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Conserved domains on  [gi|17535499|ref|NP_496882|]
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Arrestin C-terminal-like domain-containing protein [Caenorhabditis elegans]

Protein Classification

arrestin family protein( domain architecture ID 10448464)

arrestin family protein with both N-terminal and C-terminal Ig-like beta-sandwich domains found in arrestin (S antigen); similar to Homo sapiens beta-arrestin-1 and arrestin domain-containing protein

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_N pfam00339
Arrestin (or S-antigen), N-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 6-159 8.84e-61

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


:

Pssm-ID: 425619  Cd Length: 148  Bit Score: 195.20  E-value: 8.84e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535499     6 LHVIFDQPNEVFFPGQPISGRVVLSTTKEKyKARAVNIKILGLAHTSWTDYESVRRvdadGKVSHHRqsVHYSANVNYLD 85
Cdd:pfam00339   1 FTIEFDKPDGVYFPGETVTGRVLLENEEPK-KARAVKIELRGKARTGWEESEVRKE----GLTFRKD--LYYKGTEVYLP 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535499    86 YTLLLWAC-KDGSNELAAGEYAWSFSYNLPLNVPPSFEGKYGYLRYSVTAEVDRPWRLDKAKKRCITVSPLIDLN 159
Cdd:pfam00339  74 TETSLWGSkTGGQNKLPAGTHTFPFSFTLPPNCPSSFEGKHGGIRYEVKVTLDRPWKFNKSFRRVFTVIPKLDLN 148
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 182-332 9.23e-36

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: 129.00  E-value: 9.23e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535499    182 KKGYLELRVNIPKTGFVPGETVPMNIHILNHSSVPVTEVKAKIIQQCKFIAYRngttfhygGGYETGMSGQLQETKHDTK 261
Cdd:smart01017   1 WSGPLSLEVSLPKKGYVPGETIPVTIKITNLSKKTVKKIKVSLVQTVTYVSSD--------GPVKRSLAEKSKEKKADRK 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17535499    262 TVVKHGQEMTVAPRNEHKFAMELRLPSVTPTInQFSPVITVEYIVQFHVETSStFGSDVDCEMGILIGTVP 332
Cdd:smart01017  73 TLVKELDGGPVLPGNKDKFEGQLKVPPLPPTS-RTCRLIKVEYKLKVKLRLSG-KHSELRLELPITIGTVP 141
 
Name Accession Description Interval E-value
Arrestin_N pfam00339
Arrestin (or S-antigen), N-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 6-159 8.84e-61

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


Pssm-ID: 425619  Cd Length: 148  Bit Score: 195.20  E-value: 8.84e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535499     6 LHVIFDQPNEVFFPGQPISGRVVLSTTKEKyKARAVNIKILGLAHTSWTDYESVRRvdadGKVSHHRqsVHYSANVNYLD 85
Cdd:pfam00339   1 FTIEFDKPDGVYFPGETVTGRVLLENEEPK-KARAVKIELRGKARTGWEESEVRKE----GLTFRKD--LYYKGTEVYLP 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535499    86 YTLLLWAC-KDGSNELAAGEYAWSFSYNLPLNVPPSFEGKYGYLRYSVTAEVDRPWRLDKAKKRCITVSPLIDLN 159
Cdd:pfam00339  74 TETSLWGSkTGGQNKLPAGTHTFPFSFTLPPNCPSSFEGKHGGIRYEVKVTLDRPWKFNKSFRRVFTVIPKLDLN 148
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 182-332 9.23e-36

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: 129.00  E-value: 9.23e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535499    182 KKGYLELRVNIPKTGFVPGETVPMNIHILNHSSVPVTEVKAKIIQQCKFIAYRngttfhygGGYETGMSGQLQETKHDTK 261
Cdd:smart01017   1 WSGPLSLEVSLPKKGYVPGETIPVTIKITNLSKKTVKKIKVSLVQTVTYVSSD--------GPVKRSLAEKSKEKKADRK 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17535499    262 TVVKHGQEMTVAPRNEHKFAMELRLPSVTPTInQFSPVITVEYIVQFHVETSStFGSDVDCEMGILIGTVP 332
Cdd:smart01017  73 TLVKELDGGPVLPGNKDKFEGQLKVPPLPPTS-RTCRLIKVEYKLKVKLRLSG-KHSELRLELPITIGTVP 141
Arrestin_C pfam02752
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 182-333 1.85e-27

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: 106.64  E-value: 1.85e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535499   182 KKGYLELRVNIPKTGFVPGETVPMNIHILNHSSVPVTEVKAKIIQQCKFIAyrngttfhygggyetgmSGQLQETKHDTK 261
Cdd:pfam02752   1 WSGKVSYSVSLPKKGYVPGETIPVTIEIDNQSKKKIKKIKISLVQQLTYKA-----------------KTPLGESKREER 63

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535499   262 TVVKHgQEMTVAPRNEHKF--AMELRLP-SVTPTINQfSPVITVEYIVQFHVETSSTfGSDVDCEMGILIGTVPI 333
Cdd:pfam02752  64 VVAKE-KNPGVAPGSKDKWekELQLQIPtDLPPSSTK-CKIIKVEYKLKVTVDLSGS-ASELRLELPITIGTSPL 135
ART10-like cd22952
Arrestin-related trafficking adapter 10 and similar proteins; Arrestin-related trafficking ...
 5-142 1.83e-03

Arrestin-related trafficking adapter 10 and similar proteins; Arrestin-related trafficking adaptors (ARTs) function by targeting specific plasma membrane proteins to the endocytic system. They contain multiple PY motifs that are required for recruitment of Rsp5/Nedd4-like ubiquitin ligase which modifies the cargoes. It has been proposed that ARTs remodel the cell surface in response to environmental cues and may serve as part of a quality-control system at the plasma membrane, targeting damaged and misfolded membrane proteins for ubiquitination and subsequent degradation in the lysosome/vacuole. The specific target protein for ART10 is not yet known.


Pssm-ID: 438568 [Multi-domain]  Cd Length: 409  Bit Score: 40.43  E-value: 1.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535499   5 ELHVIFDQPNEVFFPGQPISGRVVLSTTKE---KykarAVNIKILGLAHTSWTDYESVRRVDADGKVS--------HHRQ 73
Cdd:cd22952   1 SVRILLDDNGEFYTNLDVISGRVILKLTKSesiS----AIVVKLEGESRTRLKVPKGNYNGQNDRGRTatevhkllYKVQ 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535499  74 SVHYSANV----NYLDYTLLLW--------------ACKD--------GSNELAAGEYAWSFSYNLPLNVPPSFEGKYGY 127
Cdd:cd22952  77 QVFPPPNVrsvsSSKSFTLTPGeyeypfefkipfnnSCSDphskstsgGLGGSLMDGLPPSFNRHVKKTLPPSLTGFPGE 156

                       170
                ....*....|....*..
gi 17535499 128 --LRYSVTAEVDRPWRL 142
Cdd:cd22952 157 aeIRYYVKVTVQRPSFF 173
 
Name Accession Description Interval E-value
Arrestin_N pfam00339
Arrestin (or S-antigen), N-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 6-159 8.84e-61

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


Pssm-ID: 425619  Cd Length: 148  Bit Score: 195.20  E-value: 8.84e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535499     6 LHVIFDQPNEVFFPGQPISGRVVLSTTKEKyKARAVNIKILGLAHTSWTDYESVRRvdadGKVSHHRqsVHYSANVNYLD 85
Cdd:pfam00339   1 FTIEFDKPDGVYFPGETVTGRVLLENEEPK-KARAVKIELRGKARTGWEESEVRKE----GLTFRKD--LYYKGTEVYLP 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535499    86 YTLLLWAC-KDGSNELAAGEYAWSFSYNLPLNVPPSFEGKYGYLRYSVTAEVDRPWRLDKAKKRCITVSPLIDLN 159
Cdd:pfam00339  74 TETSLWGSkTGGQNKLPAGTHTFPFSFTLPPNCPSSFEGKHGGIRYEVKVTLDRPWKFNKSFRRVFTVIPKLDLN 148
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 182-332 9.23e-36

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: 129.00  E-value: 9.23e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535499    182 KKGYLELRVNIPKTGFVPGETVPMNIHILNHSSVPVTEVKAKIIQQCKFIAYRngttfhygGGYETGMSGQLQETKHDTK 261
Cdd:smart01017   1 WSGPLSLEVSLPKKGYVPGETIPVTIKITNLSKKTVKKIKVSLVQTVTYVSSD--------GPVKRSLAEKSKEKKADRK 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17535499    262 TVVKHGQEMTVAPRNEHKFAMELRLPSVTPTInQFSPVITVEYIVQFHVETSStFGSDVDCEMGILIGTVP 332
Cdd:smart01017  73 TLVKELDGGPVLPGNKDKFEGQLKVPPLPPTS-RTCRLIKVEYKLKVKLRLSG-KHSELRLELPITIGTVP 141
Arrestin_C pfam02752
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 182-333 1.85e-27

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: 106.64  E-value: 1.85e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535499   182 KKGYLELRVNIPKTGFVPGETVPMNIHILNHSSVPVTEVKAKIIQQCKFIAyrngttfhygggyetgmSGQLQETKHDTK 261
Cdd:pfam02752   1 WSGKVSYSVSLPKKGYVPGETIPVTIEIDNQSKKKIKKIKISLVQQLTYKA-----------------KTPLGESKREER 63

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535499   262 TVVKHgQEMTVAPRNEHKF--AMELRLP-SVTPTINQfSPVITVEYIVQFHVETSSTfGSDVDCEMGILIGTVPI 333
Cdd:pfam02752  64 VVAKE-KNPGVAPGSKDKWekELQLQIPtDLPPSSTK-CKIIKVEYKLKVTVDLSGS-ASELRLELPITIGTSPL 135
LDB19 pfam13002
Arrestin_N terminal like; This is a family of proteins related to the Arrestin_N terminal ...
 67-136 1.19e-03

Arrestin_N terminal like; This is a family of proteins related to the Arrestin_N terminal family.


Pssm-ID: 404030  Cd Length: 183  Bit Score: 39.85  E-value: 1.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535499    67 KVSHHRQSVHYSANVNYLDYTLLLWACKDGSNELAAGEYAWSFSYNLPLNVPPSFEGKYGYLRYSVTAEV 136
Cdd:pfam13002   8 KVHFHKPAIQTCSACKTKTEVLKSWDIQKNTTDLSVGSHSYPFSYLFPGSLPASTSNSETQVKYELIATV 77
ART10-like cd22952
Arrestin-related trafficking adapter 10 and similar proteins; Arrestin-related trafficking ...
 5-142 1.83e-03

Arrestin-related trafficking adapter 10 and similar proteins; Arrestin-related trafficking adaptors (ARTs) function by targeting specific plasma membrane proteins to the endocytic system. They contain multiple PY motifs that are required for recruitment of Rsp5/Nedd4-like ubiquitin ligase which modifies the cargoes. It has been proposed that ARTs remodel the cell surface in response to environmental cues and may serve as part of a quality-control system at the plasma membrane, targeting damaged and misfolded membrane proteins for ubiquitination and subsequent degradation in the lysosome/vacuole. The specific target protein for ART10 is not yet known.


Pssm-ID: 438568 [Multi-domain]  Cd Length: 409  Bit Score: 40.43  E-value: 1.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535499   5 ELHVIFDQPNEVFFPGQPISGRVVLSTTKE---KykarAVNIKILGLAHTSWTDYESVRRVDADGKVS--------HHRQ 73
Cdd:cd22952   1 SVRILLDDNGEFYTNLDVISGRVILKLTKSesiS----AIVVKLEGESRTRLKVPKGNYNGQNDRGRTatevhkllYKVQ 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535499  74 SVHYSANV----NYLDYTLLLW--------------ACKD--------GSNELAAGEYAWSFSYNLPLNVPPSFEGKYGY 127
Cdd:cd22952  77 QVFPPPNVrsvsSSKSFTLTPGeyeypfefkipfnnSCSDphskstsgGLGGSLMDGLPPSFNRHVKKTLPPSLTGFPGE 156

                       170
                ....*....|....*..
gi 17535499 128 --LRYSVTAEVDRPWRL 142
Cdd:cd22952 157 aeIRYYVKVTVQRPSFF 173
 
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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