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Conserved domains on  [gi|1907189452|ref|XP_036009954|]
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homer protein homolog 3 isoform X3 [Mus musculus]

Protein Classification

PH domain-containing protein( domain architecture ID 106840)

Pleckstrin homology (PH) domain-containing protein may be involved in targeting a protein to the appropriate cellular location or interacting with a binding partner

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 58-116 3.56e-38

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd01206:

Pssm-ID: 473070  Cd Length: 109  Bit Score: 132.47  E-value: 3.56e-38
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189452  58 SQAIINSTVTPNMTFTKTSQKFGQWADSRANTVYGLGFASEQQLTQFAEKFQEVKEAAR 116
Cdd:cd01206    51 SKAIINSTITPNMTFTKTSQKFGQWADSRANTVYGLGFASEAELTKFAEKFQEAKEAAK 109
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 168-341 2.28e-07

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: 52.75  E-value: 2.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452  168 TERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEpvrA 247
Cdd:TIGR02168  323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---N 399

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452  248 GEKEATSQSVEQLEARVQTKDQEIQTLKNQSTGTREAPDTAEREETQQQVQDLETRNAELEQQLRSMECNLEEARAERER 327
Cdd:TIGR02168  400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479

                          170
                   ....*....|....
gi 1907189452  328 ARAEVGRAAQLLDV 341
Cdd:TIGR02168  480 AERELAQLQARLDS 493
 
Name Accession Description Interval E-value
EVH1_Homer_Vesl cd01206
Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, ...
 58-116 3.56e-38

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: 132.47  E-value: 3.56e-38
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189452  58 SQAIINSTVTPNMTFTKTSQKFGQWADSRANTVYGLGFASEQQLTQFAEKFQEVKEAAR 116
Cdd:cd01206    51 SKAIINSTITPNMTFTKTSQKFGQWADSRANTVYGLGFASEAELTKFAEKFQEAKEAAK 109
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 57-112 6.10e-20

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: 84.04  E-value: 6.10e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189452  57 HSQAIINSTVTPNMTFTKTSQKFGQWADSRAntVYGLGFASEQQLTQFAEKFQEVK 112
Cdd:pfam00568  58 DGKVIWNQEIYPNMEYNQARPFFHTFADSRC--VYGLNFASEEEATKFAKAVQEAL 111
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 55-110 7.35e-13

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: 64.30  E-value: 7.35e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189452   55 NVHSQAIINSTVTPNMTFTKTSQKFGQWADsrANTVYGLGFASEQQLTQFAEKFQE 110
Cdd:smart00461  51 KGQDKVIWNQELYKNFKYNQATPTFHQWAD--DKCVYGLNFASEEEAKKFRKKVLK 104
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 168-341 2.28e-07

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: 52.75  E-value: 2.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452  168 TERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEpvrA 247
Cdd:TIGR02168  323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---N 399

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452  248 GEKEATSQSVEQLEARVQTKDQEIQTLKNQSTGTREAPDTAEREETQQQVQDLETRNAELEQQLRSMECNLEEARAERER 327
Cdd:TIGR02168  400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479

                          170
                   ....*....|....
gi 1907189452  328 ARAEVGRAAQLLDV 341
Cdd:TIGR02168  480 AERELAQLQARLDS 493
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 188-360 1.01e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452 188 EAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEpvrAGEKEATSQSVEQLEARVQTK 267
Cdd:COG1196   252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL---EERRRELEERLEELEEELAEL 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452 268 DQEIQTLKNQSTGTRE--APDTAEREETQQQVQDLETRNAELEQQLRSMECNLEEARAERERARAEVGRAAQLLDVRLFE 345
Cdd:COG1196   329 EEELEELEEELEELEEelEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408

                         170
                  ....*....|....*
gi 1907189452 346 LSELREGLARLAEAA 360
Cdd:COG1196   409 EEALLERLERLEEEL 423
mukB PRK04863
chromosome partition protein MukB;
186-314 8.16e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 38.40  E-value: 8.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452  186 QWEAEFFALQDSnqrlagaLREANAAATQWRQQLEVQRAE-AELLRQRVAELEAQVAVEPVRA--GEKEATSQSVEQLea 262
Cdd:PRK04863   562 ELEARLESLSES-------VSEARERRMALRQQLEQLQARiQRLAARAPAWLAAQDALARLREqsGEEFEDSQDVTEY-- 632

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907189452  263 rvqtkdqeIQTLknqstgtreapdtAERE-ETQQQVQDLETRNAELEQQLRSM 314
Cdd:PRK04863   633 --------MQQL-------------LERErELTVERDELAARKQALDEEIERL 664
antiphage_ZorA_2 NF033915
anti-phage ZorAB system protein ZorA; Proteins of this subfamily are putative H+ channel ...
 98-264 8.78e-03

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


Pssm-ID: 411476 [Multi-domain]  Cd Length: 383  Bit Score: 37.82  E-value: 8.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452  98 EQQLTQFAEKFQEVKEAARLAREKSQDGGEFTSTGLALASHQVPPSPLVSTNGPGEEKLFRSQSADTPGPTERERLKKML 177
Cdd:NF033915  205 EQSLVHIAEYSKESKEALQELHERIGDRLQESLNGMSEAMQTALTDALNNIMAPAIQTLVSTTSQQSTQVLESLVGNFMD 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452 178 SEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQlevQRAEAELLRQRVAELEAQVAVEPVRAGEKEAtsqsv 257
Cdd:NF033915  285 GMTSAGREQGLQMQQAAADVNAAVSGMSERLNQLFNSLSEQ---QGRQMERAQQQSSTFETQLQRLSGSANERQA----- 356


                  ....*..
gi 1907189452 258 eQLEARV 264
Cdd:NF033915  357 -QLEQRF 362
 
Name Accession Description Interval E-value
EVH1_Homer_Vesl cd01206
Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, ...
 58-116 3.56e-38

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: 132.47  E-value: 3.56e-38
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189452  58 SQAIINSTVTPNMTFTKTSQKFGQWADSRANTVYGLGFASEQQLTQFAEKFQEVKEAAR 116
Cdd:cd01206    51 SKAIINSTITPNMTFTKTSQKFGQWADSRANTVYGLGFASEAELTKFAEKFQEAKEAAK 109
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 57-112 6.10e-20

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: 84.04  E-value: 6.10e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189452  57 HSQAIINSTVTPNMTFTKTSQKFGQWADSRAntVYGLGFASEQQLTQFAEKFQEVK 112
Cdd:pfam00568  58 DGKVIWNQEIYPNMEYNQARPFFHTFADSRC--VYGLNFASEEEATKFAKAVQEAL 111
EVH1_family cd00837
EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; ...
 59-112 1.25e-18

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: 80.20  E-value: 1.25e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907189452  59 QAIINSTVTPNMTFTKTSQKFGQWADSRanTVYGLGFASEQQLTQFAEKFQEVK 112
Cdd:cd00837    52 KVVINCTITKNLVYNKATQTFHQWADDR--TVFGLNFASEEDATKFAEAVQEAL 103
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 55-110 7.35e-13

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: 64.30  E-value: 7.35e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189452   55 NVHSQAIINSTVTPNMTFTKTSQKFGQWADsrANTVYGLGFASEQQLTQFAEKFQE 110
Cdd:smart00461  51 KGQDKVIWNQELYKNFKYNQATPTFHQWAD--DKCVYGLNFASEEEAKKFRKKVLK 104
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 168-341 2.28e-07

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: 52.75  E-value: 2.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452  168 TERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEpvrA 247
Cdd:TIGR02168  323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---N 399

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452  248 GEKEATSQSVEQLEARVQTKDQEIQTLKNQSTGTREAPDTAEREETQQQVQDLETRNAELEQQLRSMECNLEEARAERER 327
Cdd:TIGR02168  400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479

                          170
                   ....*....|....
gi 1907189452  328 ARAEVGRAAQLLDV 341
Cdd:TIGR02168  480 AERELAQLQARLDS 493
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 188-360 1.01e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452 188 EAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEpvrAGEKEATSQSVEQLEARVQTK 267
Cdd:COG1196   252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL---EERRRELEERLEELEEELAEL 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452 268 DQEIQTLKNQSTGTRE--APDTAEREETQQQVQDLETRNAELEQQLRSMECNLEEARAERERARAEVGRAAQLLDVRLFE 345
Cdd:COG1196   329 EEELEELEEELEELEEelEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408

                         170
                  ....*....|....*
gi 1907189452 346 LSELREGLARLAEAA 360
Cdd:COG1196   409 EEALLERLERLEEEL 423
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 169-360 1.27e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452 169 ERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAV-EPVRA 247
Cdd:COG1196   275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEaEEELE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452 248 GEKEATSQSVEQLEARVQTKDQEIQTLKN-----QSTGTREAPDTAEREETQQQVQDLETRNAELEQQLRSMECNLEEAR 322
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEElaeelLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907189452 323 AERERARAEVGRAAQLLDVRLFELSELREGLARLAEAA 360
Cdd:COG1196   435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 205-360 1.37e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452 205 LREANAAATQWR---QQLEVQRAEAELLRQRVAELEAQVAvepVRAGEKEATSQSVEQLEARVQTKDQEIQTLKNQ--ST 279
Cdd:COG1196   224 ELEAELLLLKLReleAELEELEAELEELEAELEELEAELA---ELEAELEELRLELEELELELEEAQAEEYELLAElaRL 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452 280 GTREAPDTAEREETQQQVQDLETRNAELEQQLRSMECNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARLAEA 359
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380


                  .
gi 1907189452 360 A 360
Cdd:COG1196   381 L 381
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
168-313 1.48e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452 168 TERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAgALREANAAATQWRQQLEVQRAEAELLrQRVAELEAQVAVEPVRA 247
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELE-ELEAELEELREELEKLEKLLQLLPLY-QELEALEAELAELPERL 148

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189452 248 GEKEATSQSVEQLEARVQTKDQEIQTLKNQSTGTREAPDTAEREE---TQQQVQDLETRNAELEQQLRS 313
Cdd:COG4717   149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdLAEELEELQQRLAELEEELEE 217
EVH1_Ena_VASP-like cd01207
Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: ...
 58-105 4.15e-05

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: 42.29  E-value: 4.15e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907189452  58 SQAIINSTVTPNMTFTKTSQKFGQWADSRanTVYGLGFASEQQLTQFA 105
Cdd:cd01207    52 HEVVINCAILKGLKYNQATPTFHQWRDAR--QVYGLNFASKEEATEFA 97
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 186-360 4.57e-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: 4.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452 186 QWEAEFFALQDsnQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRAGEKEATSQSVEQLEARVQ 265
Cdd:COG1196   224 ELEAELLLLKL--RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452 266 tKDQEIQTLKNQSTGTREAPDTAEREETQQQVQDLETRNAELEQQLRSMECNLEEARAERERARAEVGRAAQLLDVRLFE 345
Cdd:COG1196   302 -QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                         170
                  ....*....|....*
gi 1907189452 346 LSELREGLARLAEAA 360
Cdd:COG1196   381 LEELAEELLEALRAA 395
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 169-360 1.02e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452 169 ERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEpvrAG 248
Cdd:COG1196   324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL---AA 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452 249 EKEATSQSVEQLEARVQTKDQEIQTLKNQSTGTREAPDTAEREETQQQ--VQDLETRNAELEQQLRSMECNLEEARAERE 326
Cdd:COG1196   401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAeeEAELEEEEEALLELLAELLEEAALLEAALA 480

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1907189452 327 RARAEVGRAAQLLDVRLfELSELREGLARLAEAA 360
Cdd:COG1196   481 ELLEELAEAAARLLLLL-EAEADYEGFLEGVKAA 513
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 199-360 2.45e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 2.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452  199 QRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVepvRAGEKEATSQSVEQLEARVQTKDQEIQTLKNQS 278
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA---LRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452  279 TGTREAPD--TAEREETQQQVQDLETRNAELEQQLRSMECNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARL 356
Cdd:TIGR02168  764 EELEERLEeaEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843


                   ....
gi 1907189452  357 AEAA 360
Cdd:TIGR02168  844 EEQI 847
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
189-315 4.70e-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: 4.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452  189 AEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAvepvragekEATSQSVEQLEARVQTKD 268
Cdd:COG4913    281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIR---------GNGGDRLEQLEREIERLE 351

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452  269 QEIQTLKNQSTGTRE--------APDTAE-----REETQQQVQDLETRNAELEQQLRSME 315
Cdd:COG4913    352 RELEERERRRARLEAllaalglpLPASAEefaalRAEAAALLEALEEELEALEEALAEAE 411
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
194-314 6.03e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 6.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452 194 LQDSNQRLAGA---LREANAAATQWRQQLEVQRAEA---------ELLRQRVAELEAQVAVEPVRAGEKeatSQSVEQLE 261
Cdd:COG3206   221 LSELESQLAEAraeLAEAEARLAALRAQLGSGPDALpellqspviQQLRAQLAELEAELAELSARYTPN---HPDVIALR 297

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907189452 262 ARVQTKDQEIQTLKNQSTGTREApdtaEREETQQQVQDLETRNAELEQQLRSM 314
Cdd:COG3206   298 AQIAALRAQLQQEAQRILASLEA----ELEALQAREASLQAQLAQLEARLAEL 346
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 96-354 6.16e-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: 6.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452   96 ASEQQLTQFAEKFQEVKEAARLAREKSQDggefTSTGLALASHQVppSPLVSTNGPGEEKLFRSQSADTPGPTERERLKK 175
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQLRKELEE----LSRQISALRKDL--ARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452  176 MLSEGSVGEVQWEAEFFALQDSnqrlagaLREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRAGEKEatsQ 255
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQ-------IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE---R 838

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452  256 SVEQLEARVQTKDQEIQTLKNQSTGTREAPD---------TAEREETQQQVQDLETRNAELEQQLRSMECNLEEARAERE 326
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEIEELEELIEeleselealLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918

                          250       260
                   ....*....|....*....|....*...
gi 1907189452  327 RARAEVGRAAQLLDVRLFELSELREGLA 354
Cdd:TIGR02168  919 ELREKLAQLELRLEGLEVRIDNLQERLS 946
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 193-359 1.01e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452 193 ALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRAGEKEATSQSVEQLEARVQTKDQEIQ 272
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452 273 TLKNQSTGTREAPDTAEREETQQQVQDLETRNAELEQQLRSMECNLEEARAERERARAEVGRAAQLLDVRLfELSELREG 352
Cdd:COG1196   393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE-LLAELLEE 471


                  ....*..
gi 1907189452 353 LARLAEA 359
Cdd:COG1196   472 AALLEAA 478
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
188-315 1.49e-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: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452  188 EAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAEL---------LRQRVAELEAQVAvepvragEKEATSQSVE 258
Cdd:COG4913    616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeidvasAEREIAELEAELE-------RLDASSDDLA 688

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189452  259 QLEARVQTKDQEIQTLKNQSTGTREapdtaEREETQQQVQDLETRNAELEQQLRSME 315
Cdd:COG4913    689 ALEEQLEELEAELEELEEELDELKG-----EIGRLEKELEQAEEELDELQDRLEAAE 740
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
205-359 1.84e-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: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452  205 LREANAAATQWRQQLEVQRAEAELLR-----QRVAELEAQVAVEpvrAGEKEATSQSVEQLEARVQTKDQEIQTLKNQ-- 277
Cdd:COG4913    257 IRELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEEL---RAELARLEAELERLEARLDALREELDELEAQir 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452  278 -STGTREAPDTAEREETQQQVQDLETRNAELEQQLRSMEcnlEEARAERERARAEVGRAAQLLDVRLFELSELREGLARL 356
Cdd:COG4913    334 gNGGDRLEQLEREIERLERELEERERRRARLEALLAALG---LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEA 410


                   ...
gi 1907189452  357 AEA 359
Cdd:COG4913    411 EAA 413
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 222-356 2.06e-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: 2.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452  222 QRAEAELLRQRVAELEAQVavepvRAGEKE--ATSQSVEQLEARVQTKDQEIQTLKNQSTGTREAPDTAEREETQ--QQV 297
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKI-----AELEKAlaELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQleERI 749

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189452  298 QDLETRNAELEQQLRSMECNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARL 356
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 206-360 2.93e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 2.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452 206 REANAA--ATQWRQQLEvqRAEAELLRQRVAELEAQVAVEpvrAGEKEATSQSVEQLEARVQTKDQEIQTLKNQSTGTRE 283
Cdd:COG1196   207 RQAEKAerYRELKEELK--ELEAELLLLKLRELEAELEEL---EAELEELEAELEELEAELAELEAELEELRLELEELEL 281

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189452 284 apdtaEREETQQQVQDLETRNAELEQQLRSMECNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARLAEAA 360
Cdd:COG1196   282 -----ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
199-360 3.10e-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: 3.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452  199 QRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEaqvavepvRAGEKEATSQSVEQLEARVQTKDQEIQTLKNQS 278
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQ--------RLAEYSWDEIDVASAEREIAELEAELERLDASS 684

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452  279 TGTREApdTAEREETQQQVQDLETRNAELEQQLRSMECNLEEARAERERARAEVGRAAQLLDVRLFELSElreglARLAE 358
Cdd:COG4913    685 DDLAAL--EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE-----ERFAA 757


                   ..
gi 1907189452  359 AA 360
Cdd:COG4913    758 AL 759
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
169-315 5.37e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 5.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452 169 ERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQlEVQRAEAELLRQRVAELEAQVAVEPVRAG 248
Cdd:COG4717   317 EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE-ELEQEIAALLAEAGVEDEEELRAALEQAE 395

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189452 249 EKEATSQSVEQLEARVQTKDQEIQTLKNQSTGT----REAPDTAEREETQQQVQDLETRNAELEQQLRSME 315
Cdd:COG4717   396 EYQELKEELEELEEQLEELLGELEELLEALDEEeleeELEELEEELEELEEELEELREELAELEAELEQLE 466
mukB PRK04863
chromosome partition protein MukB;
186-314 8.16e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 38.40  E-value: 8.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452  186 QWEAEFFALQDSnqrlagaLREANAAATQWRQQLEVQRAE-AELLRQRVAELEAQVAVEPVRA--GEKEATSQSVEQLea 262
Cdd:PRK04863   562 ELEARLESLSES-------VSEARERRMALRQQLEQLQARiQRLAARAPAWLAAQDALARLREqsGEEFEDSQDVTEY-- 632

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907189452  263 rvqtkdqeIQTLknqstgtreapdtAERE-ETQQQVQDLETRNAELEQQLRSM 314
Cdd:PRK04863   633 --------MQQL-------------LERErELTVERDELAARKQALDEEIERL 664
antiphage_ZorA_2 NF033915
anti-phage ZorAB system protein ZorA; Proteins of this subfamily are putative H+ channel ...
 98-264 8.78e-03

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


Pssm-ID: 411476 [Multi-domain]  Cd Length: 383  Bit Score: 37.82  E-value: 8.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452  98 EQQLTQFAEKFQEVKEAARLAREKSQDGGEFTSTGLALASHQVPPSPLVSTNGPGEEKLFRSQSADTPGPTERERLKKML 177
Cdd:NF033915  205 EQSLVHIAEYSKESKEALQELHERIGDRLQESLNGMSEAMQTALTDALNNIMAPAIQTLVSTTSQQSTQVLESLVGNFMD 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452 178 SEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQlevQRAEAELLRQRVAELEAQVAVEPVRAGEKEAtsqsv 257
Cdd:NF033915  285 GMTSAGREQGLQMQQAAADVNAAVSGMSERLNQLFNSLSEQ---QGRQMERAQQQSSTFETQLQRLSGSANERQA----- 356


                  ....*..
gi 1907189452 258 eQLEARV 264
Cdd:NF033915  357 -QLEQRF 362
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
170-315 9.58e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.10  E-value: 9.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189452 170 RERLKKMLSEGSVGEvqweAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRAGE 249
Cdd:PRK02224  292 EEERDDLLAEAGLDD----ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAE 367

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189452 250 KEATSQS----VEQLEARVQTKDQEIQTLKNQSTGTREAPDTAE--REETQQQVQDLETRNAELEQQLRSME 315
Cdd:PRK02224  368 LESELEEareaVEDRREEIEELEEEIEELRERFGDAPVDLGNAEdfLEELREERDELREREAELEATLRTAR 439
 
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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