|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
84-405 |
5.10e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.55 E-value: 5.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 84 VQKGGSVGSLSVNKHRGLSLTETELEELRAQVLQLVAELEETR----ELAGQHEDDSLELQGLLEDERLASAQ------Q 153
Cdd:TIGR02168 655 VRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEkalaELRKELEELEEELEQLRKELEELSRQisalrkD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 154 AEVFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQ---ELHLAQAEIQSLRQAAEDSATEH---ESDIASLQEDLCR 227
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeELAEAEAEIEELEAQIEQLKEELkalREALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 228 MQNELEDMERIRGDYEMEIASLRAEMEMkssepsgslglsdysgLQEELQELRERYHFLNEEYRALQESNSSLTGQLADL 307
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLED----------------LEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 308 ESERTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELC--------CELEELQH 379
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerlseeysLTLEEAEA 958
|
330 340
....*....|....*....|....*.
gi 767948502 380 HRQVSEEEQRRLQRELKCAQNEVLRF 405
Cdd:TIGR02168 959 LENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
101-359 |
1.33e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 101 LSLTETELEELRAQVLQLVAELEETRElagQHEDDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELRSLREEISlleh 180
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRL---ELEELELELEEAQAEEYELLAELARL-EQDIARLEERRRELEERLE---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 181 EKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEp 260
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL- 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 261 sgslgLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERwLQSQTLSMTSAESQTSEMDfl 340
Cdd:COG1196 399 -----AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE-AELEEEEEALLELLAELLE-- 470
|
250
....*....|....*....
gi 767948502 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 |
9.58e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.24 E-value: 9.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEvftKQIQQLQGELRSLREEISLLE---HEKE 183
Cdd:TIGR02169 188 RLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALE---RQKEAIERQLASLEEELEKLTeeiSELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 184 SELKEIEQELHLAQAEIQSL-----RQAAEDSAtEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEmkss 258
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIG-ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE---- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 259 epsgslglsdysGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLEsERTQRATERWLQSQT-LSMTSAESQTSEM 337
Cdd:TIGR02169 340 ------------ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD-KEFAETRDELKDYREkLEKLKREINELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 338 DFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNE-- 415
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEls 486
|
330 340
....*....|....*....|..
gi 767948502 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 |
4.28e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 160 QIQQLQGELRSLREEISLLE---HEKESELKEIEQELHLAQAEIQSLRQAAEDSATEhesdIASLQEDLCRMQNELEDME 236
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEekiAELEKALAELRKELEELEEELEQLRKELEELSRQ----ISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 237 RIRGDYEMEIASLRAEMEmkssepsgsLGLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQraT 316
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIE---------ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL--L 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 317 ERWLQSQTLSMTSAESQTSEMdflepDPEMQLLRQQLRDAEEQMhgmknkcqelccelEELQHHRQVSEEEQRRLQRELK 396
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAAT-----ERRLEDLEEQIEELSEDI--------------ESLAAEIEELEELIEELESELE 876
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767948502 397 CAQNEVlrfqtshsvtqnEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKEL 468
Cdd:TIGR02168 877 ALLNER------------ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV 936
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-702 |
7.68e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 7.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQqaevFTKQIQQLQGELRSLREEISLLEH 180
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ----LELQIASLNNEIERLEARLERLED 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 181 EKESELKEIEQ--------ELHLAQAEIQSLRQAAEDSATEHEsdiaSLQEDLCRMQNELEDMERIRGDYEMEIASLRAE 252
Cdd:TIGR02168 415 RRERLQQEIEEllkkleeaELKELQAELEELEEELEELQEELE----RLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 253 MEMkssepsgslglsdysglqeeLQELRERYHFLNEEYRALQESNSSLTG---QLADLES--ERTQRATERWLQS--QTL 325
Cdd:TIGR02168 491 LDS--------------------LERLQENLEGFSEGVKALLKNQSGLSGilgVLSELISvdEGYEAAIEAALGGrlQAV 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 326 SMTSAESQTSEMDFLEPD--------PEMQLLRQQLRDAEEQMHGMKNKCQELCCELEE------------LQHHRQVSE 385
Cdd:TIGR02168 551 VVENLNAAKKAIAFLKQNelgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKfdpklrkalsylLGGVLVVDD 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 386 EEQ-RRLQRELKCAQNEVL---------------RFQTSHSVTQN----EELKSRLCTLQKKYDTSQDEQNELLKMQLQL 445
Cdd:TIGR02168 631 LDNaLELAKKLRPGYRIVTldgdlvrpggvitggSAKTNSSILERrreiEELEEKIEELEEKIAELEKALAELRKELEEL 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 446 QTELRQLKVM------------KSTLVENQSEKELLCRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCHEAELQHLRDT 513
Cdd:TIGR02168 711 EEELEQLRKEleelsrqisalrKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 514 VASFKESNEKDTETHAQLQEMkqlYQASKDELERQKHMYDQLEQDLLLCQLELKELKASHPIPEDKGKCANK-------- 585
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAE---LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAeieeleel 867
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 586 CDTLLSRLTELQEKYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPKSGLLLKS--QELLTKLEDLCE 663
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGleVRIDNLQERLSE 947
|
650 660 670
....*....|....*....|....*....|....*....
gi 767948502 664 lqlLYQGMQEEqkkLIQNQDCVLKEQLEIHEELRRFKES 702
Cdd:TIGR02168 948 ---EYSLTLEE---AEALENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
153-467 |
8.29e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 8.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 153 QAEVFTKQIQQLQGELRSLREEISllehEKESELKEIEQELHLAQAEIQSLRqaaeDSATEHESDIASLQEDLCRMQNEL 232
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELK----EAEEELEELTAELQELEEKLEELR----LEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 233 EDMERirgdyemEIASLRAEMEMKSSEpsgslglsdYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESErt 312
Cdd:TIGR02168 298 SRLEQ-------QKQILRERLANLERQ---------LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE-- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 313 qraterwlqsqtLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQ 392
Cdd:TIGR02168 360 ------------LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767948502 393 RELKCAQNEVLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKE 467
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
108-361 |
7.98e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 7.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 108 LEELRAQVLQLVAELEETRELAGQHEDdsleLQGLLEDERLASAQQAEVFTKQI--QQLQGELRSLREEISLLEhEKESE 185
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEA----ELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLD-ASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 186 LKEIEQELHLAQAEIQSLRQ---AAEDSATEHESDIASLQEDLCRMQNELEDMERI-RGDYEMEIASLRAEMEMKSSEPS 261
Cdd:COG4913 687 LAALEEQLEELEAELEELEEeldELKGEIGRLEKELEQAEEELDELQDRLEAAEDLaRLELRALLEERFAAALGDAVERE 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 262 GSLGLSD-YSGLQEELQELRER-----------YHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTs 329
Cdd:COG4913 767 LRENLEErIDALRARLNRAEEEleramrafnreWPAETADLDADLESLPEYLALLDRLEEDGLPEYEERFKELLNENSI- 845
|
250 260 270
....*....|....*....|....*....|..
gi 767948502 330 aESQTsemDFLepdpemQLLRQQLRDAEEQMH 361
Cdd:COG4913 846 -EFVA---DLL------SKLRRAIREIKERID 867
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
98-254 |
8.69e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 8.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 98 HRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDdslELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISL 177
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALRE---ELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 178 LEH----------EKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIA 247
Cdd:COG4913 364 LEAllaalglplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
....*..
gi 767948502 248 SLRAEME 254
Cdd:COG4913 444 ALRDALA 450
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
148-378 |
2.65e-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: 57.08 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 148 LASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKES---ELKEIEQELHLAQAEIQSLrqaaEDSATEHESDIASLQED 224
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAllkQLAALERRIAALARRIRAL----EQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 225 LCRMQNELEDMERirgdyemEIASLRAEMEMKSSEPSGSLGLSdysglQEELQELRERYHFLNEEYRALQESNSSLTGQL 304
Cdd:COG4942 92 IAELRAELEAQKE-------ELAELLRALYRLGRQPPLALLLS-----PEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767948502 305 ADLESERTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQ 378
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-314 |
3.35e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDerlaSAQQAEVFTKQIQQLQGELRSLREEISlleh 180
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED----LEEQIEELSEDIESLAAEIEELEELIE---- 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 181 EKESELKEIEQELHLAQAEIQSLRQAAEDSAT---EHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASL------RA 251
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEelrELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLqerlseEY 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 252 EMEMKSSEPSGSLGLSDYSGLQ---------------------EELQELRERYHFLNEEYRALQESNSSLTGQLADLESE 310
Cdd:TIGR02168 950 SLTLEEAEALENKIEDDEEEARrrlkrlenkikelgpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDRE 1029
|
....
gi 767948502 311 RTQR 314
Cdd:TIGR02168 1030 ARER 1033
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
163-490 |
3.60e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.77 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 163 QLQGELRSLREEISLLEHEKES---ELKEIEQELHlaqaEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIR 239
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSlqsELRRIENRLD----ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 240 GDYEMEIASLRAEMEMKSSEpsgslgLSDY----SGLQEELQEL-----RERYHFLNEEYRALQESNSSLTGQLADLESE 310
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEAR------IEELeedlHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 311 RTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRR 390
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 391 LQRELK--CAQNEVLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELL---KMQLQLQTELRQLKVMKS-TLVENQS 464
Cdd:TIGR02169 901 LERKIEelEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELsleDVQAELQRVEEEIRALEPvNMLAIQE 980
|
330 340
....*....|....*....|....*.
gi 767948502 465 EKELLCRLQKLHLQHQNVTCEKEKLL 490
Cdd:TIGR02169 981 YEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
105-407 |
8.36e-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: 8.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 105 ETELEELRAQVLQLVAELEETRelAGQHEDDslelqgllederlasaqqaevftKQIQQLQGELRSLREEISLLEHEKEs 184
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELR--LEVSELE-----------------------EEIEELQKELYALANEISRLEQQKQ- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 185 elkEIEQELHLAQAEIQSLrqaaEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMkssepsgsl 264
Cdd:TIGR02168 306 ---ILRERLANLERQLEEL----EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE--------- 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 265 glsdysgLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLES--ERTQRATERWLQSQtlsmTSAESQTSEMDFLEP 342
Cdd:TIGR02168 370 -------LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEArlERLEDRRERLQQEI----EELLKKLEEAELKEL 438
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767948502 343 DPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQT 407
Cdd:TIGR02168 439 QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
107-537 |
1.53e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEhEKESEL 186
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE-EALAEL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 187 KEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLGL 266
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 267 SDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEM 346
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALA 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 347 QLLRQQLRDAEEqmhgmknkcQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNEELKSRlctLQK 426
Cdd:COG1196 594 RGAIGAAVDLVA---------SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA---GGS 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 427 KYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCHEAE 506
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
410 420 430
....*....|....*....|....*....|.
gi 767948502 507 LQHLRDTVASFKESNEKDTETHAQLQEMKQL 537
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLEELERELERL 772
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
105-310 |
2.33e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 105 ETELEELRAQVLQLVAELEETRElagQHEDDSLELQGLLEDERLASAQQaevftkQIQQLQGELRSLREEISLLEHEKES 184
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQ---KNGLVDLSEEAKLLLQQLSELES------QLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 185 ELKEIEQELhlAQAEIQSLRQAAEDSatehESDIASLQEdlcRMQNELEDMERIRGdyemEIASLRAEMEMKSSEPSGSL 264
Cdd:COG3206 252 GPDALPELL--QSPVIQQLRAQLAEL----EAELAELSA---RYTPNHPDVIALRA----QIAALRAQLQQEAQRILASL 318
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767948502 265 GlSDYSGLQEELQELRERYhflnEEYRALQESNSSLTGQLADLESE 310
Cdd:COG3206 319 E-AELEALQAREASLQAQL----AQLEARLAELPELEAELRRLERE 359
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
107-333 |
2.68e-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: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 107 ELEELRAQVLQLVAELEETRELAGQhEDDSLELQGLLEDERLASAQQaevftkQIQQLQGELRSLREEisllEHEKESEL 186
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEE-ELAELEEELEELEEELEELEE------ELEEAEEELEEAEAE----LAEAEEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 187 KEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEpsgslgL 266
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE------E 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767948502 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 |
7.43e-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: 53.53 E-value: 7.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 110 ELRAQVLQLVAELEE-TRELAG-QHEDDSLE-LQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISllehEKESEL 186
Cdd:TIGR02169 671 SEPAELQRLRERLEGlKRELSSlQSELRRIEnRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE----ELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 187 KEIEQELHLAQAEIQSLrqaaedsatehESDIASLQEDLCRMQNELEDMERirgdyemeiaslraememkssepsgslgl 266
Cdd:TIGR02169 747 SSLEQEIENVKSELKEL-----------EARIEELEEDLHKLEEALNDLEA----------------------------- 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 267 sdysglqeelQELRERYHFLNEEYRALQESNSSLTGQLADLESErtqraterwLQSQTLSMTSAESqtsemdflepdpEM 346
Cdd:TIGR02169 787 ----------RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQK---------LNRLTLEKEYLEK------------EI 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 347 QLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQtshsvTQNEELKSRLCTLQK 426
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE-----AQLRELERKIEELEA 910
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767948502 427 KYDTSQDEQNELlkmQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCEKEK 488
Cdd:TIGR02169 911 QIEKKRKRLSEL---KAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRA 969
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
154-400 |
9.61e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 9.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 154 AEVFTKQ-IQQLQGELRSLREEIsllehekESELKEIEQELHLAQAEIQSLRQ-----AAEDSATEHESDIASLQEDLCR 227
Cdd:COG3206 158 AEAYLEQnLELRREEARKALEFL-------EEQLPELRKELEEAEAALEEFRQknglvDLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 228 MQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLGLSDYSGLQEELQELRERYHFLNEEYRALQEsnssltgQLADL 307
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRA-------QIAAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 308 ESERTQRATERWLQSQTlsmtsaesqtsemdflepdpEMQLLRQQLRDAEEQMHGMKNKCQELcceleelqhhrQVSEEE 387
Cdd:COG3206 304 RAQLQQEAQRILASLEA--------------------ELEALQAREASLQAQLAQLEARLAEL-----------PELEAE 352
|
250
....*....|...
gi 767948502 388 QRRLQRELKCAQN 400
Cdd:COG3206 353 LRRLEREVEVARE 365
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
105-246 |
2.06e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 105 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDerlASAQQAEVFT-KQIQQLQGELRSLREEISLLEheke 183
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK---YEEQLGNVRNnKEYEALQKEIESLKRRISDLE---- 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767948502 184 SELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEI 246
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
185-395 |
2.71e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 185 ELKEIEQELHLAQAEIQSLRQAAEDsATEHESDIASLQE-DLCRMQNELEDMERIRGDYEMEIASLRAEMEmkssepsgs 263
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIREL-AERYAAARERLAElEYLRAALRLWFAQRRLELLEAELEELRAELA--------- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 264 lglsdysGLQEELQELRERYHFLNEEYRALQE---SNS-----SLTGQLADLESERTQRATERWLQSQTLSMTSAESQTS 335
Cdd:COG4913 306 -------RLEAELERLEARLDALREELDELEAqirGNGgdrleQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767948502 336 EMDFLE-----------PDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQREL 395
Cdd:COG4913 379 AEEFAAlraeaaalleaLEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
107-314 |
3.04e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKESEL 186
Cdd:COG1196 621 TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 187 KEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERI---------RGDYEMEIASLRAEMEmks 257
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAleelpeppdLEELERELERLEREIE--- 777
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767948502 258 sepsgSLG----LSDysglqEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQR 314
Cdd:COG1196 778 -----ALGpvnlLAI-----EEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
99-255 |
3.67e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.01 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 99 RGLSLtETELEELRAQVLqlvAELEETRELAGQHEDDSLELqgllEDERlasaqqaevftkqIQQLQGELRSLREEISLL 178
Cdd:COG2433 374 RGLSI-EEALEELIEKEL---PEEEPEAEREKEHEERELTE----EEEE-------------IRRLEEQVERLEAEVEEL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 179 E---HEKESELKEIEQELHLAQAEiqslrqaaEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEM 255
Cdd:COG2433 433 EaelEEKDERIERLERELSEARSE--------ERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKL 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
108-807 |
4.77e-06 |
|
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: 50.83 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 108 LEELRAQV--LQLVAEL-EETRELAGQHEDDSLELQGL----LEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLE- 179
Cdd:TIGR02168 195 LNELERQLksLERQAEKaERYKELKAELRELELALLVLrleeLREELEELQEELKEAEEELEELTAELQELEEKLEELRl 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 180 --HEKESELKEIEQELHLAQAEIQSLRQAAEdsatEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKS 257
Cdd:TIGR02168 275 evSELEEEIEELQKELYALANEISRLEQQKQ----ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 258 SEpsgslglsdYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAESQTSEM 337
Cdd:TIGR02168 351 EE---------LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 338 DFLEPDPEMQllrqqlrdaEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNEel 417
Cdd:TIGR02168 422 EIEELLKKLE---------EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR-- 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 418 KSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKvmKSTLVENQSEKELLCRLQKlHLQhqNVTCEKEKLLERQQQLQ 497
Cdd:TIGR02168 491 LDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLS--ELISVDEGYEAAIEAALGG-RLQ--AVVVENLNAAKKAIAFL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 498 EELQCHEAELQHLRDTVASFKESNEKDTETH--------AQLQEMKQLYQASKDELERQKHMYDQLEQDLLLcqleLKEL 569
Cdd:TIGR02168 566 KQNELGRVTFLPLDSIKGTEIQGNDREILKNiegflgvaKDLVKFDPKLRKALSYLLGGVLVVDDLDNALEL----AKKL 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 570 KASHPIPEDKGKCANKC-----------DTLLSR---LTELQEKYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEEL 635
Cdd:TIGR02168 642 RPGYRIVTLDGDLVRPGgvitggsaktnSSILERrreIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 636 HRLTlplPKSGLLLKSQELLTK----LEDLCELQLLYQGMQEEQKKLIQNQDCVLKEQLEIHEELRRFKESHFQEVLENP 711
Cdd:TIGR02168 722 EELS---RQISALRKDLARLEAeveqLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 712 DDSKLAKSSKCNRNK-------QPRSQAQHAQRPDSELGQEIQELI-QSKLLMEQMQALQVMYDAGQAKQELLQQEQGRL 783
Cdd:TIGR02168 799 KALREALDELRAELTllneeaaNLRERLESLERRIAATERRLEDLEeQIEELSEDIESLAAEIEELEELIEELESELEAL 878
|
730 740
....*....|....*....|....
gi 767948502 784 LEERKRLQADLQLCLEEMQLLQVQ 807
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEE 902
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
110-465 |
5.13e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.82 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 110 ELRAQvlqLVAELEETRELAGQHEDDSLElQGLLEderlASAQQAEVfTKQIQQLQGELRSLREEISLL---EHEKESEL 186
Cdd:PRK10929 83 ELRQQ---LNNERDEPRSVPPNMSTDALE-QEILQ----VSSQLLEK-SRQAQQEQDRAREISDSLSQLpqqQTEARRQL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 187 KEIEQELHLAQAEIQSLRQAAedsatehesdIASLQEDLCRMQ---NELEdMERIRGDYEMEIASLRAEMEMKSSEPsgs 263
Cdd:PRK10929 154 NEIERRLQTLGTPNTPLAQAQ----------LTALQAESAALKalvDELE-LAQLSANNRQELARLRSELAKKRSQQ--- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 264 lglsdysgLQEELQELRERYHFL--NEEYRALqESNSSLTGQLADL-ESERTQRATERWLqSQTLSmtsaeSQTSEMDFL 340
Cdd:PRK10929 220 --------LDAYLQALRNQLNSQrqREAERAL-ESTELLAEQSGDLpKSIVAQFKINREL-SQALN-----QQAQRMDLI 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 341 -----EPDPEMQLLRQQLRDAEEQMH--GMKN-----------------KCQELCCELEELQHHRQVSEEEQRRLQRELK 396
Cdd:PRK10929 285 asqqrQAASQTLQVRQALNTLREQSQwlGVSNalgealraqvarlpempKPQQLDTEMAQLRVQRLRYEDLLNKQPQLRQ 364
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767948502 397 CAQNEvlrfqtSHSVTQNEelksrlctlQKKYDTSQDEQNELLKMQLQ----LQTELRQLKVMKSTLVENQSE 465
Cdd:PRK10929 365 IRQAD------GQPLTAEQ---------NRILDAQLRTQRELLNSLLSggdtLILELTKLKVANSQLEDALKE 422
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
101-467 |
8.14e-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: 50.17 E-value: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLE- 179
Cdd:pfam01576 150 LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQa 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 180 --HEKESELKEIEQELHLAQAEI---QSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEME 254
Cdd:pfam01576 230 qiAELRAQLAKKEEELQAALARLeeeTAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 255 mkssepsgslGLSDYSGLQEELQELRERYhfLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAE--- 331
Cdd:pfam01576 310 ----------DTLDTTAAQQELRSKREQE--VTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANlek 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 332 -SQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVlrfqtSHS 410
Cdd:pfam01576 378 aKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLL-----NEA 452
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 767948502 411 VTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKE 467
Cdd:pfam01576 453 EGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEE 509
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
158-395 |
1.11e-05 |
|
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: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 158 TKQIQQLQGELRSLREEISLLEhekeSELKEIEQELHLAQAEIQSLRQAAEDSatEHESDIASLQEDLCRMQNELEDMER 237
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAE----ERLEALEAELDALQERREALQRLAEYS--WDEIDVASAEREIAELEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 238 irgdyemeiaslraememkssepsgslGLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQrate 317
Cdd:COG4913 683 ---------------------------SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE---- 731
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767948502 318 rwLQSQTLSMTSAESQTSEMDFLEpdpemQLLRQQLRDAEEQMHgmknkcqelccelEELQHHRQVSEEEQRRLQREL 395
Cdd:COG4913 732 --LQDRLEAAEDLARLELRALLEE-----RFAAALGDAVERELR-------------ENLEERIDALRARLNRAEEEL 789
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
101-428 |
1.42e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISlleh 180
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE---- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 181 EKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASL---------RA 251
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLlallflllaRE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 252 EMEMKSSEPSGSLGLSDYSGLQEELQELRERYHFL----NEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSM 327
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEELLAALGLPpdlsPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 328 TSAESQTSEM--DFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCC---------ELEELQHHRQVSEEEQRRLQRELK 396
Cdd:COG4717 377 AEAGVEDEEElrAALEQAEEYQELKEELEELEEQLEELLGELEELLEaldeeeleeELEELEEELEELEEELEELREELA 456
|
330 340 350
....*....|....*....|....*....|....*.
gi 767948502 397 CAQNEVLRFQTSHSVTQN----EELKSRLCTLQKKY 428
Cdd:COG4717 457 ELEAELEQLEEDGELAELlqelEELKAELRELAEEW 492
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
99-263 |
1.72e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 99 RGLSLTETELEELRAQVLQLVAELEETREL----------AGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGEL 168
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEElaellralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 169 RSLREEISLLEHEKESELKEIEQELHLAQAEIQSLRQAAEdsatEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIAS 248
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKA----ERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
170
....*....|....*
gi 767948502 249 LRAEMEMKSSEPSGS 263
Cdd:COG4942 232 LEAEAAAAAERTPAA 246
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
101-237 |
2.07e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSlELQGLLEDERLASAQQAEV---FTK---QIQQLQGELRSLREE 174
Cdd:COG3206 228 LAEARAELAEAEARLAALRAQLGSGPDALPELLQSP-VIQQLRAQLAELEAELAELsarYTPnhpDVIALRAQIAALRAQ 306
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767948502 175 IsllEHEKESELKEIEQELHLAQAEIQSLRQAAEdsatEHESDIASLQEDlcrmQNELEDMER 237
Cdd:COG3206 307 L---QQEAQRILASLEAELEALQAREASLQAQLA----QLEARLAELPEL----EAELRRLER 358
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
86-559 |
2.50e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 86 KGGSVGSLSVNKHRGLSLTETELEELRAQVLQLVAELEETRelagqheddslelqglledERLASAQQaevftkQIQQLQ 165
Cdd:COG4717 61 PQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELE-------------------EELEELEA------ELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 166 GELRSLREEISLLEHEKesELKEIEQELHLAQAEIQSLRQAAEDSAtEHESDIASLQEDLCRMQNELEDmerirgdyEME 245
Cdd:COG4717 116 EELEKLEKLLQLLPLYQ--ELEALEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEELEE--------LLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 246 IASLRAEMEMKSSepsgslgLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTL 325
Cdd:COG4717 185 QLSLATEEELQDL-------AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 326 SMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMhgMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKcaqneVLRF 405
Cdd:COG4717 258 LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLL--LAREKASLGKEAEELQALPALEELEEEELEELLA-----ALGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 406 QTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLkmQLQLQTELRQLkvMKSTLVEN-----------QSEKELLCRLQK 474
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAAL--LAEAGVEDeeelraaleqaEEYQELKEELEE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 475 LHLQhqnvtCEKEKLLERQQQLQEELQCHEAELQHLRDTVASFKESNEKDTETHAQL-QEMKQLyqASKDELERQKHMYD 553
Cdd:COG4717 407 LEEQ-----LEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELeAELEQL--EEDGELAELLQELE 479
|
....*.
gi 767948502 554 QLEQDL 559
Cdd:COG4717 480 ELKAEL 485
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
107-415 |
3.14e-05 |
|
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: 47.37 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASaqqaevftkqiQQLQGELRSLREEISLLEhekeSEL 186
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAY-----------GKLRRELAGLTRRLSAAE----GEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 187 KEIEQELHLAQAEIQSLRQAAEDSATEhESDIASLQEDLcrmQNELEDMERIRGDYEMEIASLRAEMEMKSSepsgslgl 266
Cdd:pfam19220 86 EELVARLAKLEAALREAEAAKEELRIE-LRDKTAQAEAL---ERQLAAETEQNRALEEENKALREEAQAAEK-------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 267 sDYSGLQEELQELRERYHFLNEEYRALQ----ESN---SSLTGQLADLESER-TQRATERWLQSQtLSMTSAESQTSEMD 338
Cdd:pfam19220 154 -ALQRAEGELATARERLALLEQENRRLQalseEQAaelAELTRRLAELETQLdATRARLRALEGQ-LAAEQAERERAEAQ 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767948502 339 FLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELcceLEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNE 415
Cdd:pfam19220 232 LEEAVEAHRAERASLRMKLEALTARAAATEQL---LAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEAD 305
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
140-453 |
4.60e-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: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 140 QGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQELHLAQAEiqSLRQAAEDSA----TEHE 215
Cdd:pfam17380 263 QTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAE--KARQAEMDRQaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 216 SDIASLQEDLCRMQNE--LEDMERIRG-DYEMEIASLRA------EMEMKSSEPSGSL-GLSDYSGLQEELQELRERYHF 285
Cdd:pfam17380 341 RMAMERERELERIRQEerKRELERIRQeEIAMEISRMRElerlqmERQQKNERVRQELeAARKVKILEEERQRKIQQQKV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 286 LNEEYRALQESNSSLTGQLADLESERT-----QRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQL--------LRQQ 352
Cdd:pfam17380 421 EMEQIRAEQEEARQREVRRLEEERAREmervrLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRaeeqrrkiLEKE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 353 LRDAEEQMHGMKNKCQELCCELEELQhhRQVSEEEQRRLQRELKCAQNEV-LRFQTSHSVTQNEELKSRLCTLQKKYD-T 430
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKEMEERQ--KAIYEEERRREAEEERRKQQEMeERRRIQEQMRKATEERSRLEAMEREREmM 578
|
330 340
....*....|....*....|...
gi 767948502 431 SQDEQNELLKMQLQLQTELRQLK 453
Cdd:pfam17380 579 RQIVESEKARAEYEATTPITTIK 601
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
104-318 |
4.61e-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: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 104 TETELEELRAQVLQLVAELEETRELAGQHEDdslelqglLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKE 183
Cdd:COG4913 666 AEREIAELEAELERLDASSDDLAALEEQLEE--------LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 184 S--ELKEIEQELHLAQAEIQSLRQAAEDSATEH-ESDIASLQEDLCRMQNELED-MERIRGDYEMEIASLRAEMEmksse 259
Cdd:COG4913 738 AaeDLARLELRALLEERFAAALGDAVERELRENlEERIDALRARLNRAEEELERaMRAFNREWPAETADLDADLE----- 812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767948502 260 psgslglsDYSGLQEELQELRER--YHFLNEEYRALQE-SNSSLTGQLADLESERtQRATER 318
Cdd:COG4913 813 --------SLPEYLALLDRLEEDglPEYEERFKELLNEnSIEFVADLLSKLRRAI-REIKER 865
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-790 |
5.33e-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: 47.36 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEvftkQIQQLQGELRSLREEISLLEH 180
Cdd:TIGR02168 227 LALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE----EIEELQKELYALANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 181 EKE---SELKEIEQELHLAQAEIQSLRQA---AEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEME 254
Cdd:TIGR02168 303 QKQilrERLANLERQLEELEAQLEELESKldeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 255 MKSSEpSGSLGLSDYSgLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERwlQSQTLSMTSAESQT 334
Cdd:TIGR02168 383 TLRSK-VAQLELQIAS-LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE--LEEELEELQEELER 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 335 SEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQ-HHRQVSEEEQRRLQR---------------ELKCA 398
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgFSEGVKALLKNQSGLsgilgvlselisvdeGYEAA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 399 QNEVLR--------------FQTSHSVTQNEELKSRLCTL-QKKYDTSQDEQNELLKMQ---LQLQTELRQLKVMKSTLV 460
Cdd:TIGR02168 539 IEAALGgrlqavvvenlnaaKKAIAFLKQNELGRVTFLPLdSIKGTEIQGNDREILKNIegfLGVAKDLVKFDPKLRKAL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 461 EN--------QSEKELLCRLQKLHLQHQNVTCEKEKLLER------QQQLQEELQCHEAELQHLRDTVASFKESNEkdtE 526
Cdd:TIGR02168 619 SYllggvlvvDDLDNALELAKKLRPGYRIVTLDGDLVRPGgvitggSAKTNSSILERRREIEELEEKIEELEEKIA---E 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 527 THAQLQEMKQLYQASKDELERQKHMYDQLEQDLLLCQLELKELKASHPIPEDK--------GKCANKCDTLLSRLTELQE 598
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlskelTELEAEIEELEERLEEAEE 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 599 KYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPKSGLLLKS------------QELLTKLEDLCELQL 666
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESlerriaaterrlEDLEEQIEELSEDIE 855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 667 LYQGMQEEQKKLIQNqdcvLKEQLEIHEELRRFKESHFQEVLENPDDSKLAKSSKCNRNKQPRSQAQHAQRPDSELGQEI 746
Cdd:TIGR02168 856 SLAAEIEELEELIEE----LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 767948502 747 QEL------IQSKLLMEQ---MQALQVMYDAGQAKQELLQQEQGRLLEERKRL 790
Cdd:TIGR02168 932 EGLevridnLQERLSEEYsltLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
106-251 |
6.04e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 106 TELEELRAQVLQLVAELEETRELAGQHEDDSLE-LQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEIS-------- 176
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLELLEaELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggdrle 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 177 LLEHE---KESELKEIEQE----------LHLA----QAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIR 239
Cdd:COG4913 342 QLEREierLERELEERERRrarleallaaLGLPlpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
170
....*....|..
gi 767948502 240 GDYEMEIASLRA 251
Cdd:COG4913 422 RELEAEIASLER 433
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
105-469 |
6.19e-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: 46.94 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 105 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQaevfTKQIQQLQGELRSLREEISLLEHEKE- 183
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN----NKKIKELEKQLNQLKSEISDLNNQKEq 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 184 -------SELKEIEQELHLAQAEIQSLRQAA----------EDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEI 246
Cdd:TIGR04523 307 dwnkelkSELKNQEKKLEEIQNQISQNNKIIsqlneqisqlKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 247 ASLRA-----EMEMKSSEPSGSLGLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQ 321
Cdd:TIGR04523 387 KNLESqindlESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 322 SQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNE 401
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767948502 402 VLrfqTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELL 469
Cdd:TIGR04523 547 LN---KDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKK 611
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-540 |
6.67e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 173 EEISLLEHEKESELKEIEQelhlaQAEIQSLRQAAEDSATEHESDIASLQEDlcRMQNELEDMERIRGDYEMEIASLRAE 252
Cdd:COG1196 189 ERLEDILGELERQLEPLER-----QAEKAERYRELKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 253 MEmkssepsgslglsdysGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERtQRATERWLQSQTlsmtsaes 332
Cdd:COG1196 262 LA----------------ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI-ARLEERRRELEE-------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 333 qtsemdflepdpEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVT 412
Cdd:COG1196 317 ------------RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 413 QNEELksrlcTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELLcrLQKLHLQHQNVTCEKEKLLER 492
Cdd:COG1196 385 AEELL-----EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE--EEEEEEALEEAAEEEAELEEE 457
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 767948502 493 QQQLQEELQCHEAELQHLRDTVASFKESNEKDTETHAQLQEMKQLYQA 540
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
107-267 |
1.59e-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: 44.75 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKESEL 186
Cdd:pfam09787 62 EIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 187 KEIEQELHLAQAEIQSlRQAAEDSATEHESDIASLQEDLCRMQNELEDM--ERIRGDYEMEiaslRAEMEMKSSEPSGSL 264
Cdd:pfam09787 142 KDREAEIEKLRNQLTS-KSQSSSSQSELENRLHQLTETLIQKQTMLEALstEKNSLVLQLE----RMEQQIKELQGEGSN 216
|
...
gi 767948502 265 GLS 267
Cdd:pfam09787 217 GTS 219
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
107-593 |
2.13e-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: 45.60 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLElQGLLEDERLASAQ-QAEVFTKQIQQLQGELRSLREEISLLEHEKESE 185
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQHGAFLDADIE-TAAADQEQLPSWQsELENLEERLKALTGKHQDVTAKYNRRRSKIKEQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 186 LKEIEQELHLAQAEIqslRQAAEDSATEHESDIASLQEDLcRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLg 265
Cdd:pfam12128 388 NNRDIAGIKDKLAKI---REARDRQLAVAEDDLQALESEL-REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPEL- 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 266 LSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGqLADLESERTQRATERWLQSQtlsmtSAESQTSEMDFLEPDPE 345
Cdd:pfam12128 463 LLQLENFDERIERAREEQEAANAEVERLQSELRQARK-RRDQASEALRQASRRLEERQ-----SALDELELQLFPQAGTL 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 346 MQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQrrlqreLKCAQNEVLRFQTSHSVTQNEELKSRLCTLQ 425
Cdd:pfam12128 537 LHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELN------LYGVKLDLKRIDVPEWAASEEELRERLDKAE 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 426 KKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELlcRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCH-E 504
Cdd:pfam12128 611 EALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARL--DLRRLFDEKQSEKDKKNKALAERKDSANERLNSlE 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 505 AELQHLRDTVASFKESNEKDTETH--AQLQEMKQLYQASKDELERQKH----MYDQLEQDLLLCQLELK-ELKASHPIPE 577
Cdd:pfam12128 689 AQLKQLDKKHQAWLEEQKEQKREArtEKQAYWQVVEGALDAQLALLKAaiaaRRSGAKAELKALETWYKrDLASLGVDPD 768
|
490
....*....|....*.
gi 767948502 578 DKGKCANKCDTLLSRL 593
Cdd:pfam12128 769 VIAKLKREIRTLERKI 784
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
101-296 |
2.76e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGL-------------LEDERLASAQQAEVFTKQIQQLQGE 167
Cdd:PRK02224 215 LAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLeaeiedlretiaeTEREREELAEEVRDLRERLEELEEE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 168 LRSLREE----------ISLLEHEKESELKEIEQELHLAQAEIQSLRQAAE---DSATEHESDIASLQEDLCRMQNELED 234
Cdd:PRK02224 295 RDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAEslrEDADDLEERAEELREEAAELESELEE 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767948502 235 MERIRGDYEMEIASLRAEMEMKSSE----PSGSLGLSDYSG-LQEELQELRERYHFLNEEYRALQES 296
Cdd:PRK02224 375 AREAVEDRREEIEELEEEIEELRERfgdaPVDLGNAEDFLEeLREERDELREREAELEATLRTARER 441
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
138-816 |
2.90e-04 |
|
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: 44.96 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 138 ELQGLLEDERLASAqqAEVFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESD 217
Cdd:pfam02463 161 EAAGSRLKRKKKEA--LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 218 IASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLGLSDYSGLQEELQE-----LRERYHFLNEEYRA 292
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKsellkLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 293 LQESNSSLTGQLADLESERTQRATERWLQS-QTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELC 371
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEiKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 372 CELEELQHHRQVSEEEQRRL----------------QRELKCAQNEVLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQ 435
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEdllkeekkeeleileeEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 436 NELLKMQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCE-KEKLLERQQQLQEELQCHEAELQHLRDTV 514
Cdd:pfam02463 479 LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHgRLGDLGVAVENYKVAISTAVIVEVSATAD 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 515 ASFKESNEKDTETHAQLQEMKQLYQASKDELERQKHMYDQLEQDLLLCQLELKELKASHpipEDKGKCANKCDTLLSRLT 594
Cdd:pfam02463 559 EVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADE---DDKRAKVVEGILKDTELT 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 595 ELQEKYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPKSGLLLK----SQELLTKLEDLCELQLLYQG 670
Cdd:pfam02463 636 KLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKeeilRRQLEIKKKEQREKEELKKL 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 671 MQEEQKKLIQNQDCVLKEQLEIHEELRRfKESHFQEVLENPDDSKLAKSSKCNRNKQPRSQAQHAQRPDSELGQEIQ--- 747
Cdd:pfam02463 716 KLEAEELLADRVQEAQDKINEELKLLKQ-KIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEkee 794
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 748 -ELIQSKLLMEQMQALQVMYDAGQAKQELLQQEQGRLLEERKRLQADLQLCLEEMQLLQVQSPSIKMSLE 816
Cdd:pfam02463 795 kLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEIT 864
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
101-252 |
3.19e-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: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 101 LSLTETELEELRAQVLQLVAELEETRELAGQH-------EDDSLELQGLLEDERLASA-QQAEVFTKQIQQLQGELRSLR 172
Cdd:COG3883 60 LEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsGGSVSYLDVLLGSESFSDFlDRLSALSKIADADADLLEELK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 173 EEISLLEhEKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAE 252
Cdd:COG3883 140 ADKAELE-AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
191-317 |
7.65e-04 |
|
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: 42.22 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 191 QELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLGLSDYS 270
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYE 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 767948502 271 GLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATE 317
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE 139
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
105-616 |
8.11e-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: 43.57 E-value: 8.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 105 ETELEELRAQVLQLVAELE----ETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEH 180
Cdd:pfam15921 259 ELLLQQHQDRIEQLISEHEveitGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 181 EKESELKEIEQELHLAQAEIQSLRQAAEDSATEH---ESDIASLQEDLCRMQNEL---------------------EDME 236
Cdd:pfam15921 339 MYEDKIEELEKQLVLANSELTEARTERDQFSQESgnlDDQLQKLLADLHKREKELslekeqnkrlwdrdtgnsitiDHLR 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 237 RIRGDYEMEIASLRAEMEMKSSEPSGSL--GLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLE-SERTQ 313
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSECQGQMerQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLEsSERTV 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 314 RATERWLQSQTLSMtsaESQTSEMDFLEPDPEMQLLR-QQLRDAEEQMHGMKNKCQELCCELEEL--------------- 377
Cdd:pfam15921 499 SDLTASLQEKERAI---EATNAEITKLRSRVDLKLQElQHLKNEGDHLRNVQTECEALKLQMAEKdkvieilrqqienmt 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 378 ----QHHRQVS--EEEQRRLQRELKCAQNEVLRFQT--SHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTE- 448
Cdd:pfam15921 576 qlvgQHGRTAGamQVEKAQLEKEINDRRLELQEFKIlkDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQEr 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 449 ---LRQLKVMKSTLVENQSEKELLCRlqklhlqhqNVTCEKEKLLERQQQLQEELQCHEAELQHLRDTVASFKESNEKDT 525
Cdd:pfam15921 656 dqlLNEVKTSRNELNSLSEDYEVLKR---------NFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAM 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 526 ETHAQLQEMKQLYQASKDELERQKHMYDQLEQDLLLCQLELKELKAS-----HPIPEDKGKCANKCDTLLSRLTELQEKY 600
Cdd:pfam15921 727 KVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKlsqelSTVATEKNKMAGELEVLRSQERRLKEKV 806
|
570
....*....|....*...
gi 767948502 601 KASQKEM--GQLQMEQCE 616
Cdd:pfam15921 807 ANMEVALdkASLQFAECQ 824
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
272-421 |
1.23e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 272 LQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAESQTSEMDflEPDPEMQLLRQ 351
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLD--ASSDDLAALEE 692
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 352 QLRDAEEQMhgmknkcQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNEELKSRL 421
Cdd:COG4913 693 QLEELEAEL-------EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF 755
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
101-698 |
1.89e-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: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 101 LSLTETELEELRAQVLQLvaelEETRELAGQHEDDSLELQGLledERLASAQQAEVFTKQIQQLQGELRSLREEISLLEH 180
Cdd:COG4913 237 LERAHEALEDAREQIELL----EPIRELAERYAAARERLAEL---EYLRAALRLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 181 EKEselkEIEQELHLAQAEIQSLRQAAEDSATEhesDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEmkssep 260
Cdd:COG4913 310 ELE----RLEARLDALREELDELEAQIRGNGGD---RLEQLEREIERLERELEERERRRARLEALLAALGLPLP------ 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 261 sgsLGLSDYSGLQEELQELRERyhfLNEEYRALQESNSSLTGQLADLESERTQRATERwlqsqtlsmTSAESQTSEMDfl 340
Cdd:COG4913 377 ---ASAEEFAALRAEAAALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEI---------ASLERRKSNIP-- 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 341 epdPEMQLLRQQLRDAeeqmhgMKNKCQELC--CELEEL--------------------------QHHRQVSEE-EQRRL 391
Cdd:COG4913 440 ---ARLLALRDALAEA------LGLDEAELPfvGELIEVrpeeerwrgaiervlggfaltllvppEHYAAALRWvNRLHL 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 392 QRELkcaqnEVLRFQTSHSVTQNEELKSRlcTLQKKYDTSQDEQNELLKMQLQlqtelRQLKVMKstlVENQSE------ 465
Cdd:COG4913 511 RGRL-----VYERVRTGLPDPERPRLDPD--SLAGKLDFKPHPFRAWLEAELG-----RRFDYVC---VDSPEElrrhpr 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 466 --------KELLCRLQK---LHLQHQNVTCE--KEKLLERqqqlqeelqchEAELQHLRDTVASFKESNEKDTETHAQLQ 532
Cdd:COG4913 576 aitragqvKGNGTRHEKddrRRIRSRYVLGFdnRAKLAAL-----------EAELAELEEELAEAEERLEALEAELDALQ 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 533 EMKQLYQASKDELERQKHMyDQLEQDLLLCQLELKELKASHPipedkgkcankcdtllsRLTELQEKYKASQKEMGQLQM 612
Cdd:COG4913 645 ERREALQRLAEYSWDEIDV-ASAEREIAELEAELERLDASSD-----------------DLAALEEQLEELEAELEELEE 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 613 EQCELLEDQRRMQEEQGQLQEELHRLTLPLpKSGLLLKSQELLTKLEDLCELQLLYQGMQEEQKKLIQNQDCVLKEQLEI 692
Cdd:COG4913 707 ELDELKGEIGRLEKELEQAEEELDELQDRL-EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRA 785
|
....*.
gi 767948502 693 HEELRR 698
Cdd:COG4913 786 EEELER 791
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
109-295 |
2.33e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 109 EELRAQV--LQLVAELEETRELAGQHEDDSLELQGLLEDERlasaQQAEVFTKQIQQLQGELRSLREEISLLEHEKESEL 186
Cdd:PRK11281 39 ADVQAQLdaLNKQKLLEAEDKLVQQDLEQTLALLDKIDRQK----EETEQLKQQLAQAPAKLRQAQAELEALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 187 KEIEQELHLAQ-----AEIQSLRQAAEDSATEHESDIASLQEDLCRMQNEL-EDMERI---------------------R 239
Cdd:PRK11281 115 RETLSTLSLRQlesrlAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALyANSQRLqqirnllkggkvggkalrpsqR 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767948502 240 GDYEMEIASLRAEMEMKSSEPSGSLGLSDYsgLQEELQELRERYHFLNEEYRALQE 295
Cdd:PRK11281 195 VLLQAEQALLNAQNDLQRKSLEGNTQLQDL--LQKQRDYLTARIQRLEHQLQLLQE 248
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
99-249 |
2.54e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 99 RGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQgllederlASAQQAEVFTKQIQQLQGELRSLREEISLL 178
Cdd:PRK09039 46 REISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLR--------ASLSAAEAERSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767948502 179 EHEKESELKEIEQELHLAQAEIQSLRQaaedsatehesDIASLQEDLCRMQNELEDMERIRGDYEMEIASL 249
Cdd:PRK09039 118 AGELAQELDSEKQVSARALAQVELLNQ-----------QIAALRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
186-451 |
2.58e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 186 LKEIEQELHLAQAEIQSLRQAAE--DSATEHESDIASLQEDLCRMQNELEDMERirgdyemEIASLRAEMEMKSSEPSGS 263
Cdd:PRK11281 48 LNKQKLLEAEDKLVQQDLEQTLAllDKIDRQKEETEQLKQQLAQAPAKLRQAQA-------ELEALKDDNDEETRETLST 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 264 LGLSDysgLQEELQELRERyhfLNEEYRALQESNSSLTGQlaDLESERTQRA-TERWLQSQTLSMTSAESQTSEMDfLEP 342
Cdd:PRK11281 121 LSLRQ---LESRLAQTLDQ---LQNAQNDLAEYNSQLVSL--QTQPERAQAAlYANSQRLQQIRNLLKGGKVGGKA-LRP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 343 DpemqllRQQLRDAEEQMHGMKNKCQELccELEE-------LQHHRQVSEEEQRRLQRELKCAQ---NEVLRFQTSHSVT 412
Cdd:PRK11281 192 S------QRVLLQAEQALLNAQNDLQRK--SLEGntqlqdlLQKQRDYLTARIQRLEHQLQLLQeaiNSKRLTLSEKTVQ 263
|
250 260 270
....*....|....*....|....*....|....*....
gi 767948502 413 QNEELKsrlctlqkkyDTSQDEQNELLKMQLQLQTELRQ 451
Cdd:PRK11281 264 EAQSQD----------EAARIQANPLVAQELEINLQLSQ 292
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
465-781 |
2.60e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 465 EKELLCRLQKLHLQHQNVtcEKEKLLERQQQLQEELQCHEAELQHLRDTVASFKESNEKDTETHAQLQEMKQLYQASKDE 544
Cdd:COG1196 222 LKELEAELLLLKLRELEA--ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 545 LERQKHMYDQLEQDLLLCQLELKELKASHpipedkgkcANKCDTLLSRLTELQEKYKASQKEMGQLQMEQCELLEDQRRM 624
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAEL---------EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 625 QEEQGQLQEELHRLtlplpKSGLLLKSQELLTKLEDLCELQLLYQGMQEEQKKLIQNQDcVLKEQLEIHEELRRFKESHF 704
Cdd:COG1196 371 EAELAEAEEELEEL-----AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE-ELEEALAELEEEEEEEEEAL 444
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767948502 705 QEVLENPDDSKLAKSSKCNRNKQPRSQAQHAQRPDSELGQEIQELIQSKLLMEQMQALQVMYDAGQAKQELLQQEQG 781
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
104-619 |
3.08e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 104 TETELEELRAQVLQLvaeleETRELAGQHEDDSLELQGLLEDERLASAQQaevFTKQIQQLQGELRSLREEISLLEHEKE 183
Cdd:PRK04863 584 LRQQLEQLQARIQRL-----AARAPAWLAAQDALARLREQSGEEFEDSQD---VTEYMQQLLERERELTVERDELAARKQ 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 184 SELKEIEQELHLAQAEIQSLRQAAED----SATEHESDIaSLQE------------------DLCRMQNELEDMERIRGD 241
Cdd:PRK04863 656 ALDEEIERLSQPGGSEDPRLNALAERfggvLLSEIYDDV-SLEDapyfsalygparhaivvpDLSDAAEQLAGLEDCPED 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 242 Y---EMEIASLR-AEMEMKSSEPSGSLGLSD----YSG------------------LQEELQELRERYHFLNEEYRALQE 295
Cdd:PRK04863 735 LyliEGDPDSFDdSVFSVEELEKAVVVKIADrqwrYSRfpevplfgraarekrieqLRAEREELAERYATLSFDVQKLQR 814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 296 SNSSLTGQLA-------DLESERTQRATERWLQSQTLSMTSAESQTsemdflepdpemQLLRQQLRDAEEQMHGMkNKCQ 368
Cdd:PRK04863 815 LHQAFSRFIGshlavafEADPEAELRQLNRRRVELERALADHESQE------------QQQRSQLEQAKEGLSAL-NRLL 881
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 369 ---------ELCCELEELQHHRQVSEEEQRRLQRElkcaQNEVLRFQTSHSVTQNEElkSRLCTLQKKYDTSQDEQnELL 439
Cdd:PRK04863 882 prlnlladeTLADRVEEIREQLDEAEEAKRFVQQH----GNALAQLEPIVSVLQSDP--EQFEQLKQDYQQAQQTQ-RDA 954
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 440 KMQLQLQTELRQLKVMKS------TLVENQSEKELLcrLQKLHLQHQNVTCEKEKLLErqqqlqeelqcHEAELQHLRDT 513
Cdd:PRK04863 955 KQQAFALTEVVQRRAHFSyedaaeMLAKNSDLNEKL--RQRLEQAEQERTRAREQLRQ-----------AQAQLAQYNQV 1021
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 514 VASFKESNEKDTETHAQL-QEMKQL-YQASKDELERQKHMYDQLEQDLLLCQLELKELKAshpipeDKGKCANKCDTLLS 591
Cdd:PRK04863 1022 LASLKSSYDAKRQMLQELkQELQDLgVPADSGAEERARARRDELHARLSANRSRRNQLEK------QLTFCEAEMDNLTK 1095
|
570 580
....*....|....*....|....*...
gi 767948502 592 RLTELQEKYKASQKEMGQLQMEQCELLE 619
Cdd:PRK04863 1096 KLRKLERDYHEMREQVVNAKAGWCAVLR 1123
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
105-623 |
3.25e-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: 41.49 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 105 ETELEELRAQVLQLVAELEETRELAGQHED--DSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEK 182
Cdd:TIGR00618 337 QSSIEEQRRLLQTLHSQEIHIRDAHEVATSirEISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRT 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 183 ESE------LKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQE----------DLCRMQNELEDMERI---RGDYE 243
Cdd:TIGR00618 417 SAFrdlqgqLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQEsaqslkereqQLQTKEQIHLQETRKkavVLARL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 244 MEIASLRAEMEMKSSEPSGSLGLSDYSG-LQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESE--RTQRATERWL 320
Cdd:TIGR00618 497 LELQEEPCPLCGSCIHPNPARQDIDNPGpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQmqEIQQSFSILT 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 321 QSQTLSMTSAESQTSEMDFLEPDPEMQllrqqlrDAEEQMHGMKNKCQELccELEELQHHRQVSEEEQRRLQRElkcAQN 400
Cdd:TIGR00618 577 QCDNRSKEDIPNLQNITVRLQDLTEKL-------SEAEDMLACEQHALLR--KLQPEQDLQDVRLHLQQCSQEL---ALK 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 401 EVLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQ 480
Cdd:TIGR00618 645 LTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIE 724
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 481 NVTCEKEKLLERQQQLQEELQcheAELQHLRDTV--ASFKESNEKDTETHAQLQEMKQLYQASKDELERQKhmydQLEQD 558
Cdd:TIGR00618 725 NASSSLGSDLAAREDALNQSL---KELMHQARTVlkARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNR----LREED 797
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767948502 559 lllcQLELKELKASHP--IPEDKGKCANKCDTLLSRLTELQEKYKASQKEMGQLQMEQCELLEDQRR 623
Cdd:TIGR00618 798 ----THLLKTLEAEIGqeIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
244-460 |
3.39e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 244 MEIASLRAEMEM--KSSEPSGSLGLSDYSGLQEELQELRERyhflNEEYRALQESNSSLTGQLADLESERTQRATERWLQ 321
Cdd:COG4717 46 MLLERLEKEADElfKPQGRKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 322 SQTLsmtsaesqtsemDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNE 401
Cdd:COG4717 122 EKLL------------QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767948502 402 VLRfQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNEL------LKMQLQLQTELRQLKVMKSTLV 460
Cdd:COG4717 190 TEE-ELQDLAEELEELQQRLAELEEELEEAQEELEELeeeleqLENELEAAALEERLKEARLLLL 253
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
106-224 |
3.94e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 106 TELEELRAQVLQLVAELEEtrelagqheddslelqgLLEDERLASAQQAEVFTKQIQQLQGELRSLREEislLEHEKE-- 183
Cdd:COG0542 411 EELDELERRLEQLEIEKEA-----------------LKKEQDEASFERLAELRDELAELEEELEALKAR---WEAEKEli 470
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 767948502 184 SELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQED 224
Cdd:COG0542 471 EEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
107-401 |
4.06e-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: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 107 ELEELRAQVLQLVAELEETRELAGQHeDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLrEEISLLEHEKESEL 186
Cdd:pfam05557 22 ELEHKRARIELEKKASALKRQLDRES-DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYL-EALNKKLNEKESQL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 187 KEIEQELHLAQAEIQSLRQAAEDSA---TEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLR-AEMEMKSSEPSG 262
Cdd:pfam05557 100 ADAREVISCLKNELSELRRQIQRAElelQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAeAEQRIKELEFEI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 263 SLGLSDYSGLQE---------ELQELRERYHFLNEEYRALQESNSSLTGQLADLES-------------------ERTQR 314
Cdd:pfam05557 180 QSQEQDSEIVKNskselaripELEKELERLREHNKHLNENIENKLLLKEEVEDLKRklereekyreeaatlelekEKLEQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 315 ATERWL---QSQTLSMTSAESQTSEMDFLEPD-----PEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEE 386
Cdd:pfam05557 260 ELQSWVklaQDTGLNLRSPEDLSRRIEQLQQReivlkEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKA 339
|
330
....*....|....*
gi 767948502 387 EQRRLQRELKCAQNE 401
Cdd:pfam05557 340 LVRRLQRRVLLLTKE 354
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
209-459 |
4.59e-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: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 209 DSATEHESDIASLQEDLCRMQNELEDMERIRGDYEmEIASLRAEMEMKSSEpsgsLGLSDYSGLQEELQELRERYHFLNE 288
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEPIRELAE-RYAAARERLAELEYL----RAALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 289 EYRALQESNSSLTGQLADLESERtQRATERWLQSQTlsmtsaesqtsemdflepdPEMQLLRQQLRDAEEQMHGMKNKCQ 368
Cdd:COG4913 303 ELARLEAELERLEARLDALREEL-DELEAQIRGNGG-------------------DRLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 369 ELCCELEELQHHRQVSEEEQRRLQRELKCAQnevlrfqtshsvtqnEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTE 448
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRAEAAALL---------------EALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
250
....*....|.
gi 767948502 449 LRQLKVMKSTL 459
Cdd:COG4913 428 IASLERRKSNI 438
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
159-317 |
5.62e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 159 KQIQQLQGELRSLREEISLLEHEK---ESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASL-----QEDLCRMQN 230
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELaalEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnNKEYEALQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 231 ELEDMERIRGDYEMEIASLRAEMEMKSSEpsgslglsdYSGLQEELQELRERyhfLNEEYRALQESNSSLTGQLADLESE 310
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEE---------LAELEAELAELEAE---LEEKKAELDEELAELEAELEELEAE 164
|
....*..
gi 767948502 311 RTQRATE 317
Cdd:COG1579 165 REELAAK 171
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
104-606 |
5.78e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 104 TETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLlederlasaqqaevfTKQIQQLQGELRSLREEISLLEhEKE 183
Cdd:PRK03918 205 VLREINEISSELPELREELEKLEKEVKELEELKEEIEEL---------------EKELESLEGSKRKLEEKIRELE-ERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 184 SELKEIEQELHLAQAEIQSLRQAAEDSATehesdiasLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGS 263
Cdd:PRK03918 269 EELKKEIEELEEKVKELKELKEKAEEYIK--------LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 264 LGLSD-YSGLQEELQELRERyHFLNEEYRALQESNSSLTGQLADLESERTQRATERwlqsqtLSMTSAESQTSEMDFLEP 342
Cdd:PRK03918 341 EELKKkLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTGLTPEKLEKELEE------LEKAKEEIEEEISKITAR 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 343 DPEMQLLRQQLRDAEEQMHGMKNKC----------------QELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLR-- 404
Cdd:PRK03918 414 IGELKKEIKELKKAIEELKKAKGKCpvcgrelteehrkellEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKes 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 405 --FQTSHSVTQNEELKSRLCTLQ--------KKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSE-KELLCRLQ 473
Cdd:PRK03918 494 elIKLKELAEQLKELEEKLKKYNleelekkaEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKlDELEEELA 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 474 KLH--LQHQNVTCEKE------------KLLERQQQLQEELQCHEAELQHLRDTV-ASFKESNEKDT---ETHAQLQEMK 535
Cdd:PRK03918 574 ELLkeLEELGFESVEEleerlkelepfyNEYLELKDAEKELEREEKELKKLEEELdKAFEELAETEKrleELRKELEELE 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 536 QLYqaSKDELERQKHMYDQLEQDL--LLCQLE------------LKELKASHPIPEDKGKCANKCDTLLSRLTELQEK-- 599
Cdd:PRK03918 654 KKY--SEEEYEELREEYLELSRELagLRAELEelekrreeikktLEKLKEELEEREKAKKELEKLEKALERVEELREKvk 731
|
....*...
gi 767948502 600 -YKASQKE 606
Cdd:PRK03918 732 kYKALLKE 739
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
104-402 |
7.13e-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: 40.42 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 104 TETELEE----LRAQVLQLVAELEETRELAGQHEDDSLELQGLLEderlASAQQAEVFTKQIQQLQGELRSLREEISlle 179
Cdd:TIGR00606 689 TEAELQEfisdLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAP----GRQSIIDLKEKEIPELRNKLQKVNRDIQ--- 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 180 hEKESELKEIEQELHLAQAEiqslrqaaEDSATEHESDIASLQedlcRMQNELEDMERirgdyemeiaslraEMEMKSSE 259
Cdd:TIGR00606 762 -RLKNDIEEQETLLGTIMPE--------EESAKVCLTDVTIME----RFQMELKDVER--------------KIAQQAAK 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 260 PSGSLGLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWlqsqTLSMTSAESQTSEMDF 339
Cdd:TIGR00606 815 LQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKL----QIGTNLQRRQQFEEQL 890
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767948502 340 LEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRqvsEEEQRRLQRELKCAQNEV 402
Cdd:TIGR00606 891 VELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSK---ETSNKKAQDKVNDIKEKV 950
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
162-259 |
7.81e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.32 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948502 162 QQLQGELRSLREEISLLEHEKESELKEIEQElhlaqaeiQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGD 241
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQ--------QQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQ 216
|
90
....*....|....*...
gi 767948502 242 YEMEIASlRAEMEMKSSE 259
Cdd:PRK11448 217 KRKEITD-QAAKRLELSE 233
|
|
| |
