|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
205-559 |
8.02e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.92 E-value: 8.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 205 QSLQTRVLELQQQLAVAvaADRKKDTMIEQLDKTLArvvegwnrheaERTEVLRGLQEEHQAAELTRSKQQETVTRLEQS 284
Cdd:COG1196 216 RELKEELKELEAELLLL--KLRELEAELEELEAELE-----------ELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 285 LSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQ 364
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 365 QEHQLKEHYQALQEEsQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQR 444
Cdd:COG1196 363 AEEALLEAEAELAEA-EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 445 IQLESELAVQLEQrvtERLAQAQESSLRQAASLREHHRKQLQDLsgqhQQELASQLAQFKVEMAEREERQQQVAEDYELR 524
Cdd:COG1196 442 EALEEAAEEEAEL---EEEEEALLELLAELLEEAALLEAALAEL----LEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
330 340 350
....*....|....*....|....*....|....*.
gi 191252785 525 LAREQARVC-ELQSGNQQLEEQRVELVERLQAMLQA 559
Cdd:COG1196 515 LLAGLRGLAgAVAVLIGVEAAYEAALEAALAAALQN 550
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
226-567 |
8.01e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.29 E-value: 8.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 226 RKKDTMiEQLDKT---LARVvegwnrhEAERTEV---LRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEALNREQESA 299
Cdd:COG1196 173 RKEEAE-RKLEATeenLERL-------EDILGELerqLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 300 RLQQRERETLEEerqaltlRLEAEQQRccvLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLkEHYQALQEE 379
Cdd:COG1196 245 EAELEELEAELE-------ELEAELAE---LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI-ARLEERRRE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 380 SQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRV 459
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 460 TERLAQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVcELQSGN 539
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA-ELLEEA 472
|
330 340
....*....|....*....|....*...
gi 191252785 540 QQLEEQRVELVERLQAMLQAHWDEANQL 567
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
198-488 |
5.00e-14 |
|
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: 76.63 E-value: 5.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 198 KHCERHIQSLQTRVLELQQQLAVAvaadRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQET 277
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAEL----RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 278 VTRLEQSLSEAMEALNREQESARLQQRERETLEEE-------RQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELET 350
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQieqlkeeLKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 351 LRAALEEERQTWAQQEHQLK------EHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARR 424
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIEslaaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 191252785 425 ERDALQLEMSLVQARY---ESQRIQLESELAV--QLEQRVTERLAQAQESSLRQAASLREHHRKQLQDL 488
Cdd:TIGR02168 916 ELEELREKLAQLELRLeglEVRIDNLQERLSEeySLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
314-599 |
6.07e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.13 E-value: 6.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 314 QALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQR 393
Cdd:COG1196 214 RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 394 EAQAAwETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQ 473
Cdd:COG1196 294 LAELA-RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 474 AASLREHHRKQLQDLSGQHQQELASQLAQfkvemaerEERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERL 553
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQ--------LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 191252785 554 QAMLQAHWDEANQLLSTTLPPPNPPAPPAGPSSPGPQEPEKEERRV 599
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
284-558 |
8.02e-13 |
|
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: 72.78 E-value: 8.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 284 SLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSE--HRELETLRAALEEERQT 361
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 362 WAQQEHQLkehyQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYE 441
Cdd:TIGR02168 745 LEERIAQL----SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 442 SQRIQLESEL--AVQLEQRVTERLAQAQESSLRQAASlrEHHRKQLQDLSGQHQQELAS---QLAQFKVEMAEREERQQQ 516
Cdd:TIGR02168 821 NLRERLESLErrIAATERRLEDLEEQIEELSEDIESL--AAEIEELEELIEELESELEAllnERASLEEALALLRSELEE 898
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 191252785 517 VAEdyELRLAREQARvcELQSGNQQLEEQRVELVERLQAMLQ 558
Cdd:TIGR02168 899 LSE--ELRELESKRS--ELRRELEELREKLAQLELRLEGLEV 936
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
328-559 |
1.27e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.79 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 328 CVLQEERDAARAGQLSEH-RELETLRAALEEERQtwaQQEH--QLKEHYQALQEesqAQLEREKEKSQREAQAAWETQHQ 404
Cdd:COG4913 216 YMLEEPDTFEAADALVEHfDDLERAHEALEDARE---QIELlePIRELAERYAA---ARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 405 LALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQrVTERLAQAQESsLRQAASLREHHRKQ 484
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ-LEREIERLERE-LEERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 485 LQDLSGQHQ------QELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAMLQ 558
Cdd:COG4913 368 LAALGLPLPasaeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
.
gi 191252785 559 A 559
Cdd:COG4913 448 A 448
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
250-543 |
3.59e-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: 67.39 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 250 EAERTEVLRGLQEEHQAAELT------------RSKQQETVTRLEQSLSEAMEALNREQES---ARLQQRERETLEEERQ 314
Cdd:TIGR02168 208 QAEKAERYKELKAELRELELAllvlrleelreeLEELQEELKEAEEELEELTAELQELEEKleeLRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 315 ALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKsqRE 394
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL--EA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 395 AQAAWETQhqlalvqseVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLEselavQLEQRVtERLAQAQESslrQA 474
Cdd:TIGR02168 366 ELEELESR---------LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE-----RLEDRR-ERLQQEIEE---LL 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 191252785 475 ASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAE------DYELRLAREQARVCELQSGNQQLE 543
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEaeqaldAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
180-552 |
1.83e-10 |
|
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: 65.09 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 180 PPDFQGLRDALDSEHTRRKHCERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEgwnrheaERTEVLRG 259
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE-------RLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 260 LQEEHQAAELTRSKQQEtvtrLEQSLSEAMEALNREQES-ARLQQRERETLEEERQALTLRLEAEQQRccvlQEERDAAR 338
Cdd:TIGR02169 746 LSSLEQEIENVKSELKE----LEARIEELEEDLHKLEEAlNDLEARLSHSRIPEIQAELSKLEEEVSR----IEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 339 AGQLSEhreLETLRAALEEERQTWAQQEHQLKEHYQALQEEsQAQLEREKEKSQREaqaawetqhqLALVQSEVRRLEGE 418
Cdd:TIGR02169 818 EQKLNR---LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE-IENLNGKKEELEEE----------LEELEAALRDLESR 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 419 LDTARRERDALQLEMSLVQARYESQRIQLEselavQLEQRVTERLAQAQEsslrQAASLREHHRKQLQDLSGQHQQELAS 498
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEELEAQIE-----KKRKRLSELKAKLEA----LEEELSEIEDPKGEDEEIPEEELSLE 954
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 191252785 499 QLAQFKVEMAEREERQQQV----AEDYElrlaREQARVCELQSGNQQLEEQRVELVER 552
Cdd:TIGR02169 955 DVQAELQRVEEEIRALEPVnmlaIQEYE----EVLKRLDELKEKRAKLEEERKAILER 1008
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
251-551 |
1.52e-09 |
|
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: 62.01 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 251 AERTEVLRgLQEEHQAAELTRSKQQETVTRLEQSLSEA---MEALNREQESARLQQRERETLEEERQALTLRLEAEQQRC 327
Cdd:TIGR02169 671 SEPAELQR-LRERLEGLKRELSSLQSELRRIENRLDELsqeLSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 328 cvlQEERDAARAgqlsehrELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKsqreaqaawetqhqlal 407
Cdd:TIGR02169 750 ---EQEIENVKS-------ELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSK----------------- 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 408 VQSEVRRLEGELDTARRERDALQLEMslvqaRYESQRIQLESELAVQLEQRVTERLAQAQESSLRQAASLRE--HHRKQL 485
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEK-----EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEleELEAAL 877
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 191252785 486 QDLSGQHqQELASQLAQFKVEMAEREERQQQVAEDYEL---RLAREQARVCELQSGNQQLEEQRVELVE 551
Cdd:TIGR02169 878 RDLESRL-GDLKKERDELEAQLRELERKIEELEAQIEKkrkRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
334-559 |
2.76e-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: 61.23 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 334 RDAARAGQLSEHRELETLRAALEEerqtwaqQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAwETQHQLALVQSEVR 413
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEE-------LEEKIAELEKALAELRKELEELEEELEQLRKELE-ELSRQISALRKDLA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 414 RLEGELDTARRERDALQLEMSLVQAR---YESQRIQLESELAVQLEQRVT--ERLAQAQEsslrQAASLREHH---RKQL 485
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEieeLEERLEEAEEELAEAEAEIEEleAQIEQLKE----ELKALREALdelRAEL 812
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 191252785 486 QDLSG-QHQQELASQLAQFKVEMAERE-ERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAMLQA 559
Cdd:TIGR02168 813 TLLNEeAANLRERLESLERRIAATERRlEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
313-553 |
4.84e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 313 RQALTLRLEAEQQRCCVLQEERDAARAgQLSEHRELETLRAAlEEERQTWAQQEHQLKEHYQALQEESQ--AQLEREKEK 390
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQE-RREALQRLAEYSWD-EIDVASAEREIAELEAELERLDASSDdlAALEEQLEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 391 SQREAQAAwetQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYES-QRIQLESELAVQLEQRVTERLAQAQES 469
Cdd:COG4913 697 LEAELEEL---EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLRALLEERFAAALGDAVERELRENLEE 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 470 SLRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREE----RQQQVAED--------YELRLAREQARVCELQS 537
Cdd:COG4913 774 RIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEylalLDRLEEDGlpeyeerfKELLNENSIEFVADLLS 853
|
250
....*....|....*.
gi 191252785 538 gnqQLEEQRVELVERL 553
Cdd:COG4913 854 ---KLRRAIREIKERI 866
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
235-567 |
5.28e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.36 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 235 LDKTLARVVEGWNRHEAERTEVLRG---LQEEHQAAELTRSKQQETVTR--------------LEQSLSEAMEALNREQE 297
Cdd:PRK04863 263 ITESTNYVAADYMRHANERRVHLEEaleLRRELYTSRRQLAAEQYRLVEmarelaelneaesdLEQDYQAASDHLNLVQT 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 298 sARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALE------EERQTWAQQEHQLKe 371
Cdd:PRK04863 343 -ALRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAdyqqalDVQQTRAIQYQQAV- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 372 hyQALQEESQ-------------AQLEREKEKSQREAQAAWETQHQLALVQ----------SEVRRLEGELDTARRERDA 428
Cdd:PRK04863 421 --QALERAKQlcglpdltadnaeDWLEEFQAKEQEATEELLSLEQKLSVAQaahsqfeqayQLVRKIAGEVSRSEAWDVA 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 429 LQLEmslvqARYESQRIQleselAVQLEQRvterlaQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQlAQFKVEMA 508
Cdd:PRK04863 499 RELL-----RRLREQRHL-----AEQLQQL------RMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE-DELEQLQE 561
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 191252785 509 EREERQqqvaEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAMLQAHwDEANQL 567
Cdd:PRK04863 562 ELEARL----ESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQ-DALARL 615
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
201-555 |
1.63e-08 |
|
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: 58.70 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 201 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQETVTR 280
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 281 LEqslSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSE-HRELETLRAALEEER 359
Cdd:pfam12128 327 LE---DQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnNRDIAGIKDKLAKIR 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 360 QTWAQQEHQLKEHYQALQEESQAQLEREK-----EKSQREAQAAW------------ETQHQLALVQSEVRRLEGELDTA 422
Cdd:pfam12128 404 EARDRQLAVAEDDLQALESELREQLEAGKlefneEEYRLKSRLGElklrlnqatatpELLLQLENFDERIERAREEQEAA 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 423 RRERDALQLEMSLVQARYESQRIQLESELAVQLEQRvtERLAQAQESSLRQAASLREHHRKQLQDLSgQHQQELAS--QL 500
Cdd:pfam12128 484 NAEVERLQSELRQARKRRDQASEALRQASRRLEERQ--SALDELELQLFPQAGTLLHFLRKEAPDWE-QSIGKVISpeLL 560
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 191252785 501 AQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQA 555
Cdd:pfam12128 561 HRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQS 615
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
336-555 |
2.14e-08 |
|
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: 57.08 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 336 AARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQeesqaQLEREKEKSQREAQaawETQHQLALVQSEVRRL 415
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-----ALERRIAALARRIR---ALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 416 EGELDTARRERDALQLEMS-LVQARYESQRIQ-----LESELAVQLEQRVT--ERLAQAQESSLRQAASLREHHRKQLQD 487
Cdd:COG4942 89 EKEIAELRAELEAQKEELAeLLRALYRLGRQPplallLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 488 LSGQHQQ--ELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQA 555
Cdd:COG4942 169 LEAERAEleALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
263-556 |
2.97e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 57.44 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 263 EHQAAeLTRSKQQETVTRLEQS-LSEAMEALNREQESAR-LQQRERETLEEERQALTLRleAEQQRCcVLQEERDAARAG 340
Cdd:pfam17380 279 QHQKA-VSERQQQEKFEKMEQErLRQEKEEKAREVERRRkLEEAEKARQAEMDRQAAIY--AEQERM-AMERERELERIR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 341 QLSEHRELETLRA---ALEEERQ---TWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRR 414
Cdd:pfam17380 355 QEERKRELERIRQeeiAMEISRMrelERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 415 LEGELDTARRERdalqlEMSLVQARyESQRIQLESELAVQLEQRVTERLAQAQESSLRQAAslREHHRKQLQDLSGQHQQ 494
Cdd:pfam17380 435 REVRRLEEERAR-----EMERVRLE-EQERQQQVERLRQQEEERKRKKLELEKEKRDRKRA--EEQRRKILEKELEERKQ 506
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 191252785 495 ELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVE---RLQAM 556
Cdd:pfam17380 507 AMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEersRLEAM 571
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
196-534 |
3.08e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 57.67 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 196 RRKHCERHIQSLQTRVLELQQQLAVAVAADRKK-DTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQ 274
Cdd:TIGR00618 159 KAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSlHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 275 QETVTRLEQSLSEAMEALNREQEsARLQQRERETLEEERQALTLRLEAEQQRCCVLQ--------EERDAARAGQLSEHR 346
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQLKKQQL-LKQLRARIEELRAQEAVLEETQERINRARKAAPlaahikavTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 347 ELETLRAALEEERQTWAQQEHQLKEHYQALQ----EESQAQLEREKEKSQRE--AQAAWETQHQLALvQSEVRRLEGELD 420
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQtlhsQEIHIRDAHEVATSIREisCQQHTLTQHIHTL-QQQKTTLTQKLQ 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 421 TARRERDALQLEMSLVQARYESQRIqLESELAV-----QLEQRVTERLAQAQESSLrQAASLREHHRKQLQdlsgQHQQE 495
Cdd:TIGR00618 397 SLCKELDILQREQATIDTRTSAFRD-LQGQLAHakkqqELQQRYAELCAAAITCTA-QCEKLEKIHLQESA----QSLKE 470
|
330 340 350
....*....|....*....|....*....|....*....
gi 191252785 496 LASQLAQFKVeMAEREERQQQVAEDYELRLAREQARVCE 534
Cdd:TIGR00618 471 REQQLQTKEQ-IHLQETRKKAVVLARLLELQEEPCPLCG 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
317-567 |
3.18e-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: 57.77 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 317 TLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTwAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQ 396
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSD-ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 397 aawETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQEssLRQAAS 476
Cdd:TIGR02169 748 ---SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE--IEQKLN 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 477 LREHHRKQLQDLSgqhqQELASQLAQFKVEMAEREERQqqvaEDYELRLAREQARVCELQSGNQQLEEQRVEL---VERL 553
Cdd:TIGR02169 823 RLTLEKEYLEKEI----QELQEQRIDLKEQIKSIEKEI----ENLNGKKEELEEELEELEAALRDLESRLGDLkkeRDEL 894
|
250
....*....|....
gi 191252785 554 QAMLQAHWDEANQL 567
Cdd:TIGR02169 895 EAQLRELERKIEEL 908
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
182-572 |
7.42e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 7.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 182 DFQGLRDALDSEHTRRKHCERHIQSLQTRVLELQQQLAVA------VAADRKKDTMIEQLDKTLARVVEgWNRHEAERTE 255
Cdd:COG4717 89 EYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLplyqelEALEAELAELPERLEELEERLEE-LRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 256 VLRGLQEEHQ----AAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQ 331
Cdd:COG4717 168 LEAELAELQEeleeLLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 332 EERDAARAGQLSehrELETLRAALEEERQTWA------------QQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAW 399
Cdd:COG4717 248 ARLLLLIAAALL---ALLGLGGSLLSLILTIAgvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 400 ETQHQLALVQS-----EVRRLEGELDTARRERDALQLEMSLvqARYESQRIQLESELAVQLEQRVTERLAQAQEssLRQA 474
Cdd:COG4717 325 LAALGLPPDLSpeellELLDRIEELQELLREAEELEEELQL--EELEQEIAALLAEAGVEDEEELRAALEQAEE--YQEL 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 475 ASLREHHRKQLQDLSGQHQQ--------ELASQLAQFKVEMAEREERQQQVAEdyelRLAREQARVCELQSGN--QQLEE 544
Cdd:COG4717 401 KEELEELEEQLEELLGELEEllealdeeELEEELEELEEELEELEEELEELRE----ELAELEAELEQLEEDGelAELLQ 476
|
410 420
....*....|....*....|....*...
gi 191252785 545 QRVELVERLQAMLQAHwdEANQLLSTTL 572
Cdd:COG4717 477 ELEELKAELRELAEEW--AALKLALELL 502
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
251-569 |
8.68e-08 |
|
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: 56.50 E-value: 8.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 251 AERTEVLRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQreretleeerQALTlRLEaEQQRCCVL 330
Cdd:COG3096 364 EEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQ----------QAVQ-ALE-KARALCGL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 331 qEERDAARAGQlsehrELETLRAALEEERQTWAQQEHQL-------KEHYQALQ---------EESQA-QLEREKEKSQR 393
Cdd:COG3096 432 -PDLTPENAED-----YLAAFRAKEQQATEEVLELEQKLsvadaarRQFEKAYElvckiagevERSQAwQTARELLRRYR 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 394 EAQAAWETQHQLALVQSEVRRLEGELDTARRerdaLQLEMSLVQARYESQRIQLESELAVQLEQRvtERLAQAQESSLRQ 473
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRLRQQQNAER----LLEEFCQRIGQQLDAAEELEELLAELEAQL--EELEEQAAEAVEQ 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 474 AASLReHHRKQLQDLSGQHQQ------ELASQLAQFKVEMAEREERQQQVAEDYELRLAREQarvcELQSGNQQLEEQRV 547
Cdd:COG3096 580 RSELR-QQLEQLRARIKELAArapawlAAQDALERLREQSGEALADSQEVTAAMQQLLERER----EATVERDELAARKQ 654
|
330 340
....*....|....*....|..
gi 191252785 548 ELVERLQAMLQAHWDEANQLLS 569
Cdd:COG3096 655 ALESQIERLSQPGGAEDPRLLA 676
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
186-556 |
1.49e-07 |
|
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: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 186 LRDALDSEHTRRKHCERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARV---VEGWNRHEAERTEVLRGLQE 262
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELeeeEEEEEEALEEAAEEEAELEE 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 263 EHQAAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQ---------------------------- 314
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEgvkaalllaglrglagavavligveaay 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 315 --ALTLRLEAEQQRCCVLQEERDAARAGQLSEHRE--LETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEK 390
Cdd:COG1196 537 eaALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYY 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 391 SQREAQAAWE-TQHQLALVQSEVRRLEGELDTARRERDALQL----------EMSLVQARYESQRIQLESELAVQLEQRV 459
Cdd:COG1196 617 VLGDTLLGRTlVAARLEAALRRAVTLAGRLREVTLEGEGGSAggsltggsrrELLAALLEAEAELEELAERLAEEELELE 696
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 460 TERLAQAQEsslRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREqarvcelqsgn 539
Cdd:COG1196 697 EALLAEEEE---ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL----------- 762
|
410
....*....|....*..
gi 191252785 540 QQLEEQRVELVERLQAM 556
Cdd:COG1196 763 EELERELERLEREIEAL 779
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
346-555 |
2.30e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 346 RELETLRAALEEERQTWAQQEHQLKEHYQALQeesqaQLEREKEKSQR--------EAQAAWETQHQLALVQSEVRRLEG 417
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLE-----RLRREREKAERyqallkekREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 418 ELDTARRERDALQLEMSLVQARYESQRIQLEsELAVQLEQRVTERLAQAQESSLRQAASLREHHRKqlQDLSGQHQQELA 497
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLE-ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERS--IAEKERELEDAE 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 191252785 498 SQLAQFKVEMaereERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQA 555
Cdd:TIGR02169 322 ERLAKLEAEI----DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
287-467 |
5.23e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 287 EAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARagQLSEHRELETLRAALEEERQTWAQQE 366
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE--KLLQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 367 HQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQ 446
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180
....*....|....*....|.
gi 191252785 447 LESELAVQLEQRVTERLAQAQ 467
Cdd:COG4717 229 LEQLENELEAAALEERLKEAR 249
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
226-546 |
6.99e-07 |
|
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: 53.30 E-value: 6.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 226 RKKDTMIEQLDKTLARVVEGWN-RHEAERTEVLRGLQEEHQAAEltrskqqetvtRLEQSLSEAMEALNREQESARLQQR 304
Cdd:pfam12128 375 AKYNRRRSKIKEQNNRDIAGIKdKLAKIREARDRQLAVAEDDLQ-----------ALESELREQLEAGKLEFNEEEYRLK 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 305 ERETLEEERQA-------LTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLR--------------AALEEERQTWA 363
Cdd:pfam12128 444 SRLGELKLRLNqatatpeLLLQLENFDERIERAREEQEAANAEVERLQSELRQARkrrdqasealrqasRRLEERQSALD 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 364 QQEHQL------------------------------------------------------KEHYQALQEESQAQLEREKE 389
Cdd:pfam12128 524 ELELQLfpqagtllhflrkeapdweqsigkvispellhrtdldpevwdgsvggelnlygvKLDLKRIDVPEWAASEEELR 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 390 KSQREAQAAWETQHQLAlvqsevRRLEGELDTARRERDALQLEMSLVQARYESQRIQL------ESELAVQLEQRVTERL 463
Cdd:pfam12128 604 ERLDKAEEALQSAREKQ------AAAEEQLVQANGELEKASREETFARTALKNARLDLrrlfdeKQSEKDKKNKALAERK 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 464 AQAQEsSLRQAAslrehhrKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGN---- 539
Cdd:pfam12128 678 DSANE-RLNSLE-------AQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAkael 749
|
....*..
gi 191252785 540 QQLEEQR 546
Cdd:pfam12128 750 KALETWY 756
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
128-555 |
7.66e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 7.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 128 SERREEDSFDSDSTATLLNTRPLQDLSPSSSAQALEELFPRYTSLRPGPPLNPPDFQGLRDALDSEHTRRKHCERHIQSL 207
Cdd:PRK02224 282 RDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEEL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 208 QTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEvlrgLQEEHQAAELTRSKQQETVTRLEQSLSE 287
Cdd:PRK02224 362 REEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGN----AEDFLEELREERDELREREAELEATLRT 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 288 AMEALNREQEsarlqqreretleeerqaltLRLEAEQQRCCvlQEERDAARAGQLSEHRE-LETLRAALEEERQTWAQQE 366
Cdd:PRK02224 438 ARERVEEAEA--------------------LLEAGKCPECG--QPVEGSPHVETIEEDRErVEELEAELEDLEEEVEEVE 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 367 HQLKEHYQALQEESQAQLEREKEK------SQREAQAAwETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQ--- 437
Cdd:PRK02224 496 ERLERAEDLVEAEDRIERLEERREdleeliAERRETIE-EKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAReev 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 438 ARYESQRIQLESELAvQLEqRVTERLAQAQEssLRQAASLREHHRKQLQDLSGQHQQELAsqlaqfkvemaEREERQQQV 517
Cdd:PRK02224 575 AELNSKLAELKERIE-SLE-RIRTLLAAIAD--AEDEIERLREKREALAELNDERRERLA-----------EKRERKREL 639
|
410 420 430
....*....|....*....|....*....|....*...
gi 191252785 518 AEDYElrlareQARVCELQSGNQQLEEQRVELVERLQA 555
Cdd:PRK02224 640 EAEFD------EARIEEAREDKERAEEYLEQVEEKLDE 671
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
274-513 |
1.01e-06 |
|
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: 52.07 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 274 QQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRA 353
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 354 ALEEerqtwaqQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAwetqHQLALVQSEVRRLEGELDTARRERDALQlem 433
Cdd:COG4942 98 ELEA-------QKEELAELLRALYRLGRQPPLALLLSPEDFLDAV----RRLQYLKYLAPARREQAEELRADLAELA--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 434 sLVQARYESQRIQLESELAVQLEQRVT-ERLAQAQESSLRQAASLREHHRKQLQDLSGQhQQELASQLAQFKVEMAEREE 512
Cdd:COG4942 164 -ALRAELEAERAELEALLAELEEERAAlEALKAERQKLLARLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAE 241
|
.
gi 191252785 513 R 513
Cdd:COG4942 242 R 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
250-566 |
1.53e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 250 EAERTEVLRGLQEEHQAAELTRSKQQETVTRLEQsLSEAMEALNREQESARLQQR----ERETLEEERQALTLRLEAEQQ 325
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE-AKKAAEAKKKADEAKKAEEAkkadEAKKAEEAKKADEAKKAEEKK 1546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 326 RCcvlQEERDAARAGQLSEHRELETLRAAlEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQL 405
Cdd:PTZ00121 1547 KA---DELKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 406 ALVQ--SEVRRLEGELDTARRE--RDALQL----EMSLVQARYESQRIQLESELAVQL-----EQRVTERLAQAQESSLR 472
Cdd:PTZ00121 1623 EELKkaEEEKKKVEQLKKKEAEekKKAEELkkaeEENKIKAAEEAKKAEEDKKKAEEAkkaeeDEKKAAEALKKEAEEAK 1702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 473 QAASLRehhRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDyELRLAREQARvcELQSGNQQLEEQRVELVER 552
Cdd:PTZ00121 1703 KAEELK---KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE-EAKKDEEEKK--KIAHLKKEEEKKAEEIRKE 1776
|
330
....*....|....
gi 191252785 553 LQAMLQAHWDEANQ 566
Cdd:PTZ00121 1777 KEAVIEEELDEEDE 1790
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
330-553 |
1.92e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 51.98 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 330 LQEERDAARAGQLSEHRELETLRAALEEERQTW--AQQEHQLKEHYQALQEESQAQL--EREKEKSQREAQAAWETQHQL 405
Cdd:PRK10929 32 LEQAKAAKTPAQAEIVEALQSALNWLEERKGSLerAKQYQQVIDNFPKLSAELRQQLnnERDEPRSVPPNMSTDALEQEI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 406 ALVQSEV----RRLEGELDTARRERDALQLemsLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQAASLREHH 481
Cdd:PRK10929 112 LQVSSQLleksRQAQQEQDRAREISDSLSQ---LPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQAESAALKAL 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 191252785 482 RKQLQ--DLSGQHQQElasqLAQFKVEMAEReeRQQQVaeDYELRLAREQarvceLQSGNQQLEEQRVELVERL 553
Cdd:PRK10929 189 VDELElaQLSANNRQE----LARLRSELAKK--RSQQL--DAYLQALRNQ-----LNSQRQREAERALESTELL 249
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
200-402 |
2.02e-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: 51.99 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 200 CERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQETVT 279
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 280 RLEQsLSEAMEALNREQEsaRLQQRERETLEEERQaLTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEER 359
Cdd:TIGR02169 393 KLEK-LKREINELKRELD--RLQEELQRLSEELAD-LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 191252785 360 qtwaQQEHQLKEHYQALQEEsQAQLEREKEKSQREAQAAWETQ 402
Cdd:TIGR02169 469 ----QELYDLKEEYDRVEKE-LSKLQRELAEAEAQARASEERV 506
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
375-567 |
2.47e-06 |
|
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: 50.92 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 375 ALQEESQAQLEREKEKSQREAQAA----WETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQAR---YESQRIQL 447
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELekelAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaeLEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 448 ESELAvQLEQRVTERLAQAQESS--------LRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAE 519
Cdd:COG4942 96 RAELE-AQKEELAELLRALYRLGrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 191252785 520 DYELRLAREQARVCELqsgnQQLEEQRVELVERLQAMLQAHWDEANQL 567
Cdd:COG4942 175 ELEALLAELEEERAAL----EALKAERQKLLARLEKELAELAAELAEL 218
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
190-569 |
3.35e-06 |
|
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: 50.94 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 190 LDSEHTRRKHCERHIQSLQTRVLELQQQLAVAVAADRKKdtmieQLDKTLArvvegwnrhEAErtevLRGLQEEHQAAEL 269
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKL-----QLEKVTT---------EAK----IKKLEEDILLLED 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 270 TRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELE 349
Cdd:pfam01576 146 QNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 350 TLRAALEEERQTWAQQEHQLKEHYQALQEESQAQleREKEKSQREAQAawetqhQLALVQSEVRRLEGELDTARRERDAL 429
Cdd:pfam01576 226 ELQAQIAELRAQLAKKEEELQAALARLEEETAQK--NNALKKIRELEA------QISELQEDLESERAARNKAEKQRRDL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 430 QLEMSLVQARYES--QRIQLESELAVQLEQRVTErLAQAQESSLRQaaslrehHRKQLQDLSGQHQQ---ELASQLAQFK 504
Cdd:pfam01576 298 GEELEALKTELEDtlDTTAAQQELRSKREQEVTE-LKKALEEETRS-------HEAQLQEMRQKHTQaleELTEQLEQAK 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 505 -----------------VEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAmLQAHWDEANQL 567
Cdd:pfam01576 370 rnkanlekakqalesenAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSK-LQSELESVSSL 448
|
..
gi 191252785 568 LS 569
Cdd:pfam01576 449 LN 450
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
185-565 |
6.06e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 185 GLRDALDSEHTRRKHCERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEgwnRHEAERTEVlRGLQEEH 264
Cdd:PRK02224 297 DLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE---RAEELREEA-AELESEL 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 265 QAAELTRSKQQETVTRLEQSLSEAMEALNreqesarlqqreretleeerqALTLRLEAEQQRCCVLQEERDAARAGQLSE 344
Cdd:PRK02224 373 EEAREAVEDRREEIEELEEEIEELRERFG---------------------DAPVDLGNAEDFLEELREERDELREREAEL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 345 HRELETLRAALEEERQTWAQ-------QEHQLKEHYQALQE--ESQAQLEREKEKSqREAQAAWETQHQLAlvqSEVRRL 415
Cdd:PRK02224 432 EATLRTARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEdrERVEELEAELEDL-EEEVEEVEERLERA---EDLVEA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 416 EGELDTARRERDALQLEMSLVQARYESQRIQLES--ELAVQLEQRVTERLAQAQEssLRQAAslrEHHRKQLQDLSGQhQ 493
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEElrERAAELEAEAEEKREAAAE--AEEEA---EEAREEVAELNSK-L 581
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 191252785 494 QELASQLaqfkvEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAmLQAHWDEAN 565
Cdd:PRK02224 582 AELKERI-----ESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRE-LEAEFDEAR 647
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
231-555 |
6.10e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 6.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 231 MIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQETVTRLEQsLSEAMEALNREQESARLQQRERETLE 310
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE-LEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 311 EERQALTLRLEAEQQRccvlqeERDAARAGQLSEH-RELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKE 389
Cdd:COG4717 126 QLLPLYQELEALEAEL------AELPERLEELEERlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 390 KSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARY----ESQRIQLESELAVQLEQRVT----- 460
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliAAALLALLGLGGSLLSLILTiagvl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 461 ---ERLAQAQESSLRQAASLREHHRKQLQDLSGQ---HQQELASQLAQFKVEMAEREERQQQVAEDY-ELRLAREQARVC 533
Cdd:COG4717 280 flvLGLLALLFLLLAREKASLGKEAEELQALPALeelEEEELEELLAALGLPPDLSPEELLELLDRIeELQELLREAEEL 359
|
330 340
....*....|....*....|..
gi 191252785 534 ELQSGNQQLEEQRVELVERLQA 555
Cdd:COG4717 360 EEELQLEELEQEIAALLAEAGV 381
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
196-455 |
6.46e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.12 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 196 RRKHCERHIQSLQTRVLEL--QQQLAVAVAADRKKDTMIEQLDKTLARVvegwnRHEAERTEVLRGLQEEHQAAELTRSK 273
Cdd:pfam17380 346 RERELERIRQEERKRELERirQEEIAMEISRMRELERLQMERQQKNERV-----RQELEAARKVKILEEERQRKIQQQKV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 274 QQETVtRLEQSLSEAMEALNREQESARLQQRERETLEEERQALT-LRLEAEQQRCCVLQ---EERDAARAGQLSE---HR 346
Cdd:pfam17380 421 EMEQI-RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVErLRQQEEERKRKKLElekEKRDRKRAEEQRRkilEK 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 347 ELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEgeldtarrer 426
Cdd:pfam17380 500 ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE---------- 569
|
250 260
....*....|....*....|....*....
gi 191252785 427 dALQLEMSLVQARYESQRIQLESELAVQL 455
Cdd:pfam17380 570 -AMEREREMMRQIVESEKARAEYEATTPI 597
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
182-557 |
7.18e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.97 E-value: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 182 DFQGLRDALDSEHTRRKHCERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVV--------EGWNRHEAER 253
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEiqelqekaESELAKEEIL 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 254 TEVLRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEALNREQEsaRLQQRERETLEEERQALTLRLEAEQQRCCVLQEE 333
Cdd:pfam02463 696 RRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELK--LLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 334 RDAA----RAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQ 409
Cdd:pfam02463 774 KELAeereKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAE 853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 410 SEVRRLEGELdtarrerdaLQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQAASLREHHRKqlqdlS 489
Cdd:pfam02463 854 EELERLEEEI---------TKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE-----I 919
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 191252785 490 GQHQQELASQLAQFKVEmaEREERQQQVAEDYELRLAREQARVcelqsgNQQLEEQRVELVERLQAML 557
Cdd:pfam02463 920 EERIKEEAEILLKYEEE--PEELLLEEADEKEKEENNKEEEEE------RNKRLLLAKEELGKVNLMA 979
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
382-569 |
8.86e-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: 49.68 E-value: 8.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 382 AQLEREKEKSQREAQAAWETQHQLALVQSEVR----RLEGELDTARRERDAL----QLEMSLVQARYES---QRIQLESE 450
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRqqleRLRREREKAERYQALLkekrEYEGYELLKEKEAlerQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 451 LAvQLEQRVTERLAQAQESSLR--QAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMA-------EREERQQQVAE-- 519
Cdd:TIGR02169 246 LA-SLEEELEKLTEEISELEKRleEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAslersiaEKERELEDAEErl 324
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 191252785 520 -DYELRLAREQARVCELQsgnQQLEEQRVElVERLQAMLQAHWDEANQLLS 569
Cdd:TIGR02169 325 aKLEAEIDKLLAEIEELE---REIEEERKR-RDKLTEEYAELKEELEDLRA 371
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
255-530 |
1.01e-05 |
|
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: 49.57 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 255 EVLRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEALnreQESARLQqreretleeeRQALTLRLEAEQQRCCVLQEER 334
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQL---QLLNKLL----------PQANLLADETLADRLEELREEL 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 335 DAARAGQ--LSEH----RELETLRAALeeerQTWAQQEHQLKEHYQAL---QEESQAQLEREKEKSQREAQAAWE-TQHQ 404
Cdd:COG3096 903 DAAQEAQafIQQHgkalAQLEPLVAVL----QSDPEQFEQLQADYLQAkeqQRRLKQQIFALSEVVQRRPHFSYEdAVGL 978
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 405 LALVQSEVRRLEGELDTARRERDALQLEMSLVQARYES---QRIQLES------ELAVQLEQRVTERLAQAQESSLRQAA 475
Cdd:COG3096 979 LGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQynqVLASLKSsrdakqQTLQELEQELEELGVQADAEAEERAR 1058
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 191252785 476 SlrehHRKQLQDLSGQHQQ---ELASQLAQFKVEMAEREERQQQVAEDYelRLAREQA 530
Cdd:COG3096 1059 I----RRDELHEELSQNRSrrsQLEKQLTRCEAEMDSLQKRLRKAERDY--KQEREQV 1110
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
190-556 |
1.08e-05 |
|
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: 49.40 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 190 LDSEHTRRKhCERHIQSLQTRVLELQQQLAVAVAADRKKDtmiEQLDKTLARVVEgwnrHEAERTEVLRGLQE-EHQAAE 268
Cdd:pfam01576 204 QELEKAKRK-LEGESTDLQEQIAELQAQIAELRAQLAKKE---EELQAALARLEE----ETAQKNNALKKIRElEAQISE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 269 LTRSKQQETVTR-----LEQSLSEAMEALNREQESarlqqreretleeerqalTLRLEAEQQRccvLQEERDaaragqls 343
Cdd:pfam01576 276 LQEDLESERAARnkaekQRRDLGEELEALKTELED------------------TLDTTAAQQE---LRSKRE-------- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 344 ehRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTAR 423
Cdd:pfam01576 327 --QEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 424 RERDALQLEMSLVQARY---ESQRIQLESELA-VQLE-QRVTERLAQAQESSLRQAASLREHHrKQLQDLSGQHQQE--- 495
Cdd:pfam01576 405 HKRKKLEGQLQELQARLsesERQRAELAEKLSkLQSElESVSSLLNEAEGKNIKLSKDVSSLE-SQLQDTQELLQEEtrq 483
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 191252785 496 ---LASQLAQFKvemAEREERQQQVAEDYELRLAREQarvcELQSGNQQLEEQRVELVERLQAM 556
Cdd:pfam01576 484 klnLSTRLRQLE---DERNSLQEQLEEEEEAKRNVER----QLSTLQAQLSDMKKKLEEDAGTL 540
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
237-559 |
1.10e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.58 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 237 KTLARVVEGWNRHEAERTEVLRGLQ-EEHQAAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQA 315
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELkLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 316 LTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTwAQQEHQLKEHYQALQEESQAQLER-EKEKSQRE 394
Cdd:pfam02463 256 SKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE-LLKLERRKVDDEEKLKESEKEKKKaEKELKKEK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 395 AQAAwETQHQLALVQ-SEVRRLEGELDTARRERDALQLEMSLV--QARYESQRIQLESELAVQLEQRVTE--------RL 463
Cdd:pfam02463 335 EEIE-ELEKELKELEiKREAEEEEEEELEKLQEKLEQLEEELLakKKLESERLSSAAKLKEEELELKSEEekeaqlllEL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 464 AQAQESSLR----QAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRL-AREQARVCELQSG 538
Cdd:pfam02463 414 ARQLEDLLKeekkEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLvKLQEQLELLLSRQ 493
|
330 340
....*....|....*....|.
gi 191252785 539 NQQLEEQRVELVERLQAMLQA 559
Cdd:pfam02463 494 KLEERSQKESKARSGLKVLLA 514
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
260-473 |
1.14e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 260 LQEEHQAAEltrsKQQETVTRLEQsLSEAMEALNREQESARLQQReretleeerQALTLRLEAEQQRCCVLQEERDAARA 339
Cdd:COG4913 237 LERAHEALE----DAREQIELLEP-IRELAERYAAARERLAELEY---------LRAALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 340 gqlsehrELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLER-EKEKSQREAQAAwETQHQLALVQSEVRRLEGE 418
Cdd:COG4913 303 -------ELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELE-ERERRRARLEALLAALGLP 374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 191252785 419 LDTARRERDALQLEMSLVQARYESQRIQLESELAvqlEQRVTERLAQAQESSLRQ 473
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALA---EAEAALRDLRRELRELEA 426
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
197-560 |
1.21e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.20 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 197 RKHCERHIQSLQTRVLELQQQLA--VAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQ 274
Cdd:TIGR00618 306 EQQAQRIHTELQSKMRSRAKLLMkrAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 275 Q--ETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLR 352
Cdd:TIGR00618 386 QqkTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESA 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 353 AALEEERQTWAQQE---------HQLKEHYQALQEESQAQLEREKEKSQREAQAAWET----------QHQLALVQSEVR 413
Cdd:TIGR00618 466 QSLKEREQQLQTKEqihlqetrkKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPgpltrrmqrgEQTYAQLETSEE 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 414 RLEGELDTARRERDALQLEMSLVQ-------------------ARYESQRIQ----LESELAVQLEQRVTERLAQAQESS 470
Cdd:TIGR00618 546 DVYHQLTSERKQRASLKEQMQEIQqsfsiltqcdnrskedipnLQNITVRLQdlteKLSEAEDMLACEQHALLRKLQPEQ 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 471 LRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQvaedyELRLAREQARVCELQSGNQQLEEQRVELV 550
Cdd:TIGR00618 626 DLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLP-----KELLASRQLALQKMQSEKEQLTYWKEMLA 700
|
410
....*....|
gi 191252785 551 ERLQAMLQAH 560
Cdd:TIGR00618 701 QCQTLLRELE 710
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
187-463 |
1.35e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 187 RDALDSEHTRRK---HCERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARvvegwnrHEAERTEVLRGLQEE 263
Cdd:PRK02224 491 VEEVEERLERAEdlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE-------LEAEAEEKREAAAEA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 264 HQAAELTRSKQQETVTRLEQsLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDaaragqls 343
Cdd:PRK02224 564 EEEAEEAREEVAELNSKLAE-LKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRE-------- 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 344 EHRELEtlrAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAawetqhqlalVQSEVRRLEgeldTAR 423
Cdd:PRK02224 635 RKRELE---AEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGA----------VENELEELE----ELR 697
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 191252785 424 RERDALQLEMSLVQARYESQRiQLES---ELAVQLEQRVTERL 463
Cdd:PRK02224 698 ERREALENRVEALEALYDEAE-ELESmygDLRAELRQRNVETL 739
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
183-567 |
1.36e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 183 FQGLRDALDSEHTRRKhcerhIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVL----R 258
Cdd:COG4913 274 LEYLRAALRLWFAQRR-----LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLereiE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 259 GLQEEHQAAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCC----VLQEER 334
Cdd:COG4913 349 RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRrelrELEAEI 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 335 DAARAGQLSEHRELETLRAALEE-----------------------------ER-------------------------- 359
Cdd:COG4913 429 ASLERRKSNIPARLLALRDALAEalgldeaelpfvgelievrpeeerwrgaiERvlggfaltllvppehyaaalrwvnrl 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 360 ---------------------------------------QTWAQQEhqLKEHYQALQEESQAQLEREK------------ 388
Cdd:COG4913 509 hlrgrlvyervrtglpdperprldpdslagkldfkphpfRAWLEAE--LGRRFDYVCVDSPEELRRHPraitragqvkgn 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 389 ----EKSQREAQAA-----WETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYES-QRIQLESELAVQLEQ- 457
Cdd:COG4913 587 gtrhEKDDRRRIRSryvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlQRLAEYSWDEIDVASa 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 458 -----RVTERLAQAQESS--LRQAASLREHHRKQLQDLSGQhQQELASQLAQFKVEMAEREERQQQV---AEDYELRLAR 527
Cdd:COG4913 667 ereiaELEAELERLDASSddLAALEEQLEELEAELEELEEE-LDELKGEIGRLEKELEQAEEELDELqdrLEAAEDLARL 745
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 191252785 528 EQARVCELQSGNQQLEEQRVELVERLQAMLQAHWDEANQL 567
Cdd:COG4913 746 ELRALLEERFAAALGDAVERELRENLEERIDALRARLNRA 785
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
261-552 |
1.73e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 261 QEEHQAAELTRSKQQETVTRLEQS---------------------------LSEAMEALNREQESARLQQRERETLEEER 313
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAeekaeaaekkkeeakkkadaakkkaeeKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 314 QALTLRLEAEQQRCC-----VLQEERDAARAGQLSEH-RELETLRAALEEERQTwaqQEHQLKEHYQALQEESQAQLERE 387
Cdd:PTZ00121 1419 KADEAKKKAEEKKKAdeakkKAEEAKKADEAKKKAEEaKKAEEAKKKAEEAKKA---DEAKKKAEEAKKADEAKKKAEEA 1495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 388 KEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSlvQARYESQRIQLESELAVQLEQRVTERLAQAQ 467
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA--EEKKKADELKKAEELKKAEEKKKAEEAKKAE 1573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 468 E---SSLRQAASLREHHRKQLQDLSGQHQQElasqlAQFKVEMAEREERQQQVAEdyELRLAREQARVCELQSGNQQLEE 544
Cdd:PTZ00121 1574 EdknMALRKAEEAKKAEEARIEEVMKLYEEE-----KKMKAEEAKKAEEAKIKAE--ELKKAEEEKKKVEQLKKKEAEEK 1646
|
....*...
gi 191252785 545 QRVELVER 552
Cdd:PTZ00121 1647 KKAEELKK 1654
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
94-699 |
2.50e-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: 48.19 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 94 KHIFEMESVRGQLQTMLQTSRDTaYRDPL------IPGAGSE----RREEDSFDSDStATLLNT--RPLQDLSPSSSAQA 161
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRM-YEDKIeelekqLVLANSElteaRTERDQFSQES-GNLDDQlqKLLADLHKREKELS 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 162 LEE-----LFPRYTSlrpgpplNPPDFQGLRDALDSEHTRRKHCERHIQSLQTrvlELQQQLAVAVAADRKKDTMIEQLD 236
Cdd:pfam15921 395 LEKeqnkrLWDRDTG-------NSITIDHLRRELDDRNMEVQRLEALLKAMKS---ECQGQMERQMAAIQGKNESLEKVS 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 237 KTLARVvegwnrheAERTEVLRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEALnrEQESARLQQRERETLEEERQAL 316
Cdd:pfam15921 465 SLTAQL--------ESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAI--EATNAEITKLRSRVDLKLQELQ 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 317 TLRLEAEQQRCcvLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKehyqALQEEsQAQLEREKEKSQREAQ 396
Cdd:pfam15921 535 HLKNEGDHLRN--VQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAG----AMQVE-KAQLEKEINDRRLELQ 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 397 aawetqhqlalvqsEVRRLEGELDTARRERDA----LQLE-MSLVQAryESQRIQLESELAVQLEQRVTErlAQAQESSL 471
Cdd:pfam15921 608 --------------EFKILKDKKDAKIRELEArvsdLELEkVKLVNA--GSERLRAVKDIKQERDQLLNE--VKTSRNEL 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 472 RQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQ-------------QVAEDYELRLAREQARVCELQSG 538
Cdd:pfam15921 670 NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNtlksmegsdghamKVAMGMQKQITAKRGQIDALQSK 749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 539 NQQLEEQRVElVERLQAMLQAHWDEANQLLSTTlpPPNPPAPPAGPSSPGPQEPEKEERrvwtMPPMAVALKPVLQQSRE 618
Cdd:pfam15921 750 IQFLEEAMTN-ANKEKHFLKEEKNKLSQELSTV--ATEKNKMAGELEVLRSQERRLKEK----VANMEVALDKASLQFAE 822
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 619 ARD----ELPGAPPVLCSSSSDLSLLLGPSFQSQHSFQPLEPKP---DLTSSTAGAFSALGAFHPDHRAERPFPEEDPGP 691
Cdd:pfam15921 823 CQDiiqrQEQESVRLKLQHTLDVKELQGPGYTSNSSMKPRLLQPasfTRTHSNVPSSQSTASFLSHHSRKTNALKEDPTR 902
|
....*...
gi 191252785 692 DGEGLLKQ 699
Cdd:pfam15921 903 DLKQLLQE 910
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
381-566 |
2.54e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 381 QAQLEREKEKSqREAQAAWE---TQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAV---- 453
Cdd:COG3206 181 EEQLPELRKEL-EEAEAALEefrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAlpel 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 454 ---QLEQRVTERLAQAQESSLRQAASLREHH------RKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEdyelR 524
Cdd:COG3206 260 lqsPVIQQLRAQLAELEAELAELSARYTPNHpdvialRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQA----Q 335
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 191252785 525 LAREQARVCELQSGNQQLE--EQRVELVERLQAMLQAHWDEANQ 566
Cdd:COG3206 336 LAQLEARLAELPELEAELRrlEREVEVARELYESLLQRLEEARL 379
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
377-559 |
2.60e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 377 QEESQAQLEREKEKSQREAQAAWEtqhQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLE 456
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQA---ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 457 QRVT----ERLAQAQESS--LRQAASLR---EHHRKQLQDlsgqhQQELASQLAQFKVEMAEREERQQQVAEDYELRLAR 527
Cdd:COG3883 98 SGGSvsylDVLLGSESFSdfLDRLSALSkiaDADADLLEE-----LKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190
....*....|....*....|....*....|..
gi 191252785 528 EQARVCELQSGNQQLEEQRVELVERLQAMLQA 559
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
213-488 |
2.78e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 213 ELQQQLAVAVAADRKKdtmIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEAL 292
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKK---AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 293 NREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARagqlsEHRELETLRAALEEERqtwaQQEHQLKEh 372
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE-----DKKKAEEAKKAEEDEK----KAAEALKK- 1696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 373 yqalQEESQAQLEREKEKSQREAQAAWETQHqlalvQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELA 452
Cdd:PTZ00121 1697 ----EAEEAKKAEELKKKEAEEKKKAEELKK-----AEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
250 260 270
....*....|....*....|....*....|....*.
gi 191252785 453 VQLEQRVTERLAQAQESSLRQAASLREHHRKQLQDL 488
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDI 1803
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
205-415 |
3.32e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 205 QSLQTRVLELQQQLAVAVAADRKkdtmIEQLDKTLARVVEGWNRHEAERT--EVLRGLQEE-HQAAELTRSKQQetVTRL 281
Cdd:PRK04863 452 QEATEELLSLEQKLSVAQAAHSQ----FEQAYQLVRKIAGEVSRSEAWDVarELLRRLREQrHLAEQLQQLRMR--LSEL 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 282 EQSLSEAMEAlNREQESARLQQRERETLEEERQALTLRLEAEQQRccvLQEERDAARAGQLSEHRELETLRAALEEERQT 361
Cdd:PRK04863 526 EQRLRQQQRA-ERLLAEFCKRLGKNLDDEDELEQLQEELEARLES---LSESVSEARERRMALRQQLEQLQARIQRLAAR 601
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 191252785 362 wAQQEHQLKEHYQALQEES--------------QAQLEREKEKSQREAQAAWETQHqlalVQSEVRRL 415
Cdd:PRK04863 602 -APAWLAAQDALARLREQSgeefedsqdvteymQQLLERERELTVERDELAARKQA----LDEEIERL 664
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
213-444 |
4.40e-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: 46.68 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 213 ELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAErtevLRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEAL 292
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 293 NREQESARlQQRERETLEEERQALTLRLEAEQqrccVLQEERDAARAGQLSEHR--ELETLRAALEEERQTWAQQEHQLK 370
Cdd:COG4942 100 EAQKEELA-ELLRALYRLGRQPPLALLLSPED----FLDAVRRLQYLKYLAPARreQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 191252785 371 EHYQALQEESQAQLEREKEKSQREAqaawetqhQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQR 444
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQK--------LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
344-568 |
4.71e-05 |
|
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: 47.25 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 344 EHRELETLRAALEEERQTWAQQEHQLKEHYQALQ----------EESQAQLEREKEksqREAQAAWETQHQLALVQSEVR 413
Cdd:COG3096 844 RRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNkllpqanllaDETLADRLEELR---EELDAAQEAQAFIQQHGKALA 920
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 414 RLEGELDTARR---ERDALQLEMSLVQARYESQRIQLESelAVQLEQRVT--------ERLAQAQESS------LRQAAS 476
Cdd:COG3096 921 QLEPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIFA--LSEVVQRRPhfsyedavGLLGENSDLNeklrarLEQAEE 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 477 LREHHRKQLQDLSGQHQ---QELAS----------QLAQFKVEMAEREERQQQVAEdyelrlAREQARVCELQSGNQQLE 543
Cdd:COG3096 999 ARREAREQLRQAQAQYSqynQVLASlkssrdakqqTLQELEQELEELGVQADAEAE------ERARIRRDELHEELSQNR 1072
|
250 260
....*....|....*....|....*
gi 191252785 544 EQRVELvERLQAMLQAHWDEANQLL 568
Cdd:COG3096 1073 SRRSQL-EKQLTRCEAEMDSLQKRL 1096
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
186-519 |
5.31e-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: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 186 LRDALDSEHTRRKH-CERHIQSLQTRVLELQQQLAvavaadrKKDTMIEQLDKTLARVVEgwnRHEAERTEVLRGLQEEH 264
Cdd:TIGR02169 220 KREYEGYELLKEKEaLERQKEAIERQLASLEEELE-------KLTEEISELEKRLEEIEQ---LLEELNKKIKDLGEEEQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 265 QAAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAgqlse 344
Cdd:TIGR02169 290 LRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE----- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 345 hrELETLRAALEEERqtwaqqehqlKEHYQALQEESQAQLEREKEKSQREaqaawETQHQLALVQSEVRRLEGELdtarr 424
Cdd:TIGR02169 365 --ELEDLRAELEEVD----------KEFAETRDELKDYREKLEKLKREIN-----ELKRELDRLQEELQRLSEEL----- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 425 erdaLQLEMSLvqARYESQRIQLESEL-AVQLEQRvterlaqAQESSLRQAASLREHHRKQLQDLSgQHQQELASQLAQF 503
Cdd:TIGR02169 423 ----ADLNAAI--AGIEAKINELEEEKeDKALEIK-------KQEWKLEQLAADLSKYEQELYDLK-EEYDRVEKELSKL 488
|
330
....*....|....*.
gi 191252785 504 KVEMAEREERQQQVAE 519
Cdd:TIGR02169 489 QRELAEAEAQARASEE 504
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
201-557 |
5.62e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 201 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARV--VEGWNRHEAERTEVLRGLQEEHQAAEltrSKQQETV 278
Cdd:PRK04863 382 EARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALerAKQLCGLPDLTADNAEDWLEEFQAKE---QEATEEL 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 279 TRLEQSLSEAMEALNREQESARLQQreretleeerqaltlRLEAEQQRccvlQEERDAARagqlsehrelETLRAAleEE 358
Cdd:PRK04863 459 LSLEQKLSVAQAAHSQFEQAYQLVR---------------KIAGEVSR----SEAWDVAR----------ELLRRL--RE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 359 RQTWAQQEHQLKEHYQALQEESQAQleREKEKSQREAQAAWETQHQLAlvqSEVRRLEGELDTarrERDALQLEMSLVQA 438
Cdd:PRK04863 508 QRHLAEQLQQLRMRLSELEQRLRQQ--QRAERLLAEFCKRLGKNLDDE---DELEQLQEELEA---RLESLSESVSEARE 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 439 RYESQRIQLEselavQLEQRVTERLAQAQESSLRQAASlrehhrKQLQDLSGQHqQELASQLAQFKVEMAEREERQQQVA 518
Cdd:PRK04863 580 RRMALRQQLE-----QLQARIQRLAARAPAWLAAQDAL------ARLREQSGEE-FEDSQDVTEYMQQLLERERELTVER 647
|
330 340 350
....*....|....*....|....*....|....*....
gi 191252785 519 EDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAML 557
Cdd:PRK04863 648 DELAARKQALDEEIERLSQPGGSEDPRLNALAERFGGVL 686
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
402-563 |
6.08e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 402 QHQLALVQSEVRRLEGELDTARRERDALQLEmsLVQARYESQRIQLESELAVQLEQRVTERLAQAqeSSLRQAASLR--- 478
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTE--LEDLEKEIKRLELEIEEVEARIKKYEEQLGNV--RNNKEYEALQkei 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 479 EHHRKQLQDLSgQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARVCELQSGNQQLEEQRVELVERLQAMLQ 558
Cdd:COG1579 99 ESLKRRISDLE-DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELL 177
|
....*
gi 191252785 559 AHWDE 563
Cdd:COG1579 178 ALYER 182
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
188-546 |
9.25e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 188 DALDSEHTRRKHCERHIQSlqTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAA 267
Cdd:PTZ00121 1138 DARKAEEARKAEDAKRVEI--ARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAE 1215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 268 ELTR---SKQQETVTRLEQSLSEAMEALNREQ----------ESARLQQRERETLEEERQ----ALTLRlEAEqqrccvl 330
Cdd:PTZ00121 1216 EARKaedAKKAEAVKKAEEAKKDAEEAKKAEEernneeirkfEEARMAHFARRQAAIKAEearkADELK-KAE------- 1287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 331 qEERDAARAGQLSEHRELETLRAALEEERQTwaqqehqlkehyqalqEESQAQLEREKEKSQREAQAAWETQHQLALVQS 410
Cdd:PTZ00121 1288 -EKKKADEAKKAEEKKKADEAKKKAEEAKKA----------------DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKA 1350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 411 EVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLEselavqlEQRVTERLAQAQESSLRQAASLR--EHHRKQLQDL 488
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE-------EKKKADEAKKKAEEDKKKADELKkaAAAKKKADEA 1423
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 191252785 489 SGQHQQELASQLAQFKVEMAEREERQQQVAEDY----ELRLAREQARVCElqSGNQQLEEQR 546
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkaeEAKKKAEEAKKAD--EAKKKAEEAK 1483
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
260-541 |
9.78e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.20 E-value: 9.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 260 LQEEHQAAELTRSKQQE---------TVTRLEQSLSEAMEALNreqESARLQQRERETLEEERQALTLRLEAEQQRCCVL 330
Cdd:PRK10929 112 LQVSSQLLEKSRQAQQEqdrareisdSLSQLPQQQTEARRQLN---EIERRLQTLGTPNTPLAQAQLTALQAESAALKAL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 331 QEERDAAragQLSEH--RELETLRAALEEERQtwaqqeHQLKEHYQALQEESQAQlerekekSQREAQAAWETQHQLAlv 408
Cdd:PRK10929 189 VDELELA---QLSANnrQELARLRSELAKKRS------QQLDAYLQALRNQLNSQ-------RQREAERALESTELLA-- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 409 qsevrrlEGELDTARRERDALQLEMSLVQA-RYESQRIQLeseLAVQleqrvtERLAQAQESSLRQAAS-LREHH----- 481
Cdd:PRK10929 251 -------EQSGDLPKSIVAQFKINRELSQAlNQQAQRMDL---IASQ------QRQAASQTLQVRQALNtLREQSqwlgv 314
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 191252785 482 --------RKQLQDLSGQHQ-QELASQLAQFKV------EMAEREERQQQVAEDYELRLAREQARVCELQSGNQQ 541
Cdd:PRK10929 315 snalgealRAQVARLPEMPKpQQLDTEMAQLRVqrlryeDLLNKQPQLRQIRQADGQPLTAEQNRILDAQLRTQR 389
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
186-514 |
1.02e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.37 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 186 LRDALDSEHTRRKHCERHIQSLQTRVLELQQQLAVAVAAdrkkdtmIEQLDKTLARVVegwNRHEAERTEVLRGLQEEHQ 265
Cdd:pfam12128 609 AEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA-------LKNARLDLRRLF---DEKQSEKDKKNKALAERKD 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 266 AAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETL---------EEERQALTLRLEAEQQRCCVLQEERDA 336
Cdd:pfam12128 679 SANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVvegaldaqlALLKAAIAARRSGAKAELKALETWYKR 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 337 ARAGQ-------LSEHRELETLRAALEEErqtwAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQ 409
Cdd:pfam12128 759 DLASLgvdpdviAKLKREIRTLERKIERI----AVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLI 834
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 410 SEVRRLEGELDTARRERDALQLEMS--LVQARYESQRIQL--ESELAVQLEQRVTERLAQAQEsSLRQAASLREHHRKQL 485
Cdd:pfam12128 835 ADTKLRRAKLEMERKASEKQQVRLSenLRGLRCEMSKLATlkEDANSEQAQGSIGERLAQLED-LKLKRDYLSESVKKYV 913
|
330 340
....*....|....*....|....*....
gi 191252785 486 QDLSGQHQQELASQLAQFKVEMAEREERQ 514
Cdd:pfam12128 914 EHFKNVIADHSGSGLAETWESLREEDHYQ 942
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
182-476 |
1.09e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 182 DFQGLRDALDSEHTRRKHCERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQ 261
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 262 ------EEHQAAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERD 335
Cdd:COG4717 280 flvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 336 AARAGQLSEHRELETLRAALE-------EERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQhqLALV 408
Cdd:COG4717 360 EEELQLEELEQEIAALLAEAGvedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEE--LEEL 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 409 QSEVRRLEGELDTARRERDALQLEMSLV---------QARYESQRIQLESE--------LAVQLEQRVTERLAQAQESSL 471
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLeedgelaelLQELEELKAELRELaeewaalkLALELLEEAREEYREERLPPV 517
|
....*
gi 191252785 472 RQAAS 476
Cdd:COG4717 518 LERAS 522
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
207-439 |
1.48e-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: 45.83 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 207 LQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEhqaaeltrSKQQETVTRLEQSLS 286
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEE--------RKRRDKLTEEYAELK 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 287 EAMEALNREQESarlqqreretLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQTWAQQE 366
Cdd:TIGR02169 364 EELEDLRAELEE----------VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 191252785 367 HQLKEhYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQAR 439
Cdd:TIGR02169 434 AKINE-LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
193-429 |
1.64e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 193 EHTRRKHCERHIQSLqtRVLELQQQLAVAVAADRKKDTMIEQLDKTlarvvegwnRHEAERTEVLRGLQEEHQAAELTRS 272
Cdd:PTZ00121 1572 AEEDKNMALRKAEEA--KKAEEARIEEVMKLYEEEKKMKAEEAKKA---------EEAKIKAEELKKAEEEKKKVEQLKK 1640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 273 KQQETVTRLEQSLSEamealnREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAaragqlSEHRELETLR 352
Cdd:PTZ00121 1641 KEAEEKKKAEELKKA------EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA------EEAKKAEELK 1708
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 191252785 353 AALEEERQTwAQQEHQLKEHYQALQEesqaQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDAL 429
Cdd:PTZ00121 1709 KKEAEEKKK-AEELKKAEEENKIKAE----EAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
378-567 |
2.12e-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: 45.05 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 378 EESQAQLEREKEKSQREAQaawetqhqLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLeSELAVQLEQ 457
Cdd:TIGR02168 667 KTNSSILERRREIEELEEK--------IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI-SALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 458 rvterlAQAQESSLRQAASLREHHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVaEDYELRLAREQARVCELQS 537
Cdd:TIGR02168 738 ------LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI-EQLKEELKALREALDELRA 810
|
170 180 190
....*....|....*....|....*....|
gi 191252785 538 GNQQLEEQRVELVERLQAMLQAHWDEANQL 567
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRL 840
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
314-570 |
2.81e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.96 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 314 QALTLRLEAEQQrccVLQEERDAARAGQLSEHRELETLRAALEEERQT--WAQQEHQLKEHYQALQEESQAQLEREKEKS 391
Cdd:TIGR00618 197 ELLTLRSQLLTL---CTPCMPDTYHERKQVLEKELKHLREALQQTQQShaYLTQKREAQEEQLKKQQLLKQLRARIEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 392 QREA-------------QAAWETQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQR 458
Cdd:TIGR00618 274 AQEAvleetqerinrarKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 459 VTERLAQAQESSLR-----QAASLREHHRKQLQDLSGQHQQE--LASQLAQFKVEMA--------EREERQQQVAEDYEL 523
Cdd:TIGR00618 354 EIHIRDAHEVATSIreiscQQHTLTQHIHTLQQQKTTLTQKLqsLCKELDILQREQAtidtrtsaFRDLQGQLAHAKKQQ 433
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 191252785 524 RLAREQARVCELQSGNQQLEEQrveLVERLQAMLQAHWDEANQLLST 570
Cdd:TIGR00618 434 ELQQRYAELCAAAITCTAQCEK---LEKIHLQESAQSLKEREQQLQT 477
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
201-398 |
2.99e-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: 43.98 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 201 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLArvvegwnRHEAERTEVLRGLQEEHQAAELTRSKQQETVTR 280
Cdd:COG4942 61 ERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE-------AQKEELAELLRALYRLGRQPPLALLLSPEDFLD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 281 LEQSLsEAMEALNREQESarlQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELETLRAALEEERQ 360
Cdd:COG4942 134 AVRRL-QYLKYLAPARRE---QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209
|
170 180 190
....*....|....*....|....*....|....*...
gi 191252785 361 TWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAA 398
Cdd:COG4942 210 ELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
201-461 |
3.01e-04 |
|
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: 44.94 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 201 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQ-------LDKTLARVVEGWNRHEAERTEVLRGLQEEHQAAELTRSK 273
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQlkeqlqlLNKLLPQANLLADETLADRLEELREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 274 QQETVTRLEQSLSeameALNREQES-ARLQQreretleeERQALTLRLEAEQQRCCVLQE--ERDAA-----RAGQLSEH 345
Cdd:COG3096 915 HGKALAQLEPLVA----VLQSDPEQfEQLQA--------DYLQAKEQQRRLKQQIFALSEvvQRRPHfsyedAVGLLGEN 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 346 REL-ETLRAALEEERQTWAQQEHQLKehyQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARR 424
Cdd:COG3096 983 SDLnEKLRARLEQAEEARREAREQLR---QAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARI 1059
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 191252785 425 ERDALQLEMSLVQAR---YESQRIQLESELAvQLEQRVTE 461
Cdd:COG3096 1060 RRDELHEELSQNRSRrsqLEKQLTRCEAEMD-SLQKRLRK 1098
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
186-571 |
3.05e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 186 LRDALDSEHTRRKHCERHIQSLQTRVLELQQQLAvavaadrKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRglQEEHQ 265
Cdd:TIGR00618 443 CAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ-------TKEQIHLQETRKKAVVLARLLELQEEPCPLCG--SCIHP 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 266 AAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEH 345
Cdd:TIGR00618 514 NPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNIT 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 346 RELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLErEKEKSQREAQA-AWETQHQLALVQSEVR------RLEGE 418
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLH-LQQCSQELALKlTALHALQLTLTQERVRehalsiRVLPK 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 419 LDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQAAslrehhrkQLQDLSGQ---HQQE 495
Cdd:TIGR00618 673 ELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSS--------LGSDLAARedaLNQS 744
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 191252785 496 LASQLAQFKVEMAEREERQQQVAEDY---ELRLAREQARVCELQSGNQQLEEqRVELVERLQAMLQAHWDEANQLLSTT 571
Cdd:TIGR00618 745 LKELMHQARTVLKARTEAHFNNNEEVtaaLQTGAELSHLAAEIQFFNRLREE-DTHLLKTLEAEIGQEIPSDEDILNLQ 822
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
250-549 |
3.13e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.79 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 250 EAERTEVLRGLQ----EEHQAAELTRSKQQET--VTRLEqslsEAMEALNREQESARLQQRERETLEEERQALTLRLEAE 323
Cdd:PRK10246 215 PEQVQSLTASLQvltdEEKQLLTAQQQQQQSLnwLTRLD----ELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPAR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 324 QQRCCVL-QEERDAARAGQLSEHRELET-LRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWET 401
Cdd:PRK10246 291 QLRPHWErIQEQSAALAHTRQQIEEVNTrLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNNELAGWRA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 402 Q-HQLALVQSEVRRLEGELDTARRERDAL-QLEMSLVqaryesqriqlESELAVQLEQRVTERLAQAQESSLRQAASLRE 479
Cdd:PRK10246 371 QfSQQTSDREQLRQWQQQLTHAEQKLNALpAITLTLT-----------ADEVAAALAQHAEQRPLRQRLVALHGQIVPQQ 439
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 480 HHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAedyelrlarEQARVCELQSGNQQLEEQRVEL 549
Cdd:PRK10246 440 KRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLA---------DVKTICEQEARIKDLEAQRAQL 500
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
404-532 |
5.60e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 43.30 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 404 QLALVQSEVRRLEGELDTARRERDALQ-------------LEMSLVqARYESQRIQLESELAvQLEQRVTE---RLAQAQ 467
Cdd:COG3524 178 AVRFAEEEVERAEERLRDAREALLAFRnrngildpeataeALLQLI-ATLEGQLAELEAELA-ALRSYLSPnspQVRQLR 255
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 191252785 468 esslRQAASLREHHRKQLQDLSGQHQQE-LASQLAQFKVEMAEREERQQQvaedYELRLAR-EQARV 532
Cdd:COG3524 256 ----RRIAALEKQIAAERARLTGASGGDsLASLLAEYERLELEREFAEKA----YTSALAAlEQARI 314
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
242-398 |
6.58e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 242 VVEGWNRHE-----AERTEVLRGLQEEHQAAELtRSKQQETVTRLEQslseamealnREQESARLQQRERETLEEERQAL 316
Cdd:PRK09510 60 VVEQYNRQQqqqksAKRAEEQRKKKEQQQAEEL-QQKQAAEQERLKQ----------LEKERLAAQEQKKQAEEAAKQAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 317 TLRLEAEQQRccvlQEERDAARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQA---LQEESQAQLERE-KEKSQ 392
Cdd:PRK09510 129 LKQKQAEEAA----AKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAkkkAEAEAAAKAAAEaKKKAE 204
|
....*.
gi 191252785 393 REAQAA 398
Cdd:PRK09510 205 AEAKKK 210
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
330-467 |
9.50e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.44 E-value: 9.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 330 LQEERDAARAGQLSEHRELETLRAALEEerqtwaqqehqLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQ 409
Cdd:pfam09787 52 LRQERDLLREEIQKLRGQIQQLRTELQE-----------LEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQ 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 191252785 410 SEVRRLEGELdtaRRERDALQLEMSLVQARYESQRIQL---------ESELAVQLEQrVTERLAQAQ 467
Cdd:pfam09787 121 EELRYLEEEL---RRSKATLQSRIKDREAEIEKLRNQLtsksqssssQSELENRLHQ-LTETLIQKQ 183
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
193-546 |
1.07e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 193 EHTRRKHCERHIQSLQtRVLELQQQLAVAVAADRKKDT-----MIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAA 267
Cdd:PTZ00121 1215 EEARKAEDAKKAEAVK-KAEEAKKDAEEAKKAEEERNNeeirkFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 268 ELTRSKQQETVTRLEQSLSEAMEA--LNREQESARlqqreretleeeRQALTLRLEAEqqrccvlqEERDAARAGQLSEH 345
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKAdeAKKKAEEAK------------KKADAAKKKAE--------EAKKAAEAAKAEAE 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 346 RELETLRAALEEERQTWAQQEhqlkehyqalQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGEldtaRRE 425
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKE----------EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA----KKK 1419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 426 RDALQLEMSLVQARYESQRIQLESELAVQLEQRVTErlAQAQESSLRQAASLR--EHHRKQLQDLSGQHQQELASQLAQF 503
Cdd:PTZ00121 1420 ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEE--AKKAEEAKKKAEEAKkaDEAKKKAEEAKKADEAKKKAEEAKK 1497
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 191252785 504 KVEMAEREERQQQVAEdyELRLAREQARVCELQSGnqqlEEQR 546
Cdd:PTZ00121 1498 KADEAKKAAEAKKKAD--EAKKAEEAKKADEAKKA----EEAK 1534
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
221-556 |
1.24e-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: 42.85 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 221 AVAADRKKDTMIEQLDKTLARVVEgwNRHEAERTEvlRGLQEEHQaaELTRSKqqETVTRLEQSLSEAMEALNREQESAR 300
Cdd:pfam01576 627 AEAEAREKETRALSLARALEEALE--AKEELERTN--KQLRAEME--DLVSSK--DDVGKNVHELERSKRALEQQVEEMK 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 301 LQQRERETLEEERQALTLRLEAEQQRCCVlQEERD-AARAGQLSEHReletlRAALEEERQTWAQQEHQLKEHYQALQEE 379
Cdd:pfam01576 699 TQLEELEDELQATEDAKLRLEVNMQALKA-QFERDlQARDEQGEEKR-----RQLVKQVRELEAELEDERKQRAQAVAAK 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 380 SQAQLEREKEKSQREA--QAAWETQHQLALVQSEVRRLEGELDTARRERDALqlemsLVQAR--------YESQRIQLES 449
Cdd:pfam01576 773 KKLELDLKELEAQIDAanKGREEAVKQLKKLQAQMKDLQRELEEARASRDEI-----LAQSKesekklknLEAELLQLQE 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 450 ELAV---QLEQRVTER--LAQAQESSLRQAASLREHHRkQLQDLSGQHQQELASQlaQFKVEM-AEREERQQQVAEDYEL 523
Cdd:pfam01576 848 DLAAserARRQAQQERdeLADEIASGASGKSALQDEKR-RLEARIAQLEEELEEE--QSNTELlNDRLRKSTLQVEQLTT 924
|
330 340 350
....*....|....*....|....*....|...
gi 191252785 524 RLAREQARVCELQSGNQQLEEQRVELVERLQAM 556
Cdd:pfam01576 925 ELAAERSTSQKSESARQQLERQNKELKAKLQEM 957
|
|
| FUSC |
pfam04632 |
Fusaric acid resistance protein family; This family includes a conserved region found in two ... |
392-559 |
1.31e-03 |
|
Fusaric acid resistance protein family; This family includes a conserved region found in two proteins associated with fusaric acid resistance, from Burkholderia cepacia and Klebsiella oxytoca. These proteins are likely to be membrane transporter proteins.
Pssm-ID: 428044 [Multi-domain] Cd Length: 655 Bit Score: 42.27 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 392 QREAQAAWetQHQLALVQSEVR-RLEGELDTARRER---DALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAq 467
Cdd:pfam04632 158 RARLRARL--RDALRLAAAALAgAPGAEAFEAARLRlaaDILALEALRSHAAFESPRGRARARALRRLLARMLALLPRL- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 468 eSSLRQaaslrehHRKQLQDLSGQHQQELASQLAqfkvEMAEREERQQqvAEDYELRLAREQARVCELQSGNQQLEEQRV 547
Cdd:pfam04632 235 -RSLAR-------LLARLRTEGAGTVPELAALLD----ELAAWEAALA--AEALQAALAALRARLRALRPALPLDFDTAA 300
|
170
....*....|..
gi 191252785 548 ELVERLQAMLQA 559
Cdd:pfam04632 301 ELLARLADLLAE 312
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
330-507 |
1.38e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.96 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 330 LQEERDAArAGQLSEHRELETLRAALEEERQTWAQQEHQLKEH------YQALQEESQAQLEREKEKSQREAQAAwetqh 403
Cdd:COG1842 39 LVEARQAL-AQVIANQKRLERQLEELEAEAEKWEEKARLALEKgredlaREALERKAELEAQAEALEAQLAQLEE----- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 404 QLALVQSEVRRLEGELDTARRERDALQlemslvqARYESQRIQ---------LESELAV----QLEQRVTERLAQAQESS 470
Cdd:COG1842 113 QVEKLKEALRQLESKLEELKAKKDTLK-------ARAKAAKAQekvnealsgIDSDDATsaleRMEEKIEEMEARAEAAA 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 191252785 471 -LRQAASLREhhrkQLQDLSGQHqqELASQLAQFKVEM 507
Cdd:COG1842 186 eLAAGDSLDD----ELAELEADS--EVEDELAALKAKM 217
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
188-570 |
1.44e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 42.43 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 188 DALDSEHTRRkhCERHIQSLQTRVLELQQQLAvavAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEHQAA 267
Cdd:pfam07111 294 DSLEPEFPKK--CRSLLNRWREKVFALMVQLK---AQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEV 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 268 ELTRSkqqeTVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCcvlqeERDAARAGQLSEH-- 345
Cdd:pfam07111 369 EVERM----SAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRV-----EQAVARIPSLSNRls 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 346 ---RELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAwETQHQLALVQSEVRRL--EGELD 420
Cdd:pfam07111 440 yavRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDA-ELQLSAHLIQQEVGRAreQGEAE 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 421 TARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQaaslREHHRKQLQDLSGQHQQELASQL 500
Cdd:pfam07111 519 RQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQ----QEIYGQALQEKVAEVETRLREQL 594
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 191252785 501 AQFKVEMAE-REERQQQVAEDYEL--RLAREQARVCELQsgnQQLEEQRVELVERLQAMLQAHWDEANQLLST 570
Cdd:pfam07111 595 SDTKRRLNEaRREQAKAVVSLRQIqhRATQEKERNQELR---RLQDEARKEEGQRLARRVQELERDKNLMLAT 664
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
196-488 |
1.62e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 196 RRKHCERHIQSLQTRVLELQQQLAvavAADRKKDTMIEQLD--KTLARVVEGWNRHEAERTEvLRGLQEEHQAAELTRS- 272
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLE---ALEAELDALQERREalQRLAEYSWDEIDVASAERE-IAELEAELERLDASSDd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 273 --KQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSEHRELET 350
Cdd:COG4913 687 laALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 351 LRAALEEERQTWAQQEHQL-----------KEHYQALQEESQAQLER-----------------EKEKSQREAQAAWETQ 402
Cdd:COG4913 767 LRENLEERIDALRARLNRAeeeleramrafNREWPAETADLDADLESlpeylalldrleedglpEYEERFKELLNENSIE 846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 403 HQLALVQsevrRLEGELDTARRERDalQLEMSLVQARYESQR-IQLE-SELAVQLEQRVTERLAQAQESSLRQAASLREH 480
Cdd:COG4913 847 FVADLLS----KLRRAIREIKERID--PLNDSLKRIPFGPGRyLRLEaRPRPDPEVREFRQELRAVTSGASLFDEELSEA 920
|
....*...
gi 191252785 481 HRKQLQDL 488
Cdd:COG4913 921 RFAALKRL 928
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
200-406 |
1.99e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 200 CERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKTLARVVEGWNRHEAERTEVLRGLQEEH---QAAELTRSKQQE 276
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEaelEELESRLEELEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 277 TVTRLEQ---SLSEAMEALNREQESARLQ----QRERETLEEERQALTLRL-EAEQQRCCVLQEERDAARAGQLSEHREL 348
Cdd:TIGR02168 380 QLETLRSkvaQLELQIASLNNEIERLEARlerlEDRRERLQQEIEELLKKLeEAELKELQAELEELEEELEELQEELERL 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 349 ETLRAALEEERQTWAQQEHQLKEHYQALQE--ESQAQLEREKEKSQREAQAAWETQHQLA 406
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQArlDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
205-466 |
2.77e-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: 41.48 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 205 QSLQTRVLELQQQLAVAVAADRKKDTMIEQLDKtLARVVEGWNRHEAERTEVLRGLQEEHQAaeltrskqqETVTRLEQS 284
Cdd:COG3096 451 QQATEEVLELEQKLSVADAARRQFEKAYELVCK-IAGEVERSQAWQTARELLRRYRSQQALA---------QRLQQLRAQ 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 285 LSEAMEALNREQESARLQQreretleeerqaltlrleaeqqRCCVLQeerdaarAGQLSEHRELETLRAALEEERQTWAQ 364
Cdd:COG3096 521 LAELEQRLRQQQNAERLLE----------------------EFCQRI-------GQQLDAAEELEELLAELEAQLEELEE 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 365 QEHQLKEHYQALQEESQAQLEREKEKSQREaqAAWETqhqlalVQSEVRRLEGELDTARRERDALQLEMSlVQARYESQR 444
Cdd:COG3096 572 QAAEAVEQRSELRQQLEQLRARIKELAARA--PAWLA------AQDALERLREQSGEALADSQEVTAAMQ-QLLEREREA 642
|
250 260
....*....|....*....|....
gi 191252785 445 IQLESELAVQLEQ--RVTERLAQA 466
Cdd:COG3096 643 TVERDELAARKQAleSQIERLSQP 666
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
186-513 |
2.78e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.49 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 186 LRDALDSEHTRRKHCERHIQSLQTRVLELQQQLAvAVAADRKKDTMIEQLdktlarvVEGWNRHEAERTEVLRGLQEEHQ 265
Cdd:TIGR00618 547 VYHQLTSERKQRASLKEQMQEIQQSFSILTQCDN-RSKEDIPNLQNITVR-------LQDLTEKLSEAEDMLACEQHALL 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 266 -AAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDAARAGQLSE 344
Cdd:TIGR00618 619 rKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEM 698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 345 HRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQR-EAQAAWETQHQ-----------LALVQ--S 410
Cdd:TIGR00618 699 LAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKElMHQARTVLKARteahfnnneevTAALQtgA 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 411 EVRRLEGELDTARRERDALQLEMSLVQARYESQRIQLESELAVQLEQRVTERlAQAQESSLRQAASLREHHRKQLQDLSG 490
Cdd:TIGR00618 779 ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEE-EQFLSRLEEKSATLGEITHQLLKYEEC 857
|
330 340
....*....|....*....|...
gi 191252785 491 QHQQElasQLAQFKVEMAEREER 513
Cdd:TIGR00618 858 SKQLA---QLTQEQAKIIQLSDK 877
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
366-531 |
2.87e-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: 40.29 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 366 EHQLKEHYQALQEesqaqLEREKEKSQREAQAAwetQHQLALVQSEVRRLEGELDTARRERDALQLEMSLVQARYESQRI 445
Cdd:COG1579 23 EHRLKELPAELAE-----LEDELAALEARLEAA---KTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 446 QLESELAvqleqrvtERLAQAQESSLRQAASLREHHRKQLQDLsgqhQQELASQLAQFKVEMAEREERQQQVAEDYE-LR 524
Cdd:COG1579 95 QKEIESL--------KRRISDLEDEILELMERIEELEEELAEL----EAELAELEAELEEKKAELDEELAELEAELEeLE 162
|
....*..
gi 191252785 525 LAREQAR 531
Cdd:COG1579 163 AEREELA 169
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
352-465 |
3.28e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 38.39 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 352 RAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKE---KSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDA 428
Cdd:pfam07926 3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREaqqNYERELVLHAEDIKALQALREELNELKAEIAELKAEAES 82
|
90 100 110
....*....|....*....|....*....|....*..
gi 191252785 429 LQLEMSLVQARYESQRIQLESELAvQLEQRVTERLAQ 465
Cdd:pfam07926 83 AKAELEESEESWEEQKKELEKELS-ELEKRIEDLNEQ 118
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
386-554 |
4.13e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 40.71 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 386 REKEKSQREAQAAWETQHQLALV------QSEVRRLEGE-LDTARRERDALQLEMslvQARYESQRIQLESELAVQLEQR 458
Cdd:pfam15709 328 REQEKASRDRLRAERAEMRRLEVerkrreQEEQRRLQQEqLERAEKMREELELEQ---QRRFEEIRLRKQRLEEERQRQE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 459 VTERLAQAQESSLRQAASLR-EHHRKQLQDLSGQHQQElasqlaqfkveMAEREERQQQVAEDYELRLAREQARVCELQs 537
Cdd:pfam15709 405 EEERKQRLQLQAAQERARQQqEEFRRKLQELQRKKQQE-----------EAERAEAEKQRQKELEMQLAEEQKRLMEMA- 472
|
170
....*....|....*..
gi 191252785 538 gnqqlEEQRVELVERLQ 554
Cdd:pfam15709 473 -----EEERLEYQRQKQ 484
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
201-447 |
4.69e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 40.44 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 201 ERHIQSLQTRVLELQQQLAVAVAADRKKDTMIEQL-----DKT-LARVVEGWNRHEAERTEVLRG----LQEEHQAAElt 270
Cdd:pfam19220 75 TRRLSAAEGELEELVARLAKLEAALREAEAAKEELrielrDKTaQAEALERQLAAETEQNRALEEenkaLREEAQAAE-- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 271 rskqqETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEaeqqrccvlqeERDAARAGQLSEHRELET 350
Cdd:pfam19220 153 -----KALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLA-----------ELETQLDATRARLRALEG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 351 LRAALEEERQtwaQQEHQLKEHYQALQEESQAQLEREKEKSQREA---QAAWETQHQLALVQSEVRRLEGELDTARRERD 427
Cdd:pfam19220 217 QLAAEQAERE---RAEAQLEEAVEAHRAERASLRMKLEALTARAAateQLLAEARNQLRDRDEAIRAAERRLKEASIERD 293
|
250 260
....*....|....*....|
gi 191252785 428 ALQLEMSLVQARYESQRIQL 447
Cdd:pfam19220 294 TLERRLAGLEADLERRTQQF 313
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
201-481 |
5.78e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.90 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 201 ERHIQSLQTRVLELQQQLAVAVAADRKK-DTMIEQLDKTLARVVEGWNRHEAErtevLRGLQEEHQAAEltrsKQQETVT 279
Cdd:pfam00038 24 EQQNKLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLE----LDNLRLAAEDFR----QKYEDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 280 RLEQSLSEAMEALNREQESARLQQREretleeerqaLTLRLEAEQQRCCVL----QEERDAARAGQLSEHRELET----- 350
Cdd:pfam00038 96 NLRTSAENDLVGLRKDLDEATLARVD----------LEAKIESLKEELAFLkknhEEEVRELQAQVSDTQVNVEMdaark 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 351 --LRAALEEERqtwAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLEGELDTARRERDA 428
Cdd:pfam00038 166 ldLTSALAEIR---AQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKAS 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 191252785 429 LQLEMSLVQARYESQRIQLESELAvQLEqrvtERLAQAQESSLRQaasLREHH 481
Cdd:pfam00038 243 LERQLAETEERYELQLADYQELIS-ELE----AELQETRQEMARQ---LREYQ 287
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
257-522 |
6.74e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 257 LRGLQEEHQAAELTRSKQQETVTRLEQSLSEAMEALNREQESARLQQRERETLEEERQALTLRLEAEQQRCCVLQEERDA 336
Cdd:COG4372 54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 337 ARAGQLSEHRELETLRAALEEERQTWAQQEHQLKEHYQALQEESQAQLEREKEKSQREAQAAWETQHQLALVQSEVRRLE 416
Cdd:COG4372 134 LEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 417 GELDTARRERDALqLEMSLVQARYESQRIQLESELAVQLEQRVTERLAQAQESSLRQAASLREHHRKQLQDLSGQHQQEL 496
Cdd:COG4372 214 RELAEELLEAKDS-LEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
250 260
....*....|....*....|....*.
gi 191252785 497 ASQLAQFKVEMAEREERQQQVAEDYE 522
Cdd:COG4372 293 LELKLLALLLNLAALSLIGALEDALL 318
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
387-532 |
8.59e-03 |
|
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: 39.33 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 191252785 387 EKEKSQREAQAAwETQHQLALVQSEVRRLE---GELDTARRERDALQLEMSLVQARYESQRIQLESelaVQLEQRVTERL 463
Cdd:pfam00529 57 QAALDSAEAQLA-KAQAQVARLQAELDRLQaleSELAISRQDYDGATAQLRAAQAAVKAAQAQLAQ---AQIDLARRRVL 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 191252785 464 AQAQESSLRQAASLREhHRKQLQDLSGQHQQELASQLAQFKVEMAEREERQQQVAEDYELRLAREQARV 532
Cdd:pfam00529 133 APIGGISRESLVTAGA-LVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAEL 200
|
|
| |
