|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
106-449 |
2.63e-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: 70.47 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 106 LEELRAQV--LQLVAEL-EETRELAGQHEDDSLELQGL----LEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEH 178
Cdd:TIGR02168 195 LNELERQLksLERQAEKaERYKELKAELRELELALLVLrleeLREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 179 EKEselkEMEQELHLAQAEIQNLRQAAAD---SATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKT 255
Cdd:TIGR02168 275 EVS----ELEEEIEELQKELYALANEISRleqQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 256 SEPSNLSiSDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRraterwLESHLLRSTMSSESQTSEL 335
Cdd:TIGR02168 351 EELESLE-AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER------LEARLERLEDRRERLQQEI 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 336 dfpepdpvmQLLRQQLlgAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELKCAQNEVLRFQTSHSTQHEELK 415
Cdd:TIGR02168 424 ---------EELLKKL--EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
330 340 350
....*....|....*....|....*....|....
gi 1907172355 416 SrLCTLQQKYDASQDEHSELLKVQMQLETELQQL 449
Cdd:TIGR02168 493 S-LERLQENLEGFSEGVKALLKNQSGLSGILGVL 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
99-307 |
1.13e-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: 65.46 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 99 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDerlaSAQQAEVFTKQIQQLQGELQHLREEIslleH 178
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ----LKEELKALREALDELRAELTLLNEEA----A 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 179 EKESELKEMEQELHLAQAEIQNLRQAAAD---SATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKT 255
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEElseDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907172355 256 SEPSNLSiSDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESD 307
Cdd:TIGR02168 901 EELRELE-SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
103-450 |
1.38e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 103 ETELEELRAQV------LQLVAELEETRELAGQHEDDSLELQ-GLLEDERLASAQQAEVFTKQIQQLQGELQHLREEIsl 175
Cdd:COG1196 199 ERQLEPLERQAekaeryRELKEELKELEAELLLLKLRELEAElEELEAELEELEAELEELEAELAELEAELEELRLEL-- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 176 leHEKESELKEMEQELHLAQAEIQNLrqaaadsatehESDIASLQDDLCRLQNDLDDMERirgdyemEIASLRAEMELkt 255
Cdd:COG1196 277 --EELELELEEAQAEEYELLAELARL-----------EQDIARLEERRRELEERLEELEE-------ELAELEEELEE-- 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 256 sepsnlsisdfsgIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATErwlESHLLRSTMSSESQTSEl 335
Cdd:COG1196 335 -------------LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE---LEELAEELLEALRAAAE- 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 336 dfpepdpvmqlLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELKCAQNEVLRFQTSHSTQHEELK 415
Cdd:COG1196 398 -----------LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
330 340 350
....*....|....*....|....*....|....*
gi 1907172355 416 SRLCTLQQKYDASQDEHSELLKVQMQLETELQQLR 450
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
99-335 |
6.57e-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: 6.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 99 LSLTETELEELRAQVLQLVAELEET----RELAGQHEDDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELQHLREEIS 174
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELeaelEELRLELEELELELEEAQAEEYELLAELARL-EQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 175 llehEKESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDdlcrLQNDLDDMERIRGDYEMEIASLRAEMELK 254
Cdd:COG1196 320 ----ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE----AEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 255 TSEPSNLSISDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATERWLESHLLRSTMSSESQTSE 334
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
.
gi 1907172355 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 |
1.24e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 102 TETELEELRAQVLQLVAELEETR----ELAGQHEDDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELQHLREEISLLE 177
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEkalaELRKELEELEEELEQLRKELEELSRQISAL-RKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 178 HekesELKEMEQELHLAQAEIQNLRQAAAdsatEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSE 257
Cdd:TIGR02168 754 K----ELTELEAEIEELEERLEEAEEELA----EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 258 PSNLsisdfsgiQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATErwLESHLLRSTMSSESqtseldf 337
Cdd:TIGR02168 826 LESL--------ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE--LEALLNERASLEEA------- 888
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907172355 338 pepdpvMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQREL 393
Cdd:TIGR02168 889 ------LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
99-356 |
1.49e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 99 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQG---LLEDERLASAQQAEVFTKQIQQLQGELQHLREEISL 175
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQdiaRLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 176 LEHEK---ESELKEMEQELHLAQAEIQNL---RQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRA 249
Cdd:COG1196 342 LEEELeeaEEELEEAEAELAEAEEALLEAeaeLAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 250 EMELKTSEPSNLSISdfsgIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATERW-LESHLLRSTMSS 328
Cdd:COG1196 422 ELEELEEALAELEEE----EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEeLAEAAARLLLLL 497
|
250 260
....*....|....*....|....*...
gi 1907172355 329 ESQTSELDFPEPDPVMQLLRQQLLGAEE 356
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
99-616 |
2.89e-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: 60.84 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 99 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQ----------QAEVFTKQIQQLQGELQH 168
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQlelqiaslnnEIERLEARLERLEDRRER 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 169 LREEISLLE--------HEKESELKEMEQELHLAQAEIQNLRQA---AADSATEHESDIASLQDDLCRLQNDLDDMERIR 237
Cdd:TIGR02168 419 LQQEIEELLkkleeaelKELQAELEELEEELEELQEELERLEEAleeLREELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 238 GDYEMEIASLRAEM--------------ELKTSEPS--------------NLSISDFSGIQDELHHLRE----------- 278
Cdd:TIGR02168 499 ENLEGFSEGVKALLknqsglsgilgvlsELISVDEGyeaaieaalggrlqAVVVENLNAAKKAIAFLKQnelgrvtflpl 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 279 ---RYNLLNEEYQALRESNSSLTGQLAELES--DRTRRATERWL--------------ESHLLRSTMSSESQTSELDFP- 338
Cdd:TIGR02168 579 dsiKGTEIQGNDREILKNIEGFLGVAKDLVKfdPKLRKALSYLLggvlvvddldnaleLAKKLRPGYRIVTLDGDLVRPg 658
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 339 --------EPDPVMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELqhhrrtsEEEQKRLQRELKCAQNEVLRFQTSHSTQ 410
Cdd:TIGR02168 659 gvitggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAEL-------RKELEELEEELEQLRKELEELSRQISAL 731
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 411 HEELKSRLCTLQQKYDASQDEHSELLKVQMQLETELQQLRLLRCTPVESQSEKE-LMCRLQKLQAQHQcsvNEKEQLLEV 489
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEeLEAQIEQLKEELK---ALREALDEL 808
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 490 QHHLHD----------KLRCHESEVHRLRSMVDCLREKNEKNSGIHLQLQEMKGLYQFSRDELERQ-KHMYDQLEQDfll 558
Cdd:TIGR02168 809 RAELTLlneeaanlreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESElEALLNERASL--- 885
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907172355 559 cQQELTELKSS-QSLCEENGNCSNKCDALLARLTELQDKFKASQEEIGHLQMEQCELLE 616
Cdd:TIGR02168 886 -EEALALLRSElEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
99-392 |
4.45e-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: 4.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 99 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERlasaqqaevftkqIQQLQGELQHLREEISLLE- 177
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR-------------IPEIQAELSKLEEEVSRIEa 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 178 --HEKESELKEMEQELHLAQAEIQNLRQAAADSatehESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKT 255
Cdd:TIGR02169 813 rlREIEQKLNRLTLEKEYLEKEIQELQEQRIDL----KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 256 SEPSNLsisdfsgiQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDrtrraterwlESHLLRSTMSSESQtsel 335
Cdd:TIGR02169 889 KERDEL--------EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE----------LSEIEDPKGEDEEI---- 946
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907172355 336 dfPEPDPVMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRE 392
Cdd:TIGR02169 947 --PEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
161-488 |
1.30e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 161 QLQGELQHLREEISLLEHEKESELKEmeqelhlaQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDY 240
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSE--------LRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 241 EMEIASLRAEMELKTSEPSNLsISDFSGIQDELHHLRERYNLL------------NEEYQALRESNSSLTGQLAELESDR 308
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKEL-EARIEELEEDLHKLEEALNDLearlshsripeiQAELSKLEEEVSRIEARLREIEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 309 TRRaterwlesHLLRSTMSSESQTSELDFPEPDPVMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKR 388
Cdd:TIGR02169 822 NRL--------TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 389 LQRELKCAQNEvlrfQTSHSTQHEELKSRLCTLQQKYDASQDEHSELL-----------------KVQMQLETELQQLRL 451
Cdd:TIGR02169 894 LEAQLRELERK----IEELEAQIEKKRKRLSELKAKLEALEEELSEIEdpkgedeeipeeelsleDVQAELQRVEEEIRA 969
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1907172355 452 LRctPVES---QSEKELMCRLQKLQAQHQCSVNEKEQLLE 488
Cdd:TIGR02169 970 LE--PVNMlaiQEYEEVLKRLDELKEKRAKLEEERKAILE 1007
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
99-315 |
4.13e-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: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 99 LSLTETELEELRAQVLQLvaelEETRELAGQHEDDSLELQGLledERLASAQQAEVFTKQIQQLQGELQHLREEISLLEH 178
Cdd:COG4913 237 LERAHEALEDAREQIELL----EPIRELAERYAAARERLAEL---EYLRAALRLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 179 EK---ESELKEmeqelhlAQAEIQNLRQAAADSATEhesDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLraemelkt 255
Cdd:COG4913 310 ELerlEARLDA-------LREELDELEAQIRGNGGD---RLEQLEREIERLERELEERERRRARLEALLAAL-------- 371
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 256 SEPSNLSISDFSGIQDELHHLRERynlLNEEYQALRESNSSLTGQLAELESDRTRRATER 315
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
146-385 |
1.05e-07 |
|
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: 54.77 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 146 LASAQQAEVFTKQIQQLQGELQHLREEISLLEHEKES---ELKEMEQELHLAQAEIQNLRQAAADSatehESDIASLQDD 222
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAllkQLAALERRIAALARRIRALEQELAAL----EAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 223 LCRLQNDLDDM-----ERIRGDYEMEIASlrAEMELKTSEPSNLSISDFSGIQDELHHLRERYNLLNEEYQALRESNSSL 297
Cdd:COG4942 92 IAELRAELEAQkeelaELLRALYRLGRQP--PLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 298 TGQLAELESDRTRRATERwlesHLLRSTMSSESQTseldfpepdpvMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQH 377
Cdd:COG4942 170 EAERAELEALLAELEEER----AALEALKAERQKL-----------LARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
....*...
gi 1907172355 378 HRRTSEEE 385
Cdd:COG4942 235 EAAAAAER 242
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
105-417 |
1.17e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 105 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQaevfTKQIQQLQGELQHLREEISLLEHEKESEL 184
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL----ELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 185 KEMEQelhlAQAEIQNLRQAAADSATEHESDIASLQddlcRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEPSNLSIS 264
Cdd:COG1196 309 ERRRE----LEERLEELEEELAELEEELEELEEELE----ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 265 DFSGIQDELHHLRERYNLLNEEyQALRESNSSLTGQLAELESDRTRRATERwleshllrstmssesqtseldfpepdpvm 344
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQL-EELEEAEEALLERLERLEEELEELEEAL----------------------------- 430
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907172355 345 QLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELKCAQNEVLRFQTSHSTQHEELKSR 417
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
96-249 |
1.23e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 96 HRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDdslELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISL 175
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALRE---ELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907172355 176 LEHEkeseLKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRA 249
Cdd:COG4913 364 LEAL----LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
106-318 |
1.27e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 106 LEELRAQVLQLVAELEETRELAGQHEDdsleLQGLLEDERLASAQQAEVFTKQI--QQLQGELQHLREEISLLEhEKESE 183
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEA----ELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLD-ASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 184 LKEMEQELHLAQAEIQNLRQ---AAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEmeiaSLRAEMELKTSEPSN 260
Cdd:COG4913 687 LAALEEQLEELEAELEELEEeldELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL----RALLEERFAAALGDA 762
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907172355 261 LSISDFSGIQDELHHLRERYNLLNEEYQALR------------------ESNSSLTGQLAELESDRTRRATERWLE 318
Cdd:COG4913 763 VERELRENLEERIDALRARLNRAEEELERAMrafnrewpaetadldadlESLPEYLALLDRLEEDGLPEYEERFKE 838
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
97-339 |
2.59e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 97 RGLSLTETELEELRAQVLQLVAELEE--TRELAGQHEDDSLELQGLLEDERLASAQ-QAEVFTKQIQQLQGELQHLREEI 173
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEElqKELYALANEISRLEQQKQILRERLANLErQLEELEAQLEELESKLDELAEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 174 SLLEHEKES---ELKEMEQELHLAQAEIQNLRQAAADSATEHE---SDIASLQDDLCRLQNDLDDMERIRGDYEMEIASL 247
Cdd:TIGR02168 340 AELEEKLEElkeELESLEAELEELEAELEELESRLEELEEQLEtlrSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 248 RAEMElktSEPSNLSISDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDrtRRATERWLESHLLRSTMS 327
Cdd:TIGR02168 420 QQEIE---ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA--LDAAERELAQLQARLDSL 494
|
250
....*....|..
gi 1907172355 328 SESQTSELDFPE 339
Cdd:TIGR02168 495 ERLQENLEGFSE 506
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
103-290 |
2.92e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 103 ETELEELRAQVLQLVAELEETRElagQHEDDSLELQGLLEDERLASAQQAEVFTK-QIQQLQGELQHLREEISLLEHE-- 179
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQ---KNGLVDLSEEAKLLLQQLSELESQLAEARaELAEAEARLAALRAQLGSGPDAlp 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 180 ---KESELKEMEQELHLAQAEIQNLRQaaadSATEHESDIASLQDDLCRLQNDLDD-MERIRGDYEMEIASLRAEMELKT 255
Cdd:COG3206 258 ellQSPVIQQLRAQLAELEAELAELSA----RYTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQ 333
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907172355 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 |
1.57e-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: 49.92 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 103 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDerlASAQQAEVFT-KQIQQLQGELQHLREEISLLEheke 181
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK---YEEQLGNVRNnKEYEALQKEIESLKRRISDLE---- 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907172355 182 SELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEI 244
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
136-482 |
2.53e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 136 ELQGLLE-DERLASA-QQAEVFTKQIQQLQGELQHLREEISLLEHEKE---------SELKEMEQELHLAQAEiqnlrqa 204
Cdd:TIGR02169 161 EIAGVAEfDRKKEKAlEELEEVEENIERLDLIIDEKRQQLERLRREREkaeryqallKEKREYEGYELLKEKE------- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 205 aadsatEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEPSNLSISDFSGIQDELHHLRERYNLLN 284
Cdd:TIGR02169 234 ------ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 285 EEYQALRESNSSLTGQLAELESDRTR-RATERWLESHLLRSTMSSESQTSELDfpEPDPVMQLLRQQLLGAEEQMQDMQD 363
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKlLAEIEELEREIEEERKRRDKLTEEYA--ELKEELEDLRAELEEVDKEFAETRD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 364 KCKNLYCELEELQHHRRTSEEEQKRLQRELKCAQNEVLRFQ---TSHSTQHEELKSRLCTLQQKYDASQDEHSELLKvqm 440
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNaaiAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA--- 462
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1907172355 441 QLETELQQLRLLRCTPVESQSE-KELMCRLQKLQAQHQCSVNE 482
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDRVEKElSKLQRELAEAEAQARASEER 505
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
107-551 |
4.20e-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: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 107 EELRAQVLQLVAELEETRELAgqheddslelQGLLEDerlaSAQQAEVFTKQIQQLQGELQHLReeiSLLEHEKESELKE 186
Cdd:pfam15921 141 EDLRNQLQNTVHELEAAKCLK----------EDMLED----SNTQIEQLRKMMLSHEGVLQEIR---SILVDFEEASGKK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 187 MEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLD--------DMERIRGDYEMEIASLRAEMELKT--- 255
Cdd:pfam15921 204 IYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEalksesqnKIELLLQQHQDRIEQLISEHEVEItgl 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 256 SEPSNLSISDFSGIQDELHHLRERynllneeyqaLRESNSSLTGQLAELESDRTRraterwleshlLRSTMSSESQTSEL 335
Cdd:pfam15921 284 TEKASSARSQANSIQSQLEIIQEQ----------ARNQNSMYMRQLSDLESTVSQ-----------LRSELREAKRMYED 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 336 DFPEPDPVMQLLRQQLLGAEEQMQDMQDKCKNLYCELEEL--QHHRRTSE-----EEQKR--------------LQRELK 394
Cdd:pfam15921 343 KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLlaDLHKREKElslekEQNKRlwdrdtgnsitidhLRRELD 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 395 CAQNEVLRFQTSHSTQHEELKSRlctLQQKYDASQDEHSELLKVQmQLETELQQLR-LLRCTPVESQSEKELMCRLQKLQ 473
Cdd:pfam15921 423 DRNMEVQRLEALLKAMKSECQGQ---MERQMAAIQGKNESLEKVS-SLTAQLESTKeMLRKVVEELTAKKMTLESSERTV 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 474 AQHQCSVNEKEQLLEVQHHLHDKLRCHE----SEVHRLRSMVDCLREKNEKNSGIHLQLQEMKGLYQFSRDELERQKHMY 549
Cdd:pfam15921 499 SDLTASLQEKERAIEATNAEITKLRSRVdlklQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLV 578
|
..
gi 1907172355 550 DQ 551
Cdd:pfam15921 579 GQ 580
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
150-572 |
4.23e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 150 QQAEVFTKQIQQLQGELQHLREEISllehEKESELKEMEQELHLAQAEIQNLRQAAADSATEHEsdIASLQDDLCRLQND 229
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELE----ELEAELEELREELEKLEKLLQLLPLYQELEALEAE--LAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 230 LDDMERIRGDYEM---EIASLRAEMELKTSEPSNLSISDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELES 306
Cdd:COG4717 155 LEELRELEEELEEleaELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 307 DRTRRATERWLESHLLRSTMSSE------SQTSELDFPEPDPVMQLLRQQLLGAEEQMQDMQDKCKNLycELEELQHHRR 380
Cdd:COG4717 235 ELEAAALEERLKEARLLLLIAAAllallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK--EAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 381 TSEEEQKRLQRELKcaqneVLRFQTSHSTQH-EELKSRLCTLQQKYDASQDEHSELLkvQMQLETELQQLrllrCTPVES 459
Cdd:COG4717 313 LEELEEEELEELLA-----ALGLPPDLSPEElLELLDRIEELQELLREAEELEEELQ--LEELEQEIAAL----LAEAGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 460 QSEKELMCRLQKLQaqhqcsvnEKEQLLEVQHHLHDKLRCHESEVHRLRSMVDclrekneknsgihlqLQEMKGLYQFSR 539
Cdd:COG4717 382 EDEEELRAALEQAE--------EYQELKEELEELEEQLEELLGELEELLEALD---------------EEELEEELEELE 438
|
410 420 430
....*....|....*....|....*....|...
gi 1907172355 540 DELERQKHMYDQLEQDFLLCQQELTELKSSQSL 572
Cdd:COG4717 439 EELEELEEELEELREELAELEAELEQLEEDGEL 471
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
181-448 |
6.12e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 6.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 181 ESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQddLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEPSN 260
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQ--LSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 261 LSIsdfsgiqdelhhlrerynllNEEYQALRESNSSLTGQLAELESdrtrrateRWLESHllrstmssesqtseldfpep 340
Cdd:COG3206 259 LLQ--------------------SPVIQQLRAQLAELEAELAELSA--------RYTPNH-------------------- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 341 dPVMQLLRQQLLGAEEQMQDMQDKcknlycELEELQHHRRTSEEEQKRLQRELKCAQNEVLRFQtshstqheELKSRLCT 420
Cdd:COG3206 291 -PDVIALRAQIAALRAQLQQEAQR------ILASLEAELEALQAREASLQAQLAQLEARLAELP--------ELEAELRR 355
|
250 260
....*....|....*....|....*...
gi 1907172355 421 LQQKYDASQDEHSELLKVQMQLETELQQ 448
Cdd:COG3206 356 LEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
99-619 |
1.04e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 99 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQiQQLQGELQHLREEISLLEH 178
Cdd:PRK02224 215 LAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERER-EELAEEVRDLRERLEELEE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 179 EK-----ESELKEMEQE-LHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEME 252
Cdd:PRK02224 294 ERddllaEAGLDDADAEaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 253 lKTSEPSNLSISDFSGIQDELHHLRERYNL-------LNEEYQALRESNSSLTGQLAELESDRtRRATERWLESHLLRst 325
Cdd:PRK02224 374 -EAREAVEDRREEIEELEEEIEELRERFGDapvdlgnAEDFLEELREERDELREREAELEATL-RTARERVEEAEALL-- 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 326 mssesqtSELDFPEpdpvmqlLRQQLLGAE--EQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQrELKCAQNEVLRF 403
Cdd:PRK02224 450 -------EAGKCPE-------CGQPVEGSPhvETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 404 QtshsTQHEELKSRLCTLQQKYDASQDEHSELLKVQMQLETELQQLRlLRCTPVESQSEKELMcRLQKLQAQHQCSVNEK 483
Cdd:PRK02224 515 E----ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKR-EAAAEAEEEAEEARE-EVAELNSKLAELKERI 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 484 EQLlevqhhlhDKLRCHESEVHRLRSMVDCLREKNEknsgihlQLQEMKGLyqfSRDELERQKHMYDQLEQDFLlcQQEL 563
Cdd:PRK02224 589 ESL--------ERIRTLLAAIADAEDEIERLREKRE-------ALAELNDE---RRERLAEKRERKRELEAEFD--EARI 648
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907172355 564 TELKSSQSLCEEN-GNCSNKCDALLARLTELQDKFKASQEEIghlqmEQCELLEDQR 619
Cdd:PRK02224 649 EEAREDKERAEEYlEQVEEKLDELREERDDLQAEIGAVENEL-----EELEELRERR 700
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
97-268 |
1.21e-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: 48.22 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 97 RGLSLTETELEELRAQVLQLVAELEETREL----------AGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGEL 166
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEElaellralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 167 QHLREEISLLEHEKESELKEMEQELHLAQAEIQNLRQAAAdsatEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIAS 246
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKA----ERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
170 180
....*....|....*....|..
gi 1907172355 247 LRAEMELKTSEPSNLSISDFSG 268
Cdd:COG4942 232 LEAEAAAAAERTPAAGFAALKG 253
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
103-578 |
1.30e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.96 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 103 ETELEELRAQVLQLVAELE----ETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEH 178
Cdd:pfam15921 259 ELLLQQHQDRIEQLISEHEveitGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 179 EKESELKEMEQELHLAQAEIQNLRQAAADSATEHesdiASLQDDLCRLQNDLDDMERirgdyemeiaslraEMELKTSEP 258
Cdd:pfam15921 339 MYEDKIEELEKQLVLANSELTEARTERDQFSQES----GNLDDQLQKLLADLHKREK--------------ELSLEKEQN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 259 SNLSISDfSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQlAELESDRTRRATERWLESHLLRSTMSSESQTSEldfp 338
Cdd:pfam15921 401 KRLWDRD-TGNSITIDHLRRELDDRNMEVQRLEALLKAMKSE-CQGQMERQMAAIQGKNESLEKVSSLTAQLESTK---- 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 339 epdPVMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQR--ELKCAQNEVLRFQTSHsTQHEELKS 416
Cdd:pfam15921 475 ---EMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSrvDLKLQELQHLKNEGDH-LRNVQTEC 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 417 RLCTLQQkydASQDEHSELLKVQMQLETEL--QQLRLLRCTPVE-SQSEKELMCRLQKLQAQHQCSVNEKEQLLEVQHHL 493
Cdd:pfam15921 551 EALKLQM---AEKDKVIEILRQQIENMTQLvgQHGRTAGAMQVEkAQLEKEINDRRLELQEFKILKDKKDAKIRELEARV 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 494 HD----KLRCHESEVHRLRSMVDCLREKNEknsgihlQLQEMKGlyqfSRDELERQKHMYDQLEQDFLLCQQEL------ 563
Cdd:pfam15921 628 SDleleKVKLVNAGSERLRAVKDIKQERDQ-------LLNEVKT----SRNELNSLSEDYEVLKRNFRNKSEEMetttnk 696
|
490
....*....|....*..
gi 1907172355 564 --TELKSSQSLCEENGN 578
Cdd:pfam15921 697 lkMQLKSAQSELEQTRN 713
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
203-450 |
1.97e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 203 QAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEPSNLsisdfsgiQDELHHLRERYNL 282
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL--------EQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 283 LNEEYQALRESNSSLTGQLAELEsdrtrRATERWLESHLLRSTMSSEsqtselDFPEPDPVMQLLRQQLLGAEEQMQDMQ 362
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELL-----RALYRLGRQPPLALLLSPE------DFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 363 DkcknlycELEELQHHRRTSEEEQKRLQRELKCAQNEVLRFQTSHSTQHEELKSrlctLQQKYDASQDEHSELLKVQMQL 442
Cdd:COG4942 157 A-------DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR----LEKELAELAAELAELQQEAEEL 225
|
....*...
gi 1907172355 443 ETELQQLR 450
Cdd:COG4942 226 EALIARLE 233
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
104-292 |
2.35e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 104 TELEELRAQVLQLVAELEETRELAGQHEDDSLE-LQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEHEK-- 180
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLELLEaELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRle 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 181 --ESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEp 258
Cdd:COG4913 342 qlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE- 420
|
170 180 190
....*....|....*....|....*....|....
gi 1907172355 259 snlsisdFSGIQDELHHLRERYNLLNEEYQALRE 292
Cdd:COG4913 421 -------LRELEAEIASLERRKSNIPARLLALRD 447
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
141-321 |
2.52e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 141 LEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLehEKESELKEMEQELHLAQAEIQNLRQAAADsATEHESDIASLQ 220
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREAL--QRLAEYSWDEIDVASAEREIAELEAELER-LDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 221 DDLCRLQNDLDDMERIRGDYEMEIASLRAEMElktsepsnlsisdfsGIQDELHHLRERYNLLNEEYQAlrESNSSLTGQ 300
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELE---------------QAEEELDELQDRLEAAEDLARL--ELRALLEER 754
|
170 180
....*....|....*....|.
gi 1907172355 301 LAELESDRTRRATERWLESHL 321
Cdd:COG4913 755 FAAALGDAVERELRENLEERI 775
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
102-315 |
2.56e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 102 TETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELQHLREEISLLEHEKE 181
Cdd:COG4913 666 AEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRL-EKELEQAEEELDELQDRLEAAEDLAR 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 182 SELKEmEQELHLAQAEIQNLRQAAADSAtehESDIASLQDDLCRLQNDLDD-MERIRGDYEMEIASLRAEMElktsepsn 260
Cdd:COG4913 745 LELRA-LLEERFAAALGDAVERELRENL---EERIDALRARLNRAEEELERaMRAFNREWPAETADLDADLE-------- 812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907172355 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]; |
204-450 |
7.94e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 7.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 204 AAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEmEIASLRAEMELktsepsnlsisdfsgIQDELHHLR-----E 278
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELLEPIRELAE-RYAAARERLAE---------------LEYLRAALRlwfaqR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 279 RYNLLNEEYQALRESNSSLTGQLAELESDRTR-RATERWLESHLLrstmssESQTSELDfpepdpvmqLLRQQLLGAEEQ 357
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDAlREELDELEAQIR------GNGGDRLE---------QLEREIERLERE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 358 MQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELKCAQNEVLRFQTSHSTQHEELKSRLCTLQQKYDASQDEHSELLK 437
Cdd:COG4913 354 LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
250
....*....|...
gi 1907172355 438 VQMQLETELQQLR 450
Cdd:COG4913 434 RKSNIPARLLALR 446
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
102-314 |
9.23e-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: 45.53 E-value: 9.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 102 TETELEELRAQVLQLVAELEETRelagQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEHEKE 181
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALK----KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 182 SELKEMEQELHLAQAEIQNLR----------QAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEM 251
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPlalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907172355 252 ELKTSEPSNLSiSDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATE 314
Cdd:COG4942 181 AELEEERAALE-ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
138-486 |
1.04e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.88 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 138 QGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEHEKESELKEMEQELHLAQAEiqNLRQAAADSA----TEHE 213
Cdd:pfam17380 263 QTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAE--KARQAEMDRQaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 214 SDIASLQDDLCRLQND--LDDMERIRG-DYEMEIASLRaEMELKTSEPSNLSisdfSGIQDELHHLReRYNLLNEEYQal 290
Cdd:pfam17380 341 RMAMERERELERIRQEerKRELERIRQeEIAMEISRMR-ELERLQMERQQKN----ERVRQELEAAR-KVKILEEERQ-- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 291 resnSSLTGQLAELESDRTRRATERWLESHLLRSTMSSESQTSELDFPEPDPVMQLLRQQllgAEEQmqdmqdKCKNLYC 370
Cdd:pfam17380 413 ----RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ---EEER------KRKKLEL 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 371 ELEElQHHRRTSEEEQKRLQRELKCAQNEVLRFQTSHSTQHEELKSRLCTLQQKYDASQDEHSELLKVQMQLETELQQlR 450
Cdd:pfam17380 480 EKEK-RDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQE-Q 557
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907172355 451 LLRCTpvESQSEKELMCRLQKLQAQHQCSVNEKEQL 486
Cdd:pfam17380 558 MRKAT--EERSRLEAMEREREMMRQIVESEKARAEY 591
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
99-250 |
1.50e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 99 LSLTETELEELRAQVLQLVAELEETRELAGQH-------EDDSLELQGLLEDERLASA-QQAEVFTKQIQQLQGELQHLR 170
Cdd:COG3883 60 LEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsGGSVSYLDVLLGSESFSDFlDRLSALSKIADADADLLEELK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 171 EEISLLEhEKESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAE 250
Cdd:COG3883 140 ADKAELE-AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
100-241 |
2.78e-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: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 100 SLTETELEELRAQVLQLVAELEETR----ELAGQHEDDSLELQGLLEDERLASAQQaevftkQIQQLQGELQHLRE---- 171
Cdd:COG3206 215 KLLLQQLSELESQLAEARAELAEAEarlaALRAQLGSGPDALPELLQSPVIQQLRA------QLAELEAELAELSArytp 288
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907172355 172 ---EISLLEHEKESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYE 241
Cdd:COG3206 289 nhpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
132-377 |
3.44e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 132 DDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELQHLREEISLlEHEKESELKEMEQElhlAQAEIQNLRQAAADSATE 211
Cdd:PHA02562 157 EDLLDISVLSEMDKLNKDKIREL-NQQIQTLDMKIDHIQQQIKT-YNKNIEEQRKKNGE---NIARKQNKYDELVEEAKT 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 212 HESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTSE----------PSNLS-ISD----FSGIQDELHHL 276
Cdd:PHA02562 232 IKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVikmyekggvcPTCTQqISEgpdrITKIKDKLKEL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 277 RERYNLLNEEYQALRESNSSLTGQlaelesdrTRRATErwleshlLRSTMSSESQTseldfpepdpvMQLLRQQLLGAEE 356
Cdd:PHA02562 312 QHSLEKLDTAIDELEEIMDEFNEQ--------SKKLLE-------LKNKISTNKQS-----------LITLVDKAKKVKA 365
|
250 260
....*....|....*....|.
gi 1907172355 357 QMQDMQDKCKNLYCELEELQH 377
Cdd:PHA02562 366 AIEELQAEFVDNAEELAKLQD 386
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
99-231 |
3.59e-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: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 99 LSLTETELEELRAQVLQLVAELEETRELAGQHED------DSLELQGLLEDERLASAQQAEV---FTK---QIQQLQGEL 166
Cdd:COG3206 221 LSELESQLAEARAELAEAEARLAALRAQLGSGPDalpellQSPVIQQLRAQLAELEAELAELsarYTPnhpDVIALRAQI 300
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907172355 167 QHLREEIsllEHEKESELKEMEQELHLAQAEIQNLRQAAADsATEHESDIASLQDDLCRLQNDLD 231
Cdd:COG3206 301 AALRAQL---QQEAQRILASLEAELEALQAREASLQAQLAQ-LEARLAELPELEAELRRLEREVE 361
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
97-247 |
3.91e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 97 RGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQgllederlASAQQAEVFTKQIQQLQGELQHLREEISLL 176
Cdd:PRK09039 46 REISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLR--------ASLSAAEAERSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907172355 177 EHEKESELKEMEQELHLAQAEIQNLRQaaadsatehesDIASLQDDLCRLQNDLDDMERIRGDYEMEIASL 247
Cdd:PRK09039 118 AGELAQELDSEKQVSARALAQVELLNQ-----------QIAALRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
103-450 |
3.93e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 103 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEHEKES 182
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 183 E------------LKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAE 250
Cdd:COG1196 500 EadyegflegvkaALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 251 MELKTSEPSNLSIS------DFSGIQDELHHLRERY-NLLNEEYQALRESNSSLTGQLAELESDRTRRATERWLESHLLR 323
Cdd:COG1196 580 DKIRARAALAAALArgaigaAVDLVASDLREADARYyVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 324 STMSSESQtseldfpepdpvmQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELKCAQNEVLRF 403
Cdd:COG1196 660 GSLTGGSR-------------RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1907172355 404 QTSHSTQHEELKSRLCTLQQKYDASQDEHSELLKVQMQLETELQQLR 450
Cdd:COG1196 727 EEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
105-399 |
6.31e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.19 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 105 ELEELRAQVLQLVAELEETRELAGQHeDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLrEEISLLEHEKESEL 184
Cdd:pfam05557 22 ELEHKRARIELEKKASALKRQLDRES-DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYL-EALNKKLNEKESQL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 185 KEMEQELHLAQAEIQNLRQAAADSA---TEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRA------------ 249
Cdd:pfam05557 100 ADAREVISCLKNELSELRRQIQRAElelQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqrikelefei 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 250 ------EMELKTSEPSNLSISDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATERWLESHLLR 323
Cdd:pfam05557 180 qsqeqdSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 324 STMSSES--QTSELDFPEPDP----VMQLLR-------------QQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEE 384
Cdd:pfam05557 260 ELQSWVKlaQDTGLNLRSPEDlsrrIEQLQQreivlkeenssltSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKA 339
|
330
....*....|....*
gi 1907172355 385 EQKRLQRELKCAQNE 399
Cdd:pfam05557 340 LVRRLQRRVLLLTKE 354
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
133-455 |
6.42e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 133 DSLELQGLLEDERLASAQ---QAEVFTKQIQQLQGELQHLREEISllehekeselkEMEQELHLAQAEIQNLRQAAADSA 209
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQdleQTLALLDKIDRQKEETEQLKQQLA-----------QAPAKLRQAQAELEALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 210 TEH---------ESDIASLQDDLCRLQNDLddmerirGDYEMEIASLRaemelktSEPsnlsisdfsgiqdelhhlrER- 279
Cdd:PRK11281 115 RETlstlslrqlESRLAQTLDQLQNAQNDL-------AEYNSQLVSLQ-------TQP-------------------ERa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 280 YNLLNEEYQALRESNSSLTGQLAELESDRTRRATERWLESHLLrstmssESQTSeldfpepdpvmqlLRQQLLGAEEQMQ 359
Cdd:PRK11281 162 QAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALL------NAQND-------------LQRKSLEGNTQLQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 360 DmqdkcknlyceLEELQHHRRTseEEQKRLQRELKCAQNEVLRFQTSHSTQHEElksrlcTLQQKYDASQDEHSELLKVQ 439
Cdd:PRK11281 223 D-----------LLQKQRDYLT--ARIQRLEHQLQLLQEAINSKRLTLSEKTVQ------EAQSQDEAARIQANPLVAQE 283
|
330
....*....|....*.
gi 1907172355 440 MQLETELQQlRLLRCT 455
Cdd:PRK11281 284 LEINLQLSQ-RLLKAT 298
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
99-449 |
7.94e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 7.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 99 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISLLEH 178
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 179 EKESELKEMEQ--ELHLAQAEIQNLRQAAADSAtehesdIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKTS 256
Cdd:COG4717 221 ELEELEEELEQleNELEAAALEERLKEARLLLL------IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 257 EPSNLSISDFsgiqDELHHLRERYNLLNEEYQALRES---NSSLTGQLAELESDRTRRATERWLESHLLRSTMSSESQTS 333
Cdd:COG4717 295 REKASLGKEA----EELQALPALEELEEEELEELLAAlglPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 334 ELDfpepdpvmQLLRQQLLGAEEQMQDMQDKCKnlycELEELqhhrrtsEEEQKRLQRELKCAQNEVLRFQTSHSTqhEE 413
Cdd:COG4717 371 EIA--------ALLAEAGVEDEEELRAALEQAE----EYQEL-------KEELEELEEQLEELLGELEELLEALDE--EE 429
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907172355 414 LKSRLCTLQQKYDASQDEHSELLKVQMQLETELQQL 449
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAELEQL 465
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
71-488 |
9.85e-04 |
|
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: 9.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 71 EEEEEEVEEEQVEKGGSLGSLsmgkhrglsltETELEELRAQVLQLVAELEETRELAGQHEDDSLELQglleDERLASAQ 150
Cdd:COG1196 329 EEELEELEEELEELEEELEEA-----------EEELEEAEAELAEAEEALLEAEAELAEAEEELEELA----EELLEALR 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 151 QAEVFTKQIQQLQGELQHLREEISLLEHEKES---ELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQ 227
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEEleeALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 228 NDLDDMERIRGDYEMEIASLRAEMELKTSEPSNLS-------ISDFSGIQDELHHLRERYN---------LLNEEYQALR 291
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEgvkaallLAGLRGLAGAVAVLIGVEAayeaaleaaLAAALQNIVV 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 292 ESNSSLTGQLAELESDRTRRATERWLESHLLRSTMSSESQTSELDFP----EPDPVMQLLRQQLLGAEEQMQDMQDKckn 367
Cdd:COG1196 554 EDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAvdlvASDLREADARYYVLGDTLLGRTLVAA--- 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 368 lycELEELQHHRRTSEEEQKRLQRELKCAQNEVLRFQTSHSTQHEELKSRLCTLQQKYDASQDEHSELLKVQMQLETELQ 447
Cdd:COG1196 631 ---RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1907172355 448 QLRLLRCTPVESQSEKELMCRLQKLQAQHQCSVNEKEQLLE 488
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
271-574 |
1.04e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 271 DELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRraterwLESHLLRSTMSSESQTSELdfpepdpvmQLLRQQ 350
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE------LRLEVSELEEEIEELQKEL---------YALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 351 LLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELKCAQNEVLRFQtshsTQHEELKSRLCTLQQKYdasQD 430
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK----EELESLEAELEELEAEL---EE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 431 EHSELLKVQMQLETELQQLRLLRctpvesQSEKELMCRLQKLQAQHQCSVNEKEQLLEVQHHLHDKLrcHESEVHRLRSM 510
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQLE------LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL--EEAELKELQAE 441
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907172355 511 VDCLREKNEKNSGIHLQLQEmkglyqfsrdELERQKHMYDQLEQDFLLCQQELTELKSSQSLCE 574
Cdd:TIGR02168 442 LEELEEELEELQEELERLEE----------ALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
102-210 |
1.28e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.25 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 102 TETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLlederlasAQQAEvftKQIQQLQGELQHLREEISLLEHEKE 181
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGL--------AAELE---EKQQELEAQLEQLQEKAAETSQERK 215
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1907172355 182 SELKEMEQE----LHLAQAEI-----QNLRQAA--ADSAT 210
Cdd:PRK11448 216 QKRKEITDQaakrLELSEEETrilidQQLRKAGweADSKT 255
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
103-449 |
1.53e-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: 41.93 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 103 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQaevfTKQIQQLQGELQHLREEISLLEHEKE- 181
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN----NKKIKELEKQLNQLKSEISDLNNQKEq 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 182 -------SELKEMEQELHLAQAEIQNLRQaaadSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELK 254
Cdd:TIGR04523 307 dwnkelkSELKNQEKKLEEIQNQISQNNK----IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 255 TSEPSNL--SISDF-SGIQD----------ELHHLRERYNLLNEEYQALRESNSSLTGQLAELES------------DRT 309
Cdd:TIGR04523 383 KQEIKNLesQINDLeSKIQNqeklnqqkdeQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNqdsvkeliiknlDNT 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 310 RRATERWLEShLLRSTMS----SESQTSELDFPEpdpvmqllrQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEE 385
Cdd:TIGR04523 463 RESLETQLKV-LSRSINKikqnLEQKQKELKSKE---------KELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907172355 386 QKRLQRELKCAQNEVLRFQTshSTQHEELKSRLCTLQQKYDASQDEHSELLKVQMQLETELQQL 449
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDDF--ELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQK 594
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
102-311 |
2.16e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 102 TETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEvftkQIQQLQGELQHLREEISLLEHEKE 181
Cdd:COG1196 629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE----LEELAERLAEEELELEEALLAEEE 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 182 SELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERI--RGDYEMEIASLRAEMELKtsEPS 259
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPpdLEELERELERLEREIEAL--GPV 782
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907172355 260 NL-SIsdfsgiqDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRR 311
Cdd:COG1196 783 NLlAI-------EEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
108-292 |
4.03e-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: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 108 ELRAQVLQLVAELEETRELAGQHEDdslELQGLLEDerlaSAQQAEVFTKQIQQLQGELQHLREEISllehEKESELKEM 187
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIE---NLNGKKEE----LEEELEELEAALRDLESRLGDLKKERD----ELEAQLREL 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 188 EQELHLAQAEIQNLRQAAAD---SATEHESDIASLQDDLCRLQNDLDDmERIRGDYEMEIasLRAEMELKTSEPSN-LSI 263
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRLSElkaKLEALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAEL--QRVEEEIRALEPVNmLAI 978
|
170 180
....*....|....*....|....*....
gi 1907172355 264 SDFSGIQDELHHLRERYNLLNEEYQALRE 292
Cdd:TIGR02169 979 QEYEEVLKRLDELKEKRAKLEEERKAILE 1007
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
85-204 |
4.08e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 85 GGSLGSLSMGKHRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQG 164
Cdd:COG1196 656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1907172355 165 ELQHLREEISLLEHEKESELKEMEQELHLAQAEIQNLRQA 204
Cdd:COG1196 736 ELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
189-314 |
4.23e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 189 QELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEME-LKTSEPSNLSISDFS 267
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkYEEQLGNVRNNKEYE 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1907172355 268 GIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAELESDRTRRATE 314
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE 139
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
106-448 |
4.52e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 106 LEELRAQVLQLVAELEETRElagqhEDDSLElqglledERLASAQQAEVFTKQIQQLQ------GELQHLREEISLLEHE 179
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEE-----EVEEVE-------ERLERAEDLVEAEDRIERLEerredlEELIAERRETIEEKRE 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 180 KESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRgdyemEIASLRAEMElktseps 259
Cdd:PRK02224 538 RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIR-----TLLAAIADAE------- 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 260 nlsisdfsgiqDELHHLRERynllneeyqalREsnssltgQLAELESDRTRRATERwleshllrstmssESQTSELDFPE 339
Cdd:PRK02224 606 -----------DEIERLREK-----------RE-------ALAELNDERRERLAEK-------------RERKRELEAEF 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 340 PDPVMQLLRQQLLGAEEQMQDMQDKcknlyceLEELqhhrrtsEEEQKRLQRELKCAQNEVLRFqtshstqhEELKSRLC 419
Cdd:PRK02224 644 DEARIEEAREDKERAEEYLEQVEEK-------LDEL-------REERDDLQAEIGAVENELEEL--------EELRERRE 701
|
330 340 350
....*....|....*....|....*....|..
gi 1907172355 420 TLQQKYDASQ---DEHSELLKVQMQLETELQQ 448
Cdd:PRK02224 702 ALENRVEALEalyDEAEELESMYGDLRAELRQ 733
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
348-688 |
4.54e-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: 40.44 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 348 RQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELKCAQNEVLRFQTSHSTQHEELKSRLCTLQQKYDA 427
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 428 SQDEHSELLKVQMQLETELQQL--RLLRCTPVESQSEKELMCRLQKLQAQHQCSVNEKEQLLEvqhHLHDKLRCHESEVH 505
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELnkKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELE---DAEERLAKLEAEID 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 506 RLRSMVDCLREkneknsgihlqlqemkglyqfsrdELERQKHMYDQLEQDFLLCQQELTELKSsqslceengncsnKCDA 585
Cdd:TIGR02169 333 KLLAEIEELER------------------------EIEEERKRRDKLTEEYAELKEELEDLRA-------------ELEE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 586 LLARLTELQDKFKASQEEIGHLQMEQCELLEDQRRLQEEQGQLQEELHRLTfpQPKCGILQKSQELLSKLQDLCEmqlly 665
Cdd:TIGR02169 376 VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN--AAIAGIEAKINELEEEKEDKAL----- 448
|
330 340
....*....|....*....|...
gi 1907172355 666 qNMQEQQRKLTQNQECVLKEQLE 688
Cdd:TIGR02169 449 -EIKKQEWKLEQLAADLSKYEQE 470
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
96-310 |
4.80e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 96 HRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELQHLREEISL 175
Cdd:COG1196 598 GAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEA 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 176 LEHEKESELKEMEQELHLAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEMEIASLRAEMELKT 255
Cdd:COG1196 678 EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELP 757
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907172355 256 SEPSnlsisdfsgiqdeLHHLRERYNLLN--------------EEYQALRESNSSLTGQLAELESDRTR 310
Cdd:COG1196 758 EPPD-------------LEELERELERLEreiealgpvnllaiEEYEELEERYDFLSEQREDLEEARET 813
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
105-496 |
5.10e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.59 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 105 ELEELRAQVLQLVAELEETRELAGQHEDDSLElQGLLEDERLASAQ-QAEVFTKQIQQLQGELQHLREEISLLEHEKESE 183
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQHGAFLDADIE-TAAADQEQLPSWQsELENLEERLKALTGKHQDVTAKYNRRRSKIKEQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 184 LKEMEQELHLAQAEIqnlRQAAADSATEHESDIASLQDDLcRLQNDLDDMERIRGDYEMEIASLRAEMELKTSEPSNLSI 263
Cdd:pfam12128 388 NNRDIAGIKDKLAKI---REARDRQLAVAEDDLQALESEL-REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELL 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 264 SDFSGIQDELHHLRerynllnEEYQALRESNSSLTGQLAELESDRTRRATERWLESHLLRSTMSSESQTSELDFPEPDPV 343
Cdd:pfam12128 464 LQLENFDERIERAR-------EEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTL 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 344 MQLLRQQLLGAEEQMQDMQDKCKNLYCELEElqhhrrTSEEEQKRLQRELKCAQNEVLRFQTSHSTQHEE-LKSRLCTLQ 422
Cdd:pfam12128 537 LHFLRKEAPDWEQSIGKVISPELLHRTDLDP------EVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEeLRERLDKAE 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 423 QKYDASQDEHSELLKVQMQLETELQQLRL---------------LRCTPVESQSEKElmcRLQKLQAQHQCSVNEKEQLL 487
Cdd:pfam12128 611 EALQSAREKQAAAEEQLVQANGELEKASReetfartalknarldLRRLFDEKQSEKD---KKNKALAERKDSANERLNSL 687
|
....*....
gi 1907172355 488 EVQHHLHDK 496
Cdd:pfam12128 688 EAQLKQLDK 696
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
166-614 |
6.64e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 166 LQHLREEISLLEHEKESELKemeqelhlAQAEIQNLRQAAADSATEHESDIASLQDDLCRLQNDLDDMERIRGDYEmEIA 245
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIK--------RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE-ELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 246 SLRAEMELKTSEPSnlsiSDFSGIQDELHHLRERYNLLNEEYQALRESnsslTGQLAELESDrtrraTERWLESHLLRST 325
Cdd:PRK03918 238 EEIEELEKELESLE----GSKRKLEEKIRELEERIEELKKEIEELEEK----VKELKELKEK-----AEEYIKLSEFYEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 326 MSSESQTSELDfpepdpvMQLLRQQLLGAEEQMQDMQDK---CKNLYCELEELQhhRRTSE-EEQKRLQRELKCAQNEVL 401
Cdd:PRK03918 305 YLDELREIEKR-------LSRLEEEINGIEERIKELEEKeerLEELKKKLKELE--KRLEElEERHELYEEAKAKKEELE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 402 RFQTSHSTQH-EELKSRLCTLQQKYDASQDEHSELLKVQMQLETELQQLRL---------LRC----TPVESQSEKELMC 467
Cdd:PRK03918 376 RLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaieelkkakGKCpvcgRELTEEHRKELLE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 468 R----LQKLQAQHQCSVNEKEQLLEVQHHLhDKLRCHESEVHRLRSMVDCLREKNEKNSGIHLQlqemkglyqfsrdELE 543
Cdd:PRK03918 456 EytaeLKRIEKELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQLKELEEKLKKYNLE-------------ELE 521
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907172355 544 RQKHMYDQLEQDFLLCQQELTELKSSqslceengncSNKCDALLARLTELQDKFKASQEEIGHLQMEQCEL 614
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGEIKSLKKE----------LEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
106-283 |
7.95e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.61 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 106 LEELRAQVLQLVAELE----ETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTK----------QIQQLQGEL----- 166
Cdd:PHA02562 204 IEEQRKKNGENIARKQnkydELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKlntaaakiksKIEQFQKVIkmyek 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 167 --------QHLREEISLLEhEKESELKEMEQELHLAQAEIQNLRQ------AAADSATEHESDIASLQDDLCRLQNDLDD 232
Cdd:PHA02562 284 ggvcptctQQISEGPDRIT-KIKDKLKELQHSLEKLDTAIDELEEimdefnEQSKKLLELKNKISTNKQSLITLVDKAKK 362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907172355 233 MERI-------RGDYEMEIASLRAEMELKtsepsnlsISDFSGIQDELHHLRERYNLL 283
Cdd:PHA02562 363 VKAAieelqaeFVDNAEELAKLQDELDKI--------VKTKSELVKEKYHRGIVTDLL 412
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
103-431 |
9.08e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.11 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 103 ETELEELRAQVLQLVAELEETRE----LAGQHEDDSLELQGLLEDERLASAQQAE-------------VFTKQIQQLQGE 165
Cdd:pfam07888 72 ERQRRELESRVAELKEELRQSREkheeLEEKYKELSASSEELSEEKDALLAQRAAhearireleedikTLTQRVLERETE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 166 LQHLREE---ISLLEHEKESELKEMEQELHLAQAEIQNLR---QAAADSATEHESDIASLQDDLCRLQNDLDDMERirgd 239
Cdd:pfam07888 152 LERMKERakkAGAQRKEEEAERKQLQAKLQQTEEELRSLSkefQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHR---- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 240 YEMEIASLRAEMElKTSEPSNLSISDFSGIQDELHHLRERYNLLNEEYQALRESNSSLTGQLAE----LESDRTRRATER 315
Cdd:pfam07888 228 KEAENEALLEELR-SLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADaslaLREGRARWAQER 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 316 wleshllrstmSSESQTSELDFPEpdpvMQLLRQQLLGAEEQMQDMQDKCKNLYCELEELQHHRRTSEEEQKRLQRELKC 395
Cdd:pfam07888 307 -----------ETLQQSAEADKDR----IEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKA 371
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907172355 396 AQNEVLRFQTSHSTQHEELKSRLCTLQQKYDASQDE 431
Cdd:pfam07888 372 SLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVADA 407
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
103-192 |
9.60e-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: 37.21 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907172355 103 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERlasaqqaEVFTKQIQQLQGELQHLREEISLLEHEKES 182
Cdd:pfam09744 49 NVELEELREDNEQLETQYEREKALRKRAEEELEEIEDQWEQET-------KDLLSQVESLEEENRRLEADHVSRLEEKEA 121
|
90
....*....|
gi 1907172355 183 ELKEMEQELH 192
Cdd:pfam09744 122 ELKKEYSKLH 131
|
|
| |
