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Conserved domains on  [gi|568947920|ref|XP_006540972|]
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homer protein homolog 2 isoform X1 [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

CATH:  2.30.29.30
Gene Ontology:  GO:0005515
PubMed:  22728242|17233582|15493994

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 ...
 1-47 1.91e-27

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: 102.43  E-value: 1.91e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 568947920   1 MTFTKTSQKFGQWADSRANTVFGLGFSSELQLTKFAEKFQEVREAAR 47
Cdd:cd01206   63 MTFTKTSQKFGQWADSRANTVYGLGFASEAELTKFAEKFQEAKEAAK 109
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-278 1.78e-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: 52.37  E-value: 1.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   103 DKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQC----SEINRE 178
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIaslnNEIERL 405

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   179 KEKNTQLKRRIEELESEVRD--KEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQR 256
Cdd:TIGR02168  406 EARLERLEDRRERLQQEIEEllKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485

                          170       180
                   ....*....|....*....|..
gi 568947920   257 HLKGELKSfLEVLDGKIDDLHD 278
Cdd:TIGR02168  486 QLQARLDS-LERLQENLEGFSE 506
 
Name Accession Description Interval E-value
EVH1_Homer_Vesl cd01206
Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, ...
 1-47 1.91e-27

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: 102.43  E-value: 1.91e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 568947920   1 MTFTKTSQKFGQWADSRANTVFGLGFSSELQLTKFAEKFQEVREAAR 47
Cdd:cd01206   63 MTFTKTSQKFGQWADSRANTVYGLGFASEAELTKFAEKFQEAKEAAK 109
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 1-42 7.46e-11

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: 58.23  E-value: 7.46e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568947920    1 MTFTKTSQKFGQWADSRAntVFGLGFSSELQLTKFAEKFQEV 42
Cdd:pfam00568  71 MEYNQARPFFHTFADSRC--VYGLNFASEEEATKFAKAVQEA 110
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-278 1.78e-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: 52.37  E-value: 1.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   103 DKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQC----SEINRE 178
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIaslnNEIERL 405

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   179 KEKNTQLKRRIEELESEVRD--KEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQR 256
Cdd:TIGR02168  406 EARLERLEDRRERLQQEIEEllKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485

                          170       180
                   ....*....|....*....|..
gi 568947920   257 HLKGELKSfLEVLDGKIDDLHD 278
Cdd:TIGR02168  486 QLQARLDS-LERLQENLEGFSE 506
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 1-41 2.73e-06

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: 45.04  E-value: 2.73e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568947920     1 MTFTKTSQKFGQWADsrANTVFGLGFSSELQLTKFAEKFQE 41
Cdd:smart00461  66 FKYNQATPTFHQWAD--DKCVYGLNFASEEEAKKFRKKVLK 104
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
86-211 4.87e-06

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 47.55  E-value: 4.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920  86 EKASHASPADTHLKSENDKLK--IALTQSAANVKKWEMELQTLRESNARLTTALQEsaasveqwkrqfsiCRDENDRLRS 163
Cdd:COG2433  383 EELIEKELPEEEPEAEREKEHeeRELTEEEEEIRRLEEQVERLEAEVEELEAELEE--------------KDERIERLER 448

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568947920 164 KIEELEEQCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQSE 211
Cdd:COG2433  449 ELSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLE 496
PTZ00121 PTZ00121
MAEBL; Provisional
 27-272 1.64e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   27 SSELQLTKFAEKFQEVREAARLARDKSQEKTETSSNHSQESGCETPSSTQASSVNGTDDEKASHASPADTHLKSENDKLK 106
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920  107 IALTQSAANVKKWEMElqtlRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINREKEKNTQLK 186
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEE----KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA 1691

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920  187 RRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSFL 266
Cdd:PTZ00121 1692 EALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771


                  ....*.
gi 568947920  267 EVLDGK 272
Cdd:PTZ00121 1772 EIRKEK 1777
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 91-276 1.33e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.10  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920    91 ASPADTHLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAAS----VEQWKRQFSICRDE--------- 157
Cdd:pfam15921  287 ASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMyedkIEELEKQLVLANSEltearterd 366

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   158 ---------NDRLRSKIEELEEQCSEINREKEKNTQLKRR-------IEELESEVRDKEMELKDLRKqseIIPQLMSECE 221
Cdd:pfam15921  367 qfsqesgnlDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEA---LLKAMKSECQ 443

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568947920   222 YVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGEL---KSFLEVLDGKIDDL 276
Cdd:pfam15921  444 GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakKMTLESSERTVSDL 501
 
Name Accession Description Interval E-value
EVH1_Homer_Vesl cd01206
Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, ...
 1-47 1.91e-27

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: 102.43  E-value: 1.91e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 568947920   1 MTFTKTSQKFGQWADSRANTVFGLGFSSELQLTKFAEKFQEVREAAR 47
Cdd:cd01206   63 MTFTKTSQKFGQWADSRANTVYGLGFASEAELTKFAEKFQEAKEAAK 109
EVH1_family cd00837
EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; ...
 1-43 7.56e-14

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: 66.33  E-value: 7.56e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 568947920   1 MTFTKTSQKFGQWADSRanTVFGLGFSSELQLTKFAEKFQEVR 43
Cdd:cd00837   63 LVYNKATQTFHQWADDR--TVFGLNFASEEDATKFAEAVQEAL 103
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 1-42 7.46e-11

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: 58.23  E-value: 7.46e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568947920    1 MTFTKTSQKFGQWADSRAntVFGLGFSSELQLTKFAEKFQEV 42
Cdd:pfam00568  71 MEYNQARPFFHTFADSRC--VYGLNFASEEEATKFAKAVQEA 110
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-278 1.78e-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: 52.37  E-value: 1.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   103 DKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQC----SEINRE 178
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIaslnNEIERL 405

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   179 KEKNTQLKRRIEELESEVRD--KEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQR 256
Cdd:TIGR02168  406 EARLERLEDRRERLQQEIEEllKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485

                          170       180
                   ....*....|....*....|..
gi 568947920   257 HLKGELKSfLEVLDGKIDDLHD 278
Cdd:TIGR02168  486 QLQARLDS-LERLQENLEGFSE 506
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 96-285 5.36e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.84  E-value: 5.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920    96 THLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQcseI 175
Cdd:TIGR02169  698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED---L 774

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   176 NREKEKNTQLKRR-----IEELESEVRDKEMELKDLRKQSEIIPQ----LMSECEYVSEKLEAAERDNQNLEDKVRSLKT 246
Cdd:TIGR02169  775 HKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQklnrLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 568947920   247 DIEESKYRqrhlKGELKSFLEVLDGKIDDLHDFRRGLSK 285
Cdd:TIGR02169  855 EIENLNGK----KEELEEELEELEAALRDLESRLGDLKK 889
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 98-269 8.10e-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: 50.44  E-value: 8.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920    98 LKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFsicrdenDRLRSKIEELEEQCSEINR 177
Cdd:TIGR02168  787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL-------EDLEEQIEELSEDIESLAA 859

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   178 EKEkntQLKRRIEELESEVrdkEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 257
Cdd:TIGR02168  860 EIE---ELEELIEELESEL---EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933

                          170
                   ....*....|..
gi 568947920   258 LKGELKSFLEVL 269
Cdd:TIGR02168  934 LEVRIDNLQERL 945
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 98-289 2.11e-06

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: 48.90  E-value: 2.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920    98 LKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQcseINR 177
Cdd:TIGR02168  717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQ 793

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   178 EKEKNTQLKRRIEELESEVRDKEmelKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 257
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLN---EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870

                          170       180       190
                   ....*....|....*....|....*....|..
gi 568947920   258 LKGELKSFLEVLDGKIDDLHDFRRGLSKLGTD 289
Cdd:TIGR02168  871 LESELEALLNERASLEEALALLRSELEELSEE 902
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 1-41 2.73e-06

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: 45.04  E-value: 2.73e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568947920     1 MTFTKTSQKFGQWADsrANTVFGLGFSSELQLTKFAEKFQE 41
Cdd:smart00461  66 FKYNQATPTFHQWAD--DKCVYGLNFASEEEAKKFRKKVLK 104
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
86-211 4.87e-06

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 47.55  E-value: 4.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920  86 EKASHASPADTHLKSENDKLK--IALTQSAANVKKWEMELQTLRESNARLTTALQEsaasveqwkrqfsiCRDENDRLRS 163
Cdd:COG2433  383 EELIEKELPEEEPEAEREKEHeeRELTEEEEEIRRLEEQVERLEAEVEELEAELEE--------------KDERIERLER 448

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568947920 164 KIEELEEQCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQSE 211
Cdd:COG2433  449 ELSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLE 496
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 98-256 9.43e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 9.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920    98 LKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINR 177
Cdd:TIGR02169  334 LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE 413

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   178 EKEKNTQ-----------LKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSEceyVSEKLEAAERDNQNLEDKVRSLKT 246
Cdd:TIGR02169  414 ELQRLSEeladlnaaiagIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK---YEQELYDLKEEYDRVEKELSKLQR 490

                          170
                   ....*....|
gi 568947920   247 DIEESKYRQR 256
Cdd:TIGR02169  491 ELAEAEAQAR 500
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 99-276 1.27e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 1.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920    99 KSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINRE 178
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   179 ----KEKNTQLKRRIEELESEVRDKEMELKDLRKQseiIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYR 254
Cdd:TIGR02168  756 ltelEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832

                          170       180
                   ....*....|....*....|..
gi 568947920   255 qrhlKGELKSFLEVLDGKIDDL 276
Cdd:TIGR02168  833 ----IAATERRLEDLEEQIEEL 850
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
155-246 1.47e-05

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 46.00  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920 155 RDENDRLRSKIEELEEQCSEInreKEKNTQLKRRIEELESEVRDKEMELK-DLRKQSEIIpQLMSECEYVSEKLEAAERD 233
Cdd:COG2433  412 EEEIRRLEEQVERLEAEVEEL---EAELEEKDERIERLERELSEARSEERrEIRKDREIS-RLDREIERLERELEEERER 487

                         90
                 ....*....|...
gi 568947920 234 NQNLEDKVRSLKT 246
Cdd:COG2433  488 IEELKRKLERLKE 500
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 122-287 1.76e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 1.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   122 ELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCS-----EINREKEKNTQLKRRIEELESEV 196
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlgeeEQLRVKEKIGELEAEIASLERSI 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   197 RDKEMELKDLRKQSEI----IPQLMSECEYVSEKLE--AAERDN-----QNLEDKVRSLKTDIEESKYRQRHLKGELKSF 265
Cdd:TIGR02169  311 AEKERELEDAEERLAKleaeIDKLLAEIEELEREIEeeRKRRDKlteeyAELKEELEDLRAELEEVDKEFAETRDELKDY 390

                          170       180
                   ....*....|....*....|..
gi 568947920   266 LEVLDGKIDDLHDFRRGLSKLG 287
Cdd:TIGR02169  391 REKLEKLKREINELKRELDRLQ 412
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
97-290 1.88e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 1.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   97 HLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQES---------AASVEQWKRQFSICRDENDRLRSKIEE 167
Cdd:COG4913   614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvasaEREIAELEAELERLDASSDDLAALEEQ 693

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920  168 LEEQCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLmsECEYVSEKLEA--AERDNQNLEDKVR-SL 244
Cdd:COG4913   694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL--ARLELRALLEErfAAALGDAVERELReNL 771

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568947920  245 KTDIEESKYRQRHLKGEL----KSFLEV-------LDGKIDDLHDFRRGLSKLGTDN 290
Cdd:COG4913   772 EERIDALRARLNRAEEELeramRAFNREwpaetadLDADLESLPEYLALLDRLEEDG 828
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 98-267 5.25e-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: 5.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920  98 LKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQE-------SAASVEQWKRQFSICRDENDRLRSKIEELEE 170
Cdd:COG1196  244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEaqaeeyeLLAELARLEQDIARLEERRRELEERLEELEE 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920 171 QCSEINREKEKNTQ----LKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEyvsEKLEAAERDNQNLEDKVRSLKT 246
Cdd:COG1196  324 ELAELEEELEELEEeleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE---EELEELAEELLEALRAAAELAA 400

                        170       180
                 ....*....|....*....|.
gi 568947920 247 DIEESKYRQRHLKGELKSFLE 267
Cdd:COG1196  401 QLEELEEAEEALLERLERLEE 421
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 116-268 1.59e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   116 VKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINREKE----KNTQLKRRIEE 191
Cdd:TIGR02169  793 IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEnlngKKEELEEELEE 872

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568947920   192 LESEVRDKEMELKDLRKQseiIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEV 268
Cdd:TIGR02169  873 LEAALRDLESRLGDLKKE---RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
PTZ00121 PTZ00121
MAEBL; Provisional
 27-272 1.64e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   27 SSELQLTKFAEKFQEVREAARLARDKSQEKTETSSNHSQESGCETPSSTQASSVNGTDDEKASHASPADTHLKSENDKLK 106
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920  107 IALTQSAANVKKWEMElqtlRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINREKEKNTQLK 186
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEE----KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA 1691

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920  187 RRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSFL 266
Cdd:PTZ00121 1692 EALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771


                  ....*.
gi 568947920  267 EVLDGK 272
Cdd:PTZ00121 1772 EIRKEK 1777
PRK12704 PRK12704
phosphodiesterase; Provisional
 160-269 2.07e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920 160 RLRSKIEELEEQCSEINREK--EKNTQLKRRIEELESEVRDKEMELKDLRKQseiipqLMSECEYVSEKLEAAERDNQNL 237
Cdd:PRK12704  39 EAKRILEEAKKEAEAIKKEAllEAKEEIHKLRNEFEKELRERRNELQKLEKR------LLQKEENLDRKLELLEKREEEL 112

                         90       100       110
                 ....*....|....*....|....*....|..
gi 568947920 238 EDKVRSLKTDIEESKYRQRHLKGELKSFLEVL 269
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEELEELIEEQLQEL 144
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 155-285 3.02e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 3.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   155 RDENDRLRSKIEELEEQCS----EINREKEKNTQLKRRIEELESEVRDKEMEL----KDLRKQSEIIPQLMSECEYVSEK 226
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSslqsELRRIENRLDELSQELSDASRKIGEIEKEIeqleQEEEKLKERLEELEEDLSSLEQE 752

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   227 LEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGEL-KSFLEVLDGKIDDLHDFRRGLSK 285
Cdd:TIGR02169  753 IENVKSELKELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEA 812
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 159-276 3.39e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.06  E-value: 3.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920 159 DRLRSKIEELEEQCSEINREKEKN----TQLKRRIEELESEVRDKEMELKDLRKQ----SEIIPQLMSECEY--VSEKLE 228
Cdd:COG1579   20 DRLEHRLKELPAELAELEDELAALearlEAAKTELEDLEKEIKRLELEIEEVEARikkyEEQLGNVRNNKEYeaLQKEIE 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568947920 229 AAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEVLDGKIDDL 276
Cdd:COG1579  100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
137-286 5.49e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 5.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920 137 LQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQL 216
Cdd:PRK03918 195 IKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE 274

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920 217 MSECEYVSEKLEAAERDNQNLEdKVRSLKTDIEESKYRQRHLKGELKSFLEVLDGKIDDLHDFRRGLSKL 286
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYI-KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 155-286 6.03e-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: 41.20  E-value: 6.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   155 RDENDRLRSKIEELEEQCSEINRE-KEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERD 233
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKAlAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568947920   234 NQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEVLDGKIDDLHDFRRGLSKL 286
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
37-250 7.53e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 7.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920  37 EKFQEVREAARLARDKSQEKTETSSNHSQE-SGCETPSSTQASSVNGTDDEKASHASPADTH------LKSENDKLKIAL 109
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEERREElETLEAEIEDLRETIAETEREREELAEEVRDLrerleeLEEERDDLLAEA 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920 110 TQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINREKEKNtqlKRRI 189
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEA---REAV 379

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568947920 190 EELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLeAAERDnqNLEDKVRSLKTDIEE 250
Cdd:PRK02224 380 EDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEEL-REERD--ELREREAELEATLRT 437
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 98-250 7.68e-04

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: 7.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920  98 LKSENDKLKIALTqsAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIE----------- 166
Cdd:COG1196  218 LKEELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeaqaeeyella 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920 167 ELEEQCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQ-SEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLK 245
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEElEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375


                 ....*
gi 568947920 246 TDIEE 250
Cdd:COG1196  376 EAEEE 380
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
96-250 7.82e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 7.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920  96 THLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTtALQESAASVEQWKRQFSI----CRDENDRLRSKIEELEEQ 171
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIE-ELEKELESLEGSKRKLEEkireLEERIEELKKEIEELEEK 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920 172 CSEINREKEKNTQ---LKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDI 248
Cdd:PRK03918 282 VKELKELKEKAEEyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH 361


                 ..
gi 568947920 249 EE 250
Cdd:PRK03918 362 EL 363
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 122-276 1.21e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.52  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920 122 ELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINREKEKNTQLKRRIEELESEVRDKEm 201
Cdd:COG1579   11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK- 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568947920 202 ELKDLRKQSEIIPQLMSECEY----VSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEVLDGKIDDL 276
Cdd:COG1579   90 EYEALQKEIESLKRRISDLEDeileLMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 159-250 1.23e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.06  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920 159 DRLRSKIEELEEQCSEInrEKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLE 238
Cdd:COG0542  414 DELERRLEQLEIEKEAL--KKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELE 491

                         90
                 ....*....|..
gi 568947920 239 DKVRSLKTDIEE 250
Cdd:COG0542  492 KELAELEEELAE 503
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
122-283 1.26e-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: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920  122 ELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLRS-----KIEELEEQCSEINREKEKNTQLKRRIEELESEV 196
Cdd:COG4913   243 ALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRAELARLEAELERLEARLDAL 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920  197 RDKEMELKDLRKQS--EIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEVLDGKID 274
Cdd:COG4913   322 REELDELEAQIRGNggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401


                  ....*....
gi 568947920  275 DLHDFRRGL 283
Cdd:COG4913   402 ALEEALAEA 410
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 91-276 1.33e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.10  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920    91 ASPADTHLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAAS----VEQWKRQFSICRDE--------- 157
Cdd:pfam15921  287 ASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMyedkIEELEKQLVLANSEltearterd 366

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   158 ---------NDRLRSKIEELEEQCSEINREKEKNTQLKRR-------IEELESEVRDKEMELKDLRKqseIIPQLMSECE 221
Cdd:pfam15921  367 qfsqesgnlDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEA---LLKAMKSECQ 443

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568947920   222 YVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGEL---KSFLEVLDGKIDDL 276
Cdd:pfam15921  444 GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakKMTLESSERTVSDL 501
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
98-285 1.60e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920  98 LKSENDKLKIALTQsAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINR 177
Cdd:PRK02224 487 LEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920 178 EKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEA-AERDNQNLE------DKVRSLKTDIEE 250
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREAlAELNDERRErlaekrERKRELEAEFDE 645

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568947920 251 SKYRQ-RHLKGELKSFLEVLDGKIDDLHDFRRGLSK 285
Cdd:PRK02224 646 ARIEEaREDKERAEEYLEQVEEKLDELREERDDLQA 681
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
94-264 1.69e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   94 ADTHLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFsicrdenDRLRSKIEELEEQCS 173
Cdd:COG4913   261 AERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL-------DALREELDELEAQIR 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920  174 EINREKEKntQLKRRIEELESEVRDKEMELKDLRKQSEII--PQLMSECEYVSEKLEAAERDNQ------NLEDKVRSLK 245
Cdd:COG4913   334 GNGGDRLE--QLEREIERLERELEERERRRARLEALLAALglPLPASAEEFAALRAEAAALLEAleeeleALEEALAEAE 411

                         170
                  ....*....|....*....
gi 568947920  246 TDIEESKYRQRHLKGELKS 264
Cdd:COG4913   412 AALRDLRRELRELEAEIAS 430
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 133-286 2.13e-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: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   133 LTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINRE----KEKNTQLKRRIEELESEVRDKEMELKDLRK 208
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEvselEEEIEELQKELYALANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568947920   209 QSEiipQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEEskyrqrhLKGELKSFLEVLDGKIDDLHDFRRGLSKL 286
Cdd:TIGR02168  310 RLA---NLERQLEELEAQLEELESKLDELAEELAELEEKLEE-------LKEELESLEAELEELEAELEELESRLEEL 377
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 98-250 2.66e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 39.03  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   98 LKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSIcrdendrLRSKIEELEEQCseinR 177
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINV-------LQKKIENLQEQL----R 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920  178 EKEKN-TQLKRRIEELESE--------------VRDKEMELKDLRKQSEiipqlmSECEYVSEKLEAAERDNQNLEDKVR 242
Cdd:pfam10174 412 DKDKQlAGLKERVKSLQTDssntdtalttleeaLSEKERIIERLKEQRE------REDRERLEELESLKKENKDLKEKVS 485


                  ....*...
gi 568947920  243 SLKTDIEE 250
Cdd:pfam10174 486 ALQPELTE 493
PLN02939 PLN02939
transferase, transferring glycosyl groups
 100-252 3.10e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 39.11  E-value: 3.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920 100 SENDKLKIALTQSAANVKKWEMELQTLRESnarLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINREK 179
Cdd:PLN02939 180 SETDARIKLAAQEKIHVEILEEQLEKLRNE---LLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETE 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920 180 EKNTQLKRRIEELESEVRDKEMEL----KDLRKQSEI-IPQLMSECEYVSEKLEAAER----------DNQNLEDKVRSL 244
Cdd:PLN02939 257 ERVFKLEKERSLLDASLRELESKFivaqEDVSKLSPLqYDCWWEKVENLQDLLDRATNqvekaalvldQNQDLRDKVDKL 336


                 ....*...
gi 568947920 245 KTDIEESK 252
Cdd:PLN02939 337 EASLKEAN 344
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
116-265 3.78e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 3.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920 116 VKKWEMELQTLRESNAR---LTTALQESAASVEQWKRQFSICRDENDRLR---------SKIEELEEQCSEINREKEKNT 183
Cdd:COG4717   73 LKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEkllqllplyQELEALEAELAELPERLEELE 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920 184 QLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSecEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELK 263
Cdd:COG4717  153 ERLEELRELEEELEELEAELAELQEELEELLEQLS--LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230


                 ..
gi 568947920 264 SF 265
Cdd:COG4717  231 QL 232
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
155-259 4.40e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.51  E-value: 4.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920 155 RDENDRLRSKIEEL---EEQCSEINREKEKN-TQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAA 230
Cdd:PRK03918 171 IKEIKRRIERLEKFikrTENIEELIKEKEKElEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESL 250

                         90       100
                 ....*....|....*....|....*....
gi 568947920 231 ERDNQNLEDKVRSLKTDIEESKYRQRHLK 259
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELE 279
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 127-281 4.81e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 38.67  E-value: 4.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   127 RESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIE-ELEEQCSEINREKEkntQLKRRIEELESEVRDKEMELKD 205
Cdd:pfam12128  375 AKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEdDLQALESELREQLE---AGKLEFNEEEYRLKSRLGELKL 451

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   206 LRKQSEIIPQLM-------SECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQR-------HLKGELKSFLEVLDG 271
Cdd:pfam12128  452 RLNQATATPELLlqlenfdERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRqasrrleERQSALDELELQLFP 531

                          170
                   ....*....|
gi 568947920   272 KIDDLHDFRR 281
Cdd:pfam12128  532 QAGTLLHFLR 541
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
98-264 5.34e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.12  E-value: 5.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920  98 LKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTaLQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINR 177
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920 178 EKEKNTQLKRRIEELE---SEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKL-----EAAERDNQNLEDKVRSLKTDIE 249
Cdd:PRK03918 329 RIKELEEKEERLEELKkklKELEKRLEELEERHELYEEAKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEIS 408

                        170
                 ....*....|....*
gi 568947920 250 ESKYRQRHLKGELKS 264
Cdd:PRK03918 409 KITARIGELKKEIKE 423
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
159-259 6.04e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.12  E-value: 6.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920 159 DRLRSKIEELEEQCSEINrekekntQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLE 238
Cdd:PRK03918 193 ELIKEKEKELEEVLREIN-------EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265

                         90       100
                 ....*....|....*....|.
gi 568947920 239 DKVRSLKTDIEESKYRQRHLK 259
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELK 286
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
149-250 6.54e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 37.82  E-value: 6.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920 149 RQFSICRDENDRLRSKIEELEEQCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQL---------MSE 219
Cdd:COG4717   64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYqelealeaeLAE 143

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568947920 220 CEYVSEKLEAAERDNQNLEDKVRSLKTDIEE 250
Cdd:COG4717  144 LPERLEELEERLEELRELEEELEELEAELAE 174
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
117-250 6.78e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.12  E-value: 6.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920 117 KKWEMELQTLRESNARLTTALQESAASVEQWKRQFSicRDENDRLRSKIEELEeqcSEINREKEKNTQLKRRIEELESEV 196
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELS---RELAGLRAELEELEKRREEIKKTL 696

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568947920 197 RDKEMELKDLRKQSEIIpqlmseceyvsEKLEAAERDNQNLEDKVRSLKTDIEE 250
Cdd:PRK03918 697 EKLKEELEEREKAKKEL-----------EKLEKALERVEELREKVKKYKALLKE 739
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 177-276 7.02e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.13  E-value: 7.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920   177 REKEKNTQLKRRIEELEsevRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQR 256
Cdd:TIGR02169  671 SEPAELQRLRERLEGLK---RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747

                           90       100
                   ....*....|....*....|...
gi 568947920   257 HLKGEL---KSFLEVLDGKIDDL 276
Cdd:TIGR02169  748 SLEQEIenvKSELKELEARIEEL 770
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 171-269 7.76e-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: 7.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920 171 QCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSEceyVSEKLEAAERDNQNLEDKVRSLKTDIEE 250
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA---LARRIRALEQELAALEAELAELEKEIAE 94

                         90
                 ....*....|....*....
gi 568947920 251 SKYRQRHLKGELKSFLEVL 269
Cdd:COG4942   95 LRAELEAQKEELAELLRAL 113
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
159-262 8.53e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 37.59  E-value: 8.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947920  159 DRLRSKIEELEEQCSEINREKEKNTQLKRRIEE--------------------LESEVRDKEMELKDLRKQSEIIPQLMS 218
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALQErrealqrlaeyswdeidvasAEREIAELEAELERLDASSDDLAALEE 692

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568947920  219 ECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGEL 262
Cdd:COG4913   693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
 
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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