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Conserved domains on  [gi|13543212|gb|AAH05773|]
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Homer homolog 3 (Drosophila) [Mus musculus]

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 3.21e-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: 234.94  E-value: 3.21e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212   6 EQPIFSTRAHVFQIDPTTKRNWIPAGKHALTVSYFYDATRNVYRIISIGGAKAIINSTVTPNMTFTKTSQKFGQWADSRA 85
Cdd:cd01206   1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                        90       100
                ....*....|....*....|....*....
gi 13543212  86 NTVYGLGFASEQQLTQFAEKFQEVKEAAR 114
Cdd:cd01206  81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 191-355 4.34e-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: 48.78  E-value: 4.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212 191 ALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVepVRAGEKEATSQSVEQLEARVQTKDQTLK 270
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE--AEEALLEAEAELAEAEEELEELAEELLE 390

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212 271 NQstgTREAPDTAEREETQQQVQDLETRNAELEQQLRAMECNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLAR 350
Cdd:COG1196 391 AL---RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467


                ....*
gi 13543212 351 LAEAA 355
Cdd:COG1196 468 LLEEA 472
 
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 3.21e-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: 234.94  E-value: 3.21e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212   6 EQPIFSTRAHVFQIDPTTKRNWIPAGKHALTVSYFYDATRNVYRIISIGGAKAIINSTVTPNMTFTKTSQKFGQWADSRA 85
Cdd:cd01206   1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                        90       100
                ....*....|....*....|....*....
gi 13543212  86 NTVYGLGFASEQQLTQFAEKFQEVKEAAR 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 2.42e-42

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: 142.97  E-value: 2.42e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212     7 QPIFSTRAHVFQIDPTTKRNWIPAgKHALTVSYFYDATRNVYRIISIG--GAKAIINSTVTPNMTFTKTSQKFGQWADSR 84
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*.
gi 13543212    85 AntVYGLGFASEQQLTQFAEKFQEVK 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 2.73e-29

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: 108.98  E-value: 2.73e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212      6 EQPIFSTRAHVFQIDPTTKRnWIPAGKH-ALTVSYFYDATRNVYRIISI-GGAKAIINSTVTPNMTFTKTSQKFGQWADs 83
Cdd:smart00461   3 SQCIILARAVVQLYDADTKK-WVPTGEGgAANLVIDKNQRSYFFRIVGIkGQDKVIWNQELYKNFKYNQATPTFHQWAD- 80

                           90       100
                   ....*....|....*....|....*
gi 13543212     84 rANTVYGLGFASEQQLTQFAEKFQE 108
Cdd:smart00461  81 -DKCVYGLNFASEEEAKKFRKKVLK 104
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 191-355 4.34e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 4.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212 191 ALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVepVRAGEKEATSQSVEQLEARVQTKDQTLK 270
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE--AEEALLEAEAELAEAEEELEELAEELLE 390

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212 271 NQstgTREAPDTAEREETQQQVQDLETRNAELEQQLRAMECNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLAR 350
Cdd:COG1196 391 AL---RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467


                ....*
gi 13543212 351 LAEAA 355
Cdd:COG1196 468 LLEEA 472
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 167-354 1.89e-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: 43.51  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212    167 ERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAvepvrag 246
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA------- 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212    247 ekeatSQSVEQLEARVQTKDQTLKNQSTGTREAPDTAEREETQQQVQDLETRNA-------ELEQQLRAMECNLEEARAE 319
Cdd:TIGR02168  751 -----QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrealdELRAELTLLNEEAANLRER 825

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 13543212    320 RERARAEVGRAAQLLDVRLFELSELREGLARLAEA 354
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
antiphage_ZorA_2 NF033915
anti-phage ZorAB system protein ZorA; Proteins of this subfamily are putative H+ channel ...
 96-279 1.35e-03

anti-phage ZorAB system protein ZorA; Proteins of this subfamily are putative H+ channel proteins, but it has been reported that they are also involved in anti-phage defense.


Pssm-ID: 411476 [Multi-domain]  Cd Length: 383  Bit Score: 40.13  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212   96 EQQLTQFAEKFQEVKEAARLAREKSQDGGEFTSTGLALASHQVPPSPLVSTNGPGEEKLFRSQSADTPGPTERERLKKML 175
Cdd:NF033915 205 EQSLVHIAEYSKESKEALQELHERIGDRLQESLNGMSEAMQTALTDALNNIMAPAIQTLVSTTSQQSTQVLESLVGNFMD 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212  176 SEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQlevQRAEAELLRQRVAELEAQVAVEPVRAGEKEAtsqsv 255
Cdd:NF033915 285 GMTSAGREQGLQMQQAAADVNAAVSGMSERLNQLFNSLSEQ---QGRQMERAQQQSSTFETQLQRLSGSANERQA----- 356

                        170       180
                 ....*....|....*....|....
gi 13543212  256 eQLEARVQTKDQTLKNQSTGTREA 279
Cdd:NF033915 357 -QLEQRFEELMSGLTEQLQTQLGA 379
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
191-354 4.03e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 4.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212  191 ALQDSNQRLAGALREANAAatqwRQQLEVQRAEAELLRQRVAELEAQVAVEpvrAGEKEATSQSVEQLEARVQTKDQTLK 270
Cdd:PRK02224 259 EIEDLRETIAETEREREEL----AEEVRDLRERLEELEEERDDLLAEAGLD---DADAEAVEARREELEDRDEELRDRLE 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212  271 NQSTGTREAPDTAEREetQQQVQDLETRNAELEQQLRAMECNLEEaraereraraevgrAAQLLDVRLFELSELREGLAR 350
Cdd:PRK02224 332 ECRVAAQAHNEEAESL--REDADDLEERAEELREEAAELESELEE--------------AREAVEDRREEIEELEEEIEE 395


                 ....
gi 13543212  351 LAEA 354
Cdd:PRK02224 396 LRER 399
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 191-308 4.05e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 38.12  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212   191 ALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRAgeKEATSQSVEQLEARVQTKDQTLK 270
Cdd:pfam04012  19 KAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKA--QAALTKGNEELAREALAEKKSLE 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 13543212   271 NQSTGTREAPDTAE--REETQQQVQDLETRNAELEQQLRA 308
Cdd:pfam04012  97 KQAEALETQLAQQRsaVEQLRKQLAALETKIQQLKAKKNL 136
 
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 3.21e-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: 234.94  E-value: 3.21e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212   6 EQPIFSTRAHVFQIDPTTKRNWIPAGKHALTVSYFYDATRNVYRIISIGGAKAIINSTVTPNMTFTKTSQKFGQWADSRA 85
Cdd:cd01206   1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                        90       100
                ....*....|....*....|....*....
gi 13543212  86 NTVYGLGFASEQQLTQFAEKFQEVKEAAR 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 2.42e-42

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: 142.97  E-value: 2.42e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212     7 QPIFSTRAHVFQIDPTTKRNWIPAgKHALTVSYFYDATRNVYRIISIG--GAKAIINSTVTPNMTFTKTSQKFGQWADSR 84
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*.
gi 13543212    85 AntVYGLGFASEQQLTQFAEKFQEVK 110
Cdd:pfam00568  88 C--VYGLNFASEEEATKFAKAVQEAL 111
EVH1_family cd00837
EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; ...
 8-110 2.65e-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: 2.65e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212   8 PIFSTRAHVFQIDPTTKrNWIPA-GKHALTVSYFYDATRNVYRIISIGGA--KAIINSTVTPNMTFTKTSQKFGQWADSR 84
Cdd:cd00837   1 SIFSARAHVMQIDDSNK-NWVPAgGKGASRVSYFKDTTRNSFRIIGVDIKdkKVVINCTITKNLVYNKATQTFHQWADDR 79

                        90       100
                ....*....|....*....|....*.
gi 13543212  85 anTVYGLGFASEQQLTQFAEKFQEVK 110
Cdd:cd00837  80 --TVFGLNFASEEDATKFAEAVQEAL 103
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 6-108 2.73e-29

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: 108.98  E-value: 2.73e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212      6 EQPIFSTRAHVFQIDPTTKRnWIPAGKH-ALTVSYFYDATRNVYRIISI-GGAKAIINSTVTPNMTFTKTSQKFGQWADs 83
Cdd:smart00461   3 SQCIILARAVVQLYDADTKK-WVPTGEGgAANLVIDKNQRSYFFRIVGIkGQDKVIWNQELYKNFKYNQATPTFHQWAD- 80

                           90       100
                   ....*....|....*....|....*
gi 13543212     84 rANTVYGLGFASEQQLTQFAEKFQE 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 1.89e-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: 63.10  E-value: 1.89e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212   8 PIFSTRAHVFQIDPTTKRnWIPAG-KHALTVSYFYDATR-NVYRIIsigGAKA-----IINSTVTPNMTFTKTSQKFGQW 80
Cdd:cd01207   1 SVASARASVMVYDDENKR-WVPSGgSQGLSRVQIYHNTRnNTFRVV---GRKLqdhevVINCAILKGLKYNQATPTFHQW 76

                        90       100
                ....*....|....*....|...
gi 13543212  81 ADSRanTVYGLGFASEQQLTQFA 103
Cdd:cd01207  77 RDAR--QVYGLNFASKEEATEFA 97
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 191-355 4.34e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 4.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212 191 ALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVepVRAGEKEATSQSVEQLEARVQTKDQTLK 270
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE--AEEALLEAEAELAEAEEELEELAEELLE 390

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212 271 NQstgTREAPDTAEREETQQQVQDLETRNAELEQQLRAMECNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLAR 350
Cdd:COG1196 391 AL---RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467


                ....*
gi 13543212 351 LAEAA 355
Cdd:COG1196 468 LLEEA 472
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 186-355 1.05e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 1.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212 186 EAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEpvrAGEKEATSQSVEQLEARVQTK 265
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL---EERRRELEERLEELEEELAEL 328

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212 266 DQTLKNQSTGTREApdTAEREETQQQVQDLETRNAELEQQLRAMECNLEEARAERERARAEVGRAAQLLDVRLFELSELR 345
Cdd:COG1196 329 EEELEELEEELEEL--EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406

                       170
                ....*....|
gi 13543212 346 EGLARLAEAA 355
Cdd:COG1196 407 EAEEALLERL 416
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 167-355 1.76e-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: 1.76e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212 167 ERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEpvrAG 246
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA---EE 351

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212 247 EKEATSQSVEQLEARVQTKDQTLKNQSTGTREApdTAEREETQQQVQDLETRNAELEQQLRAMECNLEEARAERERARAE 326
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEEL--AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429

                       170       180
                ....*....|....*....|....*....
gi 13543212 327 VGRAAQLLDVRLFELSELREGLARLAEAA 355
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEE 458
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 203-355 3.22e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 3.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212 203 LREANAAATQWR---QQLEVQRAEAELLRQRVAELEAQVAVepvRAGEKEATSQSVEQLEARVQTKDQTLknQSTGTREA 279
Cdd:COG1196 224 ELEAELLLLKLReleAELEELEAELEELEAELEELEAELAE---LEAELEELRLELEELELELEEAQAEE--YELLAELA 298

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13543212 280 PDTAEREETQQQVQDLETRNAELEQQLRAMECNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARLAEAA 355
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 191-355 4.73e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 4.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212 191 ALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVepvRAGEKEATSQSVEQLEARVQTKDQTLK 270
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE---AQAEEYELLAELARLEQDIARLEERRR 312

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212 271 N-----QSTGTREAPDTAEREETQQQVQDLETRNAELEQQLRAMECNLEEARAERERARAEVGRAAQLLDVRLFELSELR 345
Cdd:COG1196 313 EleerlEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                       170
                ....*....|
gi 13543212 346 EGLARLAEAA 355
Cdd:COG1196 393 RAAAELAAQL 402
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 167-355 1.55e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212 167 ERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRAG 246
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212 247 EKEATSQSVEQLEARVQTKDQTLKNQSTGTREAPDTAEREETQQQVQDLETRNAELEQQLRAMECNLEEARAERERAR-- 324
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEll 483

                       170       180       190
                ....*....|....*....|....*....|.
gi 13543212 325 AEVGRAAQLLDVRLfELSELREGLARLAEAA 355
Cdd:COG1196 484 EELAEAAARLLLLL-EAEADYEGFLEGVKAA 513
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 167-354 1.89e-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: 43.51  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212    167 ERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAvepvrag 246
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA------- 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212    247 ekeatSQSVEQLEARVQTKDQTLKNQSTGTREAPDTAEREETQQQVQDLETRNA-------ELEQQLRAMECNLEEARAE 319
Cdd:TIGR02168  751 -----QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrealdELRAELTLLNEEAANLRER 825

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 13543212    320 RERARAEVGRAAQLLDVRLFELSELREGLARLAEA 354
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 197-355 4.13e-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: 42.35  E-value: 4.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212    197 QRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRAGEKEATSQSVEQLEARVQTKDQTLKNQSTGT 276
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212    277 REAPD--TAEREETQQQVQDLETRNAELEQQLRAMECNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARLAEA 354
Cdd:TIGR02168  767 EERLEeaEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846


                   .
gi 13543212    355 A 355
Cdd:TIGR02168  847 I 847
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 94-349 6.91e-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: 41.58  E-value: 6.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212     94 ASEQQLTQFAEKFQEVKEAARLAREKSQDggefTSTGLALASHQVppSPLVSTNGPGEEKLFRSQSADTPGPTERERLKK 173
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQLRKELEE----LSRQISALRKDL--ARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212    174 MLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRAGE----KE 249
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDleeqIE 848

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212    250 ATSQSVEQLEARVQTKDQTLKNQSTGTREApdTAEREETQQQVQDLETRNAELEQQLRAMECNLEEARAERERARAEVGR 329
Cdd:TIGR02168  849 ELSEDIESLAAEIEELEELIEELESELEAL--LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926

                          250       260
                   ....*....|....*....|
gi 13543212    330 AAQLLDVRLFELSELREGLA 349
Cdd:TIGR02168  927 LELRLEGLEVRIDNLQERLS 946
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
187-310 1.30e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212  187 AEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRagEKEATSQSVEQLEARVQTKD 266
Cdd:COG4913  281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD--RLEQLEREIERLERELEERE 358

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 13543212  267 QTLKNQSTGTR----EAPDTAE-----REETQQQVQDLETRNAELEQQLRAME 310
Cdd:COG4913  359 RRRARLEALLAalglPLPASAEefaalRAEAAALLEALEEELEALEEALAEAE 411
antiphage_ZorA_2 NF033915
anti-phage ZorAB system protein ZorA; Proteins of this subfamily are putative H+ channel ...
 96-279 1.35e-03

anti-phage ZorAB system protein ZorA; Proteins of this subfamily are putative H+ channel proteins, but it has been reported that they are also involved in anti-phage defense.


Pssm-ID: 411476 [Multi-domain]  Cd Length: 383  Bit Score: 40.13  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212   96 EQQLTQFAEKFQEVKEAARLAREKSQDGGEFTSTGLALASHQVPPSPLVSTNGPGEEKLFRSQSADTPGPTERERLKKML 175
Cdd:NF033915 205 EQSLVHIAEYSKESKEALQELHERIGDRLQESLNGMSEAMQTALTDALNNIMAPAIQTLVSTTSQQSTQVLESLVGNFMD 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212  176 SEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQlevQRAEAELLRQRVAELEAQVAVEPVRAGEKEAtsqsv 255
Cdd:NF033915 285 GMTSAGREQGLQMQQAAADVNAAVSGMSERLNQLFNSLSEQ---QGRQMERAQQQSSTFETQLQRLSGSANERQA----- 356

                        170       180
                 ....*....|....*....|....
gi 13543212  256 eQLEARVQTKDQTLKNQSTGTREA 279
Cdd:NF033915 357 -QLEQRFEELMSGLTEQLQTQLGA 379
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
166-318 3.83e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 3.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212 166 TERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAgALREANAAATQWRQQLEVQRAEAELLrQRVAELEAQVAVEPVRA 245
Cdd:COG4717  71 KELKELEEELKEAEEKEEEYAELQEELEELEEELE-ELEAELEELREELEKLEKLLQLLPLY-QELEALEAELAELPERL 148

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13543212 246 GEKEATSQSVEQLEARVQTKDQTLKNQSTGTREAPDTaEREETQQQVQDLETRNAELEQQLRAMECNLEEARA 318
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQ-LSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
191-354 4.03e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 4.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212  191 ALQDSNQRLAGALREANAAatqwRQQLEVQRAEAELLRQRVAELEAQVAVEpvrAGEKEATSQSVEQLEARVQTKDQTLK 270
Cdd:PRK02224 259 EIEDLRETIAETEREREEL----AEEVRDLRERLEELEEERDDLLAEAGLD---DADAEAVEARREELEDRDEELRDRLE 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212  271 NQSTGTREAPDTAEREetQQQVQDLETRNAELEQQLRAMECNLEEaraereraraevgrAAQLLDVRLFELSELREGLAR 350
Cdd:PRK02224 332 ECRVAAQAHNEEAESL--REDADDLEERAEELREEAAELESELEE--------------AREAVEDRREEIEELEEEIEE 395


                 ....
gi 13543212  351 LAEA 354
Cdd:PRK02224 396 LRER 399
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 191-308 4.05e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 38.12  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212   191 ALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRAgeKEATSQSVEQLEARVQTKDQTLK 270
Cdd:pfam04012  19 KAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKA--QAALTKGNEELAREALAEKKSLE 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 13543212   271 NQSTGTREAPDTAE--REETQQQVQDLETRNAELEQQLRA 308
Cdd:pfam04012  97 KQAEALETQLAQQRsaVEQLRKQLAALETKIQQLKAKKNL 136
mukB PRK04863
chromosome partition protein MukB;
184-307 4.43e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.17  E-value: 4.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212   184 QWEAEFFALQDSnqrlagaLREANAAATQWRQQLEVQRAE-AELLRQRVAELEAQVAVEPVRA--GEKEATSQSVEQLEA 260
Cdd:PRK04863  562 ELEARLESLSES-------VSEARERRMALRQQLEQLQARiQRLAARAPAWLAAQDALARLREqsGEEFEDSQDVTEYMQ 634

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 13543212   261 rvqtkdqtlknqstgtreapDTAERE-ETQQQVQDLETRNAELEQQLR 307
Cdd:PRK04863  635 --------------------QLLERErELTVERDELAARKQALDEEIE 662
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 166-355 4.87e-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: 38.88  E-value: 4.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212    166 TERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAvepvra 245
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE------ 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212    246 gEKEATSQSVEQLEARVQTKDQTLKNQSTGTREapdtaEREETQQQVQDLETRNAELEQQLRAMECNLEEARAERERARA 325
Cdd:TIGR02168  327 -ELESKLDELAEELAELEEKLEELKEELESLEA-----ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400

                          170       180       190
                   ....*....|....*....|....*....|...
gi 13543212    326 EVGRAAQL---LDVRLFELSELREGLARLAEAA 355
Cdd:TIGR02168  401 EIERLEARlerLEDRRERLQQEIEELLKKLEEA 433
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
167-310 8.48e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.21  E-value: 8.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543212 167 ERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQlEVQRAEAELLRQRVAELEAQVAVEPVRAG 246
Cdd:COG4717 317 EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE-ELEQEIAALLAEAGVEDEEELRAALEQAE 395

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13543212 247 EKEATSQSVEQLEARVQTKDQTLKNQSTGTREAPDTAEREETQQQVQDLE-------TRNAELEQQLRAME 310
Cdd:COG4717 396 EYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEeeleelrEELAELEAELEQLE 466
 
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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