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Conserved domains on  [gi|1907189471|ref|XP_036009955|]
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homer protein homolog 3 isoform X6 [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 9.69e-39

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: 133.24  E-value: 9.69e-39
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189471  58 SQAIINSTVTPNMTFTKTSQKFGQWADSRANTVYGLGFASEQQLTQFAEKFQEVKEAAR 116
Cdd:cd01206    51 SKAIINSTITPNMTFTKTSQKFGQWADSRANTVYGLGFASEAELTKFAEKFQEAKEAAK 109
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 188-331 2.24e-05

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471 188 EAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRAGEKEATSQSVEQLEARVQTK 267
Cdd:COG1196   252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189471 268 DQDLETRNAELEQQLRSMECNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARLAEAA 331
Cdd:COG1196   332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
 
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 9.69e-39

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: 133.24  E-value: 9.69e-39
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189471  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 3.44e-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: 84.42  E-value: 3.44e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189471  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 6.20e-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: 6.20e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189471   55 NVHSQAIINSTVTPNMTFTKTSQKFGQWADsrANTVYGLGFASEQQLTQFAEKFQE 110
Cdd:smart00461  51 KGQDKVIWNQELYKNFKYNQATPTFHQWAD--DKCVYGLNFASEEEAKKFRKKVLK 104
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 188-331 2.24e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471 188 EAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRAGEKEATSQSVEQLEARVQTK 267
Cdd:COG1196   252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189471 268 DQDLETRNAELEQQLRSMECNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARLAEAA 331
Cdd:COG1196   332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 199-331 3.86e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 3.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471  199 QRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRAGEKEATSQSVEQLEARVQTKDQDLETRNAEL 278
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907189471  279 EQQLRSMECNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARLAEAA 331
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
antiphage_ZorA_2 NF033915
anti-phage ZorAB system protein ZorA; Proteins of this subfamily are putative H+ channel ...
 98-289 4.98e-04

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: 41.67  E-value: 4.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471  98 EQQLTQFAEKFQEVKEAARLAREKSQDGGEFTSTGLALASHQVPPSPLVSTNGPGEEKLFRSQSADTPGPTERERLKKML 177
Cdd:NF033915  205 EQSLVHIAEYSKESKEALQELHERIGDRLQESLNGMSEAMQTALTDALNNIMAPAIQTLVSTTSQQSTQVLESLVGNFMD 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471 178 SEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQlevQRAEAELLRQRVAELEAQVavepvragekeatSQSV 257
Cdd:NF033915  285 GMTSAGREQGLQMQQAAADVNAAVSGMSERLNQLFNSLSEQ---QGRQMERAQQQSSTFETQL-------------QRLS 348

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1907189471 258 EQLEARVQTKDQDLETRNAELEQQLRSMECNL 289
Cdd:NF033915  349 GSANERQAQLEQRFEELMSGLTEQLQTQLGAA 380
mukB PRK04863
chromosome partition protein MukB;
186-286 1.33e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.71  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471  186 QWEAEFFALQDSnqrlagaLREANAAATQWRQQLEVQRAE-AELLRQRVAELEAQVAVEPVRA--GEKEATSQSVEQLEA 262
Cdd:PRK04863   562 ELEARLESLSES-------VSEARERRMALRQQLEQLQARiQRLAARAPAWLAAQDALARLREqsGEEFEDSQDVTEYMQ 634

                           90       100
                   ....*....|....*....|....
gi 1907189471  263 RVQTKDQDLETRNAELEQQLRSME 286
Cdd:PRK04863   635 QLLERERELTVERDELAARKQALD 658
 
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 9.69e-39

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: 133.24  E-value: 9.69e-39
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189471  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 3.44e-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: 84.42  E-value: 3.44e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189471  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 9.23e-19

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: 9.23e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907189471  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 6.20e-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: 6.20e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189471   55 NVHSQAIINSTVTPNMTFTKTSQKFGQWADsrANTVYGLGFASEQQLTQFAEKFQE 110
Cdd:smart00461  51 KGQDKVIWNQELYKNFKYNQATPTFHQWAD--DKCVYGLNFASEEEAKKFRKKVLK 104
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 188-331 2.24e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471 188 EAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRAGEKEATSQSVEQLEARVQTK 267
Cdd:COG1196   252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189471 268 DQDLETRNAELEQQLRSMECNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARLAEAA 331
Cdd:COG1196   332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
EVH1_Ena_VASP-like cd01207
Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: ...
 58-105 3.28e-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: 3.28e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907189471  58 SQAIINSTVTPNMTFTKTSQKFGQWADSRanTVYGLGFASEQQLTQFA 105
Cdd:cd01207    52 HEVVINCAILKGLKYNQATPTFHQWRDAR--QVYGLNFASKEEATEFA 97
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 194-331 7.07e-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: 7.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471 194 LQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRAGEKEATSQSVEQLEARVQTKDQDLET 273
Cdd:COG1196   321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189471 274 RNAELEQQLRSMECNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARLAEAA 331
Cdd:COG1196   401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 169-331 3.08e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 3.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471 169 ERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRAG 248
Cdd:COG1196   324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471 249 EKEATSQSVEQLEARVQTKDQDLETRNAELEQQLRSMECNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARLA 328
Cdd:COG1196   404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483


                  ...
gi 1907189471 329 EAA 331
Cdd:COG1196   484 EEL 486
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 186-331 3.22e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 3.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471 186 QWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVepvRAGEKEATSQSVEQLEARVQ 265
Cdd:COG1196   299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE---AEAELAEAEEALLEAEAELA 375

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189471 266 TKDQDLETRNAELEQQLRSMECNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARLAEAA 331
Cdd:COG1196   376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 169-331 3.48e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 3.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471 169 ERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAV-EPVRA 247
Cdd:COG1196   275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEaEEELE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471 248 GEKEATSQSVEQLEARVQTKDQDLETRNAELEQQLRSMEcNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARL 327
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR-AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433


                  ....
gi 1907189471 328 AEAA 331
Cdd:COG1196   434 EEEE 437
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 199-331 3.86e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 3.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471  199 QRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRAGEKEATSQSVEQLEARVQTKDQDLETRNAEL 278
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907189471  279 EQQLRSMECNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARLAEAA 331
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 193-331 3.97e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 3.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471 193 ALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRAGEKEATSQSVEQLEARVQTKDQDLE 272
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189471 273 TRNAELEQQLRSMECNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARLAEAA 331
Cdd:COG1196   393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
antiphage_ZorA_2 NF033915
anti-phage ZorAB system protein ZorA; Proteins of this subfamily are putative H+ channel ...
 98-289 4.98e-04

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: 41.67  E-value: 4.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471  98 EQQLTQFAEKFQEVKEAARLAREKSQDGGEFTSTGLALASHQVPPSPLVSTNGPGEEKLFRSQSADTPGPTERERLKKML 177
Cdd:NF033915  205 EQSLVHIAEYSKESKEALQELHERIGDRLQESLNGMSEAMQTALTDALNNIMAPAIQTLVSTTSQQSTQVLESLVGNFMD 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471 178 SEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQlevQRAEAELLRQRVAELEAQVavepvragekeatSQSV 257
Cdd:NF033915  285 GMTSAGREQGLQMQQAAADVNAAVSGMSERLNQLFNSLSEQ---QGRQMERAQQQSSTFETQL-------------QRLS 348

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1907189471 258 EQLEARVQTKDQDLETRNAELEQQLRSMECNL 289
Cdd:NF033915  349 GSANERQAQLEQRFEELMSGLTEQLQTQLGAA 380
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 168-312 5.42e-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: 5.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471  168 TERERLKKMLSEGsvgevqwEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVA--VEPV 245
Cdd:TIGR02168  351 EELESLEAELEEL-------EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErlQQEI 423

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471  246 RAGEKEATSQSVEQLEARVQTKDQ---DLETRNAELEQQLRSMECNLEEARAERERARAEVGRAAQLLDV 312
Cdd:TIGR02168  424 EELLKKLEEAELKELQAELEELEEeleELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
189-330 9.90e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 9.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471  189 AEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAvepvragekEATSQSVEQLEARVQTKD 268
Cdd:COG4913    281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIR---------GNGGDRLEQLEREIERLE 351

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189471  269 QDLETRN---AELEQQLRSMEcnlEEARAERERARAEVGRAAQLLDVRLFELSELREGLARLAEA 330
Cdd:COG4913    352 RELEERErrrARLEALLAALG---LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAA 413
mukB PRK04863
chromosome partition protein MukB;
186-286 1.33e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.71  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471  186 QWEAEFFALQDSnqrlagaLREANAAATQWRQQLEVQRAE-AELLRQRVAELEAQVAVEPVRA--GEKEATSQSVEQLEA 262
Cdd:PRK04863   562 ELEARLESLSES-------VSEARERRMALRQQLEQLQARiQRLAARAPAWLAAQDALARLREqsGEEFEDSQDVTEYMQ 634

                           90       100
                   ....*....|....*....|....
gi 1907189471  263 RVQTKDQDLETRNAELEQQLRSME 286
Cdd:PRK04863   635 QLLERERELTVERDELAARKQALD 658
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 205-332 1.40e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471 205 LREANAAATQWR---QQLEVQRAEAELLRQRVAELEAQVAvepVRAGEKEATSQSVEQLEARVQTKDQDLETRNAELEQQ 281
Cdd:COG1196   224 ELEAELLLLKLReleAELEELEAELEELEAELEELEAELA---ELEAELEELRLELEELELELEEAQAEEYELLAELARL 300

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907189471 282 LRSMECNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARLAEAAP 332
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 153-330 1.45e-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: 40.43  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471  153 EEKLFRSQSADTPGPTERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQR 232
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471  233 VAELEAQVAVEPVRAGEKEATSQSVEQLEARVQTKDQDLETRNAELEQQLRSMECNLEEARAERERARAEVGRAAQLLDV 312
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842

                          170
                   ....*....|....*...
gi 1907189471  313 RLFELSELREGLARLAEA 330
Cdd:TIGR02168  843 LEEQIEELSEDIESLAAE 860
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 170-331 1.51e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471 170 RERLKKMLSEGSVGEVQW-EAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRAG 248
Cdd:COG1196   219 KEELKELEAELLLLKLRElEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471 249 EKEATSQSVEQLEARVQTKDQDLETRNAELEQQLRSMECNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARLA 328
Cdd:COG1196   299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378


                  ...
gi 1907189471 329 EAA 331
Cdd:COG1196   379 EEL 381
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
168-330 1.94e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471 168 TERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAgALREANAAATQWRQQLEVQRAEAELLrQRVAELEAQVAVEPVRA 247
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELE-ELEAELEELREELEKLEKLLQLLPLY-QELEALEAELAELPERL 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471 248 GEKEATSQSVEQLEARVQTKDQDLETRNAELEQQLRSMEcnlEEARAERERARAEVGRAAQLLDVRLFELSELREGLARL 327
Cdd:COG4717   149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLS---LATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225


                  ...
gi 1907189471 328 AEA 330
Cdd:COG4717   226 EEE 228
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 194-284 2.52e-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: 2.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471  194 LQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRAGEKEATSQsveQLEARVQTKDQDLET 273
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE---ELESRLEELEEQLET 383

                           90
                   ....*....|....
gi 1907189471  274 RN---AELEQQLRS 284
Cdd:TIGR02168  384 LRskvAQLELQIAS 397
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 154-283 2.52e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.94  E-value: 2.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471  154 EKLFRSQSadtpgptERERLKKMLSEGSVGEVQWEAEFFALQDSNQ----RLAGALREANAAATQWRQQLEVQRAEAELL 229
Cdd:COG3096    525 EQRLRQQQ-------NAERLLEEFCQRIGQQLDAAEELEELLAELEaqleELEEQAAEAVEQRSELRQQLEQLRARIKEL 597

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189471  230 RQRV-AELEAQVAVEPVRA--GEKEATSQSV--------EQLEARVQTKDQdLETRNAELEQQLR 283
Cdd:COG3096    598 AARApAWLAAQDALERLREqsGEALADSQEVtaamqqllEREREATVERDE-LAARKQALESQIE 661
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
196-332 7.10e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 7.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471  196 DSNQRLAGALREANAAATQWRQQLEVQRAEAEL--LRQRVAELEAQVAvepVRAGEKEATSQSVEQLEARVQTKDQDlet 273
Cdd:COG4913    265 AAARERLAELEYLRAALRLWFAQRRLELLEAELeeLRAELARLEAELE---RLEARLDALREELDELEAQIRGNGGD--- 338

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189471  274 RNAELEQQLRSMEcnleearAERERARAEVGRAAQLLDVRLFELSELREGLARLAEAAP 332
Cdd:COG4913    339 RLEQLEREIERLE-------RELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 169-330 7.27e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 7.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471 169 ERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRAG 248
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471 249 EKEATSQSVEQLEARVQTKDQDLETRNAELEQQLRSMECNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARLA 328
Cdd:COG1196   397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476


                  ..
gi 1907189471 329 EA 330
Cdd:COG1196   477 AA 478
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 169-331 7.61e-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: 38.11  E-value: 7.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471  169 ERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRAG 248
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471  249 EKEATSQSVEQLEARVQTKDQDLETRNAELEQQLRSMECNLEEARAERERARAEVgraaQLLDVRLFELSELREGLARLA 328
Cdd:TIGR02168  758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL----TLLNEEAANLRERLESLERRI 833


                   ...
gi 1907189471  329 EAA 331
Cdd:TIGR02168  834 AAT 836
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 96-282 9.88e-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: 37.73  E-value: 9.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471   96 ASEQQLTQFAEKFQEVKEAARLAREKSQDggefTSTGLALASHQVppSPLVSTNGPGEEKLFRSQSADTPGPTERERLKK 175
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQLRKELEE----LSRQISALRKDL--ARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471  176 MLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRAGEKEATSQ 255
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848

                          170       180
                   ....*....|....*....|....*..
gi 1907189471  256 SVEQLEARVQTKDQDLETRNAELEQQL 282
Cdd:TIGR02168  849 ELSEDIESLAAEIEELEELIEELESEL 875
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 192-285 9.93e-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: 37.44  E-value: 9.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189471 192 FALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAV--EPVRAGEKE--ATSQSVEQLEARVQTK 267
Cdd:COG4942    16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAlaRRIRALEQElaALEAELAELEKEIAEL 95

                          90
                  ....*....|....*...
gi 1907189471 268 DQDLETRNAELEQQLRSM 285
Cdd:COG4942    96 RAELEAQKEELAELLRAL 113
 
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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