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Conserved domains on  [gi|3452564|dbj|BAA32479|]
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Vesl-2(delta 11) [Rattus norvegicus]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EVH1_Homer_Vesl cd01206
Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, ...
 3-111 1.17e-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: 233.01  E-value: 1.17e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564    3 EQPIFTTRAHVFQIDPSTKKNWVPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRA 82
Cdd:cd01206   1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                        90       100
                ....*....|....*....|....*....
gi 3452564   83 NTVFGLGFSSEQQLTKFAEKFQEVREAAR 111
Cdd:cd01206  81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 98-331 1.30e-08

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.60  E-value: 1.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564      98 KFAEKFQEVREAARLARDKSQEKIETSSNHSQAssvngtdDEKASHASPADTHLKSENDKLKialtqsaANVKKWEIELQ 177
Cdd:TIGR02168  282 EIEELQKELYALANEISRLEQQKQILRERLANL-------ERQLEELEAQLEELESKLDELA-------EELAELEEKLE 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     178 TLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQC----GEINREKEKNTQLKRRIEELESEVRE-- 251
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIaslnNEIERLEARLERLEDRRERLQQEIEEll 427

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     252 KEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSfLEVLDGKIDDLHD 331
Cdd:TIGR02168  428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS-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 1.17e-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: 233.01  E-value: 1.17e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564    3 EQPIFTTRAHVFQIDPSTKKNWVPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRA 82
Cdd:cd01206   1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                        90       100
                ....*....|....*....|....*....
gi 3452564   83 NTVFGLGFSSEQQLTKFAEKFQEVREAAR 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 1.48e-40

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: 137.97  E-value: 1.48e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564      4 QPIFTTRAHVFQIDPSTKKNWVPAsKQAVTVSYFYDVTRNSYRIISVD--GAKVIINSTITPNMTFTKTSQKFGQWADSR 81
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*
gi 3452564     82 AntVFGLGFSSEQQLTKFAEKFQEV 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 1.61e-29

WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains point mutations in the majority of patients with WAS. Unknown function. Ena-like WH1 domains bind polyproline-containing peptides, and that Homer contains a WH1 domain.


Pssm-ID: 214674  Cd Length: 106  Bit Score: 108.98  E-value: 1.61e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564       1 MGEQPIFTTRAHVFQIDPSTKKnWVPASK-QAVTVSYFYDVTRNSYRIISVDG-AKVIINSTITPNMTFTKTSQKFGQWA 78
Cdd:smart00461   1 LGSQCIILARAVVQLYDADTKK-WVPTGEgGAANLVIDKNQRSYFFRIVGIKGqDKVIWNQELYKNFKYNQATPTFHQWA 79

                           90       100
                   ....*....|....*....|....*..
gi 3452564      79 DsrANTVFGLGFSSEQQLTKFAEKFQE 105
Cdd:smart00461  80 D--DKCVYGLNFASEEEAKKFRKKVLK 104
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 98-331 1.30e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.60  E-value: 1.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564      98 KFAEKFQEVREAARLARDKSQEKIETSSNHSQAssvngtdDEKASHASPADTHLKSENDKLKialtqsaANVKKWEIELQ 177
Cdd:TIGR02168  282 EIEELQKELYALANEISRLEQQKQILRERLANL-------ERQLEELEAQLEELESKLDELA-------EELAELEEKLE 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     178 TLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQC----GEINREKEKNTQLKRRIEELESEVRE-- 251
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIaslnNEIERLEARLERLEDRRERLQQEIEEll 427

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     252 KEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSfLEVLDGKIDDLHD 331
Cdd:TIGR02168  428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS-LERLQENLEGFSE 506
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 151-320 3.13e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 3.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  151 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQE-------SAASVEQWKRQFSICRDENDRLRSKIEELEE 223
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEaqaeeyeLLAELARLEQDIARLEERRRELEERLEELEE 323

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  224 QCGEINREKEKNTQ----LKRRIEELESEVREKEMELKDLRKQSEIIPQLMSECEyvsEKLEAAERDNQNLEDKVRSLKT 299
Cdd:COG1196 324 ELAELEEELEELEEeleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE---EELEELAEELLEALRAAAELAA 400

                       170       180
                ....*....|....*....|.
gi 3452564  300 DIEESKYRQRHLKGELKSFLE 320
Cdd:COG1196 401 QLEELEEAEEALLERLERLEE 421
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
190-339 5.58e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 5.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564   190 LQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINREKEKNTQLKRRIEELESEVREKEMELKDLRKQSEIIPQL 269
Cdd:PRK03918 195 IKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE 274

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564   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 3452564    151 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSIcrdendrLRSKIEELEEQCgeinR 230
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINV-------LQKKIENLQEQL----R 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564    231 EKEKN-TQLKRRIEELESE--------------VREKEMELKDLRKQSEiipqlmSECEYVSEKLEAAERDNQNLEDKVR 295
Cdd:pfam10174 412 DKDKQlAGLKERVKSLQTDssntdtalttleeaLSEKERIIERLKEQRE------REDRERLEELESLKKENKDLKEKVS 485


                  ....*...
gi 3452564    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 1.17e-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: 233.01  E-value: 1.17e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564    3 EQPIFTTRAHVFQIDPSTKKNWVPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRA 82
Cdd:cd01206   1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                        90       100
                ....*....|....*....|....*....
gi 3452564   83 NTVFGLGFSSEQQLTKFAEKFQEVREAAR 111
Cdd:cd01206  81 NTVYGLGFASEAELTKFAEKFQEAKEAAK 109
EVH1_family cd00837
EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; ...
 5-107 4.22e-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: 4.22e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564    5 PIFTTRAHVFQIDPStKKNWVPAS-KQAVTVSYFYDVTRNSYRIISVDGA--KVIINSTITPNMTFTKTSQKFGQWADSR 81
Cdd:cd00837   1 SIFSARAHVMQIDDS-NKNWVPAGgKGASRVSYFKDTTRNSFRIIGVDIKdkKVVINCTITKNLVYNKATQTFHQWADDR 79

                        90       100
                ....*....|....*....|....*.
gi 3452564   82 anTVFGLGFSSEQQLTKFAEKFQEVR 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 1.48e-40

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: 137.97  E-value: 1.48e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564      4 QPIFTTRAHVFQIDPSTKKNWVPAsKQAVTVSYFYDVTRNSYRIISVD--GAKVIINSTITPNMTFTKTSQKFGQWADSR 81
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*
gi 3452564     82 AntVFGLGFSSEQQLTKFAEKFQEV 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 1.61e-29

WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains point mutations in the majority of patients with WAS. Unknown function. Ena-like WH1 domains bind polyproline-containing peptides, and that Homer contains a WH1 domain.


Pssm-ID: 214674  Cd Length: 106  Bit Score: 108.98  E-value: 1.61e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564       1 MGEQPIFTTRAHVFQIDPSTKKnWVPASK-QAVTVSYFYDVTRNSYRIISVDG-AKVIINSTITPNMTFTKTSQKFGQWA 78
Cdd:smart00461   1 LGSQCIILARAVVQLYDADTKK-WVPTGEgGAANLVIDKNQRSYFFRIVGIKGqDKVIWNQELYKNFKYNQATPTFHQWA 79

                           90       100
                   ....*....|....*....|....*..
gi 3452564      79 DsrANTVFGLGFSSEQQLTKFAEKFQE 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 5.42e-13

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: 64.64  E-value: 5.42e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564    5 PIFTTRAHVFQIDPSTKKnWVPA-SKQAVTVSYFYDVTR-NSYRIISVDGA--KVIINSTITPNMTFTKTSQKFGQWADS 80
Cdd:cd01207   1 SVASARASVMVYDDENKR-WVPSgGSQGLSRVQIYHNTRnNTFRVVGRKLQdhEVVINCAILKGLKYNQATPTFHQWRDA 79

                        90       100
                ....*....|....*....|
gi 3452564   81 RanTVFGLGFSSEQQLTKFA 100
Cdd:cd01207  80 R--QVYGLNFASKEEATEFA 97
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 98-331 1.30e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.60  E-value: 1.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564      98 KFAEKFQEVREAARLARDKSQEKIETSSNHSQAssvngtdDEKASHASPADTHLKSENDKLKialtqsaANVKKWEIELQ 177
Cdd:TIGR02168  282 EIEELQKELYALANEISRLEQQKQILRERLANL-------ERQLEELEAQLEELESKLDELA-------EELAELEEKLE 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     178 TLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQC----GEINREKEKNTQLKRRIEELESEVRE-- 251
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIaslnNEIERLEARLERLEDRRERLQQEIEEll 427

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     252 KEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSfLEVLDGKIDDLHD 331
Cdd:TIGR02168  428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS-LERLQENLEGFSE 506
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 100-315 1.39e-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: 56.23  E-value: 1.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     100 AEKFQEVREAARLARDKSQE-----KIETSSNHSQASSVNGTDDEKASHASPADTHLK---SENDKLKIALTQSAANVKK 171
Cdd:TIGR02169  268 EEIEQLLEELNKKIKDLGEEeqlrvKEKIGELEAEIASLERSIAEKERELEDAEERLAkleAEIDKLLAEIEELEREIEE 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     172 WEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINREKEKntqLKRRIEELESEVRE 251
Cdd:TIGR02169  348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR---LQEELQRLSEELAD 424

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3452564     252 KEMELKDLRKQseiIPQLMSECEYVSEKLEAAER-------DNQNLEDKVRSLKTDIEESKYRQRHLKGEL 315
Cdd:TIGR02169  425 LNAAIAGIEAK---INELEEEKEDKALEIKKQEWkleqlaaDLSKYEQELYDLKEEYDRVEKELSKLQREL 492
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 149-338 2.29e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 55.84  E-value: 2.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     149 THLKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQcgeI 228
Cdd:TIGR02169  698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED---L 774

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     229 NREKEKNTQLKRRIeeLESEVREKEMELKDLRKQ----SEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEES 304
Cdd:TIGR02169  775 HKLEEALNDLEARL--SHSRIPEIQAELSKLEEEvsriEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI 852

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 3452564     305 KYRQRHLKGELKSFLEVLD---GKIDDLHDFRRGLSK 338
Cdd:TIGR02169  853 EKEIENLNGKKEELEEELEeleAALRDLESRLGDLKK 889
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 88-315 8.95e-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: 53.91  E-value: 8.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564      88 LGFSSEQQLTKFAEKFQEVR-EAARLARDKSQEKIETSSNHSQASSVNGTDDEKASHASPADTHLKSEN---DKLKIALT 163
Cdd:TIGR02168  720 ELEELSRQISALRKDLARLEaEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEaqiEQLKEELK 799

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     164 QSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEeqcGEINREKEKNTQLKRRIE 243
Cdd:TIGR02168  800 ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA---AEIEELEELIEELESELE 876

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3452564     244 ELESEVREKEMELKDLRKQSEiipQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGEL 315
Cdd:TIGR02168  877 ALLNERASLEEALALLRSELE---ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 151-342 3.74e-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: 51.98  E-value: 3.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     151 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQcgeINR 230
Cdd:TIGR02168  717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQ 793

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     231 EKEKNTQLKRRIEELESEVREKEmelKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 310
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLN---EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870

                          170       180       190
                   ....*....|....*....|....*....|..
gi 3452564     311 LKGELKSFLEVLDGKIDDLHDFRRGLSKLGTD 342
Cdd:TIGR02168  871 LESELEALLNERASLEEALALLRSELEELSEE 902
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 152-329 5.51e-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: 51.21  E-value: 5.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     152 KSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINRE 231
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     232 ----KEKNTQLKRRIEELESEVREKEMELKDLRKQseiIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYR 307
Cdd:TIGR02168  756 ltelEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832

                          170       180
                   ....*....|....*....|..
gi 3452564     308 qrhlKGELKSFLEVLDGKIDDL 329
Cdd:TIGR02168  833 ----IAATERRLEDLEEQIEEL 850
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 175-340 6.50e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.22  E-value: 6.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     175 ELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQC-----GEINREKEKNTQLKRRIEELESEV 249
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeEEQLRVKEKIGELEAEIASLERSI 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     250 REKEMELKDLRKQSEI----IPQLMSECEYVSEKLE--AAERDN-----QNLEDKVRSLKTDIEESKYRQRHLKGELKSF 318
Cdd:TIGR02169  311 AEKERELEDAEERLAKleaeIDKLLAEIEELEREIEeeRKRRDKlteeyAELKEELEDLRAELEEVDKEFAETRDELKDY 390

                          170       180
                   ....*....|....*....|..
gi 3452564     319 LEVLDGKIDDLHDFRRGLSKLG 340
Cdd:TIGR02169  391 REKLEKLKREINELKRELDRLQ 412
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 151-320 3.13e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 3.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  151 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQE-------SAASVEQWKRQFSICRDENDRLRSKIEELEE 223
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEaqaeeyeLLAELARLEQDIARLEERRRELEERLEELEE 323

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  224 QCGEINREKEKNTQ----LKRRIEELESEVREKEMELKDLRKQSEIIPQLMSECEyvsEKLEAAERDNQNLEDKVRSLKT 299
Cdd:COG1196 324 ELAELEEELEELEEeleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE---EELEELAEELLEALRAAAELAA 400

                       170       180
                ....*....|....*....|.
gi 3452564  300 DIEESKYRQRHLKGELKSFLE 320
Cdd:COG1196 401 QLEELEEAEEALLERLERLEE 421
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
139-264 7.91e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 47.55  E-value: 7.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  139 EKASHASPADTHLKSENDKLK--IALTQSAANVKKWEIELQTLRESNARLTTALQEsaasveqwkrqfsiCRDENDRLRS 216
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHeeRELTEEEEEIRRLEEQVERLEAEVEELEAELEE--------------KDERIERLER 448

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 3452564  217 KIEELEEQCGEINREKEKNTQLKRRIEELESEVREKEMELKDLRKQSE 264
Cdd:COG2433 449 ELSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLE 496
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
208-312 1.56e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 46.77  E-value: 1.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  208 RDENDRLRSKIEELEEQCGEInreKEKNTQLKRRIEELESEVREKEMELK-DLRKQSEIipqlmseceyvseklEAAERD 286
Cdd:COG2433 412 EEEIRRLEEQVERLEAEVEEL---EAELEEKDERIERLERELSEARSEERrEIRKDREI---------------SRLDRE 473

                        90       100
                ....*....|....*....|....*.
gi 3452564  287 NQNLEDKVRSLKTDIEESKYRQRHLK 312
Cdd:COG2433 474 IERLERELEEERERIEELKRKLERLK 499
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
150-343 1.60e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564   150 HLKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQES---------AASVEQWKRQFSICRDENDRLRSKIEE 220
Cdd:COG4913  614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvasaEREIAELEAELERLDASSDDLAALEEQ 693

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564   221 LEEQCGEINREKEKNTQLKRRIEELESEVREKEMELKDLRKQSEIIPQLmsECEYVSEKLEA--AERDNQNLEDKVR-SL 297
Cdd:COG4913  694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL--ARLELRALLEErfAAALGDAVERELReNL 771

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 3452564   298 KTDIEESKYRQRHLKGEL----KSFLEV-------LDGKIDDLHDFRRGLSKLGTDN 343
Cdd:COG4913  772 EERIDALRARLNRAEEELeramRAFNREwpaetadLDADLESLPEYLALLDRLEEDG 828
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 212-329 2.04e-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: 45.30  E-value: 2.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  212 DRLRSKIEELEEQCGEINREKEKN----TQLKRRIEELESEVREKEMELKDLRKQ----SEIIPQLMSECEY--VSEKLE 281
Cdd:COG1579  20 DRLEHRLKELPAELAELEDELAALearlEAAKTELEDLEKEIKRLELEIEEVEARikkyEEQLGNVRNNKEYeaLQKEIE 99

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 3452564  282 AAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEVLDGKIDDL 329
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 153-329 2.16e-05

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: 46.17  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564    153 SENDKLKIALTQSAANVKKweiELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQcgeINREK 232
Cdd:TIGR04523 331 SQNNKIISQLNEQISQLKK---ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQE 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564    233 EKNTQLKRRIEELESEVREKEMELKDLRKQseiIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLK 312
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIERLKET---IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481

                         170
                  ....*....|....*..
gi 3452564    313 GELKSFLEVLDGKIDDL 329
Cdd:TIGR04523 482 QNLEQKQKELKSKEKEL 498
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
190-339 5.58e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 5.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564   190 LQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINREKEKNTQLKRRIEELESEVREKEMELKDLRKQSEIIPQL 269
Cdd:PRK03918 195 IKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE 274

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564   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 3452564    151 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSIcrdendrLRSKIEELEEQCgeinR 230
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINV-------LQKKIENLQEQL----R 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564    231 EKEKN-TQLKRRIEELESE--------------VREKEMELKDLRKQSEiipqlmSECEYVSEKLEAAERDNQNLEDKVR 295
Cdd:pfam10174 412 DKDKQlAGLKERVKSLQTDssntdtalttleeaLSEKERIIERLKEQRE------REDRERLEELESLKKENKDLKEKVS 485


                  ....*...
gi 3452564    296 SLKTDIEE 303
Cdd:pfam10174 486 ALQPELTE 493
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 208-338 7.41e-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: 44.67  E-value: 7.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     208 RDENDRLRSKIEELEEQCG----EINREKEKNTQLKRRIEELESEVREKEMEL----KDLRKQSEIIPQLMSECEYVSEK 279
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSslqsELRRIENRLDELSQELSDASRKIGEIEKEIeqleQEEEKLKERLEELEEDLSSLEQE 752

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     280 LEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGEL-KSFLEVLDGKIDDLHDFRRGLSK 338
Cdd:TIGR02169  753 IENVKSELKELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEA 812
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 79-329 1.24e-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: 43.95  E-value: 1.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564      79 DSRANTVFGLGFSSEQQLTKFAEKFQEVREaarLARDKSQEKIETSSNHSQASSVNGTddEKASHASPADTHLKSEndkL 158
Cdd:pfam15921  230 DTEISYLKGRIFPVEDQLEALKSESQNKIE---LLLQQHQDRIEQLISEHEVEITGLT--EKASSARSQANSIQSQ---L 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     159 KIALTQSAANVKKWEIELQTLRESNARLTTALQESAAS----VEQWKRQFSICRDE------------------NDRLRS 216
Cdd:pfam15921  302 EIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMyedkIEELEKQLVLANSEltearterdqfsqesgnlDDQLQK 381

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     217 KIEELEEQCGEINREKEKNTQLKRR-------IEELESEVREKEMELKDLRKqseIIPQLMSECE-YVSEKLEAAERDNQ 288
Cdd:pfam15921  382 LLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEA---LLKAMKSECQgQMERQMAAIQGKNE 458

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 3452564     289 NLEdKVRSLKTDIEESKYRQRHLKGEL---KSFLEVLDGKIDDL 329
Cdd:pfam15921  459 SLE-KVSSLTAQLESTKEMLRKVVEELtakKMTLESSERTVSDL 501
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 175-303 1.40e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.60  E-value: 1.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  175 ELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINREKEKN------TQLKRRIEELESE 248
Cdd:COG1579  32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEalqkeiESLKRRISDLEDE 111

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 3452564  249 VREKEMELKDLRKQseiIPQLMSECEYVSEKLEAAERDnqnLEDKVRSLKTDIEE 303
Cdd:COG1579 112 ILELMERIEELEEE---LAELEAELAELEAELEEKKAE---LDEELAELEAELEE 160
PRK12704 PRK12704
phosphodiesterase; Provisional
 213-322 1.79e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564   213 RLRSKIEELEEQCGEINREK--EKNTQLKRRIEELESEVREKEMELKDLRKQseiipqLMSECEYVSEKLEAAERDNQNL 290
Cdd:PRK12704  39 EAKRILEEAKKEAEAIKKEAllEAKEEIHKLRNEFEKELRERRNELQKLEKR------LLQKEENLDRKLELLEKREEEL 112

                         90       100       110
                 ....*....|....*....|....*....|..
gi 3452564   291 EDKVRSLKTDIEESKYRQRHLKGELKSFLEVL 322
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEELEELIEEQLQEL 144
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
151-338 2.42e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 2.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564   151 LKSENDKLKIALTQsAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINR 230
Cdd:PRK02224 487 LEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564   231 EKEKNTQLKRRIEELESEVREKEMELKDLRKQSEIIPQLMSECEYVSEKLEA-AERDNQNLE------DKVRSLKTDIEE 303
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREAlAELNDERRErlaekrERKRELEAEFDE 645

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 3452564   304 SKYRQ-RHLKGELKSFLEVLDGKIDDLHDFRRGLSK 338
Cdd:PRK02224 646 ARIEEaREDKERAEEYLEQVEEKLDELREERDDLQA 681
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 172-339 2.56e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 2.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     172 WEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEqcgEINREKEKNTQLKRRIEELESEVRE 251
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE---EIEELQKELYALANEISRLEQQKQI 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     252 KEMELKDLRKQSeiipqlmsecEYVSEKLEAAERDNQNLEDKVRSLKTDIEEskyrqrhLKGELKSFLEVLDGKIDDLHD 331
Cdd:TIGR02168  307 LRERLANLERQL----------EELEAQLEELESKLDELAEELAELEEKLEE-------LKEELESLEAELEELEAELEE 369


                   ....*...
gi 3452564     332 FRRGLSKL 339
Cdd:TIGR02168  370 LESRLEEL 377
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 174-338 2.82e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.83  E-value: 2.82e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  174 IELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINREKEKNTQLKRRIEELESEVReKE 253
Cdd:COG1579  10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-NN 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  254 MELKDLRKQSEIIPQLMSECEY----VSEKLEAAERDNQNLEDKVRSLKTDIEEskyrqrhLKGELKSFLEVLDGKIDDL 329
Cdd:COG1579  89 KEYEALQKEIESLKRRISDLEDeileLMERIEELEEELAELEAELAELEAELEE-------KKAELDEELAELEAELEEL 161


                ....*....
gi 3452564  330 HDFRRGLSK 338
Cdd:COG1579 162 EAEREELAA 170
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
169-318 2.92e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 2.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  169 VKKWEIELQTLRESNAR---LTTALQESAASVEQWKRQFSICRDENDRLR---------SKIEELEEQCGEINREKEKNT 236
Cdd:COG4717  73 LKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEkllqllplyQELEALEAELAELPERLEELE 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  237 QLKRRIEELESEVREKEMELKDLRKQSEIIPQLMSecEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELK 316
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLS--LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230


                ..
gi 3452564  317 SF 318
Cdd:COG4717 231 QL 232
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 208-339 3.10e-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: 3.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     208 RDENDRLRSKIEELEEQCGEINRE-KEKNTQLKRRIEELESEVREKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERD 286
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKAlAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 3452564     287 NQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEVLDGKIDDLHDFRRGLSKL 339
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
202-329 3.42e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 3.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  202 RQFSICRDENDRLRSKIEELEEQCGEINREKEKNTQLKRRIEELESEVREKEMELKDLRKQSEIIPQLmseceyvsEKLE 281
Cdd:COG4717  64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY--------QELE 135

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 3452564  282 AAERDNQNLEDKVRSLKTDIEESKYRQRHLKgELKSFLEVLDGKIDDL 329
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELE-ELEAELAELQEELEEL 182
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
175-336 3.82e-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: 3.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564   175 ELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLRS-----KIEELEEQCGEINREKEKNTQLKRRIEELESEV 249
Cdd:COG4913  243 ALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRAELARLEAELERLEARLDAL 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564   250 REKEMELKDLRKQS--EIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEVLDGKID 327
Cdd:COG4913  322 REELDELEAQIRGNggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401


                 ....*....
gi 3452564   328 DLHDFRRGL 336
Cdd:COG4913  402 ALEEALAEA 410
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 93-329 3.99e-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: 3.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564      93 EQQLTKFAEKFQEVREAARLARDKSQEKIETSSNHSQASSVNGTDDEKASHASPADThLKSENDKLKIALTQSAANVKKW 172
Cdd:pfam12128  695 DKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKA-LETWYKRDLASLGVDPDVIAKL 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     173 EIELQTLRESNARLTTALQEsAASVEQWKR-QFSICRDEndrlrskieeLEEQCGEINRE-KEKNTQLKRRIEELESEVR 250
Cdd:pfam12128  774 KREIRTLERKIERIAVRRQE-VLRYFDWYQeTWLQRRPR----------LATQLSNIERAiSELQQQLARLIADTKLRRA 842

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     251 EKEMELKDLRKQ----SEIIPQLMSECEYVSEKLEAAerDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEVLDGKI 326
Cdd:pfam12128  843 KLEMERKASEKQqvrlSENLRGLRCEMSKLATLKEDA--NSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVI 920


                   ...
gi 3452564     327 DDL 329
Cdd:pfam12128  921 ADH 923
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
208-312 4.03e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 4.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564   208 RDENDRLRSKIEELEEQCGEIN---REKEKN-TQLKRRIEELESEVREKEMELKDLRKQSEIIPQLMSECEYVSEKLEAA 283
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEeliKEKEKElEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESL 250

                         90       100
                 ....*....|....*....|....*....
gi 3452564   284 ERDNQNLEDKVRSLKTDIEESKYRQRHLK 312
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELE 279
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 104-303 4.45e-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: 4.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  104 QEVREAARLARDKSQEKIETSSNHSQASSVNGTDDEKASHASPADTHLKSENDKLKIALTQSAANVKKWEIELQTLRESN 183
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  184 ARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINREKEKNTQLKRRIEELESEVREKEMELKDLRKQS 263
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 3452564  264 eiipqlmsecEYVSEKLEAAERDNQNLEDKVRSLKTDIEE 303
Cdd:COG1196 469 ----------LEEAALLEAALAELLEELAEAAARLLLLLE 498
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
147-334 4.67e-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: 4.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564   147 ADTHLKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFsicrdenDRLRSKIEELEEQCG 226
Cdd:COG4913  261 AERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL-------DALREELDELEAQIR 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564   227 EINREKEKntQLKRRIEELESEVREKEMELKDLRKQSEII--PQLMSECEYVSEKLEAAERDNQ------NLEDKVRSLK 298
Cdd:COG4913  334 GNGGDRLE--QLEREIERLERELEERERRRARLEALLAALglPLPASAEEFAALRAEAAALLEAleeeleALEEALAEAE 411

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 3452564   299 TDIEESKYRQRHLKGELKSfLEVLDGKID-DLHDFRR 334
Cdd:COG4913  412 AALRDLRRELRELEAEIAS-LERRKSNIPaRLLALRD 447
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 92-334 6.85e-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: 41.75  E-value: 6.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564      92 SEQQLTKFAEKFQEVREAARLARDKSQEKIETSSnhSQASSVNGTDDEKASHASPADTHLKSENDKLKIALTQSAANVKK 171
Cdd:pfam12128  274 IASRQEERQETSAELNQLLRTLDDQWKEKRDELN--GELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPS 351

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     172 WEIELQTLRESNARLTTALQ---------------ESAASVEQWKRQFSICRDENDRLRSKIE-ELEEQCGEINREKEkn 235
Cdd:pfam12128  352 WQSELENLEERLKALTGKHQdvtakynrrrskikeQNNRDIAGIKDKLAKIREARDRQLAVAEdDLQALESELREQLE-- 429

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     236 tQLKRRIEELESEVREKEMELKDLRKQSEIIPQLM-------SECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQ 308
Cdd:pfam12128  430 -AGKLEFNEEEYRLKSRLGELKLRLNQATATPELLlqlenfdERIERAREEQEAANAEVERLQSELRQARKRRDQASEAL 508

                          250       260       270
                   ....*....|....*....|....*....|...
gi 3452564     309 R-------HLKGELKSFLEVLDGKIDDLHDFRR 334
Cdd:pfam12128  509 RqasrrleERQSALDELELQLFPQAGTLLHFLR 541
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 230-329 7.29e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 7.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     230 REKEKNTQLKRRIEELEsevREKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQR 309
Cdd:TIGR02169  671 SEPAELQRLRERLEGLK---RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747

                           90       100
                   ....*....|....*....|...
gi 3452564     310 HLKGEL---KSFLEVLDGKIDDL 329
Cdd:TIGR02169  748 SLEQEIenvKSELKELEARIEEL 770
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
206-312 7.42e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 7.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564   206 ICRDEN--DRLRSKIEELEEQCGEINrekekntQLKRRIEELESEVREKEMELKDLRKQSEIIPQLMSECEYVSEKLEAA 283
Cdd:PRK03918 185 IKRTENieELIKEKEKELEEVLREIN-------EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKL 257

                         90       100
                 ....*....|....*....|....*....
gi 3452564   284 ERDNQNLEDKVRSLKTDIEESKYRQRHLK 312
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELK 286
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
101-297 8.96e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 8.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  101 EKFQEVREAARLARDKSQEKIETSSNHSQASSVNGTDDEKASHASpadtHLKSENDKLKIALTQSAANVKKWEIElQTLR 180
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELL----ELLDRIEELQELLREAEELEEELQLE-ELEQ 370

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  181 ESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINREKEKNT--QLKRRIEELESEVREKEMELKD 258
Cdd:COG4717 371 EIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELEELEEELEE 450

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 3452564  259 LRKQSEIIPQLMSECEyVSEKLEAAERDNQNLEDKVRSL 297
Cdd:COG4717 451 LREELAELEAELEQLE-EDGELAELLQELEELKAELREL 488
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
170-303 1.12e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564   170 KKWEIELQTLRESNARLTTALQESAASVEQWKRQFSicRDENDRLRSKIEELEEqcgEINREKEKNTQLKRRIEELESEV 249
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELSR---ELAGLRAELEELEKRREEIKKTL 696

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 3452564   250 REKEMELKDLRKQSEIIpqlmseceyvsEKLEAAERDNQNLEDKVRSLKTDIEE 303
Cdd:PRK03918 697 EKLKEELEEREKAKKEL-----------EKLEKALERVEELREKVKKYKALLKE 739
PTZ00121 PTZ00121
MAEBL; Provisional
 101-325 1.19e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564    101 EKFQEVREAARLARDKSQEKIETSSNHSQASSVNGTDDEKASHASPADTHLKSENDKLKIALTQSAANVKKWEI-ELQTL 179
Cdd:PTZ00121 1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkKAEEE 1631

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564    180 RESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINREKEKNTQLKRRIEELESEVREKEMELKDL 259
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3452564    260 RKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEVLDGK 325
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 149-331 1.30e-03

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: 40.77  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564    149 THLKSENDKLKIALTQSaanvkkwEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEI 228
Cdd:TIGR04523 352 TNSESENSEKQRELEEK-------QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564    229 NRE----KEKNTQLKRRIEELESEVREKEMELKDLRKQSEIIPQLMSECEYVSEK------------------LEAAERD 286
Cdd:TIGR04523 425 EKEierlKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKikqnleqkqkelkskekeLKKLNEE 504

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 3452564    287 NQNLEDKVRSLKTDIEESKYRQRHLKGELKSflevLDGKIDDLHD 331
Cdd:TIGR04523 505 KKELEEKVKDLTKKISSLKEKIEKLESEKKE----KESKISDLED 545
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 173-303 1.31e-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: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     173 EIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINRE----KEKNTQLKRRIEELESE 248
Cdd:TIGR02169  818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAlrdlESRLGDLKKERDELEAQ 897

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 3452564     249 VREKEMELKDLRKQSEIIPQLMSECEyvsEKLEAAERDNQNLEDKVRSLKTDIEE 303
Cdd:TIGR02169  898 LRELERKIEELEAQIEKKRKRLSELK---AKLEALEEELSEIEDPKGEDEEIPEE 949
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 212-303 1.69e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.45  E-value: 1.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  212 DRLRSKIEELEEqcgEINR-EKEKNTQLKRRIEELESEVREKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNL 290
Cdd:COG0542 414 DELERRLEQLEI---EKEAlKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPEL 490

                        90
                ....*....|...
gi 3452564  291 EDKVRSLKTDIEE 303
Cdd:COG0542 491 EKELAELEEELAE 503
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
149-288 2.27e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 2.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  149 THLKSENDKLKIALtQSAANVKKWEIELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEI 228
Cdd:COG4717 112 EELREELEKLEKLL-QLLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  229 NREKEKntQLKRRIEELESEVREKEMELKDLRKQSEiipQLMSECEYVSEKLEAAERDNQ 288
Cdd:COG4717 190 TEEELQ--DLAEELEELQQRLAELEEELEEAQEELE---ELEEELEQLENELEAAALEER 244
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
170-322 3.24e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 3.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564   170 KKWEIELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINREKEKNTQLKRRIEELESEV 249
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIE-RLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI 240

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3452564   250 REKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDnqnLEDKVRSLKtDIEESKYRQRHLKGELKSFLEVL 322
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE---LEEKVKELK-ELKEKAEEYIKLSEFYEEYLDEL 309
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
144-329 4.24e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 4.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564   144 ASPADTHLKSENDKLKIALTQSAANVKkwEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEE 223
Cdd:PRK02224 171 ASDARLGVERVLSDQRGSLDQLKAQIE--EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEE 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564   224 QCGEINREKEKNTQLKRRIEELESEVREKEMELKDLRKQ----SEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKT 299
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERleelEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328

                        170       180       190
                 ....*....|....*....|....*....|
gi 3452564   300 DIEESKYRQRHLKGELKSFLEvldgKIDDL 329
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLRE----DADDL 354
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 224-322 4.98e-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: 38.59  E-value: 4.98e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  224 QCGEINREKEKNTQLKRRIEELESEVREKEMELKDLRKQSEIIPQLMSEceyVSEKLEAAERDNQNLEDKVRSLKTDIEE 303
Cdd:COG4942  18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA---LARRIRALEQELAALEAELAELEKEIAE 94

                        90
                ....*....|....*....
gi 3452564  304 SKYRQRHLKGELKSFLEVL 322
Cdd:COG4942  95 LRAELEAQKEELAELLRAL 113
PLN02939 PLN02939
transferase, transferring glycosyl groups
 148-305 5.10e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 38.73  E-value: 5.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564   148 DTHLKSENDKLKIAlTQSAANVKKWEIELQTLRESnarLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGE 227
Cdd:PLN02939 176 EMRLSETDARIKLA-AQEKIHVEILEEQLEKLRNE---LLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIE 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564   228 INREKEKNTQLKRRIEELESEVREKEMEL----KDLRKQSEI-IPQLMSECEYVSEKLEAAER----------DNQNLED 292
Cdd:PLN02939 252 VAETEERVFKLEKERSLLDASLRELESKFivaqEDVSKLSPLqYDCWWEKVENLQDLLDRATNqvekaalvldQNQDLRD 331

                        170
                 ....*....|...
gi 3452564   293 KVRSLKTDIEESK 305
Cdd:PLN02939 332 KVDKLEASLKEAN 344
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 173-323 5.15e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 38.57  E-value: 5.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564    173 EIELQTLRESNARLTTALQEsaasvEQWKRQFSIcrdenDRLRSKIEELEEQCGEINREKEKntqlKRRIEELESEVREK 252
Cdd:pfam17380 434 QREVRRLEEERAREMERVRL-----EEQERQQQV-----ERLRQQEEERKRKKLELEKEKRD----RKRAEEQRRKILEK 499

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3452564    253 EMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLK--GELKSFLEVLD 323
Cdd:pfam17380 500 ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRkaTEERSRLEAME 572
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 93-303 5.39e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 5.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564      93 EQQLTKFAEKFQEVREAARLARDKSQEKIETSSNHSQASSV----NGTDDEKASHASPADTHLKSENDKLKIALTQSAAN 168
Cdd:TIGR02168  795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAterrLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564     169 VKKWEIELQTLRESNARLTTALQESAASVEQWkrqfsicRDENDRLRSKIEELEEQCGEINREKEKntqLKRRIEELESE 248
Cdd:TIGR02168  875 LEALLNERASLEEALALLRSELEELSEELREL-------ESKRSELRRELEELREKLAQLELRLEG---LEVRIDNLQER 944

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 3452564     249 VREK-EMELkdlrkqseiipqlmsecEYVSEKLEAAERDNQNLEDKVRSLKTDIEE 303
Cdd:TIGR02168  945 LSEEySLTL-----------------EEAEALENKIEDDEEEARRRLKRLENKIKE 983
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 208-301 5.47e-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: 5.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564    208 RDENDRLRSKIEELEEqcgEINREKEKNTQLKRRIEELESEVREKEMELKD-LRKQSEIIPQLMSECEYVSEKLEAAERD 286
Cdd:pfam06785  96 QSEEERLEEELSQKEE---ELRRLTEENQQLQIQLQQISQDFAEFRLESEEqLAEKQLLINEYQQTIEEQRSVLEKRQDQ 172

                          90
                  ....*....|....*
gi 3452564    287 NQNLEDKVRSLKTDI 301
Cdd:pfam06785 173 IENLESKVRDLNYEI 187
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
238-322 6.14e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.46  E-value: 6.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  238 LKRRIEELESEVREKEMELKDLRKQSEIIPqlmseceyVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKS 317
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGLVD--------LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251


                ....*
gi 3452564  318 FLEVL 322
Cdd:COG3206 252 GPDAL 256
PRK01156 PRK01156
chromosome segregation protein; Provisional
 212-342 6.77e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 38.34  E-value: 6.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564   212 DRLRSKIEELEEQCGEINREKEKNTQLKRRIEELESEVREKE-------MELKDLRKQSEIIPQLMSECEYVSEKLEAAE 284
Cdd:PRK01156 190 EKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMddynnlkSALNELSSLEDMKNRYESEIKTAESDLSMEL 269

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3452564   285 RDNQNLEDKVRSLKTDIEESKYRQRH-------LKGEL---KSFLEVLDGKIDDLHDFRRGLSKLGTD 342
Cdd:PRK01156 270 EKNNYYKELEERHMKIINDPVYKNRNyindyfkYKNDIenkKQILSNIDAEINKYHAIIKKLSVLQKD 337
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
138-303 7.02e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 37.96  E-value: 7.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  138 DEKASHASPADTHLKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSK 217
Cdd:COG4372   2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  218 IEELEEQcgeINREKEKNTQLKRRIEELESEVREKEMELKDLRKQSEiipQLMSECEYVSEKLEAAERDNQNLEDKVRSL 297
Cdd:COG4372  82 LEELNEQ---LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ---DLEQQRKQLEAQIAELQSEIAEREEELKEL 155


                ....*.
gi 3452564  298 KTDIEE 303
Cdd:COG4372 156 EEQLES 161
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
151-316 8.23e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.12  E-value: 8.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564   151 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEinr 230
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE--- 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564   231 ekekntqLKRRIEELESEVREKEmELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 310
Cdd:PRK03918 271 -------LKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE 342


                 ....*.
gi 3452564   311 LKGELK 316
Cdd:PRK03918 343 LKKKLK 348
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
175-265 9.41e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 37.82  E-value: 9.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  175 ELQTLRESNARLTTALQESAASVEQWKRQFSIcrDENDRLRSKIEELEEQCGEINREKEKNTQLKRRIEELESEVREKEM 254
Cdd:COG4717 157 ELRELEEELEELEAELAELQEELEELLEQLSL--ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234

                        90
                ....*....|.
gi 3452564  255 ELKDLRKQSEI 265
Cdd:COG4717 235 ELEAAALEERL 245
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
151-288 9.74e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 37.57  E-value: 9.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3452564  151 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINR 230
Cdd:COG4372  50 LREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQ 129

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 3452564  231 EKEkntQLKRRIEELESEVREKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQ 288
Cdd:COG4372 130 QRK---QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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