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Conserved domains on  [gi|530426823|ref|XP_005266176|]
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arrestin domain-containing protein 1 isoform X2 [Homo sapiens]

Protein Classification

arrestin family protein( domain architecture ID 10432288)

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

CATH:  2.60.40.840
PubMed:  7720881|7833798
SCOP:  4007521

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Arrestin_C pfam02752
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 179-301 1.17e-21

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: 90.46  E-value: 1.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426823  179 KTGSVVLTASTDLRGYVVGQALQLHADVENQSGKDTSPVVASLLQKVSYKAK----RWIHDVRTIAEVEGAGVKAWRRAQ 254
Cdd:pfam02752   1 WSGKVSYSVSLPKKGYVPGETIPVTIEIDNQSKKKIKKIKISLVQQLTYKAKtplgESKREERVVAKEKNPGVAPGSKDK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530426823  255 WHEQILVPaLPQSALP---GCSLIHIDYYLQVSLKAP----EATVTLPVFIGNI 301
Cdd:pfam02752  81 WEKELQLQ-IPTDLPPsstKCKIIKVEYKLKVTVDLSgsasELRLELPITIGTS 133
Arrestin_N super family cl22903
Arrestin (or S-antigen), N-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 7-139 2.60e-19

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


The actual alignment was detected with superfamily member pfam00339:

Pssm-ID: 451447  Cd Length: 148  Bit Score: 84.26  E-value: 2.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426823    7 FEISLSHGRVVYSPGEPLAGTVRVRLGAPLPFRAIRVTCIG-----------SCGVSNKANDTAWVVEEGYFNSSLSL-- 73
Cdd:pfam00339   1 FTIEFDKPDGVYFPGETVTGRVLLENEEPKKARAVKIELRGkartgweesevRKEGLTFRKDLYYKGTEVYLPTETSLwg 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426823   74 ADKGS---LPAGEHSFPFQFLLPATAPTSFEGPFGKIVHQVRAAIHTP-RFSKdhKCSLVFYILSPLNLN 139
Cdd:pfam00339  81 SKTGGqnkLPAGTHTFPFSFTLPPNCPSSFEGKHGGIRYEVKVTLDRPwKFNK--SFRRVFTVIPKLDLN 148
 
Name Accession Description Interval E-value
Arrestin_C pfam02752
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 179-301 1.17e-21

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: 90.46  E-value: 1.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426823  179 KTGSVVLTASTDLRGYVVGQALQLHADVENQSGKDTSPVVASLLQKVSYKAK----RWIHDVRTIAEVEGAGVKAWRRAQ 254
Cdd:pfam02752   1 WSGKVSYSVSLPKKGYVPGETIPVTIEIDNQSKKKIKKIKISLVQQLTYKAKtplgESKREERVVAKEKNPGVAPGSKDK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530426823  255 WHEQILVPaLPQSALP---GCSLIHIDYYLQVSLKAP----EATVTLPVFIGNI 301
Cdd:pfam02752  81 WEKELQLQ-IPTDLPPsstKCKIIKVEYKLKVTVDLSgsasELRLELPITIGTS 133
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 179-301 5.01e-21

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: 88.94  E-value: 5.01e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426823   179 KTGSVVLTASTDLRGYVVGQALQLHADVENQSGKDTSPVVASLLQKVSY-------------KAKRWIHDVRTIAEV-EG 244
Cdd:smart01017   1 WSGPLSLEVSLPKKGYVPGETIPVTIKITNLSKKTVKKIKVSLVQTVTYvssdgpvkrslaeKSKEKKADRKTLVKElDG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530426823   245 AGVKAWRRAQWHEQILVPALPQSaLPGCSLIHIDYYLQVSL----KAPEATVTLPVFIGNI 301
Cdd:smart01017  81 GPVLPGNKDKFEGQLKVPPLPPT-SRTCRLIKVEYKLKVKLrlsgKHSELRLELPITIGTV 140
Arrestin_N pfam00339
Arrestin (or S-antigen), N-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 7-139 2.60e-19

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: 84.26  E-value: 2.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426823    7 FEISLSHGRVVYSPGEPLAGTVRVRLGAPLPFRAIRVTCIG-----------SCGVSNKANDTAWVVEEGYFNSSLSL-- 73
Cdd:pfam00339   1 FTIEFDKPDGVYFPGETVTGRVLLENEEPKKARAVKIELRGkartgweesevRKEGLTFRKDLYYKGTEVYLPTETSLwg 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426823   74 ADKGS---LPAGEHSFPFQFLLPATAPTSFEGPFGKIVHQVRAAIHTP-RFSKdhKCSLVFYILSPLNLN 139
Cdd:pfam00339  81 SKTGGqnkLPAGTHTFPFSFTLPPNCPSSFEGKHGGIRYEVKVTLDRPwKFNK--SFRRVFTVIPKLDLN 148
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 8-135 4.87e-05

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: 43.10  E-value: 4.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426823     8 EISLSHGRVVYSPGEPLAGTVRVRLGAPLPFRAIRV------TCIGSCGVSnKANDTAWVVEEGYFNSSLSLADKGS--L 79
Cdd:smart01017   6 SLEVSLPKKGYVPGETIPVTIKITNLSKKTVKKIKVslvqtvTYVSSDGPV-KRSLAEKSKEKKADRKTLVKELDGGpvL 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 530426823    80 PAGEHSFPFQFLLPATAPTSFEGPFGKIVHQVRAAIHTPRFSKDHKCSLVFYILSP 135
Cdd:smart01017  85 PGNKDKFEGQLKVPPLPPTSRTCRLIKVEYKLKVKLRLSGKHSELRLELPITIGTV 140
 
Name Accession Description Interval E-value
Arrestin_C pfam02752
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 179-301 1.17e-21

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: 90.46  E-value: 1.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426823  179 KTGSVVLTASTDLRGYVVGQALQLHADVENQSGKDTSPVVASLLQKVSYKAK----RWIHDVRTIAEVEGAGVKAWRRAQ 254
Cdd:pfam02752   1 WSGKVSYSVSLPKKGYVPGETIPVTIEIDNQSKKKIKKIKISLVQQLTYKAKtplgESKREERVVAKEKNPGVAPGSKDK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530426823  255 WHEQILVPaLPQSALP---GCSLIHIDYYLQVSLKAP----EATVTLPVFIGNI 301
Cdd:pfam02752  81 WEKELQLQ-IPTDLPPsstKCKIIKVEYKLKVTVDLSgsasELRLELPITIGTS 133
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 179-301 5.01e-21

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: 88.94  E-value: 5.01e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426823   179 KTGSVVLTASTDLRGYVVGQALQLHADVENQSGKDTSPVVASLLQKVSY-------------KAKRWIHDVRTIAEV-EG 244
Cdd:smart01017   1 WSGPLSLEVSLPKKGYVPGETIPVTIKITNLSKKTVKKIKVSLVQTVTYvssdgpvkrslaeKSKEKKADRKTLVKElDG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530426823   245 AGVKAWRRAQWHEQILVPALPQSaLPGCSLIHIDYYLQVSL----KAPEATVTLPVFIGNI 301
Cdd:smart01017  81 GPVLPGNKDKFEGQLKVPPLPPT-SRTCRLIKVEYKLKVKLrlsgKHSELRLELPITIGTV 140
Arrestin_N pfam00339
Arrestin (or S-antigen), N-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 7-139 2.60e-19

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: 84.26  E-value: 2.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426823    7 FEISLSHGRVVYSPGEPLAGTVRVRLGAPLPFRAIRVTCIG-----------SCGVSNKANDTAWVVEEGYFNSSLSL-- 73
Cdd:pfam00339   1 FTIEFDKPDGVYFPGETVTGRVLLENEEPKKARAVKIELRGkartgweesevRKEGLTFRKDLYYKGTEVYLPTETSLwg 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426823   74 ADKGS---LPAGEHSFPFQFLLPATAPTSFEGPFGKIVHQVRAAIHTP-RFSKdhKCSLVFYILSPLNLN 139
Cdd:pfam00339  81 SKTGGqnkLPAGTHTFPFSFTLPPNCPSSFEGKHGGIRYEVKVTLDRPwKFNK--SFRRVFTVIPKLDLN 148
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 8-135 4.87e-05

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: 43.10  E-value: 4.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530426823     8 EISLSHGRVVYSPGEPLAGTVRVRLGAPLPFRAIRV------TCIGSCGVSnKANDTAWVVEEGYFNSSLSLADKGS--L 79
Cdd:smart01017   6 SLEVSLPKKGYVPGETIPVTIKITNLSKKTVKKIKVslvqtvTYVSSDGPV-KRSLAEKSKEKKADRKTLVKELDGGpvL 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 530426823    80 PAGEHSFPFQFLLPATAPTSFEGPFGKIVHQVRAAIHTPRFSKDHKCSLVFYILSP 135
Cdd:smart01017  85 PGNKDKFEGQLKVPPLPPTSRTCRLIKVEYKLKVKLRLSGKHSELRLELPITIGTV 140
 
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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