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Conserved domains on  [gi|1720398213|ref|XP_030105251|]
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arrestin domain-containing protein 1 isoform X6 [Mus musculus]

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
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 ...
34-107 5.32e-09

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: 53.50  E-value: 5.32e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720398213   34 KAKRWIYDVRTIAEV-EGTGVKAWRRAQWQEQILVPALPQSaLPGCSLIHIDYYLQVSM----KAPEATVTLPLFVGNI 107
Cdd:smart01017  63 KSKEKKADRKTLVKElDGGPVLPGNKDKFEGQLKVPPLPPT-SRTCRLIKVEYKLKVKLrlsgKHSELRLELPITIGTV 140
PHA03247 super family cl33720
large tegument protein UL36; Provisional
112-252 3.68e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 38.77  E-value: 3.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398213  112 TPLSPCPGRESSPGTLslVVPSAPPQEEAEAVASGPHfSDPVSLSTKSHSQQQPLSAPLGSVSVTTTEPWVQVGSPARHS 191
Cdd:PHA03247  2721 LPPGPAAARQASPALP--AAPAPPAVPAGPATPGGPA-RPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRES 2797
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720398213  192 LHPPLCISiGATVPYFAEGSAGPVPTTSALILPPEYSSWGYPYDPSFSPQRPRRPMSRAVV 252
Cdd:PHA03247  2798 LPSPWDPA-DPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA 2857
 
Name Accession Description Interval E-value
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
34-107 5.32e-09

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: 53.50  E-value: 5.32e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720398213   34 KAKRWIYDVRTIAEV-EGTGVKAWRRAQWQEQILVPALPQSaLPGCSLIHIDYYLQVSM----KAPEATVTLPLFVGNI 107
Cdd:smart01017  63 KSKEKKADRKTLVKElDGGPVLPGNKDKFEGQLKVPPLPPT-SRTCRLIKVEYKLKVKLrlsgKHSELRLELPITIGTV 140
Arrestin_C pfam02752
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
22-107 1.30e-07

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: 49.25  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398213  22 RLTLRTSQKVSYKAK----RWIYDVRTIAEVEGTGVKAWRRAQWQEQILVPaLPQSALP---GCSLIHIDYYLQVSMKAP 94
Cdd:pfam02752  38 KIKISLVQQLTYKAKtplgESKREERVVAKEKNPGVAPGSKDKWEKELQLQ-IPTDLPPsstKCKIIKVEYKLKVTVDLS 116
                          90
                  ....*....|....*..
gi 1720398213  95 ----EATVTLPLFVGNI 107
Cdd:pfam02752 117 gsasELRLELPITIGTS 133
PHA03247 PHA03247
large tegument protein UL36; Provisional
112-252 3.68e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 38.77  E-value: 3.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398213  112 TPLSPCPGRESSPGTLslVVPSAPPQEEAEAVASGPHfSDPVSLSTKSHSQQQPLSAPLGSVSVTTTEPWVQVGSPARHS 191
Cdd:PHA03247  2721 LPPGPAAARQASPALP--AAPAPPAVPAGPATPGGPA-RPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRES 2797
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720398213  192 LHPPLCISiGATVPYFAEGSAGPVPTTSALILPPEYSSWGYPYDPSFSPQRPRRPMSRAVV 252
Cdd:PHA03247  2798 LPSPWDPA-DPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA 2857
 
Name Accession Description Interval E-value
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
34-107 5.32e-09

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: 53.50  E-value: 5.32e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720398213   34 KAKRWIYDVRTIAEV-EGTGVKAWRRAQWQEQILVPALPQSaLPGCSLIHIDYYLQVSM----KAPEATVTLPLFVGNI 107
Cdd:smart01017  63 KSKEKKADRKTLVKElDGGPVLPGNKDKFEGQLKVPPLPPT-SRTCRLIKVEYKLKVKLrlsgKHSELRLELPITIGTV 140
Arrestin_C pfam02752
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
22-107 1.30e-07

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: 49.25  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398213  22 RLTLRTSQKVSYKAK----RWIYDVRTIAEVEGTGVKAWRRAQWQEQILVPaLPQSALP---GCSLIHIDYYLQVSMKAP 94
Cdd:pfam02752  38 KIKISLVQQLTYKAKtplgESKREERVVAKEKNPGVAPGSKDKWEKELQLQ-IPTDLPPsstKCKIIKVEYKLKVTVDLS 116
                          90
                  ....*....|....*..
gi 1720398213  95 ----EATVTLPLFVGNI 107
Cdd:pfam02752 117 gsasELRLELPITIGTS 133
PHA03247 PHA03247
large tegument protein UL36; Provisional
112-252 3.68e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 38.77  E-value: 3.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398213  112 TPLSPCPGRESSPGTLslVVPSAPPQEEAEAVASGPHfSDPVSLSTKSHSQQQPLSAPLGSVSVTTTEPWVQVGSPARHS 191
Cdd:PHA03247  2721 LPPGPAAARQASPALP--AAPAPPAVPAGPATPGGPA-RPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRES 2797
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720398213  192 LHPPLCISiGATVPYFAEGSAGPVPTTSALILPPEYSSWGYPYDPSFSPQRPRRPMSRAVV 252
Cdd:PHA03247  2798 LPSPWDPA-DPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA 2857
 
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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