|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
122-426 |
3.44e-11 |
|
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: 66.23 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 122 YDEMRQKIRQLtqELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQKTLVDVTLENSNIKDQIRNLQQTYEA 201
Cdd:TIGR02168 215 YKELKAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 202 SMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREmtkklysqyEEKLQEEQRKHSAEKEALLEETNSFLKAIEEA 281
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESK---------LDELAEELAELEEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 282 NKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETemsgELTDSDKERYQQLEEASASLRERIRHLDDMVH 361
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA----RLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 70166414 362 CQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKIS----FLEGENNELQSRLDYLTETQAKTEVETREI 426
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEqaldAAERELAQLQARLDSLERLQENLEGFSEGV 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
96-426 |
4.59e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 96 QLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQ 175
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 176 KTLVDVTLENSNIKDQIRNLQQT---YEASMDKLREKQRQLEVAQVENQLLKMKVESSQeaNAEVMREMTKKLYS-QYEE 251
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDlhkLEEALNDLEARLSHSRIPEIQAELSKLEEEVSR--IEARLREIEQKLNRlTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 252 KLQEEQRKHSAEKEALLEET-NSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGE 330
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 331 LTDSDKERYQ--QLEEASASLRERIRHLDDMvhcqqkkvKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGENN----- 403
Cdd:TIGR02169 909 EAQIEKKRKRlsELKAKLEALEEELSEIEDP--------KGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMlaiqe 980
|
330 340
....*....|....*....|....*
gi 70166414 404 --ELQSRLDYLTETQAKTEVETREI 426
Cdd:TIGR02169 981 yeEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
180-426 |
5.48e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 180 DVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREMTKklySQYEEKLQEEQRK 259
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR---LEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 260 HSAEKEALLEEtnsflkAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELTDSDKERY 339
Cdd:COG1196 313 ELEERLEELEE------ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 340 QQLEEASA--SLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGENNELQSRLDYLTETQA 417
Cdd:COG1196 387 ELLEALRAaaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
....*....
gi 70166414 418 KTEVETREI 426
Cdd:COG1196 467 ELLEEAALL 475
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
174-418 |
6.68e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 174 LQKTLVDVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVEssQEANAEVMREMTKKLYSQYEEKL 253
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA--RLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 254 QEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELTD 333
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 334 --SDKERYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGENNELQSRLDY 411
Cdd:COG1196 402 leELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
....*..
gi 70166414 412 LTETQAK 418
Cdd:COG1196 482 LLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
108-375 |
1.28e-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: 54.68 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 108 RATLEKVRKRMygdyDEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQKTLVDVTLENSN 187
Cdd:TIGR02168 676 RREIEELEEKI----EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 188 IKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANaevmremtkklySQYEEKLQEEQRKHSAEKEAL 267
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL------------KALREALDELRAELTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 268 LEETNsflkAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELtdsdkERYQQLEEASA 347
Cdd:TIGR02168 820 ANLRE----RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL-----NERASLEEALA 890
|
250 260
....*....|....*....|....*...
gi 70166414 348 SLRERIRHLDDMVHCQQKKVKQMVEEIE 375
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELE 918
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
108-347 |
1.63e-07 |
|
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: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 108 RATLEKVRKRMYGDYDEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQKTLVDVTLENSN 187
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 188 IKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREMTKKLysQYEEKLQEEQRKHSAEKEAL 267
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA--AQLEELEEAEEALLERLERL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 268 LEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELTDSDKERYQQLEEASA 347
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
93-356 |
2.58e-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: 53.91 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 93 STSQLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSI 172
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 173 GLQKTLVDVTLENSNIKDQIRNLQ--------------QTYEASMDKLREKQRQLEVAQ---VENQLLKMKVESSQEANA 235
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRaeltllneeaanlrERLESLERRIAATERRLEDLEeqiEELSEDIESLAAEIEELE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 236 EVMREMTKKLysqyeEKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQ 315
Cdd:TIGR02168 866 ELIEELESEL-----EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 70166414 316 LQLQLLEHEtEMSGELtdsDKERYQQLEEASASLRERIRHL 356
Cdd:TIGR02168 941 LQERLSEEY-SLTLEE---AEALENKIEDDEEEARRRLKRL 977
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
192-426 |
3.80e-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: 53.14 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 192 IRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREMTKKLYSQyeEKLQEEQRKHSAEKEALLEET 271
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL--ARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 272 NSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLleheTEMSGELTDSdKERYQQLEEASASLRE 351
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL----DELRAELTLL-NEEAANLRERLESLER 831
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 70166414 352 RIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGENNELQSRLDYLTETQAKTEVETREI 426
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
127-418 |
1.71e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.71 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 127 QKIRQLTQELSVSHAQQEYLENHIQTQSsalDRFNAMNSALASdsigLQKTLVDVTLENSNIKDQIRNLQQTYEASMDKL 206
Cdd:TIGR04523 211 QKNKSLESQISELKKQNNQLKDNIEKKQ---QEINEKTTEISN----TQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 207 REKQRQLEvaQVENQLLKMKVESSQEANAEVMREMTK----------------KLYSQYEE-----------------KL 253
Cdd:TIGR04523 284 KELEKQLN--QLKSEISDLNNQKEQDWNKELKSELKNqekkleeiqnqisqnnKIISQLNEqisqlkkeltnsesensEK 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 254 QEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKErhqlqLQLLEHETEMSGELTD 333
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQE-----KELLEKEIERLKETII 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 334 SDKERYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGENNELQSRLDYLT 413
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLT 516
|
....*
gi 70166414 414 ETQAK 418
Cdd:TIGR04523 517 KKISS 521
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
95-359 |
2.13e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 95 SQLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQELSVSHAQQ-----EYLENHIQTQSSALDRFNAMNSALAS 169
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEiqaelSKLEEEVSRIEARLREIEQKLNRLTL 826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 170 DSIGLQKTLVDVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLE-----VAQVENQLLKMKVESSQ-EANAEVMREMTK 243
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEeleaaLRDLESRLGDLKKERDElEAQLRELERKIE 906
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 244 KLYSQYEEKlqeeqRKHSAEKEALLEETNSFLKAIEEANKKMQ---AAEISLEEKDQRIGELDRLIERMEkERHQLQLQL 320
Cdd:TIGR02169 907 ELEAQIEKK-----RKRLSELKAKLEALEEELSEIEDPKGEDEeipEEELSLEDVQAELQRVEEEIRALE-PVNMLAIQE 980
|
250 260 270
....*....|....*....|....*....|....*....
gi 70166414 321 LEHETEMSGELtdsdKERYQQLEEASASLRERIRHLDDM 359
Cdd:TIGR02169 981 YEEVLKRLDEL----KEKRAKLEEERKAILERIEEYEKK 1015
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
95-313 |
6.64e-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: 45.14 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 95 SQLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQELSVshaqqeyLENHIQTQSSALDRFNAMNSALASDSIGL 174
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA-------LEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 175 QKTLvdvtlensniKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKmKVESSQEANAEVMREMTKKLYSQYEE--- 251
Cdd:COG4942 103 KEEL----------AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLK-YLAPARREQAEELRADLAELAALRAElea 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 70166414 252 ---KLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKER 313
Cdd:COG4942 172 eraELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
96-414 |
6.93e-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: 45.87 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 96 QLKEEMNYIKDVRATLEKVRKRMygdyDEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQ 175
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKA----NQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIAT 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 176 KTLVDVTLENSNIKDQIRNLQQTYEASMDK-----------LREKQRQLEVAQVENQLLKMKVESSQEAnaevMREMTKk 244
Cdd:pfam05483 324 KTICQLTEEKEAQMEELNKAKAAHSFVVTEfeattcsleelLRTEQQRLEKNEDQLKIITMELQKKSSE----LEEMTK- 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 245 lYSQYEEKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQaaeisleekdqrigELDRLIERMEKERHQLQLQLLehe 324
Cdd:pfam05483 399 -FKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQ--------------ELIFLLQAREKEIHDLEIQLT--- 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 325 temsgELTDSDKERYQQLEEASASL-RERIRHLDDMVHC-----QQKKVKQ----MVEEIESLKKKLQQKQLLILQLLEK 394
Cdd:pfam05483 461 -----AIKTSEEHYLKEVEDLKTELeKEKLKNIELTAHCdklllENKELTQeasdMTLELKKHQEDIINCKKQEERMLKQ 535
|
330 340
....*....|....*....|
gi 70166414 395 ISFLEGENNELQSRLDYLTE 414
Cdd:pfam05483 536 IENLEEKEMNLRDELESVRE 555
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
246-426 |
1.18e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 246 YSQYEEKLQE-EQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHE 324
Cdd:COG1196 215 YRELKEELKElEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 325 TEMSGELTDSD--KERYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGEN 402
Cdd:COG1196 295 AELARLEQDIArlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180
....*....|....*....|....
gi 70166414 403 NELQSRLDYLTETQAKTEVETREI 426
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAEL 398
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
189-375 |
1.59e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 189 KDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMR-------EMTKKLYSQYEEKLQEEQRKHS 261
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaeelkkaEEEKKKVEQLKKKEAEEKKKAE 1650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 262 AEKEallEETNSFLKAIEEANK----KMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELTDSDKE 337
Cdd:PTZ00121 1651 ELKK---AEEENKIKAAEEAKKaeedKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 70166414 338 RYQQLEEASASLRERIRHLDDMV--HCQQKKVKQMVEEIE 375
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEEAKkdEEEKKKIAHLKKEEE 1767
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
178-357 |
1.70e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 178 LVDVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLEvaQVENQLLKMKVESSQEANAEVMREMTKKLY---SQYEEKLQ 254
Cdd:COG3206 207 LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA--ALRAQLGSGPDALPELLQSPVIQQLRAQLAeleAELAELSA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 255 EEQRKHSA--EKEALLEETNSFLKaiEEANKKMQAAEISLEEKDQRIGELDRLIERMEKE-----RHQLQLQLLEHETEM 327
Cdd:COG3206 285 RYTPNHPDviALRAQIAALRAQLQ--QEAQRILASLEAELEALQAREASLQAQLAQLEARlaelpELEAELRRLEREVEV 362
|
170 180 190
....*....|....*....|....*....|
gi 70166414 328 SGELTDSDKERYQQLEEASASLRERIRHLD 357
Cdd:COG3206 363 ARELYESLLQRLEEARLAEALTVGNVRVID 392
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
95-297 |
2.34e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 95 SQLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDS--I 172
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 173 GLQKTLVDVTLENSNIKDQIRNLQ-------------QTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMR 239
Cdd:COG3883 99 GGSVSYLDVLLGSESFSDFLDRLSalskiadadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 70166414 240 EMTKKLysqyeEKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQ 297
Cdd:COG3883 179 EQEALL-----AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
186-408 |
2.51e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 186 SNIKDQIRNLQQTYEA---SMDKLREKQRQL--EVAQVENQLLKMKVESSQEANAEVMREMTKKLYSQYEEKLQ--EEQR 258
Cdd:PRK03918 189 ENIEELIKEKEKELEEvlrEINEISSELPELreELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRelEERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 259 KHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQL--LEHETEMSGELTDSDK 336
Cdd:PRK03918 269 EELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIkeLEEKEERLEELKKKLK 348
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 70166414 337 ERYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGENNELQSR 408
Cdd:PRK03918 349 ELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE 420
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
187-376 |
3.53e-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: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 187 NIKDQIRNLQQTYEAsMDKLREKQRQLEVAQVENQLLKMKVESSQEANAevMREMTKKLYSQYE-EKLQEEQRKHSAEKE 265
Cdd:COG4913 229 ALVEHFDDLERAHEA-LEDAREQIELLEPIRELAERYAAARERLAELEY--LRAALRLWFAQRRlELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 266 ALLEETNSFLKAIEEANKKMQAAEISLEEKD-QRIGELDRLIERMEKERHQLQLQLLEHET-----EMSGELTDSD---- 335
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEAllaalGLPLPASAEEfaal 385
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 70166414 336 ----KERYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIES 376
Cdd:COG4913 386 raeaAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
89-359 |
3.56e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 89 VYGWSTSQLKEEmnyIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQELSVSHAQQEY---------LENHIQTQSSALDR 159
Cdd:COG4913 603 VLGFDNRAKLAA---LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeidvasAEREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 160 FNAMNSALAsdsiGLQKTLVDVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMR 239
Cdd:COG4913 680 LDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 240 --EMTKKLYSQYEEKLQEEQRKHSAEKEALLEEtnsFLKAIEEANKK----MQAAEISLEEKDQRIGELDRLI-ERMEKE 312
Cdd:COG4913 756 aaALGDAVERELRENLEERIDALRARLNRAEEE---LERAMRAFNREwpaeTADLDADLESLPEYLALLDRLEeDGLPEY 832
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 70166414 313 RHQLQLQLLEHETEMSGELtdsdkerYQQLEEASASLRERIRHLDDM 359
Cdd:COG4913 833 EERFKELLNENSIEFVADL-------LSKLRRAIREIKERIDPLNDS 872
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
205-426 |
3.97e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 205 KLREKQRQLEVAQVENQLLKMKVESSQeanAEVMREMTKKL--YSQYEekLQEEQRKHSAEKEALLEETNSFLKAIEEAN 282
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREK---AERYQALLKEKreYEGYE--LLKEKEALERQKEAIERQLASLEEELEKLT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 283 KKMQAAEISLEEKDQRIGELDRLIERM-EKERHQLQLQLLEHETEMSG----------ELTDSDKERyQQLEEASASLRE 351
Cdd:TIGR02169 258 EEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASlersiaekerELEDAEERL-AKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 352 RIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLL--------------ILQLLEKISFLEGENNELQSRLDYLTETQA 417
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEleevdkefaetrdeLKDYREKLEKLKREINELKRELDRLQEELQ 416
|
....*....
gi 70166414 418 KTEVETREI 426
Cdd:TIGR02169 417 RLSEELADL 425
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
96-376 |
6.30e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 96 QLKEEMNYIKDVRATLEKVRKrMYGDYDEMRQKIRQLTQELSvshAQQEYLENHIQTQSSaldrfnaMNSALASDSIGLQ 175
Cdd:pfam15921 445 QMERQMAAIQGKNESLEKVSS-LTAQLESTKEMLRKVVEELT---AKKMTLESSERTVSD-------LTASLQEKERAIE 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 176 KTLVDVTLENSNIKDQIRNLQQtyeasmdkLREKQRQLEVAQVENQLLKMKVeSSQEANAEVMRemtkklysQYEEKLQE 255
Cdd:pfam15921 514 ATNAEITKLRSRVDLKLQELQH--------LKNEGDHLRNVQTECEALKLQM-AEKDKVIEILR--------QQIENMTQ 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 256 EQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERhqlqLQLLEHETEMSGELTDSD 335
Cdd:pfam15921 577 LVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEK----VKLVNAGSERLRAVKDIK 652
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 70166414 336 KERYQQLEEASASlRERIRHLDDMVHCQQKKVKQMVEEIES 376
Cdd:pfam15921 653 QERDQLLNEVKTS-RNELNSLSEDYEVLKRNFRNKSEEMET 692
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
206-360 |
6.48e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 206 LREKQRQLEVAQVENQLLKMKVESSQEANAEVMREMTKKLYSQYEEKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKM 285
Cdd:COG1196 676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 286 QAAEISLEEKDQRIGELDRLIERME-------------KERHQlqlqllehetEMSGELTDsdkeryqqLEEASASLRER 352
Cdd:COG1196 756 LPEPPDLEELERELERLEREIEALGpvnllaieeyeelEERYD----------FLSEQRED--------LEEARETLEEA 817
|
....*...
gi 70166414 353 IRHLDDMV 360
Cdd:COG1196 818 IEEIDRET 825
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
127-348 |
6.52e-04 |
|
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: 42.06 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 127 QKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQKTLVDVTLENSNIKDQIRNLQQTYEASMDKL 206
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 207 REKQ----RQLEVAQVENQLLKMKV-ESSQEANAEVMREMTKKLYSQYEEKLQEEQRKHSAEKEALLEETNSFLKAIEEA 281
Cdd:COG4942 100 EAQKeelaELLRALYRLGRQPPLALlLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 70166414 282 NKKMQAAEISLE-EKDQRIGELDRLIERMEKERHQLQlQLLEHETEMSGELTDSDKERYQQLEEASAS 348
Cdd:COG4942 180 LAELEEERAALEaLKAERQKLLARLEKELAELAAELA-ELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
251-425 |
8.47e-04 |
|
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: 41.67 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 251 EKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGE 330
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 331 LTDSDK-ERYQQLE-----EASASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGENNE 404
Cdd:COG4942 110 LRALYRlGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180
....*....|....*....|.
gi 70166414 405 LQSRLDYLTETQAKTEVETRE 425
Cdd:COG4942 190 LEALKAERQKLLARLEKELAE 210
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
251-425 |
9.75e-04 |
|
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: 41.67 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 251 EKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQL---------- 320
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaellralyrl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 321 -----------------LEHETEMSGELTDSDKERYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQ 383
Cdd:COG4942 117 grqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 70166414 384 KQLLILQLLEKISFLEGENNELQSRLDYLTETQAKTEVETRE 425
Cdd:COG4942 197 RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
203-317 |
1.20e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 203 MDKLREKQRQLEVAQVENqllkMKVESSQEANAEVMREMTK--------KLYSQYEEKLQEEQRKHSAEK-EALLEETNS 273
Cdd:PRK05771 18 KDEVLEALHELGVVHIED----LKEELSNERLRKLRSLLTKlsealdklRSYLPKLNPLREEKKKVSVKSlEELIKDVEE 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 70166414 274 FLKAIEEankkmqaaeiSLEEKDQRIGELDRLIERMEKERHQLQ 317
Cdd:PRK05771 94 ELEKIEK----------EIKELEEEISELENEIKELEQEIERLE 127
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
186-375 |
2.01e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 186 SNIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMR-EMTKKLYSQYEEKLQEEQrKHSAEK 264
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyIKLSEFYEEYLDELREIE-KRLSRL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 265 EALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERhQLQLQLLEHETEMSGELTDSDKERYQQLEE 344
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAK-AKKEELERLKKRLTGLTPEKLEKELEELEK 398
|
170 180 190
....*....|....*....|....*....|.
gi 70166414 345 ASASLRERIRHLDDMVHCQQKKVKQMVEEIE 375
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
128-338 |
2.99e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 128 KIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQKTLV----DVTLENSNIKDQIRNL---QQTYE 200
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVeeakTIKAEIEELTDELLNLvmdIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 201 ASMDKLREKQRQLEvAQVE--NQLLKMKVESSQEANAEVMREMTKKLYSQYEEKLQEEQRKHSAEKEAlLEETNSFLKAI 278
Cdd:PHA02562 255 AALNKLNTAAAKIK-SKIEqfQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTA-IDELEEIMDEF 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70166414 279 EEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSG---ELTDSDKER 338
Cdd:PHA02562 333 NEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKlqdELDKIVKTK 395
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
171-297 |
3.52e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 40.03 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 171 SIGLQKTLVDVTLENSNIKDQI-----------------RNLQQTYEASMDKLREKQRQLEvaqveNQLLKMKVessqea 233
Cdd:smart00435 230 SITLQEQLKELTAKDGNVAEKIlaynranrevailcnhqRTVSKTHEKSMEKLQEKIKALK-----YQLKRLKK------ 298
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 70166414 234 nAEVMREMTKKLYSQYEEKLQEEQRKHSAEKEALLEETNSFL---KAIEEANKKMQAAEISLEEKDQ 297
Cdd:smart00435 299 -MILLFEMISDLKRKLKSKFERDNEKLDAEVKEKKKEKKKEEkkkKQIERLEERIEKLEVQATDKEE 364
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
218-375 |
4.71e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 218 VENQLLKMKVESSQEANAEVMREMTKKLYSQYEEKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQ 297
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 298 RIGELDRLIERMEKERHQLQLQLLEHETEMSGELTDSDK--ERYQQL--EEASASLRERIRhlDDMVHCQQKKVKQMVEE 373
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQelERISGLtaEEAKEILLEKVE--EEARHEAAVLIKEIEEE 181
|
..
gi 70166414 374 IE 375
Cdd:PRK12704 182 AK 183
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
95-370 |
5.08e-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: 39.72 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 95 SQLKEEMNYIKDVRATLEKVRKRMYGdYDEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSiGL 174
Cdd:pfam05557 125 LELQSTNSELEELQERLDLLKAKASE-AEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIP-EL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 175 QKTLVDVTLENSNIKDQIRNLQ------QTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREM-TKKLYS 247
Cdd:pfam05557 203 EKELERLREHNKHLNENIENKLllkeevEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLrSPEDLS 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 248 QYEEKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKerhqlQLQLLEHETEM 327
Cdd:pfam05557 283 RRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQR-----RVLLLTKERDG 357
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 70166414 328 SGELTDS-DKEryQQLEEASASLRERIRHLDDMVHCQQKKVKQM 370
Cdd:pfam05557 358 YRAILESyDKE--LTMSNYSPQLLERIEEAEDMTQKMQAHNEEM 399
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
160-351 |
5.19e-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: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 160 FNAMNSALASDSIG-LQKTLVDVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVM 238
Cdd:COG3883 6 LAAPTPAFADPQIQaKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 239 REMTKKLYSQYEEKLQeeqrkhSAEKEALLEETN--------SFLKAIEEANKKM----QAAEISLEEK----DQRIGEL 302
Cdd:COG3883 86 EELGERARALYRSGGS------VSYLDVLLGSESfsdfldrlSALSKIADADADLleelKADKAELEAKkaelEAKLAEL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 70166414 303 DRLIERMEKERHQLQLQLLEHETEMSgELTDSDKERYQQLEEASASLRE 351
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLA-QLSAEEAAAEAQLAELEAELAA 207
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
136-356 |
5.89e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.98 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 136 LSVSHAQQEYLENHIQTQSSALDRFNAMNSALA---SDSIGLQKTLVDVTLENSNIKDQIRNLQQtyeasmdKLREKQRQ 212
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAalkKEEKALLKQLAALERRIAALARRIRALEQ-------ELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70166414 213 LEVAQVENQLLKMKVESSQEANAEVMREMTK-KLYSQYEEKLQEEQRKHSAEKEALLEETNSFLKA-IEEANKKMQAAEI 290
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRALYRlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREqAEELRADLAELAA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 70166414 291 SLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSG--ELTDSDKERYQQLEEASASLRERIRHL 356
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARleKELAELAAELAELQQEAEELEALIARL 232
|
|
| |
