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Conserved domains on  [gi|767919160|ref|XP_011509898|]
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S-arrestin isoform X6 [Homo sapiens]

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

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 ...
 69-230 3.67e-32

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: 115.52  E-value: 3.67e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919160    69 SDKPLHLAVSLNKEIYFHGEPIPVTVTVTNNTEKTVKKIKAFVEQVANVvlYSSDYYVKPVAMEEAQEKVPPNSTLTKTL 148
Cdd:smart01017   1 WSGPLSLEVSLPKKGYVPGETIPVTIKITNLSKKTVKKIKVSLVQTVTY--VSSDGPVKRSLAEKSKEKKADRKTLVKEL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919160   149 TLLPLLANNRERRgialDGKIKHEDTNLAsstiikegiDRTVLGILVSYQIKVKLTVSGFlgeltSSEVATEVPFRLMHP 228
Cdd:smart01017  79 DGGPVLPGNKDKF----EGQLKVPPLPPT---------SRTCRLIKVEYKLKVKLRLSGK-----HSELRLELPITIGTV 140


                   ..
gi 767919160   229 QP 230
Cdd:smart01017 141 PL 142
 
Name Accession Description Interval E-value
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 69-230 3.67e-32

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: 115.52  E-value: 3.67e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919160    69 SDKPLHLAVSLNKEIYFHGEPIPVTVTVTNNTEKTVKKIKAFVEQVANVvlYSSDYYVKPVAMEEAQEKVPPNSTLTKTL 148
Cdd:smart01017   1 WSGPLSLEVSLPKKGYVPGETIPVTIKITNLSKKTVKKIKVSLVQTVTY--VSSDGPVKRSLAEKSKEKKADRKTLVKEL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919160   149 TLLPLLANNRERRgialDGKIKHEDTNLAsstiikegiDRTVLGILVSYQIKVKLTVSGFlgeltSSEVATEVPFRLMHP 228
Cdd:smart01017  79 DGGPVLPGNKDKF----EGQLKVPPLPPT---------SRTCRLIKVEYKLKVKLRLSGK-----HSELRLELPITIGTV 140


                   ..
gi 767919160   229 QP 230
Cdd:smart01017 141 PL 142
Arrestin_C pfam02752
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 69-230 2.80e-14

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: 68.12  E-value: 2.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919160   69 SDKPLHLAVSLNKEIYFHGEPIPVTVTVTNNTEKTVKKIKA-FVEQV---ANVVLYSSDYYVKPVAmEEAQEKVPPNStl 144
Cdd:pfam02752   1 WSGKVSYSVSLPKKGYVPGETIPVTIEIDNQSKKKIKKIKIsLVQQLtykAKTPLGESKREERVVA-KEKNPGVAPGS-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919160  145 tktltllpllannrerrgialDGKIKHEDT-----NLASSTIIKEGIDrtvlgilVSYQIKVKLTVSGFLGELTssevaT 219
Cdd:pfam02752  78 ---------------------KDKWEKELQlqiptDLPPSSTKCKIIK-------VEYKLKVTVDLSGSASELR-----L 124

                         170
                  ....*....|.
gi 767919160  220 EVPFRLMHPQP 230
Cdd:pfam02752 125 ELPITIGTSPL 135
FliD COG1345
Flagellar capping protein FliD [Cell motility];
91-113 2.66e-03

Flagellar capping protein FliD [Cell motility];


Pssm-ID: 440956 [Multi-domain]  Cd Length: 450  Bit Score: 38.67  E-value: 2.66e-03
                         10        20
                 ....*....|....*....|...
gi 767919160  91 PVTVTVTNNTEKTVKKIKAFVEQ 113
Cdd:COG1345  250 PVTLTVSTDTDAIKKAIKDFVDA 272
 
Name Accession Description Interval E-value
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 69-230 3.67e-32

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: 115.52  E-value: 3.67e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919160    69 SDKPLHLAVSLNKEIYFHGEPIPVTVTVTNNTEKTVKKIKAFVEQVANVvlYSSDYYVKPVAMEEAQEKVPPNSTLTKTL 148
Cdd:smart01017   1 WSGPLSLEVSLPKKGYVPGETIPVTIKITNLSKKTVKKIKVSLVQTVTY--VSSDGPVKRSLAEKSKEKKADRKTLVKEL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919160   149 TLLPLLANNRERRgialDGKIKHEDTNLAsstiikegiDRTVLGILVSYQIKVKLTVSGFlgeltSSEVATEVPFRLMHP 228
Cdd:smart01017  79 DGGPVLPGNKDKF----EGQLKVPPLPPT---------SRTCRLIKVEYKLKVKLRLSGK-----HSELRLELPITIGTV 140


                   ..
gi 767919160   229 QP 230
Cdd:smart01017 141 PL 142
Arrestin_C pfam02752
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 69-230 2.80e-14

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: 68.12  E-value: 2.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919160   69 SDKPLHLAVSLNKEIYFHGEPIPVTVTVTNNTEKTVKKIKA-FVEQV---ANVVLYSSDYYVKPVAmEEAQEKVPPNStl 144
Cdd:pfam02752   1 WSGKVSYSVSLPKKGYVPGETIPVTIEIDNQSKKKIKKIKIsLVQQLtykAKTPLGESKREERVVA-KEKNPGVAPGS-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919160  145 tktltllpllannrerrgialDGKIKHEDT-----NLASSTIIKEGIDrtvlgilVSYQIKVKLTVSGFLGELTssevaT 219
Cdd:pfam02752  78 ---------------------KDKWEKELQlqiptDLPPSSTKCKIIK-------VEYKLKVTVDLSGSASELR-----L 124

                         170
                  ....*....|.
gi 767919160  220 EVPFRLMHPQP 230
Cdd:pfam02752 125 ELPITIGTSPL 135
FliD COG1345
Flagellar capping protein FliD [Cell motility];
91-113 2.66e-03

Flagellar capping protein FliD [Cell motility];


Pssm-ID: 440956 [Multi-domain]  Cd Length: 450  Bit Score: 38.67  E-value: 2.66e-03
                         10        20
                 ....*....|....*....|...
gi 767919160  91 PVTVTVTNNTEKTVKKIKAFVEQ 113
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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