|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
84-393 |
1.15e-13 |
|
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: 75.48 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 84 VQKGGSVGSLSVNKHRGLSLTETELEELRAQVLQLVAELEETR----ELAGQHEDDSLELQGLLEDERLASAQ------Q 153
Cdd:TIGR02168 655 VRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEkalaELRKELEELEEELEQLRKELEELSRQisalrkD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 154 AEVFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQ---ELHLAQAEIQSLRQAAEDSATEH---ESDIASLQEDLCR 227
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeELAEAEAEIEELEAQIEQLKEELkalREALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 228 MQNELEDMERIRGDYEMEIASLRAEMEmkssEPSEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERW 307
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLE----DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 308 LQSQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELC--------CELEELQHHRQVSEEEQRRL 379
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerlseeysLTLEEAEALENKIEDDEEEA 970
|
330
....*....|....
gi 1390157443 380 QRELKCAQNEVLRF 393
Cdd:TIGR02168 971 RRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
107-425 |
1.35e-11 |
|
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: 68.94 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEvftKQIQQLQGELRSLREEISLLE---HEKE 183
Cdd:TIGR02169 188 RLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALE---RQKEAIERQLASLEEELEKLTeeiSELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 184 SELKEIEQELHLAQAEIQSL-----RQAAEDSAtEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEmkss 258
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIG-ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE---- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 259 EPSEELQELRERYHFLNEEYRALQESNSSLTGQLADLEsERTQRATERWLQSQT-LSMTSAESQTSEMDFLEPDPEMQLL 337
Cdd:TIGR02169 340 ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD-KEFAETRDELKDYREkLEKLKREINELKRELDRLQEELQRL 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 338 RQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNE--ELKSRLCTLQKK 415
Cdd:TIGR02169 419 SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKElsKLQRELAEAEAQ 498
|
330
....*....|
gi 1390157443 416 YDTSQDEQNE 425
Cdd:TIGR02169 499 ARASEERVRG 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
101-306 |
2.50e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQG---LLEDERLASAQQAEVFTKQIQQLQGELRSLREEISL 177
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQdiaRLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 178 LEHEK---ESELKEIEQELHLAQA---EIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRA 251
Cdd:COG1196 342 LEEELeeaEEELEEAEAELAEAEEallEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1390157443 252 EMEMKSSEPSEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATER 306
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
105-383 |
2.84e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 105 ETELEELRAQV------LQLVAELEETRELAGQHEDDSLELQ-GLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISL 177
Cdd:COG1196 199 ERQLEPLERQAekaeryRELKEELKELEAELLLLKLRELEAElEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 178 L----------EHEKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIA 247
Cdd:COG1196 279 LeleleeaqaeEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 248 SLRAEMEMKSSEPSEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAESQTSEmdf 327
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE--- 435
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1390157443 328 lepdpEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQREL 383
Cdd:COG1196 436 -----EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-690 |
3.60e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQqaevFTKQIQQLQGELRSLREEISLLEH 180
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ----LELQIASLNNEIERLEARLERLED 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 181 EKESELKEIEQ--------ELHLAQAEIQSLRQAAEDSATEHEsdiaSLQEDLCRMQNELEDMERIRGDYEMEIASLRAE 252
Cdd:TIGR02168 415 RRERLQQEIEEllkkleeaELKELQAELEELEEELEELQEELE----RLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 253 MEMkssepseeLQELRERYHFLNEEYRALQESNSSLTG---QLADLES--ERTQRATERWLQS--QTLSMTSAESQTSEM 325
Cdd:TIGR02168 491 LDS--------LERLQENLEGFSEGVKALLKNQSGLSGilgVLSELISvdEGYEAAIEAALGGrlQAVVVENLNAAKKAI 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 326 DFLEPD--------PEMQLLRQQLRDAEEQMHGMKNKCQELCCELEE------------LQHHRQVSEEEQ-RRLQRELK 384
Cdd:TIGR02168 563 AFLKQNelgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKfdpklrkalsylLGGVLVVDDLDNaLELAKKLR 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 385 CAQNEVL---------------RFQTSHSVTQN----EELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVM-- 443
Cdd:TIGR02168 643 PGYRIVTldgdlvrpggvitggSAKTNSSILERrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEle 722
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 444 ----------KSTLVENQSEKELLCRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCHEAELQHLRDTVASFKESNEKDT 513
Cdd:TIGR02168 723 elsrqisalrKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 514 ETHAQLQEMkqlYQASKDELERQKHMYDQLEQDLLLCQLELKELKASHPIPEDKGKCANK--------CDTLLSRLTELQ 585
Cdd:TIGR02168 803 EALDELRAE---LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAeieeleelIEELESELEALL 879
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 586 EKYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPKSGLLLKS--QELLTKLEDLCElqlLYQGMQEEq 663
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGleVRIDNLQERLSE---EYSLTLEE- 955
|
650 660
....*....|....*....|....*..
gi 1390157443 664 kkLIQNQDCVLKEQLEIHEELRRFKES 690
Cdd:TIGR02168 956 --AEALENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
153-455 |
6.97e-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: 6.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 153 QAEVFTKQIQQLQGELRSLREEISllehEKESELKEIEQELHLAQAEIQSLRqaaeDSATEHESDIASLQEDLCRMQNEL 232
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELK----EAEEELEELTAELQELEEKLEELR----LEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 233 EDMERIRGDYEMEIASLRAEMEMKSsepsEELQELRERYHFLNEEYRALQESNSSLTGQLADLESErtqraterwlqsqt 312
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELE----AQLEELESKLDELAEELAELEEKLEELKEELESLEAE-------------- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 313 LSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLR 392
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390157443 393 FQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKE 455
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
108-349 |
6.33e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 6.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 108 LEELRAQVLQLVAELEETRELAGQHEDdsleLQGLLEDERLASAQQAEVFTKQI--QQLQGELRSLREEISLLEhEKESE 185
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEA----ELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLD-ASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 186 LKEIEQELHLAQAEIQSLRQ---AAEDSATEHESDIASLQEDLCRMQNELEDME-------------------------R 237
Cdd:COG4913 687 LAALEEQLEELEAELEELEEeldELKGEIGRLEKELEQAEEELDELQDRLEAAEdlarlelralleerfaaalgdaverE 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 238 IRGDYEMEIASLRAEMEMKSSEPSEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTs 317
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGLPEYEERFKELLNENSI- 845
|
250 260 270
....*....|....*....|....*....|..
gi 1390157443 318 aESQTsemDFLepdpemQLLRQQLRDAEEQMH 349
Cdd:COG4913 846 -EFVA---DLL------SKLRRAIREIKERID 867
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
161-478 |
2.30e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 161 IQQLQGELRSLREEISLLE---HEKESELKEIEQELHLAQAEIQSLRQAAEDSA---TEHESDIASLQEDLCRMQNELED 234
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIEnrlDELSQELSDASRKIGEIEKEIEQLEQEEEKLKerlEELEEDLSSLEQEIENVKSELKE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 235 MERIRGDYEMEIASLRAEME-MKSSEPSEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERwlQSQTL 313
Cdd:TIGR02169 763 LEARIEELEEDLHKLEEALNdLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI--QELQE 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 314 SMTSAESQTSEMDflepdPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELK--CAQNEVL 391
Cdd:TIGR02169 841 QRIDLKEQIKSIE-----KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEelEAQIEKK 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 392 RFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELL---KMQLQLQTELRQLKVMKS-TLVENQSEKELLCRLQKLHLQH 467
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELsleDVQAELQRVEEEIRALEPvNMLAIQEYEEVLKRLDELKEKR 995
|
330
....*....|.
gi 1390157443 468 QNVTCEKEKLL 478
Cdd:TIGR02169 996 AKLEEERKAIL 1006
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
105-395 |
2.51e-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: 61.61 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 105 ETELEELRAQVLQLVAELEETRelAGQHEDDslelqgllederlasaqqaevftKQIQQLQGELRSLREEISLLEHEKE- 183
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELR--LEVSELE-----------------------EEIEELQKELYALANEISRLEQQKQi 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 184 --SELKEIEQELHLAQAEIQSLRQA---AEDSATEHESDIASLQEDLCRMQNELEdmerirgdyemEIASLRAEMEMKSS 258
Cdd:TIGR02168 307 lrERLANLERQLEELEAQLEELESKldeLAEELAELEEKLEELKEELESLEAELE-----------ELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 259 EPSEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERwlQSQTLSMTSAESQTSEMDFLEPDPEMQLLR 338
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI--EELLKKLEEAELKELQAELEELEEELEELQ 453
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1390157443 339 QQLRDAEEQMhgmknkcQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQT 395
Cdd:TIGR02168 454 EELERLEEAL-------EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
98-264 |
5.52e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 5.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 98 HRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDdslELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISL 177
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALRE---ELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 178 LEH----------EKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIA 247
Cdd:COG4913 364 LEAllaalglplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
170
....*....|....*..
gi 1390157443 248 SLRAEMEMKSSEPSEEL 264
Cdd:COG4913 444 ALRDALAEALGLDEAEL 460
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-771 |
8.08e-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: 59.69 E-value: 8.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEvftkQIQQLQGELRSLREEISLLEH 180
Cdd:TIGR02168 227 LALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE----EIEELQKELYALANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 181 EKE---SELKEIEQELHLAQAEIQSLRQA---AEDSATEHESDIASLQEDLCRMQNELEdmerirgdyemEIASLRAEME 254
Cdd:TIGR02168 303 QKQilrERLANLERQLEELEAQLEELESKldeLAEELAELEEKLEELKEELESLEAELE-----------ELEAELEELE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 255 MKSSEPSEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERwlQSQTLSMTSAESQTSEMDFLEPDPEM 334
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI--EELLKKLEEAELKELQAELEELEEEL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 335 QLLRQQLRDAEEQMhgmknkcQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHS-----VTQNEELKSRL 409
Cdd:TIGR02168 450 EELQEELERLEEAL-------EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEgvkalLKNQSGLSGIL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 410 CTLQKKYDTSQDEQNELLK-----MQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQH-QNVTCEKEKLLERQQQ 483
Cdd:TIGR02168 523 GVLSELISVDEGYEAAIEAalggrLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEiQGNDREILKNIEGFLG 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 484 LQEELQCHEAELQHLRDT-------VASFKESNEKDTETHAQL----------------------QEMKQLYQASK-DEL 533
Cdd:TIGR02168 603 VAKDLVKFDPKLRKALSYllggvlvVDDLDNALELAKKLRPGYrivtldgdlvrpggvitggsakTNSSILERRREiEEL 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 534 ERQKhmyDQLEQDLLLCQLELKELKASHPIPEDKGkcankcDTLLSRLTELQEKYKASQKEMGQLQMEQCELLEDQRRMQ 613
Cdd:TIGR02168 683 EEKI---EELEEKIAELEKALAELRKELEELEEEL------EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 614 EEQGQLQEELHRLTLPLPKSGLLLKSQElltklEDLCELQLLYQGMQEEQKKLIQNqdcvLKEQLEIHEELRRFKESHFQ 693
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAE-----AEIEELEAQIEQLKEELKALREA----LDELRAELTLLNEEAANLRE 824
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390157443 694 EVLENPDDSKLAKSSKCNRNKQSKLLMEQMQALQVMYDAGQAKQELLQQEQGRLLEERKRLQADLQLCLEEMQLLQVQ 771
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
110-476 |
3.68e-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: 57.77 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 110 ELRAQVLQLVAELEE-TRELAG-QHEDDSLE-LQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISllehEKESEL 186
Cdd:TIGR02169 671 SEPAELQRLRERLEGlKRELSSlQSELRRIEnRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE----ELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 187 KEIEQELHLAQAEIQSLrqaaedsatehESDIASLQEDLCRMQNELEDMERirgdyemeiaslraememkssepseelQE 266
Cdd:TIGR02169 747 SSLEQEIENVKSELKEL-----------EARIEELEEDLHKLEEALNDLEA---------------------------RL 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 267 LRERYHFLNEEYRALQESNSSLTGQLADLESErtqraterwLQSQTLSMTSAESqtsemdflepdpEMQLLRQQLRDAEE 346
Cdd:TIGR02169 789 SHSRIPEIQAELSKLEEEVSRIEARLREIEQK---------LNRLTLEKEYLEK------------EIQELQEQRIDLKE 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 347 QMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQtshsvTQNEELKSRLCTLQKKYDTSQDEQNEL 426
Cdd:TIGR02169 848 QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE-----AQLRELERKIEELEAQIEKKRKRLSEL 922
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1390157443 427 lkmQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCEKEK 476
Cdd:TIGR02169 923 ---KAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRA 969
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-302 |
4.48e-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: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDerlaSAQQAEVFTKQIQQLQGELRSLREEISLLEH 180
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED----LEEQIEELSEDIESLAAEIEELEELIEELES 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 181 EKESELKE---IEQELHLAQAEIQSL----------RQAAEDSATEHESDIASLQEDLCRMQNELEDM-ERIRGDYEMEI 246
Cdd:TIGR02168 874 ELEALLNErasLEEALALLRSELEELseelreleskRSELRRELEELREKLAQLELRLEGLEVRIDNLqERLSEEYSLTL 953
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 247 ASLRAEMEMKSSEPS------------------------EELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQR 302
Cdd:TIGR02168 954 EEAEALENKIEDDEEearrrlkrlenkikelgpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
148-366 |
5.40e-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: 56.31 E-value: 5.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 148 LASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKES---ELKEIEQELHLAQAEIQSLRQ---AAEDSATEHESDIASL 221
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAllkQLAALERRIAALARRIRALEQelaALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 222 QEDLCRMQNELEdmERIRGDYEMEIASlrAEMEMKSSEPSEELQELRERYHFLNEEYRALQEsnsSLTGQLADLESERTQ 301
Cdd:COG4942 96 RAELEAQKEELA--ELLRALYRLGRQP--PLALLLSPEDFLDAVRRLQYLKYLAPARREQAE---ELRADLAELAALRAE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390157443 302 RATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQ 366
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
101-383 |
1.25e-07 |
|
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: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 101 LSLTETELEELRAQVLQLvaelEETRELAGQHEDDSLELQGLledERLASAQQAEVFTKQIQQLQGELRSLREEISLLEH 180
Cdd:COG4913 237 LERAHEALEDAREQIELL----EPIRELAERYAAARERLAEL---EYLRAALRLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 181 EKEselkEIEQELHLAQAEIQSLRQAAEDSATEhesDIASLQEDLCRMQNELEDMERIRGDYEMEIASLraemEMKSSEP 260
Cdd:COG4913 310 ELE----RLEARLDALREELDELEAQIRGNGGD---RLEQLEREIERLERELEERERRRARLEALLAAL----GLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 261 SEELQELRERyhflneeyralqesnssLTGQLADLESERTQraterwlqsqtlsmtsaesqtsemdflepdpemqlLRQQ 340
Cdd:COG4913 379 AEEFAALRAE-----------------AAALLEALEEELEA-----------------------------------LEEA 406
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1390157443 341 LRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQREL 383
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
138-547 |
1.53e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 138 ELQGLLEDERLASAQQAEVF--TKQIQQLQGELRSLREEISLLEHEKES-----ELKEIEQELHLAQAEIQSLRQAAEdS 210
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAelQEELEELEEELEELEAELEELREELEKlekllQLLPLYQELEALEAELAELPERLE-E 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 211 ATEHESDIASLQEDLCRMQNELEDMERIRgdyEMEIASLRAEMEMKSSEPSEELQELRERYHFLNEEYRALQESNSSLTG 290
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEEL---EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 291 QLADLESERTQRATERWLQSQTLSMTSA-------ESQTSEMDFLEPDPEMQLLRQQLRDAEEQMhgMKNKCQELCCELE 363
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARLLLLIAaallallGLGGSLLSLILTIAGVLFLVLGLLALLFLL--LAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 364 ELQHHRQVSEEEQRRLQRELKcaqneVLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLkmQLQLQTELRQLkvM 443
Cdd:COG4717 306 ELQALPALEELEEEELEELLA-----ALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAAL--L 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 444 KSTLVEN-----------QSEKELLCRLQKLHLQhqnvtCEKEKLLERQQQLQEELQCHEAELQHLRDTVASFKESNEKD 512
Cdd:COG4717 377 AEAGVEDeeelraaleqaEEYQELKEELEELEEQ-----LEELLGELEELLEALDEEELEEELEELEEELEELEEELEEL 451
|
410 420 430
....*....|....*....|....*....|....*.
gi 1390157443 513 TETHAQL-QEMKQLyqASKDELERQKHMYDQLEQDL 547
Cdd:COG4717 452 REELAELeAELEQL--EEDGELAELLQELEELKAEL 485
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
158-383 |
4.33e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 158 TKQIQQLQGELRSLREEISLLehekESELKEIEQELHLAQAEIQSLRQAAEDSatEHESDIASLQEDLCRMQNELEDMEr 237
Cdd:COG4913 609 RAKLAALEAELAELEEELAEA----EERLEALEAELDALQERREALQRLAEYS--WDEIDVASAEREIAELEAELERLD- 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 238 irgdyemeiaslraememkssEPSEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERwlqsQTLSMTS 317
Cdd:COG4913 682 ---------------------ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL----DELQDRL 736
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390157443 318 AESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHgmknkcqelccelEELQHHRQVSEEEQRRLQREL 383
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALGDAVERELR-------------ENLEERIDALRARLNRAEEEL 789
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
105-298 |
7.62e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 105 ETELEELRAQVLQLVAELEETRElagQHEDDSLELQGLLEDERLASAQQaevftkQIQQLQGELRSLREEISLLEHEKES 184
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQ---KNGLVDLSEEAKLLLQQLSELES------QLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 185 ELKEIEQELhlAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSEEL 264
Cdd:COG3206 252 GPDALPELL--QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQARE 329
|
170 180 190
....*....|....*....|....*....|....
gi 1390157443 265 QELRERYhflnEEYRALQESNSSLTGQLADLESE 298
Cdd:COG3206 330 ASLQAQL----AQLEARLAELPELEAELRRLERE 359
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
101-283 |
7.85e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 7.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLED----------ERLASAQQAEVFTKQIQQLQGELRS 170
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEaeeeleelaeELLEALRAAAELAAQLEELEEAEEA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 171 LREEISLLEHEKESELKEIEQELHLAQAEIQSLRQAAEDSAtEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLR 250
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA-ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
170 180 190
....*....|....*....|....*....|...
gi 1390157443 251 AEMEMkssepseeLQELRERYHFLNEEYRALQE 283
Cdd:COG1196 491 ARLLL--------LLEAEADYEGFLEGVKAALL 515
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
110-453 |
1.04e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 52.75 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 110 ELRAQvlqLVAELEETRELAGQHEDDSLElQGLLEderlASAQQAEVfTKQIQQLQGELRSLREEISLL---EHEKESEL 186
Cdd:PRK10929 83 ELRQQ---LNNERDEPRSVPPNMSTDALE-QEILQ----VSSQLLEK-SRQAQQEQDRAREISDSLSQLpqqQTEARRQL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 187 KEIEQELHLAQAEIQSLRQAAedsatehesdIASLQEDLCRMQ---NELEdMERIRGDYEMEIASLRAEMEMKSSEPSE- 262
Cdd:PRK10929 154 NEIERRLQTLGTPNTPLAQAQ----------LTALQAESAALKalvDELE-LAQLSANNRQELARLRSELAKKRSQQLDa 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 263 ELQELRERYHFL--NEEYRALqESNSSLTGQLADL-ESERTQRATERWLqSQTLSmtsaeSQTSEMDFL-----EPDPEM 334
Cdd:PRK10929 223 YLQALRNQLNSQrqREAERAL-ESTELLAEQSGDLpKSIVAQFKINREL-SQALN-----QQAQRMDLIasqqrQAASQT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 335 QLLRQQLRDAEEQMH--GMKN-----------------KCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEvlrfqt 395
Cdd:PRK10929 296 LQVRQALNTLREQSQwlGVSNalgealraqvarlpempKPQQLDTEMAQLRVQRLRYEDLLNKQPQLRQIRQAD------ 369
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390157443 396 SHSVTQNEelksrlctlQKKYDTSQDEQNELLKMQLQ----LQTELRQLKVMKSTLVENQSE 453
Cdd:PRK10929 370 GQPLTAEQ---------NRILDAQLRTQRELLNSLLSggdtLILELTKLKVANSQLEDALKE 422
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
98-302 |
1.60e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 98 HRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISL 177
Cdd:COG1196 644 GRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 178 LEHEKESELKEIEQELHLAQAEIQSLRQAAEDSATEheSDIASLQEDLCRMQNELEDMERIrgdyemeiaSLRAEmemks 257
Cdd:COG1196 724 EALEEQLEAEREELLEELLEEEELLEEEALEELPEP--PDLEELERELERLEREIEALGPV---------NLLAI----- 787
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1390157443 258 sepsEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQR 302
Cdd:COG1196 788 ----EEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
140-457 |
1.75e-06 |
|
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: 52.05 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 140 QGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQELHLAQAEiqSLRQAAEDSA----TEHE 215
Cdd:pfam17380 263 QTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAE--KARQAEMDRQaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 216 SDIASLQEDLCRMQNE--LEDMERIRgdyEMEIAslraeMEMKSSEPSEELQELRERYhflNEEYRalQESNSSLTGQLa 293
Cdd:pfam17380 341 RMAMERERELERIRQEerKRELERIR---QEEIA-----MEISRMRELERLQMERQQK---NERVR--QELEAARKVKI- 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 294 dLESERTQRATERWLQSQTLSMTSAESQTSEMDFLEPD--PEMQLLRQQLRDAEEQMHGMKNKCQEL---CCELEELQHH 368
Cdd:pfam17380 407 -LEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEEraREMERVRLEEQERQQQVERLRQQEEERkrkKLELEKEKRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 369 RQVSEEEQRR-LQRELKCAQNEVLRFQTSHSVTQNE-ELKSRLCTLQKKYDTSQDEQNELLKMQ--LQLQTELRQLKVMK 444
Cdd:pfam17380 486 RKRAEEQRRKiLEKELEERKQAMIEEERKRKLLEKEmEERQKAIYEEERRREAEEERRKQQEMEerRRIQEQMRKATEER 565
|
330
....*....|...
gi 1390157443 445 STLVENQSEKELL 457
Cdd:pfam17380 566 SRLEAMEREREMM 578
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
105-246 |
2.42e-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: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 105 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDerlASAQQAEVFT-KQIQQLQGELRSLREEISLLEheke 183
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK---YEEQLGNVRNnKEYEALQKEIESLKRRISDLE---- 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390157443 184 SELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEI 246
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
99-283 |
2.45e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.40 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 99 RGLSLtETELEELRAQVLqlvAELEETRELAGQHEDDSLELqgllEDERlasaqqaevftkqIQQLQGELRSLREEISLL 178
Cdd:COG2433 374 RGLSI-EEALEELIEKEL---PEEEPEAEREKEHEERELTE----EEEE-------------IRRLEEQVERLEAEVEEL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 179 E---HEKESELKEIEQELHLAQAEiqslrqaaEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRaemEM 255
Cdd:COG2433 433 EaelEEKDERIERLERELSEARSE--------ERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLK---EL 501
|
170 180
....*....|....*....|....*...
gi 1390157443 256 KSSEPSEELQELRERYHFLNEEYRALQE 283
Cdd:COG2433 502 WKLEHSGELVPVKVVEKFTKEAIRRLEE 529
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
107-403 |
3.43e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 50.45 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASaqqaevftkqiQQLQGELRSLREEISLLEhekeSEL 186
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAY-----------GKLRRELAGLTRRLSAAE----GEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 187 KEIEQELHLAQAEIQSLRQAAEDSATEhESDIASLQEDLcrmQNELEDMERIRGDYEMEIASLRAEM---EMKSSEPSEE 263
Cdd:pfam19220 86 EELVARLAKLEAALREAEAAKEELRIE-LRDKTAQAEAL---ERQLAAETEQNRALEEENKALREEAqaaEKALQRAEGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 264 LQELRERYHFLNEEYRALQ----ESN---SSLTGQLADLESER-TQRATERWLQSQtLSMTSAESQTSEMDFLEPDPEMQ 335
Cdd:pfam19220 162 LATARERLALLEQENRRLQalseEQAaelAELTRRLAELETQLdATRARLRALEGQ-LAAEQAERERAEAQLEEAVEAHR 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390157443 336 LLRQQLRDAEEQMHGMKNKCQELcceLEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNE 403
Cdd:pfam19220 241 AERASLRMKLEALTARAAATEQL---LAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEAD 305
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
139-449 |
1.66e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 139 LQGLLEDERLASAQQAEVFTKQIQQLQGELRslreeisllehEKESELKEIEQELHLAQAEIQSlrQAAEDSATEHESDI 218
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELE-----------EAEAALEEFRQKNGLVDLSEEA--KLLLQQLSELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 219 ASLQEDLCRMQNELEDMERIRGDYEMEIASLRAememkssepSEELQELRERYhflneeyralqesnSSLTGQLADLese 298
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDALPELLQ---------SPVIQQLRAQL--------------AELEAELAEL--- 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 299 rTQRATERwlqsqtlsmtsaesqtsemdflepDPEMQLLRQQLRDAEEQMHgmknkcQELCCELEELQHHRQVSEEEQRR 378
Cdd:COG3206 283 -SARYTPN------------------------HPDVIALRAQIAALRAQLQ------QEAQRILASLEAELEALQAREAS 331
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390157443 379 LQRELKCAQNEVLRFQtshsvtqneELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTElRQLKVMKSTLVE 449
Cdd:COG3206 332 LQAQLAQLEARLAELP---------ELEAELRRLEREVEVARELYESLLQRLEEARLA-EALTVGNVRVID 392
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
138-543 |
2.47e-05 |
|
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: 48.48 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 138 ELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEIS-------------------LLEHEKESE-----LKEIEQEL 193
Cdd:TIGR04523 211 QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISntqtqlnqlkdeqnkikkqLSEKQKELEqnnkkIKELEKQL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 194 HLAQAEIQSLR-QAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSEELQELRERyh 272
Cdd:TIGR04523 291 NQLKSEISDLNnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEK-- 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 273 flNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMK 352
Cdd:TIGR04523 369 --QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 353 NKCQELCCELEELQHHRQVSEE--------------EQRRLQRELKCAQNEVLRFQtshsvTQNEELKSRLCTLQKKYDT 418
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETqlkvlsrsinkikqNLEQKQKELKSKEKELKKLN-----EEKKELEEKVKDLTKKISS 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 419 SQDEQNELLKMQLQLQTELRQLK----VMKSTLVENQSEKELLC---RLQKLHLQHQNVTCEKEKLLERQQQLQEELQCH 491
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEdelnKDDFELKKENLEKEIDEknkEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL 601
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1390157443 492 EAELQHLRDTVASFKESNEKDTETHAQLQEMKQLYQASKDELERQ-KHMYDQL 543
Cdd:TIGR04523 602 IKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEvKQIKETI 654
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
99-261 |
2.94e-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: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 99 RGLSLTETELEELRAQVLQLVAELEETREL----------AGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGEL 168
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEElaellralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 169 RSLREEISLLEHEKESELKEIEQELHLAQAEIQSLRQAAEdsatEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIAS 248
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKA----ERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
170
....*....|...
gi 1390157443 249 LRAEMEMKSSEPS 261
Cdd:COG4942 232 LEAEAAAAAERTP 244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
104-348 |
3.88e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 104 TETELEELRAQVLQLVAELEETRElagqheddslelqglledERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHE-- 181
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKK------------------EEKALLKQLAALERRIAALARRIRALEQELAALEAEla 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 182 -KESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMemkssep 260
Cdd:COG4942 87 eLEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 261 sEELQELRERyhfLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQLLRQQ 340
Cdd:COG4942 160 -AELAALRAE---LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
....*...
gi 1390157443 341 LRDAEEQM 348
Cdd:COG4942 236 AAAAAERT 243
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
101-421 |
5.27e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGL-------------LEDERLASAQQAEVFTKQIQQLQGE 167
Cdd:PRK02224 215 LAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLeaeiedlretiaeTEREREELAEEVRDLRERLEELEEE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 168 LRSLREE----------ISLLEHEKESELKEIEQELHLAQAEIQSLRQAAE---DSATEHESDIASLQEDLCRMQNELED 234
Cdd:PRK02224 295 RDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAEslrEDADDLEERAEELREEAAELESELEE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 235 MERIRGDYEMEIASLRAEMEmkssepseelqELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERwlqsQTLS 314
Cdd:PRK02224 375 AREAVEDRREEIEELEEEIE-----------ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL----RTAR 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 315 MTSAESqtsemdflepdpemqllrQQLRDAeeqmhgmkNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQ 394
Cdd:PRK02224 440 ERVEEA------------------EALLEA--------GKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEE 493
|
330 340 350
....*....|....*....|....*....|
gi 1390157443 395 TSHSVTQNEELK---SRLCTLQKKYDTSQD 421
Cdd:PRK02224 494 VEERLERAEDLVeaeDRIERLEERREDLEE 523
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-528 |
6.50e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 173 EEISLLEHEKESELKEIEQelhlaQAEIQSLRQAAEDSATEHESDIASLQEDlcRMQNELEDMERIRGDYEMEIASLRAE 252
Cdd:COG1196 189 ERLEDILGELERQLEPLER-----QAEKAERYRELKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 253 MEMKSsepsEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERtQRATERwlqSQTLSMTSAESQTsemdflepdp 332
Cdd:COG1196 262 LAELE----AELEELRLELEELELELEEAQAEEYELLAELARLEQDI-ARLEER---RRELEERLEELEE---------- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 333 EMQLLRQQLRDAEEqmhgmknkcqelccELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHS--VTQNEELKSRLC 410
Cdd:COG1196 324 ELAELEEELEELEE--------------ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAeaEEELEELAEELL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 411 TLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELLcrLQKLHLQHQNVTCEKEKLLERQQQLQEELQC 490
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE--EEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
330 340 350
....*....|....*....|....*....|....*...
gi 1390157443 491 HEAELQHLRDTVASFKESNEKDTETHAQLQEMKQLYQA 528
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
101-416 |
7.09e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLE- 179
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQe 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 180 --HEKESELKEIEQELHLAQAE------------------IQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIR 239
Cdd:COG4717 221 elEELEEELEQLENELEAAALEerlkearlllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 240 GDYEMEIASLRAEMEMKSSEPSEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAE 319
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAG 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 320 SQTSEM--DFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCC---------ELEELQHHRQVSEEEQRRLQRELKCAQN 388
Cdd:COG4717 381 VEDEEElrAALEQAEEYQELKEELEELEEQLEELLGELEELLEaldeeeleeELEELEEELEELEEELEELREELAELEA 460
|
330 340 350
....*....|....*....|....*....|..
gi 1390157443 389 EVLRFQTSHSVTQN----EELKSRLCTLQKKY 416
Cdd:COG4717 461 ELEQLEEDGELAELlqelEELKAELRELAEEW 492
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
102-237 |
8.05e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 8.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 102 SLTETELEELRAQVLQLVAELEETR----ELAGQHEDDSLELQGLLEDERLASAQQaevftkQIQQLQGEL--------- 168
Cdd:COG3206 215 KLLLQQLSELESQLAEARAELAEAEarlaALRAQLGSGPDALPELLQSPVIQQLRA------QLAELEAELaelsarytp 288
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390157443 169 -----RSLREEISLLEHEKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDlcrmQNELEDMER 237
Cdd:COG3206 289 nhpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL----EAELRRLER 358
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
107-581 |
1.03e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.37 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLElQGLLEDERLASAQ-QAEVFTKQIQQLQGELRSLREEISLLEHEKESE 185
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQHGAFLDADIE-TAAADQEQLPSWQsELENLEERLKALTGKHQDVTAKYNRRRSKIKEQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 186 LKEIEQELHLAQAEIqslRQAAEDSATEHESDIASLQEDLcRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSEELQ 265
Cdd:pfam12128 388 NNRDIAGIKDKLAKI---REARDRQLAVAEDDLQALESEL-REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELL 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 266 ELRE----RYHFLNEEYRALQESNSSLTGQLA------DLESERTQRATERWLQSQtlsmtSAESQTSEMDFLEPDPEMQ 335
Cdd:pfam12128 464 LQLEnfdeRIERAREEQEAANAEVERLQSELRqarkrrDQASEALRQASRRLEERQ-----SALDELELQLFPQAGTLLH 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 336 LLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQrrlqreLKCAQNEVLRFQTSHSVTQNEELKSRLCTLQKK 415
Cdd:pfam12128 539 FLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELN------LYGVKLDLKRIDVPEWAASEEELRERLDKAEEA 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 416 YDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELlcRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCH-EAE 494
Cdd:pfam12128 613 LQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARL--DLRRLFDEKQSEKDKKNKALAERKDSANERLNSlEAQ 690
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 495 LQHLRDTVASFKESNEKDTETH--AQLQEMKQLYQASKDELERQKH----MYDQLEQDLLLCQLELK-ELKASHPIPEDK 567
Cdd:pfam12128 691 LKQLDKKHQAWLEEQKEQKREArtEKQAYWQVVEGALDAQLALLKAaiaaRRSGAKAELKALETWYKrDLASLGVDPDVI 770
|
490
....*....|....
gi 1390157443 568 GKCANKCDTLLSRL 581
Cdd:pfam12128 771 AKLKREIRTLERKI 784
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
101-534 |
1.13e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 101 LSLTETELEELRAQVLQLVAELEETRElagQHEDDSLELQGLLEDERLASAQQAEV-------------FTKQIQQLQGE 167
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRL---ELEELELELEEAQAEEYELLAELARLeqdiarleerrreLEERLEELEEE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 168 LRSLREEISLLE---HEKESELKEIEQELHLAQAEIQSLRQAAEDSAT-----------------EHESDIASLQEDLCR 227
Cdd:COG1196 325 LAELEEELEELEeelEELEEELEEAEEELEEAEAELAEAEEALLEAEAelaeaeeeleelaeellEALRAAAELAAQLEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 228 MQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSEELQELRERYHFLNEEYRALQESNSSLTG----------QLADLES 297
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAElleeaalleaALAELLE 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 298 ERTQRATERWLQSQTLSMTSAESQTSEMDFLEPDP----------------------------EMQLLRQQLRDAEEQMH 349
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLrglagavavligveaayeaaleaalaaaLQNIVVEDDEVAAAAIE 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 350 GMK------------NKCQELccELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVT-----QNEELKSRLCTL 412
Cdd:COG1196 565 YLKaakagratflplDKIRAR--AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRtlvaaRLEAALRRAVTL 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 413 QKKYDTSQDE----------------QNELLKMQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCEKEK 476
Cdd:COG1196 643 AGRLREVTLEgeggsaggsltggsrrELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELE 722
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1390157443 477 LLERQQQLQEELQCHEAELQHLRDTVASFKESNEKDTETHAQLQEMKQLYQASKDELE 534
Cdd:COG1196 723 EEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
101-252 |
2.15e-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: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 101 LSLTETELEELRAQVLQLVAELEETRELAGQH-------EDDSLELQGLLEDERLASA-QQAEVFTKQIQQLQGELRSLR 172
Cdd:COG3883 60 LEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsGGSVSYLDVLLGSESFSDFlDRLSALSKIADADADLLEELK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 173 EEISLLEhEKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAE 252
Cdd:COG3883 140 ADKAELE-AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
99-480 |
2.93e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 99 RGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLAsaQQAEVFTKQIQQLQGELRSLREEISLL 178
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY--QELEALEAELAELPERLEELEERLEEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 179 EhEKESELKEIEQELHLAQAEIQslrQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEmkSS 258
Cdd:COG4717 159 R-ELEEELEELEAELAELQEELE---ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE--QL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 259 EPSEELQELRERYHFLNEEYRALQESnSSLTGQLADLESERTQRATERWLQSQ------TLSMTSAESQTSEMDFLEPDP 332
Cdd:COG4717 233 ENELEAAALEERLKEARLLLLIAAAL-LALLGLGGSLLSLILTIAGVLFLVLGllallfLLLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 333 EMQLLRQQLRDAEEQMHGMKNKCQ-----ELCCELEELQhhRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNEELKS 407
Cdd:COG4717 312 ALEELEEEELEELLAALGLPPDLSpeellELLDRIEELQ--ELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRA 389
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390157443 408 RLctlqKKYDTSQDEQNELLKMQLQLQTELRQLKvmksTLVENQSEKELLCRLQKLHLQHQNVTCEKEKLLER 480
Cdd:COG4717 390 AL----EQAEEYQELKEELEELEEQLEELLGELE----ELLEALDEEELEEELEELEEELEELEEELEELREE 454
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
184-440 |
3.36e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 184 SELKEIEQELHLAQAEIQSLRQAAEDSatehESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAememkssepseE 263
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAALERRIAALARRIRALEQELAALEA-----------E 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 264 LQELRERYHFLNEEYRALQEsnsSLTGQLADLESERTQRATERWLQSQtlsmtsaesqtsemDFLEPDPEMQLLRQQLRD 343
Cdd:COG4942 85 LAELEKEIAELRAELEAQKE---ELAELLRALYRLGRQPPLALLLSPE--------------DFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 344 AEEQMHGMKNkcqelccELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQtshsvTQNEELKSRLCTLQKKYDTSQDEQ 423
Cdd:COG4942 148 RREQAEELRA-------DLAELAALRAELEAERAELEALLAELEEERAALE-----ALKAERQKLLARLEKELAELAAEL 215
|
250
....*....|....*..
gi 1390157443 424 NELLKMQLQLQTELRQL 440
Cdd:COG4942 216 AELQQEAEELEALIARL 232
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
107-258 |
5.08e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 43.21 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKESEL 186
Cdd:pfam09787 62 EIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRI 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390157443 187 KEIEQELHLAQAEIQSlRQAAEDSATEHESDIASLQEDLCRMQNELEDM--ERIRGDYEMEiaslRAEMEMKSS 258
Cdd:pfam09787 142 KDREAEIEKLRNQLTS-KSQSSSSQSELENRLHQLTETLIQKQTMLEALstEKNSLVLQLE----RMEQQIKEL 210
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
96-440 |
6.22e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 96 NKHRGLSLTETELE-ELRAQVLQLVAE---LEETRELAGQHEDDSLELQGLLE--DERLASAQQAEVFTKQIQQLQGELR 169
Cdd:PRK04863 279 NERRVHLEEALELRrELYTSRRQLAAEqyrLVEMARELAELNEAESDLEQDYQaaSDHLNLVQTALRQQEKIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 170 SLR---EEISLLEHEKESELKEIEQELHLAQAEIQSL---------------------RQA------------------- 206
Cdd:PRK04863 359 ELEerlEEQNEVVEEADEQQEENEARAEAAEEEVDELksqladyqqaldvqqtraiqyQQAvqalerakqlcglpdltad 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 207 -AEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEM-EMKSSEPSEELQELRERYhflnEEYRALQES 284
Cdd:PRK04863 439 nAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAgEVSRSEAWDVARELLRRL----REQRHLAEQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 285 NSSLTGQLADLESE-RTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQL--LRQQLRDAEEQMHGMKNKCQELCCE 361
Cdd:PRK04863 515 LQQLRMRLSELEQRlRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLesLSESVSEARERRMALRQQLEQLQAR 594
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390157443 362 LEELQHHRQVSEEEQRRLQRelkcaqnevLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQL 440
Cdd:PRK04863 595 IQRLAARAPAWLAAQDALAR---------LREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERL 664
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
105-300 |
6.50e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.82 E-value: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 105 ETELEELRaqvlqlvaeleetrelagqheddslelqgllederlasaQQAEVFTKQIQQLQGELRSLREEISLLEHEKES 184
Cdd:pfam09787 46 TLELEELR---------------------------------------QERDLLREEIQKLRGQIQQLRTELQELEAQQQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 185 ELKEIEQELHLAQAEIQSLRQAAEdsatEHESDIASLQEDLCRMQNELED-----MERIRgDYEMEIASLRAEMeMKSSE 259
Cdd:pfam09787 87 EAESSREQLQELEEQLATERSARR----EAEAELERLQEELRYLEEELRRskatlQSRIK-DREAEIEKLRNQL-TSKSQ 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1390157443 260 PSEELQELRERYHFLNEEY-------RALQESNSSLTGQLADLESERT 300
Cdd:pfam09787 161 SSSSQSELENRLHQLTETLiqkqtmlEALSTEKNSLVLQLERMEQQIK 208
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
162-439 |
9.72e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 9.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 162 QQLQGELRSLREeISLLEHEKESELKEIEQELHL------AQAEIQSLRQAAEDSATEhesdIASLQEDLCRMQNELEDM 235
Cdd:PRK11281 39 ADVQAQLDALNK-QKLLEAEDKLVQQDLEQTLALldkidrQKEETEQLKQQLAQAPAK----LRQAQAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 236 ERIRgdyeMEIASLRaEMEMKSSEPSEELQELREryhflneeyrALQESNSSLTGQlaDLESERTQRA-TERWLQSQTLS 314
Cdd:PRK11281 114 TRET----LSTLSLR-QLESRLAQTLDQLQNAQN----------DLAEYNSQLVSL--QTQPERAQAAlYANSQRLQQIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 315 MTSAESQTSEMDfLEPDpemqllRQQLRDAEEQMHGMKNKCQELccELEE-------LQHHRQVSEEEQRRLQRELKCAQ 387
Cdd:PRK11281 177 NLLKGGKVGGKA-LRPS------QRVLLQAEQALLNAQNDLQRK--SLEGntqlqdlLQKQRDYLTARIQRLEHQLQLLQ 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1390157443 388 ---NEVLRFQTSHSVTQNEELKsrlctlqkkyDTSQDEQNELLKMQLQLQTELRQ 439
Cdd:PRK11281 248 eaiNSKRLTLSEKTVQEAQSQD----------EAARIQANPLVAQELEINLQLSQ 292
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
90-306 |
1.08e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 90 VGSLSVNKHRGLSLTETELEELRAQVLQLVAELEETRELAGQHE---DDSLELQGLLEDERLASAQQAEVFTKqIQQLQG 166
Cdd:PRK02224 521 LEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEeeaEEAREEVAELNSKLAELKERIESLER-IRTLLA 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 167 ELRSLREEISLLEhEKESELKEIEQElhlAQAEIQSLRQAAEDSATEHESD-IASLQEDLCRMQNELEDMERIRGDYEME 245
Cdd:PRK02224 600 AIADAEDEIERLR-EKREALAELNDE---RRERLAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREE 675
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390157443 246 IASLRAEMEMKSSEpSEELQELRERYHFLNEEYRALQ---ESNSSLTGQLADLESERTQRATER 306
Cdd:PRK02224 676 RDDLQAEIGAVENE-LEELEELRERREALENRVEALEalyDEAEELESMYGDLRAELRQRNVET 738
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
105-608 |
1.09e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.18 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 105 ETELEELRAQVLQLVAELE----ETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEH 180
Cdd:pfam15921 259 ELLLQQHQDRIEQLISEHEveitGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 181 EKESELKEIEQELHLAQAEIQSLRQAAEDSATEH---ESDIASLQEDLCRMQNEL---------------------EDME 236
Cdd:pfam15921 339 MYEDKIEELEKQLVLANSELTEARTERDQFSQESgnlDDQLQKLLADLHKREKELslekeqnkrlwdrdtgnsitiDHLR 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 237 RIRGDYEMEIASLRAEMEMKSSEPSEELQELRERYHFLNEEYralqESNSSLTGQLADLE-------SERTQRATERWLQ 309
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESL----EKVSSLTAQLESTKemlrkvvEELTAKKMTLESS 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 310 SQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNkcqelccELEELQHHRqvSEEEQRRLQRELKCAQNE 389
Cdd:pfam15921 495 ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKN-------EGDHLRNVQ--TECEALKLQMAEKDKVIE 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 390 VLRFQTshsvtqnEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTlvENQSEKELLCRLQKLHLQHQN 469
Cdd:pfam15921 566 ILRQQI-------ENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDK--KDAKIRELEARVSDLELEKVK 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 470 VTCEKEKLLERQQQLQEELQCHEAELQHLRDTVASFKESNE--------KDTETHAQLQEMKQLYQASKDELERQKHMYD 541
Cdd:pfam15921 637 LVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEvlkrnfrnKSEEMETTTNKLKMQLKSAQSELEQTRNTLK 716
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390157443 542 QLEQDlllcqlELKELKASHPIPEDKGKCANKCDTLLSRLTELQEKYKASQKEMGQLQMEQCELLED 608
Cdd:pfam15921 717 SMEGS------DGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQE 777
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
82-780 |
1.12e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.04 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 82 EQVQKggsvgslsvNKHRGLSLTETELEELRAQVLQLVaeleetrelaGQHEDDSLELQGLLEDERLASAQQAEVfTKQI 161
Cdd:pfam02463 278 EKEKK---------LQEEELKLLAKEEEELKSELLKLE----------RRKVDDEEKLKESEKEKKKAEKELKKE-KEEI 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 162 QQLQGELRSLREEISLLEHEKESELKEIEQELHLAQAEIQSLRQAAEDSATEhESDIASLQEDLCRMQNELEDMERIRGD 241
Cdd:pfam02463 338 EELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA-AKLKEEELELKSEEEKEAQLLLELARQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 242 YEMEIASLRAEMEMKSSEPSEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAESQ 321
Cdd:pfam02463 417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 322 TSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQ--HHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSV 399
Cdd:pfam02463 497 ERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYkvAISTAVIVEVSATADEVEERQKLVRALTELPLG 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 400 TQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCEKEKLLE 479
Cdd:pfam02463 577 ARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEE 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 480 RQQQLQEELQCHEAELQHLRDTVASfKESNEKDTETHAQLQEMKQLYQASKDELERQKHMYDQLEQDLLLCQLELKELKA 559
Cdd:pfam02463 657 GLAEKSEVKASLSELTKELLEIQEL-QEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKIN 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 560 SHPIPEDKGKCANKCDTLLSRL-----------TELQEKYKASQKEMGQLQMEQCELLEDQRRMqEEQGQLQEELHRLTL 628
Cdd:pfam02463 736 EELKLLKQKIDEEEEEEEKSRLkkeekeeekseLSLKEKELAEEREKTEKLKVEEEKEEKLKAQ-EEELRALEEELKEEA 814
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 629 PLPKSGLLLKSQELLTKLEDLCELQLLYQGMQEEQKKLIQNQDCVLKEQLEIHEELRRFKESHFQEVLENPDD--SKLAK 706
Cdd:pfam02463 815 ELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDEleSKEEK 894
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390157443 707 SSKCNRNKQSKLLMEQMQALQVMYDAGQAKQELLQQEQGRLLEERKRLQADLQLCLEEMQLLQVQSPSIKMSLE 780
Cdd:pfam02463 895 EKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLA 968
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
99-268 |
1.28e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 99 RGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQgllederlASAQQAEVFTKQIQQLQGELRSLREEISLL 178
Cdd:PRK09039 46 REISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLR--------ASLSAAEAERSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 179 EHEKESELKEIEQELHLAQAEIQSLRQaaedsatehesDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSS 258
Cdd:PRK09039 118 AGELAQELDSEKQVSARALAQVELLNQ-----------QIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALA 186
|
170
....*....|
gi 1390157443 259 EPSEELQELR 268
Cdd:PRK09039 187 QRVQELNRYR 196
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
96-594 |
1.33e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 96 NKHRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGlLEDERLASAQQAEVFTKQIQQLQGELRSLREEI 175
Cdd:PRK03918 197 EKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE-LEKELESLEGSKRKLEEKIRELEERIEELKKEI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 176 SLLEhEKESELKEIEqELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMErirgdyemeiaslraEMEM 255
Cdd:PRK03918 276 EELE-EKVKELKELK-EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE---------------EKEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 256 KSSEPSEELQELRERYHFLNEEYRALQESNsSLTGQLADLESERTQRATERWLQS-QTLSMTSAESQTSEMDFLEPDPEM 334
Cdd:PRK03918 339 RLEELKKKLKELEKRLEELEERHELYEEAK-AKKEELERLKKRLTGLTPEKLEKElEELEKAKEEIEEEISKITARIGEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 335 QLLRQQLRDAEEQMHGMKNKC----------------QELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLR----FQ 394
Cdd:PRK03918 418 KKEIKELKKAIEELKKAKGKCpvcgrelteehrkellEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeselIK 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 395 TSHSVTQNEELKSRLCTLQ--------KKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSE-KELLCRLQKLH- 464
Cdd:PRK03918 498 LKELAEQLKELEEKLKKYNleelekkaEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKlDELEEELAELLk 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 465 -LQHQNVTCEKE------------KLLERQQQLQEELQCHEAELQHLRDTV-ASFKESNEKDT---ETHAQLQEMKQLYq 527
Cdd:PRK03918 578 eLEELGFESVEEleerlkelepfyNEYLELKDAEKELEREEKELKKLEEELdKAFEELAETEKrleELRKELEELEKKY- 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 528 aSKDELERQKHMYDQLEQDL--LLCQLE------------LKELKASHPIPEDKGKCANKCDTLLSRLTELQEK---YKA 590
Cdd:PRK03918 657 -SEEEYEELREEYLELSRELagLRAELEelekrreeikktLEKLKEELEEREKAKKELEKLEKALERVEELREKvkkYKA 735
|
....
gi 1390157443 591 SQKE 594
Cdd:PRK03918 736 LLKE 739
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
159-306 |
1.43e-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: 41.45 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 159 KQIQQLQGELRSLREEISLLEHEK---ESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASL-----QEDLCRMQN 230
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELaalEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnNKEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390157443 231 ELEDMERIRGDYEMEIASLRAEMEMKssepSEELQELRERYHFLNEEYRALQEsnsSLTGQLADLESERTQRATER 306
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEEL----EEELAELEAELAELEAELEEKKA---ELDEELAELEAELEELEAER 165
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
109-306 |
1.69e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 109 EELRAQV--LQLVAELEETRELAGQHEDDSLELQGLLEDERlasaQQAEVFTKQIQQLQGELRSLREEISLLEHEKESEL 186
Cdd:PRK11281 39 ADVQAQLdaLNKQKLLEAEDKLVQQDLEQTLALLDKIDRQK----EETEQLKQQLAQAPAKLRQAQAELEALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 187 KEIEQELHLAQ-----AEIQSLRQAAEDSATEHESDIASLQEDLCRMQNEL-EDMERIrgdyeMEIASLRAEMEMKSSEP 260
Cdd:PRK11281 115 RETLSTLSLRQlesrlAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALyANSQRL-----QQIRNLLKGGKVGGKAL 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1390157443 261 SEELQELreryhfLNEEYRALQESNS----SLTG--QLADLESERTQRATER 306
Cdd:PRK11281 190 RPSQRVL------LQAEQALLNAQNDlqrkSLEGntQLQDLLQKQRDYLTAR 235
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
497-780 |
1.78e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.20 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 497 HLRDTVASFKESNEKDTEthaQLQEMKQLYQASKDELERQKHMYDQLEQD-LLLCQLELKELKASHPIPEDKGKCANKCD 575
Cdd:PLN02939 97 HNRASMQRDEAIAAIDNE---QQTNSKDGEQLSDFQLEDLVGMIQNAEKNiLLLNQARLQALEDLEKILTEKEALQGKIN 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 576 TLLSRLTELQEKYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPksglLLKSQELLTKLEdlcelqll 655
Cdd:PLN02939 174 ILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELD----VLKEENMLLKDD-------- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 656 yqgMQEEQKKLIQNQDCvlKEQLEIHEELRRFKESHFQEVlenpdDSKLAkSSKCNRNKQSKL----LMEQMQALQVMYD 731
Cdd:PLN02939 242 ---IQFLKAELIEVAET--EERVFKLEKERSLLDASLREL-----ESKFI-VAQEDVSKLSPLqydcWWEKVENLQDLLD 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1390157443 732 --AGQAKQELLQQEQGRLLEER-KRLQADL------QLCLEEMQLLQVQSPSIKMSLE 780
Cdd:PLN02939 311 raTNQVEKAALVLDQNQDLRDKvDKLEASLkeanvsKFSSYKVELLQQKLKLLEERLQ 368
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
209-447 |
2.98e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 209 DSATEHESDIASLQEDLCRMQNELEDMERIRGDYEmEIASLRAEMEmkssepseELQELRE--RYHFLNEEYRALQESNS 286
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEPIRELAE-RYAAARERLA--------ELEYLRAalRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 287 SLTGQLADLESERTQRATERWLQSQTLSMTSAESQTSEMDFLEPdpemqlLRQQLRDAEEQMHGMKNKCQELCCELEELQ 366
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ------LEREIERLERELEERERRRARLEALLAALG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 367 HHRQVSEEEQRRLQRELKCAQnevlrfqtshsvtqnEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKST 446
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALL---------------EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSN 437
|
.
gi 1390157443 447 L 447
Cdd:COG4913 438 I 438
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
104-607 |
3.44e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 104 TETELEELRAQVLQLvaeleETRELAGQHEDDSLELQGLLEDERLASAQQaevFTKQIQQLQGELRSLREEISLLEHEKE 183
Cdd:PRK04863 584 LRQQLEQLQARIQRL-----AARAPAWLAAQDALARLREQSGEEFEDSQD---VTEYMQQLLERERELTVERDELAARKQ 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 184 SELKEIEQELHLAQAEIQSLRQAAED----SATEHESDIaSLQE------------------DLCRMQNEL-------ED 234
Cdd:PRK04863 656 ALDEEIERLSQPGGSEDPRLNALAERfggvLLSEIYDDV-SLEDapyfsalygparhaivvpDLSDAAEQLagledcpED 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 235 MERIRGDY-----------EMEIASL--------------------RAEMEMKSSEPSEELQELRERYHFLNEEYRALQE 283
Cdd:PRK04863 735 LYLIEGDPdsfddsvfsveELEKAVVvkiadrqwrysrfpevplfgRAAREKRIEQLRAEREELAERYATLSFDVQKLQR 814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 284 SNSSLTGQLA-------DLESERTQRATERWLQSQTLSMTSAESQTsemdflepdpemQLLRQQLRDAEEQMHGMkNKCQ 356
Cdd:PRK04863 815 LHQAFSRFIGshlavafEADPEAELRQLNRRRVELERALADHESQE------------QQQRSQLEQAKEGLSAL-NRLL 881
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 357 ---------ELCCELEELQHHRQVSEEEQRRLQRElkcaQNEVLRFQTSHSVTQNEElkSRLCTLQKKYDTSQDEQnELL 427
Cdd:PRK04863 882 prlnlladeTLADRVEEIREQLDEAEEAKRFVQQH----GNALAQLEPIVSVLQSDP--EQFEQLKQDYQQAQQTQ-RDA 954
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 428 KMQLQLQTELRQLKVMKS------TLVENQSEKELLcrLQKLHLQHQNVTCEKEKLLErqqqlqeelqcHEAELQHLRDT 501
Cdd:PRK04863 955 KQQAFALTEVVQRRAHFSyedaaeMLAKNSDLNEKL--RQRLEQAEQERTRAREQLRQ-----------AQAQLAQYNQV 1021
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 502 VASFKESNEKDTETHAQL-QEMKQL-YQASKDELERQKHMYDQLEQDLLLCQLELKELKAshpipeDKGKCANKCDTLLS 579
Cdd:PRK04863 1022 LASLKSSYDAKRQMLQELkQELQDLgVPADSGAEERARARRDELHARLSANRSRRNQLEK------QLTFCEAEMDNLTK 1095
|
570 580
....*....|....*....|....*...
gi 1390157443 580 RLTELQEKYKASQKEMGQLQMEQCELLE 607
Cdd:PRK04863 1096 KLRKLERDYHEMREQVVNAKAGWCAVLR 1123
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
106-224 |
3.77e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 106 TELEELRAQVLQLVAELEEtrelagqheddslelqgLLEDERLASAQQAEVFTKQIQQLQGELRSLREEislLEHEKE-- 183
Cdd:COG0542 411 EELDELERRLEQLEIEKEA-----------------LKKEQDEASFERLAELRDELAELEEELEALKAR---WEAEKEli 470
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1390157443 184 SELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQED 224
Cdd:COG0542 471 EEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
196-394 |
3.89e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 196 AQAEIQslRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSEELQELRERYHFLN 275
Cdd:COG3883 12 AFADPQ--IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 276 EEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSmtsaESQTSEMDFLEPDpeMQLLRQQLRDAEEQMHGMKNKC 355
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIA----DADADLLEELKAD--KAELEAKKAELEAKLAELEALK 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 1390157443 356 QELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQ 394
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
112-783 |
5.94e-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: 40.72 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 112 RAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASA-------QQAEVFTKQIQQLQGELRSLREEislLEHEKES 184
Cdd:TIGR00618 165 KKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQlltlctpCMPDTYHERKQVLEKELKHLREA---LQQTQQS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 185 ELKeIEQELHLAQAEIQSLRQAAEDSATEHEsdiASLQEDLCRMQNELEDMERIRGDYEMEIASLrAEMEMKSSEPSEEL 264
Cdd:TIGR00618 242 HAY-LTQKREAQEEQLKKQQLLKQLRARIEE---LRAQEAVLEETQERINRARKAAPLAAHIKAV-TQIEQQAQRIHTEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 265 QELRERYHFLNEEYRALQESNSSLTGQladlesertQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEmqlLRQQLRDA 344
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHVKQQSSIEEQ---------RRLLQTLHSQEIHIRDAHEVATSIREISCQQHT---LTQHIHTL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 345 EEQMHGMKNKCQELCCELE---ELQHHRQVSEEEQRRLQRELKCAQNEVlrfqtshsVTQNEELKSRLCTLQKKYDTSQD 421
Cdd:TIGR00618 385 QQQKTTLTQKLQSLCKELDilqREQATIDTRTSAFRDLQGQLAHAKKQQ--------ELQQRYAELCAAAITCTAQCEKL 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 422 EQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCHEAELQHLRDT 501
Cdd:TIGR00618 457 EKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQT 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 502 VASFKESNEKdteTHAQLQEMKQLYQASKDELERQkhmyDQLEQDLLLCQLELKELKASHPIPEDkgkcankcdtLLSRL 581
Cdd:TIGR00618 537 YAQLETSEED---VYHQLTSERKQRASLKEQMQEI----QQSFSILTQCDNRSKEDIPNLQNITV----------RLQDL 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 582 TELQEKYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPKSGLLLKSQELLTKLEDLCELQLLYQGMQE 661
Cdd:TIGR00618 600 TEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQ 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 662 EQKKLIQNqdcvLKEQLEIHEELRRFKESHFQEVLEnpddsKLAKSSKcNRNKQSKLLMEQMQALQVMYDAGQAKQELLQ 741
Cdd:TIGR00618 680 LALQKMQS----EKEQLTYWKEMLAQCQTLLRELET-----HIEEYDR-EFNEIENASSSLGSDLAAREDALNQSLKELM 749
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1390157443 742 QEQGRLLEER--------KRLQADLQLCLEEMQLLQVQSPSIKMSLESYG 783
Cdd:TIGR00618 750 HQARTVLKARteahfnnnEEVTAALQTGAELSHLAAEIQFFNRLREEDTH 799
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
182-358 |
6.86e-03 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 40.22 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 182 KESELKEIEQELHLAQAEIQSLRQaaedsaTEHE--SDIASLQEDLCRMQNELEdmeRIRGDYEMEIASLRAEMEMKSSE 259
Cdd:pfam09726 393 KPDALVRLEQDIKKLKAELQASRQ------TEQElrSQISSLTSLERSLKSELG---QLRQENDLLQTKLHNAVSAKQKD 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 260 pSEELQELRERyhfLNEEyralQESNSSLTGQLAD------LESERTQRATErwlQSQTLSMTSAESQTSEMDFLEPdpE 333
Cdd:pfam09726 464 -KQTVQQLEKR---LKAE----QEARASAEKQLAEekkrkkEEEATAARAVA---LAAASRGECTESLKQRKRELES--E 530
|
170 180
....*....|....*....|....*
gi 1390157443 334 MQLLRQQLRDAEEQMHGMKNKCQEL 358
Cdd:pfam09726 531 IKKLTHDIKLKEEQIRELEIKVQEL 555
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
138-771 |
7.20e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.34 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 138 ELQGLLEDERLASAqqAEVFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESD 217
Cdd:pfam02463 161 EAAGSRLKRKKKEA--LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 218 IASLQEDLcRMQNELEDMERIRGDYEMEIA----SLRAEMEMKSSEPSEELQELRERYHFLNEEYRALQESNSSLTGQLA 293
Cdd:pfam02463 239 IDLLQELL-RDEQEEIESSKQEIEKEEEKLaqvlKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 294 DLESERTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELE------ELQH 367
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSsaaklkEEEL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 368 HRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTL 447
Cdd:pfam02463 398 ELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKET 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 448 VENQSEKELLCRLQKLHLQHQNV-------TCEKEKLLERQQQLQEELQCHE-AELQHLRDTVASFKESNEKDTETHAQL 519
Cdd:pfam02463 478 QLVKLQEQLELLLSRQKLEERSQkeskarsGLKVLLALIKDGVGGRIISAHGrLGDLGVAVENYKVAISTAVIVEVSATA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 520 QEMKQlYQASKDELERQKHMYDQLEQDLLLCQLELKELKASHPIPEDKGKCANKCDTL--LSRLTELQEKYKASQKEMGQ 597
Cdd:pfam02463 558 DEVEE-RQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEadEDDKRAKVVEGILKDTELTK 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 598 LQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPKSGLLLKSQELLTKLEDLCELQLLYQGMQE---EQKKLIQNQDCVL 674
Cdd:pfam02463 637 LKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEikkKEQREKEELKKLK 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 675 KEQLEIHEELRRFKESHFQEVLENPDDSKLAKSSKCNRNKQSKLLMEQMQALQVMYDAGQAKQELLQQEQGRLLEERKRL 754
Cdd:pfam02463 717 LEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKL 796
|
650
....*....|....*..
gi 1390157443 755 QADLQLCLEEMQLLQVQ 771
Cdd:pfam02463 797 KAQEEELRALEEELKEE 813
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
162-259 |
7.68e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.32 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 162 QQLQGELRSLREEISLLEHEKESELKEIEQElhlaqaeiQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGD 241
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQ--------QQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQ 216
|
90
....*....|....*...
gi 1390157443 242 YEMEIASlRAEMEMKSSE 259
Cdd:PRK11448 217 KRKEITD-QAAKRLELSE 233
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
110-684 |
8.19e-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: 40.34 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 110 ELRAQVLQLVAELEETRELAGQHEDDSLELQGLlEDERLASAQQAEVFTKQIQQLQGELRSLR-----EEISLLEHEKES 184
Cdd:TIGR00618 287 NRARKAAPLAAHIKAVTQIEQQAQRIHTELQSK-MRSRAKLLMKRAAHVKQQSSIEEQRRLLQtlhsqEIHIRDAHEVAT 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 185 ELKEIEQELHLAQAEIQSLRQAAEdSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSEEL 264
Cdd:TIGR00618 366 SIREISCQQHTLTQHIHTLQQQKT-TLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 265 QELRERYHFLNEEYRALQESNSSL---TGQLADLESERTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQLLR--- 338
Cdd:TIGR00618 445 AAITCTAQCEKLEKIHLQESAQSLkerEQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDnpg 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 339 ------QQLRDAEEQMHGMKNKCQELCceLEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNEELKSRLCTL 412
Cdd:TIGR00618 525 pltrrmQRGEQTYAQLETSEEDVYHQL--TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 413 QKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCHE 492
Cdd:TIGR00618 603 LSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLAL 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 493 AELQHLRDTVASFKES-NEKDTETHAQLQEMKQLYQASKDELERQKHMYDQLEQDLLLCQLELKELKASHP-----IPED 566
Cdd:TIGR00618 683 QKMQSEKEQLTYWKEMlAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARtvlkaRTEA 762
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 567 KGKCANKCDTLLSRLTELQEkykasQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPKSGLLLKSQELLTKL 646
Cdd:TIGR00618 763 HFNNNEEVTAALQTGAELSH-----LAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRL 837
|
570 580 590
....*....|....*....|....*....|....*...
gi 1390157443 647 EDLCELQLLYQGMQEEQKKLIQNQDCVLKEQLEIHEEL 684
Cdd:TIGR00618 838 EEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
138-388 |
8.20e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.52 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 138 ELQGLleDERLASaqqaevFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQelhLAQAEIQSLRQAAEDSATEH--- 214
Cdd:pfam00038 5 QLQEL--NDRLAS------YIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYS---LYEKEIEDLRRQLDTLTVERarl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 215 ESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEME---MKSSEPSEELQELRERYHFL----NEEYRALQESNSS 287
Cdd:pfam00038 74 QLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDeatLARVDLEAKIESLKEELAFLkknhEEEVRELQAQVSD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 288 --------------LTGQLADLE------SERTQRATERWLQSQTLSMTSAESQTSEMdflepdpemqllrqqLRDAEEQ 347
Cdd:pfam00038 154 tqvnvemdaarkldLTSALAEIRaqyeeiAAKNREEAEEWYQSKLEELQQAAARNGDA---------------LRSAKEE 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1390157443 348 MHGMKNKCQELCCELEELQH-----HRQVSEEEQrRLQRELKCAQN 388
Cdd:pfam00038 219 ITELRRTIQSLEIELQSLKKqkaslERQLAETEE-RYELQLADYQE 263
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
262-409 |
8.25e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390157443 262 EELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAESQTSEMDflEPDPEMQLLRQQL 341
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLD--ASSDDLAALEEQL 694
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390157443 342 RDAEEQMhgmknkcQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNEELKSRL 409
Cdd:COG4913 695 EELEAEL-------EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF 755
|
|
| |
