|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
34-355 |
1.76e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.01 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 34 VQKGGSVGSLSVNKHRGLSLTETELEELRAQVLQLVAELEETR----ELAGQHEDDSLELQGLLEDERLASAQ------Q 103
Cdd:TIGR02168 655 VRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEkalaELRKELEELEEELEQLRKELEELSRQisalrkD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 104 AEVFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQ---ELHLAQAEIQSLRQAAEDSATEH---ESDIASLQEDLCR 177
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeELAEAEAEIEELEAQIEQLKEELkalREALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 178 MQNELEDMERIRGDYEMEIASLRAEMEMkssepsgslglsdysgLQEELQELRERYHFLNEEYRALQESNSSLTGQLADL 257
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLED----------------LEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 258 ESERTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELC--------CELEELQH 329
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerlseeysLTLEEAEA 958
|
330 340
....*....|....*....|....*.
gi 1370510769 330 HRQVSEEEQRRLQRELKCAQNEVLRF 355
Cdd:TIGR02168 959 LENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
51-309 |
3.86e-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: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 51 LSLTETELEELRAQVLQLVAELEETRElagQHEDDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELRSLREEISlleh 130
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRL---ELEELELELEEAQAEEYELLAELARL-EQDIARLEERRRELEERLE---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 131 EKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEp 210
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL- 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 211 sgslgLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERwLQSQTLSMTSAESQTSEMDfl 290
Cdd:COG1196 399 -----AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE-AELEEEEEALLELLAELLE-- 470
|
250
....*....|....*....
gi 1370510769 291 epdpEMQLLRQQLRDAEEQ 309
Cdd:COG1196 471 ----EAALLEAALAELLEE 485
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
58-413 |
2.84e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 58 LEELRAQVlqlvAELEETRELAGQH-----EDDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELRSLREEISLLEHEK 132
Cdd:COG1196 195 LGELERQL----EPLERQAEKAERYrelkeELKELEAELLLLKLRELEAELEEL-EAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 133 E---SELKEIEQELHLAQAEIQSLRQAAEdsatEHESDIASLQEdlcRMQNELEDMERIrgdyEMEIASLRAEMEmksse 209
Cdd:COG1196 270 EelrLELEELELELEEAQAEEYELLAELA----RLEQDIARLEE---RRRELEERLEEL----EEELAELEEELE----- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 210 psgslglsdysGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLsmtsAESQTSEMDF 289
Cdd:COG1196 334 -----------ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL----LEALRAAAEL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 290 LEpdpEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNEELKS 369
Cdd:COG1196 399 AA---QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1370510769 370 RLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQ 413
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
57-387 |
3.37e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.70 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 57 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEvftKQIQQLQGELRSLREEISLLE---HEKE 133
Cdd:TIGR02169 188 RLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALE---RQKEAIERQLASLEEELEKLTeeiSELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 134 SELKEIEQELHLAQAEIQSL-----RQAAEDSAtEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEmkss 208
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIG-ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE---- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 209 epsgslglsdysGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLEsERTQRATERWLQSQT-LSMTSAESQTSEM 287
Cdd:TIGR02169 340 ------------ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD-KEFAETRDELKDYREkLEKLKREINELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 288 DFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNE-- 365
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEls 486
|
330 340
....*....|....*....|..
gi 1370510769 366 ELKSRLCTLQKKYDTSQDEQNE 387
Cdd:TIGR02169 487 KLQRELAEAEAQARASEERVRG 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-418 |
1.55e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 110 QIQQLQGELRSLREEISLLE---HEKESELKEIEQELHLAQAEIQSLRQAAEDSATEhesdIASLQEDLCRMQNELEDME 186
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEekiAELEKALAELRKELEELEEELEQLRKELEELSRQ----ISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 187 RIRGDYEMEIASLRAEMEmkssepsgsLGLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQraT 266
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIE---------ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL--L 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 267 ERWLQSQTLSMTSAESQTSEMdflepDPEMQLLRQQLRDAEEQMhgmknkcqelccelEELQHHRQVSEEEQRRLQRELK 346
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAAT-----ERRLEDLEEQIEELSEDI--------------ESLAAEIEELEELIEELESELE 876
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370510769 347 CAQNEVlrfqtshsvtqnEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKEL 418
Cdd:TIGR02168 877 ALLNER------------ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV 936
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-417 |
2.78e-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: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 103 QAEVFTKQIQQLQGELRSLREEISllehEKESELKEIEQELHLAQAEIQSLRqaaeDSATEHESDIASLQEDLCRMQNEL 182
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELK----EAEEELEELTAELQELEEKLEELR----LEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 183 EDMERIRGDYEMEIASLRAEMEMkssepsgslglsdysgLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESErt 262
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEE----------------LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE-- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 263 qraterwlqsqtLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQ 342
Cdd:TIGR02168 360 ------------LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510769 343 RELKCAQNEVLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKE 417
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
51-652 |
4.63e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 51 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQqaevFTKQIQQLQGELRSLREEISLLEH 130
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ----LELQIASLNNEIERLEARLERLED 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 131 EKESELKEIEQ--------ELHLAQAEIQSLRQAAEDSATEHEsdiaSLQEDLCRMQNELEDMERIRGDYEMEIASLRAE 202
Cdd:TIGR02168 415 RRERLQQEIEEllkkleeaELKELQAELEELEEELEELQEELE----RLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 203 MEMkssepsgslglsdysglqeeLQELRERYHFLNEEYRALQESNSSLTG---QLADLES--ERTQRATERWLQS--QTL 275
Cdd:TIGR02168 491 LDS--------------------LERLQENLEGFSEGVKALLKNQSGLSGilgVLSELISvdEGYEAAIEAALGGrlQAV 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 276 SMTSAESQTSEMDFLEPD--------PEMQLLRQQLRDAEEQMHGMKNKCQELCCELEE------------LQHHRQVSE 335
Cdd:TIGR02168 551 VVENLNAAKKAIAFLKQNelgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKfdpklrkalsylLGGVLVVDD 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 336 EEQ-RRLQRELKCAQNEVL---------------RFQTSHSVTQN----EELKSRLCTLQKKYDTSQDEQNELLKMQLQL 395
Cdd:TIGR02168 631 LDNaLELAKKLRPGYRIVTldgdlvrpggvitggSAKTNSSILERrreiEELEEKIEELEEKIAELEKALAELRKELEEL 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 396 QTELRQLKVM------------KSTLVENQSEKELLCRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCHEAELQHLRDT 463
Cdd:TIGR02168 711 EEELEQLRKEleelsrqisalrKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 464 VASFKESNEKDTETHAQLQEMkqlYQASKDELERQKHMYDQLEQDLLLCQLELKELKASHPIPEDKGKCANK-------- 535
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAE---LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAeieeleel 867
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 536 CDTLLSRLTELQEKYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPKSGLLLKS--QELLTKLEDLCE 613
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGleVRIDNLQERLSE 947
|
650 660 670
....*....|....*....|....*....|....*....
gi 1370510769 614 lqlLYQGMQEEqkkLIQNQDCVLKEQLEIHEELRRFKES 652
Cdd:TIGR02168 948 ---EYSLTLEE---AEALENKIEDDEEEARRRLKRLENK 980
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
48-204 |
1.51e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 48 HRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDdslELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISL 127
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALRE---ELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 128 LEH----------EKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIA 197
Cdd:COG4913 364 LEAllaalglplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
....*..
gi 1370510769 198 SLRAEME 204
Cdd:COG4913 444 ALRDALA 450
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
58-311 |
1.68e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 58 LEELRAQVLQLVAELEETRELAGQHEDdsleLQGLLEDERLASAQQAEVFTKQI--QQLQGELRSLREEISLLEhEKESE 135
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEA----ELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLD-ASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 136 LKEIEQELHLAQAEIQSLRQ---AAEDSATEHESDIASLQEDLCRMQNELEDMERI-RGDYEMEIASLRAEMEMKSSEPS 211
Cdd:COG4913 687 LAALEEQLEELEAELEELEEeldELKGEIGRLEKELEQAEEELDELQDRLEAAEDLaRLELRALLEERFAAALGDAVERE 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 212 GSLGLSD-YSGLQEELQELRER-----------YHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTs 279
Cdd:COG4913 767 LRENLEErIDALRARLNRAEEEleramrafnreWPAETADLDADLESLPEYLALLDRLEEDGLPEYEERFKELLNENSI- 845
|
250 260 270
....*....|....*....|....*....|..
gi 1370510769 280 aESQTsemDFLepdpemQLLRQQLRDAEEQMH 311
Cdd:COG4913 846 -EFVA---DLL------SKLRRAIREIKERID 867
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
98-328 |
7.73e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 98 LASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKES---ELKEIEQELHLAQAEIQSLrqaaEDSATEHESDIASLQED 174
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAllkQLAALERRIAALARRIRAL----EQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 175 LCRMQNELEDMERirgdyemEIASLRAEMEMKSSEPSGSLGLSdysglQEELQELRERYHFLNEEYRALQESNSSLTGQL 254
Cdd:COG4942 92 IAELRAELEAQKE-------ELAELLRALYRLGRQPPLALLLS-----PEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370510769 255 ADLESERTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQ 328
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
51-264 |
9.27e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 9.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 51 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDerlaSAQQAEVFTKQIQQLQGELRSLREEISlleh 130
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED----LEEQIEELSEDIESLAAEIEELEELIE---- 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 131 EKESELKEIEQELHLAQAEIQSLRQAAEDSAT---EHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASL------RA 201
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEelrELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLqerlseEY 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 202 EMEMKSSEPSGSLGLSDYSGLQ---------------------EELQELRERYHFLNEEYRALQESNSSLTGQLADLESE 260
Cdd:TIGR02168 950 SLTLEEAEALENKIEDDEEEARrrlkrlenkikelgpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDRE 1029
|
....
gi 1370510769 261 RTQR 264
Cdd:TIGR02168 1030 ARER 1033
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
113-440 |
1.22e-07 |
|
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: 56.23 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 113 QLQGELRSLREEISLLEHEKES---ELKEIEQELHlaqaEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIR 189
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSlqsELRRIENRLD----ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 190 GDYEMEIASLRAEMEMKSSEPSGSLglSDYSGLQEELQEL-----RERYHFLNEEYRALQESNSSLTGQLADLESERTQR 264
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELE--EDLHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 265 ATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRE 344
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 345 LK--CAQNEVLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELL---KMQLQLQTELRQLKVMKS-TLVENQSEKEL 418
Cdd:TIGR02169 905 IEelEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELsleDVQAELQRVEEEIRALEPvNMLAIQEYEEV 984
|
330 340
....*....|....*....|..
gi 1370510769 419 LCRLQKLHLQHQNVTCEKEKLL 440
Cdd:TIGR02169 985 LKRLDELKEKRAKLEEERKAIL 1006
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
55-328 |
2.54e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 55 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLederLASAQQAEVFTKQIQQLQGELRSLREEISLLEH---E 131
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL----YALANEISRLEQQKQILRERLANLERQLEELEAqleE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 132 KESELKEIEQELHLAQAEIQSLRQaaedsatehesDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEM-EMKSSEP 210
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKE-----------ELESLEAELEELEAELEELESRLEELEEQLETLRSKVaQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 211 SgslglsdysgLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATErwlqsqTLSMTSAESQTSEMDFL 290
Cdd:TIGR02168 397 S----------LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE------ELEEELEELQEELERLE 460
|
250 260 270
....*....|....*....|....*....|....*...
gi 1370510769 291 EpdpEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQ 328
Cdd:TIGR02168 461 E---ALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
57-487 |
3.34e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 57 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEhEKESEL 136
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE-EALAEL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 137 KEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLGL 216
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 217 SDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEM 296
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALA 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 297 QLLRQQLRDAEEqmhgmknkcQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNEELKSRlctLQK 376
Cdd:COG1196 594 RGAIGAAVDLVA---------SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA---GGS 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 377 KYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCHEAE 456
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
410 420 430
....*....|....*....|....*....|.
gi 1370510769 457 LQHLRDTVASFKESNEKDTETHAQLQEMKQL 487
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLEELERELERL 772
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
57-283 |
6.36e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 6.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 57 ELEELRAQVLQLVAELEETRELAGQhEDDSLELQGLLEDERLASAQQaevftkQIQQLQGELRSLREEisllEHEKESEL 136
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEE-ELAELEEELEELEEELEELEE------ELEEAEEELEEAEAE----LAEAEEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 137 KEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEpsgslgL 216
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE------E 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510769 217 SDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAESQ 283
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
55-260 |
8.87e-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: 8.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 55 ETELEELRAQVLQLVAELEETRElagQHEDDSLELQGLLEDERLASAQQaevftkQIQQLQGELRSLREEISLLEHEKES 134
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQ---KNGLVDLSEEAKLLLQQLSELES------QLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 135 ELKEIEQELhlAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEmkssepsgsl 214
Cdd:COG3206 252 GPDALPELL--QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLE---------- 319
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1370510769 215 glSDYSGLQEELQELRERYhflnEEYRALQESNSSLTGQLADLESE 260
Cdd:COG3206 320 --AELEALQAREASLQAQL----AQLEARLAELPELEAELRRLERE 359
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
133-350 |
3.21e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 133 ESELKEIEQELHLAQAEIQSLRQ-----AAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKS 207
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 208 SEPSGSLGLSDYSGLQEELQELRERYHFLNEEYRALQEsnssltgQLADLESERTQRATERWLQSQTlsmtsaesqtsem 287
Cdd:COG3206 261 QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRA-------QIAALRAQLQQEAQRILASLEA------------- 320
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510769 288 dflepdpEMQLLRQQLRDAEEQMHGMKNKCQELcceleelqhhrQVSEEEQRRLQRELKCAQN 350
Cdd:COG3206 321 -------ELEALQAREASLQAQLAQLEARLAEL-----------PELEAELRRLEREVEVARE 365
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
60-438 |
3.47e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 60 ELRAQVLQLVAELEE-TRELAG-QHEDDSLE-LQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISllehEKESEL 136
Cdd:TIGR02169 671 SEPAELQRLRERLEGlKRELSSlQSELRRIEnRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE----ELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 137 KEIEQELHLAQAEIQSLrqaaedsatehESDIASLQEDLCRMQNELEDMERirgdyemeiaslraememkssepsgslgl 216
Cdd:TIGR02169 747 SSLEQEIENVKSELKEL-----------EARIEELEEDLHKLEEALNDLEA----------------------------- 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 217 sdysglqeelQELRERYHFLNEEYRALQESNSSLTGQLADLESErtqraterwLQSQTLSMTSAESqtsemdflepdpEM 296
Cdd:TIGR02169 787 ----------RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQK---------LNRLTLEKEYLEK------------EI 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 297 QLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQtshsvTQNEELKSRLCTLQK 376
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE-----AQLRELERKIEELEA 910
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370510769 377 KYDTSQDEQNELlkmQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCEKEK 438
Cdd:TIGR02169 911 QIEKKRKRLSEL---KAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRA 969
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
135-345 |
5.56e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 135 ELKEIEQELHLAQAEIQSLRQAAEDsATEHESDIASLQE-DLCRMQNELEDMERIRGDYEMEIASLRAEMEmkssepsgs 213
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIREL-AERYAAARERLAElEYLRAALRLWFAQRRLELLEAELEELRAELA--------- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 214 lglsdysGLQEELQELRERYHFLNEEYRALQESNSS--------LTGQLADLESERTQRATERWLQSQTLSMTSAESQTS 285
Cdd:COG4913 306 -------RLEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510769 286 EMDFLE-----------PDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQREL 345
Cdd:COG4913 379 AEEFAAlraeaaalleaLEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
55-196 |
6.24e-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: 48.77 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 55 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDerlASAQQAEVFT-KQIQQLQGELRSLREEISLLEheke 133
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK---YEEQLGNVRNnKEYEALQKEIESLKRRISDLE---- 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510769 134 SELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEI 196
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
57-264 |
6.66e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 57 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKESEL 136
Cdd:COG1196 621 TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 137 KEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERI---------RGDYEMEIASLRAEMEmks 207
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAleelpeppdLEELERELERLEREIE--- 777
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510769 208 sepsgSLG----LSDysglqEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQR 264
Cdd:COG1196 778 -----ALGpvnlLAI-----EEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
60-415 |
7.68e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.44 E-value: 7.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 60 ELRAQvlqLVAELEETRELAGQHEDDSLElQGLLEderlASAQQAEVfTKQIQQLQGELRSLREEISLL---EHEKESEL 136
Cdd:PRK10929 83 ELRQQ---LNNERDEPRSVPPNMSTDALE-QEILQ----VSSQLLEK-SRQAQQEQDRAREISDSLSQLpqqQTEARRQL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 137 KEIEQELHLAQAEIQSLRQAAedsatehesdIASLQEDLCRMQ---NELEdMERIRGDYEMEIASLRAEMEMKSSEPsgs 213
Cdd:PRK10929 154 NEIERRLQTLGTPNTPLAQAQ----------LTALQAESAALKalvDELE-LAQLSANNRQELARLRSELAKKRSQQ--- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 214 lglsdysgLQEELQELRERYHFL--NEEYRALqESNSSLTGQLADL-ESERTQRATERWLqSQTLSmtsaeSQTSEMDFL 290
Cdd:PRK10929 220 --------LDAYLQALRNQLNSQrqREAERAL-ESTELLAEQSGDLpKSIVAQFKINREL-SQALN-----QQAQRMDLI 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 291 -----EPDPEMQLLRQQLRDAEEQMH--GMKN-----------------KCQELCCELEELQHHRQVSEEEQRRLQRELK 346
Cdd:PRK10929 285 asqqrQAASQTLQVRQALNTLREQSQwlGVSNalgealraqvarlpempKPQQLDTEMAQLRVQRLRYEDLLNKQPQLRQ 364
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510769 347 CAQNEvlrfqtSHSVTQNEelksrlctlQKKYDTSQDEQNELLKMQLQ----LQTELRQLKVMKSTLVENQSE 415
Cdd:PRK10929 365 IRQAD------GQPLTAEQ---------NRILDAQLRTQRELLNSLLSggdtLILELTKLKVANSQLEDALKE 422
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
49-205 |
8.21e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 50.24 E-value: 8.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 49 RGLSLtETELEELRAQVLqlvAELEETRELAGQHEDDSLELqgllEDERlasaqqaevftkqIQQLQGELRSLREEISLL 128
Cdd:COG2433 374 RGLSI-EEALEELIEKEL---PEEEPEAEREKEHEERELTE----EEEE-------------IRRLEEQVERLEAEVEEL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 129 E---HEKESELKEIEQELHLAQAEiqslrqaaEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEM 205
Cdd:COG2433 433 EaelEEKDERIERLERELSEARSE--------ERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKL 504
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
108-345 |
2.15e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 108 TKQIQQLQGELRSLREEISLLehekESELKEIEQELHLAQAEIQSLRQAAEDSatEHESDIASLQEDLCRMQNELEDMER 187
Cdd:COG4913 609 RAKLAALEAELAELEEELAEA----EERLEALEAELDALQERREALQRLAEYS--WDEIDVASAEREIAELEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 188 irgdyemeiaslraememkssepsgslGLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQrate 267
Cdd:COG4913 683 ---------------------------SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE---- 731
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510769 268 rwLQSQTLSMTSAESQTSEMDFLEpdpemQLLRQQLRDAEEQMHgmknkcqelccelEELQHHRQVSEEEQRRLQREL 345
Cdd:COG4913 732 --LQDRLEAAEDLARLELRALLEE-----RFAAALGDAVERELR-------------ENLEERIDALRARLNRAEEEL 789
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
51-417 |
2.20e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.02 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 51 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLE- 129
Cdd:pfam01576 150 LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQa 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 130 --HEKESELKEIEQELHLAQAEI---QSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEME 204
Cdd:pfam01576 230 qiAELRAQLAKKEEELQAALARLeeeTAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 205 mkssepsgslGLSDYSGLQEELQELRERYhfLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAE--- 281
Cdd:pfam01576 310 ----------DTLDTTAAQQELRSKREQE--VTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANlek 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 282 -SQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVlrfqtSHS 360
Cdd:pfam01576 378 aKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLL-----NEA 452
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510769 361 VTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKE 417
Cdd:pfam01576 453 EGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEE 509
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
58-757 |
2.27e-05 |
|
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: 48.90 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 58 LEELRAQV--LQLVAEL-EETRELAGQHEDDSLELQGL----LEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLE- 129
Cdd:TIGR02168 195 LNELERQLksLERQAEKaERYKELKAELRELELALLVLrleeLREELEELQEELKEAEEELEELTAELQELEEKLEELRl 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 130 --HEKESELKEIEQELHLAQAEIQSLRQAAEdsatEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKS 207
Cdd:TIGR02168 275 evSELEEEIEELQKELYALANEISRLEQQKQ----ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 208 SEpsgslglsdYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAESQTSEM 287
Cdd:TIGR02168 351 EE---------LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 288 DFLEPDPEMQllrqqlrdaEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNEel 367
Cdd:TIGR02168 422 EIEELLKKLE---------EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR-- 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 368 KSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKvmKSTLVENQSEKELLCRLQKlHLQhqNVTCEKEKLLERQQQLQ 447
Cdd:TIGR02168 491 LDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLS--ELISVDEGYEAAIEAALGG-RLQ--AVVVENLNAAKKAIAFL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 448 EELQCHEAELQHLRDTVASFKESNEKDTETH--------AQLQEMKQLYQASKDELERQKHMYDQLEQDLLLcqleLKEL 519
Cdd:TIGR02168 566 KQNELGRVTFLPLDSIKGTEIQGNDREILKNiegflgvaKDLVKFDPKLRKALSYLLGGVLVVDDLDNALEL----AKKL 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 520 KASHPIPEDKGKCANKC-----------DTLLSR---LTELQEKYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEEL 585
Cdd:TIGR02168 642 RPGYRIVTLDGDLVRPGgvitggsaktnSSILERrreIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 586 HRLTLPLPKSGLLLKSQEL-LTKLEDLCELQLLYQGMQEEQKKLIQNQDCVLKEQLEIHEELRRFKESHFQEVLENPDDS 664
Cdd:TIGR02168 722 EELSRQISALRKDLARLEAeVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 665 KLAKSSKCNRNK-------QPRSQAQHAQRPDSELGQEIQELI-QSKLLMEQMQALQVMYDAGQAKQELLQQEQGRLLEE 736
Cdd:TIGR02168 802 REALDELRAELTllneeaaNLRERLESLERRIAATERRLEDLEeQIEELSEDIESLAAEIEELEELIEELESELEALLNE 881
|
730 740
....*....|....*....|.
gi 1370510769 737 RKRLQADLQLCLEEMQLLQVQ 757
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEE 902
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
51-378 |
3.74e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 51 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISlleh 130
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE---- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 131 EKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASL---------RA 201
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLlallflllaRE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 202 EMEMKSSEPSGSLGLSDYSGLQEELQELRERYHFL----NEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSM 277
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEELLAALGLPpdlsPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 278 TSAESQTSEM--DFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCC---------ELEELQHHRQVSEEEQRRLQRELK 346
Cdd:COG4717 377 AEAGVEDEEElrAALEQAEEYQELKEELEELEEQLEELLGELEELLEaldeeeleeELEELEEELEELEEELEELREELA 456
|
330 340 350
....*....|....*....|....*....|....*.
gi 1370510769 347 CAQNEVLRFQTSHSVTQN----EELKSRLCTLQKKY 378
Cdd:COG4717 457 ELEAELEQLEEDGELAELlqelEELKAELRELAEEW 492
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
49-213 |
3.76e-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: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 49 RGLSLTETELEELRAQVLQLVAELEETREL----------AGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGEL 118
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEElaellralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 119 RSLREEISLLEHEKESELKEIEQELHLAQAEIQSLRQAAEdsatEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIAS 198
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKA----ERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
170
....*....|....*
gi 1370510769 199 LRAEMEMKSSEPSGS 213
Cdd:COG4942 232 LEAEAAAAAERTPAA 246
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
51-187 |
6.96e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 51 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSlELQGLLEDERLASAQQAEVFTK------QIQQLQGELRSLREE 124
Cdd:COG3206 228 LAEARAELAEAEARLAALRAQLGSGPDALPELLQSP-VIQQLRAQLAELEAELAELSARytpnhpDVIALRAQIAALRAQ 306
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510769 125 IsllEHEKESELKEIEQELHLAQAEIQSLRQAAEdsatEHESDIASLQEDlcrmQNELEDMER 187
Cdd:COG3206 307 L---QQEAQRILASLEAELEALQAREASLQAQLA----QLEARLAELPEL----EAELRRLER 358
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
54-268 |
8.64e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 54 TETELEELRAQVLQLVAELEETRELAGQHEDdslelqglLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKE 133
Cdd:COG4913 666 AEREIAELEAELERLDASSDDLAALEEQLEE--------LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 134 S--ELKEIEQELHLAQAEIQSLRQAAEDSATEH-ESDIASLQEDLCRMQNELED-MERIRGDYEMEIASLRAEMEmksse 209
Cdd:COG4913 738 AaeDLARLELRALLEERFAAALGDAVERELRENlEERIDALRARLNRAEEELERaMRAFNREWPAETADLDADLE----- 812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370510769 210 psgslglsDYSGLQEELQELRER--YHFLNEEYRALQE-SNSSLTGQLADLESERtQRATER 268
Cdd:COG4913 813 --------SLPEYLALLDRLEEDglPEYEERFKELLNEnSIEFVADLLSKLRRAI-REIKER 865
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
56-201 |
1.01e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 56 TELEELRAQVLQLVAELEETRELAGQHEDDSLE-LQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEIS-------- 126
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLELLEaELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggdrle 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 127 LLEHE---KESELKEIEQE----------LHLA----QAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIR 189
Cdd:COG4913 342 QLEREierLERELEERERRrarleallaaLGLPlpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
170
....*....|..
gi 1370510769 190 GDYEMEIASLRA 201
Cdd:COG4913 422 RELEAEIASLER 433
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
90-403 |
1.09e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.66 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 90 QGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQELHLAQAEiqSLRQAAEDSA----TEHE 165
Cdd:pfam17380 263 QTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAE--KARQAEMDRQaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 166 SDIASLQEDLCRMQNE--LEDMERIRG-DYEMEIASLRA------EMEMKSSEPSGSL-GLSDYSGLQEELQELRERYHF 235
Cdd:pfam17380 341 RMAMERERELERIRQEerKRELERIRQeEIAMEISRMRElerlqmERQQKNERVRQELeAARKVKILEEERQRKIQQQKV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 236 LNEEYRALQESNSSLTGQLADLESERT-----QRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQL--------LRQQ 302
Cdd:pfam17380 421 EMEQIRAEQEEARQREVRRLEEERAREmervrLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRaeeqrrkiLEKE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 303 LRDAEEQMHGMKNKCQELCCELEELQhhRQVSEEEQRRLQRELKCAQNEV-LRFQTSHSVTQNEELKSRLCTLQKKYD-T 380
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKEMEERQ--KAIYEEERRREAEEERRKQQEMeERRRIQEQMRKATEERSRLEAMEREREmM 578
|
330 340
....*....|....*....|...
gi 1370510769 381 SQDEQNELLKMQLQLQTELRQLK 403
Cdd:pfam17380 579 RQIVESEKARAEYEATTPITTIK 601
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
57-365 |
1.09e-04 |
|
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: 46.21 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 57 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASaqqaevftkqiQQLQGELRSLREEISLLEhekeSEL 136
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAY-----------GKLRRELAGLTRRLSAAE----GEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 137 KEIEQELHLAQAEIQSLRQAAEDSATEhESDIASLQEDLcrmQNELEDMERIRGDYEMEIASLRAEMEMKSSepsgslgl 216
Cdd:pfam19220 86 EELVARLAKLEAALREAEAAKEELRIE-LRDKTAQAEAL---ERQLAAETEQNRALEEENKALREEAQAAEK-------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 217 sDYSGLQEELQELRERYHFLNEEYRALQESN-------SSLTGQLADLESER-TQRATERWLQSQtLSMTSAESQTSEMD 288
Cdd:pfam19220 154 -ALQRAEGELATARERLALLEQENRRLQALSeeqaaelAELTRRLAELETQLdATRARLRALEGQ-LAAEQAERERAEAQ 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510769 289 FLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELcceLEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNE 365
Cdd:pfam19220 232 LEEAVEAHRAERASLRMKLEALTARAAATEQL---LAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEAD 305
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
36-509 |
1.11e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 36 KGGSVGSLSVNKHRGLSLTETELEELRAQVLQLVAELEETRElagqheddslelqgllederlasaqqaevftkQIQQLQ 115
Cdd:COG4717 61 PQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEE--------------------------------ELEELE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 116 GELRSLREEISLLEHEKesELKEIEQELHLAQAEIQSLRQAAEdSATEHESDIASLQEDLCRMQNELEDMERIRgDYEME 195
Cdd:COG4717 109 AELEELREELEKLEKLL--QLLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEEL-EELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 196 IASLRAEMEMKSSepsgslgLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTL 275
Cdd:COG4717 185 QLSLATEEELQDL-------AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 276 SMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMhgMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKcaqneVLRF 355
Cdd:COG4717 258 LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLL--LAREKASLGKEAEELQALPALEELEEEELEELLA-----ALGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 356 QTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLkmQLQLQTELRQL---------KVMKSTLVENQSEKELLCRLQKLH 426
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALlaeagvedeEELRAALEQAEEYQELKEELEELE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 427 LQhqnvtCEKEKLLERQQQLQEELQCHEAELQHLRDTVASFKESNEKDTETHAQL-QEMKQLyqASKDELERQKHMYDQL 505
Cdd:COG4717 409 EQ-----LEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELeAELEQL--EEDGELAELLQELEEL 481
|
....
gi 1370510769 506 EQDL 509
Cdd:COG4717 482 KAEL 485
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
123-490 |
1.74e-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: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 123 EEISLLEHEKESELKEIEQelhlaQAEIQSLRQAAEDSATEHESDIASLQEDlcRMQNELEDMERIRGDYEMEIASLRAE 202
Cdd:COG1196 189 ERLEDILGELERQLEPLER-----QAEKAERYRELKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 203 MEmkssepsgslglsdysGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERtQRATERWLQSQTlsmtsaes 282
Cdd:COG1196 262 LA----------------ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI-ARLEERRRELEE-------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 283 qtsemdflepdpEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVT 362
Cdd:COG1196 317 ------------RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 363 QNEELksrlcTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELLcrLQKLHLQHQNVTCEKEKLLER 442
Cdd:COG1196 385 AEELL-----EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE--EEEEEEALEEAAEEEAELEEE 457
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1370510769 443 QQQLQEELQCHEAELQHLRDTVASFKESNEKDTETHAQLQEMKQLYQA 490
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
51-740 |
2.51e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 51 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEvftkQIQQLQGELRSLREEISLLEH 130
Cdd:TIGR02168 227 LALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE----EIEELQKELYALANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 131 EKE---SELKEIEQELHLAQAEIQSLRQA---AEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEME 204
Cdd:TIGR02168 303 QKQilrERLANLERQLEELEAQLEELESKldeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 205 MKSSEpSGSLGLSDYSgLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERwlQSQTLSMTSAESQT 284
Cdd:TIGR02168 383 TLRSK-VAQLELQIAS-LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE--LEEELEELQEELER 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 285 SEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQ-HHRQVSEEEQRRLQR---------------ELKCA 348
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgFSEGVKALLKNQSGLsgilgvlselisvdeGYEAA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 349 QNEVLR--------------FQTSHSVTQNEELKSRLCTL-QKKYDTSQDEQNELLKMQ---LQLQTELRQLKVMKSTLV 410
Cdd:TIGR02168 539 IEAALGgrlqavvvenlnaaKKAIAFLKQNELGRVTFLPLdSIKGTEIQGNDREILKNIegfLGVAKDLVKFDPKLRKAL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 411 EN--------QSEKELLCRLQKLHLQHQNVTCEKEKLLER------QQQLQEELQCHEAELQHLRDTVASFKESNEkdtE 476
Cdd:TIGR02168 619 SYllggvlvvDDLDNALELAKKLRPGYRIVTLDGDLVRPGgvitggSAKTNSSILERRREIEELEEKIEELEEKIA---E 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 477 THAQLQEMKQLYQASKDELERQKHMYDQLEQDLLLCQLELKELKASHPIPEDK--------GKCANKCDTLLSRLTELQE 548
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlskelTELEAEIEELEERLEEAEE 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 549 KYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPKSGLLLKS------------QELLTKLEDLCELQL 616
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESlerriaaterrlEDLEEQIEELSEDIE 855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 617 LYQGMQEEQKKLIQNqdcvLKEQLEIHEELRRFKESHFQEVLENPDDSKLAKSSKCNRNKQPRSQAQHAQRPDSELGQEI 696
Cdd:TIGR02168 856 SLAAEIEELEELIEE----LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1370510769 697 QEL------IQSKLLMEQ---MQALQVMYDAGQAKQELLQQEQGRLLEERKRL 740
Cdd:TIGR02168 932 EGLevridnLQERLSEEYsltLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
57-217 |
2.56e-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: 44.36 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 57 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKESEL 136
Cdd:pfam09787 62 EIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 137 KEIEQELHLAQAEIQSlRQAAEDSATEHESDIASLQEDLCRMQNELEDM--ERIRGDYEMEiaslRAEMEMKSSEPSGSL 214
Cdd:pfam09787 142 KDREAEIEKLRNQLTS-KSQSSSSQSELENRLHQLTETLIQKQTMLEALstEKNSLVLQLE----RMEQQIKELQGEGSN 216
|
...
gi 1370510769 215 GLS 217
Cdd:pfam09787 217 GTS 219
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
55-419 |
2.86e-04 |
|
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: 45.01 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 55 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQaevfTKQIQQLQGELRSLREEISLLEHEKE- 133
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN----NKKIKELEKQLNQLKSEISDLNNQKEq 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 134 -------SELKEIEQELHLAQAEIQSLRQAA----------EDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEI 196
Cdd:TIGR04523 307 dwnkelkSELKNQEKKLEEIQNQISQNNKIIsqlneqisqlKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 197 ASLRA-----EMEMKSSEPSGSLGLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQ 271
Cdd:TIGR04523 387 KNLESqindlESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 272 SQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNE 351
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510769 352 VLrfqTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELL 419
Cdd:TIGR04523 547 LN---KDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKK 611
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
57-543 |
5.45e-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: 44.44 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 57 ELEELRAQVLQLVAELEETRELAGQHEDDSLElQGLLEDERLASAQ-QAEVFTKQIQQLQGELRSLREEISLLEHEKESE 135
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQHGAFLDADIE-TAAADQEQLPSWQsELENLEERLKALTGKHQDVTAKYNRRRSKIKEQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 136 LKEIEQELHLAQAEIqslRQAAEDSATEHESDIASLQEDLcRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLg 215
Cdd:pfam12128 388 NNRDIAGIKDKLAKI---REARDRQLAVAEDDLQALESEL-REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPEL- 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 216 LSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGqLADLESERTQRATERWLQSQtlsmtSAESQTSEMDFLEPDPE 295
Cdd:pfam12128 463 LLQLENFDERIERAREEQEAANAEVERLQSELRQARK-RRDQASEALRQASRRLEERQ-----SALDELELQLFPQAGTL 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 296 MQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQrrlqreLKCAQNEVLRFQTSHSVTQNEELKSRLCTLQ 375
Cdd:pfam12128 537 LHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELN------LYGVKLDLKRIDVPEWAASEEELRERLDKAE 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 376 KKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELlcRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCH-E 454
Cdd:pfam12128 611 EALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARL--DLRRLFDEKQSEKDKKNKALAERKDSANERLNSlE 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 455 AELQHLRDTVASFKESNEKDTETH--AQLQEMKQLYQASKDELERQKH----MYDQLEQDLLLCQLELK-ELKASHPIPE 527
Cdd:pfam12128 689 AQLKQLDKKHQAWLEEQKEQKREArtEKQAYWQVVEGALDAQLALLKAaiaaRRSGAKAELKALETWYKrDLASLGVDPD 768
|
490
....*....|....*.
gi 1370510769 528 DKGKCANKCDTLLSRL 543
Cdd:pfam12128 769 VIAKLKREIRTLERKI 784
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
51-246 |
5.73e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 51 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGL-------------LEDERLASAQQAEVFTKQIQQLQGE 117
Cdd:PRK02224 215 LAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLeaeiedlretiaeTEREREELAEEVRDLRERLEELEEE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 118 LRSLREE----------ISLLEHEKESELKEIEQELHLAQAEIQSLRQAAE---DSATEHESDIASLQEDLCRMQNELED 184
Cdd:PRK02224 295 RDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAEslrEDADDLEERAEELREEAAELESELEE 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510769 185 MERIRGDYEMEIASLRAEMEMKSSE----PSGSLGLSDYSG-LQEELQELRERYHFLNEEYRALQES 246
Cdd:PRK02224 375 AREAVEDRREEIEELEEEIEELRERfgdaPVDLGNAEDFLEeLREERDELREREAELEATLRTARER 441
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
51-202 |
8.45e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 51 LSLTETELEELRAQVLQLVAELEETRELAGQH-------EDDSLELQGLLEDERLASA-QQAEVFTKQIQQLQGELRSLR 122
Cdd:COG3883 60 LEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsGGSVSYLDVLLGSESFSDFlDRLSALSKIADADADLLEELK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 123 EEISLLEhEKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAE 202
Cdd:COG3883 140 ADKAELE-AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
296-995 |
9.09e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 9.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 296 MQLLRQQLRDAEeqmhgmknKCQELCCELEELQHHRQVSEEEQRRLQRElkcaqneVLRFQTSHSVTQNEELKSRLCTLQ 375
Cdd:TIGR02168 202 LKSLERQAEKAE--------RYKELKAELRELELALLVLRLEELREELE-------ELQEELKEAEEELEELTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 376 KKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLveNQSEKELLCRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCHEA 455
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRL--EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 456 ELQHLRDTVASFKESNEkdtETHAQLQEMKQLYQASKDELERQKHMYDQLEQDLLLCQLELKELKAShpIPEDKGKCANK 535
Cdd:TIGR02168 345 KLEELKEELESLEAELE---ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR--LERLEDRRERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 536 CDTLLSRLTELQE-KYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPKsgLLLKSQELLTKLEDLCEL 614
Cdd:TIGR02168 420 QQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA--AERELAQLQARLDSLERL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 615 QLLYQGMQEEQKKLIQNQDC------VLKEQLEIHEELRRFKE----SHFQEVL-ENPDDSKLA----KSSKCNR----- 674
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNQSGlsgilgVLSELISVDEGYEAAIEaalgGRLQAVVvENLNAAKKAiaflKQNELGRvtflp 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 675 ---NKQPRSQAQHAQRPDSELG--QEIQELIQS----KLLMEQMQALQVMYDAGQAKQELL------------------- 726
Cdd:TIGR02168 578 ldsIKGTEIQGNDREILKNIEGflGVAKDLVKFdpklRKALSYLLGGVLVVDDLDNALELAkklrpgyrivtldgdlvrp 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 727 ---------QQEQGRLleERKRLQADLQLCLEEMQllqVQSPSIKMSLESYGKSYGSMVPSNENCRKTYDTTVDDNESYY 797
Cdd:TIGR02168 658 ggvitggsaKTNSSIL--ERRREIEELEEKIEELE---EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 798 KSYTSTQTSSKSFLKSYDSSTSASEAYGKSycttsnssitykksygstsssDTCQKSFVSSCTDEEPAEPEDMERFEEMV 877
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAE---------------------IEELEERLEEAEEELAEAEAEIEELEAQI 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 878 VKVLIKLQAVQAMYQISQEEHSQLQEQMEKLLAKQKDLKEELDACEREFKECMECLEKPMAPQNDKN-EIKELQTKLREL 956
Cdd:TIGR02168 792 EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaEIEELEELIEEL 871
|
730 740 750
....*....|....*....|....*....|....*....
gi 1370510769 957 QLQYQASMDEQGRLLVVQEQLEGQLQCCQEELRQLREKR 995
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
141-267 |
1.52e-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: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 141 QELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLGLSDYS 220
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYE 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1370510769 221 GLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATE 267
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE 139
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
222-371 |
2.01e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 222 LQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAESQTSEMDflEPDPEMQLLRQ 301
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLD--ASSDDLAALEE 692
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 302 QLRDAEEQMhgmknkcQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNEELKSRL 371
Cdd:COG4913 693 QLEELEAEL-------EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF 755
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
88-766 |
2.14e-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: 42.27 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 88 ELQGLLEDERLASAqqAEVFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESD 167
Cdd:pfam02463 161 EAAGSRLKRKKKEA--LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 168 IASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLGLSDYSGLQEELQE-----LRERYHFLNEEYRA 242
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKsellkLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 243 LQESNSSLTGQLADLESERTQRATERWLQS-QTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELC 321
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEiKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 322 CELEELQHHRQVSEEEQRRL----------------QRELKCAQNEVLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQ 385
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEdllkeekkeeleileeEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 386 NELLKMQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCE-KEKLLERQQQLQEELQCHEAELQHLRDTV 464
Cdd:pfam02463 479 LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHgRLGDLGVAVENYKVAISTAVIVEVSATAD 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 465 ASFKESNEKDTETHAQLQEMKQLYQASKDELERQKHMYDQLEQDLLLCQLELKELKASHpipEDKGKCANKCDTLLSRLT 544
Cdd:pfam02463 559 EVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADE---DDKRAKVVEGILKDTELT 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 545 ELQEKYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPKSGLLLK----SQELLTKLEDLCELQLLYQG 620
Cdd:pfam02463 636 KLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKeeilRRQLEIKKKEQREKEELKKL 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 621 MQEEQKKLIQNQDCVLKEQLEIHEELRRfKESHFQEVLENPDDSKLAKSSKCNRNKQPRSQAQHAQRPDSELGQEIQ--- 697
Cdd:pfam02463 716 KLEAEELLADRVQEAQDKINEELKLLKQ-KIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEkee 794
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 698 -ELIQSKLLMEQMQALQVMYDAGQAKQELLQQEQGRLLEERKRLQADLQLCLEEMQLLQVQSPSIKMSLE 766
Cdd:pfam02463 795 kLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEIT 864
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
55-566 |
2.18e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 55 ETELEELRAQVLQLVAELE----ETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEH 130
Cdd:pfam15921 259 ELLLQQHQDRIEQLISEHEveitGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 131 EKESELKEIEQELHLAQAEIQSLRQAAEDSATEH---ESDIASLQEDLCRMQNEL---------------------EDME 186
Cdd:pfam15921 339 MYEDKIEELEKQLVLANSELTEARTERDQFSQESgnlDDQLQKLLADLHKREKELslekeqnkrlwdrdtgnsitiDHLR 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 187 RIRGDYEMEIASLRAEMEMKSSEPSGSL--GLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLE-SERTQ 263
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSECQGQMerQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLEsSERTV 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 264 RATERWLQSQTLSMtsaESQTSEMDFLEPDPEMQLLR-QQLRDAEEQMHGMKNKCQELCCELEEL--------------- 327
Cdd:pfam15921 499 SDLTASLQEKERAI---EATNAEITKLRSRVDLKLQElQHLKNEGDHLRNVQTECEALKLQMAEKdkvieilrqqienmt 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 328 ----QHHRQVS--EEEQRRLQRELKCAQNEVLRFQT--SHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTE- 398
Cdd:pfam15921 576 qlvgQHGRTAGamQVEKAQLEKEINDRRLELQEFKIlkDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQEr 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 399 ---LRQLKVMKSTLVENQSEKELLCRlqklhlqhqNVTCEKEKLLERQQQLQEELQCHEAELQHLRDTVASFKESNEKDT 475
Cdd:pfam15921 656 dqlLNEVKTSRNELNSLSEDYEVLKR---------NFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAM 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 476 ETHAQLQEMKQLYQASKDELERQKHMYDQLEQDLLLCQLELKELKAS-----HPIPEDKGKCANKCDTLLSRLTELQEKY 550
Cdd:pfam15921 727 KVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKlsqelSTVATEKNKMAGELEVLRSQERRLKEKV 806
|
570
....*....|....*...
gi 1370510769 551 KASQKEM--GQLQMEQCE 566
Cdd:pfam15921 807 ANMEVALdkASLQFAECQ 824
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
883-994 |
2.71e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 883 KLQAVQAMYQISQEEHSQLQEQMEKLLAKQKDLKEELDACEREFKECMECLEKPMAPQ-------------NDKNEIKEL 949
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEReiaeleaelerldASSDDLAAL 690
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1370510769 950 QTKLRELQLQYQASMDEQGRLLVVQEQLEGQLQCCQEELRQLREK 994
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
59-245 |
3.70e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 59 EELRAQV--LQLVAELEETRELAGQHEDDSLELQGLLEDERlasaQQAEVFTKQIQQLQGELRSLREEISLLEHEKESEL 136
Cdd:PRK11281 39 ADVQAQLdaLNKQKLLEAEDKLVQQDLEQTLALLDKIDRQK----EETEQLKQQLAQAPAKLRQAQAELEALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 137 KEIEQELHLAQ-----AEIQSLRQAAEDSATEHESDIASLQEDLCRMQNEL-EDMERI---------------------R 189
Cdd:PRK11281 115 RETLSTLSLRQlesrlAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALyANSQRLqqirnllkggkvggkalrpsqR 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510769 190 GDYEMEIASLRAEMEMKSSEPSGSLGLSDYsgLQEELQELRERYHFLNEEYRALQE 245
Cdd:PRK11281 195 VLLQAEQALLNAQNDLQRKSLEGNTQLQDL--LQKQRDYLTARIQRLEHQLQLLQE 248
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
49-199 |
3.76e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 49 RGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQgllederlASAQQAEVFTKQIQQLQGELRSLREEISLL 128
Cdd:PRK09039 46 REISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLR--------ASLSAAEAERSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510769 129 EHEKESELKEIEQELHLAQAEIQSLRQaaedsatehesDIASLQEDLCRMQNELEDMERIRGDYEMEIASL 199
Cdd:PRK09039 118 AGELAQELDSEKQVSARALAQVELLNQ-----------QIAALRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
415-731 |
4.54e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 415 EKELLCRLQKLHLQHQNVtcEKEKLLERQQQLQEELQCHEAELQHLRDTVASFKESNEKDTETHAQLQEMKQLYQASKDE 494
Cdd:COG1196 222 LKELEAELLLLKLRELEA--ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 495 LERQKHMYDQLEQDLLLCQLELKELKASHpipedkgkcANKCDTLLSRLTELQEKYKASQKEMGQLQMEQCELLEDQRRM 574
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAEL---------EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 575 QEEQGQLQEELHRLtlplpKSGLLLKSQELLTKLEDLCELQLLYQGMQEEQKKLIQNQDcVLKEQLEIHEELRRFKESHF 654
Cdd:COG1196 371 EAELAEAEEELEEL-----AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE-ELEEALAELEEEEEEEEEAL 444
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510769 655 QEVLENPDDSKLAKSSKCNRNKQPRSQAQHAQRPDSELGQEIQELIQSKLLMEQMQALQVMYDAGQAKQELLQQEQG 731
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
136-401 |
4.57e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 136 LKEIEQELHLAQAEIQSLRQAAE--DSATEHESDIASLQEDLCRMQNELEDMERirgdyemEIASLRAEMEMKSSEPSGS 213
Cdd:PRK11281 48 LNKQKLLEAEDKLVQQDLEQTLAllDKIDRQKEETEQLKQQLAQAPAKLRQAQA-------ELEALKDDNDEETRETLST 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 214 LGLSDysgLQEELQELRERyhfLNEEYRALQESNSSLTGQlaDLESERTQRA-TERWLQSQTLSMTSAESQTSEMDfLEP 292
Cdd:PRK11281 121 LSLRQ---LESRLAQTLDQ---LQNAQNDLAEYNSQLVSL--QTQPERAQAAlYANSQRLQQIRNLLKGGKVGGKA-LRP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 293 DpemqllRQQLRDAEEQMHGMKNKCQELccELEE-------LQHHRQVSEEEQRRLQRELKCAQ---NEVLRFQTSHSVT 362
Cdd:PRK11281 192 S------QRVLLQAEQALLNAQNDLQRK--SLEGntqlqdlLQKQRDYLTARIQRLEHQLQLLQeaiNSKRLTLSEKTVQ 263
|
250 260 270
....*....|....*....|....*....|....*....
gi 1370510769 363 QNEELKsrlctlqkkyDTSQDEQNELLKMQLQLQTELRQ 401
Cdd:PRK11281 264 EAQSQD----------EAARIQANPLVAQELEINLQLSQ 292
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
51-648 |
5.16e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 51 LSLTETELEELRAQVLQLvaelEETRELAGQHEDDSLELQGLledERLASAQQAEVFTKQIQQLQGELRSLREEISLLEH 130
Cdd:COG4913 237 LERAHEALEDAREQIELL----EPIRELAERYAAARERLAEL---EYLRAALRLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 131 EKEselkEIEQELHLAQAEIQSLRQAAEDSATEhesDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEmkssep 210
Cdd:COG4913 310 ELE----RLEARLDALREELDELEAQIRGNGGD---RLEQLEREIERLERELEERERRRARLEALLAALGLPLP------ 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 211 sgsLGLSDYSGLQEELQELRERyhfLNEEYRALQESNSSLTGQLADLESERTQRATE-RWLQSQTLSMtsaesqtsemdf 289
Cdd:COG4913 377 ---ASAEEFAALRAEAAALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEiASLERRKSNI------------ 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 290 lepDPEMQLLRQQLRDAeeqmhgMKNKCQELC--CELEEL--------------------------QHHRQVSEE-EQRR 340
Cdd:COG4913 439 ---PARLLALRDALAEA------LGLDEAELPfvGELIEVrpeeerwrgaiervlggfaltllvppEHYAAALRWvNRLH 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 341 LQRELkcaqnEVLRFQTSHSVTQNEELKSRlcTLQKKYDTSQDEQNELLKMQLQlqtelRQLKVMKstlVENQSE----- 415
Cdd:COG4913 510 LRGRL-----VYERVRTGLPDPERPRLDPD--SLAGKLDFKPHPFRAWLEAELG-----RRFDYVC---VDSPEElrrhp 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 416 ---------KELLCRLQK---LHLQHQNVTCE--KEKLLERqqqlqeelqchEAELQHLRDTVASFKESNEKDTETHAQL 481
Cdd:COG4913 575 raitragqvKGNGTRHEKddrRRIRSRYVLGFdnRAKLAAL-----------EAELAELEEELAEAEERLEALEAELDAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 482 QEMKQLYQASKDELERQKHMyDQLEQDLLLCQLELKELKASHPipedkgkcankcdtllsRLTELQEKYKASQKEMGQLQ 561
Cdd:COG4913 644 QERREALQRLAEYSWDEIDV-ASAEREIAELEAELERLDASSD-----------------DLAALEEQLEELEAELEELE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 562 MEQCELLEDQRRMQEEQGQLQEELHRLTLPLpKSGLLLKSQELLTKLEDLCELQLLYQGMQEEQKKLIQNQDCVLKEQLE 641
Cdd:COG4913 706 EELDELKGEIGRLEKELEQAEEELDELQDRL-EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNR 784
|
....*..
gi 1370510769 642 IHEELRR 648
Cdd:COG4913 785 AEEELER 791
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
56-174 |
5.75e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 56 TELEELRAQVLQLVAELEEtrelagqheddslelqgLLEDERLASAQQAEVFTKQIQQLQGELRSLREEislLEHEKE-- 133
Cdd:COG0542 411 EELDELERRLEQLEIEKEA-----------------LKKEQDEASFERLAELRDELAELEEELEALKAR---WEAEKEli 470
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1370510769 134 SELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQED 174
Cdd:COG0542 471 EEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
194-410 |
8.04e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 194 MEIASLRAEMEM--KSSEPSGSLGLSDYSGLQEELQELRERyhflNEEYRALQESNSSLTGQLADLESERTQRATERWLQ 271
Cdd:COG4717 46 MLLERLEKEADElfKPQGRKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 272 SQTLsmtsaesqtsemDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNE 351
Cdd:COG4717 122 EKLL------------QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510769 352 VLRfQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNEL------LKMQLQLQTELRQLKVMKSTLV 410
Cdd:COG4717 190 TEE-ELQDLAEELEELQQRLAELEEELEEAQEELEELeeeleqLENELEAAALEERLKEARLLLL 253
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
159-409 |
8.64e-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: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 159 DSATEHESDIASLQEDLCRMQNELEDMERIRGDYEmEIASLRAEMEMKSSEpsgsLGLSDYSGLQEELQELRERYHFLNE 238
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEPIRELAE-RYAAARERLAELEYL----RAALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 239 EYRALQESNSSLTGQLADLESERtQRATERWLQSQTlsmtsaesqtsemdflepdPEMQLLRQQLRDAEEQMHGMKNKCQ 318
Cdd:COG4913 303 ELARLEAELERLEARLDALREEL-DELEAQIRGNGG-------------------DRLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 319 ELCCELEELQHHRQVSEEEQRRLQRELKCAQnevlrfqtshsvtqnEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTE 398
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRAEAAALL---------------EALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
250
....*....|.
gi 1370510769 399 LRQLKVMKSTL 409
Cdd:COG4913 428 IASLERRKSNI 438
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
54-159 |
9.44e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510769 54 TETELEELRAQVLQLvaeleETRELAGQHEDDSLELQGLLEDERLASAQQaevFTKQIQQLQGELRSLREEISLLEHEKE 133
Cdd:PRK04863 584 LRQQLEQLQARIQRL-----AARAPAWLAAQDALARLREQSGEEFEDSQD---VTEYMQQLLERERELTVERDELAARKQ 655
|
90 100
....*....|....*....|....*.
gi 1370510769 134 SELKEIEQELHLAQAEIQSLRQAAED 159
Cdd:PRK04863 656 ALDEEIERLSQPGGSEDPRLNALAER 681
|
|
| |
