|
Name |
Accession |
Description |
Interval |
E-value |
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
79-353 |
2.17e-156 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 439.91 E-value: 2.17e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 79 FARSKRGLRLKTVDSCFQDLKESRLVEDTFTIDEVSEVLNGLQAVVHSEVESELINTAYTNVLLLRQLFAQAEKWYLKLQ 158
Cdd:pfam15294 1 FARYKRGQRLKTVDSCFQDLKDSRLVEDTYTIDEVTEMLDGLQTVVRGEVESELINTSHTNVLLLRQLFSQAEKWHLKLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 159 TDISELENRELLEQVAEFEKAEITSSNKKPILDVTKPKLAPLNEGGTAELLNKEILRLQEENEKLKSRLKTIEIQATNAL 238
Cdd:pfam15294 81 ADISELENRELLEQIAEFEEREFTSSNKKPNFELNKPKLEPLNEGGGSALLHMEIERLKEENEKLKERLKTLESQATQAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 239 DEKSKLEKALQDLQLDQGNQKDFIK-AQDLSNLENTVAALKSEFQKTLNDKTENQKSLEENLATAKHDLLRVQEQLHMAE 317
Cdd:pfam15294 161 DEKSKLEKALKDLQKEQGAKKDVKSnLKEISDLEEKMAALKSDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLEMAE 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 2462590678 318 KELEKKFQQTAAYRNMKEILTKKNDQIKDLRKRLAQ 353
Cdd:pfam15294 241 KELEKKFQQTAAYRNMKEMLTKKNEQIKELRKRLSK 276
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
165-350 |
1.59e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 165 ENRELLEQVAEFEKAEITSSNKKPILDVTKPKLAPLNEGGTAELLNKEILRLQEENEKLKSRLKTIEIQATNALDEKSKL 244
Cdd:COG4913 249 EQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 245 EKALQDlqlDQGNQKDFIKAQdLSNLENTVAALK---SEFQKTLND----KTENQKSLEENLATAKHDLLRVQEQLHMAE 317
Cdd:COG4913 329 EAQIRG---NGGDRLEQLERE-IERLERELEERErrrARLEALLAAlglpLPASAEEFAALRAEAAALLEALEEELEALE 404
|
170 180 190
....*....|....*....|....*....|...
gi 2462590678 318 KELekkFQQTAAYRNMKEILTKKNDQIKDLRKR 350
Cdd:COG4913 405 EAL---AEAEAALRDLRRELRELEAEIASLERR 434
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
209-353 |
3.90e-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: 48.90 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 209 LNKEILRLQEENEKLKSRLKTIEIQATNALDEKSKLEKALQDLQLDQGN----------QKDFIKAQdLSNLENTVAALK 278
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAlaneisrleqQKQILRER-LANLERQLEELE 322
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462590678 279 SEFQKTLNDKTEnqksLEENLATAKHDLLRVQEQLHMAEKELEKKfqqTAAYRNMKEILTKKNDQIKDLRKRLAQ 353
Cdd:TIGR02168 323 AQLEELESKLDE----LAEELAELEEKLEELKEELESLEAELEEL---EAELEELESRLEELEEQLETLRSKVAQ 390
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
209-355 |
1.66e-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: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 209 LNKEILRLQEENEKLKSRLKTIEIQAT--NALDEKS-------KLEKALQDLQ-----LDQGNQkdfikaqDLSNLENTV 274
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREalQRLAEYSwdeidvaSAEREIAELEaelerLDASSD-------DLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 275 AALKSEFQ---KTLNDKTENQKSLEENLATAKHDLLRVQEQLHMAEK--------ELEKKFQQTAAYRNMKEILTKKNDQ 343
Cdd:COG4913 695 EELEAELEeleEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlarlelraLLEERFAAALGDAVERELRENLEER 774
|
170
....*....|..
gi 2462590678 344 IKDLRKRLAQYE 355
Cdd:COG4913 775 IDALRARLNRAE 786
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
112-347 |
1.91e-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: 46.59 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 112 EVSEVLNGLQAVVHSEveSELINTAYTNVLLLRQLFAQAEKWYLKLQTDISELENReLLEQVAEFEKAEITSSNKKPILD 191
Cdd:TIGR02168 278 ELEEEIEELQKELYAL--ANEISRLEQQKQILRERLANLERQLEELEAQLEELESK-LDELAEELAELEEKLEELKEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 192 VTKPKLAPLNEggTAELLNKEILRLQEENEKLKSRLKTIEIQATNALDEKSKLEKALQDLQLDQGNQKDFIKAQDLSNLE 271
Cdd:TIGR02168 355 SLEAELEELEA--ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462590678 272 NTVAALKSEF---QKTLNDKTENQKSLEENLATAKHDLLRVQEQLHMAEKELEKKFQQTAAYRNMKEILTKKNDQIKDL 347
Cdd:TIGR02168 433 AELKELQAELeelEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL 511
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-351 |
1.96e-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: 46.59 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 110 IDEVSEVLNGLQAVVHsEVESELiNTAYTNVLLLRQLFAQAEKWYLKLQTDISELEnrellEQVAEFEKAEITSSNKKPI 189
Cdd:TIGR02168 679 IEELEEKIEELEEKIA-ELEKAL-AELRKELEELEEELEQLRKELEELSRQISALR-----KDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 190 LDVTKPKLAPLNEGGTAEL--LNKEILRLQEENEKLKSRLKTIEIQATNALDEKSKLEKALQDLQLDQGNQkdfikAQDL 267
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLeeAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL-----RERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 268 SNLENTVAALksefQKTLNDKTENQKSLEENLATAKHDLLRVQEQLHMAEKELEK----KFQQTAAYRNMKEILTKKNDQ 343
Cdd:TIGR02168 827 ESLERRIAAT----ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllneRASLEEALALLRSELEELSEE 902
|
....*...
gi 2462590678 344 IKDLRKRL 351
Cdd:TIGR02168 903 LRELESKR 910
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
209-355 |
6.67e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 209 LNKEILRLQEENEKLKSRLKTIEIQATNALDEKSKLEKALQDLQL----DQGNQKDFIKAQDLSNLENTVAALKSEfQKT 284
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArikkYEEQLGNVRNNKEYEALQKEIESLKRR-ISD 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462590678 285 LNDK----TENQKSLEENLATAKHDLLRVQEQLHMAEKELEKKFQQTAAyrNMKEILTKKNDQIKDLRKRL-AQYE 355
Cdd:COG1579 108 LEDEilelMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA--ELEELEAEREELAAKIPPELlALYE 181
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
143-326 |
1.38e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 143 LRQLFAQAEKWYLKLQTDISELENR-ELLEQVAEFEKAEI-TSSNKKPILDVTKpKLAPLNEGgtaellNKEILRLQEEN 220
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERrEALQRLAEYSWDEIdVASAEREIAELEA-ELERLDAS------SDDLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 221 EKLKSRLKTIEIQATNALDEKSKLEKALQDLQLDQGNQKDFIKAQDLSNLENTVAALKSEFQKTLNDKTENQ--KSLEEN 298
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERElrENLEER 774
|
170 180
....*....|....*....|....*...
gi 2462590678 299 LATAkhdllrvQEQLHMAEKELEKKFQQ 326
Cdd:COG4913 775 IDAL-------RARLNRAEEELERAMRA 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
206-353 |
2.76e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 206 AELLNKEILRLQEENEKLKSRLKTIEIQATNALDEKSKLEKALQ---------DLQLDQGNQKDFIKAQDLSNLENTVAA 276
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEelrleleelELELEEAQAEEYELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 277 LK---SEFQKTLNDKTENQKSLEENLATAKHDLLRVQEQLHMAEKELE----KKFQQTAAYRNMKEILTKKNDQIKDLRK 349
Cdd:COG1196 307 LEerrRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEeaeaELAEAEEALLEAEAELAEAEEELEELAE 386
|
....
gi 2462590678 350 RLAQ 353
Cdd:COG1196 387 ELLE 390
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
209-357 |
5.51e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 209 LNKEILRLQEENEKLKSRLKTIEIQATNALDEKSKLEKALQDLQLD----------QGNQKDFI----KAQDLSNLENTV 274
Cdd:COG3883 42 LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgeraralyrSGGSVSYLdvllGSESFSDFLDRL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 275 AALkSEFQKTLNDKTENQKSLEENLATAKHDLLRVQEQLHMAEKELEKKFQQTAAYRN-MKEILTKKNDQIKDLRKRLAQ 353
Cdd:COG3883 122 SAL-SKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAeQEALLAQLSAEEAAAEAQLAE 200
|
....
gi 2462590678 354 YEPE 357
Cdd:COG3883 201 LEAE 204
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
139-353 |
7.97e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 139 NVLLLRQLFAQAEKWYLKLQTDISELENRELLEQVAEFEKAEITSSNKkpildvtkpklaplneggtAELLNKEILRLQE 218
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE-------------------LEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 219 ENEKLKSRLKTIEIQATNALDEKSKLEKALQDLQLDQGNQKDfiKAQDLSNLENTVAALKSEFQKTLNDKTENQKSLEEN 298
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE--ELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462590678 299 LATAKHDLLRVQEQLHMAEKELEKKFQQTAAYRNMKEILTKKNDQIKDLRKRLAQ 353
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
167-357 |
8.40e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 167 RELLEQVAEFEKAEI-TSSNKKPILDVTKPKLApLNEGGTAELLNKEILRLQEENEKLKSRLKTIEIQATNALDEKSKLE 245
Cdd:COG4717 44 RAMLLERLEKEADELfKPQGRKPELNLKELKEL-EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 246 KALQDLQLDQGNQKdfIKAQdLSNLENTVAALKSEFQkTLNDKTENQKSLEENLATAKHDLLRVQEQLHMAEKELEKKFQ 325
Cdd:COG4717 123 KLLQLLPLYQELEA--LEAE-LAELPERLEELEERLE-ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA 198
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462590678 326 QT-----AAYRNMKEILTKKNDQIKDLRKRLAQYEPE 357
Cdd:COG4717 199 EEleelqQRLAELEEELEEAQEELEELEEELEQLENE 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
209-358 |
1.65e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 209 LNKEILRLQEENEKLKSRLKTIEIQATNALDEKSKLEKALQDLQLDQGNQKDFIKaqdLSNLENTVAALKSEFQKTLNDK 288
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK---LSEFYEEYLDELREIEKRLSRL 319
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 289 TENQKSLEENLATAKHDLLRVQEqLHMAEKELEKKFQQTAAYRNMKEILTKKNDQIKDLRKRLAQYEPED 358
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEE-LKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEK 388
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
148-329 |
1.99e-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: 40.05 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 148 AQAEKWYLKLQTDISELEnRELLEQVAEFEKAEITSSNKKPILDVTKPKLAPLNEggTAELLNKEILRLQEENEKLKSRL 227
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELE-REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK--EFAETRDELKDYREKLEKLKREI 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 228 KTIEIQATNALDEKSKLEKALQDLQldqgnqkdfikaQDLSNLENTVAALKSEF---QKTLNDKTENQKSLEENLATAKH 304
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLN------------AAIAGIEAKINELEEEKedkALEIKKQEWKLEQLAADLSKYEQ 469
|
170 180
....*....|....*....|....*
gi 2462590678 305 DLLRVQEQLHMAEKELEKKFQQTAA 329
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
98-350 |
2.18e-03 |
|
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: 40.10 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 98 LKESRLVEDTFTIDEVSEVLNGLQAVVHsEVESELINtaytnvlllrqlFAQAEKWYLKLQTDISELENRELLEQVAEFE 177
Cdd:pfam15921 160 LKEDMLEDSNTQIEQLRKMMLSHEGVLQ-EIRSILVD------------FEEASGKKIYEHDSMSTMHFRSLGSAISKIL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 178 KAEITSsnkkpiLDVTKPKLAPLN---EGGTAELLNKEILRLQEENEKLKSRLKTIEIQ-------ATNALDEKSKLEKA 247
Cdd:pfam15921 227 RELDTE------ISYLKGRIFPVEdqlEALKSESQNKIELLLQQHQDRIEQLISEHEVEitgltekASSARSQANSIQSQ 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 248 LQDLQLDQGNQKDFIKAQdLSNLENTVAALKSEF---QKTLNDKTEnqkSLEENLATAKHDLLRV---QEQLHMAEKELE 321
Cdd:pfam15921 301 LEIIQEQARNQNSMYMRQ-LSDLESTVSQLRSELreaKRMYEDKIE---ELEKQLVLANSELTEArteRDQFSQESGNLD 376
|
250 260 270
....*....|....*....|....*....|.
gi 2462590678 322 KKFQQTAA--YRNMKEiLTKKNDQIKDLRKR 350
Cdd:pfam15921 377 DQLQKLLAdlHKREKE-LSLEKEQNKRLWDR 406
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
140-357 |
2.65e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 140 VLLLRQLFAQAEKWYLKLQTDISELENRelLEQVaefeKAEITSSNKKpildvtkpklaplneggtAELLNKEILRLQEE 219
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAE--LEAA----QAELDALQAE------------------LEELNEEYNELQAE 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 220 NEKLKSRLKTI--EIQATNALDEK--SKLEKALQDLQ------------LDQGNQKDFI---------------KAQDLS 268
Cdd:COG3883 60 LEALQAEIDKLqaEIAEAEAEIEErrEELGERARALYrsggsvsyldvlLGSESFSDFLdrlsalskiadadadLLEELK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 269 NLENTVAALKSEFQKTLNDKTENQKSLEENLATAKHDLLRVQEQLHMAEKELEKKFQQTAAYRNMKEILTKKNDQIKDLR 348
Cdd:COG3883 140 ADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
....*....
gi 2462590678 349 KRLAQYEPE 357
Cdd:COG3883 220 AAAAAAAAA 228
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
155-355 |
5.68e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 38.57 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 155 LKLQTDISELENRELLEQVAEFEKAEITSSNKKpildvtkpklaplNEGGTAELLNKEILRLQEENE---KLKSRLKTIE 231
Cdd:pfam05557 51 QELQKRIRLLEKREAEAEEALREQAELNRLKKK-------------YLEALNKKLNEKESQLADAREvisCLKNELSELR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 232 IQATNALDEKSKLEKALQDLQldqgnQKDFIKAQDLSNLENTVAALKSEfQKTLNDKTENQKSLEENLATAKHDLLRV-- 309
Cdd:pfam05557 118 RQIQRAELELQSTNSELEELQ-----ERLDLLKAKASEAEQLRQNLEKQ-QSSLAEAEQRIKELEFEIQSQEQDSEIVkn 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462590678 310 --QEQLHMA--EKELEKKFQQTAAYRNMKEILTKKNDQIKDLRKRLAQYE 355
Cdd:pfam05557 192 skSELARIPelEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREE 241
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
168-334 |
6.88e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 38.35 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 168 ELLEQVAEFEKAEITSSNKKPILDVtkpklapLNEggTAELLNKeILRLQEENEKLKSRLktieiqaTNALDEKSKLEKA 247
Cdd:PRK11281 40 DVQAQLDALNKQKLLEAEDKLVQQD-------LEQ--TLALLDK-IDRQKEETEQLKQQL-------AQAPAKLRQAQAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 248 LQDLQldqgNQKDFIKAQDLSNLENTvaalksEFQKTLNDKTENQKSLEENLATAKHDLLRVQEQLHMAEKELEKKFQQT 327
Cdd:PRK11281 103 LEALK----DDNDEETRETLSTLSLR------QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRL 172
|
....*..
gi 2462590678 328 AAYRNMK 334
Cdd:PRK11281 173 QQIRNLL 179
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
206-357 |
7.33e-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: 37.82 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 206 AELLNKEILRLQEENEKLKSRLKTIEIQATNALDEKSKLEKALQDLQLDQGNQKDFIK-----AQDLSNLENTVAALKSE 280
Cdd:COG4942 50 EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAellraLYRLGRQPPLALLLSPE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462590678 281 -------FQKTLNDKTENQKSLEENLATAKHDLLRVQEQLHMAEKELEK-KFQQTAAYRNMKEILTKKNDQIKDLRKRLA 352
Cdd:COG4942 130 dfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAlLAELEEERAALEALKAERQKLLARLEKELA 209
|
....*
gi 2462590678 353 QYEPE 357
Cdd:COG4942 210 ELAAE 214
|
|
| |
