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Conserved domains on  [gi|24644712|ref|NP_649688|]
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uncharacterized protein Dmel_CG1105 [Drosophila melanogaster]

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
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 ...
6-155 1.00e-66

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: 209.07  E-value: 1.00e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644712     6 CELQLDNPWNTYYAGQTVNGQVKFTFDSPKKVRGIIIRFLGEANTEWSEekSVTTSEGKTENEVTQLKGHEEYFKIQYYL 85
Cdd:pfam00339   1 FTIEFDKPDGVYFPGETVTGRVLLENEEPKKARAVKIELRGKARTGWEE--SEVRKEGLTFRKDLYYKGTEVYLPTETSL 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644712    86 LGGKNSSETELPPGTHTYPFTCALPPNLPSSFEGEFGHVRYTIKVTLDRPWKFDQDMKMAFTVIAPVDLN 155
Cdd:pfam00339  79 WGSKTGGQNKLPAGTHTFPFSFTLPPNCPSSFEGKHGGIRYEVKVTLDRPWKFNKSFRRVFTVIPKLDLN 148
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
178-310 1.03e-28

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: 109.74  E-value: 1.03e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644712    178 RSGPLAVITNIPQTGFVSGQVLPITCEVDNTSNVNLTAVKFELRKLVTFH----------TNQPRSEKRESKVIIANLSV 247
Cdd:smart01017   1 WSGPLSLEVSLPKKGYVPGETIPVTIKITNLSKKTVKKIKVSLVQTVTYVssdgpvkrslAEKSKEKKADRKTLVKELDG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24644712    248 GPVNGGESRTFTQQMEIPALPPTNlLNCGIIALDYDLHVECEVSGPHRNLTGKVPITLGTIPL 310
Cdd:smart01017  81 GPVLPGNKDKFEGQLKVPPLPPTS-RTCRLIKVEYKLKVKLRLSGKHSELRLELPITIGTVPL 142
 
Name Accession Description Interval E-value
Arrestin_N pfam00339
Arrestin (or S-antigen), N-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
6-155 1.00e-66

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: 209.07  E-value: 1.00e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644712     6 CELQLDNPWNTYYAGQTVNGQVKFTFDSPKKVRGIIIRFLGEANTEWSEekSVTTSEGKTENEVTQLKGHEEYFKIQYYL 85
Cdd:pfam00339   1 FTIEFDKPDGVYFPGETVTGRVLLENEEPKKARAVKIELRGKARTGWEE--SEVRKEGLTFRKDLYYKGTEVYLPTETSL 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644712    86 LGGKNSSETELPPGTHTYPFTCALPPNLPSSFEGEFGHVRYTIKVTLDRPWKFDQDMKMAFTVIAPVDLN 155
Cdd:pfam00339  79 WGSKTGGQNKLPAGTHTFPFSFTLPPNCPSSFEGKHGGIRYEVKVTLDRPWKFNKSFRRVFTVIPKLDLN 148
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
178-310 1.03e-28

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: 109.74  E-value: 1.03e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644712    178 RSGPLAVITNIPQTGFVSGQVLPITCEVDNTSNVNLTAVKFELRKLVTFH----------TNQPRSEKRESKVIIANLSV 247
Cdd:smart01017   1 WSGPLSLEVSLPKKGYVPGETIPVTIKITNLSKKTVKKIKVSLVQTVTYVssdgpvkrslAEKSKEKKADRKTLVKELDG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24644712    248 GPVNGGESRTFTQQMEIPALPPTNlLNCGIIALDYDLHVECEVSGPHRNLTGKVPITLGTIPL 310
Cdd:smart01017  81 GPVLPGNKDKFEGQLKVPPLPPTS-RTCRLIKVEYKLKVKLRLSGKHSELRLELPITIGTVPL 142
Arrestin_C pfam02752
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
178-310 9.14e-26

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: 101.25  E-value: 9.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644712   178 RSGPLAVITNIPQTGFVSGQVLPITCEVDNTSNVNLTAVKFELRKLVTFHTNQPRSEKRESKVIIANLSVGPVNGGESRT 257
Cdd:pfam02752   1 WSGKVSYSVSLPKKGYVPGETIPVTIEIDNQSKKKIKKIKISLVQQLTYKAKTPLGESKREERVVAKEKNPGVAPGSKDK 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 24644712   258 F--TQQMEIP-ALPPTnLLNCGIIALDYDLHVECEVSGPHRNLTGKVPITLGTIPL 310
Cdd:pfam02752  81 WekELQLQIPtDLPPS-STKCKIIKVEYKLKVTVDLSGSASELRLELPITIGTSPL 135
ART10-like cd22952
Arrestin-related trafficking adapter 10 and similar proteins; Arrestin-related trafficking ...
7-165 7.81e-06

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: 47.74  E-value: 7.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644712   7 ELQLDNPWNTYYAGQTVNGQVKFTFDSPKKVRGIIIRFLGEANTewseekSVTTSEGKTENEVTQLKGHEEYFKIQY--- 83
Cdd:cd22952   3 RILLDDNGEFYTNLDVISGRVILKLTKSESISAIVVKLEGESRT------RLKVPKGNYNGQNDRGRTATEVHKLLYkvq 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644712  84 ------YLLGGKNSSETELPPGTHTYPFT--------CA--------------------------LPPNLPSSFEG--EF 121
Cdd:cd22952  77 qvfpppNVRSVSSSKSFTLTPGEYEYPFEfkipfnnsCSdphskstsgglggslmdglppsfnrhVKKTLPPSLTGfpGE 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 24644712 122 GHVRYTIKVTLDRPWKFdqdmkmaftviapvdlNLNPRVKEPFK 165
Cdd:cd22952 157 AEIRYYVKVTVQRPSFF----------------KENIRAQVPFK 184
 
Name Accession Description Interval E-value
Arrestin_N pfam00339
Arrestin (or S-antigen), N-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
6-155 1.00e-66

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: 209.07  E-value: 1.00e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644712     6 CELQLDNPWNTYYAGQTVNGQVKFTFDSPKKVRGIIIRFLGEANTEWSEekSVTTSEGKTENEVTQLKGHEEYFKIQYYL 85
Cdd:pfam00339   1 FTIEFDKPDGVYFPGETVTGRVLLENEEPKKARAVKIELRGKARTGWEE--SEVRKEGLTFRKDLYYKGTEVYLPTETSL 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644712    86 LGGKNSSETELPPGTHTYPFTCALPPNLPSSFEGEFGHVRYTIKVTLDRPWKFDQDMKMAFTVIAPVDLN 155
Cdd:pfam00339  79 WGSKTGGQNKLPAGTHTFPFSFTLPPNCPSSFEGKHGGIRYEVKVTLDRPWKFNKSFRRVFTVIPKLDLN 148
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
178-310 1.03e-28

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: 109.74  E-value: 1.03e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644712    178 RSGPLAVITNIPQTGFVSGQVLPITCEVDNTSNVNLTAVKFELRKLVTFH----------TNQPRSEKRESKVIIANLSV 247
Cdd:smart01017   1 WSGPLSLEVSLPKKGYVPGETIPVTIKITNLSKKTVKKIKVSLVQTVTYVssdgpvkrslAEKSKEKKADRKTLVKELDG 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24644712    248 GPVNGGESRTFTQQMEIPALPPTNlLNCGIIALDYDLHVECEVSGPHRNLTGKVPITLGTIPL 310
Cdd:smart01017  81 GPVLPGNKDKFEGQLKVPPLPPTS-RTCRLIKVEYKLKVKLRLSGKHSELRLELPITIGTVPL 142
Arrestin_C pfam02752
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
178-310 9.14e-26

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: 101.25  E-value: 9.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644712   178 RSGPLAVITNIPQTGFVSGQVLPITCEVDNTSNVNLTAVKFELRKLVTFHTNQPRSEKRESKVIIANLSVGPVNGGESRT 257
Cdd:pfam02752   1 WSGKVSYSVSLPKKGYVPGETIPVTIEIDNQSKKKIKKIKISLVQQLTYKAKTPLGESKREERVVAKEKNPGVAPGSKDK 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 24644712   258 F--TQQMEIP-ALPPTnLLNCGIIALDYDLHVECEVSGPHRNLTGKVPITLGTIPL 310
Cdd:pfam02752  81 WekELQLQIPtDLPPS-STKCKIIKVEYKLKVTVDLSGSASELRLELPITIGTSPL 135
ART10-like cd22952
Arrestin-related trafficking adapter 10 and similar proteins; Arrestin-related trafficking ...
7-165 7.81e-06

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: 47.74  E-value: 7.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644712   7 ELQLDNPWNTYYAGQTVNGQVKFTFDSPKKVRGIIIRFLGEANTewseekSVTTSEGKTENEVTQLKGHEEYFKIQY--- 83
Cdd:cd22952   3 RILLDDNGEFYTNLDVISGRVILKLTKSESISAIVVKLEGESRT------RLKVPKGNYNGQNDRGRTATEVHKLLYkvq 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644712  84 ------YLLGGKNSSETELPPGTHTYPFT--------CA--------------------------LPPNLPSSFEG--EF 121
Cdd:cd22952  77 qvfpppNVRSVSSSKSFTLTPGEYEYPFEfkipfnnsCSdphskstsgglggslmdglppsfnrhVKKTLPPSLTGfpGE 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 24644712 122 GHVRYTIKVTLDRPWKFdqdmkmaftviapvdlNLNPRVKEPFK 165
Cdd:cd22952 157 AEIRYYVKVTVQRPSFF----------------KENIRAQVPFK 184
LDB19 pfam13002
Arrestin_N terminal like; This is a family of proteins related to the Arrestin_N terminal ...
94-132 9.14e-04

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: 40.23  E-value: 9.14e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 24644712    94 TELPPGTHTYPFTCALPPNLPSSFEGEFGHVRYTIKVTL 132
Cdd:pfam13002  39 TDLSVGSHSYPFSYLFPGSLPASTSNSETQVKYELIATV 77
Arrestin_C pfam02752
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
15-133 4.75e-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: 37.31  E-value: 4.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644712    15 NTYYAGQTVNGQVKFTFDSPKKVRGIIIRFLgeantewseeksvttsegktenEVTQLKGHEEYFKIQYYLLG-GKNSSE 93
Cdd:pfam02752  14 KGYVPGETIPVTIEIDNQSKKKIKKIKISLV----------------------QQLTYKAKTPLGESKREERVvAKEKNP 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 24644712    94 TELPPGTHTYPFTCAL--PPNL-PSSFEGEFGHVRYTIKVTLD 133
Cdd:pfam02752  72 GVAPGSKDKWEKELQLqiPTDLpPSSTKCKIIKVEYKLKVTVD 114
 
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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