|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
106-422 |
4.08e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 106 LEELRAQV--LQLVAEL-EETRELAGQHEDDSLELQGL----LEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEH 178
Cdd:TIGR02168 195 LNELERQLksLERQAEKaERYKELKAELRELELALLVLrleeLREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 179 EKEselkEMEQELHLAQAEIQNLRQAAAD---SATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKT 255
Cdd:TIGR02168 275 EVS----ELEEEIEELQKELYALANEISRleqQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 256 SEPSNLSiSDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRraterwLESHLLRSTMSSESQTSEL 335
Cdd:TIGR02168 351 EELESLE-AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER------LEARLERLEDRRERLQQEI 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 336 dfpepdpvmQLLRQQLlgAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELKCAQNEVLRFQTSHstQELMCR 415
Cdd:TIGR02168 424 ---------EELLKKL--EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL--AQLQAR 490
|
....*..
gi 568939544 416 LQKLQAQ 422
Cdd:TIGR02168 491 LDSLERL 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
99-307 |
1.37e-10 |
|
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: 65.85 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 99 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDerlaSAQQAEVFTKQIQQLQGELQHLREEIslleH 178
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ----LKEELKALREALDELRAELTLLNEEA----A 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 179 EKESELKEMEQELHLAQAEIQNLRQAAAD---SATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKT 255
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEElseDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568939544 256 SEPSNLSiSDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESD 307
Cdd:TIGR02168 901 EELRELE-SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
99-335 |
6.04e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 6.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 99 LSLTETELEELRAQVLQLVAELEET----RELAGQHEDDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELQHLREEIS 174
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELeaelEELRLELEELELELEEAQAEEYELLAELARL-EQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 175 llehEKESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDdlcrLQNDLDDMERIRGDYEMEIASLRAEMELK 254
Cdd:COG1196 320 ----ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE----AEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 255 TSEPSNLSISDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATERWLESHLLRSTMSSESQTSE 334
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
.
gi 568939544 335 L 335
Cdd:COG1196 472 A 472
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
99-356 |
1.22e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 99 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQG---LLEDERLASAQQAEVFTKQIQQLQGELQHLREEISL 175
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQdiaRLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 176 LEHEK---ESELKEMEQELHLAQAEIQNL---RQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRA 249
Cdd:COG1196 342 LEEELeeaEEELEEAEAELAEAEEALLEAeaeLAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 250 EMELKTSEPSNLSISdfsgIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATERW-LESHLLRSTMSS 328
Cdd:COG1196 422 ELEELEEALAELEEE----EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEeLAEAAARLLLLL 497
|
250 260
....*....|....*....|....*...
gi 568939544 329 ESQTSELDFPEPDPVMQLLRQQLLGAEE 356
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
102-393 |
1.23e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 102 TETELEELRAQVLQLVAELEETR----ELAGQHEDDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELQHLREEISLLE 177
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEkalaELRKELEELEEELEQLRKELEELSRQISAL-RKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 178 HekesELKEMEQELHLAQAEIQNLRQAAAdsatEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSE 257
Cdd:TIGR02168 754 K----ELTELEAEIEELEERLEEAEEELA----EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 258 PSNLsisdfsgiQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATErwLESHLLRSTMSSESqtseldf 337
Cdd:TIGR02168 826 LESL--------ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE--LEALLNERASLEEA------- 888
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 568939544 338 pepdpvMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQREL 393
Cdd:TIGR02168 889 ------LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
179-514 |
1.98e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 179 EKESELKEMEQELHLAQAEIQNLRQAAADSATEHEsdiaSLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEP 258
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELE----ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 259 SNLSIsdfsgiqdELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATERWLESHLLRSTMSSESQTSElDFP 338
Cdd:TIGR02168 750 AQLSK--------ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE-EAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 339 EPDPVMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELKCAQNEVlrfqtsHSTQELMCRLQK 418
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER------ASLEEALALLRS 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 419 LQAQhqcsvnekeqllevqhhLHDKLRCHESEVHRLRsmvDCLREKNEKNSGIHLQLQ--EMKGLYQFSR------DELE 490
Cdd:TIGR02168 895 ELEE-----------------LSEELRELESKRSELR---RELEELREKLAQLELRLEglEVRIDNLQERlseeysLTLE 954
|
330 340
....*....|....*....|....
gi 568939544 491 RQKHMYDQLEQDFLLCQQELTELK 514
Cdd:TIGR02168 955 EAEALENKIEDDEEEARRRLKRLE 978
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
103-435 |
3.06e-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: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 103 ETELEELRAQV------LQLVAELEETRELAGQHEDDSLELQ-GLLEDERLASAQQAEVFTKQIQQLQGELQHLREeisl 175
Cdd:COG1196 199 ERQLEPLERQAekaeryRELKEELKELEAELLLLKLRELEAElEELEAELEELEAELEELEAELAELEAELEELRL---- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 176 lehekesELKEMEQELHLAQAEIQNLRQAAAdsatEHESDIASLQDDLCRLQNDLDDMERirgdyemEIASLRAEMELkt 255
Cdd:COG1196 275 -------ELEELELELEEAQAEEYELLAELA----RLEQDIARLEERRRELEERLEELEE-------ELAELEEELEE-- 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 256 sepsnlsisdfsgIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATErwlESHLLRSTMSSESQTSEl 335
Cdd:COG1196 335 -------------LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE---LEELAEELLEALRAAAE- 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 336 dfpepdpvmqlLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELKCAQNEVLRFQTSHSTQELmcR 415
Cdd:COG1196 398 -----------LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE--L 464
|
330 340
....*....|....*....|
gi 568939544 416 LQKLQAQHQCSVNEKEQLLE 435
Cdd:COG1196 465 LAELLEEAALLEAALAELLE 484
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
102-386 |
3.79e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.24 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 102 TETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLED-----ERLASAQQAEVfTKQIQQLQGELQHLREEISll 176
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElnkkiKDLGEEEQLRV-KEKIGELEAEIASLERSIA-- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 177 ehEKESELKEMEQELHLAQAEIQNLRQAAADSATEHES---DIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEmel 253
Cdd:TIGR02169 312 --EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEerkRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE--- 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 254 ktsepsnlsisdFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTrRATERWLESHLLRSTMSSESQTS 333
Cdd:TIGR02169 387 ------------LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA-GIEAKINELEEEKEDKALEIKKQ 453
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 568939544 334 ELDFPEPDPVMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQ 386
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
99-392 |
8.48e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.08 E-value: 8.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 99 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERlasaqqaevftkqIQQLQGELQHLREEISLLE- 177
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR-------------IPEIQAELSKLEEEVSRIEa 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 178 --HEKESELKEMEQELHLAQAEIQNLRQAAADSatehESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKT 255
Cdd:TIGR02169 813 rlREIEQKLNRLTLEKEYLEKEIQELQEQRIDL----KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 256 SEPSNLsisdfsgiQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDrtrraterwlESHLLRSTMSSESQtsel 335
Cdd:TIGR02169 889 KERDEL--------EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE----------LSEIEDPKGEDEEI---- 946
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 568939544 336 dfPEPDPVMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRE 392
Cdd:TIGR02169 947 --PEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-405 |
1.23e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 101 LTETELEELRAQVLQLVAELEETR----ELAGQHEDDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELQHLREEISLL 176
Cdd:TIGR02168 222 LRELELALLVLRLEELREELEELQeelkEAEEELEELTAELQELEEKLEELRLEVSEL-EEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 177 EHEKEsELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMErirgDYEMEIASLRAEMELKTS 256
Cdd:TIGR02168 301 EQQKQ-ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE----AELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 257 EpsnlsisdfsgIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATERwleSHLLRSTMSSESQTSELD 336
Cdd:TIGR02168 376 E-----------LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI---EELLKKLEEAELKELQAE 441
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568939544 337 FPEpdpvmqlLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELKCAQNEVLRFQT 405
Cdd:TIGR02168 442 LEE-------LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
99-315 |
2.65e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 99 LSLTETELEELRAQVLQLvaelEETRELAGQHEDDSLELQGLledERLASAQQAEVFTKQIQQLQGELQHLREEISLLEH 178
Cdd:COG4913 237 LERAHEALEDAREQIELL----EPIRELAERYAAARERLAEL---EYLRAALRLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 179 EK---ESELKEmeqelhlAQAEIQNLRQAAADSATEhesDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLraemelkt 255
Cdd:COG4913 310 ELerlEARLDA-------LREELDELEAQIRGNGGD---RLEQLEREIERLERELEERERRRARLEALLAAL-------- 371
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 256 SEPSNLSISDFSGIQDELHHLRERynlLNEEYQALRESNSSLTGQLAELESDRTRRATER 315
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
106-318 |
7.97e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 7.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 106 LEELRAQVLQLVAELEETRELAGQHEDdsleLQGLLEDERLASAQQAEVFTKQI--QQLQGELQHLREEISLLEhEKESE 183
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEA----ELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLD-ASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 184 LKEMEQELHLAQAEIQNLRQ---AAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEmeiaSLRAEMELKTSEPSN 260
Cdd:COG4913 687 LAALEEQLEELEAELEELEEeldELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL----RALLEERFAAALGDA 762
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568939544 261 LSISDFSGIQDELHHLRERYNLLNEEYQALR------------------ESNSSLTGQLAELESDRTRRATERWLE 318
Cdd:COG4913 763 VERELRENLEERIDALRARLNRAEEELERAMrafnrewpaetadldadlESLPEYLALLDRLEEDGLPEYEERFKE 838
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
146-385 |
8.62e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 8.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 146 LASAQQAEVFTKQIQQLQGELQHLREEISLLEHEKES---ELKEMEQELHLAQAEIQNLRQAAADSatehESDIASLQDD 222
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAllkQLAALERRIAALARRIRALEQELAAL----EAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 223 LCRLQNDLDDM-----ERIRGDYEMEIASlrAEMELKTSEPSNLSISDFSGIQDELHHLRERYNLLNEEYQALRESNSSL 297
Cdd:COG4942 92 IAELRAELEAQkeelaELLRALYRLGRQP--PLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 298 TGQLAELESDRTRRATERwlesHLLRSTMSSESQTseldfpepdpvMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQH 377
Cdd:COG4942 170 EAERAELEALLAELEEER----AALEALKAERQKL-----------LARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
....*...
gi 568939544 378 HRRTSEEE 385
Cdd:COG4942 235 EAAAAAER 242
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
105-413 |
9.12e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 9.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 105 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQaevfTKQIQQLQGELQHLREEISLLEHEKESEL 184
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL----ELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 185 KEMEQelhlAQAEIQNLRQAAADSATEHESDIASLQddlcRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEPSNLSIS 264
Cdd:COG1196 309 ERRRE----LEERLEELEEELAELEEELEELEEELE----ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 265 DFSGIQDELHHLRERYNLLNEEyQALRESNSSLTGQLAELESDRTRRATERwleshllrstmssesqtseldfpepdpvm 344
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQL-EELEEAEEALLERLERLEEELEELEEAL----------------------------- 430
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568939544 345 QLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELKCAQNEVLRFQTSHSTQELM 413
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
96-249 |
1.13e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 96 HRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDdslELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISL 175
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALRE---ELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568939544 176 LEHEkeseLKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRA 249
Cdd:COG4913 364 LEAL----LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
103-290 |
1.98e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.41 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 103 ETELEELRAQVLQLVAELEETRElagQHEDDSLELQGLLEDERLASAQQAEVFTK-QIQQLQGELQHLREEISLLEHE-- 179
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQ---KNGLVDLSEEAKLLLQQLSELESQLAEARaELAEAEARLAALRAQLGSGPDAlp 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 180 ---KESELKEMEQELHLAQAEIQNLRQaaadSATEHESDIASLQDDLCRLQNDLDD-MERIRGDYEMEIASLRAEMELKT 255
Cdd:COG3206 258 ellQSPVIQQLRAQLAELEAELAELSA----RYTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQ 333
|
170 180 190
....*....|....*....|....*....|....*..
gi 568939544 256 SEPSNLS--ISDFSGIQDELHHLRERYNLLNEEYQAL 290
Cdd:COG3206 334 AQLAQLEarLAELPELEAELRRLEREVEVARELYESL 370
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
97-339 |
2.72e-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: 55.06 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 97 RGLSLTETELEELRAQVLQLVAELEE--TRELAGQHEDDSLELQGLLEDERLASAQ-QAEVFTKQIQQLQGELQHLREEI 173
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEElqKELYALANEISRLEQQKQILRERLANLErQLEELEAQLEELESKLDELAEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 174 SLLEHEKES---ELKEMEQELHLAQAEIQNLRQAAADSATEHE---SDIASLQDDLCRLQNDLDDMERIRGDYEMEIASL 247
Cdd:TIGR02168 340 AELEEKLEElkeELESLEAELEELEAELEELESRLEELEEQLEtlrSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 248 RAEMElktSEPSNLSISDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDrtRRATERWLESHLLRSTMS 327
Cdd:TIGR02168 420 QQEIE---ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA--LDAAERELAQLQARLDSL 494
|
250
....*....|..
gi 568939544 328 SESQTSELDFPE 339
Cdd:TIGR02168 495 ERLQENLEGFSE 506
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
103-244 |
1.55e-06 |
|
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: 50.69 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 103 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDerlASAQQAEVFT-KQIQQLQGELQHLREEISLLEheke 181
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK---YEEQLGNVRNnKEYEALQKEIESLKRRISDLE---- 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568939544 182 SELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEI 244
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
150-318 |
3.59e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 150 QQAEVFTKQIQQLQGELQHLREEISllehEKESELKEMEQELHLAQAEIQNLRQAAADSATEHEsdIASLQDDLCRLQND 229
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELE----ELEAELEELREELEKLEKLLQLLPLYQELEALEAE--LAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 230 LDDMERIRGDYEM---EIASLRAEMELKTSEPSNLSISDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELES 306
Cdd:COG4717 155 LEELRELEEELEEleaELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
170
....*....|..
gi 568939544 307 DRTRRATERWLE 318
Cdd:COG4717 235 ELEAAALEERLK 246
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
99-566 |
5.83e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 99 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQ----------QAEVFTKQIQQLQGELQH 168
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQlelqiaslnnEIERLEARLERLEDRRER 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 169 LREEISLLE--------HEKESELKEMEQELHLAQAEIQNLRQA---AADSATEHESDIASLQDDLCRLQNDLDDMERIR 237
Cdd:TIGR02168 419 LQQEIEELLkkleeaelKELQAELEELEEELEELQEELERLEEAleeLREELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 238 GDYEMEIASLRAEM--------------ELKTSEPS--------------NLSISDFSGIQDELHHLRE----------- 278
Cdd:TIGR02168 499 ENLEGFSEGVKALLknqsglsgilgvlsELISVDEGyeaaieaalggrlqAVVVENLNAAKKAIAFLKQnelgrvtflpl 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 279 ---RYNLLNEEYQALRESNSSLTGQLAELES--DRTRRATERWL--------------ESHLLRSTMSSESQTSELDFP- 338
Cdd:TIGR02168 579 dsiKGTEIQGNDREILKNIEGFLGVAKDLVKfdPKLRKALSYLLggvlvvddldnaleLAKKLRPGYRIVTLDGDLVRPg 658
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 339 --------EPDPVMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQ-------RELKCAQNEVLRF 403
Cdd:TIGR02168 659 gvitggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRkeleelsRQISALRKDLARL 738
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 404 QTSHstQELMCRLQKLQAQHQCSVNEKEQLLEVQHHLHDKLRCHESEVHRLRSMVDCLREKNEKNSgihLQLQEMKGLYQ 483
Cdd:TIGR02168 739 EAEV--EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR---EALDELRAELT 813
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 484 FSRDELERQKHMYDQLEQDFLLCQQELTELKSS--------QSLCEENGNCSNKCDALLARLTELQDKFKASQEEIGHLQ 555
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQieelsediESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
570
....*....|.
gi 568939544 556 MEQCELLEDQR 566
Cdd:TIGR02168 894 SELEELSEELR 904
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
97-268 |
1.24e-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: 48.99 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 97 RGLSLTETELEELRAQVLQLVAELEETREL----------AGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGEL 166
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEElaellralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 167 QHLREEISLLEHEKESELKEMEQELHLAQAEIQNLRQAAAdsatEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIAS 246
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKA----ERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
170 180
....*....|....*....|..
gi 568939544 247 LRAEMELKTSEPSNLSISDFSG 268
Cdd:COG4942 232 LEAEAAAAAERTPAAGFAALKG 253
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
102-315 |
1.47e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 102 TETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELQHLREEISLLEHEKE 181
Cdd:COG4913 666 AEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRL-EKELEQAEEELDELQDRLEAAEDLAR 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 182 SELKEMEQElHLAQAEIQNLRQAAADSAtehESDIASLQDDLCRLQNDLDD-MERIRGDYEMEIASLRAEMElktsepsn 260
Cdd:COG4913 745 LELRALLEE-RFAAALGDAVERELRENL---EERIDALRARLNRAEEELERaMRAFNREWPAETADLDADLE-------- 812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568939544 261 lSISDFSGI-----QDELHHLRERYN-LLNEeyqalrESNSSLTGQLAELESDRtRRATER 315
Cdd:COG4913 813 -SLPEYLALldrleEDGLPEYEERFKeLLNE------NSIEFVADLLSKLRRAI-REIKER 865
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
141-321 |
1.89e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 141 LEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLehEKESELKEMEQELHLAQAEIQNLRQAAADsATEHESDIASLQ 220
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREAL--QRLAEYSWDEIDVASAEREIAELEAELER-LDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 221 DDLCRLQNDLDDMERIRGDYEMEIASLRAEMElktsepsnlsisdfsGIQDELHHLRERYNLLNEEYQAlrESNSSLTGQ 300
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELE---------------QAEEELDELQDRLEAAEDLARL--ELRALLEER 754
|
170 180
....*....|....*....|.
gi 568939544 301 LAELESDRTRRATERWLESHL 321
Cdd:COG4913 755 FAAALGDAVERELRENLEERI 775
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
104-292 |
2.11e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 104 TELEELRAQVLQLVAELEETRELAGQHEDDSLE-LQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEHEK-- 180
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLELLEaELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRle 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 181 --ESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEp 258
Cdd:COG4913 342 qlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE- 420
|
170 180 190
....*....|....*....|....*....|....
gi 568939544 259 snlsisdFSGIQDELHHLRERYNLLNEEYQALRE 292
Cdd:COG4913 421 -------LRELEAEIASLERRKSNIPARLLALRD 447
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
161-400 |
2.16e-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: 48.91 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 161 QLQGELQHLREEISLLEHEKESELKEmeqelhlaQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDY 240
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSE--------LRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 241 EMEIASLRAEMELKTSEPSNLsISDFSGIQDELHHLRERYNLL------------NEEYQALRESNSSLTGQLAELESDR 308
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKEL-EARIEELEEDLHKLEEALNDLearlshsripeiQAELSKLEEEVSRIEARLREIEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 309 TRRaterwlesHLLRSTMSSESQTSELDFPEPDPVMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKR 388
Cdd:TIGR02169 822 NRL--------TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
250
....*....|..
gi 568939544 389 LQRELKCAQNEV 400
Cdd:TIGR02169 894 LEAQLRELERKI 905
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
102-314 |
1.02e-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: 45.91 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 102 TETELEELRAQVLQLVAELEETRelagQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEHEKE 181
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALK----KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 182 SELKEMEQELHLAQAEIQNLR----------QAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEM 251
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPlalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568939544 252 ELKTSEPSNLSiSDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATE 314
Cdd:COG4942 181 AELEEERAALE-ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
283-563 |
1.25e-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: 46.20 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 283 LNEEYQALRESNSSLTGQLAELESDRTRRATERwleshllrSTMSSESQTSELDFPEPDPVMQLLRQQLLGAEEQMQDMQ 362
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEEL--------EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 363 DKCKNLYCELEELQHHRRTSEEEQKRLQRELKCAQNEVLRFQTSHSTQELmcRLQKLQAQHQcsvnekeQLLEVQHHLHD 442
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE--ALDELRAELT-------LLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 443 KLRCHESEVHRLRSMVDCLREKNEKNSGIHLQLQEMKGLYQFSRDELERQ-KHMYDQLEQDfllcQQELTELKSS-QSLC 520
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESElEALLNERASL----EEALALLRSElEELS 900
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568939544 521 EENGNCSNKCDALLARLTELQDKFKASQEEIGHLQMEQCELLE 563
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
103-733 |
1.96e-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: 45.88 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 103 ETELEELRAQVLQLVAELEETRELagqHEDDSLELQgllederlasaQQAEVFTKQIQQLQGElqhlREEISLLEHEKES 182
Cdd:pfam15921 77 ERVLEEYSHQVKDLQRRLNESNEL---HEKQKFYLR-----------QSVIDLQTKLQEMQME----RDAMADIRRRESQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 183 ELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEPSNLS 262
Cdd:pfam15921 139 SQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 263 ISDFSGIQDEL----HHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRR-ATERWLE-SHLLRSTMSSESQTSELD 336
Cdd:pfam15921 219 GSAISKILRELdteiSYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQlISEHEVEiTGLTEKASSARSQANSIQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 337 fPEPDPVMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELqhhRRTSEEEQKRLQRELKCAQNEVL-----RFQTSHSTQE 411
Cdd:pfam15921 299 -SQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREA---KRMYEDKIEELEKQLVLANSELTearteRDQFSQESGN 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 412 LMCRLQKLQAQ-HQcsvNEKEQLLEVQH----------------HLHDKLRCHESEVHRLRSMVDCLREKNEKnsgihlQ 474
Cdd:pfam15921 375 LDDQLQKLLADlHK---REKELSLEKEQnkrlwdrdtgnsitidHLRRELDDRNMEVQRLEALLKAMKSECQG------Q 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 475 LQEMKGLYQFSRDELERQKHMYDQLEQDFLLCQQELTELKSSQSLCEengNCSNKCDALLARLTELQDKFKASQEEIGHL 554
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLE---SSERTVSDLTASLQEKERAIEATNAEITKL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 555 QMEQCELLEDQRRLQEEQGqlqeelhRLTFPQPKCGILQKSQELLSKLQDLCEMQLLYQNMQEQQRKLTQNQECVLKEQL 634
Cdd:pfam15921 523 RSRVDLKLQELQHLKNEGD-------HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQL 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 635 EAHKHLRGFKESHFQeVLANPQDArgpKSSSCENKFKVLmdQLQALQVLYDTSQKQQEVLQrehgrLMEERKRLQAELQL 714
Cdd:pfam15921 596 EKEINDRRLELQEFK-ILKDKKDA---KIRELEARVSDL--ELEKVKLVNAGSERLRAVKD-----IKQERDQLLNEVKT 664
|
650
....*....|....*....
gi 568939544 715 CMEEMQVLQTQSPMIKRSF 733
Cdd:pfam15921 665 SRNELNSLSEDYEVLKRNF 683
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
99-308 |
2.30e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 99 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQiQQLQGELQHLREEISLLEH 178
Cdd:PRK02224 215 LAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERER-EELAEEVRDLRERLEELEE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 179 EK-----ESELKEMEQE-LHLAQAEIQNLRQAAAD-------SATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIA 245
Cdd:PRK02224 294 ERddllaEAGLDDADAEaVEARREELEDRDEELRDrleecrvAAQAHNEEAESLREDADDLEERAEELREEAAELESELE 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 246 SLRAEMELKTSEPSNLsisdfsgiQDELHHLRERYNL-------LNEEYQALRESNSSLTGQLAELESDR 308
Cdd:PRK02224 374 EAREAVEDRREEIEEL--------EEEIEELRERFGDapvdlgnAEDFLEELREERDELREREAELEATL 435
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
100-241 |
2.34e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 100 SLTETELEELRAQVLQLVAELEETR----ELAGQHEDDSLELQGLLEDERLASAQQaevftkQIQQLQGELQHLRE---- 171
Cdd:COG3206 215 KLLLQQLSELESQLAEARAELAEAEarlaALRAQLGSGPDALPELLQSPVIQQLRA------QLAELEAELAELSArytp 288
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568939544 172 ---EISLLEHEKESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYE 241
Cdd:COG3206 289 nhpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
97-709 |
2.65e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 97 RGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGL---LEDERLASAQQAEVFTKQIQQLQGELQHLREEI 173
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRrdkLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 174 SLLEHEKE---SELKEMEQELHLAQAEIQNLRQAAADsateHESDIASLQDDLCRLQNDLDDM-ERIRGDyEMEIASLRA 249
Cdd:TIGR02169 388 KDYREKLEklkREINELKRELDRLQEELQRLSEELAD----LNAAIAGIEAKINELEEEKEDKaLEIKKQ-EWKLEQLAA 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 250 EMELKTSEPSNLSiSDFSGIQDELHHLRERYNLLNEEYQA--------------LRESNSSLTGQLAELESDRTR----- 310
Cdd:TIGR02169 463 DLSKYEQELYDLK-EEYDRVEKELSKLQRELAEAEAQARAseervrggraveevLKASIQGVHGTVAQLGSVGERyatai 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 311 --------------------RATERWLESHLLRST------MSSESQTSE-----------LDFPEPDP-----VMQLLR 348
Cdd:TIGR02169 542 evaagnrlnnvvveddavakEAIELLKRRKAGRATflplnkMRDERRDLSilsedgvigfaVDLVEFDPkyepaFKYVFG 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 349 QQLL---------------------------GA------------------EEQMQDMQDKCKNLYCELEELQHHRRTSE 383
Cdd:TIGR02169 622 DTLVvedieaarrlmgkyrmvtlegelfeksGAmtggsraprggilfsrsePAELQRLRERLEGLKRELSSLQSELRRIE 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 384 EEQKRLQRELKCAQNEvlrfqtshsTQELMCRLQKLQAQHQCSVNEKEQLLEVQHHLHDKLRCHESEVHRLRSMVDCLRE 463
Cdd:TIGR02169 702 NRLDELSQELSDASRK---------IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 464 KNEK---------NSGIHLQLQEMKGLYQFSRDELERQKHMYDQLEQDFLLCQQELTEL-KSSQSLCEENGNCSNKCDAL 533
Cdd:TIGR02169 773 DLHKleealndleARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLeKEIQELQEQRIDLKEQIKSI 852
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 534 LARLTELQDKFKASQEEIGHLQMEQCELLEdqrrlqeeqgqlqeelhrltfpqpKCGILQKSQELLSKlqDLCEMQLLYQ 613
Cdd:TIGR02169 853 EKEIENLNGKKEELEEELEELEAALRDLES------------------------RLGDLKKERDELEA--QLRELERKIE 906
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 614 NMQEQQRKLTQNQEcVLKEQLEAhkhlrgfKESHFQEVLANPqdARGPKSSSCENKFKVLMDQLQALQVL---------- 683
Cdd:TIGR02169 907 ELEAQIEKKRKRLS-ELKAKLEA-------LEEELSEIEDPK--GEDEEIPEEELSLEDVQAELQRVEEEiralepvnml 976
|
730 740 750
....*....|....*....|....*....|
gi 568939544 684 ----YDTSQKQQEVLQREHGRLMEERKRLQ 709
Cdd:TIGR02169 977 aiqeYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
99-231 |
2.71e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 99 LSLTETELEELRAQVLQLVAELEETRELAGQHED------DSLELQGLLEDERLASAQQAEV---FTK---QIQQLQGEL 166
Cdd:COG3206 221 LSELESQLAEARAELAEAEARLAALRAQLGSGPDalpellQSPVIQQLRAQLAELEAELAELsarYTPnhpDVIALRAQI 300
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568939544 167 QHLREEIsllEHEKESELKEMEQELHLAQAEIQNLRQAAADsATEHESDIASLQDDLCRLQNDLD 231
Cdd:COG3206 301 AALRAQL---QQEAQRILASLEAELEALQAREASLQAQLAQ-LEARLAELPELEAELRRLEREVE 361
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
138-493 |
2.85e-04 |
|
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: 45.11 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 138 QGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEHEKESELKEMEQELHLAQAEiqNLRQAAADSA----TEHE 213
Cdd:pfam17380 263 QTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAE--KARQAEMDRQaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 214 SDIASLQDDLCRLQND--LDDMERIRG-DYEMEIASLRaEMELKTSEPSNLSisdfSGIQDELHHLReRYNLLNEEYQal 290
Cdd:pfam17380 341 RMAMERERELERIRQEerKRELERIRQeEIAMEISRMR-ELERLQMERQQKN----ERVRQELEAAR-KVKILEEERQ-- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 291 resnSSLTGQLAELESDRTRRATERWLESHLLRSTMSSESQTSELDFPEPDPVMQLLRQQllgAEEQmqdmqdKCKNLYC 370
Cdd:pfam17380 413 ----RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ---EEER------KRKKLEL 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 371 ELEElQHHRRTSEEEQKRLQRELKCAQNEVLRFQTSHSTqelmcrLQKLQAQHQCSVNEKEQLLEVQHHlhdklRCHESE 450
Cdd:pfam17380 480 EKEK-RDRKRAEEQRRKILEKELEERKQAMIEEERKRKL------LEKEMEERQKAIYEEERRREAEEE-----RRKQQE 547
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 568939544 451 VHRLRSMVDCLREKNEKNSGIHLQLQEMKGLYQFSRDELERQK 493
Cdd:pfam17380 548 MEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
99-250 |
3.86e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 99 LSLTETELEELRAQVLQLVAELEETRELAGQH-------EDDSLELQGLLEDERLASA-QQAEVFTKQIQQLQGELQHLR 170
Cdd:COG3883 60 LEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsGGSVSYLDVLLGSESFSDFlDRLSALSKIADADADLLEELK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 171 EEISLLEhEKESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAE 250
Cdd:COG3883 140 ADKAELE-AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
97-247 |
4.12e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 97 RGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQgllederlASAQQAEVFTKQIQQLQGELQHLREEISLL 176
Cdd:PRK09039 46 REISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLR--------ASLSAAEAERSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568939544 177 EHEKESELKEMEQELHLAQAEIQNLRQaaadsatehesDIASLQDDLCRLQNDLDDMERIRGDYEMEIASL 247
Cdd:PRK09039 118 AGELAQELDSEKQVSARALAQVELLNQ-----------QIAALRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
105-399 |
5.12e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.35 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 105 ELEELRAQVLQLVAELEETRELAGQHeDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLrEEISLLEHEKESEL 184
Cdd:pfam05557 22 ELEHKRARIELEKKASALKRQLDRES-DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYL-EALNKKLNEKESQL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 185 KEMEQELHLAQAEIQNLRQAAADSA---TEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRA------------ 249
Cdd:pfam05557 100 ADAREVISCLKNELSELRRQIQRAElelQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqrikelefei 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 250 ------EMELKTSEPSNLSISDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATERWLESHLLR 323
Cdd:pfam05557 180 qsqeqdSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 324 STMSSES--QTSELDFPEPDP----VMQLLR-------------QQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEE 384
Cdd:pfam05557 260 ELQSWVKlaQDTGLNLRSPEDlsrrIEQLQQreivlkeenssltSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKA 339
|
330
....*....|....*
gi 568939544 385 EQKRLQRELKCAQNE 399
Cdd:pfam05557 340 LVRRLQRRVLLLTKE 354
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
203-424 |
5.35e-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: 43.60 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 203 QAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEPSNLsisdfsgiQDELHHLRERYNL 282
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL--------EQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 283 LNEEYQALRESNSSLTGQLAELESDRTRRATERWLEsHLLRSTMSSESQTSELDFPEpdpVMQLLRQQLLGAEEQMQDMQ 362
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLA-LLLSPEDFLDAVRRLQYLKY---LAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568939544 363 DKCKNLYCELEELQHHRRTSEEEQKRLQRELKcAQNEVLRfQTSHSTQELMCRLQKLQAQHQ 424
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKA-ERQKLLA-RLEKELAELAAELAELQQEAE 223
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
132-377 |
6.78e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 132 DDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELQHLREEISLlEHEKESELKEMEQElhlAQAEIQNLRQAAADSATE 211
Cdd:PHA02562 157 EDLLDISVLSEMDKLNKDKIREL-NQQIQTLDMKIDHIQQQIKT-YNKNIEEQRKKNGE---NIARKQNKYDELVEEAKT 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 212 HESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSE----------PSNLS-ISD----FSGIQDELHHL 276
Cdd:PHA02562 232 IKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVikmyekggvcPTCTQqISEgpdrITKIKDKLKEL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 277 RERYNLLNEEYQALRESNSSLTGQlaelesdrTRRATErwleshlLRSTMSSESQTseldfpepdpvMQLLRQQLLGAEE 356
Cdd:PHA02562 312 QHSLEKLDTAIDELEEIMDEFNEQ--------SKKLLE-------LKNKISTNKQS-----------LITLVDKAKKVKA 365
|
250 260
....*....|....*....|.
gi 568939544 357 QMQDMQDKCKNLYCELEELQH 377
Cdd:PHA02562 366 AIEELQAEFVDNAEELAKLQD 386
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
103-525 |
7.09e-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: 43.95 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 103 ETELEELRAQVLQLVAELE----ETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEH 178
Cdd:pfam15921 259 ELLLQQHQDRIEQLISEHEveitGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 179 EKESELKEMEQELHLAQAEIQNLRQAAADSATEHesdiASLQDDLCRLQNDL---------------------------- 230
Cdd:pfam15921 339 MYEDKIEELEKQLVLANSELTEARTERDQFSQES----GNLDDQLQKLLADLhkrekelslekeqnkrlwdrdtgnsiti 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 231 DDMERIRGDYEMEIASLRAEMELKTSEPSNLSISDFSGIQDELHHLRERYNL---LNEEYQALRESNSSLTGQLAELESd 307
Cdd:pfam15921 415 DHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLtaqLESTKEMLRKVVEELTAKKMTLES- 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 308 rtrraTERWLeshllrSTMSSESQTSELDFPEPDPVMQLLRQQLlgaEEQMQDMQdkckNLYCELEELQHHRrtSEEEQK 387
Cdd:pfam15921 494 -----SERTV------SDLTASLQEKERAIEATNAEITKLRSRV---DLKLQELQ----HLKNEGDHLRNVQ--TECEAL 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 388 RLQRELKCAQNEVLRFQTSHSTQ------ELMCRLQKLQAQHQCSVNEKEQLLEVQHHLHD----KLRCHESEVHRLR-- 455
Cdd:pfam15921 554 KLQMAEKDKVIEILRQQIENMTQlvgqhgRTAGAMQVEKAQLEKEINDRRLELQEFKILKDkkdaKIRELEARVSDLEle 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 456 --SMVDCLREKNEKNSGIHLQLQEMKGLYQFSRDELERQKHMYDQLEQDFLLCQQEL--------TELKSSQSLCEENGN 525
Cdd:pfam15921 634 kvKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMetttnklkMQLKSAQSELEQTRN 713
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
181-398 |
7.39e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 181 ESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQddLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEPSN 260
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQ--LSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 261 LSISdfSGIQDelhhLRERYNLLNEEYQALRESNS-------SLTGQLAELESDRTRRATERWLESHLLRSTMSSESQTs 333
Cdd:COG3206 259 LLQS--PVIQQ----LRAQLAELEAELAELSARYTpnhpdviALRAQIAALRAQLQQEAQRILASLEAELEALQAREAS- 331
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568939544 334 eldfpepdpvmqlLRQQLLGAEEQMQDMQDKcknlyceleelqhhrrtsEEEQKRLQRELKCAQN 398
Cdd:COG3206 332 -------------LQAQLAQLEARLAELPEL------------------EAELRRLEREVEVARE 365
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
137-334 |
9.07e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 137 LQGLLEDERLASAQQAEVFTKQIQQLQGEL-------QHLREEISLLEHEKE-----SELKEMEQELHLAQAEIQNLRQ- 203
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELeeaeaalEEFRQKNGLVDLSEEaklllQQLSELESQLAEARAELAEAEAr 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 204 -----------AAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEPSNLSISDFSGIQDE 272
Cdd:COG3206 242 laalraqlgsgPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAE 321
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568939544 273 LHHLRERYNLLNEEYQALRESNSSLTGQLAELES-DRTRRATERWLESHLLRSTMSSESQTSE 334
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAELPELEAELRRlEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
102-210 |
1.72e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 102 TETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLlederlasAQQAEvftKQIQQLQGELQHLREEISLLEHEKE 181
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGL--------AAELE---EKQQELEAQLEQLQEKAAETSQERK 215
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 568939544 182 SELKEMEQE----LHLAQAEI-----QNLRQAA--ADSAT 210
Cdd:PRK11448 216 QKRKEITDQaakrLELSEEETrilidQQLRKAGweADSKT 255
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
102-311 |
1.87e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 102 TETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEvftkQIQQLQGELQHLREEISLLEHEKE 181
Cdd:COG1196 629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE----LEELAERLAEEELELEEALLAEEE 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 182 SELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERI--RGDYEMEIASLRAEMELKtsEPS 259
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPpdLEELERELERLEREIEAL--GPV 782
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568939544 260 NL-SIsdfsgiqDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRR 311
Cdd:COG1196 783 NLlAI-------EEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
99-206 |
2.07e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 99 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEH 178
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
90 100 110
....*....|....*....|....*....|
gi 568939544 179 EKESELKEMEQ--ELHLAQAEIQNLRQAAA 206
Cdd:COG4717 221 ELEELEEELEQleNELEAAALEERLKEARL 250
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
96-310 |
4.56e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 96 HRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISL 175
Cdd:COG1196 598 GAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEA 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 176 LEHEKESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKT 255
Cdd:COG1196 678 EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELP 757
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568939544 256 SEPSnlsisdfsgiqdeLHHLRERYNLLN--------------EEYQALRESNSSLTGQLAELESDRTR 310
Cdd:COG1196 758 EPPD-------------LEELERELERLEreiealgpvnllaiEEYEELEERYDFLSEQREDLEEARET 813
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
85-204 |
4.60e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 85 GGSLGSLSMGKHRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQG 164
Cdd:COG1196 656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 568939544 165 ELQHLREEISLLEHEKESELKEMEQELHLAQAEIQNLRQA 204
Cdd:COG1196 736 ELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
189-314 |
4.86e-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: 39.91 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 189 QELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEME-LKTSEPSNLSISDFS 267
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkYEEQLGNVRNNKEYE 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 568939544 268 GIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATE 314
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE 139
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
422-723 |
6.15e-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: 40.88 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 422 QHQCSVNEKEQLLEVQHHLHDKLRCHESEVhrlrsmvdcLREKNEKNsgihlQLQEMKGLYQfsrDELERQKHMYDQLEQ 501
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEK---------AREVERRR-----KLEEAEKARQ---AEMDRQAAIYAEQER 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 502 DFLLCQQELTELKSSQSLCEENGNCSNKCDALLARLTELQDKFKASQEEIGHLQME-----QCELLEDQRRLQEEQGQLQ 576
Cdd:pfam17380 342 MAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQEleaarKVKILEEERQRKIQQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 577 EELHRLTFPQPKCGILQKSQEllSKLQDLCEMQLLYQNMQEQQRKLTQNQECVLKEQLEAHKHLRGFKESHFQ--EVLAN 654
Cdd:pfam17380 422 MEQIRAEQEEARQREVRRLEE--ERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQrrKILEK 499
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 655 PQDARGPKSSSCENKFKVLMDQLQALQ-VLYDTSQKQQEVLQREHGRLMEERKRLQAELQLCMEEMQVLQ 723
Cdd:pfam17380 500 ELEERKQAMIEEERKRKLLEKEMEERQkAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE 569
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
108-292 |
6.94e-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: 40.82 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 108 ELRAQVLQLVAELEETRELAGQHEDdslELQGLLEDerlaSAQQAEVFTKQIQQLQGELQHLREEISllehEKESELKEM 187
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIE---NLNGKKEE----LEEELEELEAALRDLESRLGDLKKERD----ELEAQLREL 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 188 EQELHLAQAEIQNLRQAAAD---SATEHESDIASLQDDLCRLQNDLDDmERIRGDYEMEIasLRAEMELKTSEPSN-LSI 263
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRLSElkaKLEALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAEL--QRVEEEIRALEPVNmLAI 978
|
170 180
....*....|....*....|....*....
gi 568939544 264 SDFSGIQDELHHLRERYNLLNEEYQALRE 292
Cdd:TIGR02169 979 QEYEEVLKRLDELKEKRAKLEEERKAILE 1007
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
108-422 |
7.74e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 108 ELRAQVLQLVAE---LEETRELAGQHEDDSLELQGLLE--DERLASAQQAEVFTKQIQQLQGELQhlreeisllehEKES 182
Cdd:PRK04863 294 ELYTSRRQLAAEqyrLVEMARELAELNEAESDLEQDYQaaSDHLNLVQTALRQQEKIERYQADLE-----------ELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 183 ELKEMEQELHLAQaEIQNLRQAAADSAtehESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELktSEPSNLS 262
Cdd:PRK04863 363 RLEEQNEVVEEAD-EQQEENEARAEAA---EEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQL--CGLPDLT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 263 ISDFSGIQDELH-HLRERYNLLNEEYQALRESNS-------------SLTGQLAELESDRTRRATERWLES--HLLRSTM 326
Cdd:PRK04863 437 ADNAEDWLEEFQaKEQEATEELLSLEQKLSVAQAahsqfeqayqlvrKIAGEVSRSEAWDVARELLRRLREqrHLAEQLQ 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 327 SSESQTSELDfpepdpvmQLLRQQlLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELkcAQNEVLRFQTS 406
Cdd:PRK04863 517 QLRMRLSELE--------QRLRQQ-QRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESV--SEARERRMALR 585
|
330
....*....|....*.
gi 568939544 407 HSTQELMCRLQKLQAQ 422
Cdd:PRK04863 586 QQLEQLQARIQRLAAR 601
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
156-561 |
7.85e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 156 TKQIQQLQGELQHLREEISLLEHEKESELKEMEQELHLAQAEIQNLrQAAADSATEHESDIASLQDDLCRLQNDLDDMER 235
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-EELKEEIEELEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 236 IRGDYEMEIASLRAEM-ELKTSEPSNLSISDFSGIQDELhhlRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATE 314
Cdd:PRK03918 267 RIEELKKEIEELEEKVkELKELKEKAEEYIKLSEFYEEY---LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 315 RWLESHLLRSTMSSESQTSELDFPEPDPV-MQLLRQQLLG-----AEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKR 388
Cdd:PRK03918 344 KKKLKELEKRLEELEERHELYEEAKAKKEeLERLKKRLTGltpekLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 389 LQR---ELKCAQNEVL---RFQTSHSTQELMCR----LQKLQAQHQCSVNEKEQLLEVQHHLhDKLRCHESEVHRLRSMV 458
Cdd:PRK03918 424 LKKaieELKKAKGKCPvcgRELTEEHRKELLEEytaeLKRIEKELKEIEEKERKLRKELREL-EKVLKKESELIKLKELA 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 459 DCLREKNEKNSGIHLQlqemkglyqfsrdELERQKHMYDQLEQDFLLCQQELTELKSSqslceengncSNKCDALLARLT 538
Cdd:PRK03918 503 EQLKELEEKLKKYNLE-------------ELEKKAEEYEKLKEKLIKLKGEIKSLKKE----------LEKLEELKKKLA 559
|
410 420
....*....|....*....|...
gi 568939544 539 ELQDKFKASQEEIGHLQMEQCEL 561
Cdd:PRK03918 560 ELEKKLDELEEELAELLKELEEL 582
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
103-192 |
7.92e-03 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 38.37 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 103 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERlasaqqaEVFTKQIQQLQGELQHLREEISLLEHEKES 182
Cdd:pfam09744 49 NVELEELREDNEQLETQYEREKALRKRAEEELEEIEDQWEQET-------KDLLSQVESLEEENRRLEADHVSRLEEKEA 121
|
90
....*....|
gi 568939544 183 ELKEMEQELH 192
Cdd:pfam09744 122 ELKKEYSKLH 131
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
108-314 |
9.12e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.42 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 108 ELRAQvlqLVAELEETRELAGQHEDDSLElQGLLEderlASAQQAEVfTKQIQQLQGELQHLREEISLLEHEKEselkem 187
Cdd:PRK10929 83 ELRQQ---LNNERDEPRSVPPNMSTDALE-QEILQ----VSSQLLEK-SRQAQQEQDRAREISDSLSQLPQQQT------ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939544 188 eqELHLAQAEIQNLRQAAADSATEH-ESDIASLQDDLCRLQNDLD--DMERIRGDYEMEIASLRAEMelktsepsnlsis 264
Cdd:PRK10929 148 --EARRQLNEIERRLQTLGTPNTPLaQAQLTALQAESAALKALVDelELAQLSANNRQELARLRSEL------------- 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568939544 265 dfsgiqdelhhLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATE 314
Cdd:PRK10929 213 -----------AKKRSQQLDAYLQALRNQLNSQRQREAERALESTELLAE 251
|
|
| |
