|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
84-405 |
1.06e-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: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 84 VQKGGSVGSLSVNKHRGLSLTETELEELRAQVLQLVAELEETR----ELAGQHEDDSLELQGLLEDERLASAQ------Q 153
Cdd:TIGR02168 655 VRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEkalaELRKELEELEEELEQLRKELEELSRQisalrkD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 154 AEVFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQ---ELHLAQAEIQSLRQAAEDSATEH---ESDIASLQEDLCR 227
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeELAEAEAEIEELEAQIEQLKEELkalREALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 228 MQNELEDMERIRGDYEMEIASLRAEMEMkssepsgslglsdysgLQEELQELRERYHFLNEEYRALQESNSSLTGQLADL 307
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLED----------------LEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 308 ESERTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELC--------CELEELQH 379
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerlseeysLTLEEAEA 958
|
330 340
....*....|....*....|....*.
gi 767948504 380 HRQVSEEEQRRLQRELKCAQNEVLRF 405
Cdd:TIGR02168 959 LENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
101-359 |
5.83e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 5.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 101 LSLTETELEELRAQVLQLVAELEETRElagQHEDDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELRSLREEISlleh 180
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRL---ELEELELELEEAQAEEYELLAELARL-EQDIARLEERRRELEERLE---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 181 EKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEp 260
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL- 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 261 sgslgLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERwLQSQTLSMTSAESQTSEMDfl 340
Cdd:COG1196 399 -----AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE-AELEEEEEALLELLAELLE-- 470
|
250
....*....|....*....
gi 767948504 341 epdpEMQLLRQQLRDAEEQ 359
Cdd:COG1196 471 ----EAALLEAALAELLEE 485
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
107-437 |
1.28e-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: 65.09 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEvftKQIQQLQGELRSLREEISLLE---HEKE 183
Cdd:TIGR02169 188 RLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALE---RQKEAIERQLASLEEELEKLTeeiSELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 184 SELKEIEQELHLAQAEIQSL-----RQAAEDSAtEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEmkss 258
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIG-ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE---- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 259 epsgslglsdysGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLEsERTQRATERWLQSQT-LSMTSAESQTSEM 337
Cdd:TIGR02169 340 ------------ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD-KEFAETRDELKDYREkLEKLKREINELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 338 DFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNE-- 415
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEls 486
|
330 340
....*....|....*....|..
gi 767948504 416 ELKSRLCTLQKKYDTSQDEQNE 437
Cdd:TIGR02169 487 KLQRELAEAEAQARASEERVRG 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
160-468 |
9.42e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 9.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 160 QIQQLQGELRSLREEISLLE---HEKESELKEIEQELHLAQAEIQSLRQAAEDSATEhesdIASLQEDLCRMQNELEDME 236
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEekiAELEKALAELRKELEELEEELEQLRKELEELSRQ----ISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 237 RIRGDYEMEIASLRAEMEmkssepsgsLGLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQraT 316
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIE---------ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL--L 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 317 ERWLQSQTLSMTSAESQTSEMdflepDPEMQLLRQQLRDAEEQMhgmknkcqelccelEELQHHRQVSEEEQRRLQRELK 396
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAAT-----ERRLEDLEEQIEELSEDI--------------ESLAAEIEELEELIEELESELE 876
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767948504 397 CAQNEVlrfqtshsvtqnEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKEL 468
Cdd:TIGR02168 877 ALLNER------------ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV 936
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
153-467 |
1.70e-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: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 153 QAEVFTKQIQQLQGELRSLREEISllehEKESELKEIEQELHLAQAEIQSLRqaaeDSATEHESDIASLQEDLCRMQNEL 232
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELK----EAEEELEELTAELQELEEKLEELR----LEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 233 EDMERIRGDYEMEIASLRAEMEMkssepsgslglsdysgLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESErt 312
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEE----------------LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE-- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 313 qraterwlqsqtLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQ 392
Cdd:TIGR02168 360 ------------LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767948504 393 RELKCAQNEVLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKE 467
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-702 |
2.69e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQqaevFTKQIQQLQGELRSLREEISLLEH 180
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ----LELQIASLNNEIERLEARLERLED 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 181 EKESELKEIEQ--------ELHLAQAEIQSLRQAAEDSATEHEsdiaSLQEDLCRMQNELEDMERIRGDYEMEIASLRAE 252
Cdd:TIGR02168 415 RRERLQQEIEEllkkleeaELKELQAELEELEEELEELQEELE----RLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 253 MEMkssepsgslglsdysglqeeLQELRERYHFLNEEYRALQESNSSLTG---QLADLES--ERTQRATERWLQS--QTL 325
Cdd:TIGR02168 491 LDS--------------------LERLQENLEGFSEGVKALLKNQSGLSGilgVLSELISvdEGYEAAIEAALGGrlQAV 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 326 SMTSAESQTSEMDFLEPD--------PEMQLLRQQLRDAEEQMHGMKNKCQELCCELEE------------LQHHRQVSE 385
Cdd:TIGR02168 551 VVENLNAAKKAIAFLKQNelgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKfdpklrkalsylLGGVLVVDD 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 386 EEQ-RRLQRELKCAQNEVL---------------RFQTSHSVTQN----EELKSRLCTLQKKYDTSQDEQNELLKMQLQL 445
Cdd:TIGR02168 631 LDNaLELAKKLRPGYRIVTldgdlvrpggvitggSAKTNSSILERrreiEELEEKIEELEEKIAELEKALAELRKELEEL 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 446 QTELRQLKVM------------KSTLVENQSEKELLCRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCHEAELQHLRDT 513
Cdd:TIGR02168 711 EEELEQLRKEleelsrqisalrKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 514 VASFKESNEKDTETHAQLQEMkqlYQASKDELERQKHMYDQLEQDLLLCQLELKELKASHPIPEDKGKCANK-------- 585
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAE---LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAeieeleel 867
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 586 CDTLLSRLTELQEKYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPKSGLLLKS--QELLTKLEDLCE 663
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGleVRIDNLQERLSE 947
|
650 660 670
....*....|....*....|....*....|....*....
gi 767948504 664 lqlLYQGMQEEqkkLIQNQDCVLKEQLEIHEELRRFKES 702
Cdd:TIGR02168 948 ---EYSLTLEE---AEALENKIEDDEEEARRRLKRLENK 980
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
98-254 |
1.80e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 98 HRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDdslELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISL 177
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALRE---ELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 178 LEH----------EKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIA 247
Cdd:COG4913 364 LEAllaalglplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
....*..
gi 767948504 248 SLRAEME 254
Cdd:COG4913 444 ALRDALA 450
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
108-361 |
3.52e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 108 LEELRAQVLQLVAELEETRELAGQHEDdsleLQGLLEDERLASAQQAEVFTKQI--QQLQGELRSLREEISLLEhEKESE 185
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEA----ELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLD-ASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 186 LKEIEQELHLAQAEIQSLRQ---AAEDSATEHESDIASLQEDLCRMQNELEDMERI-RGDYEMEIASLRAEMEMKSSEPS 261
Cdd:COG4913 687 LAALEEQLEELEAELEELEEeldELKGEIGRLEKELEQAEEELDELQDRLEAAEDLaRLELRALLEERFAAALGDAVERE 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 262 GSLGLSD-YSGLQEELQELRER-----------YHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTs 329
Cdd:COG4913 767 LRENLEErIDALRARLNRAEEEleramrafnreWPAETADLDADLESLPEYLALLDRLEEDGLPEYEERFKELLNENSI- 845
|
250 260 270
....*....|....*....|....*....|..
gi 767948504 330 aESQTsemDFLepdpemQLLRQQLRDAEEQMH 361
Cdd:COG4913 846 -EFVA---DLL------SKLRRAIREIKERID 867
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
148-378 |
4.60e-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: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 148 LASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKES---ELKEIEQELHLAQAEIQSLrqaaEDSATEHESDIASLQED 224
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAllkQLAALERRIAALARRIRAL----EQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 225 LCRMQNELEDMERirgdyemEIASLRAEMEMKSSEPSGSLGLSdysglQEELQELRERYHFLNEEYRALQESNSSLTGQL 304
Cdd:COG4942 92 IAELRAELEAQKE-------ELAELLRALYRLGRQPPLALLLS-----PEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767948504 305 ADLESERTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQ 378
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
163-490 |
4.61e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 163 QLQGELRSLREEISLLEHEKES---ELKEIEQELHlaqaEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIR 239
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSlqsELRRIENRLD----ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 240 GDYEMEIASLRAEMEMKSSEpsgslgLSDY----SGLQEELQEL-----RERYHFLNEEYRALQESNSSLTGQLADLESE 310
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEAR------IEELeedlHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 311 RTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRR 390
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 391 LQRELK--CAQNEVLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELL---KMQLQLQTELRQLKVMKS-TLVENQS 464
Cdd:TIGR02169 901 LERKIEelEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELsleDVQAELQRVEEEIRALEPvNMLAIQE 980
|
330 340
....*....|....*....|....*.
gi 767948504 465 EKELLCRLQKLHLQHQNVTCEKEKLL 490
Cdd:TIGR02169 981 YEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-314 |
5.52e-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: 5.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDerlaSAQQAEVFTKQIQQLQGELRSLREEISlleh 180
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED----LEEQIEELSEDIESLAAEIEELEELIE---- 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 181 EKESELKEIEQELHLAQAEIQSLRQAAEDSAT---EHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASL------RA 251
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEelrELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLqerlseEY 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 252 EMEMKSSEPSGSLGLSDYSGLQ---------------------EELQELRERYHFLNEEYRALQESNSSLTGQLADLESE 310
Cdd:TIGR02168 950 SLTLEEAEALENKIEDDEEEARrrlkrlenkikelgpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDRE 1029
|
....
gi 767948504 311 RTQR 314
Cdd:TIGR02168 1030 ARER 1033
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
105-378 |
1.55e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 105 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLederLASAQQAEVFTKQIQQLQGELRSLREEISLLEH---E 181
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL----YALANEISRLEQQKQILRERLANLERQLEELEAqleE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 182 KESELKEIEQELHLAQAEIQSLRQaaedsatehesDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEM-EMKSSEP 260
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKE-----------ELESLEAELEELEAELEELESRLEELEEQLETLRSKVaQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 261 SgslglsdysgLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATErwlqsqTLSMTSAESQTSEMDFL 340
Cdd:TIGR02168 397 S----------LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE------ELEEELEELQEELERLE 460
|
250 260 270
....*....|....*....|....*....|....*...
gi 767948504 341 EpdpEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQ 378
Cdd:TIGR02168 461 E---ALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
105-310 |
3.19e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 105 ETELEELRAQVLQLVAELEETRElagQHEDDSLELQGLLEDERLASAQQaevftkQIQQLQGELRSLREEISLLEHEKES 184
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQ---KNGLVDLSEEAKLLLQQLSELES------QLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 185 ELKEIEQELhlAQAEIQSLRQAAEDSatehESDIASLQEdlcRMQNELEDMERIRGdyemEIASLRAEMEMKSSEPSGSL 264
Cdd:COG3206 252 GPDALPELL--QSPVIQQLRAQLAEL----EAELAELSA---RYTPNHPDVIALRA----QIAALRAQLQQEAQRILASL 318
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767948504 265 GlSDYSGLQEELQELRERYhflnEEYRALQESNSSLTGQLADLESE 310
Cdd:COG3206 319 E-AELEALQAREASLQAQL----AQLEARLAELPELEAELRRLERE 359
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
107-537 |
4.03e-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: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEhEKESEL 186
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE-EALAEL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 187 KEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLGL 266
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 267 SDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEM 346
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALA 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 347 QLLRQQLRDAEEqmhgmknkcQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNEELKSRlctLQK 426
Cdd:COG1196 594 RGAIGAAVDLVA---------SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA---GGS 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 427 KYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCHEAE 506
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
410 420 430
....*....|....*....|....*....|.
gi 767948504 507 LQHLRDTVASFKESNEKDTETHAQLQEMKQL 537
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLEELERELERL 772
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
107-333 |
7.63e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 7.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 107 ELEELRAQVLQLVAELEETRELAGQhEDDSLELQGLLEDERLASAQQaevftkQIQQLQGELRSLREEisllEHEKESEL 186
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEE-ELAELEEELEELEEELEELEE------ELEEAEEELEEAEAE----LAEAEEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 187 KEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEpsgslgL 266
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE------E 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767948504 267 SDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAESQ 333
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
110-488 |
1.18e-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: 52.38 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 110 ELRAQVLQLVAELEE-TRELAG-QHEDDSLE-LQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISllehEKESEL 186
Cdd:TIGR02169 671 SEPAELQRLRERLEGlKRELSSlQSELRRIEnRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE----ELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 187 KEIEQELHLAQAEIQSLrqaaedsatehESDIASLQEDLCRMQNELEDMERirgdyemeiaslraememkssepsgslgl 266
Cdd:TIGR02169 747 SSLEQEIENVKSELKEL-----------EARIEELEEDLHKLEEALNDLEA----------------------------- 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 267 sdysglqeelQELRERYHFLNEEYRALQESNSSLTGQLADLESErtqraterwLQSQTLSMTSAESqtsemdflepdpEM 346
Cdd:TIGR02169 787 ----------RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQK---------LNRLTLEKEYLEK------------EI 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 347 QLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQtshsvTQNEELKSRLCTLQK 426
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE-----AQLRELERKIEELEA 910
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767948504 427 KYDTSQDEQNELlkmQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCEKEK 488
Cdd:TIGR02169 911 QIEKKRKRLSEL---KAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRA 969
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
183-400 |
1.19e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 183 ESELKEIEQELHLAQAEIQSLRQ-----AAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKS 257
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 258 SEPSGSLGLSDYSGLQEELQELRERYHFLNEEYRALQEsnssltgQLADLESERTQRATERWLQSQTlsmtsaesqtsem 337
Cdd:COG3206 261 QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRA-------QIAALRAQLQQEAQRILASLEA------------- 320
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767948504 338 dflepdpEMQLLRQQLRDAEEQMHGMKNKCQELcceleelqhhrQVSEEEQRRLQRELKCAQN 400
Cdd:COG3206 321 -------ELEALQAREASLQAQLAQLEARLAEL-----------PELEAELRRLEREVEVARE 365
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
105-246 |
4.05e-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: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 105 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDerlASAQQAEVFT-KQIQQLQGELRSLREEISLLEheke 183
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK---YEEQLGNVRNnKEYEALQKEIESLKRRISDLE---- 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767948504 184 SELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEI 246
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
110-465 |
5.50e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.05 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 110 ELRAQvlqLVAELEETRELAGQHEDDSLElQGLLEderlASAQQAEVfTKQIQQLQGELRSLREEISLL---EHEKESEL 186
Cdd:PRK10929 83 ELRQQ---LNNERDEPRSVPPNMSTDALE-QEILQ----VSSQLLEK-SRQAQQEQDRAREISDSLSQLpqqQTEARRQL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 187 KEIEQELHLAQAEIQSLRQAAedsatehesdIASLQEDLCRMQ---NELEdMERIRGDYEMEIASLRAEMEMKSSEPsgs 263
Cdd:PRK10929 154 NEIERRLQTLGTPNTPLAQAQ----------LTALQAESAALKalvDELE-LAQLSANNRQELARLRSELAKKRSQQ--- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 264 lglsdysgLQEELQELRERYHFL--NEEYRALqESNSSLTGQLADL-ESERTQRATERWLqSQTLSmtsaeSQTSEMDFL 340
Cdd:PRK10929 220 --------LDAYLQALRNQLNSQrqREAERAL-ESTELLAEQSGDLpKSIVAQFKINREL-SQALN-----QQAQRMDLI 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 341 -----EPDPEMQLLRQQLRDAEEQMH--GMKN-----------------KCQELCCELEELQHHRQVSEEEQRRLQRELK 396
Cdd:PRK10929 285 asqqrQAASQTLQVRQALNTLREQSQwlGVSNalgealraqvarlpempKPQQLDTEMAQLRVQRLRYEDLLNKQPQLRQ 364
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767948504 397 CAQNEvlrfqtSHSVTQNEelksrlctlQKKYDTSQDEQNELLKMQLQ----LQTELRQLKVMKSTLVENQSE 465
Cdd:PRK10929 365 IRQAD------GQPLTAEQ---------NRILDAQLRTQRELLNSLLSggdtLILELTKLKVANSQLEDALKE 422
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
99-255 |
5.81e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.86 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 99 RGLSLtETELEELRAQVLqlvAELEETRELAGQHEDDSLELqgllEDERlasaqqaevftkqIQQLQGELRSLREEISLL 178
Cdd:COG2433 374 RGLSI-EEALEELIEKEL---PEEEPEAEREKEHEERELTE----EEEE-------------IRRLEEQVERLEAEVEEL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 179 E---HEKESELKEIEQELHLAQAEiqslrqaaEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEM 255
Cdd:COG2433 433 EaelEEKDERIERLERELSEARSE--------ERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKL 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
107-314 |
7.55e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKESEL 186
Cdd:COG1196 621 TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 187 KEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERI---------RGDYEMEIASLRAEMEmks 257
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAleelpeppdLEELERELERLEREIE--- 777
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767948504 258 sepsgSLG----LSDysglqEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQR 314
Cdd:COG1196 778 -----ALGpvnlLAI-----EEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
185-395 |
7.65e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 7.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 185 ELKEIEQELHLAQAEIQSLRQAAEDsATEHESDIASLQE-DLCRMQNELEDMERIRGDYEMEIASLRAEMEmkssepsgs 263
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIREL-AERYAAARERLAElEYLRAALRLWFAQRRLELLEAELEELRAELA--------- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 264 lglsdysGLQEELQELRERYHFLNEEYRALQESNSS--------LTGQLADLESERTQRATERWLQSQTLSMTSAESQTS 335
Cdd:COG4913 306 -------RLEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767948504 336 EMDFLE-----------PDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQREL 395
Cdd:COG4913 379 AEEFAAlraeaaalleaLEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
101-467 |
8.67e-06 |
|
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: 49.40 E-value: 8.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLE- 179
Cdd:pfam01576 150 LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQa 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 180 --HEKESELKEIEQELHLAQAEI---QSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEME 254
Cdd:pfam01576 230 qiAELRAQLAKKEEELQAALARLeeeTAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 255 mkssepsgslGLSDYSGLQEELQELRERYhfLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAE--- 331
Cdd:pfam01576 310 ----------DTLDTTAAQQELRSKREQE--VTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANlek 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 332 -SQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVlrfqtSHS 410
Cdd:pfam01576 378 aKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLL-----NEA 452
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 767948504 411 VTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKE 467
Cdd:pfam01576 453 EGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEE 509
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
105-469 |
1.67e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 105 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQaevfTKQIQQLQGELRSLREEISLLEHEKE- 183
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN----NKKIKELEKQLNQLKSEISDLNNQKEq 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 184 -------SELKEIEQELHLAQAEIQSLRQAA----------EDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEI 246
Cdd:TIGR04523 307 dwnkelkSELKNQEKKLEEIQNQISQNNKIIsqlneqisqlKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 247 ASLRA-----EMEMKSSEPSGSLGLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQ 321
Cdd:TIGR04523 387 KNLESqindlESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 322 SQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNE 401
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767948504 402 VLrfqTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELL 469
Cdd:TIGR04523 547 LN---KDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKK 611
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
99-263 |
2.28e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 99 RGLSLTETELEELRAQVLQLVAELEETREL----------AGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGEL 168
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEElaellralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 169 RSLREEISLLEHEKESELKEIEQELHLAQAEIQSLRQAAEdsatEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIAS 248
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKA----ERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
170
....*....|....*
gi 767948504 249 LRAEMEMKSSEPSGS 263
Cdd:COG4942 232 LEAEAAAAAERTPAA 246
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
101-237 |
2.51e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSlELQGLLEDERLASAQQAEV---FTK---QIQQLQGELRSLREE 174
Cdd:COG3206 228 LAEARAELAEAEARLAALRAQLGSGPDALPELLQSP-VIQQLRAQLAELEAELAELsarYTPnhpDVIALRAQIAALRAQ 306
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767948504 175 IsllEHEKESELKEIEQELHLAQAEIQSLRQAAEdsatEHESDIASLQEDlcrmQNELEDMER 237
Cdd:COG3206 307 L---QQEAQRILASLEAELEALQAREASLQAQLA----QLEARLAELPEL----EAELRRLER 358
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
140-453 |
3.12e-05 |
|
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: 47.43 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 140 QGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQELHLAQAEiqSLRQAAEDSA----TEHE 215
Cdd:pfam17380 263 QTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAE--KARQAEMDRQaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 216 SDIASLQEDLCRMQNE--LEDMERIRG-DYEMEIASLRA------EMEMKSSEPSGSL-GLSDYSGLQEELQELRERYHF 285
Cdd:pfam17380 341 RMAMERERELERIRQEerKRELERIRQeEIAMEISRMRElerlqmERQQKNERVRQELeAARKVKILEEERQRKIQQQKV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 286 LNEEYRALQESNSSLTGQLADLESERT-----QRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQL--------LRQQ 352
Cdd:pfam17380 421 EMEQIRAEQEEARQREVRRLEEERAREmervrLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRaeeqrrkiLEKE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 353 LRDAEEQMHGMKNKCQELCCELEELQhhRQVSEEEQRRLQRELKCAQNEV-LRFQTSHSVTQNEELKSRLCTLQKKYD-T 430
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKEMEERQ--KAIYEEERRREAEEERRKQQEMeERRRIQEQMRKATEERSRLEAMEREREmM 578
|
330 340
....*....|....*....|...
gi 767948504 431 SQDEQNELLKMQLQLQTELRQLK 453
Cdd:pfam17380 579 RQIVESEKARAEYEATTPITTIK 601
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
158-395 |
3.42e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 158 TKQIQQLQGELRSLREEISLLEhekeSELKEIEQELHLAQAEIQSLRQAAEDSatEHESDIASLQEDLCRMQNELEDMER 237
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAE----ERLEALEAELDALQERREALQRLAEYS--WDEIDVASAEREIAELEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 238 irgdyemeiaslraememkssepsgslGLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQrate 317
Cdd:COG4913 683 ---------------------------SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE---- 731
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767948504 318 rwLQSQTLSMTSAESQTSEMDFLEpdpemQLLRQQLRDAEEQMHgmknkcqelccelEELQHHRQVSEEEQRRLQREL 395
Cdd:COG4913 732 --LQDRLEAAEDLARLELRALLEE-----RFAAALGDAVERELR-------------ENLEERIDALRARLNRAEEEL 789
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
101-428 |
4.28e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISlleh 180
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE---- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 181 EKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASL---------RA 251
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLlallflllaRE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 252 EMEMKSSEPSGSLGLSDYSGLQEELQELRERYHFL----NEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSM 327
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEELLAALGLPpdlsPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 328 TSAESQTSEM--DFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCC---------ELEELQHHRQVSEEEQRRLQRELK 396
Cdd:COG4717 377 AEAGVEDEEElrAALEQAEEYQELKEELEELEEQLEELLGELEELLEaldeeeleeELEELEEELEELEEELEELREELA 456
|
330 340 350
....*....|....*....|....*....|....*.
gi 767948504 397 CAQNEVLRFQTSHSVTQN----EELKSRLCTLQKKY 428
Cdd:COG4717 457 ELEAELEQLEEDGELAELlqelEELKAELRELAEEW 492
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
269-572 |
4.67e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 269 YSGLQEELQELRERYHFLneEYRALQESNSSLTGQLADLESERTQRATERwlqsqtlsmtsAESQTsemdflepdpEMQL 348
Cdd:COG1196 215 YRELKEELKELEAELLLL--KLRELEAELEELEAELEELEAELEELEAEL-----------AELEA----------ELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 349 LRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNE--VLRFQTSHSVTQNEELKSRLCTLQK 426
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEElaELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 427 KYDTSQDEQNELLKMQLQLQTELRQLKvmKSTLVENQSEKELLCRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCHEAE 506
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAE--EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767948504 507 LQHLRDTVASFKESNEKDTETHAQLQEMKQLYQASKDELERQKHMYDQLEQDLLLCQLELKELKAS 572
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
346-622 |
6.01e-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: 46.59 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 346 MQLLRQQLRDAEeqmhgmknKCQELCCELEELQHHRQVSEEEQRRLQRElkcaqneVLRFQTSHSVTQNEELKSRLCTLQ 425
Cdd:TIGR02168 202 LKSLERQAEKAE--------RYKELKAELRELELALLVLRLEELREELE-------ELQEELKEAEEELEELTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 426 KKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLveNQSEKELLCRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCHEA 505
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRL--EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 506 ELQHLRDTVASFKESNEkdtETHAQLQEMKQLYQASKDELERQKHMYDQLEQDLLLCQLELKELKA-------------- 571
Cdd:TIGR02168 345 KLEELKEELESLEAELE---ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEArlerledrrerlqq 421
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 767948504 572 ------SHPIPEDKGKCANKCDTLLSRLTELQEKYKASQKEMGQLQMEQCELLEDQR 622
Cdd:TIGR02168 422 eieellKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
107-267 |
1.03e-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: 45.13 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKESEL 186
Cdd:pfam09787 62 EIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 187 KEIEQELHLAQAEIQSlRQAAEDSATEHESDIASLQEDLCRMQNELEDM--ERIRGDYEMEiaslRAEMEMKSSEPSGSL 264
Cdd:pfam09787 142 KDREAEIEKLRNQLTS-KSQSSSSQSELENRLHQLTETLIQKQTMLEALstEKNSLVLQLE----RMEQQIKELQGEGSN 216
|
...
gi 767948504 265 GLS 267
Cdd:pfam09787 217 GTS 219
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
104-318 |
1.33e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 104 TETELEELRAQVLQLVAELEETRELAGQHEDdslelqglLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKE 183
Cdd:COG4913 666 AEREIAELEAELERLDASSDDLAALEEQLEE--------LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 184 S--ELKEIEQELHLAQAEIQSLRQAAEDSATEH-ESDIASLQEDLCRMQNELED-MERIRGDYEMEIASLRAEMEmksse 259
Cdd:COG4913 738 AaeDLARLELRALLEERFAAALGDAVERELRENlEERIDALRARLNRAEEELERaMRAFNREWPAETADLDADLE----- 812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767948504 260 psgslglsDYSGLQEELQELRER--YHFLNEEYRALQE-SNSSLTGQLADLESERtQRATER 318
Cdd:COG4913 813 --------SLPEYLALLDRLEEDglPEYEERFKELLNEnSIEFVADLLSKLRRAI-REIKER 865
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
106-251 |
1.36e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 106 TELEELRAQVLQLVAELEETRELAGQHEDDSLE-LQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEIS-------- 176
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLELLEaELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggdrle 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 177 LLEHE---KESELKEIEQE----------LHLA----QAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIR 239
Cdd:COG4913 342 QLEREierLERELEERERRrarleallaaLGLPlpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
170
....*....|..
gi 767948504 240 GDYEMEIASLRA 251
Cdd:COG4913 422 RELEAEIASLER 433
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
86-559 |
1.93e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 86 KGGSVGSLSVNKHRGLSLTETELEELRAQVLQLVAELEETRElagqheddslelqgllederlasaqqaevftkQIQQLQ 165
Cdd:COG4717 61 PQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEE--------------------------------ELEELE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 166 GELRSLREEISLLEHEKesELKEIEQELHLAQAEIQSLRQAAEdSATEHESDIASLQEDLCRMQNELEDMERIRgDYEME 245
Cdd:COG4717 109 AELEELREELEKLEKLL--QLLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEEL-EELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 246 IASLRAEMEMKSSepsgslgLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTL 325
Cdd:COG4717 185 QLSLATEEELQDL-------AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 326 SMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMhgMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKcaqneVLRF 405
Cdd:COG4717 258 LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLL--LAREKASLGKEAEELQALPALEELEEEELEELLA-----ALGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 406 QTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLkmQLQLQTELRQL---------KVMKSTLVENQSEKELLCRLQKLH 476
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALlaeagvedeEELRAALEQAEEYQELKEELEELE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 477 LQhqnvtCEKEKLLERQQQLQEELQCHEAELQHLRDTVASFKESNEKDTETHAQL-QEMKQLyqASKDELERQKHMYDQL 555
Cdd:COG4717 409 EQ-----LEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELeAELEQL--EEDGELAELLQELEEL 481
|
....
gi 767948504 556 EQDL 559
Cdd:COG4717 482 KAEL 485
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
101-252 |
2.29e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 101 LSLTETELEELRAQVLQLVAELEETRELAGQH-------EDDSLELQGLLEDERLASA-QQAEVFTKQIQQLQGELRSLR 172
Cdd:COG3883 60 LEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsGGSVSYLDVLLGSESFSDFlDRLSALSKIADADADLLEELK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 173 EEISLLEhEKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAE 252
Cdd:COG3883 140 ADKAELE-AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-540 |
2.50e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 173 EEISLLEHEKESELKEIEQelhlaQAEIQSLRQAAEDSATEHESDIASLQEDlcRMQNELEDMERIRGDYEMEIASLRAE 252
Cdd:COG1196 189 ERLEDILGELERQLEPLER-----QAEKAERYRELKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 253 MEmkssepsgslglsdysGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERtQRATERWLQSQTlsmtsaes 332
Cdd:COG1196 262 LA----------------ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI-ARLEERRRELEE-------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 333 qtsemdflepdpEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVT 412
Cdd:COG1196 317 ------------RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 413 QNEELksrlcTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELLcrLQKLHLQHQNVTCEKEKLLER 492
Cdd:COG1196 385 AEELL-----EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE--EEEEEEALEEAAEEEAELEEE 457
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 767948504 493 QQQLQEELQCHEAELQHLRDTVASFKESNEKDTETHAQLQEMKQLYQA 540
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
107-415 |
2.88e-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: 43.90 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASaqqaevftkqiQQLQGELRSLREEISLLEhekeSEL 186
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAY-----------GKLRRELAGLTRRLSAAE----GEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 187 KEIEQELHLAQAEIQSLRQAAEDSATEhESDIASLQEDLcrmQNELEDMERIRGDYEMEIASLRAEMEMKSSepsgslgl 266
Cdd:pfam19220 86 EELVARLAKLEAALREAEAAKEELRIE-LRDKTAQAEAL---ERQLAAETEQNRALEEENKALREEAQAAEK-------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 267 sDYSGLQEELQELRERYHFLNEEYRALQESN-------SSLTGQLADLESER-TQRATERWLQSQtLSMTSAESQTSEMD 338
Cdd:pfam19220 154 -ALQRAEGELATARERLALLEQENRRLQALSeeqaaelAELTRRLAELETQLdATRARLRALEGQ-LAAEQAERERAEAQ 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767948504 339 FLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELcceLEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNE 415
Cdd:pfam19220 232 LEEAVEAHRAERASLRMKLEALTARAAATEQL---LAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEAD 305
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
105-616 |
3.30e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 105 ETELEELRAQVLQLVAELE----ETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEH 180
Cdd:pfam15921 259 ELLLQQHQDRIEQLISEHEveitGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 181 EKESELKEIEQELHLAQAEIQSLRQAAEDSATEH---ESDIASLQEDLCRMQNEL---------------------EDME 236
Cdd:pfam15921 339 MYEDKIEELEKQLVLANSELTEARTERDQFSQESgnlDDQLQKLLADLHKREKELslekeqnkrlwdrdtgnsitiDHLR 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 237 RIRGDYEMEIASLRAEMEMKSSEPSGSL--GLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLE-SERTQ 313
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSECQGQMerQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLEsSERTV 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 314 RATERWLQSQTLSMtsaESQTSEMDFLEPDPEMQLLR-QQLRDAEEQMHGMKNKCQELCCELEEL--------------- 377
Cdd:pfam15921 499 SDLTASLQEKERAI---EATNAEITKLRSRVDLKLQElQHLKNEGDHLRNVQTECEALKLQMAEKdkvieilrqqienmt 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 378 ----QHHRQVS--EEEQRRLQRELKCAQNEVLRFQT--SHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTE- 448
Cdd:pfam15921 576 qlvgQHGRTAGamQVEKAQLEKEINDRRLELQEFKIlkDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQEr 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 449 ---LRQLKVMKSTLVENQSEKELLCRlqklhlqhqNVTCEKEKLLERQQQLQEELQCHEAELQHLRDTVASFKESNEKDT 525
Cdd:pfam15921 656 dqlLNEVKTSRNELNSLSEDYEVLKR---------NFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAM 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 526 ETHAQLQEMKQLYQASKDELERQKHMYDQLEQDLLLCQLELKELKAS-----HPIPEDKGKCANKCDTLLSRLTELQEKY 600
Cdd:pfam15921 727 KVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKlsqelSTVATEKNKMAGELEVLRSQERRLKEKV 806
|
570
....*....|....*...
gi 767948504 601 KASQKEM--GQLQMEQCE 616
Cdd:pfam15921 807 ANMEVALdkASLQFAECQ 824
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
107-593 |
3.82e-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: 44.06 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLElQGLLEDERLASAQ-QAEVFTKQIQQLQGELRSLREEISLLEHEKESE 185
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQHGAFLDADIE-TAAADQEQLPSWQsELENLEERLKALTGKHQDVTAKYNRRRSKIKEQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 186 LKEIEQELHLAQAEIqslRQAAEDSATEHESDIASLQEDLcRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLg 265
Cdd:pfam12128 388 NNRDIAGIKDKLAKI---REARDRQLAVAEDDLQALESEL-REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPEL- 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 266 LSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGqLADLESERTQRATERWLQSQtlsmtSAESQTSEMDFLEPDPE 345
Cdd:pfam12128 463 LLQLENFDERIERAREEQEAANAEVERLQSELRQARK-RRDQASEALRQASRRLEERQ-----SALDELELQLFPQAGTL 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 346 MQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQrrlqreLKCAQNEVLRFQTSHSVTQNEELKSRLCTLQ 425
Cdd:pfam12128 537 LHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELN------LYGVKLDLKRIDVPEWAASEEELRERLDKAE 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 426 KKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELlcRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCH-E 504
Cdd:pfam12128 611 EALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARL--DLRRLFDEKQSEKDKKNKALAERKDSANERLNSlE 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 505 AELQHLRDTVASFKESNEKDTETH--AQLQEMKQLYQASKDELERQKH----MYDQLEQDLLLCQLELK-ELKASHPIPE 577
Cdd:pfam12128 689 AQLKQLDKKHQAWLEEQKEQKREArtEKQAYWQVVEGALDAQLALLKAaiaaRRSGAKAELKALETWYKrDLASLGVDPD 768
|
490
....*....|....*.
gi 767948504 578 DKGKCANKCDTLLSRL 593
Cdd:pfam12128 769 VIAKLKREIRTLERKI 784
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
101-296 |
7.30e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 7.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGL-------------LEDERLASAQQAEVFTKQIQQLQGE 167
Cdd:PRK02224 215 LAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLeaeiedlretiaeTEREREELAEEVRDLRERLEELEEE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 168 LRSLREE----------ISLLEHEKESELKEIEQELHLAQAEIQSLRQAAE---DSATEHESDIASLQEDLCRMQNELED 234
Cdd:PRK02224 295 RDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAEslrEDADDLEERAEELREEAAELESELEE 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767948504 235 MERIRGDYEMEIASLRAEMEMKSSE----PSGSLGLSDYSG-LQEELQELRERYHFLNEEYRALQES 296
Cdd:PRK02224 375 AREAVEDRREEIEELEEEIEELRERfgdaPVDLGNAEDFLEeLREERDELREREAELEATLRTARER 441
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
191-317 |
1.01e-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: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 191 QELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLGLSDYS 270
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYE 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 767948504 271 GLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATE 317
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE 139
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
109-295 |
1.97e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 109 EELRAQV--LQLVAELEETRELAGQHEDDSLELQGLLEDERlasaQQAEVFTKQIQQLQGELRSLREEISLLEHEKESEL 186
Cdd:PRK11281 39 ADVQAQLdaLNKQKLLEAEDKLVQQDLEQTLALLDKIDRQK----EETEQLKQQLAQAPAKLRQAQAELEALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 187 KEIEQELHLAQ-----AEIQSLRQAAEDSATEHESDIASLQEDLCRMQNEL-EDMERI---------------------R 239
Cdd:PRK11281 115 RETLSTLSLRQlesrlAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALyANSQRLqqirnllkggkvggkalrpsqR 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767948504 240 GDYEMEIASLRAEMEMKSSEPSGSLGLSDYsgLQEELQELRERYHFLNEEYRALQE 295
Cdd:PRK11281 195 VLLQAEQALLNAQNDLQRKSLEGNTQLQDL--LQKQRDYLTARIQRLEHQLQLLQE 248
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
272-421 |
2.06e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 272 LQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAESQTSEMDflEPDPEMQLLRQ 351
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLD--ASSDDLAALEE 692
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 352 QLRDAEEQMhgmknkcQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNEELKSRL 421
Cdd:COG4913 693 QLEELEAEL-------EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF 755
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
107-401 |
2.70e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.26 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 107 ELEELRAQVLQLVAELEETRELAGQHeDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLrEEISLLEHEKESEL 186
Cdd:pfam05557 22 ELEHKRARIELEKKASALKRQLDRES-DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYL-EALNKKLNEKESQL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 187 KEIEQELHLAQAEIQSLRQAAEDSA---TEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLR-AEMEMKSSEPSG 262
Cdd:pfam05557 100 ADAREVISCLKNELSELRRQIQRAElelQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAeAEQRIKELEFEI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 263 SLGLSDYSGLQE---------ELQELRERYHFLNEEYRALQESNSSLTGQLADLES-------------------ERTQR 314
Cdd:pfam05557 180 QSQEQDSEIVKNskselaripELEKELERLREHNKHLNENIENKLLLKEEVEDLKRklereekyreeaatlelekEKLEQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 315 ATERWL---QSQTLSMTSAESQTSEMDFLEPD-----PEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEE 386
Cdd:pfam05557 260 ELQSWVklaQDTGLNLRSPEDLSRRIEQLQQReivlkEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKA 339
|
330
....*....|....*
gi 767948504 387 EQRRLQRELKCAQNE 401
Cdd:pfam05557 340 LVRRLQRRVLLLTKE 354
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
99-249 |
3.32e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 99 RGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQgllederlASAQQAEVFTKQIQQLQGELRSLREEISLL 178
Cdd:PRK09039 46 REISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLR--------ASLSAAEAERSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767948504 179 EHEKESELKEIEQELHLAQAEIQSLRQaaedsatehesDIASLQEDLCRMQNELEDMERIRGDYEMEIASL 249
Cdd:PRK09039 118 AGELAQELDSEKQVSARALAQVELLNQ-----------QIAALRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
104-402 |
3.87e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 104 TETELEE----LRAQVLQLVAELEETRELAGQHEDDSLELQGLLEderlASAQQAEVFTKQIQQLQGELRSLREEISlle 179
Cdd:TIGR00606 689 TEAELQEfisdLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAP----GRQSIIDLKEKEIPELRNKLQKVNRDIQ--- 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 180 hEKESELKEIEQELHLAQAEiqslrqaaEDSATEHESDIASLQedlcRMQNELEDMERirgdyemeiaslraEMEMKSSE 259
Cdd:TIGR00606 762 -RLKNDIEEQETLLGTIMPE--------EESAKVCLTDVTIME----RFQMELKDVER--------------KIAQQAAK 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 260 PSGSLGLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWlqsqTLSMTSAESQTSEMDF 339
Cdd:TIGR00606 815 LQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKL----QIGTNLQRRQQFEEQL 890
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767948504 340 LEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRqvsEEEQRRLQRELKCAQNEV 402
Cdd:TIGR00606 891 VELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSK---ETSNKKAQDKVNDIKEKV 950
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
106-224 |
4.62e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.45 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 106 TELEELRAQVLQLVAELEEtrelagqheddslelqgLLEDERLASAQQAEVFTKQIQQLQGELRSLREEislLEHEKE-- 183
Cdd:COG0542 411 EELDELERRLEQLEIEKEA-----------------LKKEQDEASFERLAELRDELAELEEELEALKAR---WEAEKEli 470
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 767948504 184 SELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQED 224
Cdd:COG0542 471 EEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
105-623 |
5.01e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.34 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 105 ETELEELRAQVLQLVAELEETRELAGQHED--DSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEK 182
Cdd:TIGR00618 337 QSSIEEQRRLLQTLHSQEIHIRDAHEVATSirEISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRT 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 183 ESE------LKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQE----------DLCRMQNELEDMERI---RGDYE 243
Cdd:TIGR00618 417 SAFrdlqgqLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQEsaqslkereqQLQTKEQIHLQETRKkavVLARL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 244 MEIASLRAEMEMKSSEPSGSLGLSDYSG-LQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESE--RTQRATERWL 320
Cdd:TIGR00618 497 LELQEEPCPLCGSCIHPNPARQDIDNPGpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQmqEIQQSFSILT 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 321 QSQTLSMTSAESQTSEMDFLEPDPEMQllrqqlrDAEEQMHGMKNKCQELccELEELQHHRQVSEEEQRRLQRElkcAQN 400
Cdd:TIGR00618 577 QCDNRSKEDIPNLQNITVRLQDLTEKL-------SEAEDMLACEQHALLR--KLQPEQDLQDVRLHLQQCSQEL---ALK 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 401 EVLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQ 480
Cdd:TIGR00618 645 LTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIE 724
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 481 NVTCEKEKLLERQQQLQEELQcheAELQHLRDTV--ASFKESNEKDTETHAQLQEMKQLYQASKDELERQKhmydQLEQD 558
Cdd:TIGR00618 725 NASSSLGSDLAAREDALNQSL---KELMHQARTVlkARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNR----LREED 797
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767948504 559 lllcQLELKELKASHP--IPEDKGKCANKCDTLLSRLTELQEKYKASQKEMGQLQMEQCELLEDQRR 623
Cdd:TIGR00618 798 ----THLLKTLEAEIGqeIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
104-209 |
6.30e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 104 TETELEELRAQVLQLvaeleETRELAGQHEDDSLELQGLLEDERLASAQQaevFTKQIQQLQGELRSLREEISLLEHEKE 183
Cdd:PRK04863 584 LRQQLEQLQARIQRL-----AARAPAWLAAQDALARLREQSGEEFEDSQD---VTEYMQQLLERERELTVERDELAARKQ 655
|
90 100
....*....|....*....|....*.
gi 767948504 184 SELKEIEQELHLAQAEIQSLRQAAED 209
Cdd:PRK04863 656 ALDEEIERLSQPGGSEDPRLNALAER 681
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-638 |
6.43e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.04 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEvftkQIQQLQGELRSLREEISLLEH 180
Cdd:TIGR02168 227 LALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE----EIEELQKELYALANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 181 EKE---SELKEIEQELHLAQAEIQSLRQA---AEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEME 254
Cdd:TIGR02168 303 QKQilrERLANLERQLEELEAQLEELESKldeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 255 MKSSEpSGSLGLSDYSgLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERwlQSQTLSMTSAESQT 334
Cdd:TIGR02168 383 TLRSK-VAQLELQIAS-LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE--LEEELEELQEELER 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 335 SEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQ-HHRQVSEEEQRRLQR---------------ELKCA 398
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgFSEGVKALLKNQSGLsgilgvlselisvdeGYEAA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 399 QNEVLR--------------FQTSHSVTQNEELKSRLCTL-QKKYDTSQDEQNELLKMQ---LQLQTELRQLKVMKSTLV 460
Cdd:TIGR02168 539 IEAALGgrlqavvvenlnaaKKAIAFLKQNELGRVTFLPLdSIKGTEIQGNDREILKNIegfLGVAKDLVKFDPKLRKAL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 461 EN--------QSEKELLCRLQKLHLQHQNVTCEKEKLLER------QQQLQEELQCHEAELQHLRDTVASFKESNEkdtE 526
Cdd:TIGR02168 619 SYllggvlvvDDLDNALELAKKLRPGYRIVTLDGDLVRPGgvitggSAKTNSSILERRREIEELEEKIEELEEKIA---E 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 527 THAQLQEMKQLYQASKDELERQKHMYDQLEQDLLLCQLELKELKASHPIPEDK--------GKCANKCDTLLSRLTELQE 598
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlskelTELEAEIEELEERLEEAEE 775
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 767948504 599 KYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELHRL 638
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
162-259 |
7.23e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 39.93 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 162 QQLQGELRSLREEISLLEHEKESELKEIEQElhlaqaeiQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGD 241
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQ--------QQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQ 216
|
90
....*....|....*...
gi 767948504 242 YEMEIASlRAEMEMKSSE 259
Cdd:PRK11448 217 KRKEITD-QAAKRLELSE 233
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
244-460 |
8.27e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 244 MEIASLRAEMEM--KSSEPSGSLGLSDYSGLQEELQELRERyhflNEEYRALQESNSSLTGQLADLESERTQRATERWLQ 321
Cdd:COG4717 46 MLLERLEKEADElfKPQGRKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948504 322 SQTLsmtsaesqtsemDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNE 401
Cdd:COG4717 122 EKLL------------QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767948504 402 VLRfQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNEL------LKMQLQLQTELRQLKVMKSTLV 460
Cdd:COG4717 190 TEE-ELQDLAEELEELQQRLAELEEELEEAQEELEELeeeleqLENELEAAALEERLKEARLLLL 253
|
|
| |
