|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
106-426 |
1.22e-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: 69.32 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 106 LEELRAQV--LQLVAEL-EETRELAGQHEDDSLELQGL----LEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEH 178
Cdd:TIGR02168 195 LNELERQLksLERQAEKaERYKELKAELRELELALLVLrleeLREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 179 EKEselkEMEQELHLAQAEIQNLRQAAAD---SATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKT 255
Cdd:TIGR02168 275 EVS----ELEEEIEELQKELYALANEISRleqQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 256 SEPSNLSiSDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRraterwLESHLLRSTMSSESQTSEL 335
Cdd:TIGR02168 351 EELESLE-AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER------LEARLERLEDRRERLQQEI 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 336 dfpepdpvmQLLRQQLlgAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELKCAQNEVLRFQTSHSTQNSGIH 415
Cdd:TIGR02168 424 ---------EELLKKL--EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
330
....*....|.
gi 1907172349 416 LqLQEMKGLYQ 426
Cdd:TIGR02168 493 S-LERLQENLE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
99-307 |
1.25e-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: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 99 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDerlaSAQQAEVFTKQIQQLQGELQHLREEIslleH 178
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ----LKEELKALREALDELRAELTLLNEEA----A 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 179 EKESELKEMEQELHLAQAEIQNLRQAAAD---SATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKT 255
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEElseDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907172349 256 SEPSNLSiSDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESD 307
Cdd:TIGR02168 901 EELRELE-SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
103-436 |
5.55e-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: 5.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 103 ETELEELRAQV------LQLVAELEETRELAGQHEDDSLELQ-GLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISL 175
Cdd:COG1196 199 ERQLEPLERQAekaeryRELKEELKELEAELLLLKLRELEAElEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 176 LEHEKEsELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKt 255
Cdd:COG1196 279 LELELE-EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 256 sepsnlsisdfsgiQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTR-RATERWLESHLLRSTMSSESQTSE 334
Cdd:COG1196 357 --------------EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAElAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 335 LdfpepdpvmQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELKCAQNEVLRFQTSHSTQNSGI 414
Cdd:COG1196 423 L---------EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
330 340
....*....|....*....|..
gi 1907172349 415 HLQLQEMKGLYQFSRDELERQK 436
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALL 515
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
99-335 |
5.89e-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: 5.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 99 LSLTETELEELRAQVLQLVAELEET----RELAGQHEDDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELQHLREEIS 174
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELeaelEELRLELEELELELEEAQAEEYELLAELARL-EQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 175 llehEKESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDdlcrLQNDLDDMERIRGDYEMEIASLRAEMELK 254
Cdd:COG1196 320 ----ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE----AEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 255 TSEPSNLSISDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATERWLESHLLRSTMSSESQTSE 334
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
.
gi 1907172349 335 L 335
Cdd:COG1196 472 A 472
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
102-393 |
1.11e-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: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 102 TETELEELRAQVLQLVAELEETR----ELAGQHEDDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELQHLREEISLLE 177
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEkalaELRKELEELEEELEQLRKELEELSRQISAL-RKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 178 HekesELKEMEQELHLAQAEIQNLRQAAAdsatEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSE 257
Cdd:TIGR02168 754 K----ELTELEAEIEELEERLEEAEEELA----EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 258 PSNLsisdfsgiQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATErwLESHLLRSTMSSESqtseldf 337
Cdd:TIGR02168 826 LESL--------ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE--LEALLNERASLEEA------- 888
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907172349 338 pepdpvMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQREL 393
Cdd:TIGR02168 889 ------LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
99-356 |
1.15e-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: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 99 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQG---LLEDERLASAQQAEVFTKQIQQLQGELQHLREEISL 175
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQdiaRLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 176 LEHEK---ESELKEMEQELHLAQAEIQNL---RQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRA 249
Cdd:COG1196 342 LEEELeeaEEELEEAEAELAEAEEALLEAeaeLAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 250 EMELKTSEPSNLSISdfsgIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATERW-LESHLLRSTMSS 328
Cdd:COG1196 422 ELEELEEALAELEEE----EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEeLAEAAARLLLLL 497
|
250 260
....*....|....*....|....*...
gi 1907172349 329 ESQTSELDFPEPDPVMQLLRQQLLGAEE 356
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
102-386 |
3.67e-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: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 102 TETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLED-----ERLASAQQAEVfTKQIQQLQGELQHLREEISll 176
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElnkkiKDLGEEEQLRV-KEKIGELEAEIASLERSIA-- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 177 ehEKESELKEMEQELHLAQAEIQNLRQAAADSATEHES---DIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEmel 253
Cdd:TIGR02169 312 --EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEerkRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE--- 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 254 ktsepsnlsisdFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTrRATERWLESHLLRSTMSSESQTS 333
Cdd:TIGR02169 387 ------------LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA-GIEAKINELEEEKEDKALEIKKQ 453
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1907172349 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 |
8.01e-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: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 99 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERlasaqqaevftkqIQQLQGELQHLREEISLLE- 177
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR-------------IPEIQAELSKLEEEVSRIEa 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 178 --HEKESELKEMEQELHLAQAEIQNLRQAAADSatehESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKT 255
Cdd:TIGR02169 813 rlREIEQKLNRLTLEKEYLEKEIQELQEQRIDL----KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 256 SEPSNLsisdfsgiQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDrtrraterwlESHLLRSTMSSESQtsel 335
Cdd:TIGR02169 889 KERDEL--------EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE----------LSEIEDPKGEDEEI---- 946
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907172349 336 dfPEPDPVMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRE 392
Cdd:TIGR02169 947 --PEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
99-315 |
2.40e-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: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 99 LSLTETELEELRAQVLQLvaelEETRELAGQHEDDSLELQGLledERLASAQQAEVFTKQIQQLQGELQHLREEISLLEH 178
Cdd:COG4913 237 LERAHEALEDAREQIELL----EPIRELAERYAAARERLAEL---EYLRAALRLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 179 EK---ESELKEmeqelhlAQAEIQNLRQAAADSATEhesDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLraemelkt 255
Cdd:COG4913 310 ELerlEARLDA-------LREELDELEAQIRGNGGD---RLEQLEREIERLERELEERERRRARLEALLAAL-------- 371
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 256 SEPSNLSISDFSGIQDELHHLRERynlLNEEYQALRESNSSLTGQLAELESDRTRRATER 315
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
106-318 |
7.16e-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: 7.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 106 LEELRAQVLQLVAELEETRELAGQHEDdsleLQGLLEDERLASAQQAEVFTKQI--QQLQGELQHLREEISLLEhEKESE 183
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEA----ELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLD-ASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 184 LKEMEQELHLAQAEIQNLRQ---AAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEmeiaSLRAEMELKTSEPSN 260
Cdd:COG4913 687 LAALEEQLEELEAELEELEEeldELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL----RALLEERFAAALGDA 762
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907172349 261 LSISDFSGIQDELHHLRERYNLLNEEYQALR------------------ESNSSLTGQLAELESDRTRRATERWLE 318
Cdd:COG4913 763 VERELRENLEERIDALRARLNRAEEELERAMrafnrewpaetadldadlESLPEYLALLDRLEEDGLPEYEERFKE 838
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
179-457 |
8.54e-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: 56.60 E-value: 8.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 179 EKESELKEMEQELHLAQAEIQNLRQAAADSATEHEsdiaSLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEP 258
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELE----ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 259 SNLSI-------------SDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATERwlesHLLRST 325
Cdd:TIGR02168 750 AQLSKelteleaeieeleERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA----ANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 326 MSSESQTSELDFPEPDPVMQLLRQ---QLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKR-------LQRELKC 395
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEElseDIESLAAEIEELEELIEELESELEALLNERASLEEALALlrseleeLSEELRE 905
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907172349 396 AQNEVLRFQTSHS---TQNSGIHLQLQ--EMKGLYQFSR------DELERQKHMYDQLEQDFLLCQQELTELK 457
Cdd:TIGR02168 906 LESKRSELRRELEelrEKLAQLELRLEglEVRIDNLQERlseeysLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
146-385 |
9.65e-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: 55.54 E-value: 9.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 146 LASAQQAEVFTKQIQQLQGELQHLREEISLLEHEKES---ELKEMEQELHLAQAEIQNLRQAAADSatehESDIASLQDD 222
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAllkQLAALERRIAALARRIRALEQELAAL----EAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 223 LCRLQNDLDDM-----ERIRGDYEMEIASlrAEMELKTSEPSNLSISDFSGIQDELHHLRERYNLLNEEYQALRESNSSL 297
Cdd:COG4942 92 IAELRAELEAQkeelaELLRALYRLGRQP--PLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 298 TGQLAELESDRTRRATERwlesHLLRSTMSSESQTseldfpepdpvMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQH 377
Cdd:COG4942 170 EAERAELEALLAELEEER----AALEALKAERQKL-----------LARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
....*...
gi 1907172349 378 HRRTSEEE 385
Cdd:COG4942 235 EAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
96-249 |
9.72e-08 |
|
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: 9.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 96 HRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDdslELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISL 175
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALRE---ELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907172349 176 LEHEkeseLKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRA 249
Cdd:COG4913 364 LEAL----LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
103-290 |
2.36e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 103 ETELEELRAQVLQLVAELEETRElagQHEDDSLELQGLLEDERLASAQQAEVFTK-QIQQLQGELQHLREEISLLEHE-- 179
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQ---KNGLVDLSEEAKLLLQQLSELESQLAEARaELAEAEARLAALRAQLGSGPDAlp 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 180 ---KESELKEMEQELHLAQAEIQNLRQaaadSATEHESDIASLQDDLCRLQNDLDD-MERIRGDYEMEIASLRAEMELKT 255
Cdd:COG3206 258 ellQSPVIQQLRAQLAELEAELAELSA----RYTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQ 333
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907172349 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 |
2.46e-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: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 97 RGLSLTETELEELRAQVLQLVAELEE--TRELAGQHEDDSLELQGLLEDERLASAQ-QAEVFTKQIQQLQGELQHLREEI 173
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEElqKELYALANEISRLEQQKQILRERLANLErQLEELEAQLEELESKLDELAEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 174 SLLEHEKES---ELKEMEQELHLAQAEIQNLRQAAADSATEHE---SDIASLQDDLCRLQNDLDDMERIRGDYEMEIASL 247
Cdd:TIGR02168 340 AELEEKLEElkeELESLEAELEELEAELEELESRLEELEEQLEtlrSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 248 RAEMElktSEPSNLSISDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDrtRRATERWLESHLLRSTMS 327
Cdd:TIGR02168 420 QQEIE---ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA--LDAAERELAQLQARLDSL 494
|
250
....*....|..
gi 1907172349 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 |
1.20e-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: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 103 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDerlASAQQAEVFT-KQIQQLQGELQHLREEISLLEheke 181
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK---YEEQLGNVRNnKEYEALQKEIESLKRRISDLE---- 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907172349 182 SELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEI 244
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
107-676 |
1.69e-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: 52.43 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 107 EELRAQVLQLVAELEETRELAgqheddslelQGLLEDerlaSAQQAEVFTKQIQQLQGELQHLReeiSLLEHEKESELKE 186
Cdd:pfam15921 141 EDLRNQLQNTVHELEAAKCLK----------EDMLED----SNTQIEQLRKMMLSHEGVLQEIR---SILVDFEEASGKK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 187 MEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLD--------DMERIRGDYEMEIASLRAEMELKTS-- 256
Cdd:pfam15921 204 IYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEalksesqnKIELLLQQHQDRIEQLISEHEVEITgl 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 257 -EPSNLSISDFSGIQDELHHLRERynllneeyqaLRESNSSLTGQLAELESDRTRraterwleshlLRSTMSSESQTSEL 335
Cdd:pfam15921 284 tEKASSARSQANSIQSQLEIIQEQ----------ARNQNSMYMRQLSDLESTVSQ-----------LRSELREAKRMYED 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 336 DFPEPDPVMQLLRQQLLGAEEQMQDMQDKCKNLYCELEEL--QHHRRTSE-----EEQKRL--------------QRELK 394
Cdd:pfam15921 343 KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLlaDLHKREKElslekEQNKRLwdrdtgnsitidhlRRELD 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 395 CAQNEVLRFQTSHSTQNSGIHLQLQEMKGLYQFSRDELERQKHMYDQLEQDFLLCQQELTELKSSQSLCEengNCSNKCD 474
Cdd:pfam15921 423 DRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLE---SSERTVS 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 475 ALLARLTELQDKFKASQEEIGHLQMEQCELLEDQRRLQEEQGqlqeelhRLTFPQPKCGILQKSQELLSKLQDLCEMQLL 554
Cdd:pfam15921 500 DLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGD-------HLRNVQTECEALKLQMAEKDKVIEILRQQIE 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 555 YQNMQEQQRKLTQNQECVLKEQLEAHKHLRGFKESHFQeVLANPQDArgpKSSSCENKFKVLmdQLQALQVLYDTSQKQQ 634
Cdd:pfam15921 573 NMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFK-ILKDKKDA---KIRELEARVSDL--ELEKVKLVNAGSERLR 646
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1907172349 635 EVLQrehgrLMEERKRLQAELQLCMEEMQVLQTQSPMIKRSF 676
Cdd:pfam15921 647 AVKD-----IKQERDQLLNEVKTSRNELNSLSEDYEVLKRNF 683
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
150-318 |
2.99e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 150 QQAEVFTKQIQQLQGELQHLREEISllehEKESELKEMEQELHLAQAEIQNLRQAAADSATEHEsdIASLQDDLCRLQND 229
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELE----ELEAELEELREELEKLEKLLQLLPLYQELEALEAE--LAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 230 LDDMERIRGDYEM---EIASLRAEMELKTSEPSNLSISDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELES 306
Cdd:COG4717 155 LEELRELEEELEEleaELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
170
....*....|..
gi 1907172349 307 DRTRRATERWLE 318
Cdd:COG4717 235 ELEAAALEERLK 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
97-268 |
1.20e-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: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 97 RGLSLTETELEELRAQVLQLVAELEETREL----------AGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGEL 166
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEElaellralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 167 QHLREEISLLEHEKESELKEMEQELHLAQAEIQNLRQAAAdsatEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIAS 246
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKA----ERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
170 180
....*....|....*....|..
gi 1907172349 247 LRAEMELKTSEPSNLSISDFSG 268
Cdd:COG4942 232 LEAEAAAAAERTPAAGFAALKG 253
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
102-315 |
1.24e-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: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 102 TETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELQHLREEISLLEHEKE 181
Cdd:COG4913 666 AEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRL-EKELEQAEEELDELQDRLEAAEDLAR 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 182 SELKEMEQElHLAQAEIQNLRQAAADSAtehESDIASLQDDLCRLQNDLDD-MERIRGDYEMEIASLRAEMElktsepsn 260
Cdd:COG4913 745 LELRALLEE-RFAAALGDAVERELRENL---EERIDALRARLNRAEEELERaMRAFNREWPAETADLDADLE-------- 812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907172349 261 lSISDFSGI-----QDELHHLRERYN-LLNEeyqalrESNSSLTGQLAELESDRtRRATER 315
Cdd:COG4913 813 -SLPEYLALldrleEDGLPEYEERFKeLLNE------NSIEFVADLLSKLRRAI-REIKER 865
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
161-510 |
1.66e-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: 49.30 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 161 QLQGELQHLREEISLLEHEKESELKEmeqelhlaQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDY 240
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSE--------LRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 241 EMEIASLRAEMELKTSEPSNLsISDFSGIQDELHHLRERYNLL------------NEEYQALRESNSSLTGQLAELESDR 308
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKEL-EARIEELEEDLHKLEEALNDLearlshsripeiQAELSKLEEEVSRIEARLREIEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 309 TRRaterwlesHLLRSTMSSESQTSELDFPEPDPVMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKR 388
Cdd:TIGR02169 822 NRL--------TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 389 LQRELKCAQNEVLRFQTSHSTQNSGIhLQLQEMKGLYQFSRDELERQKHM----------YDQLEQDFLLCQQELTELKS 458
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIEKKRKRL-SELKAKLEALEEELSEIEDPKGEdeeipeeelsLEDVQAELQRVEEEIRALEP 972
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1907172349 459 SQSLCEEngncsnKCDALLARLTELQDKFKASQEEIGHLQmEQCELLEDQRR 510
Cdd:TIGR02169 973 VNMLAIQ------EYEEVLKRLDELKEKRAKLEEERKAIL-ERIEEYEKKKR 1017
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
141-321 |
1.67e-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: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 141 LEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLehEKESELKEMEQELHLAQAEIQNLRQAAADsATEHESDIASLQ 220
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREAL--QRLAEYSWDEIDVASAEREIAELEAELER-LDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 221 DDLCRLQNDLDDMERIRGDYEMEIASLRAEMElktsepsnlsisdfsGIQDELHHLRERYNLLNEEYQAlrESNSSLTGQ 300
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELE---------------QAEEELDELQDRLEAAEDLARL--ELRALLEER 754
|
170 180
....*....|....*....|.
gi 1907172349 301 LAELESDRTRRATERWLESHL 321
Cdd:COG4913 755 FAAALGDAVERELRENLEERI 775
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
104-292 |
1.79e-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: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 104 TELEELRAQVLQLVAELEETRELAGQHEDDSLE-LQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEHEK-- 180
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLELLEaELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRle 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 181 --ESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEp 258
Cdd:COG4913 342 qlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE- 420
|
170 180 190
....*....|....*....|....*....|....
gi 1907172349 259 snlsisdFSGIQDELHHLRERYNLLNEEYQALRE 292
Cdd:COG4913 421 -------LRELEAEIASLERRKSNIPARLLALRD 447
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
105-500 |
9.87e-05 |
|
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: 46.27 E-value: 9.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 105 ELEELRAQVLQLVAELEETRELAGQHeDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLrEEISLLEHEKESEL 184
Cdd:pfam05557 22 ELEHKRARIELEKKASALKRQLDRES-DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYL-EALNKKLNEKESQL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 185 KEMEQELHLAQAEIQNLRQAAADSA---TEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRA------------ 249
Cdd:pfam05557 100 ADAREVISCLKNELSELRRQIQRAElelQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqrikelefei 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 250 ------EMELKTSEPSNLSISDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATERWLESHLLR 323
Cdd:pfam05557 180 qsqeqdSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 324 STMSSES--QTSELDFPEPDP----VMQLLR-------------QQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEE 384
Cdd:pfam05557 260 ELQSWVKlaQDTGLNLRSPEDlsrrIEQLQQreivlkeenssltSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 385 EQKRLQRELKCAQNE-------VLRFQTSHSTQNSGIHLQ---------LQEMKGLYQFSRDELERQKHMYDQLEQDFLL 448
Cdd:pfam05557 340 LVRRLQRRVLLLTKErdgyraiLESYDKELTMSNYSPQLLerieeaedmTQKMQAHNEEMEAQLSVAEEELGGYKQQAQT 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1907172349 449 CQQELTELKSSQSLcEENGNCSNKCDALLARLTELQDKFKASQEEIGHLQME 500
Cdd:pfam05557 420 LERELQALRQQESL-ADPSYSKEEVDSLRRKLETLELERQRLREQKNELEME 470
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
102-314 |
1.05e-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: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 102 TETELEELRAQVLQLVAELEETRelagQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEHEKE 181
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALK----KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 182 SELKEMEQELHLAQAEIQNLR----------QAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEM 251
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPlalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907172349 252 ELKTSEPSNLSiSDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATE 314
Cdd:COG4942 181 AELEEERAALE-ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
99-308 |
2.09e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 99 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQiQQLQGELQHLREEISLLEH 178
Cdd:PRK02224 215 LAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERER-EELAEEVRDLRERLEELEE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 179 EK-----ESELKEMEQE-LHLAQAEIQNLRQAAAD-------SATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIA 245
Cdd:PRK02224 294 ERddllaEAGLDDADAEaVEARREELEDRDEELRDrleecrvAAQAHNEEAESLREDADDLEERAEELREEAAELESELE 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 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 |
2.61e-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: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 100 SLTETELEELRAQVLQLVAELEETR----ELAGQHEDDSLELQGLLEDERLASAQQaevftkQIQQLQGELQHLRE---- 171
Cdd:COG3206 215 KLLLQQLSELESQLAEARAELAEAEarlaALRAQLGSGPDALPELLQSPVIQQLRA------QLAELEAELAELSArytp 288
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907172349 172 ---EISLLEHEKESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYE 241
Cdd:COG3206 289 nhpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
99-231 |
3.18e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 99 LSLTETELEELRAQVLQLVAELEETRELAGQHED------DSLELQGLLEDERLASAQQAEV---FTK---QIQQLQGEL 166
Cdd:COG3206 221 LSELESQLAEARAELAEAEARLAALRAQLGSGPDalpellQSPVIQQLRAQLAELEAELAELsarYTPnhpDVIALRAQI 300
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907172349 167 QHLREEIsllEHEKESELKEMEQELHLAQAEIQNLRQAAADsATEHESDIASLQDDLCRLQNDLD 231
Cdd:COG3206 301 AALRAQL---QQEAQRILASLEAELEALQAREASLQAQLAQ-LEARLAELPELEAELRRLEREVE 361
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
97-247 |
4.24e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 97 RGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQgllederlASAQQAEVFTKQIQQLQGELQHLREEISLL 176
Cdd:PRK09039 46 REISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLR--------ASLSAAEAERSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907172349 177 EHEKESELKEMEQELHLAQAEIQNLRQaaadsatehesDIASLQDDLCRLQNDLDDMERIRGDYEMEIASL 247
Cdd:PRK09039 118 AGELAQELDSEKQVSARALAQVELLNQ-----------QIAALRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
99-250 |
6.01e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 99 LSLTETELEELRAQVLQLVAELEETRELAGQH-------EDDSLELQGLLEDERLASA-QQAEVFTKQIQQLQGELQHLR 170
Cdd:COG3883 60 LEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsGGSVSYLDVLLGSESFSDFlDRLSALSKIADADADLLEELK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 171 EEISLLEhEKESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAE 250
Cdd:COG3883 140 ADKAELE-AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
132-377 |
6.61e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 132 DDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELQHLREEISLlEHEKESELKEMEQElhlAQAEIQNLRQAAADSATE 211
Cdd:PHA02562 157 EDLLDISVLSEMDKLNKDKIREL-NQQIQTLDMKIDHIQQQIKT-YNKNIEEQRKKNGE---NIARKQNKYDELVEEAKT 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 212 HESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSE----------PSNLS-ISD----FSGIQDELHHL 276
Cdd:PHA02562 232 IKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVikmyekggvcPTCTQqISEgpdrITKIKDKLKEL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 277 RERYNLLNEEYQALRESNSSLTGQlaelesdrTRRATErwleshlLRSTMSSESQTseldfpepdpvMQLLRQQLLGAEE 356
Cdd:PHA02562 312 QHSLEKLDTAIDELEEIMDEFNEQ--------SKKLLE-------LKNKISTNKQS-----------LITLVDKAKKVKA 365
|
250 260
....*....|....*....|.
gi 1907172349 357 QMQDMQDKCKNLYCELEELQH 377
Cdd:PHA02562 366 AIEELQAEFVDNAEELAKLQD 386
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
181-398 |
8.68e-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: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 181 ESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQddLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEPSN 260
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQ--LSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 261 LSISdfSGIQDelhhLRERYNLLNEEYQALRESNS-------SLTGQLAELESDRTRRATERWLESHLLRSTMSSESQTs 333
Cdd:COG3206 259 LLQS--PVIQQ----LRAQLAELEAELAELSARYTpnhpdviALRAQIAALRAQLQQEAQRILASLEAELEALQAREAS- 331
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907172349 334 eldfpepdpvmqlLRQQLLGAEEQMQDMQDKcknlyceleelqhhrrtsEEEQKRLQRELKCAQN 398
Cdd:COG3206 332 -------------LQAQLAQLEARLAELPEL------------------EAELRRLEREVEVARE 365
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
137-334 |
1.02e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 137 LQGLLEDERLASAQQAEVFTKQIQQLQGEL-------QHLREEISLLEHEKE-----SELKEMEQELHLAQAEIQNLRQ- 203
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELeeaeaalEEFRQKNGLVDLSEEaklllQQLSELESQLAEARAELAEAEAr 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 204 -----------AAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEPSNLSISDFSGIQDE 272
Cdd:COG3206 242 laalraqlgsgPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAE 321
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907172349 273 LHHLRERYNLLNEEYQALRESNSSLTGQLAELES-DRTRRATERWLESHLLRSTMSSESQTSE 334
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAELPELEAELRRlEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
102-210 |
1.64e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 102 TETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLlederlasAQQAEvftKQIQQLQGELQHLREEISLLEHEKE 181
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGL--------AAELE---EKQQELEAQLEQLQEKAAETSQERK 215
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1907172349 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 |
1.79e-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: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 102 TETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEvftkQIQQLQGELQHLREEISLLEHEKE 181
Cdd:COG1196 629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE----LEELAERLAEEELELEEALLAEEE 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 182 SELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERI--RGDYEMEIASLRAEMELKtsEPS 259
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPpdLEELERELERLEREIEAL--GPV 782
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907172349 260 NL-SIsdfsgiqDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRR 311
Cdd:COG1196 783 NLlAI-------EEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
99-206 |
1.83e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 99 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEH 178
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
90 100 110
....*....|....*....|....*....|
gi 1907172349 179 EKESELKEMEQ--ELHLAQAEIQNLRQAAA 206
Cdd:COG4717 221 ELEELEEELEQleNELEAAALEERLKEARL 250
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
138-445 |
2.12e-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: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 138 QGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEHEKESELKEMEQELHLAQAEiqNLRQAAADSA----TEHE 213
Cdd:pfam17380 263 QTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAE--KARQAEMDRQaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 214 SDIASLQDDLCRLQND--LDDMERIRG-DYEMEIASLRaEMELKTSEPSNLSisdfSGIQDELHHLReRYNLLNEEYQal 290
Cdd:pfam17380 341 RMAMERERELERIRQEerKRELERIRQeEIAMEISRMR-ELERLQMERQQKN----ERVRQELEAAR-KVKILEEERQ-- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 291 resnSSLTGQLAELESDRTRRATERWLESHLLRSTMSSESQTSELDFPEPDPVMQLLRQQ---------LLGAEEQMQDM 361
Cdd:pfam17380 413 ----RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQeeerkrkklELEKEKRDRKR 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 362 QDKCKNLYCELEELQHHRRTSEEEQKR--LQRELKCAQNEVLRFQTSHSTQ---------NSGIHLQLQEMKGLYQFSR- 429
Cdd:pfam17380 489 AEEQRRKILEKELEERKQAMIEEERKRklLEKEMEERQKAIYEEERRREAEeerrkqqemEERRRIQEQMRKATEERSRl 568
|
330
....*....|....*.
gi 1907172349 430 DELERQKHMYDQLEQD 445
Cdd:pfam17380 569 EAMEREREMMRQIVES 584
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
348-666 |
2.33e-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: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 348 RQQLLGAEEQMQDMQDKCKNLYCELEELQHHRrtsEEEQKRLQRELKCAQNEVLRFQTshstqnsgIHLQLQEMKGLyqf 427
Cdd:pfam17380 315 RRKLEEAEKARQAEMDRQAAIYAEQERMAMER---ERELERIRQEERKRELERIRQEE--------IAMEISRMREL--- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 428 SRDELERQkhmydqleQDFLLCQQELtELKSSQSLCEEngncsnkcdallarltELQDKFKASQEEIGHLQMEQCELLED 507
Cdd:pfam17380 381 ERLQMERQ--------QKNERVRQEL-EAARKVKILEE----------------ERQRKIQQQKVEMEQIRAEQEEARQR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 508 QRRLQEEQGQLQEELHRltfpqpkcgilqksQELLSKLQdlcEMQLLYQNMQEQQRKltqnqecvlKEQLEAHKHLRGFK 587
Cdd:pfam17380 436 EVRRLEEERAREMERVR--------------LEEQERQQ---QVERLRQQEEERKRK---------KLELEKEKRDRKRA 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 588 ESHFQEVLANPQDARGPKSSSCENKFKVLMDQLQALQ-VLYDTSQKQQEVLQREHGRLMEERKRLQAELQLCMEEMQVLQ 666
Cdd:pfam17380 490 EEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQkAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE 569
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
103-494 |
2.42e-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: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 103 ETELEELRAQVLQLVAELE----ETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEH 178
Cdd:pfam15921 259 ELLLQQHQDRIEQLISEHEveitGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 179 EKESELKEMEQELHLAQAEIQNLRQAAADSATEHesdiASLQDDLCRLQNDL---------------------------- 230
Cdd:pfam15921 339 MYEDKIEELEKQLVLANSELTEARTERDQFSQES----GNLDDQLQKLLADLhkrekelslekeqnkrlwdrdtgnsiti 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 231 DDMERIRGDYEMEIASLRAEMELKTSEPSNLSISDFSGIQDELHHLRERYNL---LNEEYQALRESNSSLTGQLAELE-S 306
Cdd:pfam15921 415 DHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLtaqLESTKEMLRKVVEELTAKKMTLEsS 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 307 DRTRRATERWLESHlLRSTMSSESQTSELDfPEPDPVMQLLrQQLLGAEEQMQDMQDKCKNLYCELEE------------ 374
Cdd:pfam15921 495 ERTVSDLTASLQEK-ERAIEATNAEITKLR-SRVDLKLQEL-QHLKNEGDHLRNVQTECEALKLQMAEkdkvieilrqqi 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 375 ------LQHHRRTS---EEEQKRLQRELKCAQNEVLRFQTSHSTQNSGIH--------LQLQEMKGLYQFSR--DELERQ 435
Cdd:pfam15921 572 enmtqlVGQHGRTAgamQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRelearvsdLELEKVKLVNAGSErlRAVKDI 651
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907172349 436 KHMYDQLEQDFLLCQQELTELKSSQSLCEEngNCSNKCDALLARLTELQDKFKASQEEI 494
Cdd:pfam15921 652 KQERDQLLNEVKTSRNELNSLSEDYEVLKR--NFRNKSEEMETTTNKLKMQLKSAQSEL 708
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
189-314 |
3.97e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 189 QELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEME-LKTSEPSNLSISDFS 267
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkYEEQLGNVRNNKEYE 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1907172349 268 GIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATE 314
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE 139
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
96-310 |
4.37e-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: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 96 HRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISL 175
Cdd:COG1196 598 GAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEA 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 176 LEHEKESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKT 255
Cdd:COG1196 678 EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELP 757
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907172349 256 SEPSnlsisdfsgiqdeLHHLRERYNLLN--------------EEYQALRESNSSLTGQLAELESDRTR 310
Cdd:COG1196 758 EPPD-------------LEELERELERLEreiealgpvnllaiEEYEELEERYDFLSEQREDLEEARET 813
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
203-402 |
4.72e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 203 QAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEPSNLsisdfsgiQDELHHLRERYNL 282
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL--------EQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 283 LNEEYQALRESNSSLTGQLAELESDRTRRATERWLEsHLLRSTMSSESQTSELDFPEpdpVMQLLRQQLLGAEEQMQDMQ 362
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLA-LLLSPEDFLDAVRRLQYLKY---LAPARREQAEELRADLAELA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907172349 363 DKCKNLYCELEELQHHRRTSEEEQKRLQRELKcAQNEVLR 402
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKA-ERQKLLA 202
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
279-494 |
5.43e-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: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 279 RYNLLNEEYQALRESNSSLTGQLAELE---SDRTRRATERWLESHLLRSTMSSES-QTSELDFPEPDPV----------M 344
Cdd:TIGR02169 224 EGYELLKEKEALERQKEAIERQLASLEeelEKLTEEISELEKRLEEIEQLLEELNkKIKDLGEEEQLRVkekigeleaeI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 345 QLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELKCAQNEVLRFQTSHSTQNSgihlQLQEMKGL 424
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA----ELEEVDKE 379
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907172349 425 YQFSRDELERQKHMYDQLEQDFLLCQQELTEL-KSSQSLCEENGNCSNKCDALLARLTELQDKFKASQEEI 494
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRELDRLqEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
103-192 |
5.97e-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: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 103 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERlasaqqaEVFTKQIQQLQGELQHLREEISLLEHEKES 182
Cdd:pfam09744 49 NVELEELREDNEQLETQYEREKALRKRAEEELEEIEDQWEQET-------KDLLSQVESLEEENRRLEADHVSRLEEKEA 121
|
90
....*....|
gi 1907172349 183 ELKEMEQELH 192
Cdd:pfam09744 122 ELKKEYSKLH 131
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
108-292 |
6.54e-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: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 108 ELRAQVLQLVAELEETRELAGQHEDdslELQGLLEDerlaSAQQAEVFTKQIQQLQGELQHLREEISllehEKESELKEM 187
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIE---NLNGKKEE----LEEELEELEAALRDLESRLGDLKKERD----ELEAQLREL 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 188 EQELHLAQAEIQNLRQAAAD---SATEHESDIASLQDDLCRLQNDLDDmERIRGDYEMEIasLRAEMELKTSEPSN-LSI 263
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRLSElkaKLEALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAEL--QRVEEEIRALEPVNmLAI 978
|
170 180
....*....|....*....|....*....
gi 1907172349 264 SDFSGIQDELHHLRERYNLLNEEYQALRE 292
Cdd:TIGR02169 979 QEYEEVLKRLDELKEKRAKLEEERKAILE 1007
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
97-487 |
7.54e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 97 RGLSLTETELE-ELRAQVLQLVAE---LEETRELAGQHEDDSLELQGLLE--DERLASAQQAEVFTKQIQQLQGELQhlr 170
Cdd:PRK04863 282 RVHLEEALELRrELYTSRRQLAAEqyrLVEMARELAELNEAESDLEQDYQaaSDHLNLVQTALRQQEKIERYQADLE--- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 171 eeisllehEKESELKEMEQELHLAQaEIQNLRQAAADSAtehESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAE 250
Cdd:PRK04863 359 --------ELEERLEEQNEVVEEAD-EQQEENEARAEAA---EEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERA 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 251 MELktSEPSNLSISDFSGIQDELH-HLRERYNLLNEEYQALRESNS-------------SLTGQLAELESDRTRRATERW 316
Cdd:PRK04863 427 KQL--CGLPDLTADNAEDWLEEFQaKEQEATEELLSLEQKLSVAQAahsqfeqayqlvrKIAGEVSRSEAWDVARELLRR 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 317 LES--HLLRSTMSSESQTSEL--DFPEPDPVMQLLRqQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRE 392
Cdd:PRK04863 505 LREqrHLAEQLQQLRMRLSELeqRLRQQQRAERLLA-EFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMA 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 393 LKcAQNEVLRFQTSHSTQNSGIHLQLQE-MKGLYQFSRDELErQKHMYDQLEQDFLLCQQELTELKSS-----QSLCEEN 466
Cdd:PRK04863 584 LR-QQLEQLQARIQRLAARAPAWLAAQDaLARLREQSGEEFE-DSQDVTEYMQQLLERERELTVERDElaarkQALDEEI 661
|
410 420
....*....|....*....|.
gi 1907172349 467 GNCSNKCDALLARLTELQDKF 487
Cdd:PRK04863 662 ERLSQPGGSEDPRLNALAERF 682
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
105-974 |
9.26e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.05 E-value: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 105 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEvftKQIQQLQGELQHLREEISLLE---HEKE 181
Cdd:TIGR02169 188 RLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALE---RQKEAIERQLASLEEELEKLTeeiSELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 182 SELKEMEQELHLAQAEIQNLRQAAADSATEH----ESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMElktse 257
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKIKDLGEEEQLRVKEKigelEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE----- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 258 psnlsisdfsGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESD-RTRRATERWLESHLLRSTMSSESQTSELD 336
Cdd:TIGR02169 340 ----------ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEfAETRDELKDYREKLEKLKREINELKRELD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 337 FPEPDpvMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELKCAQNEVLRFQTShstqnsgihl 416
Cdd:TIGR02169 410 RLQEE--LQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE---------- 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 417 qlqemkglYQFSRDELERQKHMYDQLEQDFLLCQQELTELKSSQSLCEENGNcsnKCDALLARLTELQDKFKASQEEIGH 496
Cdd:TIGR02169 478 --------YDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ---GVHGTVAQLGSVGERYATAIEVAAG 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 497 LQMEQCELLEDQRRLQEEQGQLQEELHRLTF-PQPKCGILQKSQELLSK------LQDLCEMQLLYQNMQEQQRKLTqnq 569
Cdd:TIGR02169 547 NRLNNVVVEDDAVAKEAIELLKRRKAGRATFlPLNKMRDERRDLSILSEdgvigfAVDLVEFDPKYEPAFKYVFGDT--- 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 570 ecVLKEQLEAHKHLRG-FKESHFQEVLANPQDA--------RGPKSSSCENKFKVLM--DQLQALQVLYDTSQKQQEVLQ 638
Cdd:TIGR02169 624 --LVVEDIEAARRLMGkYRMVTLEGELFEKSGAmtggsrapRGGILFSRSEPAELQRlrERLEGLKRELSSLQSELRRIE 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 639 REHGRLMEERKRLQAELQLCMEEMQVLQTQSPMIKRSFEycgkNSGSRAPSTENFHRSYESSIDENEGYqksyvssqpst 718
Cdd:TIGR02169 702 NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE----ELEEDLSSLEQEIENVKSELKELEAR----------- 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 719 etfLKSYDSSTSANEAFEKSYCSSSTSVSYKKSYGSVSSGETLHRSYaSSSTDEDPAEPEDLEHFEETVAKVLTKLQAVK 798
Cdd:TIGR02169 767 ---IEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRI-EARLREIEQKLNRLTLEKEYLEKEIQELQEQR 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 799 ALYQVSQEEhcqLQQRMHRLLAKQKELTEELQCCEKELRECMESLGKPlppqsdKCEIKELQTKLRELQLQYQASMDEQG 878
Cdd:TIGR02169 843 IDLKEQIKS---IEKEIENLNGKKEELEEELEELEAALRDLESRLGDL------KKERDELEAQLRELERKIEELEAQIE 913
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 879 RLLAVQEQLEGQLQCCQEELRQLKENRPSISSEARGKNVNKNMNKNangVRNKKLSMACSEDLENGFENEknlevmlyYK 958
Cdd:TIGR02169 914 KKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAE---LQRVEEEIRALEPVNMLAIQE--------YE 982
|
890 900
....*....|....*....|...
gi 1907172349 959 ASQRRLDE-------LMKEEKEI 974
Cdd:TIGR02169 983 EVLKRLDElkekrakLEEERKAI 1005
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
108-314 |
9.44e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.04 E-value: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 108 ELRAQvlqLVAELEETRELAGQHEDDSLElQGLLEderlASAQQAEVfTKQIQQLQGELQHLREEISLLEHEKEselkem 187
Cdd:PRK10929 83 ELRQQ---LNNERDEPRSVPPNMSTDALE-QEILQ----VSSQLLEK-SRQAQQEQDRAREISDSLSQLPQQQT------ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 188 eqELHLAQAEIQNLRQAAADSATEH-ESDIASLQDDLCRLQNDLD--DMERIRGDYEMEIASLRAEMelktsepsnlsis 264
Cdd:PRK10929 148 --EARRQLNEIERRLQTLGTPNTPLaQAQLTALQAESAALKALVDelELAQLSANNRQELARLRSEL------------- 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907172349 265 dfsgiqdelhhLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATE 314
Cdd:PRK10929 213 -----------AKKRSQQLDAYLQALRNQLNSQRQREAERALESTELLAE 251
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
99-319 |
9.75e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 9.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 99 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFT------KQIQQLQGELQHLREE 172
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLelldriEELQELLREAEELEEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172349 173 ISLLEHEKESElkemeqelhlaqaeiQNLRQAAADSATEHESdIASLQDDLCRLQNDLDDMERirgdyemEIASLRAEME 252
Cdd:COG4717 363 LQLEELEQEIA---------------ALLAEAGVEDEEELRA-ALEQAEEYQELKEELEELEE-------QLEELLGELE 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907172349 253 lktsepSNLSISDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATERWLES 319
Cdd:COG4717 420 ------ELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEE 480
|
|
| |
