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Conserved domains on  [gi|564388554|ref|XP_006252953|]
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homer protein homolog 3 isoform X4 [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 1.02e-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: 1.02e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554   6 EQPIFSTRAHVFQIDPATKRNWIPAGKHALTVSYFYDATRNVYRIISIGGAKAIINSTVTPNMTFTKTSQKFGQWADSRA 85
Cdd:cd01206    1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                         90       100
                 ....*....|....*....|....*....
gi 564388554  86 NTVYGLGFGSEQQLTQFAEKFQEVKEAAR 114
Cdd:cd01206   81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 95-338 4.21e-08

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.06  E-value: 4.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554    95 SEQQLTQFAEKFQEVKEAARLAREKSQDGGELTSTALAMASHQVppsplvstngpeEKLFRSQSADAPGPTERERLKKML 174
Cdd:TIGR02168  265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR------------ERLANLERQLEELEAQLEELESKL 332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554   175 SEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEpvrAGEKEATSQSV 254
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---NNEIERLEARL 409

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554   255 EQLEARVQTKDQEIQTLKNQSTGPREAPDTAEREETQQQVQDLETRNAELEQQLRAMESNLEEARAERERARAEVGRAAQ 334
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489


                   ....
gi 564388554   335 LLDV 338
Cdd:TIGR02168  490 RLDS 493
 
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 1.02e-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: 1.02e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554   6 EQPIFSTRAHVFQIDPATKRNWIPAGKHALTVSYFYDATRNVYRIISIGGAKAIINSTVTPNMTFTKTSQKFGQWADSRA 85
Cdd:cd01206    1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                         90       100
                 ....*....|....*....|....*....
gi 564388554  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 4.53e-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: 144.90  E-value: 4.53e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554    7 QPIFSTRAHVFQIDPATKRNWIPAgKHALTVSYFYDATRNVYRIISIG--GAKAIINSTVTPNMTFTKTSQKFGQWADSR 84
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*.
gi 564388554   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 1.46e-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: 1.46e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554     6 EQPIFSTRAHVFQIDPATKRnWIPAGKH-ALTVSYFYDATRNVYRIISI-GGAKAIINSTVTPNMTFTKTSQKFGQWADs 83
Cdd:smart00461   3 SQCIILARAVVQLYDADTKK-WVPTGEGgAANLVIDKNQRSYFFRIVGIkGQDKVIWNQELYKNFKYNQATPTFHQWAD- 80

                           90       100
                   ....*....|....*....|....*
gi 564388554    84 rANTVYGLGFGSEQQLTQFAEKFQE 108
Cdd:smart00461  81 -DKCVYGLNFASEEEAKKFRKKVLK 104
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 95-338 4.21e-08

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: 55.06  E-value: 4.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554    95 SEQQLTQFAEKFQEVKEAARLAREKSQDGGELTSTALAMASHQVppsplvstngpeEKLFRSQSADAPGPTERERLKKML 174
Cdd:TIGR02168  265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR------------ERLANLERQLEELEAQLEELESKL 332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554   175 SEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEpvrAGEKEATSQSV 254
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---NNEIERLEARL 409

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554   255 EQLEARVQTKDQEIQTLKNQSTGPREAPDTAEREETQQQVQDLETRNAELEQQLRAMESNLEEARAERERARAEVGRAAQ 334
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489


                   ....
gi 564388554   335 LLDV 338
Cdd:TIGR02168  490 RLDS 493
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 103-357 4.90e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 4.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554 103 AEKFQEVKEAARLAreksqdggELTSTALAMASHQVppsplvstngpEEKLFRSQSADApgPTERERLKKMLSEGSVGEV 182
Cdd:COG1196  212 AERYRELKEELKEL--------EAELLLLKLRELEA-----------ELEELEAELEEL--EAELEELEAELAELEAELE 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554 183 QWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEpvrAGEKEATSQSVEQLEARVQ 262
Cdd:COG1196  271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL---EEELEELEEELEELEEELE 347

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554 263 TKDQEIQTLKNQSTGPREApDTAEREETQQQVQDLETRNAELEQQLRAMESNLEEARAERERARAEVGRAAQLLDVRLFE 342
Cdd:COG1196  348 EAEEELEEAEAELAEAEEA-LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426

                        250
                 ....*....|....*
gi 564388554 343 LSELREGLARLAEAA 357
Cdd:COG1196  427 EEALAELEEEEEEEE 441
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
191-357 4.72e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 4.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554 191 LQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEPVRAG-----------EKEATSQSVEQLEA 259
Cdd:PRK02224 354 LEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGnaedfleelreERDELREREAELEA 433

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554 260 RVQTKD---QEIQTLKNQSTGP------REAPDTAEREETQQQVQDLETRNAELEQQLRAMES------NLEEARAERER 324
Cdd:PRK02224 434 TLRTARervEEAEALLEAGKCPecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEErleraeDLVEAEDRIER 513

                        170       180       190
                 ....*....|....*....|....*....|...
gi 564388554 325 ARAEVGRAAQLLDVRLFELSELREGLARLAEAA 357
Cdd:PRK02224 514 LEERREDLEELIAERRETIEEKRERAEELRERA 546
 
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 1.02e-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: 1.02e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554   6 EQPIFSTRAHVFQIDPATKRNWIPAGKHALTVSYFYDATRNVYRIISIGGAKAIINSTVTPNMTFTKTSQKFGQWADSRA 85
Cdd:cd01206    1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                         90       100
                 ....*....|....*....|....*....
gi 564388554  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 4.53e-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: 144.90  E-value: 4.53e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554    7 QPIFSTRAHVFQIDPATKRNWIPAgKHALTVSYFYDATRNVYRIISIG--GAKAIINSTVTPNMTFTKTSQKFGQWADSR 84
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*.
gi 564388554   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 3.54e-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: 3.54e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554   8 PIFSTRAHVFQIDPATKrNWIPA-GKHALTVSYFYDATRNVYRIISIGGA--KAIINSTVTPNMTFTKTSQKFGQWADSR 84
Cdd:cd00837    1 SIFSARAHVMQIDDSNK-NWVPAgGKGASRVSYFKDTTRNSFRIIGVDIKdkKVVINCTITKNLVYNKATQTFHQWADDR 79

                         90       100
                 ....*....|....*....|....*.
gi 564388554  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 1.46e-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: 1.46e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554     6 EQPIFSTRAHVFQIDPATKRnWIPAGKH-ALTVSYFYDATRNVYRIISI-GGAKAIINSTVTPNMTFTKTSQKFGQWADs 83
Cdd:smart00461   3 SQCIILARAVVQLYDADTKK-WVPTGEGgAANLVIDKNQRSYFFRIVGIkGQDKVIWNQELYKNFKYNQATPTFHQWAD- 80

                           90       100
                   ....*....|....*....|....*
gi 564388554    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 5.16e-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: 5.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554   8 PIFSTRAHVFQIDPATKRnWIPAG-KHALTVSYFYDATR-NVYRIIsigGAKA-----IINSTVTPNMTFTKTSQKFGQW 80
Cdd:cd01207    1 SVASARASVMVYDDENKR-WVPSGgSQGLSRVQIYHNTRnNTFRVV---GRKLqdhevVINCAILKGLKYNQATPTFHQW 76

                         90       100
                 ....*....|....*....|...
gi 564388554  81 ADSRanTVYGLGFGSEQQLTQFA 103
Cdd:cd01207   77 RDAR--QVYGLNFASKEEATEFA 97
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 95-338 4.21e-08

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: 55.06  E-value: 4.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554    95 SEQQLTQFAEKFQEVKEAARLAREKSQDGGELTSTALAMASHQVppsplvstngpeEKLFRSQSADAPGPTERERLKKML 174
Cdd:TIGR02168  265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR------------ERLANLERQLEELEAQLEELESKL 332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554   175 SEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEpvrAGEKEATSQSV 254
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---NNEIERLEARL 409

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554   255 EQLEARVQTKDQEIQTLKNQSTGPREAPDTAEREETQQQVQDLETRNAELEQQLRAMESNLEEARAERERARAEVGRAAQ 334
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489


                   ....
gi 564388554   335 LLDV 338
Cdd:TIGR02168  490 RLDS 493
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 103-357 4.90e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 4.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554 103 AEKFQEVKEAARLAreksqdggELTSTALAMASHQVppsplvstngpEEKLFRSQSADApgPTERERLKKMLSEGSVGEV 182
Cdd:COG1196  212 AERYRELKEELKEL--------EAELLLLKLRELEA-----------ELEELEAELEEL--EAELEELEAELAELEAELE 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554 183 QWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEpvrAGEKEATSQSVEQLEARVQ 262
Cdd:COG1196  271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL---EEELEELEEELEELEEELE 347

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554 263 TKDQEIQTLKNQSTGPREApDTAEREETQQQVQDLETRNAELEQQLRAMESNLEEARAERERARAEVGRAAQLLDVRLFE 342
Cdd:COG1196  348 EAEEELEEAEAELAEAEEA-LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426

                        250
                 ....*....|....*
gi 564388554 343 LSELREGLARLAEAA 357
Cdd:COG1196  427 EEALAELEEEEEEEE 441
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 166-357 1.03e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554 166 ERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVA-AEPVRA 244
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEeAEEELE 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554 245 GEKEATSQSVEQLEARVQTKDQEIQTLKNQstgpreapdTAEREETQQQVQDLETRNAELEQQLRAMESNLEEARAERER 324
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEELEEL---------AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425

                        170       180       190
                 ....*....|....*....|....*....|...
gi 564388554 325 ARAEVGRAAQLLDVRLFELSELREGLARLAEAA 357
Cdd:COG1196  426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
165-315 2.89e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 2.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554 165 TERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAgALREANAAATQWRQQLEvQRAEAEHLRQRVAELEAQVAAEPVRA 244
Cdd:COG4717   71 KELKELEEELKEAEEKEEEYAELQEELEELEEELE-ELEAELEELREELEKLE-KLLQLLPLYQELEALEAELAELPERL 148

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564388554 245 GEKEATSQSVEQLEARVQTKDQEIQTLKNQSTGPREAPDTAEREE---TQQQVQDLETRNAELEQQLRAMESNL 315
Cdd:COG4717  149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdLAEELEELQQRLAELEEELEEAQEEL 222
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 166-357 4.12e-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: 4.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554 166 ERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEpvrAG 245
Cdd:COG1196  317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA---LR 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554 246 EKEATSQSVEQLEARVQTKDQEIQTLKNQstgpREAPDTAEREETQQQVQDLETRNAELEQQLRAMESNLEEARAERERA 325
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEE----LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469

                        170       180       190
                 ....*....|....*....|....*....|..
gi 564388554 326 RAEVGRAAQLLDVRLFELSELREGLARLAEAA 357
Cdd:COG1196  470 EEAALLEAALAELLEELAEAAARLLLLLEAEA 501
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 166-357 4.27e-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: 4.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554 166 ERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEPVRAG 245
Cdd:COG1196  324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554 246 EKEATSQSVEQLEARVQTKDQEIQTLKNQSTGPREApDTAEREETQQQVQDLETRNAELEQQLRAMESNLEEARAERERA 325
Cdd:COG1196  404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEE-EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                        170       180       190
                 ....*....|....*....|....*....|..
gi 564388554 326 RAEVGRAAQLLDVRLfELSELREGLARLAEAA 357
Cdd:COG1196  483 LEELAEAAARLLLLL-EAEADYEGFLEGVKAA 513
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 183-356 4.74e-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: 4.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554 183 QWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQV-AAEPVRAGEKEATSQSVEQLEARV 261
Cdd:COG1196  299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELeEAEAELAEAEEALLEAEAELAEAE 378

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554 262 QTKDQEIQTLKNQSTgpREAPDTAEREETQQQVQDLETRNAELEQQLRAMESNLEEARAE--------RERARAEVGRAA 333
Cdd:COG1196  379 EELEELAEELLEALR--AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEeeeeeealEEAAEEEAELEE 456

                        170       180
                 ....*....|....*....|...
gi 564388554 334 QLLDVRLfELSELREGLARLAEA 356
Cdd:COG1196  457 EEEALLE-LLAELLEEAALLEAA 478
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 196-357 6.71e-05

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: 45.05  E-value: 6.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554   196 QRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAepvRAGEKEATSQSVEQLEARVQTKDQEIQTLKNQS 275
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA---LRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554   276 TGPREAPD--TAEREETQQQVQDLETRNAELEQQLRAMESNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARL 353
Cdd:TIGR02168  764 EELEERLEeaEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843


                   ....
gi 564388554   354 AEAA 357
Cdd:TIGR02168  844 EEQI 847
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
202-356 4.32e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 4.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554  202 LREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEPVRAGEKEATS--QSVEQLEARVQTKDQEIQTLKNQ---ST 276
Cdd:COG4913   257 IRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARleAELERLEARLDALREELDELEAQirgNG 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554  277 GPREAPDTAEREETQQQVQDLETRNAELEQQLRAMESNLEEARAERERARAevgRAAQLLDVRLFELSELREGLARLAEA 356
Cdd:COG4913   337 GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA---EAAALLEALEEELEALEEALAEAEAA 413
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 219-353 6.18e-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: 41.97  E-value: 6.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554   219 QRAEAEHLRQRVAELEAQVaaepvRAGEKE--ATSQSVEQLEARVQTKDQEIQTLKNQSTGPREAPDTAEREETQ--QQV 294
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKI-----AELEKAlaELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQleERI 749

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 564388554   295 QDLETRNAELEQQLRAMESNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARL 353
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 96-351 6.23e-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: 41.97  E-value: 6.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554    96 EQQLTQFAEKFQEVKEAARLAREKSQDggelTSTALAMASHQVPPSPLVSTNGpEEKLFRSQSADAPGPTERERLKKMLS 175
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEE----LSRQISALRKDLARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLE 771

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554   176 EGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEPVRAGE----KEATS 251
Cdd:TIGR02168  772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDleeqIEELS 851

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554   252 QSVEQLEARVQTKDQEIQTLKNQSTGpreapDTAEREETQQQVQDLETRNAELEQQLRAMESNLEEARAERERARAEVGR 331
Cdd:TIGR02168  852 EDIESLAAEIEELEELIEELESELEA-----LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926

                          250       260
                   ....*....|....*....|
gi 564388554   332 AAQLLDVRLFELSELREGLA 351
Cdd:TIGR02168  927 LELRLEGLEVRIDNLQERLS 946
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
196-357 7.09e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 7.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554  196 QRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEaqvaaepvRAGEKEATSQSVEQLEARVQTKDQEIQTLKNQS 275
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQ--------RLAEYSWDEIDVASAEREIAELEAELERLDASS 684

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554  276 TGPREApdTAEREETQQQVQDLETRNAELEQQLRAMESNLEEARAERERARAEVGRAAQLLDVRLFELSElreglARLAE 355
Cdd:COG4913   685 DDLAAL--EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE-----ERFAA 757


                  ..
gi 564388554  356 AA 357
Cdd:COG4913   758 AL 759
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
190-309 1.45e-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: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554  190 ALQDSNQRLAgALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEpvrAGEKEATSQSVEQLEARVQTKDQEIQ 269
Cdd:COG4913   669 EIAELEAELE-RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRL---EKELEQAEEELDELQDRLEAAEDLAR 744

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 564388554  270 TLKNQSTGPR---EAPDTAE---REETQQQVQDLETRNAELEQQLR 309
Cdd:COG4913   745 LELRALLEERfaaALGDAVErelRENLEERIDALRARLNRAEEELE 790
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 166-358 1.46e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554   166 ERERLKKMLSEGSVGEVQWEAEFfaLQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQvaaepvrag 245
Cdd:TIGR02169  780 ALNDLEARLSHSRIPEIQAELSK--LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ--------- 848

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554   246 eKEATSQSVEQLEARVQTKDQEIQTLKnqstgpreapdtAEREETQQQVQDLETRNAELEQQLRAMESNLEEARAERERA 325
Cdd:TIGR02169  849 -IKSIEKEIENLNGKKEELEEELEELE------------AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK 915

                          170       180       190
                   ....*....|....*....|....*....|...
gi 564388554   326 RAEVGRAAQLLDVRLFELSELREGLARLAEAAP 358
Cdd:TIGR02169  916 RKRLSELKAKLEALEEELSEIEDPKGEDEEIPE 948
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
185-315 1.83e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554  185 EAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEH---------LRQRVAELEAQVAAEpvragekEATSQSVE 255
Cdd:COG4913   616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeidvasAEREIAELEAELERL-------DASSDDLA 688

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554  256 QLEARVQTKDQEIQTLKnqstgpreapdtAEREETQQQVQDLETRNAELEQQLRAMESNL 315
Cdd:COG4913   689 ALEEQLEELEAELEELE------------EELDELKGEIGRLEKELEQAEEELDELQDRL 736
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 205-311 2.57e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 2.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554 205 ANAAATQWRQQLEVQRAEaehLRQRVAELEAQVAAEpvrAGEKEATSQSVEQLEARVQTKDQEIQTLKNQSTGPREAPDT 284
Cdd:COG4942   14 AAAAQADAAAEAEAELEQ---LQQEIAELEKELAAL---KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87

                         90       100
                 ....*....|....*....|....*..
gi 564388554 285 AEREETQQQvQDLETRNAELEQQLRAM 311
Cdd:COG4942   88 LEKEIAELR-AELEAQKEELAELLRAL 113
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
213-358 2.57e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554  213 RQQLEVQRAEAEHLRQRVAELEAQVAAepvRAGEKEATSQSVEQLEARVQTKDQEIQTlknqstgpreAPDTAEREETQQ 292
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEA---LEAELDALQERREALQRLAEYSWDEIDV----------ASAEREIAELEA 675

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564388554  293 QVQDLETRN---AELEQQLRAMESNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARLAEAAP 358
Cdd:COG4913   676 ELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
191-311 2.64e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554 191 LQDSNQRLAGA---LREANAAATQWRQQLEVQRAEA---------EHLRQRVAELEAQVAAEPVRAGEKeatSQSVEQLE 258
Cdd:COG3206  221 LSELESQLAEAraeLAEAEARLAALRAQLGSGPDALpellqspviQQLRAQLAELEAELAELSARYTPN---HPDVIALR 297

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564388554 259 ARVQTKDQEIQTLKNQSTGPREApdtaEREETQQQVQDLETRNAELEQQLRAM 311
Cdd:COG3206  298 AQIAALRAQLQQEAQRILASLEA----ELEALQAREASLQAQLAQLEARLAEL 346
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
191-357 4.72e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 4.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554 191 LQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEPVRAG-----------EKEATSQSVEQLEA 259
Cdd:PRK02224 354 LEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGnaedfleelreERDELREREAELEA 433

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554 260 RVQTKD---QEIQTLKNQSTGP------REAPDTAEREETQQQVQDLETRNAELEQQLRAMES------NLEEARAERER 324
Cdd:PRK02224 434 TLRTARervEEAEALLEAGKCPecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEErleraeDLVEAEDRIER 513

                        170       180       190
                 ....*....|....*....|....*....|...
gi 564388554 325 ARAEVGRAAQLLDVRLFELSELREGLARLAEAA 357
Cdd:PRK02224 514 LEERREDLEELIAERRETIEEKRERAEELRERA 546
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
202-319 5.74e-03

Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 38.29  E-value: 5.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554 202 LREANAAATQWRQQLEV--QRAEAEHLRQRVAELEAQVAAEPVRAGEKEAT----SQSVEQLEARVQTKDQEIQTLKNQS 275
Cdd:COG3524  193 LRDAREALLAFRNRNGIldPEATAEALLQLIATLEGQLAELEAELAALRSYlspnSPQVRQLRRRIAALEKQIAAERARL 272

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 564388554 276 TGPREAPDTAEReetQQQVQDLETRNAELEQQLRAMESNLEEAR 319
Cdd:COG3524  273 TGASGGDSLASL---LAEYERLELEREFAEKAYTSALAALEQAR 313
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 151-309 6.44e-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: 38.78  E-value: 6.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554  151 EKLFRSQSadapgptERERLKKMLSEGSVGEVQWEAEFFALQDSNQ----RLAGALREANAAATQWRQQLEVQRAEAEHL 226
Cdd:COG3096   525 EQRLRQQQ-------NAERLLEEFCQRIGQQLDAAEELEELLAELEaqleELEEQAAEAVEQRSELRQQLEQLRARIKEL 597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554  227 RQRV-AELEAQVAAEPVRA--GEKEATSQSVeqLEARVQTKDQEiqtlknqstgpREApdTAEREETQQQVQdletrnaE 303
Cdd:COG3096   598 AARApAWLAAQDALERLREqsGEALADSQEV--TAAMQQLLERE-----------REA--TVERDELAARKQ-------A 655


                  ....*.
gi 564388554  304 LEQQLR 309
Cdd:COG3096   656 LESQIE 661
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
186-323 6.73e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 6.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554  186 AEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAaepvragekEATSQSVEQLEARVQTKD 265
Cdd:COG4913   281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIR---------GNGGDRLEQLEREIERLE 351

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564388554  266 QEIQTLKNQSTGPREA--------PDTAE-----REETQQQVQDLETRNAELEQQLRAMESNLEEARAERE 323
Cdd:COG4913   352 RELEERERRRARLEALlaalglplPASAEefaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 190-348 9.45e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 38.11  E-value: 9.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554  190 ALQDSNQRLaGALREANAAATQwrQQLEVQRAEAEHLRQRVAELE-AQVAAEpvraGEKEATSQSVEQLEARVQTKDQEI 268
Cdd:PRK10929  152 QLNEIERRL-QTLGTPNTPLAQ--AQLTALQAESAALKALVDELElAQLSAN----NRQELARLRSELAKKRSQQLDAYL 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554  269 QTLKNQ--STGPREAPDTAER-EETQQQVQDLE-------TRNAELEQQL--RAMESNLEEARAEREraraevgrAAQLL 336
Cdd:PRK10929  225 QALRNQlnSQRQREAERALEStELLAEQSGDLPksivaqfKINRELSQALnqQAQRMDLIASQQRQA--------ASQTL 296

                         170
                  ....*....|..
gi 564388554  337 DVRLfELSELRE 348
Cdd:PRK10929  297 QVRQ-ALNTLRE 307
mukB PRK04863
chromosome partition protein MukB;
168-306 9.91e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 38.01  E-value: 9.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564388554  168 ERLKKMLSEGSVGEVQWEAEFFALQdsnQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQvaaEPVRAGEK 247
Cdd:PRK04863  536 ERLLAEFCKRLGKNLDDEDELEQLQ---EELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAAR---APAWLAAQ 609

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564388554  248 EATSQSVEQLEARVQTKDQEIQTLKNQSTGPREApdTAEREETQQQVQDLETRNAELEQ 306
Cdd:PRK04863  610 DALARLREQSGEEFEDSQDVTEYMQQLLEREREL--TVERDELAARKQALDEEIERLSQ 666
 
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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