|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
106-426 |
2.71e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 106 LEELRAQV--LQLVAEL-EETRELAGQHEDDSLELQGL----LEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEH 178
Cdd:TIGR02168 195 LNELERQLksLERQAEKaERYKELKAELRELELALLVLrleeLREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 179 EKEselkEMEQELHLAQAEIQNLRQAAAD---SATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKT 255
Cdd:TIGR02168 275 EVS----ELEEEIEELQKELYALANEISRleqQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 256 SEPSNLSiSDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRraterwLESHLLRSTMSSESQTSEL 335
Cdd:TIGR02168 351 EELESLE-AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER------LEARLERLEDRRERLQQEI 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 336 dfpepdpvmQLLRQQLlgAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELKCAQNEVLRFQTSHSTQNSGIH 415
Cdd:TIGR02168 424 ---------EELLKKL--EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
330
....*....|.
gi 1907172360 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 |
3.29e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 99 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDerlaSAQQAEVFTKQIQQLQGELQHLREEIslleH 178
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ----LKEELKALREALDELRAELTLLNEEA----A 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 179 EKESELKEMEQELHLAQAEIQNLRQAAAD---SATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKT 255
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEElseDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907172360 256 SEPSNLSiSDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESD 307
Cdd:TIGR02168 901 EELRELE-SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
103-436 |
2.66e-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: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 103 ETELEELRAQV------LQLVAELEETRELAGQHEDDSLELQ-GLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISL 175
Cdd:COG1196 199 ERQLEPLERQAekaeryRELKEELKELEAELLLLKLRELEAElEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 176 LEHEKEsELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKt 255
Cdd:COG1196 279 LELELE-EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 256 sepsnlsisdfsgiQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTR-RATERWLESHLLRSTMSSESQTSE 334
Cdd:COG1196 357 --------------EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAElAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 335 LdfpepdpvmQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELKCAQNEVLRFQTSHSTQNSGI 414
Cdd:COG1196 423 L---------EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
330 340
....*....|....*....|..
gi 1907172360 415 HLQLQEMKGLYQFSRDELERQK 436
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALL 515
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
102-393 |
2.82e-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: 63.54 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 102 TETELEELRAQVLQLVAELEETR----ELAGQHEDDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELQHLREEISLLE 177
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEkalaELRKELEELEEELEQLRKELEELSRQISAL-RKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 178 HekesELKEMEQELHLAQAEIQNLRQAAAdsatEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSE 257
Cdd:TIGR02168 754 K----ELTELEAEIEELEERLEEAEEELA----EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 258 PSNLsisdfsgiQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATErwLESHLLRSTMSSESqtseldf 337
Cdd:TIGR02168 826 LESL--------ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE--LEALLNERASLEEA------- 888
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907172360 338 pepdpvMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQREL 393
Cdd:TIGR02168 889 ------LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
99-335 |
2.87e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 99 LSLTETELEELRAQVLQLVAELEET----RELAGQHEDDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELQHLREEIS 174
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELeaelEELRLELEELELELEEAQAEEYELLAELARL-EQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 175 llehEKESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDdlcrLQNDLDDMERIRGDYEMEIASLRAEMELK 254
Cdd:COG1196 320 ----ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE----AEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 255 TSEPSNLSISDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATERWLESHLLRSTMSSESQTSE 334
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
.
gi 1907172360 335 L 335
Cdd:COG1196 472 A 472
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
102-386 |
4.58e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.16 E-value: 4.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 102 TETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLED-----ERLASAQQAEVfTKQIQQLQGELQHLREEISll 176
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElnkkiKDLGEEEQLRV-KEKIGELEAEIASLERSIA-- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 177 ehEKESELKEMEQELHLAQAEIQNLRQAAADSATEHES---DIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEmel 253
Cdd:TIGR02169 312 --EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEerkRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE--- 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 254 ktsepsnlsisdFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTrRATERWLESHLLRSTMSSESQTS 333
Cdd:TIGR02169 387 ------------LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA-GIEAKINELEEEKEDKALEIKKQ 453
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1907172360 334 ELDFPEPDPVMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQ 386
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
99-356 |
5.80e-10 |
|
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: 5.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 99 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQG---LLEDERLASAQQAEVFTKQIQQLQGELQHLREEISL 175
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQdiaRLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 176 LEHEK---ESELKEMEQELHLAQAEIQNL---RQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRA 249
Cdd:COG1196 342 LEEELeeaEEELEEAEAELAEAEEALLEAeaeLAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 250 EMELKTSEPSNLSISdfsgIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATERW-LESHLLRSTMSS 328
Cdd:COG1196 422 ELEELEEALAELEEE----EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEeLAEAAARLLLLL 497
|
250 260
....*....|....*....|....*...
gi 1907172360 329 ESQTSELDFPEPDPVMQLLRQQLLGAEE 356
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
99-392 |
9.23e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.01 E-value: 9.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 99 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERlasaqqaevftkqIQQLQGELQHLREEISLLE- 177
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR-------------IPEIQAELSKLEEEVSRIEa 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 178 --HEKESELKEMEQELHLAQAEIQNLRQAAADSatehESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKT 255
Cdd:TIGR02169 813 rlREIEQKLNRLTLEKEYLEKEIQELQEQRIDL----KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 256 SEPSNLsisdfsgiQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDrtrraterwlESHLLRSTMSSESQtsel 335
Cdd:TIGR02169 889 KERDEL--------EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE----------LSEIEDPKGEDEEI---- 946
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907172360 336 dfPEPDPVMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRE 392
Cdd:TIGR02169 947 --PEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
99-315 |
1.68e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 99 LSLTETELEELRAQVLQLvaelEETRELAGQHEDDSLELQGLledERLASAQQAEVFTKQIQQLQGELQHLREEISLLEH 178
Cdd:COG4913 237 LERAHEALEDAREQIELL----EPIRELAERYAAARERLAEL---EYLRAALRLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 179 EK---ESELKEmeqelhlAQAEIQNLRQAAADSATEhesDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLraemelkt 255
Cdd:COG4913 310 ELerlEARLDA-------LREELDELEAQIRGNGGD---RLEQLEREIERLERELEERERRRARLEALLAAL-------- 371
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 256 SEPSNLSISDFSGIQDELHHLRERynlLNEEYQALRESNSSLTGQLAELESDRTRRATER 315
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
179-457 |
2.23e-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: 57.37 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 179 EKESELKEMEQELHLAQAEIQNLRQAAADSATEHEsdiaSLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEP 258
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELE----ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 259 SNLSI-------------SDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESdrtrRATERWLESHLLRST 325
Cdd:TIGR02168 750 AQLSKelteleaeieeleERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA----ELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 326 MSSESQTSELDFPEPDPVMQLLRQ---QLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKR-------LQRELKC 395
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEElseDIESLAAEIEELEELIEELESELEALLNERASLEEALALlrseleeLSEELRE 905
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907172360 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 |
3.49e-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: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 146 LASAQQAEVFTKQIQQLQGELQHLREEISLLEHEKES---ELKEMEQELHLAQAEIQNLRQAAADSatehESDIASLQDD 222
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAllkQLAALERRIAALARRIRALEQELAAL----EAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 223 LCRLQNDLDDM-----ERIRGDYEMEIASlrAEMELKTSEPSNLSISDFSGIQDELHHLRERYNLLNEEYQALRESNSSL 297
Cdd:COG4942 92 IAELRAELEAQkeelaELLRALYRLGRQP--PLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 298 TGQLAELESDRTRRATERwlesHLLRSTMSSESQTseldfpepdpvMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQH 377
Cdd:COG4942 170 EAERAELEALLAELEEER----AALEALKAERQKL-----------LARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
....*...
gi 1907172360 378 HRRTSEEE 385
Cdd:COG4942 235 EAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
106-318 |
5.34e-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: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 106 LEELRAQVLQLVAELEETRELAGQHEDdsleLQGLLEDERLASAQQAEVFTKQI--QQLQGELQHLREEISLLEhEKESE 183
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEA----ELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLD-ASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 184 LKEMEQELHLAQAEIQNLRQ---AAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEmeiaSLRAEMELKTSEPSN 260
Cdd:COG4913 687 LAALEEQLEELEAELEELEEeldELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL----RALLEERFAAALGDA 762
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907172360 261 LSISDFSGIQDELHHLRERYNLLNEEYQALR------------------ESNSSLTGQLAELESDRTRRATERWLE 318
Cdd:COG4913 763 VERELRENLEERIDALRARLNRAEEELERAMrafnrewpaetadldadlESLPEYLALLDRLEEDGLPEYEERFKE 838
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
96-249 |
6.84e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 6.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 96 HRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDdslELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISL 175
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALRE---ELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907172360 176 LEHEkeseLKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRA 249
Cdd:COG4913 364 LEAL----LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
97-339 |
7.56e-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: 55.83 E-value: 7.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 97 RGLSLTETELEELRAQVLQLVAELEE--TRELAGQHEDDSLELQGLLEDERLASAQ-QAEVFTKQIQQLQGELQHLREEI 173
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEElqKELYALANEISRLEQQKQILRERLANLErQLEELEAQLEELESKLDELAEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 174 SLLEHEKES---ELKEMEQELHLAQAEIQNLRQAAADSATEHE---SDIASLQDDLCRLQNDLDDMERIRGDYEMEIASL 247
Cdd:TIGR02168 340 AELEEKLEElkeELESLEAELEELEAELEELESRLEELEEQLEtlrSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 248 RAEMElktSEPSNLSISDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDrtRRATERWLESHLLRSTMS 327
Cdd:TIGR02168 420 QQEIE---ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA--LDAAERELAQLQARLDSL 494
|
250
....*....|..
gi 1907172360 328 SESQTSELDFPE 339
Cdd:TIGR02168 495 ERLQENLEGFSE 506
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
103-290 |
2.19e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 103 ETELEELRAQVLQLVAELEETRElagQHEDDSLELQGLLEDERLASAQQAEVFTK-QIQQLQGELQHLREEISLLEHE-- 179
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQ---KNGLVDLSEEAKLLLQQLSELESQLAEARaELAEAEARLAALRAQLGSGPDAlp 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 180 ---KESELKEMEQELHLAQAEIQNLRQaaadSATEHESDIASLQDDLCRLQNDLDD-MERIRGDYEMEIASLRAEMELKT 255
Cdd:COG3206 258 ellQSPVIQQLRAQLAELEAELAELSA----RYTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQ 333
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907172360 256 SEPSNLS--ISDFSGIQDELHHLRERYNLLNEEYQAL 290
Cdd:COG3206 334 AQLAQLEarLAELPELEAELRRLEREVEVARELYESL 370
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
103-244 |
2.99e-07 |
|
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: 51.85 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 103 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDerlASAQQAEVFT-KQIQQLQGELQHLREEISLLEheke 181
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK---YEEQLGNVRNnKEYEALQKEIESLKRRISDLE---- 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907172360 182 SELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEI 244
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
150-318 |
1.92e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 150 QQAEVFTKQIQQLQGELQHLREEISllehEKESELKEMEQELHLAQAEIQNLRQAAADSATEHEsdIASLQDDLCRLQND 229
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELE----ELEAELEELREELEKLEKLLQLLPLYQELEALEAE--LAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 230 LDDMERIRGDYEM---EIASLRAEMELKTSEPSNLSISDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELES 306
Cdd:COG4717 155 LEELRELEEELEEleaELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
170
....*....|..
gi 1907172360 307 DRTRRATERWLE 318
Cdd:COG4717 235 ELEAAALEERLK 246
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
161-510 |
2.26e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 161 QLQGELQHLREEISLLEHEKESELKEmeqelhlaQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDY 240
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSE--------LRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 241 EMEIASLRAEMELKTSEPSNLsISDFSGIQDELHHLRERYNLL------------NEEYQALRESNSSLTGQLAELESDR 308
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKEL-EARIEELEEDLHKLEEALNDLearlshsripeiQAELSKLEEEVSRIEARLREIEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 309 TRRaterwlesHLLRSTMSSESQTSELDFPEPDPVMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKR 388
Cdd:TIGR02169 822 NRL--------TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 389 LQRELKCAQNEVLRFQTSHSTQNSGIhLQLQEMKGLYQFSRDELERQKHM----------YDQLEQDFLLCQQELTELKS 458
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIEKKRKRL-SELKAKLEALEEELSEIEDPKGEdeeipeeelsLEDVQAELQRVEEEIRALEP 972
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1907172360 459 SQSLCEEngncsnKCDALLARLTELQDKFKASQEEIGHLQmEQCELLEDQRR 510
Cdd:TIGR02169 973 VNMLAIQ------EYEEVLKRLDELKEKRAKLEEERKAIL-ERIEEYEKKKR 1017
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
107-498 |
3.03e-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: 50.50 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 107 EELRAQVLQLVAELEETRELAgqheddslelQGLLEDerlaSAQQAEVFTKQIQQLQGELQHLReeiSLLEHEKESELKE 186
Cdd:pfam15921 141 EDLRNQLQNTVHELEAAKCLK----------EDMLED----SNTQIEQLRKMMLSHEGVLQEIR---SILVDFEEASGKK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 187 MEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLD--------DMERIRGDYEMEIASLRAEMELKT--- 255
Cdd:pfam15921 204 IYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEalksesqnKIELLLQQHQDRIEQLISEHEVEItgl 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 256 SEPSNLSISDFSGIQDELHHLRERynllneeyqaLRESNSSLTGQLAELESDRTRraterwleshlLRSTMSSESQTSEL 335
Cdd:pfam15921 284 TEKASSARSQANSIQSQLEIIQEQ----------ARNQNSMYMRQLSDLESTVSQ-----------LRSELREAKRMYED 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 336 DFPEPDPVMQLLRQQLLGAEEQMQDMQDKCKNLYCELEEL--QHHRRTSE-----EEQKR--------------LQRELK 394
Cdd:pfam15921 343 KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLlaDLHKREKElslekEQNKRlwdrdtgnsitidhLRRELD 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 395 CAQNEVLRFQTSHSTQNSGIHLQLQEMKGLYQFSRDELERQKHMYDQLEQDFLLCQQELTELKSSQSLCEengNCSNKCD 474
Cdd:pfam15921 423 DRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLE---SSERTVS 499
|
410 420
....*....|....*....|....
gi 1907172360 475 ALLARLTELQDKFKASQEEIGHLQ 498
Cdd:pfam15921 500 DLTASLQEKERAIEATNAEITKLR 523
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
97-268 |
5.53e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 97 RGLSLTETELEELRAQVLQLVAELEETREL----------AGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGEL 166
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEElaellralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 167 QHLREEISLLEHEKESELKEMEQELHLAQAEIQNLRQAAAdsatEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIAS 246
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKA----ERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
170 180
....*....|....*....|..
gi 1907172360 247 LRAEMELKTSEPSNLSISDFSG 268
Cdd:COG4942 232 LEAEAAAAAERTPAAGFAALKG 253
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
102-315 |
1.08e-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: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 102 TETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELQHLREEISLLEHEKE 181
Cdd:COG4913 666 AEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRL-EKELEQAEEELDELQDRLEAAEDLAR 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 182 SELKEmEQELHLAQAEIQNLRQAAADSAtehESDIASLQDDLCRLQNDLDD-MERIRGDYEMEIASLRAEMElktsepsn 260
Cdd:COG4913 745 LELRA-LLEERFAAALGDAVERELRENL---EERIDALRARLNRAEEELERaMRAFNREWPAETADLDADLE-------- 812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907172360 261 lSISDFSGI-----QDELHHLRERY-NLLNEeyqalrESNSSLTGQLAELESDRtRRATER 315
Cdd:COG4913 813 -SLPEYLALldrleEDGLPEYEERFkELLNE------NSIEFVADLLSKLRRAI-REIKER 865
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
104-292 |
1.24e-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: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 104 TELEELRAQVLQLVAELEETRELAGQHEDDSLE-LQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEHEK-- 180
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLELLEaELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRle 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 181 --ESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEp 258
Cdd:COG4913 342 qlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE- 420
|
170 180 190
....*....|....*....|....*....|....
gi 1907172360 259 snlsisdFSGIQDELHHLRERYNLLNEEYQALRE 292
Cdd:COG4913 421 -------LRELEAEIASLERRKSNIPARLLALRD 447
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
141-321 |
1.31e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 141 LEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLehEKESELKEMEQELHLAQAEIQNLRQAAADsATEHESDIASLQ 220
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREAL--QRLAEYSWDEIDVASAEREIAELEAELER-LDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 221 DDLCRLQNDLDDMERIRGDYEMEIASLRAEMElktsepsnlsisdfsGIQDELHHLRERYNLLNEEYQAlrESNSSLTGQ 300
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELE---------------QAEEELDELQDRLEAAEDLARL--ELRALLEER 754
|
170 180
....*....|....*....|.
gi 1907172360 301 LAELESDRTRRATERWLESHL 321
Cdd:COG4913 755 FAAALGDAVERELRENLEERI 775
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
105-500 |
1.37e-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: 48.20 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 105 ELEELRAQVLQLVAELEETRELAGQHeDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLrEEISLLEHEKESEL 184
Cdd:pfam05557 22 ELEHKRARIELEKKASALKRQLDRES-DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYL-EALNKKLNEKESQL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 185 KEMEQELHLAQAEIQNLRQAAADSA---TEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRA------------ 249
Cdd:pfam05557 100 ADAREVISCLKNELSELRRQIQRAElelQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqrikelefei 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 250 ------EMELKTSEPSNLSISDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATERWLESHLLR 323
Cdd:pfam05557 180 qsqeqdSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 324 STMSSES--QTSELDFPEPDP----VMQLLR-------------QQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEE 384
Cdd:pfam05557 260 ELQSWVKlaQDTGLNLRSPEDlsrrIEQLQQreivlkeenssltSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 385 EQKRLQRELKCAQNE-------VLRFQTSHSTQNSGIHLQ---------LQEMKGLYQFSRDELERQKHMYDQLEQDFLL 448
Cdd:pfam05557 340 LVRRLQRRVLLLTKErdgyraiLESYDKELTMSNYSPQLLerieeaedmTQKMQAHNEEMEAQLSVAEEELGGYKQQAQT 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1907172360 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 |
4.40e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 102 TETELEELRAQVLQLVAELEETRelagQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEHEKE 181
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALK----KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 182 SELKEMEQELHLAQAEIQNLR----------QAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEM 251
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPlalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907172360 252 ELKTSEPSNLSiSDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATE 314
Cdd:COG4942 181 AELEEERAALE-ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
99-308 |
8.23e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 99 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQiQQLQGELQHLREEISLLEH 178
Cdd:PRK02224 215 LAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERER-EELAEEVRDLRERLEELEE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 179 EK-----ESELKEMEQE-LHLAQAEIQNLRQAAAD-------SATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIA 245
Cdd:PRK02224 294 ERddllaEAGLDDADAEaVEARREELEDRDEELRDrleecrvAAQAHNEEAESLREDADDLEERAEELREEAAELESELE 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 246 SLRAEMELKTSEPSNLsisdfsgiQDELHHLRERYNL-------LNEEYQALRESNSSLTGQLAELESDR 308
Cdd:PRK02224 374 EAREAVEDRREEIEEL--------EEEIEELRERFGDapvdlgnAEDFLEELREERDELREREAELEATL 435
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
132-377 |
1.13e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 132 DDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELQHLREEISLleHEK-ESELKEMEQElhlAQAEIQNLRQAAADSAT 210
Cdd:PHA02562 157 EDLLDISVLSEMDKLNKDKIREL-NQQIQTLDMKIDHIQQQIKT--YNKnIEEQRKKNGE---NIARKQNKYDELVEEAK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 211 EHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSE----------PSNLS-ISD----FSGIQDELHH 275
Cdd:PHA02562 231 TIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVikmyekggvcPTCTQqISEgpdrITKIKDKLKE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 276 LRERYNLLNEEYQALRESNSSLTGQlaelesdrTRRATErwleshlLRSTMSSESQTseldfpepdpvMQLLRQQLLGAE 355
Cdd:PHA02562 311 LQHSLEKLDTAIDELEEIMDEFNEQ--------SKKLLE-------LKNKISTNKQS-----------LITLVDKAKKVK 364
|
250 260
....*....|....*....|..
gi 1907172360 356 EQMQDMQDKCKNLYCELEELQH 377
Cdd:PHA02562 365 AAIEELQAEFVDNAEELAKLQD 386
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
99-250 |
1.52e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 99 LSLTETELEELRAQVLQLVAELEETRELAGQH-------EDDSLELQGLLEDERLASA-QQAEVFTKQIQQLQGELQHLR 170
Cdd:COG3883 60 LEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsGGSVSYLDVLLGSESFSDFlDRLSALSKIADADADLLEELK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 171 EEISLLEhEKESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAE 250
Cdd:COG3883 140 ADKAELE-AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
138-445 |
1.70e-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: 44.73 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 138 QGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEHEKESELKEMEQELHLAQAEiqNLRQAAADSA----TEHE 213
Cdd:pfam17380 263 QTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAE--KARQAEMDRQaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 214 SDIASLQDDLCRLQND--LDDMERIRG-DYEMEIASLRaEMELKTSEPSNLSisdfSGIQDELHHLReRYNLLNEEYQal 290
Cdd:pfam17380 341 RMAMERERELERIRQEerKRELERIRQeEIAMEISRMR-ELERLQMERQQKN----ERVRQELEAAR-KVKILEEERQ-- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 291 resnSSLTGQLAELESDRTRRATERWLESHLLRSTMSSESQTSELDFPEPDPVMQLLRQQ---------LLGAEEQMQDM 361
Cdd:pfam17380 413 ----RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQeeerkrkklELEKEKRDRKR 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 362 QDKCKNLYCELEELQHHRRTSEEEQKR--LQRELKCAQNEVLRFQTSHSTQ---------NSGIHLQLQEMKGLYQFSR- 429
Cdd:pfam17380 489 AEEQRRKILEKELEERKQAMIEEERKRklLEKEMEERQKAIYEEERRREAEeerrkqqemEERRRIQEQMRKATEERSRl 568
|
330
....*....|....*.
gi 1907172360 430 DELERQKHMYDQLEQD 445
Cdd:pfam17380 569 EAMEREREMMRQIVES 584
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
100-241 |
2.20e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 100 SLTETELEELRAQVLQLVAELEETR----ELAGQHEDDSLELQGLLEDERLASAQQaevftkQIQQLQGELQHLRE---- 171
Cdd:COG3206 215 KLLLQQLSELESQLAEARAELAEAEarlaALRAQLGSGPDALPELLQSPVIQQLRA------QLAELEAELAELSArytp 288
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907172360 172 ---EISLLEHEKESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYE 241
Cdd:COG3206 289 nhpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
103-494 |
2.52e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 103 ETELEELRAQV---LQLVAELEETR--ELAGQHEddsLELQGLLEDERLASAQ-----------------QAEVFTKQIQ 160
Cdd:pfam15921 244 EDQLEALKSESqnkIELLLQQHQDRieQLISEHE---VEITGLTEKASSARSQansiqsqleiiqeqarnQNSMYMRQLS 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 161 QLQGELQHLREEISLLEHEKESELKEMEQELHLAQAEIQNLRQAAADSATEHesdiASLQDDLCRLQNDL---------- 230
Cdd:pfam15921 321 DLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQES----GNLDDQLQKLLADLhkrekelsle 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 231 ------------------DDMERIRGDYEMEIASLRAEMELKTSEPSNLSISDFSGIQDELHHLRERYNL---LNEEYQA 289
Cdd:pfam15921 397 keqnkrlwdrdtgnsitiDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLtaqLESTKEM 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 290 LRESNSSLTGQLAELE-SDRTRRATERWLESHlLRSTMSSESQTSELDfPEPDPVMQLLrQQLLGAEEQMQDMQDKCKNL 368
Cdd:pfam15921 477 LRKVVEELTAKKMTLEsSERTVSDLTASLQEK-ERAIEATNAEITKLR-SRVDLKLQEL-QHLKNEGDHLRNVQTECEAL 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 369 YCELEE------------------LQHHRRTS---EEEQKRLQRELKCAQNEVLRFQTSHSTQNSGIH--------LQLQ 419
Cdd:pfam15921 554 KLQMAEkdkvieilrqqienmtqlVGQHGRTAgamQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRelearvsdLELE 633
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907172360 420 EMKGLYQFSR--DELERQKHMYDQLEQDFLLCQQELTELKSSQSLCEEngNCSNKCDALLARLTELQDKFKASQEEI 494
Cdd:pfam15921 634 KVKLVNAGSErlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKR--NFRNKSEEMETTTNKLKMQLKSAQSEL 708
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
99-231 |
2.87e-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: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 99 LSLTETELEELRAQVLQLVAELEETRELAGQHED------DSLELQGLLEDERLASAQQAEV---FTK---QIQQLQGEL 166
Cdd:COG3206 221 LSELESQLAEARAELAEAEARLAALRAQLGSGPDalpellQSPVIQQLRAQLAELEAELAELsarYTPnhpDVIALRAQI 300
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907172360 167 QHLREEIsllEHEKESELKEMEQELHLAQAEIQNLRQAAADsATEHESDIASLQDDLCRLQNDLD 231
Cdd:COG3206 301 AALRAQL---QQEAQRILASLEAELEALQAREASLQAQLAQ-LEARLAELPELEAELRRLEREVE 361
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
97-247 |
3.83e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.03 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 97 RGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQgllederlASAQQAEVFTKQIQQLQGELQHLREEISLL 176
Cdd:PRK09039 46 REISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLR--------ASLSAAEAERSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907172360 177 EHEKESELKEMEQELHLAQAEIQNLRQaaadsatehesDIASLQDDLCRLQNDLDDMERIRGDYEMEIASL 247
Cdd:PRK09039 118 AGELAQELDSEKQVSARALAQVELLNQ-----------QIAALRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
102-210 |
7.97e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 102 TETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLlederlasAQQAEvftKQIQQLQGELQHLREEISLLEHEKE 181
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGL--------AAELE---EKQQELEAQLEQLQEKAAETSQERK 215
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1907172360 182 SELKEMEQE----LHLAQAEI-----QNLRQAA--ADSAT 210
Cdd:PRK11448 216 QKRKEITDQaakrLELSEEETrilidQQLRKAGweADSKT 255
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
181-398 |
8.23e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 8.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 181 ESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQddLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEPSN 260
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQ--LSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 261 LSISdfSGIQDelhhLRERYNLLNEEYQALRESNS-------SLTGQLAELESDRTRRATERWLESHLLRSTMSSESQTs 333
Cdd:COG3206 259 LLQS--PVIQQ----LRAQLAELEAELAELSARYTpnhpdviALRAQIAALRAQLQQEAQRILASLEAELEALQAREAS- 331
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907172360 334 eldfpepdpvmqlLRQQLLGAEEQMQDMQDKcknlyceleelqhhrrtsEEEQKRLQRELKCAQN 398
Cdd:COG3206 332 -------------LQAQLAQLEARLAELPEL------------------EAELRRLEREVEVARE 365
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
137-334 |
8.66e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 8.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 137 LQGLLEDERLASAQQAEVFTKQIQQLQGEL-------QHLREEISLLEHEKE-----SELKEMEQELHLAQAEIQNLRQ- 203
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELeeaeaalEEFRQKNGLVDLSEEaklllQQLSELESQLAEARAELAEAEAr 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 204 -----------AAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEPSNLSISDFSGIQDE 272
Cdd:COG3206 242 laalraqlgsgPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAE 321
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907172360 273 LHHLRERYNLLNEEYQALRESNSSLTGQLAELES-DRTRRATERWLESHLLRSTMSSESQTSE 334
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAELPELEAELRRlEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
102-311 |
1.02e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 102 TETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEvftkQIQQLQGELQHLREEISLLEHEKE 181
Cdd:COG1196 629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE----LEELAERLAEEELELEEALLAEEE 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 182 SELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERI--RGDYEMEIASLRAEMELKtsEPS 259
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPpdLEELERELERLEREIEAL--GPV 782
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907172360 260 NL-SIsdfsgiqDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRR 311
Cdd:COG1196 783 NLlAI-------EEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
99-206 |
1.14e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 99 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEH 178
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
90 100 110
....*....|....*....|....*....|
gi 1907172360 179 EKESELKEMEQ--ELHLAQAEIQNLRQAAA 206
Cdd:COG4717 221 ELEELEEELEQleNELEAAALEERLKEARL 250
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
270-494 |
1.22e-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: 41.98 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 270 QDELHHLRE-RYNLLNEEYQALRESNSSLTGQLAELE---SDRTRRATERWLESHLLRSTMSSES-QTSELDFPEPDPV- 343
Cdd:TIGR02169 214 QALLKEKREyEGYELLKEKEALERQKEAIERQLASLEeelEKLTEEISELEKRLEEIEQLLEELNkKIKDLGEEEQLRVk 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 344 ---------MQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELKCAQNEVLRFQTSHSTQNSgi 414
Cdd:TIGR02169 294 ekigeleaeIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA-- 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 415 hlQLQEMKGLYQFSRDELERQKHMYDQLEQDFLLCQQELTEL-KSSQSLCEENGNCSNKCDALLARLTELQDKFKASQEE 493
Cdd:TIGR02169 372 --ELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLqEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE 449
|
.
gi 1907172360 494 I 494
Cdd:TIGR02169 450 I 450
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
108-292 |
1.23e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 108 ELRAQVLQLVAELEETRELAGQHEDdslELQGLLEDerlaSAQQAEVFTKQIQQLQGELQHLREEISllehEKESELKEM 187
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIE---NLNGKKEE----LEEELEELEAALRDLESRLGDLKKERD----ELEAQLREL 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 188 EQELHLAQAEIQNLRQAAAD---SATEHESDIASLQDDLCRLQNDLDDmERIRGDYEMEIasLRAEMELKTSEPSN-LSI 263
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRLSElkaKLEALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAEL--QRVEEEIRALEPVNmLAI 978
|
170 180
....*....|....*....|....*....
gi 1907172360 264 SDFSGIQDELHHLRERYNLLNEEYQALRE 292
Cdd:TIGR02169 979 QEYEEVLKRLDELKEKRAKLEEERKAILE 1007
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
189-314 |
1.42e-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: 40.68 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 189 QELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEME-LKTSEPSNLSISDFS 267
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkYEEQLGNVRNNKEYE 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1907172360 268 GIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATE 314
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE 139
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
203-402 |
2.03e-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: 40.90 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 203 QAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEPSNLsisdfsgiQDELHHLRERYNL 282
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL--------EQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 283 LNEEYQALRESNSSLTGQLAELESDRTRRATERWLEsHLLRSTMSSESQTSELDFPEpdpVMQLLRQQLLGAEEQMQDMQ 362
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLA-LLLSPEDFLDAVRRLQYLKY---LAPARREQAEELRADLAELA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907172360 363 DKCKNLYCELEELQHHRRTSEEEQKRLQRELKcAQNEVLR 402
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKA-ERQKLLA 202
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
153-484 |
2.07e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 153 EVFTKQIQQLQGELQHL-------REEI--SLLEHEKESE----LKEMEQELhlaQAEIQNLRQAaadsatehESDIASL 219
Cdd:PRK01156 127 DVFLNSIFVGQGEMDSLisgdpaqRKKIldEILEINSLERnydkLKDVIDML---RAEISNIDYL--------EEKLKSS 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 220 QDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEPSNLsisdfsgiQDELHHLRERYNLLNEEYQALRESNSSLtg 299
Cdd:PRK01156 196 NLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNL--------KSALNELSSLEDMKNRYESEIKTAESDL-- 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 300 QLAELESDRTRRATERWLEshlLRSTMSSESQTSELDFPEPDPVMQLLRQQLLGAEEQMQDMQDKCKnlycELEELQHHR 379
Cdd:PRK01156 266 SMELEKNNYYKELEERHMK---IINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIK----KLSVLQKDY 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 380 RTSEEEQKRLQrELKcaqNEVLRFQTSHSTQNSGIhlqlQEMKGLYQFSRDELERQKHMYDQLEQDFLLCQQELTELKS- 458
Cdd:PRK01156 339 NDYIKKKSRYD-DLN---NQILELEGYEMDYNSYL----KSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKe 410
|
330 340 350
....*....|....*....|....*....|...
gi 1907172360 459 ----SQSLCEENGNCSN---KCDALLARLTELQ 484
Cdd:PRK01156 411 lneiNVKLQDISSKVSSlnqRIRALRENLDELS 443
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
103-192 |
2.32e-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: 39.14 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 103 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERlasaqqaEVFTKQIQQLQGELQHL-REEISLLEhEKE 181
Cdd:pfam09744 49 NVELEELREDNEQLETQYEREKALRKRAEEELEEIEDQWEQET-------KDLLSQVESLEEENRRLeADHVSRLE-EKE 120
|
90
....*....|.
gi 1907172360 182 SELKEMEQELH 192
Cdd:pfam09744 121 AELKKEYSKLH 131
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
96-310 |
2.43e-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: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 96 HRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISL 175
Cdd:COG1196 598 GAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEA 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 176 LEHEKESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKT 255
Cdd:COG1196 678 EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELP 757
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907172360 256 SEPSnlsisdfsgiqdeLHHLRERYNLLN--------------EEYQALRESNSSLTGQLAELESDRTR 310
Cdd:COG1196 758 EPPD-------------LEELERELERLEreiealgpvnllaiEEYEELEERYDFLSEQREDLEEARET 813
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
106-283 |
2.85e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 106 LEELRAQVLQLVAELE----ETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTK----------QIQQLQGEL----- 166
Cdd:PHA02562 204 IEEQRKKNGENIARKQnkydELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKlntaaakiksKIEQFQKVIkmyek 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 167 --------QHLREEISLLEhEKESELKEMEQELHLAQAEIQNLRQ------AAADSATEHESDIASLQDDLCRLQNDLDD 232
Cdd:PHA02562 284 ggvcptctQQISEGPDRIT-KIKDKLKELQHSLEKLDTAIDELEEimdefnEQSKKLLELKNKISTNKQSLITLVDKAKK 362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907172360 233 MERI-------RGDYEMEIASLRAEMELKtsepsnlsISDFSGIQDELHHLRERYNLL 283
Cdd:PHA02562 363 VKAAieelqaeFVDNAEELAKLQDELDKI--------VKTKSELVKEKYHRGIVTDLL 412
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
102-308 |
4.06e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 102 TETELEELRAQVLQLVAELEETREL------AGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISL 175
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESELiklkelAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 176 LEhEKESELKEMEQELHLAQAEIQNL----RQAAADSATEHESDIASLQ---DDLCRLQNDLDDMERIrgdyEMEIASLR 248
Cdd:PRK03918 551 LE-ELKKKLAELEKKLDELEEELAELlkelEELGFESVEELEERLKELEpfyNEYLELKDAEKELERE----EKELKKLE 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907172360 249 AEMElKTSEPSNLSISDFSGIQDELHHLRERYNL-----LNEEYQALRESNSSLTGQLAELESDR 308
Cdd:PRK03918 626 EELD-KAFEELAETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRR 689
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
114-394 |
4.16e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 114 LQLvAELEETRELAGqheDDSLELQGLLEDERLASAQ-QAEVFTKQIQQLQGELQHLREEISllehEKESELKEMEQELH 192
Cdd:PRK02224 159 LQL-GKLEEYRERAS---DARLGVERVLSDQRGSLDQlKAQIEEKEEKDLHERLNGLESELA----ELDEEIERYEEQRE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 193 LAQAEiqnlRQAAADSATEHE---SDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSE------PSNLSI 263
Cdd:PRK02224 231 QARET----RDEADEVLEEHEerrEELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEErddllaEAGLDD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 264 SDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQlAELESDRTRRATERWLESHLLRSTMSSESQTSELDFPEPdpv 343
Cdd:PRK02224 307 ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEE-AESLREDADDLEERAEELREEAAELESELEEAREAVEDR--- 382
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907172360 344 mqllRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELK 394
Cdd:PRK02224 383 ----REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
87-503 |
4.18e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.48 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 87 SLGSLSMGKHRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLL-EDERLASAQqaevftKQIQQLQGE 165
Cdd:pfam05483 360 SLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILaEDEKLLDEK------KQFEKIAEE 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 166 LQHLREEISLLEHEKESELKEMEQELHLAQAEIQNLRQAAADSATEHE------------SDIASLQDDlcRLQNDLDDM 233
Cdd:pfam05483 434 LKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEkeklknieltahCDKLLLENK--ELTQEASDM 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 234 ERIRGDYEMEIASLRAEMELKTSEPSNLSISDFSgIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRAT 313
Cdd:pfam05483 512 TLELKKHQEDIINCKKQEERMLKQIENLEEKEMN-LRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMK 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 314 ERWLESHLLRSTMSSESQTSEldfpEPDPVMQLLRQQLLGAEEQMQDMQDKCKNLYCELEEL-QHHRRTSEEEQKRLQRE 392
Cdd:pfam05483 591 ILENKCNNLKKQIENKNKNIE----ELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAkQKFEEIIDNYQKEIEDK 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 393 LKCAQNEVLRFQTSHSTQNSGIHLQlQEMKGLYQFSRDE----LERQKHMYDQL--EQDFLLCQQELTELKSSQSLCEEN 466
Cdd:pfam05483 667 KISEEKLLEEVEKAKAIADEAVKLQ-KEIDKRCQHKIAEmvalMEKHKHQYDKIieERDSELGLYKNKEQEQSSAKAALE 745
|
410 420 430
....*....|....*....|....*....|....*..
gi 1907172360 467 GNCSNkcdaLLARLTELQDKFKASQEEIGHLQMEQCE 503
Cdd:pfam05483 746 IELSN----IKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
344-593 |
5.23e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 344 MQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELKCAQNEVLRFQTSHSTQNSGIHLQLQEMKG 423
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 424 LyqfsRDELERQKHMYDQLEQDFLLCQQELTELKSSQSLCEEngncsnKCDALLARLTELQDKFKASQEEIGHLQMEQCE 503
Cdd:COG1196 314 L----EERLEELEEELAELEEELEELEEELEELEEELEEAEE------ELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 504 LLEDQRRLQEEQGQlqeelhrltfpqpkcgILQKSQELLSKLQDLcemQLLYQNMQEQQRKLTQNQECVLKEQLEAHKHL 583
Cdd:COG1196 384 LAEELLEALRAAAE----------------LAAQLEELEEAEEAL---LERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
250
....*....|
gi 1907172360 584 RGFKESHFQE 593
Cdd:COG1196 445 EEAAEEEAEL 454
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
150-393 |
5.34e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 150 QQAEVFTKQIQQLQGELQHLREEISLLE----------HEKESELKEMEQELHLAQAEIQNLRQAAADSATEhesdIASL 219
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLEskiqnqeklnQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE----IKDL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 220 QDDLCRLQNDLDDMERIRGDYEMEIASLRAEMElktSEPSNLSIsdfsgIQDELHHLRERYNLLNEEYQALRESNSSLTG 299
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSIN---KIKQNLEQ-----KQKELKSKEKELKKLNEEKKELEEKVKDLTK 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 300 QLAELESdrtrraTERWLESHLLRSTMSSESQTSELDFPEPDPVMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHR 379
Cdd:TIGR04523 518 KISSLKE------KIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELI 591
|
250
....*....|....
gi 1907172360 380 RTSEEEQKRLQREL 393
Cdd:TIGR04523 592 DQKEKEKKDLIKEI 605
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
105-510 |
5.61e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.95 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 105 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQA------EVFTKQIQQLQGELQHLREEISLLEH 178
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdidnpGPLTRRMQRGEQTYAQLETSEEDVYH 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 179 EKESELKEMEQELHLAQAEIQNLrQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRgdyEMEIASLRAEMELKTSEP 258
Cdd:TIGR00618 550 QLTSERKQRASLKEQMQEIQQSF-SILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE---DMLACEQHALLRKLQPEQ 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 259 SNLSISdfsgiqdelHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATERWLESHLLRST-MSSESQTSELDF 337
Cdd:TIGR00618 626 DLQDVR---------LHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQkMQSEKEQLTYWK 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 338 PEPDPVMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELK---CAQNEVLRFQTSHSTQNSGI 414
Cdd:TIGR00618 697 EMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARtvlKARTEAHFNNNEEVTAALQT 776
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 415 HLQLQEMKGLYQFSRDELERQKHMYDQLEQDFllcQQELTELKSSQSL-CEENGNCSNKCDALLARLTELQDKFKASQEE 493
Cdd:TIGR00618 777 GAELSHLAAEIQFFNRLREEDTHLLKTLEAEI---GQEIPSDEDILNLqCETLVQEEEQFLSRLEEKSATLGEITHQLLK 853
|
410
....*....|....*..
gi 1907172360 494 IGHLQMEQCELLEDQRR 510
Cdd:TIGR00618 854 YEECSKQLAQLTQEQAK 870
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
108-487 |
6.47e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 108 ELRAQVLQLVAE---LEETRELAGQHEDDSLELQGLLE--DERLASAQQAEVFTKQIQQLQGELQhlreeisllehEKES 182
Cdd:PRK04863 294 ELYTSRRQLAAEqyrLVEMARELAELNEAESDLEQDYQaaSDHLNLVQTALRQQEKIERYQADLE-----------ELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 183 ELKEMEQELHLAQaEIQNLRQAAADSAtehESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELktSEPSNLS 262
Cdd:PRK04863 363 RLEEQNEVVEEAD-EQQEENEARAEAA---EEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQL--CGLPDLT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 263 ISDFSGIQDELH-HLRERYNLLNEEYQALRESNS-------------SLTGQLAELESDRTRRATERWLES--HLLRSTM 326
Cdd:PRK04863 437 ADNAEDWLEEFQaKEQEATEELLSLEQKLSVAQAahsqfeqayqlvrKIAGEVSRSEAWDVARELLRRLREqrHLAEQLQ 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 327 SSESQTSEL--DFPEPDPVMQLLRqQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELKcAQNEVLRFQ 404
Cdd:PRK04863 517 QLRMRLSELeqRLRQQQRAERLLA-EFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALR-QQLEQLQAR 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 405 TSHSTQNSGIHLQLQE-MKGLYQFSRDELErQKHMYDQLEQDFLLCQQELTELKSS-----QSLCEENGNCSNKCDALLA 478
Cdd:PRK04863 595 IQRLAARAPAWLAAQDaLARLREQSGEEFE-DSQDVTEYMQQLLERERELTVERDElaarkQALDEEIERLSQPGGSEDP 673
|
....*....
gi 1907172360 479 RLTELQDKF 487
Cdd:PRK04863 674 RLNALAERF 682
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
99-319 |
6.65e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 99 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFT------KQIQQLQGELQHLREE 172
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLelldriEELQELLREAEELEEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 173 ISLLEHEKESElkemeqelhlaqaeiQNLRQAAADSATEHESdIASLQDDLCRLQNDLDDMERirgdyemEIASLRAEME 252
Cdd:COG4717 363 LQLEELEQEIA---------------ALLAEAGVEDEEELRA-ALEQAEEYQELKEELEELEE-------QLEELLGELE 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907172360 253 lktsepSNLSISDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATERWLES 319
Cdd:COG4717 420 ------ELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEE 480
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
103-465 |
6.91e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.62 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 103 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQaevfTKQIQQLQGELQHLREEISLLEHEKE- 181
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN----NKKIKELEKQLNQLKSEISDLNNQKEq 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 182 -------SELKEMEQELHLAQAEIQNLRQaaadSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELK 254
Cdd:TIGR04523 307 dwnkelkSELKNQEKKLEEIQNQISQNNK----IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 255 TSEPSNL--SISDF-SGIQD----------ELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTrrATERWLEShL 321
Cdd:TIGR04523 383 KQEIKNLesQINDLeSKIQNqeklnqqkdeQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS--VKELIIKN-L 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 322 LRSTMSSESQTSELDFPepdpvMQLLRQQLlgaEEQMQDMQDKCKnlycELEELQHHRRTSEEEQKRL---QRELKCAQN 398
Cdd:TIGR04523 460 DNTRESLETQLKVLSRS-----INKIKQNL---EQKQKELKSKEK----ELKKLNEEKKELEEKVKDLtkkISSLKEKIE 527
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907172360 399 EVLRFQTSHSTQNSGIHLQLQEMKglYQFSRDELERQKHMYDQ-LEQdfllCQQELTELKSSQSLCEE 465
Cdd:TIGR04523 528 KLESEKKEKESKISDLEDELNKDD--FELKKENLEKEIDEKNKeIEE----LKQTQKSLKKKQEEKQE 589
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
71-254 |
8.65e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 71 EEEEEEVEEEQVEKGGSLGSLsmgkhrglsltETELEELRAQVLQLVAELEETRELAGQHEDDSLELQglleDERLASAQ 150
Cdd:COG1196 329 EEELEELEEELEELEEELEEA-----------EEELEEAEAELAEAEEALLEAEAELAEAEEELEELA----EELLEALR 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 151 QAEVFTKQIQQLQGELQHLREEISLLEHEKESELKEMEQELHLAQAEIQNLRQAAADSAtEHESDIASLQDDLCRLQNDL 230
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA-ELEEEEEALLELLAELLEEA 472
|
170 180
....*....|....*....|....
gi 1907172360 231 DDMERIRGDYEMEIASLRAEMELK 254
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLL 496
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
85-201 |
8.80e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 85 GGSLGSLSMGKHRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQG 164
Cdd:COG1196 656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1907172360 165 ELQHLREEISLLEHEKESE-------LKEMEQELHLAQAEIQNL 201
Cdd:COG1196 736 ELLEELLEEEELLEEEALEelpeppdLEELERELERLEREIEAL 779
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
104-218 |
9.41e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.29 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172360 104 TELEELRAQVLQLVAELEEtrelagqheddslelqgLLEDERLASAQQAEVFTKQIQQLQGELQHLRE----EISLLE-- 177
Cdd:COG0542 411 EELDELERRLEQLEIEKEA-----------------LKKEQDEASFERLAELRDELAELEEELEALKArweaEKELIEei 473
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907172360 178 HEKESELKEMEQELHLAQAEIQNLRQAAADSATEH-----ESDIAS 218
Cdd:COG0542 474 QELKEELEQRYGKIPELEKELAELEEELAELAPLLreevtEEDIAE 519
|
|
| |
