NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|255760042|ref|NP_001157558|]
View 

homer protein homolog 2 isoform 2 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 4.55e-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: 231.85  E-value: 4.55e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   3 EQPIFTTRAHVFQIDPSTKKNWVPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRA 82
Cdd:cd01206    1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                         90       100
                 ....*....|....*....|....*....
gi 255760042  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 ...
 156-331 1.61e-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: 56.22  E-value: 1.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   156 DKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQC----SEINRE 231
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIaslnNEIERL 405

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   232 KEKNTQLKRRIEELESEVRD--KEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQR 309
Cdd:TIGR02168  406 EARLERLEDRRERLQQEIEEllKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485

                          170       180
                   ....*....|....*....|..
gi 255760042   310 HLKGELKSfLEVLDGKIDDLHD 331
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 4.55e-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: 231.85  E-value: 4.55e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   3 EQPIFTTRAHVFQIDPSTKKNWVPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRA 82
Cdd:cd01206    1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                         90       100
                 ....*....|....*....|....*....
gi 255760042  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 1.28e-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: 135.66  E-value: 1.28e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042    4 QPIFTTRAHVFQIDPSTKKNWVPAsKQAVTVSYFYDVTRNSYRIISVD--GAKVIINSTITPNMTFTKTSQKFGQWADSR 81
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*
gi 255760042   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 2.81e-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: 108.60  E-value: 2.81e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042     1 MGEQPIFTTRAHVFQIDPSTKKnWVPASK-QAVTVSYFYDVTRNSYRIISVDG-AKVIINSTITPNMTFTKTSQKFGQWA 78
Cdd:smart00461   1 LGSQCIILARAVVQLYDADTKK-WVPTGEgGAANLVIDKNQRSYFFRIVGIKGqDKVIWNQELYKNFKYNQATPTFHQWA 79

                           90       100
                   ....*....|....*....|....*..
gi 255760042    79 DsrANTVFGLGFSSELQLTKFAEKFQE 105
Cdd:smart00461  80 D--DKCVYGLNFASEEEAKKFRKKVLK 104
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 156-331 1.61e-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: 56.22  E-value: 1.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   156 DKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQC----SEINRE 231
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIaslnNEIERL 405

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   232 KEKNTQLKRRIEELESEVRD--KEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQR 309
Cdd:TIGR02168  406 EARLERLEDRRERLQQEIEEllKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485

                          170       180
                   ....*....|....*....|..
gi 255760042   310 HLKGELKSfLEVLDGKIDDLHD 331
Cdd:TIGR02168  486 QLQARLDS-LERLQENLEGFSE 506
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
150-343 2.77e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 2.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  150 HLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQES---------AASVEQWKRQFSICRDENDRLRSKIEE 220
Cdd:COG4913   614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvasaEREIAELEAELERLDASSDDLAALEEQ 693

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  221 LEEQCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLmsECEYVSEKLEA--AERDNQNLEDKVR-SL 297
Cdd:COG4913   694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL--ARLELRALLEErfAAALGDAVERELReNL 771

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 255760042  298 KTDIEESKYRQRHLKGEL----KSFLEV-------LDGKIDDLHDFRRGLSKLGTDN 343
Cdd:COG4913   772 EERIDALRARLNRAEEELeramRAFNREwpaetadLDADLESLPEYLALLDRLEEDG 828
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
149-303 3.63e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 3.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 149 THLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTtALQESAASVEQWKRQFSI----CRDENDRLRSKIEELEEQ 224
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIE-ELEKELESLEGSKRKLEEkireLEERIEELKKEIEELEEK 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 225 CSEINREKEKNTQ---LKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDI 301
Cdd:PRK03918 282 VKELKELKEKAEEyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH 361


                 ..
gi 255760042 302 EE 303
Cdd:PRK03918 362 EL 363
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 151-303 6.09e-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: 44.81  E-value: 6.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  151 LKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSIcrdendrLRSKIEELEEQCseinR 230
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINV-------LQKKIENLQEQL----R 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  231 EKEKN-TQLKRRIEELESE--------------VRDKEMELKDLRKQSEiipqlmSECEYVSEKLEAAERDNQNLEDKVR 295
Cdd:pfam10174 412 DKDKQlAGLKERVKSLQTDssntdtalttleeaLSEKERIIERLKEQRE------REDRERLEELESLKKENKDLKEKVS 485


                  ....*...
gi 255760042  296 SLKTDIEE 303
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 4.55e-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: 231.85  E-value: 4.55e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   3 EQPIFTTRAHVFQIDPSTKKNWVPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRA 82
Cdd:cd01206    1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                         90       100
                 ....*....|....*....|....*....
gi 255760042  83 NTVFGLGFSSELQLTKFAEKFQEVREAAR 111
Cdd:cd01206   81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
EVH1_family cd00837
EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; ...
 5-107 4.64e-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: 144.53  E-value: 4.64e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   5 PIFTTRAHVFQIDPStKKNWVPAS-KQAVTVSYFYDVTRNSYRIISVDGA--KVIINSTITPNMTFTKTSQKFGQWADSR 81
Cdd:cd00837    1 SIFSARAHVMQIDDS-NKNWVPAGgKGASRVSYFKDTTRNSFRIIGVDIKdkKVVINCTITKNLVYNKATQTFHQWADDR 79

                         90       100
                 ....*....|....*....|....*.
gi 255760042  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 1.28e-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: 135.66  E-value: 1.28e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042    4 QPIFTTRAHVFQIDPSTKKNWVPAsKQAVTVSYFYDVTRNSYRIISVD--GAKVIINSTITPNMTFTKTSQKFGQWADSR 81
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*
gi 255760042   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 2.81e-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: 108.60  E-value: 2.81e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042     1 MGEQPIFTTRAHVFQIDPSTKKnWVPASK-QAVTVSYFYDVTRNSYRIISVDG-AKVIINSTITPNMTFTKTSQKFGQWA 78
Cdd:smart00461   1 LGSQCIILARAVVQLYDADTKK-WVPTGEgGAANLVIDKNQRSYFFRIVGIKGqDKVIWNQELYKNFKYNQATPTFHQWA 79

                           90       100
                   ....*....|....*....|....*..
gi 255760042    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 4.50e-12

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


Pssm-ID: 269918  Cd Length: 108  Bit Score: 61.94  E-value: 4.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   5 PIFTTRAHVFQIDPSTKKnWVPA-SKQAVTVSYFYDVTR-NSYRIISVDGA--KVIINSTITPNMTFTKTSQKFGQWADS 80
Cdd:cd01207    1 SVASARASVMVYDDENKR-WVPSgGSQGLSRVQIYHNTRnNTFRVVGRKLQdhEVVINCAILKGLKYNQATPTFHQWRDA 79

                         90       100
                 ....*....|....*....|
gi 255760042  81 RanTVFGLGFSSELQLTKFA 100
Cdd:cd01207   80 R--QVYGLNFASKEEATEFA 97
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 156-331 1.61e-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: 56.22  E-value: 1.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   156 DKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQC----SEINRE 231
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIaslnNEIERL 405

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   232 KEKNTQLKRRIEELESEVRD--KEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQR 309
Cdd:TIGR02168  406 EARLERLEDRRERLQQEIEEllKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485

                          170       180
                   ....*....|....*....|..
gi 255760042   310 HLKGELKSfLEVLDGKIDDLHD 331
Cdd:TIGR02168  486 QLQARLDS-LERLQENLEGFSE 506
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 149-338 3.04e-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: 55.46  E-value: 3.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   149 THLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQcseI 228
Cdd:TIGR02169  698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED---L 774

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   229 NREKEKNTQLKRR-----IEELESEVRDKEMELKDLRKQSEIIPQ----LMSECEYVSEKLEAAERDNQNLEDKVRSLKT 299
Cdd:TIGR02169  775 HKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQklnrLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 255760042   300 DIEESKYRqrhlKGELKSFLEVLDGKIDDLHDFRRGLSK 338
Cdd:TIGR02169  855 EIENLNGK----KEELEEELEELEAALRDLESRLGDLKK 889
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 92-322 4.95e-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: 4.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042    92 SELQLTKFAEKFQEVREAARLARDKSQEKTE-TSSNHSQASSVNGTDDEKASHASPADThLKSENDKLKIALTQSAANVK 170
Cdd:TIGR02168  728 ISALRKDLARLEAEVEQLEERIAQLSKELTElEAEIEELEERLEEAEEELAEAEAEIEE-LEAQIEQLKEELKALREALD 806

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   171 KWEMELQTLRESNARLTTALQESAASVEQWKRQFsicrdenDRLRSKIEELEEQCSEINREKEkntQLKRRIEELESEVr 250
Cdd:TIGR02168  807 ELRAELTLLNEEAANLRERLESLERRIAATERRL-------EDLEEQIEELSEDIESLAAEIE---ELEELIEELESEL- 875

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255760042   251 dkEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEVL 322
Cdd:TIGR02168  876 --EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 100-309 2.51e-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: 52.38  E-value: 2.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   100 AEKFQEVREAARLARDKSQE-----KTETSSNHSQASSVNGTDDEKASHASPADTH----------LKSENDKLKIALTQ 164
Cdd:TIGR02169  268 EEIEQLLEELNKKIKDLGEEeqlrvKEKIGELEAEIASLERSIAEKERELEDAEERlakleaeidkLLAEIEELEREIEE 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   165 SAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINREKEKNTQ------- 237
Cdd:TIGR02169  348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEeladlna 427

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255760042   238 ----LKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSEceyVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQR 309
Cdd:TIGR02169  428 aiagIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK---YEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 151-342 2.70e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.37  E-value: 2.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   151 LKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQcseINR 230
Cdd:TIGR02168  717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQ 793

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   231 EKEKNTQLKRRIEELESEVRDKEmelKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 310
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLN---EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870

                          170       180       190
                   ....*....|....*....|....*....|..
gi 255760042   311 LKGELKSFLEVLDGKIDDLHDFRRGLSKLGTD 342
Cdd:TIGR02168  871 LESELEALLNERASLEEALALLRSELEELSEE 902
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 175-340 1.17e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.45  E-value: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   175 ELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCS-----EINREKEKNTQLKRRIEELESEV 249
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlgeeEQLRVKEKIGELEAEIASLERSI 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   250 RDKEMELKDLRKQSEI----IPQLMSECEYVSEKLE--AAERDN-----QNLEDKVRSLKTDIEESKYRQRHLKGELKSF 318
Cdd:TIGR02169  311 AEKERELEDAEERLAKleaeIDKLLAEIEELEREIEeeRKRRDKlteeyAELKEELEDLRAELEEVDKEFAETRDELKDY 390

                          170       180
                   ....*....|....*....|..
gi 255760042   319 LEVLDGKIDDLHDFRRGLSKLG 340
Cdd:TIGR02169  391 REKLEKLKREINELKRELDRLQ 412
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 152-329 1.34e-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: 50.06  E-value: 1.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   152 KSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINRE 231
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   232 ----KEKNTQLKRRIEELESEVRDKEMELKDLRKQseiIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYR 307
Cdd:TIGR02168  756 ltelEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832

                          170       180
                   ....*....|....*....|..
gi 255760042   308 qrhlKGELKSFLEVLDGKIDDL 329
Cdd:TIGR02168  833 ----IAATERRLEDLEEQIEEL 850
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
150-343 2.77e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 2.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  150 HLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQES---------AASVEQWKRQFSICRDENDRLRSKIEE 220
Cdd:COG4913   614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvasaEREIAELEAELERLDASSDDLAALEEQ 693

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  221 LEEQCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLmsECEYVSEKLEA--AERDNQNLEDKVR-SL 297
Cdd:COG4913   694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL--ARLELRALLEErfAAALGDAVERELReNL 771

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 255760042  298 KTDIEESKYRQRHLKGEL----KSFLEV-------LDGKIDDLHDFRRGLSKLGTDN 343
Cdd:COG4913   772 EERIDALRARLNRAEEELeramRAFNREwpaetadLDADLESLPEYLALLDRLEEDG 828
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
139-264 3.30e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 48.70  E-value: 3.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 139 EKASHASPADTHLKSENDKLK--IALTQSAANVKKWEMELQTLRESNARLTTALQEsaasveqwkrqfsiCRDENDRLRS 216
Cdd:COG2433  383 EELIEKELPEEEPEAEREKEHeeRELTEEEEEIRRLEEQVERLEAEVEELEAELEE--------------KDERIERLER 448

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 255760042 217 KIEELEEQCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQSE 264
Cdd:COG2433  449 ELSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLE 496
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 151-320 6.00e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 6.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 151 LKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQE-------SAASVEQWKRQFSICRDENDRLRSKIEELEE 223
Cdd:COG1196  244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEaqaeeyeLLAELARLEQDIARLEERRRELEERLEELEE 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 224 QCSEINREKEKNTQ----LKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEyvsEKLEAAERDNQNLEDKVRSLKT 299
Cdd:COG1196  324 ELAELEEELEELEEeleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE---EELEELAEELLEALRAAAELAA 400

                        170       180
                 ....*....|....*....|.
gi 255760042 300 DIEESKYRQRHLKGELKSFLE 320
Cdd:COG1196  401 QLEELEEAEEALLERLERLEE 421
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
208-299 8.87e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 47.55  E-value: 8.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 208 RDENDRLRSKIEELEEQCSEInreKEKNTQLKRRIEELESEVRDKEMELK-DLRKQSEIIpQLMSECEYVSEKLEAAERD 286
Cdd:COG2433  412 EEEIRRLEEQVERLEAEVEEL---EAELEEKDERIERLERELSEARSEERrEIRKDREIS-RLDREIERLERELEEERER 487

                         90
                 ....*....|...
gi 255760042 287 NQNLEDKVRSLKT 299
Cdd:COG2433  488 IEELKRKLERLKE 500
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 212-329 1.35e-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: 45.69  E-value: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 212 DRLRSKIEELEEQCSEINREKEKN----TQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSEC----EY--VSEKLE 281
Cdd:COG1579   20 DRLEHRLKELPAELAELEDELAALearlEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkEYeaLQKEIE 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 255760042 282 AAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEVLDGKIDDL 329
Cdd:COG1579  100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 169-321 2.38e-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: 2.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   169 VKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINREKE----KNTQLKRRIEE 244
Cdd:TIGR02169  793 IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEnlngKKEELEEELEE 872

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255760042   245 LESEVRDKEMELKDLRKQseiIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEV 321
Cdd:TIGR02169  873 LEAALRDLESRLGDLKKE---RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 208-338 3.31e-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: 45.83  E-value: 3.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   208 RDENDRLRSKIEELEEQCS----EINREKEKNTQLKRRIEELESEVRDKEMEL----KDLRKQSEIIPQLMSECEYVSEK 279
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSslqsELRRIENRLDELSQELSDASRKIGEIEKEIeqleQEEEKLKERLEELEEDLSSLEQE 752

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   280 LEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGEL-KSFLEVLDGKIDDLHDFRRGLSK 338
Cdd:TIGR02169  753 IENVKSELKELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEA 812
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
149-303 3.63e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 3.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 149 THLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTtALQESAASVEQWKRQFSI----CRDENDRLRSKIEELEEQ 224
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIE-ELEKELESLEGSKRKLEEkireLEERIEELKKEIEELEEK 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 225 CSEINREKEKNTQ---LKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDI 301
Cdd:PRK03918 282 VKELKELKEKAEEyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH 361


                 ..
gi 255760042 302 EE 303
Cdd:PRK03918 362 EL 363
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
190-339 5.63e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 5.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 190 LQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQL 269
Cdd:PRK03918 195 IKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE 274

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 270 MSECEYVSEKLEAAERDNQNLEdKVRSLKTDIEESKYRQRHLKGELKSFLEVLDGKIDDLHDFRRGLSKL 339
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYI-KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 151-303 6.09e-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: 44.81  E-value: 6.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  151 LKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSIcrdendrLRSKIEELEEQCseinR 230
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINV-------LQKKIENLQEQL----R 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  231 EKEKN-TQLKRRIEELESE--------------VRDKEMELKDLRKQSEiipqlmSECEYVSEKLEAAERDNQNLEDKVR 295
Cdd:pfam10174 412 DKDKQlAGLKERVKSLQTDssntdtalttleeaLSEKERIIERLKEQRE------REDRERLEELESLKKENKDLKEKVS 485


                  ....*...
gi 255760042  296 SLKTDIEE 303
Cdd:pfam10174 486 ALQPELTE 493
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 175-338 6.90e-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: 43.76  E-value: 6.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 175 ELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINREKEKNTQLKRRIEELESEVRDKEm 254
Cdd:COG1579   11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 255 ELKDLRKQSEIIPQLMSECEY----VSEKLEAAERDNQNLEDKVRSLKTDIEEskyrqrhLKGELKSFLEVLDGKIDDLH 330
Cdd:COG1579   90 EYEALQKEIESLKRRISDLEDeileLMERIEELEEELAELEAELAELEAELEE-------KKAELDEELAELEAELEELE 162


                 ....*...
gi 255760042 331 DFRRGLSK 338
Cdd:COG1579  163 AEREELAA 170
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 151-303 9.90e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 9.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 151 LKSENDKLKIALTqsAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIE----------- 219
Cdd:COG1196  218 LKEELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeaqaeeyella 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 220 ELEEQCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQ-SEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLK 298
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEElEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375


                 ....*
gi 255760042 299 TDIEE 303
Cdd:COG1196  376 EAEEE 380
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
151-338 1.02e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 151 LKSENDKLKIALTQsAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINR 230
Cdd:PRK02224 487 LEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 231 EKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEA-AERDNQNLE------DKVRSLKTDIEE 303
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREAlAELNDERRErlaekrERKRELEAEFDE 645

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 255760042 304 SKYRQ-RHLKGELKSFLEVLDGKIDDLHDFRRGLSK 338
Cdd:PRK02224 646 ARIEEaREDKERAEEYLEQVEEKLDELREERDDLQA 681
PRK12704 PRK12704
phosphodiesterase; Provisional
 213-322 1.33e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.61  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 213 RLRSKIEELEEQCSEINREK--EKNTQLKRRIEELESEVRDKEMELKDLRKQseiipqLMSECEYVSEKLEAAERDNQNL 290
Cdd:PRK12704  39 EAKRILEEAKKEAEAIKKEAllEAKEEIHKLRNEFEKELRERRNELQKLEKR------LLQKEENLDRKLELLEKREEEL 112

                         90       100       110
                 ....*....|....*....|....*....|..
gi 255760042 291 EDKVRSLKTDIEESKYRQRHLKGELKSFLEVL 322
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEELEELIEEQLQEL 144
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 208-339 1.40e-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: 43.89  E-value: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   208 RDENDRLRSKIEELEEQCSEINRE-KEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERD 286
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKAlAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 255760042   287 NQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEVLDGKIDDLHDFRRGLSKL 339
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
169-318 2.41e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 2.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 169 VKKWEMELQTLRESNAR---LTTALQESAASVEQWKRQFSICRDENDRLR---------SKIEELEEQCSEINREKEKNT 236
Cdd:COG4717   73 LKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEkllqllplyQELEALEAELAELPERLEELE 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 237 QLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSecEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELK 316
Cdd:COG4717  153 ERLEELRELEEELEELEAELAELQEELEELLEQLS--LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230


                 ..
gi 255760042 317 SF 318
Cdd:COG4717  231 QL 232
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 186-339 2.89e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 2.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   186 LTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINRE----KEKNTQLKRRIEELESEVRDKEMELKDLRK 261
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEvselEEEIEELQKELYALANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255760042   262 QSEiipQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEEskyrqrhLKGELKSFLEVLDGKIDDLHDFRRGLSKL 339
Cdd:TIGR02168  310 RLA---NLERQLEELEAQLEELESKLDELAEELAELEEKLEE-------LKEELESLEAELEELEAELEELESRLEEL 377
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
170-325 3.47e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 3.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 170 KKWEMELQTLRESNARLTTALQESAASVEQWKRQFSicRDENDRLRSKIEELEeqcSEINREKEKNTQLKRRIEELESEV 249
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELS---RELAGLRAELEELEKRREEIKKTL 696

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255760042 250 RDKEMELKDLRKQSEIIpqlmseceyvsEKLEAAERDNQNLEDKVRSLKTDIEESKYRQrhlKGELKS--FLEVLDGK 325
Cdd:PRK03918 697 EKLKEELEEREKAKKEL-----------EKLEKALERVEELREKVKKYKALLKERALSK---VGEIASeiFEELTEGK 760
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
208-312 3.50e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 3.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 208 RDENDRLRSKIEEL---EEQCSEINREKEKN-TQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAA 283
Cdd:PRK03918 171 IKEIKRRIERLEKFikrTENIEELIKEKEKElEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESL 250

                         90       100
                 ....*....|....*....|....*....
gi 255760042 284 ERDNQNLEDKVRSLKTDIEESKYRQRHLK 312
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELE 279
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 93-334 3.89e-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: 42.52  E-value: 3.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042    93 ELQLTKFAEKFQEVREAARLARDKSQEKTETSSNHSQASSVNGTDDEKASHASPADTHLKSENDKLKIA----------- 161
Cdd:pfam12128  259 RLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALedqhgafldad 338

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   162 ---LTQSAANVKKWEMELQTLRESNARLTTALQ---------------ESAASVEQWKRQFSICRDENDRLRSKIE-ELE 222
Cdd:pfam12128  339 ietAAADQEQLPSWQSELENLEERLKALTGKHQdvtakynrrrskikeQNNRDIAGIKDKLAKIREARDRQLAVAEdDLQ 418

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   223 EQCSEINREKEkntQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLM-------SECEYVSEKLEAAERDNQNLEDKVR 295
Cdd:pfam12128  419 ALESELREQLE---AGKLEFNEEEYRLKSRLGELKLRLNQATATPELLlqlenfdERIERAREEQEAANAEVERLQSELR 495

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 255760042   296 SLKTDIEESKYRQR-------HLKGELKSFLEVLDGKIDDLHDFRR 334
Cdd:pfam12128  496 QARKRRDQASEALRqasrrleERQSALDELELQLFPQAGTLLHFLR 541
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
175-336 3.99e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 3.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  175 ELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLRS-----KIEELEEQCSEINREKEKNTQLKRRIEELESEV 249
Cdd:COG4913   243 ALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRAELARLEAELERLEARLDAL 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  250 RDKEMELKDLRKQS--EIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEVLDGKID 327
Cdd:COG4913   322 REELDELEAQIRGNggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401


                  ....*....
gi 255760042  328 DLHDFRRGL 336
Cdd:COG4913   402 ALEEALAEA 410
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
147-334 4.17e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 4.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  147 ADTHLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFsicrdenDRLRSKIEELEEQCS 226
Cdd:COG4913   261 AERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL-------DALREELDELEAQIR 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  227 EINREKEKntQLKRRIEELESEVRDKEMELKDLRKQSEII--PQLMSECEYVSEKLEAAERDNQ------NLEDKVRSLK 298
Cdd:COG4913   334 GNGGDRLE--QLEREIERLERELEERERRRARLEALLAALglPLPASAEEFAALRAEAAALLEAleeeleALEEALAEAE 411

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 255760042  299 TDIEESKYRQRHLKGELKSfLEVLDGKID-DLHDFRR 334
Cdd:COG4913   412 AALRDLRRELRELEAEIAS-LERRKSNIPaRLLALRD 447
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 104-303 4.53e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 4.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 104 QEVREAARLARDKSQEKTETSSNHSQASSVNGTDDEKASHASPADTHLKSENDKLKIALTQSAANVKKWEMELQTLRESN 183
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 184 ARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQS 263
Cdd:COG1196  389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 255760042 264 eiipqlmsecEYVSEKLEAAERDNQNLEDKVRSLKTDIEE 303
Cdd:COG1196  469 ----------LEEAALLEAALAELLEELAEAAARLLLLLE 498
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
206-312 5.28e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 5.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 206 ICRDEN--DRLRSKIEELEEQCSEINrekekntQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAA 283
Cdd:PRK03918 185 IKRTENieELIKEKEKELEEVLREIN-------EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKL 257

                         90       100
                 ....*....|....*....|....*....
gi 255760042 284 ERDNQNLEDKVRSLKTDIEESKYRQRHLK 312
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELK 286
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 93-329 5.31e-04

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: 42.03  E-value: 5.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042    93 ELQLTKFAEKFQEVREAA-----RLARDKSQEKTETSSNHSQASSVNGTDDEKASHASPADTHLKSENDKLKIALTQSAA 167
Cdd:pfam15921  277 EVEITGLTEKASSARSQAnsiqsQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANS 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   168 NVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRskieeleeqcseinrekEKNTQLKRRIEELES 247
Cdd:pfam15921  357 ELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLW-----------------DRDTGNSITIDHLRR 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   248 EVRDKEMELKDLRKqseIIPQLMSECE-YVSEKLEAAERDNQNLEdKVRSLKTDIEESKYRQRHLKGEL---KSFLEVLD 323
Cdd:pfam15921  420 ELDDRNMEVQRLEA---LLKAMKSECQgQMERQMAAIQGKNESLE-KVSSLTAQLESTKEMLRKVVEELtakKMTLESSE 495


                   ....*.
gi 255760042   324 GKIDDL 329
Cdd:pfam15921  496 RTVSDL 501
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 149-331 5.34e-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: 41.93  E-value: 5.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  149 THLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTalqesaaSVEQWKRQFSICRDENDRLRSKIEELEEQCSEI 228
Cdd:TIGR04523 352 TNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLES-------QINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  229 NRE----KEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMS--ECEYVSEK----------------LEAAERD 286
Cdd:TIGR04523 425 EKEierlKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlSRSINKIKqnleqkqkelkskekeLKKLNEE 504

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 255760042  287 NQNLEDKVRSLKTDIEESKYRQRHLKGELKSflevLDGKIDDLHD 331
Cdd:TIGR04523 505 KKELEEKVKDLTKKISSLKEKIEKLESEKKE----KESKISDLED 545
PTZ00121 PTZ00121
MAEBL; Provisional
 91-325 5.58e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 5.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   91 SSELQLTKFAEKFQEVREAARlARDKSQEKTETSSNHSQASSVNGTDDEKASHASPADTHLKSENDKLKIALTQSAANVK 170
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEE-AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  171 KWEMElqtlRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINREKEKNTQLKRRIEELESEVR 250
Cdd:PTZ00121 1627 KAEEE----KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255760042  251 DKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEVLDGK 325
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
202-329 7.08e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 7.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 202 RQFSICRDENDRLRSKIEELEEQCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLmseceyvsEKLE 281
Cdd:COG4717   64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY--------QELE 135

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 255760042 282 AAERDNQNLEDKVRSLKTDIEESKYRQRHLKgELKSFLEVLDGKIDDL 329
Cdd:COG4717  136 ALEAELAELPERLEELEERLEELRELEEELE-ELEAELAELQEELEEL 182
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
91-339 8.03e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 8.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  91 SSELQLTKFAEKFQEVREAARLARDKSQEKTETSSNHSQA-------SSVNGTDDEKASHASPADTHLKSENDKLKIALT 163
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAeqlkeleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 164 QSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDEndrLRSKIEELEE----------QCSEINREKE 233
Cdd:PRK03918 543 SLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEE---LEERLKELEPfyneylelkdAEKELEREEK 619

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 234 KNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEY--VSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHL 311
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699

                        250       260       270
                 ....*....|....*....|....*....|....
gi 255760042 312 KGELKSF------LEVLDGKIDDLHDFRRGLSKL 339
Cdd:PRK03918 700 KEELEERekakkeLEKLEKALERVEELREKVKKY 733
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 212-303 1.05e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.84  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 212 DRLRSKIEELEEQCSEInrEKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLE 291
Cdd:COG0542  414 DELERRLEQLEIEKEAL--KKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELE 491

                         90
                 ....*....|..
gi 255760042 292 DKVRSLKTDIEE 303
Cdd:COG0542  492 KELAELEEELAE 503
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
93-303 1.10e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  93 ELQLTKFAEKFQEVREAARLAR--DKSQEKTETSSN---------HSQASSVNGTDDEKASHASPADTHlKSENDKLKIA 161
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVEAEDriERLEERREDLEEliaerretiEEKRERAEELRERAAELEAEAEEK-REAAAEAEEE 566

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 162 LTQSAANVKKWEMELQTLRESNARLTTaLQESAASVEQwkrqfsiCRDENDRLRSKIEELEEQCSEinrEKEKNTQLKRR 241
Cdd:PRK02224 567 AEEAREEVAELNSKLAELKERIESLER-IRTLLAAIAD-------AEDEIERLREKREALAELNDE---RRERLAEKRER 635

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255760042 242 IEELESEVRDKEMElkDLRKQSEiipQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEE 303
Cdd:PRK02224 636 KRELEAEFDEARIE--EAREDKE---RAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 230-329 1.25e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042   230 REKEKNTQLKRRIEELEsevRDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQR 309
Cdd:TIGR02169  671 SEPAELQRLRERLEGLK---RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747

                           90       100
                   ....*....|....*....|...
gi 255760042   310 HLKGEL---KSFLEVLDGKIDDL 329
Cdd:TIGR02169  748 SLEQEIenvKSELKELEARIEEL 770
PLN02939 PLN02939
transferase, transferring glycosyl groups
 148-305 1.52e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 40.66  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 148 DTHLKSENDKLKIAlTQSAANVKKWEMELQTLRESnarLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSE 227
Cdd:PLN02939 176 EMRLSETDARIKLA-AQEKIHVEILEEQLEKLRNE---LLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIE 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 228 INREKEKNTQLKRRIEELESEVRDKEMEL----KDLRKQSEI-IPQLMSECEYVSEKLEAAER----------DNQNLED 292
Cdd:PLN02939 252 VAETEERVFKLEKERSLLDASLRELESKFivaqEDVSKLSPLqYDCWWEKVENLQDLLDRATNqvekaalvldQNQDLRD 331

                        170
                 ....*....|...
gi 255760042 293 KVRSLKTDIEESK 305
Cdd:PLN02939 332 KVDKLEASLKEAN 344
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 151-290 1.61e-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: 38.76  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  151 LKSENDKLKIAL-----TQSAANVKKWEMELQTLRESNARLTtALQESAASVEQWKRQFSicrdenDRLRSKIEELEEQC 225
Cdd:pfam08614  19 LEAENAKLQSEPesvlpSTSSSKLSKASPQSASIQSLEQLLA-QLREELAELYRSRGELA------QRLVDLNEELQELE 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255760042  226 SEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQlmsecEYVS---------EKLEAAERDNQNL 290
Cdd:pfam08614  92 KKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQD-----ELVAlqlqlnmaeEKLRKLEKENREL 160
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
149-288 1.92e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 149 THLKSENDKLKIALtQSAANVKKWEMELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEI 228
Cdd:COG4717  112 EELREELEKLEKLL-QLLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 229 NREKEKntQLKRRIEELESEVRDKEMELKDLRKQSEiipQLMSECEYVSEKLEAAERDNQ 288
Cdd:COG4717  190 TEEELQ--DLAEELEELQQRLAELEEELEEAQEELE---ELEEELEQLENELEAAALEER 244
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
210-316 2.82e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 2.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 210 ENDRLRSKIEELEEQCSEINREK----EKNTQLKRRIEELESEVRD---KEMELKDLRKQSEIIPQLMSECEYVSEKLEA 282
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKrkleEKIRELEERIEELKKEIEEleeKVKELKELKEKAEEYIKLSEFYEEYLDELRE 311

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 255760042 283 AERDNQNLEDKVRSLK---TDIEESKYRQRHLKGELK 316
Cdd:PRK03918 312 IEKRLSRLEEEINGIEeriKELEEKEERLEELKKKLK 348
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
212-315 2.94e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  212 DRLRSKIEELEEQCSEINREKEKNTQLKRRIEE--------------------LESEVRDKEMELKDLRKQSEIIPQLMS 271
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALQErrealqrlaeyswdeidvasAEREIAELEAELERLDASSDDLAALEE 692

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 255760042  272 ECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGEL 315
Cdd:COG4913   693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 224-322 3.50e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 3.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 224 QCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSEceyVSEKLEAAERDNQNLEDKVRSLKTDIEE 303
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA---LARRIRALEQELAALEAELAELEKEIAE 94

                         90
                 ....*....|....*....
gi 255760042 304 SKYRQRHLKGELKSFLEVL 322
Cdd:COG4942   95 LRAELEAQKEELAELLRAL 113
PRK01156 PRK01156
chromosome segregation protein; Provisional
 212-342 3.62e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.11  E-value: 3.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 212 DRLRSKIEELEEQCSEINREKEKNTQLKRRIEELESEVRDKE-------MELKDLRKQSEIIPQLMSECEYVSEKLEAAE 284
Cdd:PRK01156 190 EKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMddynnlkSALNELSSLEDMKNRYESEIKTAESDLSMEL 269

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255760042 285 RDNQNLEDKVRSLKTDIEESKYRQRH-------LKGEL---KSFLEVLDGKIDDLHDFRRGLSKLGTD 342
Cdd:PRK01156 270 EKNNYYKELEERHMKIINDPVYKNRNyindyfkYKNDIenkKQILSNIDAEINKYHAIIKKLSVLQKD 337
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
138-308 3.95e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 3.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 138 DEKASHASPADTHLKSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSK 217
Cdd:COG4372    2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 218 IEELEEQC-----------SEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIPQLMSECEyvsEKLEAAERD 286
Cdd:COG4372   82 LEELNEQLqaaqaelaqaqEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAERE---EELKELEEQ 158

                        170       180
                 ....*....|....*....|..
gi 255760042 287 NQNLEDKVRSLKTDIEESKYRQ 308
Cdd:COG4372  159 LESLQEELAALEQELQALSEAE 180
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
170-322 4.03e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 4.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 170 KKWEMELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCSEINREKEKNTQLKRRIEELESEV 249
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIE-RLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI 240

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255760042 250 RDKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDnqnLEDKVRSLKtDIEESKYRQRHLKGELKSFLEVL 322
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE---LEEKVKELK-ELKEKAEEYIKLSEFYEEYLDEL 309
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 208-301 4.68e-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: 4.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  208 RDENDRLRSKIEELEEqcsEINREKEKNTQLKRRIEELESEVRDKEMELKD-LRKQSEIIPQLMSECEYVSEKLEAAERD 286
Cdd:pfam06785  96 QSEEERLEEELSQKEE---ELRRLTEENQQLQIQLQQISQDFAEFRLESEEqLAEKQLLINEYQQTIEEQRSVLEKRQDQ 172

                          90
                  ....*....|....*
gi 255760042  287 NQNLEDKVRSLKTDI 301
Cdd:pfam06785 173 IENLESKVRDLNYEI 187
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 115-259 5.04e-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: 37.49  E-value: 5.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  115 DKSQEKTETSSNHSQASSVNGTDDEKASHASPADTHLKSENDKLKIALTQSaanvkkwEMELQTLRESNARLTTALQESA 194
Cdd:pfam06785  59 DALKEKFEKSFLEEKEAKLTELDAEGFKILEETLEELQSEEERLEEELSQK-------EEELRRLTEENQQLQIQLQQIS 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255760042  195 ASVEQWKRqfsicrDENDRLRSKIEELEEQCSEINREKEKNTQLKRRIEELESEVRDKEMELKDL 259
Cdd:pfam06785 132 QDFAEFRL------ESEEQLAEKQLLINEYQQTIEEQRSVLEKRQDQIENLESKVRDLNYEIKTL 190
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
144-329 7.03e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.48  E-value: 7.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 144 ASPADTHLKSENDKLKIALTQSAANVKkwEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEE 223
Cdd:PRK02224 171 ASDARLGVERVLSDQRGSLDQLKAQIE--EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEE 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042 224 QCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQ----SEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKT 299
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERleelEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328

                        170       180       190
                 ....*....|....*....|....*....|
gi 255760042 300 DIEESKYRQRHLKGELKSFLEvldgKIDDL 329
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLRE----DADDL 354
COG5022 COG5022
Myosin heavy chain [General function prediction only];
111-305 7.44e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 38.52  E-value: 7.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  111 RLARDKSQEKTETSSNHSQASSVNGTDDEKASHaspadthLKSENDKLKIAltqsaanvkkwemELQTLRESNARLTTAL 190
Cdd:COG5022   878 ELAERQLQELKIDVKSISSLKLVNLELESEIIE-------LKKSLSSDLIE-------------NLEFKTELIARLKKLL 937

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  191 QESAASVEQWKRQFSicRDENDRLRSKIEELEEQCSEINREKEKNTQLKRRIEELESEVRDKEMELKDLRKQSEIIP--- 267
Cdd:COG5022   938 NNIDLEEGPSIEYVK--LPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQest 1015

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 255760042  268 -QLMSECEYVSEKLEAAERDNQnlEDKVRSLKTDIEESK 305
Cdd:COG5022  1016 kQLKELPVEVAELQSASKIISS--ESTELSILKPLQKLK 1052
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 152-333 8.84e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 37.95  E-value: 8.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  152 KSENDKLKIALTQSAANVKKWEMELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQC------ 225
Cdd:pfam07888  65 KRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIktltqr 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255760042  226 -----SEINREKEK--------------NTQLKRRIEELESEVRDKEMELKDLR----KQSEIIPQLMSECEYVSEKLEA 282
Cdd:pfam07888 145 vlereTELERMKERakkagaqrkeeeaeRKQLQAKLQQTEEELRSLSKEFQELRnslaQRDTQVLQLQDTITTLTQKLTT 224

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 255760042  283 AER---DNQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEVLDGKIDDLHDFR 333
Cdd:pfam07888 225 AHRkeaENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQAR 278
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH