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Conserved domains on  [gi|1958683516|ref|XP_038950360|]
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homer protein homolog 3 isoform X6 [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 5.20e-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: 234.16  E-value: 5.20e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516   6 EQPIFSTRAHVFQIDPATKRNWIPAGKHALTVSYFYDATRNVYRIISIGGAKAIINSTVTPNMTFTKTSQKFGQWADSRA 85
Cdd:cd01206     1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                          90       100
                  ....*....|....*....|....*....
gi 1958683516  86 NTVYGLGFGSEQQLTQFAEKFQEVKEAAR 114
Cdd:cd01206    81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
165-322 8.38e-05

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


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 8.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516 165 TERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAgALREANAAATQWRQQLEvQRAEAEHLRQRVAELEAQVAAEPVRA 244
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELE-ELEAELEELREELEKLE-KLLQLLPLYQELEALEAELAELPERL 148

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683516 245 GEKEATSQSVEQLEARVQTKDQEIQTLKNQSTGPREAPDTAEREETQQQVqvgcRTSPDLETRNAELEQQLRAMESNL 322
Cdd:COG4717   149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA----EELEELQQRLAELEEELEEAQEEL 222
 
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 5.20e-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: 234.16  E-value: 5.20e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516   6 EQPIFSTRAHVFQIDPATKRNWIPAGKHALTVSYFYDATRNVYRIISIGGAKAIINSTVTPNMTFTKTSQKFGQWADSRA 85
Cdd:cd01206     1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                          90       100
                  ....*....|....*....|....*....
gi 1958683516  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 4.02e-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: 4.02e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516   7 QPIFSTRAHVFQIDPATKRNWIPAgKHALTVSYFYDATRNVYRIISIG--GAKAIINSTVTPNMTFTKTSQKFGQWADSR 84
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*.
gi 1958683516  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 1.52e-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: 106.67  E-value: 1.52e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516    6 EQPIFSTRAHVFQIDPATKRnWIPAGKH-ALTVSYFYDATRNVYRIISI-GGAKAIINSTVTPNMTFTKTSQKFGQWADs 83
Cdd:smart00461   3 SQCIILARAVVQLYDADTKK-WVPTGEGgAANLVIDKNQRSYFFRIVGIkGQDKVIWNQELYKNFKYNQATPTFHQWAD- 80

                           90       100
                   ....*....|....*....|....*
gi 1958683516   84 rANTVYGLGFGSEQQLTQFAEKFQE 108
Cdd:smart00461  81 -DKCVYGLNFASEEEAKKFRKKVLK 104
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
165-322 8.38e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 8.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516 165 TERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAgALREANAAATQWRQQLEvQRAEAEHLRQRVAELEAQVAAEPVRA 244
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELE-ELEAELEELREELEKLE-KLLQLLPLYQELEALEAELAELPERL 148

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683516 245 GEKEATSQSVEQLEARVQTKDQEIQTLKNQSTGPREAPDTAEREETQQQVqvgcRTSPDLETRNAELEQQLRAMESNL 322
Cdd:COG4717   149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA----EELEELQQRLAELEEELEEAQEEL 222
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 96-317 4.96e-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: 4.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516   96 EQQLTQFAEKFQEVKEAARLAREKSQDggelTSTALAMASHQVPPSPLVSTNGpEEKLFRSQSADAPGPTERERLKKMLS 175
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEE----LSRQISALRKDLARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLE 771

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516  176 EGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEPVRAGEKEAT----- 250
Cdd:TIGR02168  772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQieels 851

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683516  251 ------SQSVEQLEARVQTKDQEIQTLKNQSTGPREAPDTAEREETQQQVQVGcrtspDLETRNAELEQQLRA 317
Cdd:TIGR02168  852 edieslAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR-----ELESKRSELRRELEE 919
PRK09039 PRK09039
peptidoglycan -binding protein;
215-313 1.36e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.33  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516 215 QLEVQRAEAEHLRQRV----AELEAQVAAEPVRAGEKEATSQSVEQLEARVQTK----DQEIQTLKNQSTGPREAPDTAE 286
Cdd:PRK09039   85 NLRASLSAAEAERSRLqallAELAGAGAAAEGRAGELAQELDSEKQVSARALAQvellNQQIAALRRQLAALEAALDASE 164

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958683516 287 REETQQQVQV---GCRTSPDLETRNAELEQ 313
Cdd:PRK09039  165 KRDRESQAKIadlGRRLNVALAQRVQELNR 194
 
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 5.20e-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: 234.16  E-value: 5.20e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516   6 EQPIFSTRAHVFQIDPATKRNWIPAGKHALTVSYFYDATRNVYRIISIGGAKAIINSTVTPNMTFTKTSQKFGQWADSRA 85
Cdd:cd01206     1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                          90       100
                  ....*....|....*....|....*....
gi 1958683516  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 4.02e-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: 4.02e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516   7 QPIFSTRAHVFQIDPATKRNWIPAgKHALTVSYFYDATRNVYRIISIG--GAKAIINSTVTPNMTFTKTSQKFGQWADSR 84
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*.
gi 1958683516  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 7.24e-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: 131.04  E-value: 7.24e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516   8 PIFSTRAHVFQIDPATKrNWIPA-GKHALTVSYFYDATRNVYRIISIGGA--KAIINSTVTPNMTFTKTSQKFGQWADSR 84
Cdd:cd00837     1 SIFSARAHVMQIDDSNK-NWVPAgGKGASRVSYFKDTTRNSFRIIGVDIKdkKVVINCTITKNLVYNKATQTFHQWADDR 79

                          90       100
                  ....*....|....*....|....*.
gi 1958683516  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 1.52e-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: 106.67  E-value: 1.52e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516    6 EQPIFSTRAHVFQIDPATKRnWIPAGKH-ALTVSYFYDATRNVYRIISI-GGAKAIINSTVTPNMTFTKTSQKFGQWADs 83
Cdd:smart00461   3 SQCIILARAVVQLYDADTKK-WVPTGEGgAANLVIDKNQRSYFFRIVGIkGQDKVIWNQELYKNFKYNQATPTFHQWAD- 80

                           90       100
                   ....*....|....*....|....*
gi 1958683516   84 rANTVYGLGFGSEQQLTQFAEKFQE 108
Cdd:smart00461  81 -DKCVYGLNFASEEEAKKFRKKVLK 104
EVH1_Ena_VASP-like cd01207
Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: ...
 8-103 4.84e-12

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


Pssm-ID: 269918  Cd Length: 108  Bit Score: 61.94  E-value: 4.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516   8 PIFSTRAHVFQIDPATKRnWIPAG-KHALTVSYFYDATR-NVYRIIsigGAKA-----IINSTVTPNMTFTKTSQKFGQW 80
Cdd:cd01207     1 SVASARASVMVYDDENKR-WVPSGgSQGLSRVQIYHNTRnNTFRVV---GRKLqdhevVINCAILKGLKYNQATPTFHQW 76

                          90       100
                  ....*....|....*....|...
gi 1958683516  81 ADSRanTVYGLGFGSEQQLTQFA 103
Cdd:cd01207    77 RDAR--QVYGLNFASKEEATEFA 97
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
165-322 8.38e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 8.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516 165 TERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAgALREANAAATQWRQQLEvQRAEAEHLRQRVAELEAQVAAEPVRA 244
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELE-ELEAELEELREELEKLE-KLLQLLPLYQELEALEAELAELPERL 148

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683516 245 GEKEATSQSVEQLEARVQTKDQEIQTLKNQSTGPREAPDTAEREETQQQVqvgcRTSPDLETRNAELEQQLRAMESNL 322
Cdd:COG4717   149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA----EELEELQQRLAELEEELEEAQEEL 222
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 202-319 8.83e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 8.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516 202 LREANAAATQWR---QQLEVQRAEAEHLRQRVAELEAQVAAepvRAGEKEATSQSVEQLEARVQTKDQEIQTLknqstgp 278
Cdd:COG1196   224 ELEAELLLLKLReleAELEELEAELEELEAELEELEAELAE---LEAELEELRLELEELELELEEAQAEEYEL------- 293

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958683516 279 reapdTAEREETQQQVQVGCRTSPDLETRNAELEQQLRAME 319
Cdd:COG1196   294 -----LAELARLEQDIARLEERRRELEERLEELEEELAELE 329
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 190-322 1.78e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516 190 ALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEpvRAGEKEATSQSVEQLEARVQTKDQEIQ 269
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA--EEALLEAEAELAEAEEELEELAEELLE 390

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958683516 270 TLKnqstgpREAPDTAEREETQQQVQvgcrtspDLETRNAELEQQLRAMESNL 322
Cdd:COG1196   391 ALR------AAAELAAQLEELEEAEE-------ALLERLERLEEELEELEEAL 430
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 103-319 1.87e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516 103 AEKFQEVKEAARLAreksqdggELTSTALAMASHQVppsplvstngpEEKLFRSQSADApgPTERERLKKMLSEGSVGEV 182
Cdd:COG1196   212 AERYRELKEELKEL--------EAELLLLKLRELEA-----------ELEELEAELEEL--EAELEELEAELAELEAELE 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516 183 QWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEpvrAGEKEATSQSVEQLEARVQ 262
Cdd:COG1196   271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL---EEELEELEEELEELEEELE 347

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683516 263 TKDQEIQTLKNQstgpREAPDTAEREETQQQVQvgcrtspDLETRNAELEQQLRAME 319
Cdd:COG1196   348 EAEEELEEAEAE----LAEAEEALLEAEAELAE-------AEEELEELAEELLEALR 393
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 96-317 4.96e-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: 4.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516   96 EQQLTQFAEKFQEVKEAARLAREKSQDggelTSTALAMASHQVPPSPLVSTNGpEEKLFRSQSADAPGPTERERLKKMLS 175
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEE----LSRQISALRKDLARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLE 771

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516  176 EGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEPVRAGEKEAT----- 250
Cdd:TIGR02168  772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQieels 851

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683516  251 ------SQSVEQLEARVQTKDQEIQTLKNQSTGPREAPDTAEREETQQQVQVGcrtspDLETRNAELEQQLRA 317
Cdd:TIGR02168  852 edieslAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR-----ELESKRSELRRELEE 919
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 150-291 1.13e-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: 41.09  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516  150 EEKLFRSQSAdapgpterERLKKMLSEGSVGEVQWEAEFFALQDSNQ----RLAGALREANAAATQWRQQLEVQRAEAEH 225
Cdd:COG3096    525 EQRLRQQQNA--------ERLLEEFCQRIGQQLDAAEELEELLAELEaqleELEEQAAEAVEQRSELRQQLEQLRARIKE 596

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958683516  226 LRQRV-AELEAQVAAEPVRA--GEKEATSQSVEQLEARVQTKDQEIQTLKNQSTGPREAPDTAEREETQ 291
Cdd:COG3096    597 LAARApAWLAAQDALERLREqsGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQ 665
PRK09039 PRK09039
peptidoglycan -binding protein;
215-313 1.36e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.33  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516 215 QLEVQRAEAEHLRQRV----AELEAQVAAEPVRAGEKEATSQSVEQLEARVQTK----DQEIQTLKNQSTGPREAPDTAE 286
Cdd:PRK09039   85 NLRASLSAAEAERSRLqallAELAGAGAAAEGRAGELAQELDSEKQVSARALAQvellNQQIAALRRQLAALEAALDASE 164

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958683516 287 REETQQQVQV---GCRTSPDLETRNAELEQ 313
Cdd:PRK09039  165 KRDRESQAKIadlGRRLNVALAQRVQELNR 194
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 196-323 2.50e-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: 40.04  E-value: 2.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516  196 QRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAepvRAGEKEATSQSVEQLEARVQTKDQEIQTLKNQS 275
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA---LRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958683516  276 TGPREapdtaEREETQQQVQVGCRTSPDLETRNAELEQQLRAMESNLE 323
Cdd:TIGR02168  764 EELEE-----RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-320 2.56e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 2.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516  165 TERERLKKMLSEGsvgevqwEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVA--AEPV 242
Cdd:TIGR02168  351 EELESLEAELEEL-------EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErlQQEI 423

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516  243 RAGEKEATSQSVEQLEARVQTKDQEIQTLKNQSTGPREAPDTA--EREETQQQVQvgcrtspDLETRNAELEQQLRAMES 320
Cdd:TIGR02168  424 EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELreELEEAEQALD-------AAERELAQLQARLDSLER 496
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
186-322 3.60e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 3.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516  186 AEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAaepvragekEATSQSVEQLEARVQTKD 265
Cdd:COG4913    281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIR---------GNGGDRLEQLEREIERLE 351

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958683516  266 QEIQTLKNQSTGPRE--------APDTAER-EETQQQVQvgcRTSPDLETRNAELEQQLRAMESNL 322
Cdd:COG4913    352 RELEERERRRARLEAllaalglpLPASAEEfAALRAEAA---ALLEALEEELEALEEALAEAEAAL 414
mukB PRK04863
chromosome partition protein MukB;
168-292 5.00e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 38.78  E-value: 5.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516  168 ERLKKMLSEGSVGEVQWEAEFFALQdsnQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELE--------AQVAA 239
Cdd:PRK04863   536 ERLLAEFCKRLGKNLDDEDELEQLQ---EELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAarapawlaAQDAL 612

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958683516  240 EPVRA--GEKEATSQSVEQLEARVQTKDQEIQTLKNQSTGPREAPDtAEREETQQ 292
Cdd:PRK04863   613 ARLREqsGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALD-EEIERLSQ 666
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 205-318 5.45e-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: 38.21  E-value: 5.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516 205 ANAAATQWRQQLEVQRAEaehLRQRVAELEAQVAAEpvrAGEKEATSQSVEQLEARVQTKDQEIQTLKNQSTGPREAPDT 284
Cdd:COG4942    14 AAAAQADAAAEAEAELEQ---LQQEIAELEKELAAL---KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958683516 285 AEREETQQQVQvgcrtspdLETRNAELEQQLRAM 318
Cdd:COG4942    88 LEKEIAELRAE--------LEAQKEELAELLRAL 113
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 185-322 5.56e-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: 5.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516  185 EAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEHLRQRVAELEAQVAAEPVRageKEATSQSVEQLEARVQTK 264
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER---LANLERQLEELEAQLEEL 328

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516  265 DQEIQTLKNQST--GPREAPDTAEREETQQQVQVGCRTSPDLETRNAELEQQLRAMESNL 322
Cdd:TIGR02168  329 ESKLDELAEELAelEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
185-322 5.71e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 5.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516  185 EAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEH--LRQRVAELEAQVAAEpvragekEATSQSVEQLEARVQ 262
Cdd:COG4913    623 EEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVasAEREIAELEAELERL-------DASSDDLAALEEQLE 695

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516  263 TKDQEIQTLKnqstgpreapdtAEREETQQQVQvgcrtspDLETRNAELEQQLRAMESNL 322
Cdd:COG4913    696 ELEAELEELE------------EELDELKGEIG-------RLEKELEQAEEELDELQDRL 736
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 190-289 6.29e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 38.50  E-value: 6.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683516  190 ALQDSNQRLaGALREANAAATQwrQQLEVQRAEAEHLRQRVAELE-AQVAAEpvraGEKEATSQSVEQLEARVQTKDQEI 268
Cdd:PRK10929   152 QLNEIERRL-QTLGTPNTPLAQ--AQLTALQAESAALKALVDELElAQLSAN----NRQELARLRSELAKKRSQQLDAYL 224

                           90       100
                   ....*....|....*....|...
gi 1958683516  269 QTLKNQ--STGPREAPDTAEREE 289
Cdd:PRK10929   225 QALRNQlnSQRQREAERALESTE 247
 
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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