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Conserved domains on  [gi|1034615692|ref|XP_016860132|]
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S-arrestin isoform X5 [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)

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_N super family cl22903
Arrestin (or S-antigen), N-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 26-184 7.50e-34

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: 120.09  E-value: 7.50e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034615692  26 VTIYLGNRDYIDHVSQvqPVDGVVLVDPDLVKG-KKVYVTLTCAFRYGQEDIDV--IGLTFRRDLYFSRVQVYPPVGA-A 101
Cdd:pfam00339   1 FTIEFDKPDGVYFPGE--TVTGRVLLENEEPKKaRAVKIELRGKARTGWEESEVrkEGLTFRKDLYYKGTEVYLPTETsL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034615692 102 STPTK-LQESLLKklGSNTYPFLLTFPDYLPCSVmlqpapqdSGKSCGVDFEVKAFATDStdaeeDKIPKKSS-VRLLIR 179
Cdd:pfam00339  79 WGSKTgGQNKLPA--GTHTFPFSFTLPPNCPSSF--------EGKHGGIRYEVKVTLDRP-----WKFNKSFRrVFTVIP 143


                  ....*
gi 1034615692 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 ...
 203-270 1.19e-13

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: 66.60  E-value: 1.19e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034615692  203 SDKPLHLAVSLNKEIYFHGEPIPVTVTVTNNTEKTVKKIKAFVEQVANVvlYSSDYYVKPVAMEEAQS 270
Cdd:smart01017   1 WSGPLSLEVSLPKKGYVPGETIPVTIKITNLSKKTVKKIKVSLVQTVTY--VSSDGPVKRSLAEKSKE 66
 
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 7.50e-34

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: 120.09  E-value: 7.50e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034615692  26 VTIYLGNRDYIDHVSQvqPVDGVVLVDPDLVKG-KKVYVTLTCAFRYGQEDIDV--IGLTFRRDLYFSRVQVYPPVGA-A 101
Cdd:pfam00339   1 FTIEFDKPDGVYFPGE--TVTGRVLLENEEPKKaRAVKIELRGKARTGWEESEVrkEGLTFRKDLYYKGTEVYLPTETsL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034615692 102 STPTK-LQESLLKklGSNTYPFLLTFPDYLPCSVmlqpapqdSGKSCGVDFEVKAFATDStdaeeDKIPKKSS-VRLLIR 179
Cdd:pfam00339  79 WGSKTgGQNKLPA--GTHTFPFSFTLPPNCPSSF--------EGKHGGIRYEVKVTLDRP-----WKFNKSFRrVFTVIP 143


                  ....*
gi 1034615692 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 ...
 203-270 1.19e-13

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: 66.60  E-value: 1.19e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034615692  203 SDKPLHLAVSLNKEIYFHGEPIPVTVTVTNNTEKTVKKIKAFVEQVANVvlYSSDYYVKPVAMEEAQS 270
Cdd:smart01017   1 WSGPLSLEVSLPKKGYVPGETIPVTIKITNLSKKTVKKIKVSLVQTVTY--VSSDGPVKRSLAEKSKE 66
Arrestin_C pfam02752
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 203-261 1.76e-08

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: 51.94  E-value: 1.76e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034615692 203 SDKPLHLAVSLNKEIYFHGEPIPVTVTVTNNTEKTVKKIKAFVEQVANVVLYSSDYYVK 261
Cdd:pfam02752   1 WSGKVSYSVSLPKKGYVPGETIPVTIEIDNQSKKKIKKIKISLVQQLTYKAKTPLGESK 59
FliD COG1345
Flagellar capping protein FliD [Cell motility];
225-247 2.47e-03

Flagellar capping protein FliD [Cell motility];


Pssm-ID: 440956 [Multi-domain]  Cd Length: 450  Bit Score: 39.05  E-value: 2.47e-03
                          10        20
                  ....*....|....*....|...
gi 1034615692 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 7.50e-34

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: 120.09  E-value: 7.50e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034615692  26 VTIYLGNRDYIDHVSQvqPVDGVVLVDPDLVKG-KKVYVTLTCAFRYGQEDIDV--IGLTFRRDLYFSRVQVYPPVGA-A 101
Cdd:pfam00339   1 FTIEFDKPDGVYFPGE--TVTGRVLLENEEPKKaRAVKIELRGKARTGWEESEVrkEGLTFRKDLYYKGTEVYLPTETsL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034615692 102 STPTK-LQESLLKklGSNTYPFLLTFPDYLPCSVmlqpapqdSGKSCGVDFEVKAFATDStdaeeDKIPKKSS-VRLLIR 179
Cdd:pfam00339  79 WGSKTgGQNKLPA--GTHTFPFSFTLPPNCPSSF--------EGKHGGIRYEVKVTLDRP-----WKFNKSFRrVFTVIP 143


                  ....*
gi 1034615692 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 ...
 203-270 1.19e-13

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: 66.60  E-value: 1.19e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034615692  203 SDKPLHLAVSLNKEIYFHGEPIPVTVTVTNNTEKTVKKIKAFVEQVANVvlYSSDYYVKPVAMEEAQS 270
Cdd:smart01017   1 WSGPLSLEVSLPKKGYVPGETIPVTIKITNLSKKTVKKIKVSLVQTVTY--VSSDGPVKRSLAEKSKE 66
Arrestin_C pfam02752
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 203-261 1.76e-08

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: 51.94  E-value: 1.76e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034615692 203 SDKPLHLAVSLNKEIYFHGEPIPVTVTVTNNTEKTVKKIKAFVEQVANVVLYSSDYYVK 261
Cdd:pfam02752   1 WSGKVSYSVSLPKKGYVPGETIPVTIEIDNQSKKKIKKIKISLVQQLTYKAKTPLGESK 59
FliD COG1345
Flagellar capping protein FliD [Cell motility];
225-247 2.47e-03

Flagellar capping protein FliD [Cell motility];


Pssm-ID: 440956 [Multi-domain]  Cd Length: 450  Bit Score: 39.05  E-value: 2.47e-03
                          10        20
                  ....*....|....*....|...
gi 1034615692 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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