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Conserved domains on  [gi|1958644854|ref|XP_038965466|]
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homer protein homolog 2 isoform X1 [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

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 1958644854   3 EQPIFTTRAHVFQIDPSTKKNWVPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRA 82
Cdd:cd01206     1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                          90       100
                  ....*....|....*....|....*....
gi 1958644854  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 1958644854   98 KFAEKFQEVREAARLARDKSQEKIETSSNHSQAssvngtdDEKASHASPADTHLKSENDKLKialtqsaANVKKWEIELQ 177
Cdd:TIGR02168  282 EIEELQKELYALANEISRLEQQKQILRERLANL-------ERQLEELEAQLEELESKLDELA-------EELAELEEKLE 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  178 TLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQC----GEINREKEKNTQLKRRIEELESEVRE-- 251
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIaslnNEIERLEARLERLEDRRERLQQEIEEll 427

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  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 1958644854   3 EQPIFTTRAHVFQIDPSTKKNWVPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRA 82
Cdd:cd01206     1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                          90       100
                  ....*....|....*....|....*....
gi 1958644854  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 1958644854   4 QPIFTTRAHVFQIDPSTKKNWVPAsKQAVTVSYFYDVTRNSYRIISVD--GAKVIINSTITPNMTFTKTSQKFGQWADSR 81
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*
gi 1958644854  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 1958644854    1 MGEQPIFTTRAHVFQIDPSTKKnWVPASK-QAVTVSYFYDVTRNSYRIISVDG-AKVIINSTITPNMTFTKTSQKFGQWA 78
Cdd:smart00461   1 LGSQCIILARAVVQLYDADTKK-WVPTGEgGAANLVIDKNQRSYFFRIVGIKGqDKVIWNQELYKNFKYNQATPTFHQWA 79

                           90       100
                   ....*....|....*....|....*..
gi 1958644854   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 1958644854   98 KFAEKFQEVREAARLARDKSQEKIETSSNHSQAssvngtdDEKASHASPADTHLKSENDKLKialtqsaANVKKWEIELQ 177
Cdd:TIGR02168  282 EIEELQKELYALANEISRLEQQKQILRERLANL-------ERQLEELEAQLEELESKLDELA-------EELAELEEKLE 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  178 TLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQC----GEINREKEKNTQLKRRIEELESEVRE-- 251
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIaslnNEIERLEARLERLEDRRERLQQEIEEll 427

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  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 1958644854 151 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQE-------SAASVEQWKRQFSICRDENDRLRSKIEELEE 223
Cdd:COG1196   244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEaqaeeyeLLAELARLEQDIARLEERRRELEERLEELEE 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854 224 QCGEINREKEKNTQ----LKRRIEELESEVREKEMELKDLRKQSEIIPQLMSECEyvsEKLEAAERDNQNLEDKVRSLKT 299
Cdd:COG1196   324 ELAELEEELEELEEeleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE---EELEELAEELLEALRAAAELAA 400

                         170       180
                  ....*....|....*....|.
gi 1958644854 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 1958644854 190 LQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINREKEKNTQLKRRIEELESEVREKEMELKDLRKQSEIIPQL 269
Cdd:PRK03918  195 IKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE 274

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854 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 1958644854 151 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSIcrdendrLRSKIEELEEQCgeinR 230
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINV-------LQKKIENLQEQL----R 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854 231 EKEKN-TQLKRRIEELESE--------------VREKEMELKDLRKQSEiipqlmSECEYVSEKLEAAERDNQNLEDKVR 295
Cdd:pfam10174 412 DKDKQlAGLKERVKSLQTDssntdtalttleeaLSEKERIIERLKEQRE------REDRERLEELESLKKENKDLKEKVS 485


                  ....*...
gi 1958644854 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 1958644854   3 EQPIFTTRAHVFQIDPSTKKNWVPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRA 82
Cdd:cd01206     1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                          90       100
                  ....*....|....*....|....*....
gi 1958644854  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 1958644854   5 PIFTTRAHVFQIDPStKKNWVPAS-KQAVTVSYFYDVTRNSYRIISVDGA--KVIINSTITPNMTFTKTSQKFGQWADSR 81
Cdd:cd00837     1 SIFSARAHVMQIDDS-NKNWVPAGgKGASRVSYFKDTTRNSFRIIGVDIKdkKVVINCTITKNLVYNKATQTFHQWADDR 79

                          90       100
                  ....*....|....*....|....*.
gi 1958644854  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 1958644854   4 QPIFTTRAHVFQIDPSTKKNWVPAsKQAVTVSYFYDVTRNSYRIISVD--GAKVIINSTITPNMTFTKTSQKFGQWADSR 81
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*
gi 1958644854  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 1958644854    1 MGEQPIFTTRAHVFQIDPSTKKnWVPASK-QAVTVSYFYDVTRNSYRIISVDG-AKVIINSTITPNMTFTKTSQKFGQWA 78
Cdd:smart00461   1 LGSQCIILARAVVQLYDADTKK-WVPTGEgGAANLVIDKNQRSYFFRIVGIKGqDKVIWNQELYKNFKYNQATPTFHQWA 79

                           90       100
                   ....*....|....*....|....*..
gi 1958644854   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 1958644854   5 PIFTTRAHVFQIDPSTKKnWVPA-SKQAVTVSYFYDVTR-NSYRIISVDGA--KVIINSTITPNMTFTKTSQKFGQWADS 80
Cdd:cd01207     1 SVASARASVMVYDDENKR-WVPSgGSQGLSRVQIYHNTRnNTFRVVGRKLQdhEVVINCAILKGLKYNQATPTFHQWRDA 79

                          90       100
                  ....*....|....*....|
gi 1958644854  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 1958644854   98 KFAEKFQEVREAARLARDKSQEKIETSSNHSQAssvngtdDEKASHASPADTHLKSENDKLKialtqsaANVKKWEIELQ 177
Cdd:TIGR02168  282 EIEELQKELYALANEISRLEQQKQILRERLANL-------ERQLEELEAQLEELESKLDELA-------EELAELEEKLE 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  178 TLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQC----GEINREKEKNTQLKRRIEELESEVRE-- 251
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIaslnNEIERLEARLERLEDRRERLQQEIEEll 427

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  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 1958644854  100 AEKFQEVREAARLARDKSQE-----KIETSSNHSQASSVNGTDDEKASHASPADTHLK---SENDKLKIALTQSAANVKK 171
Cdd:TIGR02169  268 EEIEQLLEELNKKIKDLGEEeqlrvKEKIGELEAEIASLERSIAEKERELEDAEERLAkleAEIDKLLAEIEELEREIEE 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  172 WEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINREKEKntqLKRRIEELESEVRE 251
Cdd:TIGR02169  348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR---LQEELQRLSEELAD 424

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958644854  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 1958644854  149 THLKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQcgeI 228
Cdd:TIGR02169  698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED---L 774

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  229 NREKEKNTQLKRRIeeLESEVREKEMELKDLRKQ----SEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEES 304
Cdd:TIGR02169  775 HKLEEALNDLEARL--SHSRIPEIQAELSKLEEEvsriEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI 852

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1958644854  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 1958644854   88 LGFSSEQQLTKFAEKFQEVR-EAARLARDKSQEKIETSSNHSQASSVNGTDDEKASHASPADTHLKSEN---DKLKIALT 163
Cdd:TIGR02168  720 ELEELSRQISALRKDLARLEaEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEaqiEQLKEELK 799

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  164 QSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEeqcGEINREKEKNTQLKRRIE 243
Cdd:TIGR02168  800 ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA---AEIEELEELIEELESELE 876

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958644854  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 1958644854  151 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQcgeINR 230
Cdd:TIGR02168  717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQ 793

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  231 EKEKNTQLKRRIEELESEVREKEmelKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 310
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLN---EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1958644854  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 1958644854  152 KSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINRE 231
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  232 ----KEKNTQLKRRIEELESEVREKEMELKDLRKQseiIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYR 307
Cdd:TIGR02168  756 ltelEAEIEELEERLEEAEEELAEAEAEIEELEAQ---IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832

                          170       180
                   ....*....|....*....|..
gi 1958644854  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 1958644854  175 ELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQC-----GEINREKEKNTQLKRRIEELESEV 249
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeEEQLRVKEKIGELEAEIASLERSI 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  250 REKEMELKDLRKQSEI----IPQLMSECEYVSEKLE--AAERDN-----QNLEDKVRSLKTDIEESKYRQRHLKGELKSF 318
Cdd:TIGR02169  311 AEKERELEDAEERLAKleaeIDKLLAEIEELEREIEeeRKRRDKlteeyAELKEELEDLRAELEEVDKEFAETRDELKDY 390

                          170       180
                   ....*....|....*....|..
gi 1958644854  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 1958644854 151 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQE-------SAASVEQWKRQFSICRDENDRLRSKIEELEE 223
Cdd:COG1196   244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEaqaeeyeLLAELARLEQDIARLEERRRELEERLEELEE 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854 224 QCGEINREKEKNTQ----LKRRIEELESEVREKEMELKDLRKQSEIIPQLMSECEyvsEKLEAAERDNQNLEDKVRSLKT 299
Cdd:COG1196   324 ELAELEEELEELEEeleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE---EELEELAEELLEALRAAAELAA 400

                         170       180
                  ....*....|....*....|.
gi 1958644854 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 1958644854 139 EKASHASPADTHLKSENDKLK--IALTQSAANVKKWEIELQTLRESNARLTTALQEsaasveqwkrqfsiCRDENDRLRS 216
Cdd:COG2433   383 EELIEKELPEEEPEAEREKEHeeRELTEEEEEIRRLEEQVERLEAEVEELEAELEE--------------KDERIERLER 448

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958644854 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 1958644854 208 RDENDRLRSKIEELEEQCGEInreKEKNTQLKRRIEELESEVREKEMELK-DLRKQSEIipqlmseceyvseklEAAERD 286
Cdd:COG2433   412 EEEIRRLEEQVERLEAEVEEL---EAELEEKDERIERLERELSEARSEERrEIRKDREI---------------SRLDRE 473

                          90       100
                  ....*....|....*....|....*.
gi 1958644854 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 1958644854  150 HLKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQES---------AASVEQWKRQFSICRDENDRLRSKIEE 220
Cdd:COG4913    614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvasaEREIAELEAELERLDASSDDLAALEEQ 693

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  221 LEEQCGEINREKEKNTQLKRRIEELESEVREKEMELKDLRKQSEIIPQLmsECEYVSEKLEA--AERDNQNLEDKVR-SL 297
Cdd:COG4913    694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL--ARLELRALLEErfAAALGDAVERELReNL 771

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644854  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 1958644854 212 DRLRSKIEELEEQCGEINREKEKN----TQLKRRIEELESEVREKEMELKDLRKQ----SEIIPQLMSECEY--VSEKLE 281
Cdd:COG1579    20 DRLEHRLKELPAELAELEDELAALearlEAAKTELEDLEKEIKRLELEIEEVEARikkyEEQLGNVRNNKEYeaLQKEIE 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958644854 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 1958644854 153 SENDKLKIALTQSAANVKKweiELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQcgeINREK 232
Cdd:TIGR04523 331 SQNNKIISQLNEQISQLKK---ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQE 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854 233 EKNTQLKRRIEELESEVREKEMELKDLRKQseiIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLK 312
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIERLKET---IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481

                         170
                  ....*....|....*..
gi 1958644854 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 1958644854 190 LQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINREKEKNTQLKRRIEELESEVREKEMELKDLRKQSEIIPQL 269
Cdd:PRK03918  195 IKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE 274

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854 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 1958644854 151 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSIcrdendrLRSKIEELEEQCgeinR 230
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINV-------LQKKIENLQEQL----R 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854 231 EKEKN-TQLKRRIEELESE--------------VREKEMELKDLRKQSEiipqlmSECEYVSEKLEAAERDNQNLEDKVR 295
Cdd:pfam10174 412 DKDKQlAGLKERVKSLQTDssntdtalttleeaLSEKERIIERLKEQRE------REDRERLEELESLKKENKDLKEKVS 485


                  ....*...
gi 1958644854 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 1958644854  208 RDENDRLRSKIEELEEQCG----EINREKEKNTQLKRRIEELESEVREKEMEL----KDLRKQSEIIPQLMSECEYVSEK 279
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSslqsELRRIENRLDELSQELSDASRKIGEIEKEIeqleQEEEKLKERLEELEEDLSSLEQE 752

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  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 1958644854   79 DSRANTVFGLGFSSEQQLTKFAEKFQEVREaarLARDKSQEKIETSSNHSQASSVNGTddEKASHASPADTHLKSEndkL 158
Cdd:pfam15921  230 DTEISYLKGRIFPVEDQLEALKSESQNKIE---LLLQQHQDRIEQLISEHEVEITGLT--EKASSARSQANSIQSQ---L 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  159 KIALTQSAANVKKWEIELQTLRESNARLTTALQESAAS----VEQWKRQFSICRDE------------------NDRLRS 216
Cdd:pfam15921  302 EIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMyedkIEELEKQLVLANSEltearterdqfsqesgnlDDQLQK 381

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  217 KIEELEEQCGEINREKEKNTQLKRR-------IEELESEVREKEMELKDLRKqseIIPQLMSECE-YVSEKLEAAERDNQ 288
Cdd:pfam15921  382 LLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEA---LLKAMKSECQgQMERQMAAIQGKNE 458

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1958644854  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 1958644854 175 ELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINREKEKN------TQLKRRIEELESE 248
Cdd:COG1579    32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEalqkeiESLKRRISDLEDE 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958644854 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 1958644854 213 RLRSKIEELEEQCGEINREK--EKNTQLKRRIEELESEVREKEMELKDLRKQseiipqLMSECEYVSEKLEAAERDNQNL 290
Cdd:PRK12704   39 EAKRILEEAKKEAEAIKKEAllEAKEEIHKLRNEFEKELRERRNELQKLEKR------LLQKEENLDRKLELLEKREEEL 112

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958644854 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 1958644854 151 LKSENDKLKIALTQsAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINR 230
Cdd:PRK02224  487 LEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854 231 EKEKNTQLKRRIEELESEVREKEMELKDLRKQSEIIPQLMSECEYVSEKLEA-AERDNQNLE------DKVRSLKTDIEE 303
Cdd:PRK02224  566 EAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREAlAELNDERRErlaekrERKRELEAEFDE 645

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958644854 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 1958644854  172 WEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEqcgEINREKEKNTQLKRRIEELESEVRE 251
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE---EIEELQKELYALANEISRLEQQKQI 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  252 KEMELKDLRKQSeiipqlmsecEYVSEKLEAAERDNQNLEDKVRSLKTDIEEskyrqrhLKGELKSFLEVLDGKIDDLHD 331
Cdd:TIGR02168  307 LRERLANLERQL----------EELEAQLEELESKLDELAEELAELEEKLEE-------LKEELESLEAELEELEAELEE 369


                   ....*...
gi 1958644854  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 1958644854 174 IELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINREKEKNTQLKRRIEELESEVReKE 253
Cdd:COG1579    10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-NN 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854 254 MELKDLRKQSEIIPQLMSECEY----VSEKLEAAERDNQNLEDKVRSLKTDIEEskyrqrhLKGELKSFLEVLDGKIDDL 329
Cdd:COG1579    89 KEYEALQKEIESLKRRISDLEDeileLMERIEELEEELAELEAELAELEAELEE-------KKAELDEELAELEAELEEL 161


                  ....*....
gi 1958644854 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 1958644854 169 VKKWEIELQTLRESNAR---LTTALQESAASVEQWKRQFSICRDENDRLR---------SKIEELEEQCGEINREKEKNT 236
Cdd:COG4717    73 LKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEkllqllplyQELEALEAELAELPERLEELE 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854 237 QLKRRIEELESEVREKEMELKDLRKQSEIIPQLMSecEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELK 316
Cdd:COG4717   153 ERLEELRELEEELEELEAELAELQEELEELLEQLS--LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230


                  ..
gi 1958644854 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 1958644854  208 RDENDRLRSKIEELEEQCGEINRE-KEKNTQLKRRIEELESEVREKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERD 286
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKAlAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958644854  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 1958644854 202 RQFSICRDENDRLRSKIEELEEQCGEINREKEKNTQLKRRIEELESEVREKEMELKDLRKQSEIIPQLmseceyvsEKLE 281
Cdd:COG4717    64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY--------QELE 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958644854 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 1958644854  175 ELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLRS-----KIEELEEQCGEINREKEKNTQLKRRIEELESEV 249
Cdd:COG4913    243 ALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRAELARLEAELERLEARLDAL 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  250 REKEMELKDLRKQS--EIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEVLDGKID 327
Cdd:COG4913    322 REELDELEAQIRGNggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401


                   ....*....
gi 1958644854  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 1958644854   93 EQQLTKFAEKFQEVREAARLARDKSQEKIETSSNHSQASSVNGTDDEKASHASPADThLKSENDKLKIALTQSAANVKKW 172
Cdd:pfam12128  695 DKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKA-LETWYKRDLASLGVDPDVIAKL 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  173 EIELQTLRESNARLTTALQEsAASVEQWKR-QFSICRDEndrlrskieeLEEQCGEINRE-KEKNTQLKRRIEELESEVR 250
Cdd:pfam12128  774 KREIRTLERKIERIAVRRQE-VLRYFDWYQeTWLQRRPR----------LATQLSNIERAiSELQQQLARLIADTKLRRA 842

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  251 EKEMELKDLRKQ----SEIIPQLMSECEYVSEKLEAAerDNQNLEDKVRSLKTDIEESKYRQRHLKGELKSFLEVLDGKI 326
Cdd:pfam12128  843 KLEMERKASEKQqvrlSENLRGLRCEMSKLATLKEDA--NSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVI 920


                   ...
gi 1958644854  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 1958644854 208 RDENDRLRSKIEELEEQCGEIN---REKEKN-TQLKRRIEELESEVREKEMELKDLRKQSEIIPQLMSECEYVSEKLEAA 283
Cdd:PRK03918  171 IKEIKRRIERLEKFIKRTENIEeliKEKEKElEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESL 250

                          90       100
                  ....*....|....*....|....*....
gi 1958644854 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 1958644854 104 QEVREAARLARDKSQEKIETSSNHSQASSVNGTDDEKASHASPADTHLKSENDKLKIALTQSAANVKKWEIELQTLRESN 183
Cdd:COG1196   309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854 184 ARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINREKEKNTQLKRRIEELESEVREKEMELKDLRKQS 263
Cdd:COG1196   389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958644854 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 1958644854  147 ADTHLKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFsicrdenDRLRSKIEELEEQCG 226
Cdd:COG4913    261 AERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL-------DALREELDELEAQIR 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  227 EINREKEKntQLKRRIEELESEVREKEMELKDLRKQSEII--PQLMSECEYVSEKLEAAERDNQ------NLEDKVRSLK 298
Cdd:COG4913    334 GNGGDRLE--QLEREIERLERELEERERRRARLEALLAALglPLPASAEEFAALRAEAAALLEAleeeleALEEALAEAE 411

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1958644854  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 1958644854   92 SEQQLTKFAEKFQEVREAARLARDKSQEKIETSSnhSQASSVNGTDDEKASHASPADTHLKSENDKLKIALTQSAANVKK 171
Cdd:pfam12128  274 IASRQEERQETSAELNQLLRTLDDQWKEKRDELN--GELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPS 351

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  172 WEIELQTLRESNARLTTALQ---------------ESAASVEQWKRQFSICRDENDRLRSKIE-ELEEQCGEINREKEkn 235
Cdd:pfam12128  352 WQSELENLEERLKALTGKHQdvtakynrrrskikeQNNRDIAGIKDKLAKIREARDRQLAVAEdDLQALESELREQLE-- 429

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  236 tQLKRRIEELESEVREKEMELKDLRKQSEIIPQLM-------SECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQ 308
Cdd:pfam12128  430 -AGKLEFNEEEYRLKSRLGELKLRLNQATATPELLlqlenfdERIERAREEQEAANAEVERLQSELRQARKRRDQASEAL 508

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1958644854  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 1958644854  230 REKEKNTQLKRRIEELEsevREKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQR 309
Cdd:TIGR02169  671 SEPAELQRLRERLEGLK---RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747

                           90       100
                   ....*....|....*....|...
gi 1958644854  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 1958644854 206 ICRDEN--DRLRSKIEELEEQCGEINrekekntQLKRRIEELESEVREKEMELKDLRKQSEIIPQLMSECEYVSEKLEAA 283
Cdd:PRK03918  185 IKRTENieELIKEKEKELEEVLREIN-------EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKL 257

                          90       100
                  ....*....|....*....|....*....
gi 1958644854 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 1958644854 101 EKFQEVREAARLARDKSQEKIETSSNHSQASSVNGTDDEKASHASpadtHLKSENDKLKIALTQSAANVKKWEIElQTLR 180
Cdd:COG4717   296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELL----ELLDRIEELQELLREAEELEEELQLE-ELEQ 370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854 181 ESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINREKEKNT--QLKRRIEELESEVREKEMELKD 258
Cdd:COG4717   371 EIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELEELEEELEE 450

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958644854 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 1958644854 170 KKWEIELQTLRESNARLTTALQESAASVEQWKRQFSicRDENDRLRSKIEELEEqcgEINREKEKNTQLKRRIEELESEV 249
Cdd:PRK03918  622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELSR---ELAGLRAELEELEKRREEIKKTL 696

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958644854 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 1958644854  101 EKFQEVREAARLARDKSQEKIETSSNHSQASSVNGTDDEKASHASPADTHLKSENDKLKIALTQSAANVKKWEI-ELQTL 179
Cdd:PTZ00121  1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkKAEEE 1631

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  180 RESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINREKEKNTQLKRRIEELESEVREKEMELKDL 259
Cdd:PTZ00121  1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644854  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 1958644854 149 THLKSENDKLKIALTQSaanvkkwEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEI 228
Cdd:TIGR04523 352 TNSESENSEKQRELEEK-------QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854 229 NRE----KEKNTQLKRRIEELESEVREKEMELKDLRKQSEIIPQLMSECEYVSEK------------------LEAAERD 286
Cdd:TIGR04523 425 EKEierlKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKikqnleqkqkelkskekeLKKLNEE 504

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958644854 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 1958644854  173 EIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINRE----KEKNTQLKRRIEELESE 248
Cdd:TIGR02169  818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAlrdlESRLGDLKKERDELEAQ 897

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958644854  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 1958644854 212 DRLRSKIEELEEqcgEINR-EKEKNTQLKRRIEELESEVREKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNL 290
Cdd:COG0542   414 DELERRLEQLEI---EKEAlKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPEL 490

                          90
                  ....*....|...
gi 1958644854 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 1958644854 149 THLKSENDKLKIALtQSAANVKKWEIELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEI 228
Cdd:COG4717   112 EELREELEKLEKLL-QLLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854 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 1958644854 170 KKWEIELQTLRESNARLTtALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINREKEKNTQLKRRIEELESEV 249
Cdd:PRK03918  162 NAYKNLGEVIKEIKRRIE-RLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI 240

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958644854 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 1958644854 144 ASPADTHLKSENDKLKIALTQSAANVKkwEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEE 223
Cdd:PRK02224  171 ASDARLGVERVLSDQRGSLDQLKAQIE--EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEE 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854 224 QCGEINREKEKNTQLKRRIEELESEVREKEMELKDLRKQ----SEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKT 299
Cdd:PRK02224  249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERleelEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328

                         170       180       190
                  ....*....|....*....|....*....|
gi 1958644854 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 1958644854 224 QCGEINREKEKNTQLKRRIEELESEVREKEMELKDLRKQSEIIPQLMSEceyVSEKLEAAERDNQNLEDKVRSLKTDIEE 303
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA---LARRIRALEQELAALEAELAELEKEIAE 94

                          90
                  ....*....|....*....
gi 1958644854 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 1958644854 148 DTHLKSENDKLKIAlTQSAANVKKWEIELQTLRESnarLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGE 227
Cdd:PLN02939  176 EMRLSETDARIKLA-AQEKIHVEILEEQLEKLRNE---LLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIE 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854 228 INREKEKNTQLKRRIEELESEVREKEMEL----KDLRKQSEI-IPQLMSECEYVSEKLEAAER----------DNQNLED 292
Cdd:PLN02939  252 VAETEERVFKLEKERSLLDASLRELESKFivaqEDVSKLSPLqYDCWWEKVENLQDLLDRATNqvekaalvldQNQDLRD 331

                         170
                  ....*....|...
gi 1958644854 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 1958644854 173 EIELQTLRESNARLTTALQEsaasvEQWKRQFSIcrdenDRLRSKIEELEEQCGEINREKEKntqlKRRIEELESEVREK 252
Cdd:pfam17380 434 QREVRRLEEERAREMERVRL-----EEQERQQQV-----ERLRQQEEERKRKKLELEKEKRD----RKRAEEQRRKILEK 499

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958644854 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 1958644854   93 EQQLTKFAEKFQEVREAARLARDKSQEKIETSSNHSQASSV----NGTDDEKASHASPADTHLKSENDKLKIALTQSAAN 168
Cdd:TIGR02168  795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAterrLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854  169 VKKWEIELQTLRESNARLTTALQESAASVEQWkrqfsicRDENDRLRSKIEELEEQCGEINREKEKntqLKRRIEELESE 248
Cdd:TIGR02168  875 LEALLNERASLEEALALLRSELEELSEELREL-------ESKRSELRRELEELREKLAQLELRLEG---LEVRIDNLQER 944

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958644854  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 1958644854 208 RDENDRLRSKIEELEEqcgEINREKEKNTQLKRRIEELESEVREKEMELKD-LRKQSEIIPQLMSECEYVSEKLEAAERD 286
Cdd:pfam06785  96 QSEEERLEEELSQKEE---ELRRLTEENQQLQIQLQQISQDFAEFRLESEEqLAEKQLLINEYQQTIEEQRSVLEKRQDQ 172

                          90
                  ....*....|....*
gi 1958644854 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 1958644854 238 LKRRIEELESEVREKEMELKDLRKQSEIIPqlmseceyVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRHLKGELKS 317
Cdd:COG3206   180 LEEQLPELRKELEEAEAALEEFRQKNGLVD--------LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251


                  ....*
gi 1958644854 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 1958644854 212 DRLRSKIEELEEQCGEINREKEKNTQLKRRIEELESEVREKE-------MELKDLRKQSEIIPQLMSECEYVSEKLEAAE 284
Cdd:PRK01156  190 EKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMddynnlkSALNELSSLEDMKNRYESEIKTAESDLSMEL 269

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644854 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 1958644854 138 DEKASHASPADTHLKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSK 217
Cdd:COG4372     2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854 218 IEELEEQcgeINREKEKNTQLKRRIEELESEVREKEMELKDLRKQSEiipQLMSECEYVSEKLEAAERDNQNLEDKVRSL 297
Cdd:COG4372    82 LEELNEQ---LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ---DLEQQRKQLEAQIAELQSEIAEREEELKEL 155


                  ....*.
gi 1958644854 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 1958644854 151 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEinr 230
Cdd:PRK03918  194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE--- 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644854 231 ekekntqLKRRIEELESEVREKEmELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQRH 310
Cdd:PRK03918  271 -------LKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE 342


                  ....*.
gi 1958644854 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 1958644854 175 ELQTLRESNARLTTALQESAASVEQWKRQFSIcrDENDRLRSKIEELEEQCGEINREKEKNTQLKRRIEELESEVREKEM 254
Cdd:COG4717   157 ELRELEEELEELEAELAELQEELEELLEQLSL--ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234

                          90
                  ....*....|.
gi 1958644854 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 1958644854 151 LKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINR 230
Cdd:COG4372    50 LREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQ 129

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958644854 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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