCRLIKVEYKLKVKLRLSGkHSELRLELPITIG 138
Arrestin_C pfam02752
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 185-338 1.45e-03

Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports duplication with N-terminal domain.


Pssm-ID: 460676  Cd Length: 135  Bit Score: 38.46  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226293511  185 TDHLVRLGISLPRWSYGPLDPISVYVKLSPNPDwiNKARRVTIQkisISIDEEIIYNHEGDEPQRKTKTLTKRTENVNLK 264
Cdd:pfam02752   1 WSGKVSYSVSLPKKGYVPGETIPVTIEIDNQSK--KKIKKIKIS---LVQQLTYKAKTPLGESKREERVVAKEKNPGVAP 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226293511  265 LPEAGYISNLGLVFPsrdlrdsegilprgKPAFPMyavsgfTTTASLYRIEYYLTVKAHL-TSARDIVLRQPIVV 338
Cdd:pfam02752  76 GSKDKWEKELQLQIP--------------TDLPPS------STKCKIIKVEYKLKVTVDLsGSASELRLELPITI 130
 
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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