|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
71-465 |
1.19e-12 |
|
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: 71.24 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 71 ELTTKLSTVTQGLQQLQEEKTRVDKTNEILLESVRVAQTQKdiycEEQEKIQNLQQIEIDKLKNLLSFREQESVDRMGLM 150
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL----EELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 151 RQQTQQIESLSEELERLRPIESVAEDLRDELEQLRHSTQQEKNLLTTTLAAVQEENRHLKKRMkiveesrleslgkLNSE 230
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA-------------ANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 231 QQVQALIREHKLLEQHLEEAHLQLSDIKGswsgqnlaletQVSRLSKQVAEETTEKRKALKSRDDAIESRKQVSFELEKA 310
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSE-----------DIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 311 KDEIKQRDDKVKLLEEEIDELSVALKECREENEQqvlfERNKSQNLETEVKDLKTRLTAaddrfsEYSSNAEqVAQKLRV 390
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQ----LELRLEGLEVRIDNLQERLSE------EYSLTLE-EAEALEN 961
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19922172 391 QVTEKQEQLDETIMQLEIEREE----KMTAILRNAEIAQSEDILRQQlrlerseasdlqernnqlVRDISEARQTLQQV 465
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLENKIKElgpvNLAAIEEYEELKERYDFLTAQ------------------KEDLTEAKETLEEA 1022
|
|
| Grip |
smart00755 |
golgin-97, RanBP2alpha,Imh1p and p230/golgin-245; |
553-598 |
1.97e-12 |
|
golgin-97, RanBP2alpha,Imh1p and p230/golgin-245;
Pssm-ID: 197860 Cd Length: 46 Bit Score: 61.85 E-value: 1.97e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 19922172 553 EVNFQYLKHVIVKFLTSREVEARHLVRAVSTLLQLTTEEEKLLHDT 598
Cdd:smart00755 1 EANFEYLKNVLLQFLTLRESERETLLPVISTVLQLSPEEMQKLLEV 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
162-478 |
3.05e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 162 EELERLrpiesvaEDLRDELE-QLRHSTQQeknlltttlAAVQEENRHLKKRMKIVEeSRLESLGKLNSEQQVQALIREH 240
Cdd:COG1196 186 ENLERL-------EDILGELErQLEPLERQ---------AEKAERYRELKEELKELE-AELLLLKLRELEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 241 KLLEQHLEEAHLQLSDIKGSWSGQNLALET---QVSRLSKQVAEETTEKRKALKSRDDAIESRKQVSFELEKAKDEIKQR 317
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEElelELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 318 DDKVKLLEEEIDELSVALKECREENEQQVLFERNKSQNLETEVKDLKTRLTAADDRFSEYsSNAEQVAQKLRVQVTEKQE 397
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL-LEALRAAAELAAQLEELEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 398 QLDETIMQLEIEREEKMTAILRNAEIAQSEDILRQQLRLERSEASDLQERNNQLVRDISEARQTLQQVSSTAQDNADKLT 477
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
.
gi 19922172 478 E 478
Cdd:COG1196 488 E 488
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
58-505 |
1.10e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 58 ESEQLCELRSQCNELTTKLSTVTQGLQQLQEEKTRVDKTNEILLESVRVAQTQKDiycEEQEKIQNLQQIEIDKLKNLLS 137
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA---EAEEELEELAEELLEALRAAAE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 138 FREQESVDRMGLMRQQTQQIESLSEELERLRPIESVAEDLRDELEQLRHSTQQEKNLLTTTLAAVQEENRHLKKRMKIVE 217
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 218 ESRLESLGKLNSEQQVQALIREHKLLEQHLEEAHLQLSDIKGSWSGQNLALETQVSRLSKQVAEETTEKRKALKSRDDAI 297
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 298 ESRKQVSFELEKAK--------DEIKQRDDKVKLLEEEIDELSVALKECREENEQQVLFERNKSQNLETEVKDlktRLTA 369
Cdd:COG1196 558 VAAAAIEYLKAAKAgratflplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA---RLEA 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 370 ADDRFSEYSSNAEQVAQKLRVQVTEKQEQLDETIMQLEIEREEKMTAILRNAEIAQSEDILRQQLRLERSEASDLQERNN 449
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 450 QLVRDISEARQTLQQVSSTAQDNADKLTEFERVQLEIIEKNKT----IKTLNQRLIDLKK 505
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPeppdLEELERELERLER 774
|
|
| GRIP |
pfam01465 |
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ... |
553-595 |
1.91e-09 |
|
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in many large coiled-coil proteins. It has been shown to be sufficient for targeting to the Golgi. The GRIP domain contains a completely conserved tyrosine residue. At least some of these domains have been shown to bind to GTPase Arl1, see structures in.
Pssm-ID: 460221 [Multi-domain] Cd Length: 44 Bit Score: 53.13 E-value: 1.91e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 19922172 553 EVNFQYLKHVIVKFLTSREVEAR-HLVRAVSTLLQLTTEEEKLL 595
Cdd:pfam01465 1 GANLEYLKNVLLQFLESKESSERkQLLPVIATLLKFSPEEEQKI 44
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
218-515 |
3.35e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 218 ESRLESLGKlnseQQVQAliREHKLLEQHLEEAHLQLsdikgsWSGQNLALETQVSRLSKQVAEETTEKRKA---LKSRD 294
Cdd:COG1196 199 ERQLEPLER----QAEKA--ERYRELKEELKELEAEL------LLLKLRELEAELEELEAELEELEAELEELeaeLAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 295 DAIESRKQVSFELEKAKDEIKQR----DDKVKLLEEEID---ELSVALKECREENEQQVLFERNKSQNLETEVKDLKTRL 367
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEeyelLAELARLEQDIArleERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 368 TAADDRFSEYSSNAEQVAQKLRVQVTEKQEQLDETIMQLEIEREEKMTAILRNAEIAQSEDILRQQLRLERSEASDLQER 447
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19922172 448 NNQLVRDISEARQTLQQVSSTAQDNADKLTEFERVQLEIIEKNKTIKTLNQRLIDLKKTVQKELRSAQ 515
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-464 |
5.28e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 156 QIESLSEELERLrpiESVAEDLRDELEQLRHSTQQEKNLLTTTLAAVQEENRHLKKRmkiVEESRLESLGKLNSEQQVQA 235
Cdd:COG1196 233 KLRELEAELEEL---EAELEELEAELEELEAELAELEAELEELRLELEELELELEEA---QAEEYELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 236 LIREHKLLEQHLEEAHLQLSdikgSWSGQNLALETQVSRLSKQVAEETTEKRKALKSRDDAIESRKQvsfELEKAKDEIK 315
Cdd:COG1196 307 LEERRRELEERLEELEEELA----ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE---AEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 316 QRDDKVKLLEEEIDELSVALKEcREENEQQVLFERNKSQNLETEVKDLKTRLTAADDrfseyssnAEQVAQKLRVQVTEK 395
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQ-LEELEEAEEALLERLERLEEELEELEEALAELEE--------EEEEEEEALEEAAEE 450
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19922172 396 QEQLDETIMQLEIEREEKMTAILRNAEIAQSEDILRQQLRLERSEASDLQERNNQLVRDISEARQTLQQ 464
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
84-448 |
2.56e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 84 QQLQEEKTRVDKT---NEILLESVRVAQTQKDIycEEQEKIQNLQQIEIDKLKNLLSFREQESVDRMGLMRQQTQQIESL 160
Cdd:COG1196 216 RELKEELKELEAElllLKLRELEAELEELEAEL--EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 161 SEELERLRPIESVAEDLRDELEQLRHSTQQEKNLLTTTLAAVQEENRHLKKRMKIVEESRLESLGKL-NSEQQVQALIRE 239
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELaEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 240 HKLLEQHLEEAHLQLSDIkgswsgQNLALETQVSRLSKQVAEETTEKRKAlkSRDDAIESRKQVSFELEKAKDEIKQRDD 319
Cdd:COG1196 374 LAEAEEELEELAEELLEA------LRAAAELAAQLEELEEAEEALLERLE--RLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 320 KVKLLEEEIDELSVALKECREENEQQVLFERNKSQNLETEVKDLKTRLTAADDRFSEYSSNAEQVAQKLRVQvtekQEQL 399
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA----GLRG 521
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 19922172 400 DETIMQLEIEREEKMTAILRNAEIAQSEDILRQQLRLERSEASDLQERN 448
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAK 570
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
268-515 |
2.17e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 268 LETQVSRLSKQV--AEETTEKRKALKSRD---------DAIESRKQVSFELEKAKDEIKQRDDKVKLLEEEIDELSVALK 336
Cdd:TIGR02168 198 LERQLKSLERQAekAERYKELKAELRELElallvlrleELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 337 ECREEN-----------------EQQVLFERNKSQNLETEVKDLKTRLTAADDRFSEYSSNAEQVAQK---LRVQVTEKQ 396
Cdd:TIGR02168 278 ELEEEIeelqkelyalaneisrlEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKleeLKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 397 EQLDETIMQLE------IEREEKMTAILRN-AEIAQSEDILRQQLRLERSEASDLQERNNQLVRDISEARQTLQqvssta 469
Cdd:TIGR02168 358 AELEELEAELEelesrlEELEEQLETLRSKvAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE------ 431
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 19922172 470 qdnadkLTEFERVQLEIIEKNKTIKTLNQRLIDL---KKTVQKELRSAQ 515
Cdd:TIGR02168 432 ------EAELKELQAELEELEEELEELQEELERLeeaLEELREELEEAE 474
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
116-455 |
4.55e-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: 53.15 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 116 EEQEKIQNLQQiEIDKLKNLLSFREQESVDRMGLMRQQTQQIESLSEELERLR----PIESVAEDLRDELEQLRHSTQQe 191
Cdd:TIGR02169 671 SEPAELQRLRE-RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEkeieQLEQEEEKLKERLEELEEDLSS- 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 192 knlLTTTLAAVQEENRHLKKRMKIVEES------RLESLGKLNSEQQVQALIREHKLLEQHLEEAHLQLSDIKGSWSG-- 263
Cdd:TIGR02169 749 ---LEQEIENVKSELKELEARIEELEEDlhkleeALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRlt 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 264 QNLALETQVSRLSKQVAEETTEKRKALKSRDDAIESRK-QVSFELEKAKDEIKQRDDKVKLLEEEIDELSVALKECREEN 342
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKeELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 343 EQQVLfernKSQNLETEVKDLKTRLTAADDRFSEYSSNaeqvaqkLRVQVTEKQEQLDETIMQLEIEREEK--------- 413
Cdd:TIGR02169 906 EELEA----QIEKKRKRLSELKAKLEALEEELSEIEDP-------KGEDEEIPEEELSLEDVQAELQRVEEeiralepvn 974
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 19922172 414 MTAILRNAEIAQSEDIL---RQQLRLERSEASDLQERNNQLVRDI 455
Cdd:TIGR02169 975 MLAIQEYEEVLKRLDELkekRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
64-488 |
4.63e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 64 ELRSQCNELTTKLSTVTQGLQQLQEEKTRVDKTNEILLESVRVAQTQKDiycEEQEKIQNLQQIEIDKLKNLLSFREQES 143
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA---ELEEELEELEEELEELEEELEEAEEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 144 VDRMGLMRQQTQQIESLSEELERLRPIESVAEDLRDELEQLRHSTQQEKNLLTTTLAAVQEENRHLKKRMKIVEESRLES 223
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 224 LGKLNSEQQVQALIREHKLLEQHLEEAHLQLSDIKGSWSGQNLALETQVSRLSKQVAEETT----EKRKALKSRDDAIES 299
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLlleaEADYEGFLEGVKAAL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 300 RKQVSFELEKAKDEIKQRDDKVKLLEEEIDELSVALKECREENEQQVLFERNKSQNL----------------------- 356
Cdd:COG1196 515 LLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratflpldkiraraalaaalar 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 357 ----------ETEVKDLKTRLTAADDRFSEYSSNAEQVAQKLRVQVTEKQEQLDETIMQLEIEREEKMTAILRNAEIAQS 426
Cdd:COG1196 595 gaigaavdlvASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL 674
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19922172 427 EDILRQQLRLERSEASDLQERNNQLVRDISEARQTLQQVSSTAQDNADKLTEFERVQLEIIE 488
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
71-480 |
4.87e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 71 ELTTKLSTVTQGLQQLQEEKTRVDKTNEILLESVRVAQTQKDIYCEEQEKI------QNLQQIEIDKLKNLLSFREQESV 144
Cdd:PRK02224 248 ERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaeaglDDADAEAVEARREELEDRDEELR 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 145 DRMglmRQQTQQIESLSEELERLRP----IESVAEDLRDELEQLRHSTQQEKNLLT---TTLAAVQEENRHLKKRMKIVE 217
Cdd:PRK02224 328 DRL---EECRVAAQAHNEEAESLREdaddLEERAEELREEAAELESELEEAREAVEdrrEEIEELEEEIEELRERFGDAP 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 218 ------ESRLESLGKLNSE--QQVQALIREHKLLEQHLEEAHLQLSDIKGSWSGQNLALETQVSRLS--KQVAEETTEKR 287
Cdd:PRK02224 405 vdlgnaEDFLEELREERDElrEREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEedRERVEELEAEL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 288 KALKSRDDAIESRKQVSFELEKAKDEIKQRDDKVKLLEEEIDELSVALKECREENEQQvlfeRNKSQNLETEVKDLKTRL 367
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL----RERAAELEAEAEEKREAA 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 368 TAADDRFSEYSSNAEQVAQKlRVQVTEKQEQLdETIMQLEIEREEKMTAILRNAE----IAQSEDILRQQLRLERSEASD 443
Cdd:PRK02224 561 AEAEEEAEEAREEVAELNSK-LAELKERIESL-ERIRTLLAAIADAEDEIERLREkreaLAELNDERRERLAEKRERKRE 638
|
410 420 430
....*....|....*....|....*....|....*..
gi 19922172 444 LQERNNQlvRDISEARQTLQQVSSTAQDNADKLTEFE 480
Cdd:PRK02224 639 LEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELR 673
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
306-515 |
1.76e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 306 ELEKAKDEIKQRDDKVKLLEEEIDELSVALKECREENEQQVLFERNKSQNLETEVKDLKT------RLTAADDRFSEYSS 379
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARleaeveQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 380 NAEQVAQKLRVQVTEKQEQLDETIMQLEIEREEKMTAILRNAEIAQSEDILRQQLRLERSEASDLQERNNQLVRDISEAR 459
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19922172 460 QTLQQVSSTAQDNADKLTEFERVQLEIIEKNKTIKTLNQRLIDLKKTVQKELRSAQ 515
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
125-444 |
7.68e-06 |
|
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: 49.35 E-value: 7.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 125 QQIEIDKLKNLLSFREQESvdrMGLMRQQTQQIESLSEELERLRPI----ESVAEDLRDELEQL---RHSTQQEKNLLTT 197
Cdd:pfam15921 424 RNMEVQRLEALLKAMKSEC---QGQMERQMAAIQGKNESLEKVSSLtaqlESTKEMLRKVVEELtakKMTLESSERTVSD 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 198 TLAAVQEENRHLK------KRMKIVEESRLESLGKLNSE----QQVQALIREHKL-----------LEQHLEEAhLQLSD 256
Cdd:pfam15921 501 LTASLQEKERAIEatnaeiTKLRSRVDLKLQELQHLKNEgdhlRNVQTECEALKLqmaekdkvieiLRQQIENM-TQLVG 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 257 IKGSWSGqnlALETQVSRLSKQVAEETTEKR--KALKSRDDAI--ESRKQVS-FELEKAK--DEIKQRDDKVKLLEEEID 329
Cdd:pfam15921 580 QHGRTAG---AMQVEKAQLEKEINDRRLELQefKILKDKKDAKirELEARVSdLELEKVKlvNAGSERLRAVKDIKQERD 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 330 ELSVALKECREE-----NEQQVLFE--RNKSQNLETEVKDLKTRLTAADDRFSEYSS----------NAEQVAQKLRVQV 392
Cdd:pfam15921 657 QLLNEVKTSRNElnslsEDYEVLKRnfRNKSEEMETTTNKLKMQLKSAQSELEQTRNtlksmegsdgHAMKVAMGMQKQI 736
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 19922172 393 TEKQEQLDETIMQLEIEREEKMTAILRNAEIAQSEDILRQQLRLERSEASDL 444
Cdd:pfam15921 737 TAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKM 788
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
155-366 |
8.82e-06 |
|
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: 8.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 155 QQIESLSEELERLRPIESVAEDLRDELEQLRHstqQEKNLLTTTLAAVQEENRHLKKRMKIVEEsRLESLgklnsEQQVQ 234
Cdd:COG4913 242 EALEDAREQIELLEPIRELAERYAAARERLAE---LEYLRAALRLWFAQRRLELLEAELEELRA-ELARL-----EAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 235 ALIREHKLLEQHLEEAHLQLSDIKGSwsgqnlaletQVSRLSKQVAEETTEKRKALKSRDDAIESRKQVSFELEKAKDEI 314
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNGGD----------RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19922172 315 KQRDDKVKLLEEEIDELSVALKECREENEQQVLFERNKSQNLETEVKDLKTR 366
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
310-509 |
1.29e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.09 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 310 AKDEIKQRDDKVKLLEEEIDELSVALKECREENEQQVLFERNKSQNLETEVKDLKTRLTAADDRFSEYSSNAEQVA---Q 386
Cdd:PHA02562 179 LNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSaalN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 387 KLRVQVTEKQEQLDE---------------TIMQLEIEREEKMTAIL-RNAEIAQS---EDILRQQLRLERSEASDLQER 447
Cdd:PHA02562 259 KLNTAAAKIKSKIEQfqkvikmyekggvcpTCTQQISEGPDRITKIKdKLKELQHSlekLDTAIDELEEIMDEFNEQSKK 338
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19922172 448 NNQLVRDISEARQTLQQVSSTAQDNADkltEFERVQLEIIEKNKTIKTLNQRLIDLKKTVQK 509
Cdd:PHA02562 339 LLELKNKISTNKQSLITLVDKAKKVKA---AIEELQAEFVDNAEELAKLQDELDKIVKTKSE 397
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
60-412 |
1.49e-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: 48.14 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 60 EQLCELRSQCNELTTKLSTVTQGLQQLQEEKTRVDKTNEILLESVRVAQT----QKDIYCEEQEKIQN---LQQIEIDKL 132
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYellkEKEALERQKEAIERqlaSLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 133 KNLLSFREQESVDRMGLMRQQTQQIESLSEEleRLRPIESVAEDLRDELEQLRHStqqeknlltttLAAVQEENRHLKKR 212
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKKIKDLGEE--EQLRVKEKIGELEAEIASLERS-----------IAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 213 MKIVEEsrleslgklnseqQVQALIREHKLLEQHLEEAHLQLSDIKGSWSGQNLALETQVSRLsKQVAEETTEKRKALKS 292
Cdd:TIGR02169 324 LAKLEA-------------EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL-EEVDKEFAETRDELKD 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 293 R----DDAIESRKQVSFELEKAKDEIKQRDDKVKLLEEEIDELSVALKECREENEQQVLFERNKSQNLETEVKDLKTrlt 368
Cdd:TIGR02169 390 YreklEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK--- 466
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 19922172 369 aADDRFSEYSSNAEQVAQKLRvqvtEKQEQLDETIMQLEIEREE 412
Cdd:TIGR02169 467 -YEQELYDLKEEYDRVEKELS----KLQRELAEAEAQARASEER 505
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
267-469 |
1.96e-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: 47.07 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 267 ALETQVSRLSKQVAEETTEKRKALKSRDDAIESRKQVSFELEKAKDEIKQRDDKVKLLEEEIDELSVALKECREENEQQ- 345
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQk 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 346 --------------------VLFERNKSQNLETEVKDLKTRLTAADDRFSEYSSNAEQVAQkLRVQVTEKQEQLDETIMQ 405
Cdd:COG4942 104 eelaellralyrlgrqpplaLLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA-LRAELEAERAELEALLAE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19922172 406 LEIEREEKMTAILRNAEIAQSediLRQQLRLERSEASDLQERNNQLVRDISEARQTLQQVSSTA 469
Cdd:COG4942 183 LEEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
69-555 |
2.72e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 69 CNELTTKLSTVTQGLQQLQEEKTRVDKTNEILLESVRVAQTQ---------------KDIYCEEQEKIQNLQQIE----- 128
Cdd:TIGR00606 414 CADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEElkfvikelqqlegssDRILELDQELRKAERELSkaekn 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 129 --IDKLKNLLSFREQESVDRMGLMRQQTQQIESLSEELERLRPIESVAEDLRDELEQLRHSTQQEKNLLTTTLA-----A 201
Cdd:TIGR00606 494 slTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGyfpnkK 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 202 VQEENRHLKKRMKIVEESRLESLGK--LNSEQQVQALIREHKLLEQHLEEAHLQLSDIKGSW---------------SGQ 264
Cdd:TIGR00606 574 QLEDWLHSKSKEINQTRDRLAKLNKelASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQdeesdlerlkeeiekSSK 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 265 NLALETQVSRLSKQVAEETTEK--------RKALKSRDDAIESRKQVSFELEKAKDEIKQRDDKVKLLEEEIDELsVALK 336
Cdd:TIGR00606 654 QRAMLAGATAVYSQFITQLTDEnqsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEM-LGLA 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 337 ECREENEQQVLFE----RNKSQNLETEVKDLKTRLtaaddrfseySSNAEQVAQKLRVQVTEKQEQLDETIMQ-LEIERE 411
Cdd:TIGR00606 733 PGRQSIIDLKEKEipelRNKLQKVNRDIQRLKNDI----------EEQETLLGTIMPEEESAKVCLTDVTIMErFQMELK 802
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 412 EKMTAILRNAEIAQSEDILRQQLRLeRSEASDLQERNNQLVRDISEARQTLQQVSSTAQDNADKLTEFERVQLEIIEKNK 491
Cdd:TIGR00606 803 DVERKIAQQAAKLQGSDLDRTVQQV-NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQ 881
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19922172 492 TIKTLNQRLIDLKKTVQkELRSAQISTDSESHPTTTPGHRISSSSLEAFSTGDKGNCVIMDEVN 555
Cdd:TIGR00606 882 RRQQFEEQLVELSTEVQ-SLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVN 944
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
58-497 |
5.14e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 58 ESEQLCELRSQCNELTTKLSTVTQGLQQLQEEKTRVDKtneiLLESVRVAQTQKDIYcEEQEKIQNLQQIEIDKLKNLLS 137
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELRE----ELEKLEKLLQLLPLY-QELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 138 fREQESVDRMGLMRQQTQQIESLSEELERLRPIESVA-----EDLRDELEQLrhstQQEKNLLTTTLAAVQEENRHLKKR 212
Cdd:COG4717 154 -RLEELRELEEELEELEAELAELQEELEELLEQLSLAteeelQDLAEELEEL----QQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 213 MKIVEES--RLESLGKLNSEQQVQALIREHKLLEQHLEEAHLQLSDIKGSWSGQNLALETQVSRLSKQVAEETTEKRKAL 290
Cdd:COG4717 229 LEQLENEleAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 291 KSRDDAIESRKQVSFELEKAKDEIKQRDDKVKLLEEEIDELSVALKECREENEQqvlferNKSQNLETEVKDLKTRLTAA 370
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE------LQLEELEQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 371 DDrfSEYSSNAEQVAQklRVQVTEKQEQLDETIMQLEIEREEKMTAilrnaeiaQSEDILRQQLRLERSEASDLQERNNQ 450
Cdd:COG4717 383 DE--EELRAALEQAEE--YQELKEELEELEEQLEELLGELEELLEA--------LDEEELEEELEELEEELEELEEELEE 450
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 19922172 451 LVRDISEARQTLQQVsSTAQDNADKLTEFERVQLEIIEKNKTIKTLN 497
Cdd:COG4717 451 LREELAELEAELEQL-EEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
59-509 |
1.05e-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: 45.43 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 59 SEQLCELRSQCNELTTKLSTVTQGLQQLQEEKTRV-------------------DKTNEILLESVRVAQTQKDIYCEEQE 119
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLeaeleeleaeleelesrleELEEQLETLRSKVAQLELQIASLNNE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 120 KIQNLQQIEI--DKLKNLLSFREQESVDRMGLMRQQTQ--------QIESLSEELERLRPIESVAEDLRDELEQLRHSTQ 189
Cdd:TIGR02168 402 IERLEARLERleDRRERLQQEIEELLKKLEEAELKELQaeleeleeELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 190 QEKNLLTTTLAAVQEENRHLKKRMKIVEESRLESLGKLNSEQQVQALIREHKLLEQHLEEA---HLQ------------- 253
Cdd:TIGR02168 482 RELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAAlggRLQavvvenlnaakka 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 254 ----------------LSDIKG----SWSGQNLALETQVSRLSKQVAEETTEKRKAL----------KSRDDAIESRKQV 303
Cdd:TIGR02168 562 iaflkqnelgrvtflpLDSIKGteiqGNDREILKNIEGFLGVAKDLVKFDPKLRKALsyllggvlvvDDLDNALELAKKL 641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 304 SFE----------------------------LEKAKdEIKQRDDKVKLLEEEIDELSVALKECREENEqqvlfernksqN 355
Cdd:TIGR02168 642 RPGyrivtldgdlvrpggvitggsaktnssiLERRR-EIEELEEKIEELEEKIAELEKALAELRKELE-----------E 709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 356 LETEVKDLKTRLTAADDRFSEYSSNAEQVAQKLRvQVTEKQEQLDETIMQLEIEREE--KMTAILRNAEIAQSEDILRQQ 433
Cdd:TIGR02168 710 LEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQLSKELTELEAEIEEleERLEEAEEELAEAEAEIEELE 788
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19922172 434 LRLERseasdLQERNNQLVRDISEARQTLQQVSSTAQDNADKLtefERVQLEIIEKNKTIKTLNQRLIDLKKTVQK 509
Cdd:TIGR02168 789 AQIEQ-----LKEELKALREALDELRAELTLLNEEAANLRERL---ESLERRIAATERRLEDLEEQIEELSEDIES 856
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
60-239 |
2.13e-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: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 60 EQLCELRSQCNELTTKLSTVTQGLQQLQEEKTRVDKTNEILLESVrvaQTQKDIYceeQEKIQNLQQI-EIDKLKNLLSF 138
Cdd:COG4942 55 KQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL---EAQKEEL---AELLRALYRLgRQPPLALLLSP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 139 REQESVDRMG-----LMRQQTQQIESLSEELERLRPIESVAEDLRDELEQLRHSTQQEKNLLTTTLAAVQEENRHLKKRM 213
Cdd:COG4942 129 EDFLDAVRRLqylkyLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
170 180
....*....|....*....|....*.
gi 19922172 214 KiVEESRLESLGKlnSEQQVQALIRE 239
Cdd:COG4942 209 A-ELAAELAELQQ--EAEELEALIAR 231
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
156-514 |
2.57e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 156 QIESLSEELERlrPIESVAEDLRDELEQLRHSTQQEKNLLTTTLAAVQEENRHLKKRMKIVEEsrleslgklNSEQQVQA 235
Cdd:pfam15921 246 QLEALKSESQN--KIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE---------QARNQNSM 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 236 LIREHKLLEQHLEEAHLQLSDIKGSWSGQNLALETQVSRLSKQVAEETTEKRKALKSRDDAIESRKQVSFELEKAKDEIK 315
Cdd:pfam15921 315 YMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELS 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 316 QRDDKVKLLEEEIDELSVALKECREEneqqvLFERN-KSQNLETEVKDLKTRLTAADDRFSEYSSNAEQVAQK---LRVQ 391
Cdd:pfam15921 395 LEKEQNKRLWDRDTGNSITIDHLRRE-----LDDRNmEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKvssLTAQ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 392 VTEKQEQLDETIMQLEierEEKMTaiLRNAEIAQSEDILRQQLRLERSEASDLQErnNQLVRDISEARQTLQQVSSTAQD 471
Cdd:pfam15921 470 LESTKEMLRKVVEELT---AKKMT--LESSERTVSDLTASLQEKERAIEATNAEI--TKLRSRVDLKLQELQHLKNEGDH 542
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 19922172 472 NADKLTEFERVQLEIIEKNKTIKTLNQRLIDLKKTVQKELRSA 514
Cdd:pfam15921 543 LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTA 585
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
278-422 |
2.89e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 278 QVAEETTEKRKALKSRDDAIESRKQVsFELEKAKDEIKQRDDKVKLLEEEIDELSVALKECREENEQqvlfernksqnLE 357
Cdd:COG2433 380 EALEELIEKELPEEEPEAEREKEHEE-RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIER-----------LE 447
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19922172 358 TEVKDLKTRLTAADDRFSEYSSNAEQVAQkLRVQVTEKQEQLDETimQLEIEREEKMTAILRNAE 422
Cdd:COG2433 448 RELSEARSEERREIRKDREISRLDREIER-LERELEEERERIEEL--KRKLERLKELWKLEHSGE 509
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
97-513 |
3.20e-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: 43.79 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 97 NEILLESVRVAQTQKDIYCEEQEKIQNLqqIEIDKLKNllSFREQESVDRM-GLMRQQTQQIESLSEELERLrpiesvaE 175
Cdd:COG3096 241 NRMTLEAIRVTQSDRDLFKHLITEATNY--VAADYMRH--ANERRELSERAlELRRELFGARRQLAEEQYRL-------V 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 176 DLRDELEQL---RHSTQQEKNLLTTTLAAVQEENRHLKKRMKIVEEsrLESLGKLNSEQQ--VQALIREHKLLEQHLEEA 250
Cdd:COG3096 310 EMARELEELsarESDLEQDYQAASDHLNLVQTALRQQEKIERYQED--LEELTERLEEQEevVEEAAEQLAEAEARLEAA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 251 HLQLSDIKGSWSGQNLALETQVSR-LSKQVAEETTEKRKALKSRDDAieSRKQVSFELEKAKDEIKQRDDKVKLLEEEID 329
Cdd:COG3096 388 EEEVDSLKSQLADYQQALDVQQTRaIQYQQAVQALEKARALCGLPDL--TPENAEDYLAAFRAKEQQATEEVLELEQKLS 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 330 ELSVALKECRE------------------ENEQQVLFERNKSQNLETEVKDLKTRLTAADDRFSEySSNAEQVAQKLRV- 390
Cdd:COG3096 466 VADAARRQFEKayelvckiageversqawQTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQ-QQNAERLLEEFCQr 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 391 --QVTEKQEQLDETIMQLEIEREE----KMTAILRNAEIAQSEDILRQQLRLERSEAS---DLQERNNQLVRDISEARQT 461
Cdd:COG3096 545 igQQLDAAEELEELLAELEAQLEEleeqAAEAVEQRSELRQQLEQLRARIKELAARAPawlAAQDALERLREQSGEALAD 624
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19922172 462 LQQVSSTAQDNADKLTEFERVQLEIIEK----NKTIKTLNQ-------RLIDLKKTVQKELRS 513
Cdd:COG3096 625 SQEVTAAMQQLLEREREATVERDELAARkqalESQIERLSQpggaedpRLLALAERLGGVLLS 687
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
64-457 |
3.30e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 64 ELRSQCNELTTKLSTVTQGLQQLQEEKTRVDKTNEILLESVRVAQTQKdiycEEQEKIQNLQQIEIDKLKNLLSFREQES 143
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE----EEEEEALEEAAEEEAELEEEEEALLELL 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 144 VDRMGLMRQQTQQIESLSEELERLRPIESVAEDLRDELEQLRHSTQQEKNLLTTTLAAVQ-EENRHLKKRMKIVEESRLE 222
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAvAVLIGVEAAYEAALEAALA 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 223 SLGKLNSEQQVQALIREHKLLEQHLEEAH--LQLSDIKGSWSGQNLALETQVSRLSKQVAEETTEKRKALKSRDDAIESR 300
Cdd:COG1196 546 AALQNIVVEDDEVAAAAIEYLKAAKAGRAtfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 301 KQVSFELEKAKDEIKQRDDKVKLLEEEIDELSvalkecrEENEQQVLFERNKSQNLETEVKDLKTRLTAADDRFSEYSSN 380
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLEGEGGS-------AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 381 AEQVAQKLRVQVTEKQEQLDETIMQLEIEREEKMTAILRNAEIAQSEDILRQQLRLERSE---ASDLQERNNQLVRDISE 457
Cdd:COG1196 699 LLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEppdLEELERELERLEREIEA 778
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
57-451 |
3.45e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 57 NESEQLCELRSQCNELTTKLSTVTQGLQQLQEEKTRVDKTNEILLESVRVAQTQKDIYCEEQEKIQNLQQiEIDKLKnll 136
Cdd:PRK03918 197 EKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE-RIEELK--- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 137 sfreqesvdrmglmrqqtQQIESLSEELERLRPIESVAEDLRdELEQLRHSTQQEKNLLTTTLAAVQEENRHLKKRMKIV 216
Cdd:PRK03918 273 ------------------KEIEELEEKVKELKELKEKAEEYI-KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 217 E--ESRLESLGKLNSEQQvqalirehKLLEQhLEEAHLQLSDIKgswsgqnlALETQVSRLSKQVAEETTEKRKalKSRD 294
Cdd:PRK03918 334 EekEERLEELKKKLKELE--------KRLEE-LEERHELYEEAK--------AKKEELERLKKRLTGLTPEKLE--KELE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 295 DAIESRKQVSFELEKAKDEIKQRDDKVKLLEEEIDELSVALKEC----REENEQQvlfERNKSQNLETEVKDLKTRLTAA 370
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgRELTEEH---RKELLEEYTAELKRIEKELKEI 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 371 DDRFSEYSSNAEQVAQKLRVQVT-----EKQEQLDETIMQLEIEREEKMTAILRNAEIAQSEDI-LRQQLRLERSEASDL 444
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESEliklkELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIkLKGEIKSLKKELEKL 551
|
....*..
gi 19922172 445 QERNNQL 451
Cdd:PRK03918 552 EELKKKL 558
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
83-521 |
3.47e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 83 LQQLQEEKTRVDKTNEILLESVRVAQTQKDiyCEEQEKIQNLQQIEIDKLKNLLSFREQESVDRMGLMRQQTQQIESLSE 162
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAEEAKKADEAKKK--AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAD 1500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 163 ELERLRPIESVAEDLRdELEQLRHSTQQEKnlltTTLAAVQEENRHLKKRMKIVEESRLESLGKLNSEQQVQALIREHKL 242
Cdd:PTZ00121 1501 EAKKAAEAKKKADEAK-KAEEAKKADEAKK----AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 243 LEQHLEEAHLQLSDIKGSWSGQNLALETQVSRLSKQVAEETTEKRKALKSRDDaiESRKQVSFELEKAKDEIKQRDDKVK 322
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA--EEEKKKVEQLKKKEAEEKKKAEELK 1653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 323 LLEEEIDELSVALKECREEneqqvlfERNKSQNLETEVKDlKTRLTAADDRFSEYSSNAEQVAQKlrvqvTEKQEQLDET 402
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAEE-------DKKKAEEAKKAEED-EKKAAEALKKEAEEAKKAEELKKK-----EAEEKKKAEE 1720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 403 IMQLEIEREEKMTAILRNAEiaqSEDILRQQLRLERSEASDLQERNNQLVRDISEARQTLQQVSSTAQDNAD--KLTEFE 480
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAE---EDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDekRRMEVD 1797
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 19922172 481 RVQLEIIEKNKTIKTLNQR----LIDLKKTVQKELRSAQISTDSE 521
Cdd:PTZ00121 1798 KKIKDIFDNFANIIEGGKEgnlvINDSKEMEDSAIKEVADSKNMQ 1842
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
131-504 |
3.84e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 131 KLKNLLSFREQESVDRMGLMRQQTQQIESLSEELERLRPIESVAEDLRDELEQLR---HSTQQEKNLLTTTLAAVQEENR 207
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEaelEELREELEKLEKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 208 HLKKRMKIVE-ESRLESLgkLNSEQQVQALIREHKLLEQHLEEAHLQLSDIKGSWSgqnLALETQVSRLSKQVAEETTEK 286
Cdd:COG4717 134 LEALEAELAElPERLEEL--EERLEELRELEEELEELEAELAELQEELEELLEQLS---LATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 287 RKALKSRDDAIESRKQVSFELEKAKDEIKQRDDKVKLLEEEIDELSVA-------------------------------- 334
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallallglggsllsliltiagvlflvlgllal 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 335 --LKECREENEQQVLFERNKSQNLETEVKDLKTRLTAADDRFSEYSSNAEQVAQKLRV-QVTEKQEQLDETIMQLEIERE 411
Cdd:COG4717 289 lfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIeELQELLREAEELEEELQLEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 412 EKMTAILRNAEIAQSEDILRQQLRLERsEASDLQERNNQLVRDISEARQTLQQVSStAQDNADKLTEFERVQLEIIEKNK 491
Cdd:COG4717 369 EQEIAALLAEAGVEDEEELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLE-ALDEEELEEELEELEEELEELEE 446
|
410
....*....|...
gi 19922172 492 TIKTLNQRLIDLK 504
Cdd:COG4717 447 ELEELREELAELE 459
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
60-331 |
3.85e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 60 EQLCELRSQCNELTTKLSTVTQGLQQLQEEKTRVDktneillESVRVAQTQKDIYCEEQEKIQNLQQIEIDKLKNLLSFR 139
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELE-------EEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 140 EQESVDRMGLMRQQTQQIESLSEELERLRPIESVAEDLRDELEQLRhstqqeknlltttlAAVQEENRHLKKRMKIVEES 219
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE--------------AELEELESRLEELEEQLETL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 220 RLESLGKLNSEQQVQALIREHKLLEQHLEEAHLQLSDIKGSWSGQnlALETQVSRLSKQVAEETTEKRKALKSRDDAIES 299
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK--LEEAELKELQAELEELEEELEELQEELERLEEA 462
|
250 260 270
....*....|....*....|....*....|..
gi 19922172 300 RKQVSFELEKAKDEIKQRDDKVKLLEEEIDEL 331
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
58-433 |
5.16e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.17 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 58 ESEQLCELRSQCNELTTKLSTVTQGLQQLQEEKTRVDKTNEILLESVRVAQTQKDIYCEEQEKIQNLQQIEIDKLKNLLS 137
Cdd:pfam05483 336 QMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 138 FREQesvdrmglMRQQTQQIESLSEELErlrpiesvaeDLRDELEQLRHSTQQEKNLLTTTLAAVQEENRHLKKRMKIVE 217
Cdd:pfam05483 416 EDEK--------LLDEKKQFEKIAEELK----------GKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLK 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 218 -ESRLESLGKLNSEQQVQALIREHKLLEQHLEEAHLQLSDIKgswsgqnlaletqvsrlsKQVAEETTEKRKALKSRDDA 296
Cdd:pfam05483 478 tELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQ------------------EDIINCKKQEERMLKQIENL 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 297 IESRKQVSFELEKAKDEIKQRDDKVKLLEEEIDELSVALKECREENEQQVLFERNKSQNLETEV--------------KD 362
Cdd:pfam05483 540 EEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIenknknieelhqenKA 619
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19922172 363 LKTRLTAADDRFSEYSSNAEQVAQKLRVQVTEKQEQLDETIMQLEIER--EEKMTAILRNAEIAQSEDILRQQ 433
Cdd:pfam05483 620 LKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKisEEKLLEEVEKAKAIADEAVKLQK 692
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
280-517 |
5.39e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 280 AEETTEKRKALKSRDDAIESRKQvsfELEKAKDEIKQRDDKVKLLEEEIDELSVALKEcreeNEQQVLFERNKSQNLETE 359
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEK---ELAALKKEEKALLKQLAALERRIAALARRIRA----LEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 360 VKDLKTRLTAADDRFSEYSSNAEQVAQKLRVQVTEKQEQLDETIMQLEIEREekmtaiLRNAEIAQSEDILRQQLRLERS 439
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKY------LAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 440 EASDLQERN--NQLVRDISEARQTLQQVSSTAQDNADKL-TEFERVQLEIIEKNKTIKTLNQRLIDLKKTVQKELRSAQI 516
Cdd:COG4942 166 RAELEAERAelEALLAELEEERAALEALKAERQKLLARLeKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
.
gi 19922172 517 S 517
Cdd:COG4942 246 A 246
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
269-473 |
5.80e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 269 ETQVSRLSKQVAEETTEKRKALKSRDDAIESRKQVSFELEKAKDEIKQRDDKVKLLEEEIDELSVALKECREENEQQVLF 348
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 349 ERNKSQNLE--------TEVKDLKTRLTAAdDRFSEYSSNAEQVAQKLRVQVTEKQEQLDETIMQLEiEREEKMTAILRN 420
Cdd:COG3883 95 LYRSGGSVSyldvllgsESFSDFLDRLSAL-SKIADADADLLEELKADKAELEAKKAELEAKLAELE-ALKAELEAAKAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19922172 421 AEIAQSEdiLRQQLRLERSEASDLQERNNQLVRDISEARQTLQQVSSTAQDNA 473
Cdd:COG3883 173 LEAQQAE--QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
106-341 |
6.64e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 106 VAQTQKDIYCEEQEKIQNLQQiEIDKLKNLLsfreqesvdrmglmRQQTQQIESLSEELERLRPIESVAEDLRDELEQLR 185
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQ-EIAELEKEL--------------AALKKEEKALLKQLAALERRIAALARRIRALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 186 HSTQQEKNLLTTTLAAVQEENRHLKKRM--------KIVEESRLESLGKLNSEQQVQALIREHKLLEQHLEEAHLQLSDI 257
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELaellralyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 258 KGSWSGQNLALETQVSRLSKQVAEETTEKRKALKSRDDAIESRKQVSFELEKAKDEIKQRDDKVKLLEEEIDELSVALKE 337
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
....
gi 19922172 338 CREE 341
Cdd:COG4942 239 AAER 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
319-516 |
8.15e-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: 42.75 E-value: 8.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 319 DKVKLLEEEIDELSVALKECREENEQQvlfernksqnlETEVKDLKTRLTAADDRFSEYSSNAEQVAQKLRvQVTEKQEQ 398
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRI-----------ENRLDELSQELSDASRKIGEIEKEIEQLEQEEE-KLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 399 LDETIMQLEIEREEKMTAILR-NAEIAQ-SEDILRQQLRLERSEASDLQERNNQLVRDISEARQTLQQVSSTAQDNADKL 476
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKElEARIEElEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL 821
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 19922172 477 tefERVQLEIIEKNKTIKTLNQRLIDLKKtvQKELRSAQI 516
Cdd:TIGR02169 822 ---NRLTLEKEYLEKEIQELQEQRIDLKE--QIKSIEKEI 856
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
151-341 |
8.59e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 8.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 151 RQQTQQIESLSEELERLRPIESVAEDLRDELEQLRHSTQQEKNLLTTTLAAVQEENRHLKKRMK-------IVEESRLES 223
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTdellnlvMDIEDPSAA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 224 LGKLNSEQ-----QVQALIREHKLLEQH----------------LEEAHLQLSDIKGSWSgqnlALETQVSRLSKQVAEE 282
Cdd:PHA02562 257 LNKLNTAAakiksKIEQFQKVIKMYEKGgvcptctqqisegpdrITKIKDKLKELQHSLE----KLDTAIDELEEIMDEF 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19922172 283 TTEKRKALKSRDD----------AIESRKQVSFELEKAKDEIKQRDDKVKLLEEEIDELSVALKECREE 341
Cdd:PHA02562 333 NEQSKKLLELKNKistnkqslitLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
109-364 |
8.70e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.58 E-value: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 109 TQKDIYCEEQEKIQNLQQI-----EIDKLK---NLLSFREQESVDRMGLMRQQTQQIESLSEELERLRpiesvaedlrDE 180
Cdd:PLN02939 140 AEKNILLLNQARLQALEDLekiltEKEALQgkiNILEMRLSETDARIKLAAQEKIHVEILEEQLEKLR----------NE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 181 LEQLRHSTQQEKNLLTTTLAAVQEENRHLKKRMKIVEESRLESlgkLNSEQQVQALIREHKLLEQHLEEAHLQL----SD 256
Cdd:PLN02939 210 LLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEV---AETEERVFKLEKERSLLDASLRELESKFivaqED 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 257 IKGSWSGQNLALETQVSRLSKQVAEETTEKRKALKSRDDAIESRKQVSfELEKAKDEI---KQRDDKVKLLEEEIDELSV 333
Cdd:PLN02939 287 VSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVD-KLEASLKEAnvsKFSSYKVELLQQKLKLLEE 365
|
250 260 270
....*....|....*....|....*....|.
gi 19922172 334 ALKECREENEQQVLFERNKSQNLETEVKDLK 364
Cdd:PLN02939 366 RLQASDHEIHSYIQLYQESIKEFQDTLSKLK 396
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
102-521 |
9.57e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.52 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 102 ESVRVAQTQKDIYCEEQEKIQNLQQI--EIDKLKN----LLSFREQESVDRMGLMRQQTQQIESLSEELERLRPIESVAE 175
Cdd:pfam12128 214 PKSRLNRQQVEHWIRDIQAIAGIMKIrpEFTKLQQefntLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLR 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 176 DLRDELEQLRHSTQQEKNLLTTTLAAVQEENRHLKKRMKIVEESRLESLgKLNSEQ------QVQALIREHKLLE---QH 246
Cdd:pfam12128 294 TLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETA-AADQEQlpswqsELENLEERLKALTgkhQD 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 247 LEEAHLQL-----SDIKGSWSGQNLALETQVSRLSKQVAEETTEKRK---ALKSR-DDAIESRKQVSFELEKAKDEIKQR 317
Cdd:pfam12128 373 VTAKYNRRrskikEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQAlesELREQlEAGKLEFNEEEYRLKSRLGELKLR 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 318 DDKVKLLEEEIDELSVALKECREENEQQVlfERNKSQ-NLETEVKDLKTRLTAADDRFSEYSSNAEQVAQK--------- 387
Cdd:pfam12128 453 LNQATATPELLLQLENFDERIERAREEQE--AANAEVeRLQSELRQARKRRDQASEALRQASRRLEERQSAldelelqlf 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 388 ---------LRVQVTEKQEQLDETIMQLEIEREEkMTAILRNAEIAQSEDILRQQLRLERSEASDLQERNNQLVRDISEA 458
Cdd:pfam12128 531 pqagtllhfLRKEAPDWEQSIGKVISPELLHRTD-LDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKA 609
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19922172 459 RQTLQQVSSTAQDNADKLT----EFERVQLEIIEKNKTIKTLNQRLIDLKKTVQKELRSAQISTDSE 521
Cdd:pfam12128 610 EEALQSAREKQAAAEEQLVqangELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAER 676
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
64-413 |
9.98e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.40 E-value: 9.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 64 ELRSQCNELTTKLSTVTQGLQQLQEEKTRVDKTNEILLESVRVAQTQKdiyceEQEKIQNlqqIEIDKLKNLLSFRE--- 140
Cdd:pfam05483 433 ELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL-----EKEKLKN---IELTAHCDKLLLENkel 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 141 -QESVDRMGLMRQQTQQIESLSEELER-LRPIESVAE---DLRDELEQLRHSTQQEKNLLTTTLAAVQEENRHLKKRMKI 215
Cdd:pfam05483 505 tQEASDMTLELKKHQEDIINCKKQEERmLKQIENLEEkemNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLK 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 216 VEESRLESLGKLNSeqqvqaLIREHKLLEQHLEEAHLQLSDIKGSWSGQNLAL---ETQVSRLSKQVAEETTEKRKALKS 292
Cdd:pfam05483 585 KEKQMKILENKCNN------LKKQIENKNKNIEELHQENKALKKKGSAENKQLnayEIKVNKLELELASAKQKFEEIIDN 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 293 RDDAIESRKQVSFELEKAKDEIKQRDDKVKLLEEEIDelsvalKECREENEQQVLFERNKSQNLETEVKDLKTRLTAADD 372
Cdd:pfam05483 659 YQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEID------KRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKN 732
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 19922172 373 RFSEYSSnaeqVAQKLRVQVTEKQEQLDETIMQLEIEREEK 413
Cdd:pfam05483 733 KEQEQSS----AKAALEIELSNIKAELLSLKKQLEIEKEEK 769
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
58-340 |
1.17e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 58 ESEQLCELRSQCNELTTKLSTVTQGLQQLQEEKTRVdktnEILLESVRVAQTQKDIYCEEQEKIQNLQQIEIDKLKNllS 137
Cdd:PRK03918 450 RKELLEEYTAELKRIEKELKEIEEKERKLRKELREL----EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEK--K 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 138 FREQESVDRmgLMRQQTQQIESLSEELERLRPIESVAEDLRDELEQLRhstQQEKNLLTTTLAAVQEENRHLKKRMKIVE 217
Cdd:PRK03918 524 AEEYEKLKE--KLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELE---EELAELLKELEELGFESVEELEERLKELE 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 218 ESRLESLGKLNSEQQVQALIREHKLLEQHLEEAHLQLSDIKGSWSGQNLALETQVSRLS----KQVAEETTEKRKALKSR 293
Cdd:PRK03918 599 PFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSeeeyEELREEYLELSRELAGL 678
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 19922172 294 DDAIESRKQVSFELEKAKDEIKQRDDKVKLLEEEIDELSVALKECRE 340
Cdd:PRK03918 679 RAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE 725
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
203-470 |
1.20e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 203 QEENRHLKKRMKIVE-----ESRLESLGKLNSEQQVQALIREHKLLEQHLEEAHLQLSDIKGswsgQNLALEtqVSRLSK 277
Cdd:pfam17380 306 EEKAREVERRRKLEEaekarQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQ----EEIAME--ISRMRE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 278 QVAEETTEKRKALKSRDDAIESRKQVSFELEKAKDEIKQRDDKVKLLEEEIDELSVALKECREENEQQVlfERNKSQNLE 357
Cdd:pfam17380 380 LERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREM--ERVRLEEQE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 358 TEVKDLKTRLTAADDRFSEYSSNAEQ----VAQKLRVQVTEKQEQLDETIM--------QLEIEREEKMTAILRNAEIAQ 425
Cdd:pfam17380 458 RQQQVERLRQQEEERKRKKLELEKEKrdrkRAEEQRRKILEKELEERKQAMieeerkrkLLEKEMEERQKAIYEEERRRE 537
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 19922172 426 SEDILR------------QQLRLERSEASDLQ--ERNNQLVRDISEARQTLQQVSSTAQ 470
Cdd:pfam17380 538 AEEERRkqqemeerrriqEQMRKATEERSRLEamEREREMMRQIVESEKARAEYEATTP 596
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
189-455 |
1.33e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 189 QQEKNLLTTTLAAVQEENRHLKKRMKIVEEsRLESLGKLnseQQVQALIREHKLLEQHLEEAHLQLSDIKGSWSgqnlal 268
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQE-RREALQRL---AEYSWDEIDVASAEREIAELEAELERLDASSD------ 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 269 etQVSRLSKQVAEETTEKRKALKSRDDAIESRKQVSFELEKAKDEIKQRDDKVKLLEEEIDELSVALKECREENEQQVLF 348
Cdd:COG4913 686 --DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 349 ERNKSQNLETEVKDLKTRLTAADDR----FSEYSSNAEQVAQKLRVQV---TEKQEQLDetimQLE----IEREEKMTAI 417
Cdd:COG4913 764 ERELRENLEERIDALRARLNRAEEEleraMRAFNREWPAETADLDADLeslPEYLALLD----RLEedglPEYEERFKEL 839
|
250 260 270
....*....|....*....|....*....|....*...
gi 19922172 418 LRNAEIAQSEDiLRQQLRLERSEASDLQERNNQLVRDI 455
Cdd:COG4913 840 LNENSIEFVAD-LLSKLRRAIREIKERIDPLNDSLKRI 876
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
150-521 |
1.37e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 150 MRQQTQQIESLSEELERLRPIESVA-EDLRDELEQLRHSTQQEKNLLTTTLAAVQEENRHLKKRM--------------- 213
Cdd:pfam15921 115 LQTKLQEMQMERDAMADIRRRESQSqEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMlshegvlqeirsilv 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 214 --------KIVEESRLESLGKLNSEQQVQALIREH----KLLEQHLEEAHLQLSDIKG-SWSGQNLALETQVSRLSKQVA 280
Cdd:pfam15921 195 dfeeasgkKIYEHDSMSTMHFRSLGSAISKILRELdteiSYLKGRIFPVEDQLEALKSeSQNKIELLLQQHQDRIEQLIS 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 281 EETTE----KRKALKSRDDAIESRKQVSFELEKAKDEIKQRDDKVKLLEEEIDELSVALKECREENEqqvlferNKSQNL 356
Cdd:pfam15921 275 EHEVEitglTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYE-------DKIEEL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 357 ETEVKDLKTRLTAA---DDRFSEYSSNAEQVAQKLRVQVTEKQEqldetimQLEIEREEKMTAILRNAEIAQSEDILRQQ 433
Cdd:pfam15921 348 EKQLVLANSELTEArteRDQFSQESGNLDDQLQKLLADLHKREK-------ELSLEKEQNKRLWDRDTGNSITIDHLRRE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 434 L--------RLE---RSEASDLQERNNQLVRDISEARQTLQQVSS-TAQDNADKlTEFERVQLEIIEKNKTIKTLNQRLI 501
Cdd:pfam15921 421 LddrnmevqRLEallKAMKSECQGQMERQMAAIQGKNESLEKVSSlTAQLESTK-EMLRKVVEELTAKKMTLESSERTVS 499
|
410 420
....*....|....*....|
gi 19922172 502 DLKKTVQKELRSAQiSTDSE 521
Cdd:pfam15921 500 DLTASLQEKERAIE-ATNAE 518
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
282-416 |
1.50e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 282 ETTEKRKALKSRDDAIESRKQVSFELEKAKDEIKQRDDKVKLLEEEIDELSVALKECREENEQQVLFERNKSQNLETEVK 361
Cdd:PRK12704 52 EAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEE 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 19922172 362 DLKTRLTAADDRFSEYSS-NAEQvAQKLRVQVTEKQEQLDETIMQLEIEREEKMTA 416
Cdd:PRK12704 132 ELEELIEEQLQELERISGlTAEE-AKEILLEKVEEEARHEAAVLIKEIEEEAKEEA 186
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
306-517 |
1.77e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 306 ELEKAKDEIKQRddkVKLLEEEIDELSVALKECREEN-----EQQVLFERNKSQNLETEVKDLKTRLTAADDRFSEYSSN 380
Cdd:COG3206 172 EARKALEFLEEQ---LPELRKELEEAEAALEEFRQKNglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 381 AEQVAQKL-RVQVTEKQEQLDETIMQLEIEREEKMT--------AILRNAEIAQSEDILRQQLRLERSEASDLQERNNQL 451
Cdd:COG3206 249 LGSGPDALpELLQSPVIQQLRAQLAELEAELAELSArytpnhpdVIALRAQIAALRAQLQQEAQRILASLEAELEALQAR 328
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19922172 452 VRDISEARQTLQQVSSTAQDNADKLTEFERvQLEIieKNKTIKTLNQRLIDLKktVQKELRSAQIS 517
Cdd:COG3206 329 EASLQAQLAQLEARLAELPELEAELRRLER-EVEV--ARELYESLLQRLEEAR--LAEALTVGNVR 389
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
60-511 |
1.91e-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: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 60 EQLCELRSQCNELTTKLSTvtqgLQQLQEEKTRVDKTNEILLESVRVAQTQKDIYCEEQEkiqnlQQIEIDKLKNLLSFR 139
Cdd:TIGR00618 260 QLLKQLRARIEELRAQEAV----LEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTE-----LQSKMRSRAKLLMKR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 140 EQESVDRMGLMRQQTQQIESLSEElERLRPIESVAEDLRDELEQLRHSTQQEKNLLTTTLAAVQEENRHLKKRMKIVEES 219
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTLHSQE-IHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 220 rleslGKLNSEQQVQALIREHKLLEQHLEEAHLQLSDIKGSWSGQNLALETQVSRLSKQVAEETTEKRKALKSRDDAIES 299
Cdd:TIGR00618 410 -----ATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQ 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 300 RKQVSFELEKAKDEIKQRDdkvKLLEEEIDELSVALKECREENEQQVLFER--NKSQNLETEVKDLKTRLTAADDRFSEY 377
Cdd:TIGR00618 485 ETRKKAVVLARLLELQEEP---CPLCGSCIHPNPARQDIDNPGPLTRRMQRgeQTYAQLETSEEDVYHQLTSERKQRASL 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 378 SSNAE---QVAQKLRVQVTEKQEQLDETIMQLEIEREEkmtailrnaeiAQSEDILRQQLRLERSEasdlQERNNQLVRD 454
Cdd:TIGR00618 562 KEQMQeiqQSFSILTQCDNRSKEDIPNLQNITVRLQDL-----------TEKLSEAEDMLACEQHA----LLRKLQPEQD 626
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 19922172 455 ISEARQTLQQVSstaQDNADKLTEFERVQLEIIEKNKTIKTLNQRLIDLKKTVQKEL 511
Cdd:TIGR00618 627 LQDVRLHLQQCS---QELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQL 680
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
119-500 |
2.02e-03 |
|
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: 41.50 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 119 EKIQNLQQIEIDKLKNLLSFREQESVDRMGLMRQQTQQIESLSEELERLRPIESVAEDLRDELEQLRHSTQQEKNLLTTT 198
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 199 LAAVQEENRHLKKRMKI---VEESRLESLGKLNSEQQVQALIREHKLLEQHLEEAHLQLSDIKGSWSGQNLALETQVSRL 275
Cdd:pfam02463 260 IEKEEEKLAQVLKENKEeekEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 276 SKQVAEETTEKRKALKSRDDAIESRKQVSFELEKAKDEIKQRDDKVKLLEEEIDELSVALKECREENEQQVLFERNKSQN 355
Cdd:pfam02463 340 LEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLED 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 356 LETEVKDLKTRLTAADDRFSEYSSNAEQVAQKLRVQVTEKQEQLDETIMQLEIEREEKMTAILRNAEIAQSEDILRQQLR 435
Cdd:pfam02463 420 LLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERS 499
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19922172 436 LERSEASDLQERNNQLVRDISEARQTLQQVSSTAQDNADKLTEFERVQLEIIEKNKTIKTLNQRL 500
Cdd:pfam02463 500 QKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQ 564
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
285-511 |
2.81e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 285 EKRKALKSRDDAIESRKqvsfELEKAKDEIKQRDDKVKLLE------EEIDELSVALKECRE--------ENEQQVLFER 350
Cdd:COG4913 219 EEPDTFEAADALVEHFD----DLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYlraalrlwFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 351 NKSQNLETEVKDLKTRLTAADDRFSEYSSNAEQVAQKLRVQVTEKQEQLDETIMQLEIEREEKMTAILRNAEIAQSediL 430
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAA---L 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 431 RQQLRLERSEASDLQERNNQLVRDISEARQTLQQ-VSSTAQDNADKLTEFERVQLEI--IEKNKtiKTLNQRLIDLKKTV 507
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAALLEALEEELEALEEaLAEAEAALRDLRRELRELEAEIasLERRK--SNIPARLLALRDAL 449
|
....
gi 19922172 508 QKEL 511
Cdd:COG4913 450 AEAL 453
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
306-506 |
4.23e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 306 ELEKAKDEIKQRDDKVKLLEEEIDELSVALKECREENEQQVLFERNKSQNLETEVKDLKTRLTAADDRFSEYSSNAEQVA 385
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 386 QKLRvQVTEKQEQLDETIMQLEIEREEKMTAILRNAEIAQS------EDILRQQLRLERSEA---SDLQERNNQLVRDIS 456
Cdd:TIGR02169 251 EELE-KLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLrvkekiGELEAEIASLERSIAekeRELEDAEERLAKLEA 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 19922172 457 EARQTLQQVSSTAQDNADKLTEFERVQLEIIEKNKTIKTLNQRLIDLKKT 506
Cdd:TIGR02169 330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE 379
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
157-417 |
4.68e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 157 IESLSEELERLRPIESVAEDLRDELEQlrhsTQQEKNLLTTTLAAVQEENRHLKKRMKIVEE--SRLESLGKLNS--EQQ 232
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEE----VLREINEISSELPELREELEKLEKEVKELEElkEEIEELEKELEslEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 233 VQALIREHKLLEQHLEEAHLQLSDikgswsgqnlaLETQVSRLsKQVAEETTEKRKALKSRDDAIESRKQVSFELEKAKD 312
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEE-----------LEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 313 EIKQRDDKVKLLEE---EIDELSVALKECREENEqqvlfERNKSQNLETEVKDLKTRLTAADDRFSEYS----SNAEQVA 385
Cdd:PRK03918 322 EINGIEERIKELEEkeeRLEELKKKLKELEKRLE-----ELEERHELYEEAKAKKEELERLKKRLTGLTpeklEKELEEL 396
|
250 260 270
....*....|....*....|....*....|..
gi 19922172 386 QKLRVQVTEKQEQLDETIMQLEIEREEKMTAI 417
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
267-412 |
6.48e-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: 38.75 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 267 ALETQVSRLSKQVAEETTEKRKALKSRDDAIESRKQVSFELEKAKDEIKQRDDKVKLLEEEIDELSVALKECREENEQQV 346
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEA 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19922172 347 L-----FERNKSQNLETEVKDLKTRLTAADDRFSEyssnAEQVAQKLRVQVTEKQEQLDETIMQLEIEREE 412
Cdd:COG1579 94 LqkeieSLKRRISDLEDEILELMERIEELEEELAE----LEAELAELEAELEEKKAELDEELAELEAELEE 160
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
59-513 |
6.78e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.62 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 59 SEQLCELRSQCNELTTKLSTVTQGLQQLQEEKTRV-----DKTNEILLESVRVAQTQKDIYcEEQEKIQNL----QQIEI 129
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIkkqlsEKQKELEQNNKKIKELEKQLN-QLKSEISDLnnqkEQDWN 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 130 DKLKNLLSFREQESVDRMGLMRQQTQQIESLSEELERLRP----IESVAEDLRDELEQLRHSTQQ---EKNLLTTTLAAV 202
Cdd:TIGR04523 310 KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKeltnSESENSEKQRELEEKQNEIEKlkkENQSYKQEIKNL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 203 QEENRHLKKRMKIVEESRLESLGKLNS-EQQVQALIREHKLLEQHLEEAHLQLSDIKGswsgQNLALETQVSRLSKQVAE 281
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKlQQEKELLEKEIERLKETIIKNNSEIKDLTN----QDSVKELIIKNLDNTRES 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 282 ETTEKRKALKSRDDAIESRKQVSFELEKAKDEIKQRDDKVKLLEEEIDEL---SVALKECREENEQQVLFERNKSQNLET 358
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLtkkISSLKEKIEKLESEKKEKESKISDLED 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 359 EVKDLKTRLTAADDRFSEYSSNAEQVAQKLRVQ-VTEKQEQLDETIMQLEIEREEKMTAILRNaeiaqseDILRQQLRLE 437
Cdd:TIGR04523 546 ELNKDDFELKKENLEKEIDEKNKEIEELKQTQKsLKKKQEEKQELIDQKEKEKKDLIKEIEEK-------EKKISSLEKE 618
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19922172 438 RSEASDLQERNNQLVRDISEARQTLQQVSSTAQDNADKLTEFERvqlEIIEKNKTIKTLNQRLIDLKKTVQKELRS 513
Cdd:TIGR04523 619 LEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWP---EIIKKIKESKTKIDDIIELMKDWLKELSL 691
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
145-494 |
7.46e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.56 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 145 DRMGLMRQQTQQIESLSEELERLRPIESVAEDLRDELEQL---RHSTQQEKNLLTTTLAAVQEENRHLKKRMKIVEEsrL 221
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELneaESDLEQDYQAASDHLNLVQTALRQQEKIERYQAD--L 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 222 ESLG-KLNSEQQVQALIREHKL-LEQHLEEAHLQLSDIKGSWSGQNLALETQVSR-LSKQVAEETTEKRKALKSRDDaie 298
Cdd:PRK04863 358 EELEeRLEEQNEVVEEADEQQEeNEARAEAAEEEVDELKSQLADYQQALDVQQTRaIQYQQAVQALERAKQLCGLPD--- 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 299 srkqvsFELEKAKDEIKQRDDKVKLLEEEIDEL----------------------------------SVALKECREENEQ 344
Cdd:PRK04863 435 ------LTADNAEDWLEEFQAKEQEATEELLSLeqklsvaqaahsqfeqayqlvrkiagevsrseawDVARELLRRLREQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 345 QVLFERnkSQNLETEVKDLKTRLT---AADDRFSEYSS------NAEQVAQKLRVQVTEKQEQLDETIMQLeIEREEKMT 415
Cdd:PRK04863 509 RHLAEQ--LQQLRMRLSELEQRLRqqqRAERLLAEFCKrlgknlDDEDELEQLQEELEARLESLSESVSEA-RERRMALR 585
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19922172 416 AILRNAeiaqseDILRQQLRLERSEASDLQERNNQLVRDISEARQTLQQVSSTAQDNADKLTEFERVQLEIIEKNKTIK 494
Cdd:PRK04863 586 QQLEQL------QARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALD 658
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
162-475 |
9.05e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 39.08 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 162 EELERLRPIESVAEDLRDELEQLRHSTQQEKNLLTTTLAAVQEENRHLKKRMKIVEESRLESLGK-LNSEQQVQALIREH 240
Cdd:pfam02029 17 EERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEaLERQKEFDPTIADE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 241 KlLEQHLEEAHLQLSDiKGSWsgqnlALETQVSRLSKQVAEETTEKRKALKSRDDAIESRKQVSFELEKAKD---EIKQR 317
Cdd:pfam02029 97 K-ESVAERKENNEEEE-NSSW-----EKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDkseEAEEV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 318 DDKVKLLEEEIDELSVALKECREEN----EQQVLFERNKSQNLETEVKDLK---------TRLTAADDRFSEYSSNAEQV 384
Cdd:pfam02029 170 PTENFAKEEVKDEKIKKEKKVKYESkvflDQKRGHPEVKSQNGEEEVTKLKvttkrrqggLSQSQEREEEAEVFLEAEQK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922172 385 AQKLRVQVTEKQEQLDETIMQLEIEREEKMTAILRNAE----IAQSEDILRQQLRLER--SEASDLQERNNQLVRDISEA 458
Cdd:pfam02029 250 LEELRRRRQEKESEEFEKLRQKQQEAELELEELKKKREerrkLLEEEEQRRKQEEAERklREEEEKRRMKEEIERRRAEA 329
|
330
....*....|....*..
gi 19922172 459 RQTLQQVSSTAQDNADK 475
Cdd:pfam02029 330 AEKRQKLPEDSSSEGKK 346
|
|
| |
