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Conserved domains on  [gi|672079631|ref|XP_008769317|]
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homer protein homolog 3 isoform X3 [Rattus norvegicus]

Protein Classification

Homer/Vesl family EVH1 domain-containing protein( domain architecture ID 10100433)

Homer/Vesl family EVH1 (WH1, RanBP1-WASP) domain-containing protein is a synaptic scaffolding protein, required for long-term potentiation, a form of synaptic plasticity thought to underlie memory formation

CATH:  2.30.29.30
Gene Ontology:  GO:0007216|GO:0035256|GO:0005515
PubMed:  11911879|17316461
SCOP:  4002440

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EVH1_Homer_Vesl cd01206
Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, ...
 6-114 1.10e-78

Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, required for long-term potentiation, a form of synaptic plasticity thought to underlie memory formation. They contains an N-terminal EVH1 domain and bind to both neurotransmitter receptors, such as the metabotropic group 1 glutamate receptor (mGluR) and to other scaffolding proteins via PPXXF motifs, in order to target them to the synaptic junction. These mGluRs possess a long C-terminal intracellular tail that may be important for subcellular localization of the receptor. The C-terminus is also the site of binding by the immediate early gene (IEG), Homer 1a. In contrast to Homer 1a, other Homer members additionally encode a C-terminal coiled-coil (CC) domain and form multivalent complexes that bind group 1 mGluRs. Homer 1a competes with constitutively expressed CC-Homers to modify the association of group 1 mGluRs with CC-Homer complexes. Since Homer proteins are strikingly enriched at the postsynaptic density (PSD), these observations suggest a role for the Homer family in regulating synaptic metabotropic receptor function. PSD-Zip45 (also named Homer 1c/Vesl-1L) has an EVH1 domain with a longer alpha-helix and its linking part included in the conserved region of Homer 1 (CRH1) interacts with the EVH1 domain of the neighbour CRH1 molecule in the crystal, suggesting that the EVH1 domain recognizes the PPXXF motif found in the binding partners, and the SPLTP sequence (P-motif) in the linking region of the CRH1. The two types of binding are partly overlapped in the EVH1 domain, implying a mechanism to regulate multimerization of Homer 1 family proteins. Homer 2 and Homer 3 are negative regulators of T cell activation. They bind the nuclear factor of activated T cells (NFAT) and compete with calcineurin binding. NFAT plays a critical role in calcium-dependent signaling in other cell types, including muscle and neurons. Homer-NFAT binding is also antagonized by active serine-threonine kinase AKT, enhancing TCR signaling via calcineurin-dependent dephosphorylation of NFAT resulting in changes in cytokine expression and an increase in effector-memory T cell populations in Homer-deficient mice. The EVH1 domains are part of the PH domain superamily. There are 5 EVH1 subfamilies: Enables/VASP, Homer/Vesl, WASP, Dcp1, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.


:

Pssm-ID: 269917  Cd Length: 109  Bit Score: 236.48  E-value: 1.10e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631   6 EQPIFSTRAHVFQIDPATKRNWIPAGKHALTVSYFYDATRNVYRIISIGGAKAIINSTVTPNMTFTKTSQKFGQWADSRA 85
Cdd:cd01206    1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                         90       100
                 ....*....|....*....|....*....
gi 672079631  86 NTVYGLGFGSEQQLTQFAEKFQEVKEAAR 114
Cdd:cd01206   81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 202-364 5.59e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 5.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631 202 LREANAAATQWR---QQLEVQRAEAEHLRQRVAELEAQVAAepvRAGEKEATSQSVEQLEARVQTKDQEIQTLknqstgp 278
Cdd:COG1196  224 ELEAELLLLKLReleAELEELEAELEELEAELEELEAELAE---LEAELEELRLELEELELELEEAQAEEYEL------- 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631 279 reapdTAEREETQQQVQVGCRTSPDLETRNAELEQQLRAMESNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLA 358
Cdd:COG1196  294 -----LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368


                 ....*.
gi 672079631 359 RLAEAA 364
Cdd:COG1196  369 EAEAEL 374
 
Name Accession Description Interval E-value
EVH1_Homer_Vesl cd01206
Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, ...
 6-114 1.10e-78

Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, required for long-term potentiation, a form of synaptic plasticity thought to underlie memory formation. They contains an N-terminal EVH1 domain and bind to both neurotransmitter receptors, such as the metabotropic group 1 glutamate receptor (mGluR) and to other scaffolding proteins via PPXXF motifs, in order to target them to the synaptic junction. These mGluRs possess a long C-terminal intracellular tail that may be important for subcellular localization of the receptor. The C-terminus is also the site of binding by the immediate early gene (IEG), Homer 1a. In contrast to Homer 1a, other Homer members additionally encode a C-terminal coiled-coil (CC) domain and form multivalent complexes that bind group 1 mGluRs. Homer 1a competes with constitutively expressed CC-Homers to modify the association of group 1 mGluRs with CC-Homer complexes. Since Homer proteins are strikingly enriched at the postsynaptic density (PSD), these observations suggest a role for the Homer family in regulating synaptic metabotropic receptor function. PSD-Zip45 (also named Homer 1c/Vesl-1L) has an EVH1 domain with a longer alpha-helix and its linking part included in the conserved region of Homer 1 (CRH1) interacts with the EVH1 domain of the neighbour CRH1 molecule in the crystal, suggesting that the EVH1 domain recognizes the PPXXF motif found in the binding partners, and the SPLTP sequence (P-motif) in the linking region of the CRH1. The two types of binding are partly overlapped in the EVH1 domain, implying a mechanism to regulate multimerization of Homer 1 family proteins. Homer 2 and Homer 3 are negative regulators of T cell activation. They bind the nuclear factor of activated T cells (NFAT) and compete with calcineurin binding. NFAT plays a critical role in calcium-dependent signaling in other cell types, including muscle and neurons. Homer-NFAT binding is also antagonized by active serine-threonine kinase AKT, enhancing TCR signaling via calcineurin-dependent dephosphorylation of NFAT resulting in changes in cytokine expression and an increase in effector-memory T cell populations in Homer-deficient mice. The EVH1 domains are part of the PH domain superamily. There are 5 EVH1 subfamilies: Enables/VASP, Homer/Vesl, WASP, Dcp1, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.


Pssm-ID: 269917  Cd Length: 109  Bit Score: 236.48  E-value: 1.10e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631   6 EQPIFSTRAHVFQIDPATKRNWIPAGKHALTVSYFYDATRNVYRIISIGGAKAIINSTVTPNMTFTKTSQKFGQWADSRA 85
Cdd:cd01206    1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                         90       100
                 ....*....|....*....|....*....
gi 672079631  86 NTVYGLGFGSEQQLTQFAEKFQEVKEAAR 114
Cdd:cd01206   81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 7-110 3.53e-43

WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in Wiskott-Aldrich syndrome (WAS). The majority of point mutations occur within the amino- terminal WH1 domain. The metabotropic glutamate receptors mGluR1alpha and mGluR5 bind a protein called homer, which is a WH1 domain homolog. A subset of WH1 domains has been termed a "EVH1" domain and appear to bind a polyproline motif.


Pssm-ID: 395450  Cd Length: 111  Bit Score: 145.67  E-value: 3.53e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631    7 QPIFSTRAHVFQIDPATKRNWIPAgKHALTVSYFYDATRNVYRIISIG--GAKAIINSTVTPNMTFTKTSQKFGQWADSR 84
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*.
gi 672079631   85 AntVYGLGFGSEQQLTQFAEKFQEVK 110
Cdd:pfam00568  88 C--VYGLNFASEEEATKFAKAVQEAL 111
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 6-108 1.49e-28

WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains point mutations in the majority of patients with WAS. Unknown function. Ena-like WH1 domains bind polyproline-containing peptides, and that Homer contains a WH1 domain.


Pssm-ID: 214674  Cd Length: 106  Bit Score: 107.06  E-value: 1.49e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631     6 EQPIFSTRAHVFQIDPATKRnWIPAGKH-ALTVSYFYDATRNVYRIISI-GGAKAIINSTVTPNMTFTKTSQKFGQWADs 83
Cdd:smart00461   3 SQCIILARAVVQLYDADTKK-WVPTGEGgAANLVIDKNQRSYFFRIVGIkGQDKVIWNQELYKNFKYNQATPTFHQWAD- 80

                           90       100
                   ....*....|....*....|....*
gi 672079631    84 rANTVYGLGFGSEQQLTQFAEKFQE 108
Cdd:smart00461  81 -DKCVYGLNFASEEEAKKFRKKVLK 104
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 202-364 5.59e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 5.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631 202 LREANAAATQWR---QQLEVQRAEAEHLRQRVAELEAQVAAepvRAGEKEATSQSVEQLEARVQTKDQEIQTLknqstgp 278
Cdd:COG1196  224 ELEAELLLLKLReleAELEELEAELEELEAELEELEAELAE---LEAELEELRLELEELELELEEAQAEEYEL------- 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631 279 reapdTAEREETQQQVQVGCRTSPDLETRNAELEQQLRAMESNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLA 358
Cdd:COG1196  294 -----LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368


                 ....*.
gi 672079631 359 RLAEAA 364
Cdd:COG1196  369 EAEAEL 374
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 196-364 2.80e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 2.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631   196 QRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAepvRAGEKEATSQSVEQLEARVQTKDQEIQTLKNQS 275
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA---LRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631   276 TGPREapdtaEREETQQQVQVGCRTSPDLETRNAELEQQLRAMESNLEEARAERERARAEVGRAAQLLDVRLFELSELRE 355
Cdd:TIGR02168  764 EELEE-----RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838


                   ....*....
gi 672079631   356 GLARLAEAA 364
Cdd:TIGR02168  839 RLEDLEEQI 847
 
Name Accession Description Interval E-value
EVH1_Homer_Vesl cd01206
Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, ...
 6-114 1.10e-78

Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, required for long-term potentiation, a form of synaptic plasticity thought to underlie memory formation. They contains an N-terminal EVH1 domain and bind to both neurotransmitter receptors, such as the metabotropic group 1 glutamate receptor (mGluR) and to other scaffolding proteins via PPXXF motifs, in order to target them to the synaptic junction. These mGluRs possess a long C-terminal intracellular tail that may be important for subcellular localization of the receptor. The C-terminus is also the site of binding by the immediate early gene (IEG), Homer 1a. In contrast to Homer 1a, other Homer members additionally encode a C-terminal coiled-coil (CC) domain and form multivalent complexes that bind group 1 mGluRs. Homer 1a competes with constitutively expressed CC-Homers to modify the association of group 1 mGluRs with CC-Homer complexes. Since Homer proteins are strikingly enriched at the postsynaptic density (PSD), these observations suggest a role for the Homer family in regulating synaptic metabotropic receptor function. PSD-Zip45 (also named Homer 1c/Vesl-1L) has an EVH1 domain with a longer alpha-helix and its linking part included in the conserved region of Homer 1 (CRH1) interacts with the EVH1 domain of the neighbour CRH1 molecule in the crystal, suggesting that the EVH1 domain recognizes the PPXXF motif found in the binding partners, and the SPLTP sequence (P-motif) in the linking region of the CRH1. The two types of binding are partly overlapped in the EVH1 domain, implying a mechanism to regulate multimerization of Homer 1 family proteins. Homer 2 and Homer 3 are negative regulators of T cell activation. They bind the nuclear factor of activated T cells (NFAT) and compete with calcineurin binding. NFAT plays a critical role in calcium-dependent signaling in other cell types, including muscle and neurons. Homer-NFAT binding is also antagonized by active serine-threonine kinase AKT, enhancing TCR signaling via calcineurin-dependent dephosphorylation of NFAT resulting in changes in cytokine expression and an increase in effector-memory T cell populations in Homer-deficient mice. The EVH1 domains are part of the PH domain superamily. There are 5 EVH1 subfamilies: Enables/VASP, Homer/Vesl, WASP, Dcp1, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.


Pssm-ID: 269917  Cd Length: 109  Bit Score: 236.48  E-value: 1.10e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631   6 EQPIFSTRAHVFQIDPATKRNWIPAGKHALTVSYFYDATRNVYRIISIGGAKAIINSTVTPNMTFTKTSQKFGQWADSRA 85
Cdd:cd01206    1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                         90       100
                 ....*....|....*....|....*....
gi 672079631  86 NTVYGLGFGSEQQLTQFAEKFQEVKEAAR 114
Cdd:cd01206   81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 7-110 3.53e-43

WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in Wiskott-Aldrich syndrome (WAS). The majority of point mutations occur within the amino- terminal WH1 domain. The metabotropic glutamate receptors mGluR1alpha and mGluR5 bind a protein called homer, which is a WH1 domain homolog. A subset of WH1 domains has been termed a "EVH1" domain and appear to bind a polyproline motif.


Pssm-ID: 395450  Cd Length: 111  Bit Score: 145.67  E-value: 3.53e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631    7 QPIFSTRAHVFQIDPATKRNWIPAgKHALTVSYFYDATRNVYRIISIG--GAKAIINSTVTPNMTFTKTSQKFGQWADSR 84
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*.
gi 672079631   85 AntVYGLGFGSEQQLTQFAEKFQEVK 110
Cdd:pfam00568  88 C--VYGLNFASEEEATKFAKAVQEAL 111
EVH1_family cd00837
EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; ...
 8-110 3.86e-38

EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; The EVH1 domains are part of the PH domain superfamily. EVH1 subfamilies include Enables/VASP, Homer/Vesl, WASP, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.


Pssm-ID: 269909  Cd Length: 103  Bit Score: 132.20  E-value: 3.86e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631   8 PIFSTRAHVFQIDPATKrNWIPA-GKHALTVSYFYDATRNVYRIISIGGA--KAIINSTVTPNMTFTKTSQKFGQWADSR 84
Cdd:cd00837    1 SIFSARAHVMQIDDSNK-NWVPAgGKGASRVSYFKDTTRNSFRIIGVDIKdkKVVINCTITKNLVYNKATQTFHQWADDR 79

                         90       100
                 ....*....|....*....|....*.
gi 672079631  85 anTVYGLGFGSEQQLTQFAEKFQEVK 110
Cdd:cd00837   80 --TVFGLNFASEEDATKFAEAVQEAL 103
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 6-108 1.49e-28

WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains point mutations in the majority of patients with WAS. Unknown function. Ena-like WH1 domains bind polyproline-containing peptides, and that Homer contains a WH1 domain.


Pssm-ID: 214674  Cd Length: 106  Bit Score: 107.06  E-value: 1.49e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631     6 EQPIFSTRAHVFQIDPATKRnWIPAGKH-ALTVSYFYDATRNVYRIISI-GGAKAIINSTVTPNMTFTKTSQKFGQWADs 83
Cdd:smart00461   3 SQCIILARAVVQLYDADTKK-WVPTGEGgAANLVIDKNQRSYFFRIVGIkGQDKVIWNQELYKNFKYNQATPTFHQWAD- 80

                           90       100
                   ....*....|....*....|....*
gi 672079631    84 rANTVYGLGFGSEQQLTQFAEKFQE 108
Cdd:smart00461  81 -DKCVYGLNFASEEEAKKFRKKVLK 104
EVH1_Ena_VASP-like cd01207
Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: ...
 8-103 4.51e-12

Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: Vasodilator-stimulated phosphoprotein (VASP), enabled gene product from Drosophila (Ena), mammalian enabled (Mena) and Ena/VASP-Like protein (EVL) localize to focal adhesions and to sites of actin filament dynamics. These proteins share a common modular organization with a highly conserved N- and C-terminal domains, termed Ena/VASP homology domains 1 and 2 (EVH1 and EVH2), that are separated by a central proline-rich domain. The EVH1 domain binds to other proteins at proline rich sequences. The majority of Ena-VASP type EVH1 domains recognize FPPPP motifs such as in the focal adhesion proteins zyxin and vinculin, and the ActA surface protein of Listeria monocytogenes, however the LIM3 domain of Tes lacks the FPPPP motif but still binds the EVH1 domain of Mena. It has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains. EVH2 mediates oligomerization within the family. The proline-rich region binds SH3 and WW domains as well as profilin, a protein that regulates actin filament dynamics. The EVH1 domains are part of the PH domain superamily. There are 5 EVH1 subfamilies: Enables/VASP, Homer/Vesl, WASP, Dcp1, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.


Pssm-ID: 269918  Cd Length: 108  Bit Score: 61.94  E-value: 4.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631   8 PIFSTRAHVFQIDPATKRnWIPAG-KHALTVSYFYDATR-NVYRIIsigGAKA-----IINSTVTPNMTFTKTSQKFGQW 80
Cdd:cd01207    1 SVASARASVMVYDDENKR-WVPSGgSQGLSRVQIYHNTRnNTFRVV---GRKLqdhevVINCAILKGLKYNQATPTFHQW 76

                         90       100
                 ....*....|....*....|...
gi 672079631  81 ADSRanTVYGLGFGSEQQLTQFA 103
Cdd:cd01207   77 RDAR--QVYGLNFASKEEATEFA 97
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 202-364 5.59e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 5.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631 202 LREANAAATQWR---QQLEVQRAEAEHLRQRVAELEAQVAAepvRAGEKEATSQSVEQLEARVQTKDQEIQTLknqstgp 278
Cdd:COG1196  224 ELEAELLLLKLReleAELEELEAELEELEAELEELEAELAE---LEAELEELRLELEELELELEEAQAEEYEL------- 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631 279 reapdTAEREETQQQVQVGCRTSPDLETRNAELEQQLRAMESNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLA 358
Cdd:COG1196  294 -----LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368


                 ....*.
gi 672079631 359 RLAEAA 364
Cdd:COG1196  369 EAEAEL 374
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 103-364 1.45e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631 103 AEKFQEVKEAARLAreksqdggELTSTALAMASHQVppsplvstngpEEKLFRSQSADApgPTERERLKKMLSEGSVGEV 182
Cdd:COG1196  212 AERYRELKEELKEL--------EAELLLLKLRELEA-----------ELEELEAELEEL--EAELEELEAELAELEAELE 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631 183 QWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEpvrAGEKEATSQSVEQLEARVQ 262
Cdd:COG1196  271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL---EEELEELEEELEELEEELE 347

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631 263 TKDQEIQTLKNQSTGPREAPDTAEREETQQQVQvgcrtspdLETRNAELEQQLRAMESNLEEARAERERARAEVGRAAQL 342
Cdd:COG1196  348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEE--------LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419

                        250       260
                 ....*....|....*....|..
gi 672079631 343 LDVRLFELSELREGLARLAEAA 364
Cdd:COG1196  420 EEELEELEEALAELEEEEEEEE 441
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 190-364 2.30e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 2.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631 190 ALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAepVRAGEKEATSQSVEQLEARVQTKDQEIQ 269
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE--AEEALLEAEAELAEAEEELEELAEELLE 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631 270 TLKnqstgpREAPDTAEREETQQQVQvgcrtspDLETRNAELEQQLRAMESNLEEARAERERARAEVGRAAQLLDVRLFE 349
Cdd:COG1196  391 ALR------AAAELAAQLEELEEAEE-------ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                        170
                 ....*....|....*
gi 672079631 350 LSELREGLARLAEAA 364
Cdd:COG1196  458 EEALLELLAELLEEA 472
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 196-364 2.80e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 2.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631   196 QRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAepvRAGEKEATSQSVEQLEARVQTKDQEIQTLKNQS 275
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA---LRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631   276 TGPREapdtaEREETQQQVQVGCRTSPDLETRNAELEQQLRAMESNLEEARAERERARAEVGRAAQLLDVRLFELSELRE 355
Cdd:TIGR02168  764 EELEE-----RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838


                   ....*....
gi 672079631   356 GLARLAEAA 364
Cdd:TIGR02168  839 RLEDLEEQI 847
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
165-322 6.62e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 6.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631 165 TERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAgALREANAAATQWRQQLEvQRAEAEHLRQRVAELEAQVAAEPVRA 244
Cdd:COG4717   71 KELKELEEELKEAEEKEEEYAELQEELEELEEELE-ELEAELEELREELEKLE-KLLQLLPLYQELEALEAELAELPERL 148

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672079631 245 GEKEATSQSVEQLEARVQTKDQEIQTLKNQSTGPREAPDTAEREETQQQVqvgcRTSPDLETRNAELEQQLRAMESNL 322
Cdd:COG4717  149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA----EELEELQQRLAELEEELEEAQEEL 222
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 166-364 1.74e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631 166 ERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEPVRAG 245
Cdd:COG1196  317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631 246 EKEATSQSVEQ----LEARVQTKDQEIQTLKNQSTGPREAPDTAEREETQQQVQVGcrtspDLETRNAELEQQLRAMESN 321
Cdd:COG1196  397 ELAAQLEELEEaeeaLLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA-----ELEEEEEALLELLAELLEE 471

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 672079631 322 LEEARAERERARAEVGRAAQLLDVRLfELSELREGLARLAEAA 364
Cdd:COG1196  472 AALLEAALAELLEELAEAAARLLLLL-EAEADYEGFLEGVKAA 513
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 185-364 3.13e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631   185 EAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEPVRAGEKEATSQSVEQLEARVQTK 264
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631   265 DQEIQTLKNQStGPREAPDTAEREETQQQVQVGCRTSPDLETRNAELEQQLRAMESNLEEARAERERARAEVGRAAQL-- 342
Cdd:TIGR02168  332 LDELAEELAEL-EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARle 410

                          170       180
                   ....*....|....*....|...
gi 672079631   343 -LDVRLFELSELREGLARLAEAA 364
Cdd:TIGR02168  411 rLEDRRERLQQEIEELLKKLEEA 433
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 151-291 3.96e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.17  E-value: 3.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631  151 EKLFRSQSadapgptERERLKKMLSEGSVGEVQWEAEFFALQDSNQ----RLAGALREANAAATQWRQQLEVQRAEAEHL 226
Cdd:COG3096   525 EQRLRQQQ-------NAERLLEEFCQRIGQQLDAAEELEELLAELEaqleELEEQAAEAVEQRSELRQQLEQLRARIKEL 597

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672079631  227 RQRV-AELEAQVAAEPVRA--GEKEATSQSVEQLEARVQTKDQEIQTLKNQSTGPREAPDTAEREETQ 291
Cdd:COG3096   598 AARApAWLAAQDALERLREqsGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQ 665
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 219-364 6.76e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.50  E-value: 6.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631   219 QRAEAEHLRQRVAELEAQVaaepvRAGEKE--ATSQSVEQLEARVQTKDQEIQTLKNQSTGPREAPDTAEREETQ--QQV 294
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKI-----AELEKAlaELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQleERI 749

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672079631   295 QVGCRTSPDLETRNAELEQQLRAMESNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARLAEAA 364
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
 
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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