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Conserved domains on  [gi|116008178|ref|NP_000532|]
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S-arrestin [Homo sapiens]

Protein Classification

arrestin family protein( domain architecture ID 10432337)

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

CATH:  2.60.40.840
Gene Ontology:  GO:0005515
PubMed:  7720881
SCOP:  4007521

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Arrestin_N super family cl22903
Arrestin (or S-antigen), N-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
26-184 8.72e-33

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: 120.47  E-value: 8.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008178   26 VTIYLGNRDYIDHVSQvqPVDGVVLVDPDLVKG-KKVYVTLTCAFRYGQEDIDV--IGLTFRRDLYFSRVQVYPPVGA-A 101
Cdd:pfam00339   1 FTIEFDKPDGVYFPGE--TVTGRVLLENEEPKKaRAVKIELRGKARTGWEESEVrkEGLTFRKDLYYKGTEVYLPTETsL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008178  102 STPTK-LQESLLKklGSNTYPFLLTFPDYLPCSVmlqpapqdSGKSCGVDFEVKAFATDStdaeeDKIPKKSS-VRLLIR 179
Cdd:pfam00339  79 WGSKTgGQNKLPA--GTHTFPFSFTLPPNCPSSF--------EGKHGGIRYEVKVTLDRP-----WKFNKSFRrVFTVIP 143

                  ....*
gi 116008178  180 KVQHA 184
Cdd:pfam00339 144 KLDLN 148
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
203-364 5.90e-30

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: 112.82  E-value: 5.90e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008178   203 SDKPLHLAVSLNKEIYFHGEPIPVTVTVTNNTEKTVKKIKAFVEQVANVvlYSSDYYVKPVAMEEAQEKVPPNSTLTKTL 282
Cdd:smart01017   1 WSGPLSLEVSLPKKGYVPGETIPVTIKITNLSKKTVKKIKVSLVQTVTY--VSSDGPVKRSLAEKSKEKKADRKTLVKEL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008178   283 TLLPLLANNRERRgialDGKIKHEDTNLAsstiikegiDRTVLGILVSYQIKVKLTVSGFlgeltSSEVATEVPFRLMHP 362
Cdd:smart01017  79 DGGPVLPGNKDKF----EGQLKVPPLPPT---------SRTCRLIKVEYKLKVKLRLSGK-----HSELRLELPITIGTV 140

                   ..
gi 116008178   363 QP 364
Cdd:smart01017 141 PL 142
 
Name Accession Description Interval E-value
Arrestin_N pfam00339
Arrestin (or S-antigen), N-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
26-184 8.72e-33

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: 120.47  E-value: 8.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008178   26 VTIYLGNRDYIDHVSQvqPVDGVVLVDPDLVKG-KKVYVTLTCAFRYGQEDIDV--IGLTFRRDLYFSRVQVYPPVGA-A 101
Cdd:pfam00339   1 FTIEFDKPDGVYFPGE--TVTGRVLLENEEPKKaRAVKIELRGKARTGWEESEVrkEGLTFRKDLYYKGTEVYLPTETsL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008178  102 STPTK-LQESLLKklGSNTYPFLLTFPDYLPCSVmlqpapqdSGKSCGVDFEVKAFATDStdaeeDKIPKKSS-VRLLIR 179
Cdd:pfam00339  79 WGSKTgGQNKLPA--GTHTFPFSFTLPPNCPSSF--------EGKHGGIRYEVKVTLDRP-----WKFNKSFRrVFTVIP 143

                  ....*
gi 116008178  180 KVQHA 184
Cdd:pfam00339 144 KLDLN 148
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
203-364 5.90e-30

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: 112.82  E-value: 5.90e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008178   203 SDKPLHLAVSLNKEIYFHGEPIPVTVTVTNNTEKTVKKIKAFVEQVANVvlYSSDYYVKPVAMEEAQEKVPPNSTLTKTL 282
Cdd:smart01017   1 WSGPLSLEVSLPKKGYVPGETIPVTIKITNLSKKTVKKIKVSLVQTVTY--VSSDGPVKRSLAEKSKEKKADRKTLVKEL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008178   283 TLLPLLANNRERRgialDGKIKHEDTNLAsstiikegiDRTVLGILVSYQIKVKLTVSGFlgeltSSEVATEVPFRLMHP 362
Cdd:smart01017  79 DGGPVLPGNKDKF----EGQLKVPPLPPT---------SRTCRLIKVEYKLKVKLRLSGK-----HSELRLELPITIGTV 140

                   ..
gi 116008178   363 QP 364
Cdd:smart01017 141 PL 142
Arrestin_C pfam02752
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
203-364 3.56e-13

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: 66.20  E-value: 3.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008178  203 SDKPLHLAVSLNKEIYFHGEPIPVTVTVTNNTEKTVKKIKA-FVEQV---ANVVLYSSDYYVKPVAMEEAQEKVPPNStl 278
Cdd:pfam02752   1 WSGKVSYSVSLPKKGYVPGETIPVTIEIDNQSKKKIKKIKIsLVQQLtykAKTPLGESKREERVVAKEKNPGVAPGSK-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008178  279 tktltllpllannrerrgialdGKIKHEDT-----NLASSTIIKEGIDrtvlgilVSYQIKVKLTVSGFLGELTssevaT 353
Cdd:pfam02752  79 ----------------------DKWEKELQlqiptDLPPSSTKCKIIK-------VEYKLKVTVDLSGSASELR-----L 124
                         170
                  ....*....|.
gi 116008178  354 EVPFRLMHPQP 364
Cdd:pfam02752 125 ELPITIGTSPL 135
FliD COG1345
Flagellar capping protein FliD [Cell motility];
225-247 5.09e-03

Flagellar capping protein FliD [Cell motility];


Pssm-ID: 440956 [Multi-domain]  Cd Length: 450  Bit Score: 39.05  E-value: 5.09e-03
                         10        20
                 ....*....|....*....|...
gi 116008178 225 PVTVTVTNNTEKTVKKIKAFVEQ 247
Cdd:COG1345  250 PVTLTVSTDTDAIKKAIKDFVDA 272
 
Name Accession Description Interval E-value
Arrestin_N pfam00339
Arrestin (or S-antigen), N-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
26-184 8.72e-33

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: 120.47  E-value: 8.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008178   26 VTIYLGNRDYIDHVSQvqPVDGVVLVDPDLVKG-KKVYVTLTCAFRYGQEDIDV--IGLTFRRDLYFSRVQVYPPVGA-A 101
Cdd:pfam00339   1 FTIEFDKPDGVYFPGE--TVTGRVLLENEEPKKaRAVKIELRGKARTGWEESEVrkEGLTFRKDLYYKGTEVYLPTETsL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008178  102 STPTK-LQESLLKklGSNTYPFLLTFPDYLPCSVmlqpapqdSGKSCGVDFEVKAFATDStdaeeDKIPKKSS-VRLLIR 179
Cdd:pfam00339  79 WGSKTgGQNKLPA--GTHTFPFSFTLPPNCPSSF--------EGKHGGIRYEVKVTLDRP-----WKFNKSFRrVFTVIP 143

                  ....*
gi 116008178  180 KVQHA 184
Cdd:pfam00339 144 KLDLN 148
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
203-364 5.90e-30

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: 112.82  E-value: 5.90e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008178   203 SDKPLHLAVSLNKEIYFHGEPIPVTVTVTNNTEKTVKKIKAFVEQVANVvlYSSDYYVKPVAMEEAQEKVPPNSTLTKTL 282
Cdd:smart01017   1 WSGPLSLEVSLPKKGYVPGETIPVTIKITNLSKKTVKKIKVSLVQTVTY--VSSDGPVKRSLAEKSKEKKADRKTLVKEL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008178   283 TLLPLLANNRERRgialDGKIKHEDTNLAsstiikegiDRTVLGILVSYQIKVKLTVSGFlgeltSSEVATEVPFRLMHP 362
Cdd:smart01017  79 DGGPVLPGNKDKF----EGQLKVPPLPPT---------SRTCRLIKVEYKLKVKLRLSGK-----HSELRLELPITIGTV 140

                   ..
gi 116008178   363 QP 364
Cdd:smart01017 141 PL 142
Arrestin_C pfam02752
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
203-364 3.56e-13

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: 66.20  E-value: 3.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008178  203 SDKPLHLAVSLNKEIYFHGEPIPVTVTVTNNTEKTVKKIKA-FVEQV---ANVVLYSSDYYVKPVAMEEAQEKVPPNStl 278
Cdd:pfam02752   1 WSGKVSYSVSLPKKGYVPGETIPVTIEIDNQSKKKIKKIKIsLVQQLtykAKTPLGESKREERVVAKEKNPGVAPGSK-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008178  279 tktltllpllannrerrgialdGKIKHEDT-----NLASSTIIKEGIDrtvlgilVSYQIKVKLTVSGFLGELTssevaT 353
Cdd:pfam02752  79 ----------------------DKWEKELQlqiptDLPPSSTKCKIIK-------VEYKLKVTVDLSGSASELR-----L 124
                         170
                  ....*....|.
gi 116008178  354 EVPFRLMHPQP 364
Cdd:pfam02752 125 ELPITIGTSPL 135
FliD COG1345
Flagellar capping protein FliD [Cell motility];
225-247 5.09e-03

Flagellar capping protein FliD [Cell motility];


Pssm-ID: 440956 [Multi-domain]  Cd Length: 450  Bit Score: 39.05  E-value: 5.09e-03
                         10        20
                 ....*....|....*....|...
gi 116008178 225 PVTVTVTNNTEKTVKKIKAFVEQ 247
Cdd:COG1345  250 PVTLTVSTDTDAIKKAIKDFVDA 272
 
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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