|
Name |
Accession |
Description |
Interval |
E-value |
| NUDE_C |
pfam04880 |
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved ... |
134-297 |
2.51e-56 |
|
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved region of the NUDE proteins. NUDE proteins are involved in nuclear migration.
Pssm-ID: 461464 [Multi-domain] Cd Length: 169 Bit Score: 181.14 E-value: 2.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 134 SLEDFEQRLNQAIERNAFLESEL----DEKENLLESVQRLKDEARDLRQELAVQQKQ------EKPRTPMPSSVDAERTD 203
Cdd:pfam04880 1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKlrnllmRSPSTPSLQTLEIFDRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 204 TAVQATgsvpSTPIAHRGPSSSLNtpgTFRRGlddSTGGTPLTPAARISAlnivgDLLRKVGALESKLASCRNFVYDQSP 283
Cdd:pfam04880 81 PAVQAV----SSPVIATPPEKSFN---SLRTG---SETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNA 145
|
170
....*....|....
gi 529006528 284 GRASGPASGRGSKN 297
Cdd:pfam04880 146 SRRGNSRSLYGSRP 159
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
26-186 |
4.01e-09 |
|
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: 58.14 E-value: 4.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 26 KQRAENTQEELREFQEESREYEAELETQLQQTEsKNRDLLMENNHLRMELETIKEKFKTQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 106 -------IKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 178
Cdd:TIGR02168 818 eaanlreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
....*...
gi 529006528 179 ELAVQQKQ 186
Cdd:TIGR02168 898 ELSEELRE 905
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
11-188 |
1.76e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 11 EEEEANYWKDLAMTYKQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEGY 90
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 91 RQISALEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLK 170
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
170
....*....|....*...
gi 529006528 171 DEARDLRQELAVQQKQEK 188
Cdd:COG1196 460 ALLELLAELLEEAALLEA 477
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
26-187 |
3.16e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 26 KQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEGYRQISALEDDLAQTKA 105
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 106 IKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
..
gi 529006528 186 QE 187
Cdd:COG1196 478 AL 479
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
34-186 |
5.76e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 5.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 34 EELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETIKEKF---KTQHSEGYRQISALEDDLAQTKAIKDKL 110
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsalRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529006528 111 QKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEnllESVQRLKDEARDLRQELAVQQKQ 186
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR---AELTLLNEEAANLRERLESLERR 832
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
26-188 |
6.07e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 26 KQRAENTQEELREFQEESREYEAELEtQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEGYRQISALEDDLAQTKA 105
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELA-RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 106 IKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQ----RLKDEARDLRQELA 181
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLerleRLEEELEELEEALA 431
|
....*..
gi 529006528 182 VQQKQEK 188
Cdd:COG1196 432 ELEEEEE 438
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
24-188 |
7.99e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 7.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 24 TYKQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRM------ELETIKEKFKTQHSEGYRQISALE 97
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEllaelaRLEQDIARLEERRRELEERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 98 DDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEARDLR 177
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE---LAEAEEELEELAEELLEALRAAAELA 399
|
170
....*....|.
gi 529006528 178 QELAVQQKQEK 188
Cdd:COG1196 400 AQLEELEEAEE 410
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
27-188 |
8.74e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 8.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 27 QRAENTQEELREFQEESREYEAELET-QLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEGYRQISALEDDLAQTKA 105
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEElEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 106 IKDKLQKYIRELEQANDDLERAKR----ATIMSLEDFEQRLNQAIERNAFLESELDEKEnllESVQRLKDEARDLRQELA 181
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEqlslATEEELQDLAEELEELQQRLAELEEELEEAQ---EELEELEEELEQLENELE 237
|
....*..
gi 529006528 182 VQQKQEK 188
Cdd:COG4717 238 AAALEER 244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
26-198 |
2.73e-07 |
|
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: 51.69 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 26 KQRAENTQEELREFQEESREYEA---ELETQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEGYR--QISALE--- 97
Cdd:COG4942 47 KKEEKALLKQLAALERRIAALARrirALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRlgRQPPLAlll 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 98 --DDLAQT-------KAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQR 168
Cdd:COG4942 127 spEDFLDAvrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 529006528 169 -----------LKDEARDLRQELAVQQKQEKPRTPMPSSVD 198
Cdd:COG4942 207 elaelaaelaeLQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
26-181 |
2.76e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 26 KQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLLmENNHLRMELETIKEKFKTQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE-SLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 106 IKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLL------------ESVQRLKDEA 173
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTleeaealenkieDDEEEARRRL 974
|
....*...
gi 529006528 174 RDLRQELA 181
Cdd:TIGR02168 975 KRLENKIK 982
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-187 |
3.39e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 27 QRAENTQEELR-EFQEESREYEA------ELETQLQQTESKNRDLLMENNHLRMELETIKE---KFKTQHSEGYRQISAL 96
Cdd:COG1196 263 AELEAELEELRlELEELELELEEaqaeeyELLAELARLEQDIARLEERRRELEERLEELEEelaELEEELEELEEELEEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 97 EDDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDL 176
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
170
....*....|.
gi 529006528 177 RQELAVQQKQE 187
Cdd:COG1196 423 LEELEEALAEL 433
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
26-187 |
3.91e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 26 KQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHL------RMELETIKEKFKTQHSEGYRQISALEDD 99
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELeelaeeLLEALRAAAELAAQLEELEEAEEALLER 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 100 LAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQE 179
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
....*...
gi 529006528 180 LAVQQKQE 187
Cdd:COG1196 496 LLEAEADY 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
26-188 |
5.18e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 26 KQRAENTQEELREFQEESREYEAELET---QLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEGYRQISALEDDLAQ 102
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEaeaELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 103 TKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAV 182
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
....*.
gi 529006528 183 QQKQEK 188
Cdd:COG1196 489 AAARLL 494
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
27-188 |
8.05e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 8.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 27 QRAENTQEELREFQEESREYeAELETQLQQTESKNRDLLMENNHLRMELETIKEKfkTQHSEGYRQISALEDDLAQTKAI 106
Cdd:COG4717 71 KELKELEEELKEAEEKEEEY-AELQEELEELEEELEELEAELEELREELEKLEKL--LQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 107 KDKLQKYIRELEQANDDLERAKRAtimsLEDFEQRLNQAIERNAF-----LESELDEKENLLESVQRLKDEARDLRQELA 181
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAE----LAELQEELEELLEQLSLateeeLQDLAEELEELQQRLAELEEELEEAQEELE 223
|
....*..
gi 529006528 182 VQQKQEK 188
Cdd:COG4717 224 ELEEELE 230
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1-201 |
1.29e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 1 MADSGKTFSSEEEEANYWKDLAMTykQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLlmenNHLRMELETIKE 80
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAA--LRLWFAQRRLELLEAELEELRAELARLEAELERLEARL----DALREELDELEA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 81 kfktQHSE-GYRQISALEDDLAQTKAIKDKLQkyiRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEK 159
Cdd:COG4913 331 ----QIRGnGGDRLEQLEREIERLERELEERE---RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEAL 403
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 529006528 160 EN----LLESVQRLKDEARDLRQELAVQQKQekpRTPMPSSVDAER 201
Cdd:COG4913 404 EEalaeAEAALRDLRRELRELEAEIASLERR---KSNIPARLLALR 446
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-191 |
1.32e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 1 MADSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEESREYEA---ELETQLQQTESKNRDLLMENNHLRMELET 77
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESkrsELRRELEELREKLAQLELRLEGLEVRIDN 940
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 78 IKEKFktqhSEGYRqiSALEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQrLNqaiERNAFLESELD 157
Cdd:TIGR02168 941 LQERL----SEEYS--LTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEE-LK---ERYDFLTAQKE 1010
|
170 180 190
....*....|....*....|....*....|....*...
gi 529006528 158 E----KENLLESVQRLKDEARDLRQELAVQQKQEKPRT 191
Cdd:TIGR02168 1011 DlteaKETLEEAIEEIDREARERFKDTFDQVNENFQRV 1048
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
11-173 |
1.51e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 11 EEEEANYWKDLAMTYKQRAENTQEELREFQEESREYEA-----------------ELETQLQQTESKNRDLLMENNHLRM 73
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAalrdlesrlgdlkkerdELEAQLRELERKIEELEAQIEKKRK 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 74 ELETIKEKFKTQHSEgyrqISALEDDLAQTKAIK------DKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIE 147
Cdd:TIGR02169 918 RLSELKAKLEALEEE----LSEIEDPKGEDEEIPeeelslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKE 993
|
170 180
....*....|....*....|....*.
gi 529006528 148 RNAFLESELDEKENLLESVQRLKDEA 173
Cdd:TIGR02169 994 KRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
30-188 |
1.57e-06 |
|
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: 50.02 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 30 ENTQEELREFQEESREYEAELE---TQLQQTESKNRDLLMENNHLRMELETIK-EKFKTQHSEGYRQISALEDDLAQTKA 105
Cdd:TIGR04523 249 SNTQTQLNQLKDEQNKIKKQLSekqKELEQNNKKIKELEKQLNQLKSEISDLNnQKEQDWNKELKSELKNQEKKLEEIQN 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 106 IKDKLQKYIRELEQANDDLERakraTIMSLEDFEQRLNQAI-ERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQ 184
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKK----ELTNSESENSEKQRELeEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE 404
|
....
gi 529006528 185 KQEK 188
Cdd:TIGR04523 405 KLNQ 408
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
26-188 |
2.35e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 26 KQRAENTQEELREFQEESREyeaeLETQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEgyrqISALEDDLAQTKA 105
Cdd:COG1196 294 LAELARLEQDIARLEERRRE----LEERLEELEEELAELEEELEELEEELEELEEELEEAEEE----LEEAEAELAEAEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 106 IKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA---EEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
...
gi 529006528 186 QEK 188
Cdd:COG1196 443 ALE 445
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
27-181 |
2.60e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 27 QRAENTQEELREFQEESREYEA--------ELETQLQQTESKnrdllmennhlRMELETIKEKFKTQHSEGYRQISALED 98
Cdd:TIGR02169 204 RREREKAERYQALLKEKREYEGyellkekeALERQKEAIERQ-----------LASLEEELEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 99 DLAQ-TKAIKDK-------LQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELD-----------EK 159
Cdd:TIGR02169 273 LLEElNKKIKDLgeeeqlrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEelereieeerkRR 352
|
170 180
....*....|....*....|..
gi 529006528 160 ENLLESVQRLKDEARDLRQELA 181
Cdd:TIGR02169 353 DKLTEEYAELKEELEDLRAELE 374
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-180 |
3.04e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 27 QRAENTQEELREFQEES-----REYEAELETQLQQTESKNRDLLMENNHLRMELETIKEKfKTQHSEGYRQISALEDDLA 101
Cdd:TIGR02168 213 ERYKELKAELRELELALlvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEEL-RLEVSELEEEIEELQKELY 291
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529006528 102 QTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQEL 180
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
20-190 |
3.82e-06 |
|
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: 48.68 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 20 DLAMTYKQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSE------GYRQ- 92
Cdd:pfam12128 643 FARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREartekqAYWQv 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 93 -ISALEDDLAQTKAIKDKLQ------------KYIREL------EQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLE 153
Cdd:pfam12128 723 vEGALDAQLALLKAAIAARRsgakaelkaletWYKRDLaslgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQ 802
|
170 180 190
....*....|....*....|....*....|....*...
gi 529006528 154 SE-LDEKENLLESVQRLKDEARDLRQELAVQQKQEKPR 190
Cdd:pfam12128 803 ETwLQRRPRLATQLSNIERAISELQQQLARLIADTKLR 840
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-188 |
4.51e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 1 MADSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLlmenNHLRMELETIK- 79
Cdd:TIGR02169 711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL----HKLEEALNDLEa 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 80 --------------EKFKTQHSEGYRQISALEDDL---AQTKAIKDK----LQKYIRELE-------QANDDLERAKRAT 131
Cdd:TIGR02169 787 rlshsripeiqaelSKLEEEVSRIEARLREIEQKLnrlTLEKEYLEKeiqeLQEQRIDLKeqiksieKEIENLNGKKEEL 866
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 529006528 132 IMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEK 188
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
26-295 |
4.82e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 26 KQRAENTQEELREFQEESREYEAELEtQLQQTESKNRDLLMEnnhlrmeleTIKEKFKTQHSEGY-------RQISALED 98
Cdd:COG3883 50 NEEYNELQAELEALQAEIDKLQAEIA-EAEAEIEERREELGE---------RARALYRSGGSVSYldvllgsESFSDFLD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 99 DLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQ 178
Cdd:COG3883 120 RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 179 ELAVQQKQEKPRTPMPSSVDAERTDTAVQATGSVPSTPIAHRGPSSSLNTPGTFRRGLDDSTGGTPLTPAARISAlNIVG 258
Cdd:COG3883 200 ELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA-GAAA 278
|
250 260 270
....*....|....*....|....*....|....*..
gi 529006528 259 DLLRKVGALESKLASCRNFVYDQSPGRASGPASGRGS 295
Cdd:COG3883 279 ASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGS 315
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
19-188 |
5.02e-06 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 47.75 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 19 KDLAMTYKQRAENTQEELREFQEESREYEAELETQlqqtESKNRDLLMENN--HLRMELETIKEKFKTQHSEgyrQISAL 96
Cdd:cd22656 127 LKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETL----EKALKDLLTDEGgaIARKEIKDLQKELEKLNEE---YAAKL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 97 EDDLAQTKAIKDKLQKYIRELEQANDDLERAKratiMSLEDFEQRLNQAIE-----RNAF--LESELDEKENLLESVQRl 169
Cdd:cd22656 200 KAKIDELKALIADDEAKLAAALRLIADLTAAD----TDLDNLLALIGPAIPaleklQGAWqaIATDLDSLKDLLEDDIS- 274
|
170
....*....|....*....
gi 529006528 170 kDEARDLRQELAVQQKQEK 188
Cdd:cd22656 275 -KIPAAILAKLELEKAIEK 292
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
11-181 |
7.36e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 11 EEEEANYWKDLAMTYKQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETIKEK---FKTQHS 87
Cdd:TIGR02169 771 EEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQridLKEQIK 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 88 EGYRQISALEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQaiernafLESELDEKENLLEsvq 167
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE-------LEAQIEKKRKRLS--- 920
|
170
....*....|....
gi 529006528 168 RLKDEARDLRQELA 181
Cdd:TIGR02169 921 ELKAKLEALEEELS 934
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
12-181 |
9.93e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 12 EEEANYWKDLAMTYKQRAENTQEELREFQEESREYE---AELETQLQQTESKNRDLLMENNHLRMELETIKEKFK-TQHS 87
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAELEELEsrlEELEEQLETLRSKVAQLELQIASLNNEIERLEARLErLEDR 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 88 EGYRQISALEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQ 167
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
170
....*....|....
gi 529006528 168 RLKDEARDLRQELA 181
Cdd:TIGR02168 496 RLQENLEGFSEGVK 509
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
37-187 |
1.26e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 37 REFQEESREYEAEL--------ETQLQQTESKNRDLLMENNHLRMELETIK---EKFKTQHSEGYRQISALEDDLAQTKA 105
Cdd:COG1196 216 RELKEELKELEAELlllklrelEAELEELEAELEELEAELEELEAELAELEaelEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 106 IKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
..
gi 529006528 186 QE 187
Cdd:COG1196 376 EA 377
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
74-191 |
1.30e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 74 ELETIKEKFKTQhSEGYRQISALEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRA--TIMSLEDFEQRLNQAIERNAF 151
Cdd:COG4717 72 ELKELEEELKEA-EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERLEE 150
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 529006528 152 LESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRT 191
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT 190
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
95-186 |
2.93e-05 |
|
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: 45.53 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 95 ALEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEnllESVQRLKDEAR 174
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE---AELAELEKEIA 93
|
90
....*....|..
gi 529006528 175 DLRQELAVQQKQ 186
Cdd:COG4942 94 ELRAELEAQKEE 105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
24-181 |
4.31e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 24 TYKQRAENTQEELREFQEESREYEAELETqlqqtesknrdLLMENNHLRMELETIKEKFKTQHSEgyrqISALEDDLAQT 103
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEE-----------LRLEVSELEEEIEELQKELYALANE----ISRLEQQKQIL 307
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529006528 104 KAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELA 181
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
19-188 |
4.65e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.49 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 19 KDLAMTYKQRAENTQEEL-REFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEGYRQISALE 97
Cdd:pfam15921 244 EDQLEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 98 DDLAQtkaIKDKLQKYIRELEQANDDLEraKRATIMSLEDFEQRlnqaIERNAFLEseldEKENLLESVQRLKDEARDLR 177
Cdd:pfam15921 324 STVSQ---LRSELREAKRMYEDKIEELE--KQLVLANSELTEAR----TERDQFSQ----ESGNLDDQLQKLLADLHKRE 390
|
170
....*....|.
gi 529006528 178 QELAVQQKQEK 188
Cdd:pfam15921 391 KELSLEKEQNK 401
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
28-187 |
5.09e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.89 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 28 RAENTQEELREFQEEsreyEAELetqLQQTESKNRDLLMEnnhlRMELETIKEKFKTQHSEGYRQISALEDDLAQTKAIK 107
Cdd:pfam07888 28 RAELLQNRLEECLQE----RAEL---LQAQEAANRQREKE----KERYKRDREQWERQRRELESRVAELKEELRQSREKH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 108 DKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLEsvqRLKDEARdlrqELAVQQKQE 187
Cdd:pfam07888 97 EELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELE---RMKERAK----KAGAQRKEE 169
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
91-163 |
5.27e-05 |
|
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: 44.75 E-value: 5.27e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529006528 91 RQISALEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLL 163
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
26-187 |
6.67e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 26 KQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEgyrqISALEDDLAQTKA 105
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE----LEELEAELEELES 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 106 IKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEAR--DLRQELAVQ 183
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEleELEEELEEL 452
|
....
gi 529006528 184 QKQE 187
Cdd:TIGR02168 453 QEEL 456
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
30-185 |
7.99e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.71 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 30 ENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEGyrqiSALEDDLA-QTKAIKD 108
Cdd:pfam05483 253 ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQ----KALEEDLQiATKTICQ 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 109 KLQKYIRELEQANddleRAK----------RATIMSLEDF----EQRLNQAIERNAFLESELDEKENLLESVQRLKD--- 171
Cdd:pfam05483 329 LTEEKEAQMEELN----KAKaahsfvvtefEATTCSLEELlrteQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNnke 404
|
170
....*....|....*
gi 529006528 172 -EARDLRQELAVQQK 185
Cdd:pfam05483 405 vELEELKKILAEDEK 419
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
37-168 |
1.00e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 37 REFQEESR-----EYEAEL---ETQLQQTESKNRDLLMENNHLRMELetikekfktqhsEGYRQISALEDDLAQTKAIKD 108
Cdd:PRK03918 443 RELTEEHRkelleEYTAELkriEKELKEIEEKERKLRKELRELEKVL------------KKESELIKLKELAEQLKELEE 510
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529006528 109 KLQKY-IRELEQANDDLERAK------RATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQR 168
Cdd:PRK03918 511 KLKKYnLEELEKKAEEYEKLKekliklKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLK 577
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
26-171 |
1.96e-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: 42.22 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 26 KQRAENTQEELREFQEESREYEAELEtQLQQTESKNRDLLM------ENNHLRMELETIKekfktqhsegyRQISALEDD 99
Cdd:COG1579 44 EARLEAAKTELEDLEKEIKRLELEIE-EVEARIKKYEEQLGnvrnnkEYEALQKEIESLK-----------RRISDLEDE 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529006528 100 LAQTKAIKDKLQKYIRE----LEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDekENLLESVQRLKD 171
Cdd:COG1579 112 ILELMERIEELEEELAEleaeLAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP--PELLALYERIRK 185
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
13-186 |
2.25e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 13 EEANYWKDLAmtykqraENTQEELREFQEESREYEAELETQLQQTESKnrdLLMENNHlrmeletikekfKTQHSEGYRQ 92
Cdd:PRK04863 424 ERAKQLCGLP-------DLTADNAEDWLEEFQAKEQEATEELLSLEQK---LSVAQAA------------HSQFEQAYQL 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 93 ISALEDDLAQTKA---IKDKLQKY----------------IRELEQANDDLERAKRAtimsLEDFEQRLNQAIERNAFLE 153
Cdd:PRK04863 482 VRKIAGEVSRSEAwdvARELLRRLreqrhlaeqlqqlrmrLSELEQRLRQQQRAERL----LAEFCKRLGKNLDDEDELE 557
|
170 180 190
....*....|....*....|....*....|...
gi 529006528 154 SELDEKENLLESVQRLKDEARDLRQELAVQQKQ 186
Cdd:PRK04863 558 QLQEELEARLESLSESVSEARERRMALRQQLEQ 590
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
26-174 |
2.80e-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: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 26 KQRAENTQEELREFQEESreyeAELETQLQQTESKNRDLLMENNHLRMELETIK---EKFKTQHSEG--YRQISALEDDL 100
Cdd:COG1579 23 EHRLKELPAELAELEDEL----AALEARLEAAKTELEDLEKEIKRLELEIEEVEariKKYEEQLGNVrnNKEYEALQKEI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529006528 101 AQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEAR 174
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELA 169
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
34-189 |
3.12e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 34 EELREFQEESREyeAELETQLQQTESKNRDLLmennhlrmELETIKEKFKTQHSEGYRQISALEDDLAQTKAIKDKLQKY 113
Cdd:TIGR02168 213 ERYKELKAELRE--LELALLVLRLEELREELE--------ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEE 282
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529006528 114 IRELEQANDDLERAkratimsLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKP 189
Cdd:TIGR02168 283 IEELQKELYALANE-------ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
19-192 |
3.17e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 19 KDLAMTYKQRAENTQEELREFQEESREYEAELET------QLQQTESKNRDLLMENNHLRMELETIKEKFKTQHS---EG 89
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKlekevkELEELKEEIEELEKELESLEGSKRKLEEKIRELEErieEL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 90 YRQISALEDDLAQTKAIKDKLQKYIReLEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLES-------------EL 156
Cdd:PRK03918 272 KKEIEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeerleelkkklkEL 350
|
170 180 190
....*....|....*....|....*....|....*.
gi 529006528 157 DEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTP 192
Cdd:PRK03918 351 EKRLEELEERHELYEEAKAKKEELERLKKRLTGLTP 386
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
12-176 |
3.59e-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: 42.35 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 12 EEEANYWKDLamtyKQRAENTQEELREFQEESREYEAE----------LETQLQQTESKNRDLLMENNHLRMELETikek 81
Cdd:TIGR02168 361 EELEAELEEL----ESRLEELEEQLETLRSKVAQLELQiaslnneierLEARLERLEDRRERLQQEIEELLKKLEE---- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 82 fktqhsegyRQISALEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKEN 161
Cdd:TIGR02168 433 ---------AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
170
....*....|....*
gi 529006528 162 LLESVQRLKDEARDL 176
Cdd:TIGR02168 504 FSEGVKALLKNQSGL 518
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
25-188 |
3.99e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 25 YKQRAENTQEELREFQEESREYEAELEtQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEGYRQISALEDdlaQTK 104
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIE-RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR---SIN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 105 AIKDKLQKYIRELEQANDDLERAKRATIMS---LEDFEQRLNQAIERNAFLESELDEKENLLESvqrLKDEARDLRQEL- 180
Cdd:TIGR04523 479 KIKQNLEQKQKELKSKEKELKKLNEEKKELeekVKDLTKKISSLKEKIEKLESEKKEKESKISD---LEDELNKDDFELk 555
|
170
....*....|....
gi 529006528 181 ------AVQQKQEK 188
Cdd:TIGR04523 556 kenlekEIDEKNKE 569
|
|
| PRK03992 |
PRK03992 |
proteasome-activating nucleotidase; Provisional |
38-84 |
4.66e-04 |
|
proteasome-activating nucleotidase; Provisional
Pssm-ID: 179699 [Multi-domain] Cd Length: 389 Bit Score: 41.74 E-value: 4.66e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 529006528 38 EFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETIK---EKFKT 84
Cdd:PRK03992 1 ERLEALEERNSELEEQIRQLELKLRDLEAENEKLERELERLKselEKLKS 50
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
12-180 |
5.35e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 12 EEEANYWKDLAMTYKQRAENTQEELREFQEEsreyEAELETQLQQTEsKNRDLLMENNHLRMELETIKEKFKTQH----- 86
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAELNSK----LAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAelnde 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 87 -----SEGYRQISALEDD-----LAQTKAIKDKLQKYIRELEQANDDLERAK---RATIMSLEDFEQRLNQAIERNAFLE 153
Cdd:PRK02224 625 rrerlAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERddlQAEIGAVENELEELEELRERREALE 704
|
170 180
....*....|....*....|....*..
gi 529006528 154 SELDEKENLLESVQRLKDEARDLRQEL 180
Cdd:PRK02224 705 NRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| PilN |
COG3166 |
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures]; |
138-193 |
5.37e-04 |
|
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];
Pssm-ID: 442399 [Multi-domain] Cd Length: 185 Bit Score: 40.34 E-value: 5.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 529006528 138 FEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTPM 193
Cdd:COG3166 43 LQGQIAQQQARNAALQQEIAKLDKQIAEIKELKKQKAELLARLQVIEQLQQSRPPW 98
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
11-173 |
5.53e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.87 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 11 EEEEANYWKDLAMTYKQRAENTQE-------ELREFQEESREYEAELETQLQQTESKNRDLLME----NNHLRMELETIK 79
Cdd:COG5185 281 NENANNLIKQFENTKEKIAEYTKSidikkatESLEEQLAAAEAEQELEESKRETETGIQNLTAEieqgQESLTENLEAIK 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 80 EKFKtqHSEGYRQISALEDDLaqtKAIKDKLQKYIRELEQANDDlerAKRATIMSLEDFEQRLNQAIERNAFLESELDEK 159
Cdd:COG5185 361 EEIE--NIVGEVELSKSSEEL---DSFKDTIESTKESLDEIPQN---QRGYAQEILATLEDTLKAADRQIEELQRQIEQA 432
|
170
....*....|....
gi 529006528 160 ENLLESVQRLKDEA 173
Cdd:COG5185 433 TSSNEEVSKLLNEL 446
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
21-190 |
7.00e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 21 LAMTYKQRAENTQEELREFQEESREYEAELE---TQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEgyrqISALE 97
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEqarEELEQLEEELEQARSELEQLEEELEELNEQLQAAQAE----LAQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 98 DDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQR--LKDEARD 175
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQelQALSEAE 180
|
170
....*....|....*
gi 529006528 176 LRQELAVQQKQEKPR 190
Cdd:COG4372 181 AEQALDELLKEANRN 195
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
10-185 |
7.27e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 10 SEEEEanywKDLAMTYKQRAENTQEELREFQEESREYEAE---LETQLQQTE--SKNRDLLMENNHLRMELETIKEKFKT 84
Cdd:PRK03918 446 TEEHR----KELLEEYTAELKRIEKELKEIEEKERKLRKElreLEKVLKKESelIKLKELAEQLKELEEKLKKYNLEELE 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 85 QHSEGYR-----------QISALEDDLAQTKAIKDKLQKYIRELEQANDDLE----RAKRATIMSLEDFE---QRLNQAI 146
Cdd:PRK03918 522 KKAEEYEklkekliklkgEIKSLKKELEKLEELKKKLAELEKKLDELEEELAellkELEELGFESVEELEerlKELEPFY 601
|
170 180 190
....*....|....*....|....*....|....*....
gi 529006528 147 ERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:PRK03918 602 NEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEK 640
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
39-234 |
7.85e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.87 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 39 FQEESREYEA---ELETQLQQTESKnrdllmennhlRMELETIKEKFKTQHSEGYRQISALEDDLAQTKAIKDKLQKYIR 115
Cdd:pfam00529 49 FQLDPTDYQAaldSAEAQLAKAQAQ-----------VARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 116 ELEQANDDLERAK-RATI--MSLEDF-EQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQekprt 191
Cdd:pfam00529 118 QLAQAQIDLARRRvLAPIggISRESLvTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQ----- 192
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 529006528 192 pmPSSVDAERTDTAVQATGSVPSTPIAHRGPSSSLNTPGTFRR 234
Cdd:pfam00529 193 --IAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVDGGTVS 233
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
25-186 |
9.86e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 9.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 25 YKQRAENTQEELREFQEESREYE------AELETQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEgYRQISALED 98
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEkfikrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKE-VKELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 99 DLAQTKAIKDKLQKYIRELEQANDDLER---AKRATIMSLEDFEQRLNQaIERNAFLESELDE-KENLLESVQRLKDEAR 174
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEErieELKKEIEELEEKVKELKE-LKEKAEEYIKLSEfYEEYLDELREIEKRLS 317
|
170
....*....|..
gi 529006528 175 DLRQELAVQQKQ 186
Cdd:PRK03918 318 RLEEEINGIEER 329
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
6-197 |
1.09e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.22 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 6 KTFSSEEEEAnywkdLAMTYKQRAENTQEELREFQEESREYeaeleTQLQQTESKNRDLLMENNHLRMELETIKEKFKTQ 85
Cdd:COG5022 859 KRFSLLKKET-----IYLQSAQRVELAERQLQELKIDVKSI-----SSLKLVNLELESEIIELKKSLSSDLIENLEFKTE 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 86 HSEGY------RQISALEDDLAQTKAIKDKLQKYIRELEQANDDLERAkratIMSLEDFEQRLNQAIERNAFLESELDEK 159
Cdd:COG5022 929 LIARLkkllnnIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDL----LKKSTILVREGNKANSELKNFKKELAEL 1004
|
170 180 190
....*....|....*....|....*....|....*...
gi 529006528 160 ENLLESVQRLKDEARDLRQELAVQQKQEKPRTPMPSSV 197
Cdd:COG5022 1005 SKQYGALQESTKQLKELPVEVAELQSASKIISSESTEL 1042
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
21-188 |
1.12e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 21 LAMTYKQRA-ENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETIKE-KFKTQhsegyRQISALED 98
Cdd:pfam01576 485 LNLSTRLRQlEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEgKKRLQ-----RELEALTQ 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 99 DLAQTKAIKDKLQKYIRELEQANDDLERA---KRATIMSLEDFEQRLNQ--AIERNAFL---------ESELDEKENLLE 164
Cdd:pfam01576 560 QLEEKAAAYDKLEKTKNRLQQELDDLLVDldhQRQLVSNLEKKQKKFDQmlAEEKAISAryaeerdraEAEAREKETRAL 639
|
170 180
....*....|....*....|....
gi 529006528 165 SVQRLKDEARDLRQELAVQQKQEK 188
Cdd:pfam01576 640 SLARALEEALEAKEELERTNKQLR 663
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
91-190 |
1.25e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.71 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 91 RQISALEDDLAQTKAIKDKLqkyiRELEQANDDLERAKRatimSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLK 170
Cdd:COG3096 502 RRYRSQQALAQRLQQLRAQL----AELEQRLRQQQNAER----LLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQA 573
|
90 100
....*....|....*....|
gi 529006528 171 DEARDLRQELAVQQKQEKPR 190
Cdd:COG3096 574 AEAVEQRSELRQQLEQLRAR 593
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
19-187 |
1.26e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.86 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 19 KDLAMTYKQRAENTQEELREFQEESREYEAELETQLQQTESKNRDL------LMENNHL---RMELETIKEKFKTQHSEG 89
Cdd:pfam05483 362 EELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELeelkkiLAEDEKLldeKKQFEKIAEELKGKEQEL 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 90 YRQISALEDDL----AQTKAIKDKLQKYIRELEQANDDLERAKRATI--------MSLEDFE------------QRLNQA 145
Cdd:pfam05483 442 IFLLQAREKEIhdleIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIeltahcdkLLLENKEltqeasdmtlelKKHQED 521
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 529006528 146 IERNAFLESE-LDEKENLLESVQRLKDEARDLRQELaVQQKQE 187
Cdd:pfam05483 522 IINCKKQEERmLKQIENLEEKEMNLRDELESVREEF-IQKGDE 563
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
26-181 |
1.36e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 26 KQRAENTQEELREFQEESREYEAELETQLQQTESKnRDLLMENNHLRMEL-ETIKEkFKTQHSEGYRQISALEDDLAQTK 104
Cdd:COG1340 21 REEIEELKEKRDELNEELKELAEKRDELNAQVKEL-REEAQELREKRDELnEKVKE-LKEERDELNEKLNELREELDELR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 105 AIKDKLQKY---IRELEQANDDLERAKRATIMSLEDfEQRLNQAIERnafLESELDEKE----------NLLESVQRLKD 171
Cdd:COG1340 99 KELAELNKAggsIDKLRKEIERLEWRQQTEVLSPEE-EKELVEKIKE---LEKELEKAKkalekneklkELRAELKELRK 174
|
170
....*....|
gi 529006528 172 EARDLRQELA 181
Cdd:COG1340 175 EAEEIHKKIK 184
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-176 |
1.45e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 27 QRAENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSEGYRQISALEDDLAQTKAI 106
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529006528 107 KDKLQKYIRELEQANDDLE----RAkratimsLEDFEqrlnQAIERNAFLESELD----EKENLLESVQRLKDEARDL 176
Cdd:COG1196 762 LEELERELERLEREIEALGpvnlLA-------IEEYE----ELEERYDFLSEQREdleeARETLEEAIEEIDRETRER 828
|
|
| PRK13922 |
PRK13922 |
rod shape-determining protein MreC; Provisional |
142-204 |
1.69e-03 |
|
rod shape-determining protein MreC; Provisional
Pssm-ID: 237560 Cd Length: 276 Bit Score: 39.58 E-value: 1.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529006528 142 LNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVqqKQEKPRTPMPSSVDAERTDT 204
Cdd:PRK13922 71 LFDLREENEELKKELLELESRLQELEQLEAENARLRELLNL--KESLDYQFITARVISRSPDP 131
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
12-186 |
2.29e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 12 EEEANYWKDLAMTYKQRAENTQEELREFQEESREYEAELET----------QLQQTESKNRDLLMENNHLRMELETIKEK 81
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEElrerfgdapvDLGNAEDFLEELREERDELREREAELEAT 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 82 FKT---------------------QHSEGYRQISALEDDLAQTKAIKDKLQKYIRELEQANDDLERAKratimSLEDFEQ 140
Cdd:PRK02224 435 LRTarerveeaealleagkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-----DLVEAED 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 529006528 141 RLNQAIERNAFLESELDEKENLLES----VQRLKDEARDLRQELAVQQKQ 186
Cdd:PRK02224 510 RIERLEERREDLEELIAERRETIEEkrerAEELRERAAELEAEAEEKREA 559
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
30-185 |
2.32e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 30 ENTQEELREFQEESREYEAELETQLQQTESKNRDLLmENNHLRMELETIKEKFKTQHSEgyrqISALEDDLAQTKAIKDK 109
Cdd:PRK03918 570 EELAELLKELEELGFESVEELEERLKELEPFYNEYL-ELKDAEKELEREEKELKKLEEE----LDKAFEELAETEKRLEE 644
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529006528 110 LQKYIRELEQANDDLE-RAKRATIMSLEDFEQRLNQAIERnafLESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:PRK03918 645 LRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEE---LEKRREEIKKTLEKLKEELEEREKAKKELEKLEK 718
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
33-196 |
2.37e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 33 QEELREFQEESREYEAELEtQLQQTESKNRDLLMENNHLRMELETIKEKFKTQhsegyRQISALE----------DDLAQ 102
Cdd:COG4913 616 EAELAELEEELAEAEERLE-ALEAELDALQERREALQRLAEYSWDEIDVASAE-----REIAELEaelerldassDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 103 TKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIER--------NAFLESELDEK--------------E 160
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleaaedlaRLELRALLEERfaaalgdaverelrE 769
|
170 180 190
....*....|....*....|....*....|....*.
gi 529006528 161 NLLESVQRLKDEARDLRQELAVQQKQEKPRTPMPSS 196
Cdd:COG4913 770 NLEERIDALRARLNRAEEELERAMRAFNREWPAETA 805
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
22-172 |
2.47e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 22 AMTYKQRAE-NTQEEL----REFQEESREYEAEL---ETQLQQTESKNRDLLMENNHLRMELETIKEkfktqhsegyrQI 93
Cdd:PRK12704 51 AEAIKKEALlEAKEEIhklrNEFEKELRERRNELqklEKRLLQKEENLDRKLELLEKREEELEKKEK-----------EL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 94 SALEDDLAQTKA-IKDKLQKYIRELEQ-ANDDLERAKRATIMSLEDfEQRLNQA-----IERNAFLESELDEKENLLESV 166
Cdd:PRK12704 120 EQKQQELEKKEEeLEELIEEQLQELERiSGLTAEEAKEILLEKVEE-EARHEAAvlikeIEEEAKEEADKKAKEILAQAI 198
|
....*.
gi 529006528 167 QRLKDE 172
Cdd:PRK12704 199 QRCAAD 204
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
91-186 |
2.90e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 91 RQISALEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRAtimsLEDFEQRLNQAIERNAfLESELDEKENLLES----- 165
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREA----LQRLAEYSWDEIDVAS-AEREIAELEAELERldass 684
|
90 100
....*....|....*....|...
gi 529006528 166 --VQRLKDEARDLRQELAVQQKQ 186
Cdd:COG4913 685 ddLAALEEQLEELEAELEELEEE 707
|
|
| PRK14160 |
PRK14160 |
heat shock protein GrpE; Provisional |
1-188 |
3.45e-03 |
|
heat shock protein GrpE; Provisional
Pssm-ID: 237629 [Multi-domain] Cd Length: 211 Bit Score: 38.20 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 1 MADSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEE--SREYEAELETQLQQTESKNRDLLMENNHLRMELETI 78
Cdd:PRK14160 1 MEKECKDAKHENMEEDCCKENENKEEDKGKEEDLEFEEIEKEeiIEDSEESNEVKIEELKDENNKLKEENKKLENELEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 79 KEKFK--TQHSEGYRQISALEDDLAQTKAIKDKLQKYIRELeqanDDLERAKrATIMSLEDFEQRLNQAIE--RNAF--- 151
Cdd:PRK14160 81 KDRLLrtVAEYDNYRKRTAKEKEGIYSDACEDVLKELLPVL----DNLERAA-AVEGSVEDLKKGIEMTVKqfKTSLekl 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 529006528 152 ----LESELDEKENLLESVQRLKDEARDLRQELAVQQKQEK 188
Cdd:PRK14160 156 gveeISTEGEFDPNLHNAVMHVEDENYGENEIVEVFQKGYK 196
|
|
| PRKG1_interact |
pfam15898 |
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ... |
97-176 |
3.56e-03 |
|
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of protein phosphatase 1 regulatory subunits 12A, 12B and 12C. In protein phosphatase 1 regulatory subunit 12A it has been found to bind to cGMP-dependent protein kinase 1 via a leucine zipper motif located at the C-terminus of this domain.
Pssm-ID: 464927 [Multi-domain] Cd Length: 102 Bit Score: 36.51 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 97 EDDLAQTKAIKDKLQKYIRELEQANDDLERA---------KRATIMSLEDFEQRlnqAIERNAF-LESELDEKENLLESV 166
Cdd:pfam15898 7 EEELQENERLKRKLQDAQQELAELKSQLERLtqqrqesfsDRSSLLETEKREKR---ALERKISeMEEELKVLEDLRAEN 83
|
90
....*....|
gi 529006528 167 QRLKDEARDL 176
Cdd:pfam15898 84 QRLKDENGAL 93
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
34-186 |
4.38e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 38.46 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 34 EELREFQEESREYEAELETQLQQTE----------SKNRDLLMEN------NHLRME------------LETIKEKFKTQ 85
Cdd:smart00787 73 KELKKYISEGRDLFKEIEEETLINNpplfkeyfsaSPDVKLLMDKqfqlvkTFARLEakkmwyewrmklLEGLKEGLDEN 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 86 HS---EGYRQISA----LEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSL-EDFEQRLNQAIERNAFLESELD 157
Cdd:smart00787 153 LEglkEDYKLLMKelelLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAkEKLKKLLQEIMIKVKKLEELEE 232
|
170 180
....*....|....*....|....*....
gi 529006528 158 EKENLLESVQRLKDEARDLRQELAVQQKQ 186
Cdd:smart00787 233 ELQELESKIEDLTNKKSELNTEIAEAEKK 261
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
26-186 |
4.66e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 38.84 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 26 KQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLLMENNHLRMELETikekfktqhSEGYRQISALEDDLAQTKA 105
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEA---------KLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 106 IKDKLQKYIRELEQANDDLERAKRATIMSledfeQRLNQAIERNAFLESELDEKENLL----ESVQRLKDEARDLRQELA 181
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQS-----PVIQQLRAQLAELEAELAELSARYtpnhPDVIALRAQIAALRAQLQ 308
|
....*
gi 529006528 182 VQQKQ 186
Cdd:COG3206 309 QEAQR 313
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
26-180 |
4.84e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.00 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 26 KQRAENTQEELREFQEESREYEAELETQLQQTESKNRDLL----------MENNHLRMELETIKEKFKTQHSEGYRQISA 95
Cdd:pfam01576 351 RQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQaelrtlqqakQDSEHKRKKLEGQLQELQARLSESERQRAE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 96 LEDdlaqtkaikdKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARD 175
Cdd:pfam01576 431 LAE----------KLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNS 500
|
....*
gi 529006528 176 LRQEL 180
Cdd:pfam01576 501 LQEQL 505
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
8-174 |
4.98e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 8 FSSEEEEANYWKDLAMTYKQ--RAENTQEELREFQEESREYEAELETQLQQTESKNRDLLMennhLRMELETIKEKF-KT 84
Cdd:PRK03918 584 FESVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEE----LRKELEELEKKYsEE 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 85 QHSEGYRQISALEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRAtimsledfeqrLNQAIERNAFLESELDEKENLLE 164
Cdd:PRK03918 660 EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE-----------REKAKKELEKLEKALERVEELRE 728
|
170
....*....|
gi 529006528 165 SVQRLKDEAR 174
Cdd:PRK03918 729 KVKKYKALLK 738
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
12-203 |
5.87e-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: 38.46 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 12 EEEANYWKDLamtyKQRAENTQEELREFQEESREYE---AELETQLQQTESKNRDLLMENNHLRMELETIKEKFKTQHSE 88
Cdd:TIGR04523 303 QKEQDWNKEL----KSELKNQEKKLEEIQNQISQNNkiiSQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 89 --GYR--------QISALEDDLAQTKAIKDKLQKYIRELEQANDDLERakraTIMSLEDFEQRLNQAIERnafLESELDE 158
Cdd:TIGR04523 379 nqSYKqeiknlesQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK----EIERLKETIIKNNSEIKD---LTNQDSV 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 529006528 159 KENLLESVQRLKD-----------EARDLRQELAVQQKQEKPRTPMPSSVDAERTD 203
Cdd:TIGR04523 452 KELIIKNLDNTREsletqlkvlsrSINKIKQNLEQKQKELKSKEKELKKLNEEKKE 507
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
27-186 |
6.17e-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: 38.21 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 27 QRAENTQEELREFQEEsreyEAELETQLQQTESKNRDLLMENNHLRmeletikekfktqhsegyRQISALEDDLAQTKAI 106
Cdd:COG4942 20 DAAAEAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALE------------------RRIAALARRIRALEQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 107 KDKLQKYIRELEQANDDLER---AKRATIMSLEDFEQRL---------------NQAIERNAFLESELDEKENLLESVQR 168
Cdd:COG4942 78 LAALEAELAELEKEIAELRAeleAQKEELAELLRALYRLgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRA 157
|
170
....*....|....*...
gi 529006528 169 LKDEARDLRQELAVQQKQ 186
Cdd:COG4942 158 DLAELAALRAELEAERAE 175
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
10-179 |
6.75e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 38.40 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 10 SEEEEANYWKDLAMTYKQRaENTQEELREFQEESREYE--AELETQLQQTESKNRDL----LMENNHLRMELETIKEKFK 83
Cdd:COG5185 210 SETGNLGSESTLLEKAKEI-INIEEALKGFQDPESELEdlAQTSDKLEKLVEQNTDLrlekLGENAESSKRLNENANNLI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 84 TQHSEGYRQISALEDDLAQTKAIkDKLQKYIRELEqANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLL 163
Cdd:COG5185 289 KQFENTKEKIAEYTKSIDIKKAT-ESLEEQLAAAE-AEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENI 366
|
170
....*....|....*.
gi 529006528 164 ESVQRLKDEARDLRQE 179
Cdd:COG5185 367 VGEVELSKSSEELDSF 382
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
31-173 |
7.10e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 37.32 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 31 NTQEELREFQEEsreyEAELETQLQQTESKNRDLLMENNHLRmeletikekfktqhsegyRQISALEDDLAQTKAIKDKL 110
Cdd:pfam00261 5 QIKEELDEAEER----LKEAMKKLEEAEKRAEKAEAEVAALN------------------RRIQLLEEELERTEERLAEA 62
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529006528 111 QKYIRELEQANDDLERAKRAtimsledFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEA 173
Cdd:pfam00261 63 LEKLEEAEKAADESERGRKV-------LENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEV 118
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
66-180 |
8.12e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 37.69 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 66 MENNHLRMELETIKEKFKTQHSEGYRQIS--ALEDDLAQTKAIKDKLqkyIRELEQANDDLERAKRATIMSLE----DFE 139
Cdd:PRK06669 33 KEKERLREEEEEQVEQLREEANDEAKEIIeeAEEDAFEIVEAAEEEA---KEELLKKTDEASSIIEKLQMQIEreqeEWE 109
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 529006528 140 QRLNQAIER---NAFLESELDEKENLLESVQRLKDEARDLRQEL 180
Cdd:PRK06669 110 EELERLIEEakaEGYEEGYEKGREEGLEEVRELIEQLNKIIEKL 153
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
6-181 |
9.55e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.10 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 6 KTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEESREYEAELEtQLQQTESknrdllmennhlrmELETIKEKFKTQ 85
Cdd:PRK02224 216 AELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIE-DLRETIA--------------ETEREREELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 86 HSEGYRQISALEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEdfEQRLnQAIERNAFLESELDEKENLLES 165
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLE--ECRV-AAQAHNEEAESLREDADDLEER 357
|
170
....*....|....*.
gi 529006528 166 VQRLKDEARDLRQELA 181
Cdd:PRK02224 358 AEELREEAAELESELE 373
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
11-185 |
9.61e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 37.78 E-value: 9.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 11 EEEEANYWKDLAMTYKQRAENTQEELREFQEESREYEAELE-------TQLQQTESKNRDLLMENNHLRMELETIKEKFK 83
Cdd:pfam05483 86 EAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQfenekvsLKLEEEIQENKDLIKENNATRHLCNLLKETCA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 84 TQHSEGYRQISALEDDLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSL-----------EDFEQRLNQAIERNAFL 152
Cdd:pfam05483 166 RSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLkedhekiqhleEEYKKEINDKEKQVSLL 245
|
170 180 190
....*....|....*....|....*....|...
gi 529006528 153 ESELDEKENLLESVQRLKDEARDLRQELAVQQK 185
Cdd:pfam05483 246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTK 278
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
24-186 |
9.72e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.10 E-value: 9.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 24 TYKQRAENTQEELREFQEESREYEAELETQLQQTESKN-RDLLMENNHLRMELETIKEKFKTQHSEGYRQISALED---- 98
Cdd:PRK02224 166 EYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDlHERLNGLESELAELDEEIERYEEQREQARETRDEADEvlee 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 99 ------DLAQTKAIKDKLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDE 172
Cdd:PRK02224 246 heerreELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE 325
|
170
....*....|....
gi 529006528 173 ARDLRQELAVQQKQ 186
Cdd:PRK02224 326 LRDRLEECRVAAQA 339
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
53-188 |
9.96e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 37.21 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006528 53 QLQQTESKNRDLLMENNHLRMELETIKEkfktqhsegyrQISALEDDLAQTKAIKDKLQKYIRELEQANDDLE-RAKRA- 130
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELED-----------ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEaRIKKYe 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 529006528 131 ----TIMS---LEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEK 188
Cdd:COG1579 80 eqlgNVRNnkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK 144
|
|
| |
