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Conserved domains on  [gi|58372172|ref|NP_036113|]
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homer protein homolog 2 isoform 1 [Mus musculus]

Protein Classification

Homer/Vesl family EVH1 domain-containing protein( domain architecture ID 10100433)

Homer/Vesl family EVH1 (WH1, RanBP1-WASP) domain-containing protein is a synaptic scaffolding protein, required for long-term potentiation, a form of synaptic plasticity thought to underlie memory formation

CATH:  2.30.29.30
Gene Ontology:  GO:0007216|GO:0035256|GO:0005515
PubMed:  11911879|17316461
SCOP:  4002440

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EVH1_Homer_Vesl cd01206
Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, ...
 3-111 8.97e-77

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: 231.47  E-value: 8.97e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172   3 EQPIFTTRAHVFQIDPSTKKNWVPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRA 82
Cdd:cd01206   1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                        90       100
                ....*....|....*....|....*....
gi 58372172  83 NTVFGLGFSSELQLTKFAEKFQEVREAAR 111
Cdd:cd01206  81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 167-342 1.29e-08

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.60  E-value: 1.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    167 DKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQC----SEINRE 242
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIaslnNEIERL 405

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    243 KEKNTQLKRRIEELESEVRD--KEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQR 320
Cdd:TIGR02168  406 EARLERLEDRRERLQQEIEEllKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485

                          170       180
                   ....*....|....*....|..
gi 58372172    321 HLKGELKSfLEVLDGKIDDLHD 342
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, ...
 3-111 8.97e-77

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: 231.47  E-value: 8.97e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172   3 EQPIFTTRAHVFQIDPSTKKNWVPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRA 82
Cdd:cd01206   1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                        90       100
                ....*....|....*....|....*....
gi 58372172  83 NTVFGLGFSSELQLTKFAEKFQEVREAAR 111
Cdd:cd01206  81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 4-106 1.01e-39

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: 136.43  E-value: 1.01e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172     4 QPIFTTRAHVFQIDPSTKKNWVPAsKQAVTVSYFYDVTRNSYRIISVD--GAKVIINSTITPNMTFTKTSQKFGQWADSR 81
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*
gi 58372172    82 AntVFGLGFSSELQLTKFAEKFQEV 106
Cdd:pfam00568  88 C--VYGLNFASEEEATKFAKAVQEA 110
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 1-105 2.52e-29

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: 108.98  E-value: 2.52e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172      1 MGEQPIFTTRAHVFQIDPSTKKnWVPASK-QAVTVSYFYDVTRNSYRIISVDG-AKVIINSTITPNMTFTKTSQKFGQWA 78
Cdd:smart00461   1 LGSQCIILARAVVQLYDADTKK-WVPTGEgGAANLVIDKNQRSYFFRIVGIKGqDKVIWNQELYKNFKYNQATPTFHQWA 79

                           90       100
                   ....*....|....*....|....*..
gi 58372172     79 DsrANTVFGLGFSSELQLTKFAEKFQE 105
Cdd:smart00461  80 D--DKCVYGLNFASEEEAKKFRKKVLK 104
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 167-342 1.29e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.60  E-value: 1.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    167 DKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQC----SEINRE 242
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIaslnNEIERL 405

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    243 KEKNTQLKRRIEELESEVRD--KEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQR 320
Cdd:TIGR02168  406 EARLERLEDRRERLQQEIEEllKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485

                          170       180
                   ....*....|....*....|..
gi 58372172    321 HLKGELKSfLEVLDGKIDDLHD 342
Cdd:TIGR02168  486 QLQARLDS-LERLQENLEGFSE 506
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
161-354 1.93e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 1.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  161 HLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQES---------AASVEQWKRQFSICRDENDRLRSKIEE 231
Cdd:COG4913  614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvasaEREIAELEAELERLDASSDDLAALEEQ 693

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  232 LEEQCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLmsECEYVSEKLEA--AERDNQNLEDKVR-SL 308
Cdd:COG4913  694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL--ARLELRALLEErfAAALGDAVERELReNL 771

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 58372172  309 KTDIEESKYRQRHLKGEL----KSFLEV-------LDGKIDDLHDFRRGLSKLGTDN 354
Cdd:COG4913  772 EERIDALRARLNRAEEELeramRAFNREwpaetadLDADLESLPEYLALLDRLEEDG 828
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
160-314 2.66e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 2.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  160 THLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTtALQESAASVEQWKRQFSI----CRDENDRLRSKIEELEEQ 235
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIE-ELEKELESLEGSKRKLEEkireLEERIEELKKEIEELEEK 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  236 CSEINREKEKNTQ---LKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDI 312
Cdd:PRK03918 282 VKELKELKEKAEEyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH 361


                 ..
gi 58372172  313 EE 314
Cdd:PRK03918 362 EL 363
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 162-314 5.63e-05

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: 45.20  E-value: 5.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172   162 LKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSIcrdendrLRSKIEELEEQCseinR 241
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINV-------LQKKIENLQEQL----R 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172   242 EKEKN-TQLKRRIEELESE--------------VRDKEMELKDLRKQSEiipqlmSECEYVSEKLEAAERDNQNLEDKVR 306
Cdd:pfam10174 412 DKDKQlAGLKERVKSLQTDssntdtalttleeaLSEKERIIERLKEQRE------REDRERLEELESLKKENKDLKEKVS 485


                  ....*...
gi 58372172   307 SLKTDIEE 314
Cdd:pfam10174 486 ALQPELTE 493
 
Name Accession Description Interval E-value
EVH1_Homer_Vesl cd01206
Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, ...
 3-111 8.97e-77

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: 231.47  E-value: 8.97e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172   3 EQPIFTTRAHVFQIDPSTKKNWVPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRA 82
Cdd:cd01206   1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                        90       100
                ....*....|....*....|....*....
gi 58372172  83 NTVFGLGFSSELQLTKFAEKFQEVREAAR 111
Cdd:cd01206  81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
EVH1_family cd00837
EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; ...
 5-107 4.05e-43

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: 144.91  E-value: 4.05e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172   5 PIFTTRAHVFQIDPStKKNWVPAS-KQAVTVSYFYDVTRNSYRIISVDGA--KVIINSTITPNMTFTKTSQKFGQWADSR 81
Cdd:cd00837   1 SIFSARAHVMQIDDS-NKNWVPAGgKGASRVSYFKDTTRNSFRIIGVDIKdkKVVINCTITKNLVYNKATQTFHQWADDR 79

                        90       100
                ....*....|....*....|....*.
gi 58372172  82 anTVFGLGFSSELQLTKFAEKFQEVR 107
Cdd:cd00837  80 --TVFGLNFASEEDATKFAEAVQEAL 103
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 4-106 1.01e-39

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: 136.43  E-value: 1.01e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172     4 QPIFTTRAHVFQIDPSTKKNWVPAsKQAVTVSYFYDVTRNSYRIISVD--GAKVIINSTITPNMTFTKTSQKFGQWADSR 81
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*
gi 58372172    82 AntVFGLGFSSELQLTKFAEKFQEV 106
Cdd:pfam00568  88 C--VYGLNFASEEEATKFAKAVQEA 110
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 1-105 2.52e-29

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: 108.98  E-value: 2.52e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172      1 MGEQPIFTTRAHVFQIDPSTKKnWVPASK-QAVTVSYFYDVTRNSYRIISVDG-AKVIINSTITPNMTFTKTSQKFGQWA 78
Cdd:smart00461   1 LGSQCIILARAVVQLYDADTKK-WVPTGEgGAANLVIDKNQRSYFFRIVGIKGqDKVIWNQELYKNFKYNQATPTFHQWA 79

                           90       100
                   ....*....|....*....|....*..
gi 58372172     79 DsrANTVFGLGFSSELQLTKFAEKFQE 105
Cdd:smart00461  80 D--DKCVYGLNFASEEEAKKFRKKVLK 104
EVH1_Ena_VASP-like cd01207
Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: ...
 5-100 3.73e-12

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


Pssm-ID: 269918  Cd Length: 108  Bit Score: 62.33  E-value: 3.73e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172   5 PIFTTRAHVFQIDPSTKKnWVPA-SKQAVTVSYFYDVTR-NSYRIISVDGA--KVIINSTITPNMTFTKTSQKFGQWADS 80
Cdd:cd01207   1 SVASARASVMVYDDENKR-WVPSgGSQGLSRVQIYHNTRnNTFRVVGRKLQdhEVVINCAILKGLKYNQATPTFHQWRDA 79

                        90       100
                ....*....|....*....|
gi 58372172  81 RanTVFGLGFSSELQLTKFA 100
Cdd:cd01207  80 R--QVYGLNFASKEEATEFA 97
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 167-342 1.29e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.60  E-value: 1.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    167 DKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQC----SEINRE 242
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIaslnNEIERL 405

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    243 KEKNTQLKRRIEELESEVRD--KEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQR 320
Cdd:TIGR02168  406 EARLERLEDRRERLQQEIEEllKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485

                          170       180
                   ....*....|....*....|..
gi 58372172    321 HLKGELKSfLEVLDGKIDDLHD 342
Cdd:TIGR02168  486 QLQARLDS-LERLQENLEGFSE 506
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 160-349 2.14e-08

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: 55.84  E-value: 2.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    160 THLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQcseI 239
Cdd:TIGR02169  698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED---L 774

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    240 NREKEKNTQLKRR-----IEELESEVRDKEMELKDLRKQSEIIPQ----LMSECEYVSEKLEAAERDNQNLEDKVRSLKT 310
Cdd:TIGR02169  775 HKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQklnrLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 58372172    311 DIEESKYRqrhlKGELKSFLEVLDGKIDDLHDFRRGLSK 349
Cdd:TIGR02169  855 EIENLNGK----KEELEEELEELEAALRDLESRLGDLKK 889
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 162-333 5.81e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.68  E-value: 5.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    162 LKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFsicrdenDRLRSKIEELEEQCSEINR 241
Cdd:TIGR02168  787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL-------EDLEEQIEELSEDIESLAA 859

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    242 EKEkntQLKRRIEELESEVrdkEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 321
Cdd:TIGR02168  860 EIE---ELEELIEELESEL---EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933

                          170
                   ....*....|..
gi 58372172    322 LKGELKSFLEVL 333
Cdd:TIGR02168  934 LEVRIDNLQERL 945
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 162-353 2.14e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 2.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    162 LKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQcseINR 241
Cdd:TIGR02168  717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQ 793

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    242 EKEKNTQLKRRIEELESEVRDKEmelKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 321
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLN---EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870

                          170       180       190
                   ....*....|....*....|....*....|..
gi 58372172    322 LKGELKSFLEVLDGKIDDLHDFRRGLSKLGTD 353
Cdd:TIGR02168  871 LESELEALLNERASLEEALALLRSELEELSEE 902
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 162-341 7.64e-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: 51.22  E-value: 7.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    162 LKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINR 241
Cdd:TIGR02169  334 LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE 413

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    242 EKEKNTQ-----------LKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSEceyVSEKLEAAERDNQNLEDKVRSLKT 310
Cdd:TIGR02169  414 ELQRLSEeladlnaaiagIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK---YEQELYDLKEEYDRVEKELSKLQR 490

                          170       180       190
                   ....*....|....*....|....*....|....
gi 58372172    311 DIEESKYRQRHLK---GELKSFLEVLDGKIDDLH 341
Cdd:TIGR02169  491 ELAEAEAQARASEervRGGRAVEEVLKASIQGVH 524
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 186-351 8.95e-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: 8.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    186 ELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCS-----EINREKEKNTQLKRRIEELESEV 260
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlgeeEQLRVKEKIGELEAEIASLERSI 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    261 RDKEMELKDLRKQSEI----IPQLMSECEYVSEKLE--AAERDN-----QNLEDKVRSLKTDIEESKYRQRHLKGELKSF 329
Cdd:TIGR02169  311 AEKERELEDAEERLAKleaeIDKLLAEIEELEREIEeeRKRRDKlteeyAELKEELEDLRAELEEVDKEFAETRDELKDY 390

                          170       180
                   ....*....|....*....|..
gi 58372172    330 LEVLDGKIDDLHDFRRGLSKLG 351
Cdd:TIGR02169  391 REKLEKLKREINELKRELDRLQ 412
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 163-340 1.14e-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: 50.44  E-value: 1.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    163 KSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINRE 242
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    243 ----KEKNTQLKRRIEELESEVRDKEMELKDLRKQseiIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYR 318
Cdd:TIGR02168  756 ltelEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832

                          170       180
                   ....*....|....*....|..
gi 58372172    319 qrhlKGELKSFLEVLDGKIDDL 340
Cdd:TIGR02168  833 ----IAATERRLEDLEEQIEEL 850
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
161-354 1.93e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 1.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  161 HLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQES---------AASVEQWKRQFSICRDENDRLRSKIEE 231
Cdd:COG4913  614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvasaEREIAELEAELERLDASSDDLAALEEQ 693

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  232 LEEQCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLmsECEYVSEKLEA--AERDNQNLEDKVR-SL 308
Cdd:COG4913  694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL--ARLELRALLEErfAAALGDAVERELReNL 771

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 58372172  309 KTDIEESKYRQRHLKGEL----KSFLEV-------LDGKIDDLHDFRRGLSKLGTDN 354
Cdd:COG4913  772 EERIDALRARLNRAEEELeramRAFNREwpaetadLDADLESLPEYLALLDRLEEDG 828
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
150-275 2.55e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 49.09  E-value: 2.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172 150 EKASHASPADTHLKSENDKLK--IALTQSAANVKKWEMELQTLRESNARLTTALQEsaasveqwkrqfsiCRDENDRLRS 227
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHeeRELTEEEEEIRRLEEQVERLEAEVEELEAELEE--------------KDERIERLER 448

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 58372172 228 KIEEL-EEQCSEINREKEKnTQLKRRIEELESEVRDKEMELKDLRKQSE 275
Cdd:COG2433 449 ELSEArSEERREIRKDREI-SRLDREIERLERELEEERERIEELKRKLE 496
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 162-331 4.25e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 4.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172 162 LKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQE-------SAASVEQWKRQFSICRDENDRLRSKIEELEE 234
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEaqaeeyeLLAELARLEQDIARLEERRRELEERLEELEE 323

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172 235 QCSEINREKEKNTQ----LKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEyvsEKLEAAERDNQNLEDKVRSLKT 310
Cdd:COG1196 324 ELAELEEELEELEEeleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE---EELEELAEELLEALRAAAELAA 400

                       170       180
                ....*....|....*....|.
gi 58372172 311 DIEESKYRQRHLKGELKSFLE 331
Cdd:COG1196 401 QLEELEEAEEALLERLERLEE 421
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
219-323 7.40e-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: 7.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172 219 RDENDRLRSKIEELEEQCSEInreKEKNTQLKRRIEELESEVRDKEMELK-DLRKQSEIipqlmseceyvseklEAAERD 297
Cdd:COG2433 412 EEEIRRLEEQVERLEAEVEEL---EAELEEKDERIERLERELSEARSEERrEIRKDREI---------------SRLDRE 473

                        90       100
                ....*....|....*....|....*.
gi 58372172 298 NQNLEDKVRSLKTDIEESKYRQRHLK 323
Cdd:COG2433 474 IERLERELEEERERIEELKRKLERLK 499
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 223-340 8.32e-06

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: 46.46  E-value: 8.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172 223 DRLRSKIEELEEQCSEINREKEKN----TQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSEC----EY--VSEKLE 292
Cdd:COG1579  20 DRLEHRLKELPAELAELEDELAALearlEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkEYeaLQKEIE 99

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 58372172 293 AAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEVLDGKIDDL 340
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 180-332 1.80e-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: 46.60  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    180 VKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINREKE----KNTQLKRRIEE 255
Cdd:TIGR02169  793 IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEnlngKKEELEEELEE 872

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 58372172    256 LESEVRDKEMELKDLRKQseiIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEV 332
Cdd:TIGR02169  873 LEAALRDLESRLGDLKKE---RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 219-349 2.63e-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: 2.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    219 RDENDRLRSKIEELEEQCS----EINREKEKNTQLKRRIEELESEVRDKEMEL----KDLRKQSEIIPQLMSECEYVSEK 290
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSslqsELRRIENRLDELSQELSDASRKIGEIEKEIeqleQEEEKLKERLEELEEDLSSLEQE 752

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    291 LEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGEL-KSFLEVLDGKIDDLHDFRRGLSK 349
Cdd:TIGR02169  753 IENVKSELKELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEA 812
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
160-314 2.66e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 2.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  160 THLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTtALQESAASVEQWKRQFSI----CRDENDRLRSKIEELEEQ 235
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIE-ELEKELESLEGSKRKLEEkireLEERIEELKKEIEELEEK 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  236 CSEINREKEKNTQ---LKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDI 312
Cdd:PRK03918 282 VKELKELKEKAEEyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH 361


                 ..
gi 58372172  313 EE 314
Cdd:PRK03918 362 EL 363
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
101-314 2.75e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.19  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  101 EKFQEVREAARLARDKSQEKTETSSNHSQE-SGCETPSSTQASSVNGTDDEKASHASPADTH------LKSENDKLKIAL 173
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEERREElETLEAEIEDLRETIAETEREREELAEEVRDLrerleeLEEERDDLLAEA 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  174 TQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINREKEKNtqlKRRI 253
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEA---REAV 379

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58372172  254 EELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLeAAERDnqNLEDKVRSLKTDIEE 314
Cdd:PRK02224 380 EDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEEL-REERD--ELREREAELEATLRT 437
PTZ00121 PTZ00121
MAEBL; Provisional
 91-336 3.16e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 3.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    91 SSELQLTKFAEKFQEVREAARLARDKSQEKTETSSNHSQESGCETPSSTQASSVNGTDDEKASHASPADTHLKSENDKLK 170
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172   171 IALTQSAANVKKWEMElqtlRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINREKEKNTQLK 250
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEE----KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA 1691

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172   251 RRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSFL 330
Cdd:PTZ00121 1692 EALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771


                  ....*.
gi 58372172   331 EVLDGK 336
Cdd:PTZ00121 1772 EIRKEK 1777
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
201-350 4.45e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 4.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  201 LQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQL 280
Cdd:PRK03918 195 IKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE 274

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  281 MSECEYVSEKLEAAERDNQNLEdKVRSLKTDIEESKYRQRHLKGELKSFLEVLDGKIDDLHDFRRGLSKL 350
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYI-KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 186-349 4.55e-05

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: 44.15  E-value: 4.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172 186 ELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINREKEKNTQLKRRIEELESEVRDKEm 265
Cdd:COG1579  11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK- 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172 266 ELKDLRKQSEIIPQLMSECEY----VSEKLEAAERDNQNLEDKVRSLKTDIEEskyrqrhLKGELKSFLEVLDGKIDDLH 341
Cdd:COG1579  90 EYEALQKEIESLKRRISDLEDeileLMERIEELEEELAELEAELAELEAELEE-------KKAELDEELAELEAELEELE 162


                ....*...
gi 58372172 342 DFRRGLSK 349
Cdd:COG1579 163 AEREELAA 170
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 162-314 5.63e-05

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: 45.20  E-value: 5.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172   162 LKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSIcrdendrLRSKIEELEEQCseinR 241
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINV-------LQKKIENLQEQL----R 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172   242 EKEKN-TQLKRRIEELESE--------------VRDKEMELKDLRKQSEiipqlmSECEYVSEKLEAAERDNQNLEDKVR 306
Cdd:pfam10174 412 DKDKQlAGLKERVKSLQTDssntdtalttleeaLSEKERIIERLKEQRE------REDRERLEELESLKKENKDLKEKVS 485


                  ....*...
gi 58372172   307 SLKTDIEE 314
Cdd:pfam10174 486 ALQPELTE 493
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 155-340 5.74e-05

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: 45.11  E-value: 5.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    155 ASPADTHLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAAS----VEQWKRQFSICRDE--------- 221
Cdd:pfam15921  287 ASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMyedkIEELEKQLVLANSEltearterd 366

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    222 ---------NDRLRSKIEELEEQCSEINREKEKNTQLKRR-------IEELESEVRDKEMELKDLRKqseIIPQLMSECE 285
Cdd:pfam15921  367 qfsqesgnlDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEA---LLKAMKSECQ 443

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 58372172    286 -YVSEKLEAAERDNQNLEdKVRSLKTDIEESKYRQRHLKGEL---KSFLEVLDGKIDDL 340
Cdd:pfam15921  444 gQMERQMAAIQGKNESLE-KVSSLTAQLESTKEMLRKVVEELtakKMTLESSERTVSDL 501
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 162-314 8.03e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 8.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172 162 LKSENDKLKIALTqsAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIE----------- 230
Cdd:COG1196 218 LKEELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeaqaeeyella 295

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172 231 ELEEQCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQ-SEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLK 309
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEElEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375


                ....*
gi 58372172 310 TDIEE 314
Cdd:COG1196 376 EAEEE 380
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
162-349 9.76e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 9.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  162 LKSENDKLKIALTQsAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINR 241
Cdd:PRK02224 487 LEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  242 EKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEA-AERDNQNLE------DKVRSLKTDIEE 314
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREAlAELNDERRErlaekrERKRELEAEFDE 645

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 58372172  315 SKYRQ-RHLKGELKSFLEVLDGKIDDLHDFRRGLSK 349
Cdd:PRK02224 646 ARIEEaREDKERAEEYLEQVEEKLDELREERDDLQA 681
PRK12704 PRK12704
phosphodiesterase; Provisional
 224-333 1.10e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  224 RLRSKIEELEEQCSEINREK--EKNTQLKRRIEELESEVRDKEMELKDLRKQseiipqLMSECEYVSEKLEAAERDNQNL 301
Cdd:PRK12704  39 EAKRILEEAKKEAEAIKKEAllEAKEEIHKLRNEFEKELRERRNELQKLEKR------LLQKEENLDRKLELLEKREEEL 112

                         90       100       110
                 ....*....|....*....|....*....|..
gi 58372172  302 EDKVRSLKTDIEESKYRQRHLKGELKSFLEVL 333
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEELEELIEEQLQEL 144
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 219-350 1.12e-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: 44.28  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    219 RDENDRLRSKIEELEEQCSEINRE-KEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERD 297
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKAlAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 58372172    298 NQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEVLDGKIDDLHDFRRGLSKL 350
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
180-329 1.52e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 1.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172 180 VKKWEMELQTLRESNAR---LTTALQESAASVEQWKRQFSICRDENDRLR---------SKIEELEEQCSEINREKEKNT 247
Cdd:COG4717  73 LKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEkllqllplyQELEALEAELAELPERLEELE 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172 248 QLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSecEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELK 327
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLS--LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230


                ..
gi 58372172 328 SF 329
Cdd:COG4717 231 QL 232
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
181-336 2.20e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  181 KKWEMELQTLRESNARLTTALQESAASVEQWKRQFSicRDENDRLRSKIEELEeqcSEINREKEKNTQLKRRIEELESEV 260
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELS---RELAGLRAELEELEKRREEIKKTL 696

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58372172  261 RDKEMELKDLRKQSEIIpqlmseceyvsEKLEAAERDNQNLEDKVRSLKTDIEESKYRQrhlKGELKS--FLEVLDGK 336
Cdd:PRK03918 697 EKLKEELEEREKAKKEL-----------EKLEKALERVEELREKVKKYKALLKERALSK---VGEIASeiFEELTEGK 760
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 197-350 2.26e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 2.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    197 LTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINRE----KEKNTQLKRRIEELESEVRDKEMELKDLRK 272
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEvselEEEIEELQKELYALANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58372172    273 QSEiipQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEEskyrqrhLKGELKSFLEVLDGKIDDLHDFRRGLSKL 350
Cdd:TIGR02168  310 RLA---NLERQLEELEAQLEELESKLDELAEELAELEEKLEE-------LKEELESLEAELEELEAELEELESRLEEL 377
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
162-328 2.42e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 2.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  162 LKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTaLQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINR 241
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  242 EKEKNTQLKRRIEELE---SEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKL-----EAAERDNQNLEDKVRSLKTDIE 313
Cdd:PRK03918 329 RIKELEEKEERLEELKkklKELEKRLEELEERHELYEEAKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEIS 408

                        170
                 ....*....|....*
gi 58372172  314 ESKYRQRHLKGELKS 328
Cdd:PRK03918 409 KITARIGELKKEIKE 423
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
219-323 2.55e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  219 RDENDRLRSKIEEL---EEQCSEINREKEKN-TQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAA 294
Cdd:PRK03918 171 IKEIKRRIERLEKFikrTENIEELIKEKEKElEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESL 250

                         90       100
                 ....*....|....*....|....*....
gi 58372172  295 ERDNQNLEDKVRSLKTDIEESKYRQRHLK 323
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELE 279
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
158-345 2.91e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 2.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  158 ADTHLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFsicrdenDRLRSKIEELEEQCS 237
Cdd:COG4913  261 AERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL-------DALREELDELEAQIR 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  238 EINREKEKntQLKRRIEELESEVRDKEMELKDLRKQSEII--PQLMSECEYVSEKLEAAERDNQ------NLEDKVRSLK 309
Cdd:COG4913  334 GNGGDRLE--QLEREIERLERELEERERRRARLEALLAALglPLPASAEEFAALRAEAAALLEAleeeleALEEALAEAE 411

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 58372172  310 TDIEESKYRQRHLKGELKSfLEVLDGKID-DLHDFRR 345
Cdd:COG4913  412 AALRDLRRELRELEAEIAS-LERRKSNIPaRLLALRD 447
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
186-347 3.12e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 3.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  186 ELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLRS-----KIEELEEQCSEINREKEKNTQLKRRIEELESEV 260
Cdd:COG4913  243 ALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRAELARLEAELERLEARLDAL 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  261 RDKEMELKDLRKQS--EIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEVLDGKID 338
Cdd:COG4913  322 REELDELEAQIRGNggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401


                 ....*....
gi 58372172  339 DLHDFRRGL 347
Cdd:COG4913  402 ALEEALAEA 410
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 160-342 3.35e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.70  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172   160 THLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQEsaasveqWKRQFSICRDENDRLRSKIEELEEQCSEI 239
Cdd:TIGR04523 352 TNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND-------LESKIQNQEKLNQQKDEQIKKLQQEKELL 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172   240 NRE----KEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMS--ECEYVSEK----------------LEAAERD 297
Cdd:TIGR04523 425 EKEierlKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlSRSINKIKqnleqkqkelkskekeLKKLNEE 504

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 58372172   298 NQNLEDKVRSLKTDIEESKYRQRHLKGELKSflevLDGKIDDLHD 342
Cdd:TIGR04523 505 KKELEEKVKDLTKKISSLKEKIEKLESEKKE----KESKISDLED 545
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
217-323 4.05e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 4.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  217 ICRDEN--DRLRSKIEELEEQCSEINrekekntQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAA 294
Cdd:PRK03918 185 IKRTENieELIKEKEKELEEVLREIN-------EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKL 257

                         90       100
                 ....*....|....*....|....*....
gi 58372172  295 ERDNQNLEDKVRSLKTDIEESKYRQRHLK 323
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELK 286
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
213-340 4.71e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 4.71e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172 213 RQFSICRDENDRLRSKIEELEEQCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLmseceyvsEKLE 292
Cdd:COG4717  64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY--------QELE 135

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 58372172 293 AAERDNQNLEDKVRSLKTDIEESKYRQRHLKgELKSFLEVLDGKIDDL 340
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELE-ELEAELAELQEELEEL 182
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
93-314 5.25e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 5.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172   93 ELQLTKFAEKFQEVREAARLAR--DKSQEKTETSSN--HSQESGCETPSSTQASSvngtDDEKASHASPADTHlKSENDK 168
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVEAEDriERLEERREDLEEliAERRETIEEKRERAEEL----RERAAELEAEAEEK-REAAAE 562

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  169 LKIALTQSAANVKKWEMELQTLRESNARLTTaLQESAASVEQwkrqfsiCRDENDRLRSKIEELEEQCSEinrEKEKNTQ 248
Cdd:PRK02224 563 AEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIAD-------AEDEIERLREKREALAELNDE---RRERLAE 631

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58372172  249 LKRRIEELESEVRDKEMElkDLRKQSEiipQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEE 314
Cdd:PRK02224 632 KRERKRELEAEFDEARIE--EAREDKE---RAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 191-345 5.40e-04

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: 42.13  E-value: 5.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    191 RESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIE-ELEEQCSEINREKEkntQLKRRIEELESEVRDKEMELKD 269
Cdd:pfam12128  375 AKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEdDLQALESELREQLE---AGKLEFNEEEYRLKSRLGELKL 451

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    270 LRKQSEIIPQLM-------SECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQR-------HLKGELKSFLEVLDG 335
Cdd:pfam12128  452 RLNQATATPELLlqlenfdERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRqasrrleERQSALDELELQLFP 531

                          170
                   ....*....|
gi 58372172    336 KIDDLHDFRR 345
Cdd:pfam12128  532 QAGTLLHFLR 541
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 241-340 9.50e-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: 41.21  E-value: 9.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172    241 REKEKNTQLKRRIEELEsevRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQR 320
Cdd:TIGR02169  671 SEPAELQRLRERLEGLK---RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747

                           90       100
                   ....*....|....*....|...
gi 58372172    321 HLKGEL---KSFLEVLDGKIDDL 340
Cdd:TIGR02169  748 SLEQEIenvKSELKELEARIEEL 770
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 223-314 9.69e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.22  E-value: 9.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172 223 DRLRSKIEELEEQCSEInrEKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLE 302
Cdd:COG0542 414 DELERRLEQLEIEKEAL--KKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELE 491

                        90
                ....*....|..
gi 58372172 303 DKVRSLKTDIEE 314
Cdd:COG0542 492 KELAELEEELAE 503
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 162-301 1.15e-03

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 39.14  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172   162 LKSENDKLKIAL-----TQSAANVKKWEMELQTLRESNARLTtALQESAASVEQWKRQFSicrdenDRLRSKIEELEEQC 236
Cdd:pfam08614  19 LEAENAKLQSEPesvlpSTSSSKLSKASPQSASIQSLEQLLA-QLREELAELYRSRGELA------QRLVDLNEELQELE 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58372172   237 SEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQlmsecEYVS---------EKLEAAERDNQNL 301
Cdd:pfam08614  92 KKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQD-----ELVAlqlqlnmaeEKLRKLEKENREL 160
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
160-299 1.32e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 1.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172 160 THLKSENDKLKIALtQSAANVKKWEMELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEI 239
Cdd:COG4717 112 EELREELEKLEKLL-QLLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172 240 NREKEKntQLKRRIEELESEVRDKEMELKDLRKQSEiipQLMSECEYVSEKLEAAERDNQ 299
Cdd:COG4717 190 TEEELQ--DLAEELEELQQRLAELEEELEEAQEELE---ELEEELEQLENELEAAALEER 244
PLN02939 PLN02939
transferase, transferring glycosyl groups
 159-316 1.57e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 40.66  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  159 DTHLKSENDKLKIAlTQSAANVKKWEMELQTLRESnarLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSE 238
Cdd:PLN02939 176 EMRLSETDARIKLA-AQEKIHVEILEEQLEKLRNE---LLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIE 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  239 INREKEKNTQLKRRIEELESEVRDKEMEL----KDLRKQSEI-IPQLMSECEYVSEKLEAAER----------DNQNLED 303
Cdd:PLN02939 252 VAETEERVFKLEKERSLLDASLRELESKFivaqEDVSKLSPLqYDCWWEKVENLQDLLDRATNqvekaalvldQNQDLRD 331

                        170
                 ....*....|...
gi 58372172  304 KVRSLKTDIEESK 316
Cdd:PLN02939 332 KVDKLEASLKEAN 344
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
149-319 1.67e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 1.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172 149 DEKASHASPADTHLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSK 228
Cdd:COG4372   2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172 229 IEELEEQC-----------SEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEyvsEKLEAAERD 297
Cdd:COG4372  82 LEELNEQLqaaqaelaqaqEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAERE---EELKELEEQ 158

                       170       180
                ....*....|....*....|..
gi 58372172 298 NQNLEDKVRSLKTDIEESKYRQ 319
Cdd:COG4372 159 LESLQEELAALEQELQALSEAE 180
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
142-350 1.93e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 1.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  142 SSVNGTDDEKASHASPADTHLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDE 221
Cdd:PRK03918 510 EKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEE 589

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  222 ndrLRSKIEELEE----------QCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEY--VSE 289
Cdd:PRK03918 590 ---LEERLKELEPfyneylelkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYeeLRE 666

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 58372172  290 KLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSF------LEVLDGKIDDLHDFRRGLSKL 350
Cdd:PRK03918 667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERekakkeLEKLEKALERVEELREKVKKY 733
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
221-327 2.21e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  221 ENDRLRSKIEELEEQCSEINREK----EKNTQLKRRIEELESEVRD---KEMELKDLRKQSEIIPQLMSECEYVSEKLEA 293
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKrkleEKIRELEERIEELKKEIEEleeKVKELKELKEKAEEYIKLSEFYEEYLDELRE 311

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 58372172  294 AERDNQNLEDKVRSLK---TDIEESKYRQRHLKGELK 327
Cdd:PRK03918 312 IEKRLSRLEEEINGIEeriKELEEKEERLEELKKKLK 348
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
223-326 2.43e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  223 DRLRSKIEELEEQCSEINREKEKNTQLKRRIEE--------------------LESEVRDKEMELKDLRKQSEIIPQLMS 282
Cdd:COG4913  613 AALEAELAELEEELAEAEERLEALEAELDALQErrealqrlaeyswdeidvasAEREIAELEAELERLDASSDDLAALEE 692

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 58372172  283 ECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGEL 326
Cdd:COG4913  693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 235-333 2.73e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 2.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172 235 QCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSEceyVSEKLEAAERDNQNLEDKVRSLKTDIEE 314
Cdd:COG4942  18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA---LARRIRALEQELAALEAELAELEKEIAE 94

                        90
                ....*....|....*....
gi 58372172 315 SKYRQRHLKGELKSFLEVL 333
Cdd:COG4942  95 LRAELEAQKEELAELLRAL 113
PRK01156 PRK01156
chromosome segregation protein; Provisional
 223-353 2.89e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.50  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  223 DRLRSKIEELEEQCSEINREKEKNTQLKRRIEELESEVRDKE-------MELKDLRKQSEIIPQLMSECEYVSEKLEAAE 295
Cdd:PRK01156 190 EKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMddynnlkSALNELSSLEDMKNRYESEIKTAESDLSMEL 269

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58372172  296 RDNQNLEDKVRSLKTDIEESKYRQRH-------LKGEL---KSFLEVLDGKIDDLHDFRRGLSKLGTD 353
Cdd:PRK01156 270 EKNNYYKELEERHMKIINDPVYKNRNyindyfkYKNDIenkKQILSNIDAEINKYHAIIKKLSVLQKD 337
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
181-333 3.16e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  181 KKWEMELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINREKEKNTQLKRRIEELESEV 260
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIE-RLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI 240

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58372172  261 RDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDnqnLEDKVRSLKtDIEESKYRQRHLKGELKSFLEVL 333
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE---LEEKVKELK-ELKEKAEEYIKLSEFYEEYLDEL 309
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 150-314 3.49e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 3.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172 150 EKASHASPADTHLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKI 229
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172 230 EELEEQCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQSeiipqlmsecEYVSEKLEAAERDNQNLEDKVRSLK 309
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL----------LEEAALLEAALAELLEELAEAAARL 493


                ....*
gi 58372172 310 TDIEE 314
Cdd:COG1196 494 LLLLE 498
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 219-312 4.42e-03

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 37.88  E-value: 4.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172   219 RDENDRLRSKIEELEEqcsEINREKEKNTQLKRRIEELESEVRDKEMELKD-LRKQSEIIPQLMSECEYVSEKLEAAERD 297
Cdd:pfam06785  96 QSEEERLEEELSQKEE---ELRRLTEENQQLQIQLQQISQDFAEFRLESEEqLAEKQLLINEYQQTIEEQRSVLEKRQDQ 172

                          90
                  ....*....|....*
gi 58372172   298 NQNLEDKVRSLKTDI 312
Cdd:pfam06785 173 IENLESKVRDLNYEI 187
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
155-340 6.67e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.48  E-value: 6.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  155 ASPADTHLKSENDKLKIALTQSAANVKkwEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEE 234
Cdd:PRK02224 171 ASDARLGVERVLSDQRGSLDQLKAQIE--EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEE 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172  235 QCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQ----SEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKT 310
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERleelEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328

                        170       180       190
                 ....*....|....*....|....*....|
gi 58372172  311 DIEESKYRQRHLKGELKSFLEvldgKIDDL 340
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLRE----DADDL 354
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
186-276 8.11e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.21  E-value: 8.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172 186 ELQTLRESNARLTTALQESAASVEQWKRQFSIcrDENDRLRSKIEELEEQCSEINREKEKNTQLKRRIEELESEVRDKEM 265
Cdd:COG4717 157 ELRELEEELEELEAELAELQEELEELLEQLSL--ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234

                        90
                ....*....|.
gi 58372172 266 ELKDLRKQSEI 276
Cdd:COG4717 235 ELEAAALEERL 245
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 187-292 8.54e-03

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 37.40  E-value: 8.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172 187 LQTLRESNArLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINRE-----------KEKNTQLKRRIEE 255
Cdd:COG4026 124 LQNIPEYNE-LREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREEnsileeefdniKSEYSDLKSRFEE 202

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 58372172 256 LESEVRDKEMELKDLRKqsEIIPQLMSECEYVSEKLE 292
Cdd:COG4026 203 LLKKRLLEVFSLEELWK--ELFPEELPEEDFIYFATE 237
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
249-333 8.70e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.07  E-value: 8.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172 249 LKRRIEELESEVRDKEMELKDLRKQSEIIPqlmseceyVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKS 328
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGLVD--------LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251


                ....*
gi 58372172 329 FLEVL 333
Cdd:COG3206 252 GPDAL 256
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
184-308 8.93e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 37.82  E-value: 8.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58372172 184 EMELQTLRESNARL-TTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINREKEKNT--QLKRRIEELESEV 260
Cdd:COG4717 362 ELQLEELEQEIAALlAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEEL 441

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 58372172 261 RDKEMELKDLRKQSEIIPQLMSECEyVSEKLEAAERDNQNLEDKVRSL 308
Cdd:COG4717 442 EELEEELEELREELAELEAELEQLE-EDGELAELLQELEELKAELREL 488
 
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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