|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
84-405 |
2.45e-14 |
|
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: 78.17 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 84 VQKGGSVGSLSVNKHRGLSLTETELEELRAQVLQLVAELEETR----ELAGQHEDDSLELQGLLEDERLASAQ------Q 153
Cdd:TIGR02168 655 VRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEkalaELRKELEELEEELEQLRKELEELSRQisalrkD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 154 AEVFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQ---ELHLAQAEIQSLRQAAEDSATEH---ESDIASLQEDLCR 227
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeELAEAEAEIEELEAQIEQLKEELkalREALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 228 MQNELEDMERIRGDYEMEIASLRAEMEMkssepsgslglsdysgLQEELQELRERYHFLNEEYRALQESNSSLTGQLADL 307
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLED----------------LEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 308 ESERTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELC--------CELEELQH 379
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerlseeysLTLEEAEA 958
|
330 340
....*....|....*....|....*.
gi 1370510765 380 HRQVSEEEQRRLQRELKCAQNEVLRF 405
Cdd:TIGR02168 959 LENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
101-359 |
1.09e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 101 LSLTETELEELRAQVLQLVAELEETRElagQHEDDSLELQGLLEDERLASAQQAEVfTKQIQQLQGELRSLREEISlleh 180
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRL---ELEELELELEEAQAEEYELLAELARL-EQDIARLEERRRELEERLE---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 181 EKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEp 260
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL- 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 261 sgslgLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERwLQSQTLSMTSAESQTSEMDfl 340
Cdd:COG1196 399 -----AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE-AELEEEEEALLELLAELLE-- 470
|
250
....*....|....*....
gi 1370510765 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 |
5.40e-12 |
|
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: 70.48 E-value: 5.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEvftKQIQQLQGELRSLREEISLLE---HEKE 183
Cdd:TIGR02169 188 RLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALE---RQKEAIERQLASLEEELEKLTeeiSELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 184 SELKEIEQELHLAQAEIQSL-----RQAAEDSAtEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEmkss 258
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIG-ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE---- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 259 epsgslglsdysGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADlESERTQRATERWLQSQT-LSMTSAESQTSEM 337
Cdd:TIGR02169 340 ------------ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE-VDKEFAETRDELKDYREkLEKLKREINELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 338 DFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNE-- 415
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEls 486
|
330 340
....*....|....*....|..
gi 1370510765 416 ELKSRLCTLQKKYDTSQDEQNE 437
Cdd:TIGR02169 487 KLQRELAEAEAQARASEERVRG 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-702 |
6.21e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 6.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQqaevFTKQIQQLQGELRSLREEISLLEH 180
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ----LELQIASLNNEIERLEARLERLED 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 181 EKESELKEIEQ--------ELHLAQAEIQSLRQAAEDSATEHEsdiaSLQEDLCRMQNELEDMERIRGDYEMEIASLRAE 252
Cdd:TIGR02168 415 RRERLQQEIEEllkkleeaELKELQAELEELEEELEELQEELE----RLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 253 MEMkssepsgslglsdysglqeeLQELRERYHFLNEEYRALQESNSSLTG---QLADLES--ERTQRATERWLQS--QTL 325
Cdd:TIGR02168 491 LDS--------------------LERLQENLEGFSEGVKALLKNQSGLSGilgVLSELISvdEGYEAAIEAALGGrlQAV 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 326 SMTSAESQTSEMDFLEPD--------PEMQLLRQQLRDAEEQMHGMKNKCQELCCELEE------------LQHHRQVSE 385
Cdd:TIGR02168 551 VVENLNAAKKAIAFLKQNelgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKfdpklrkalsylLGGVLVVDD 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 386 EEQ-RRLQRELKCAQNEVL---------------RFQTSHSVTQN----EELKSRLCTLQKKYDTSQDEQNELLKMQLQL 445
Cdd:TIGR02168 631 LDNaLELAKKLRPGYRIVTldgdlvrpggvitggSAKTNSSILERrreiEELEEKIEELEEKIAELEKALAELRKELEEL 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 446 QTELRQLKVM---KSTLVENQSEK---------ELLCRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCHEAELQHLRDT 513
Cdd:TIGR02168 711 EEELEQLRKEleeLSRQISALRKDlarleaeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 514 VASFKESNEKDTETHAQLQEMkqlYQASKDELERQKHMYDQLEQDLLLCQLELKELKASHPIPEDKGKCANK-------- 585
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAE---LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAeieeleel 867
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 586 CDTLLSRLTELQEKYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPKSGLLLKS--QELLTKLEDLCE 663
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGleVRIDNLQERLSE 947
|
650 660 670
....*....|....*....|....*....|....*....
gi 1370510765 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 |
6.27e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.00 E-value: 6.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 153 QAEVFTKQIQQLQGELRSLREEISllehEKESELKEIEQELHLAQAEIQSLRqaaeDSATEHESDIASLQEDLCRMQNEL 232
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELK----EAEEELEELTAELQELEEKLEELR----LEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 233 EDMERirgdyemEIASLRAEMEMKSSEpsgslglsdYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESErt 312
Cdd:TIGR02168 298 SRLEQ-------QKQILRERLANLERQ---------LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE-- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 313 qraterwlqsqtLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQ 392
Cdd:TIGR02168 360 ------------LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510765 393 RELKCAQNEVLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKE 467
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
108-361 |
1.08e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.01 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 108 LEELRAQVLQLVAELEETRELAGQHEDdsleLQGLLEDERLASAQQAEVFTKQI--QQLQGELRSLREEISLLEhEKESE 185
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEA----ELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLD-ASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 186 LKEIEQELHLAQAEIQSLRQ---AAEDSATEHESDIASLQEDLCRMQNELEDMERI-RGDYEMEIASLRAEMEMKSSEPS 261
Cdd:COG4913 687 LAALEEQLEELEAELEELEEeldELKGEIGRLEKELEQAEEELDELQDRLEAAEDLaRLELRALLEERFAAALGDAVERE 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 262 GSLGLSD-YSGLQEELQELRER-----------YHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTs 329
Cdd:COG4913 767 LRENLEErIDALRARLNRAEEEleramrafnreWPAETADLDADLESLPEYLALLDRLEEDGLPEYEERFKELLNENSI- 845
|
250 260 270
....*....|....*....|....*....|..
gi 1370510765 330 aESQTsemDFLepdpemQLLRQQLRDAEEQMH 361
Cdd:COG4913 846 -EFVA---DLL------SKLRRAIREIKERID 867
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
108-783 |
1.21e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 108 LEELRAQV--LQLVAEL-EETRELAGQHEDDSLELQGL----LEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLE- 179
Cdd:TIGR02168 195 LNELERQLksLERQAEKaERYKELKAELRELELALLVLrleeLREELEELQEELKEAEEELEELTAELQELEEKLEELRl 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 180 --HEKESELKEIEQELHLAQAEIQSL---RQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEME 254
Cdd:TIGR02168 275 evSELEEEIEELQKELYALANEISRLeqqKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 255 MKSSEpsgslgLSDYSGLQEEL----QELRERYHFLNEEYRALQESNSSLTGQLADLES--ERTQRATERWLQSQTlsmt 328
Cdd:TIGR02168 355 SLEAE------LEELEAELEELesrlEELEEQLETLRSKVAQLELQIASLNNEIERLEArlERLEDRRERLQQEIE---- 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 329 SAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQT- 407
Cdd:TIGR02168 425 ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGf 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 408 SHSVTQNEELKSRLC----TLQKKYDTSQDEQNELLK-----MQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQ 478
Cdd:TIGR02168 505 SEGVKALLKNQSGLSgilgVLSELISVDEGYEAAIEAalggrLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGT 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 479 H-QNVTCEKEKLLERQQQLQEELQCHEAELQHLRDT-------VASFKESNEKDTETHAQL------------------- 531
Cdd:TIGR02168 585 EiQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDNALELAKKLRPGYrivtldgdlvrpggvitgg 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 532 ---QEMKQLYQASK-DELERQKhmyDQLEQDLLLCQLELKELKASHPIPEDKGkcankcDTLLSRLTELQEKYKASQKEM 607
Cdd:TIGR02168 665 sakTNSSILERRREiEELEEKI---EELEEKIAELEKALAELRKELEELEEEL------EQLRKELEELSRQISALRKDL 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 608 GQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPKSGLLLKSQElltklEDLCELQLLYQGMQEEQKKLIQNqdcvLK 687
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE-----AEIEELEAQIEQLKEELKALREA----LD 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 688 EQLEIHEELRRFKESHFQEVLENPDDSKLAKSSKCNRNKQSKLLMEQMQALQVMYDAGQAKQELLQQEQGRLLEERKRLQ 767
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
730
....*....|....*.
gi 1370510765 768 ADLQLCLEEMQLLQVQ 783
Cdd:TIGR02168 887 EALALLRSELEELSEE 902
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
163-490 |
2.16e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.01 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 163 QLQGELRSLREEISLLEHEKES---ELKEIEQELHlaqaEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIR 239
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSlqsELRRIENRLD----ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 240 GDYEMEIASLRAEMEMKSSEpsgslgLSDY----SGLQEELQEL-----RERYHFLNEEYRALQESNSSLTGQLADLESE 310
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEAR------IEELeedlHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 311 RTQRATERWLQSQtlSMTSAESQTSEMDFLEPD--PEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQ 388
Cdd:TIGR02169 821 LNRLTLEKEYLEK--EIQELQEQRIDLKEQIKSieKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 389 RRLQRELK--CAQNEVLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELL---KMQLQLQTELRQLKVMKS-TLVEN 462
Cdd:TIGR02169 899 RELERKIEelEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELsleDVQAELQRVEEEIRALEPvNMLAI 978
|
330 340
....*....|....*....|....*...
gi 1370510765 463 QSEKELLCRLQKLHLQHQNVTCEKEKLL 490
Cdd:TIGR02169 979 QEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
98-254 |
2.63e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 98 HRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDdslELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISL 177
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALRE---ELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 178 LEH----------EKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIA 247
Cdd:COG4913 364 LEAllaalglplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
....*..
gi 1370510765 248 SLRAEME 254
Cdd:COG4913 444 ALRDALA 450
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-314 |
2.63e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.61 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDerlaSAQQAEVFTKQIQQLQGELRSLREEISlleh 180
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED----LEEQIEELSEDIESLAAEIEELEELIE---- 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 181 EKESELKEIEQELHLAQAEIQSLRQAAEDSAT---EHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASL------RA 251
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEelrELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLqerlseEY 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 252 EMEMKSSEPSGSLGLSDYSGLQ---------------------EELQELRERYHFLNEEYRALQESNSSLTGQLADLESE 310
Cdd:TIGR02168 950 SLTLEEAEALENKIEDDEEEARrrlkrlenkikelgpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDRE 1029
|
....
gi 1370510765 311 RTQR 314
Cdd:TIGR02168 1030 ARER 1033
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
105-407 |
4.33e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 105 ETELEELRAQVLQLVAELEETRelAGQHEDDslelqgllederlasaqqaevftKQIQQLQGELRSLREEISLLEHEKEs 184
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELR--LEVSELE-----------------------EEIEELQKELYALANEISRLEQQKQ- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 185 elkEIEQELHLAQAEIQSLrqaaEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSepsgsl 264
Cdd:TIGR02168 306 ---ILRERLANLERQLEEL----EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES------ 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 265 glsdysgLQEELQELRERyhfLNEEYRALQESNSSLTGQLADLES--ERTQRATERWLQSQtlsmTSAESQTSEMDFLEP 342
Cdd:TIGR02168 373 -------RLEELEEQLET---LRSKVAQLELQIASLNNEIERLEArlERLEDRRERLQQEI----EELLKKLEEAELKEL 438
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510765 343 DPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQT 407
Cdd:TIGR02168 439 QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
148-378 |
4.59e-09 |
|
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: 59.78 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 148 LASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKES---ELKEIEQELHLAQAEIQSLrqaaEDSATEHESDIASLQED 224
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAllkQLAALERRIAALARRIRAL----EQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 225 LCRMQNELEDMERirgdyemEIASLRAEMEMKSSEPSGSLGLSdysglQEELQELRERYHFLNEEYRALQESNSSLTGQL 304
Cdd:COG4942 92 IAELRAELEAQKE-------ELAELLRALYRLGRQPPLALLLS-----PEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370510765 305 ADLESERTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQ 378
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
105-310 |
2.47e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.49 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 105 ETELEELRAQVLQLVAELEETRElagQHEDDSLELQGLLEDERLASAQQaevftkQIQQLQGELRSLREEISLLEHEKES 184
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQ---KNGLVDLSEEAKLLLQQLSELES------QLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 185 ELKEIEQELhlAQAEIQSLRQAAEDSatehESDIASLQEdlcRMQNELEDMERIRGdyemEIASLRAEMEMKSSEPSGSL 264
Cdd:COG3206 252 GPDALPELL--QSPVIQQLRAQLAEL----EAELAELSA---RYTPNHPDVIALRA----QIAALRAQLQQEAQRILASL 318
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1370510765 265 GlSDYSGLQEELQELRERYhflnEEYRALQESNSSLTGQLADLESE 310
Cdd:COG3206 319 E-AELEALQAREASLQAQL----AQLEARLAELPELEAELRRLERE 359
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
110-488 |
2.90e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 110 ELRAQVLQLVAELEE-TRELAG-QHEDDSLE-LQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISllehEKESEL 186
Cdd:TIGR02169 671 SEPAELQRLRERLEGlKRELSSlQSELRRIEnRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE----ELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 187 KEIEQELHLAQAEIQSLrqaaedsatehESDIASLQEDLCRMQNELEDMERirgdyemeiaslraememkssepsgslgl 266
Cdd:TIGR02169 747 SSLEQEIENVKSELKEL-----------EARIEELEEDLHKLEEALNDLEA----------------------------- 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 267 sdysglqeelQELRERYHFLNEEYRALQESNSSLTGQLADLESErtqraterwLQSQTLSMTSAESqtsemdflepdpEM 346
Cdd:TIGR02169 787 ----------RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQK---------LNRLTLEKEYLEK------------EI 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 347 QLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQtshsvTQNEELKSRLCTLQK 426
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE-----AQLRELERKIEELEA 910
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370510765 427 KYDTSQDEQNELlkmQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCEKEK 488
Cdd:TIGR02169 911 QIEKKRKRLSEL---KAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRA 969
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
107-547 |
3.27e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEhEKESEL 186
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE-EALAEL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 187 KEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLGL 266
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 267 SDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEM 346
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALA 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 347 QLLRQQLRDAEEqmhgmknkcQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNEELKSRlctLQK 426
Cdd:COG1196 594 RGAIGAAVDLVA---------SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA---GGS 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 427 KYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCHEAE 506
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1370510765 507 LQHLRDTVASFKESNEKDTETHAQLQEMKQLyqasKDELER 547
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLEELERELERL----EREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
107-333 |
3.91e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 107 ELEELRAQVLQLVAELEETRELAGQhEDDSLELQGLLEDERLASAQQaevftkQIQQLQGELRSLREEisllEHEKESEL 186
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEE-ELAELEEELEELEEELEELEE------ELEEAEEELEEAEAE----LAEAEEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 187 KEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEpsgslgL 266
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE------E 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510765 267 SDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSMTSAESQ 333
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
154-400 |
9.42e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.56 E-value: 9.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 154 AEVFTKQ-IQQLQGELRSLREEIsllehekESELKEIEQELHLAQAEIQSLRQ-----AAEDSATEHESDIASLQEDLCR 227
Cdd:COG3206 158 AEAYLEQnLELRREEARKALEFL-------EEQLPELRKELEEAEAALEEFRQknglvDLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 228 MQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLGLSDYSGLQEELQELRERYHFLNEEYRALQEsnssltgQLADL 307
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRA-------QIAAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 308 ESERTQRATERWLQSQTlSMTSAESQTSEmdflepdpemqlLRQQLRDAEEQMHGMKNKcqelcceleelqhhrqvsEEE 387
Cdd:COG3206 304 RAQLQQEAQRILASLEA-ELEALQAREAS------------LQAQLAQLEARLAELPEL------------------EAE 352
|
250
....*....|...
gi 1370510765 388 QRRLQRELKCAQN 400
Cdd:COG3206 353 LRRLEREVEVARE 365
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
86-559 |
1.49e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 86 KGGSVGSLSVNKHRGLSLTETELEELRAQVLQLVAELEETRelagqheddslelqglledERLASAQQaevftkQIQQLQ 165
Cdd:COG4717 61 PQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELE-------------------EELEELEA------ELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 166 GELRSLREEISLLEHEKesELKEIEQELHLAQAEIQSLRQAAEDSAtEHESDIASLQEDLCRMQNELEDmerirgdyEME 245
Cdd:COG4717 116 EELEKLEKLLQLLPLYQ--ELEALEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEELEE--------LLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 246 IASLRAEMEMKSSepsgslgLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTL 325
Cdd:COG4717 185 QLSLATEEELQDL-------AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 326 SMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMhgMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKcaqneVLRF 405
Cdd:COG4717 258 LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLL--LAREKASLGKEAEELQALPALEELEEEELEELLA-----ALGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 406 QTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLkmQLQLQTELRQLkvMKSTLVEN-----------QSEKELLCRLQK 474
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAAL--LAEAGVEDeeelraaleqaEEYQELKEELEE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 475 LHLQhqnvtCEKEKLLERQQQLQEELQCHEAELQHLRDTVASFKESNEKDTETHAQL-QEMKQLyqASKDELERQKHMYD 553
Cdd:COG4717 407 LEEQ-----LEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELeAELEQL--EEDGELAELLQELE 479
|
....*.
gi 1370510765 554 QLEQDL 559
Cdd:COG4717 480 ELKAEL 485
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
105-246 |
2.59e-07 |
|
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: 53.00 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 105 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDerlASAQQAEVFT-KQIQQLQGELRSLREEISLLEheke 183
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK---YEEQLGNVRNnKEYEALQKEIESLKRRISDLE---- 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510765 184 SELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEI 246
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
107-313 |
3.34e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKESEL 186
Cdd:COG1196 621 TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 187 KEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERI---------RGDYEMEIASLRAEMEmks 257
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAleelpeppdLEELERELERLEREIE--- 777
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 258 sepsgSLG----LSDysglqEELQELRERYHFLNEeyralqesnssltgQLADLESERTQ 313
Cdd:COG1196 778 -----ALGpvnlLAI-----EEYEELEERYDFLSE--------------QREDLEEARET 813
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
101-467 |
3.47e-07 |
|
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: 54.80 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLE- 179
Cdd:pfam01576 150 LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQa 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 180 --HEKESELKEIEQELHLAQAEI---QSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEME 254
Cdd:pfam01576 230 qiAELRAQLAKKEEELQAALARLeeeTAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 255 mkssepsgslGLSDYSGLQEELQELRERYhfLNEEYRALQESNSSLTGQLADLESERTQ---RATERWLQSQTLSMTSAE 331
Cdd:pfam01576 310 ----------DTLDTTAAQQELRSKREQE--VTELKKALEEETRSHEAQLQEMRQKHTQaleELTEQLEQAKRNKANLEK 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 332 S-QTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVlrfqtSHS 410
Cdd:pfam01576 378 AkQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLL-----NEA 452
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510765 411 VTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKE 467
Cdd:pfam01576 453 EGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEE 509
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
101-428 |
5.43e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISlleh 180
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE---- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 181 EKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASL---------RA 251
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLlallflllaRE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 252 EMEMKSSEPSGSLGLSDYSGLQEELQELRERYHFL----NEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTLSM 327
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEELLAALGLPpdlsPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 328 TSAESQTSEM--DFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCC---------ELEELQHHRQVSEEEQRRLQRELK 396
Cdd:COG4717 377 AEAGVEDEEElrAALEQAEEYQELKEELEELEEQLEELLGELEELLEaldeeeleeELEELEEELEELEEELEELREELA 456
|
330 340 350
....*....|....*....|....*....|....*.
gi 1370510765 397 CAQNEVLRFQTSHSVTQN----EELKSRLCTLQKKY 428
Cdd:COG4717 457 ELEAELEQLEEDGELAELlqelEELKAELRELAEEW 492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
185-395 |
5.65e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 185 ELKEIEQELHLAQAEIQSLRQAAEDsATEHESDIASLQE-DLCRMQNELEDMERIRGDYEMEIASLRAEMEmkssepsgs 263
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIREL-AERYAAARERLAElEYLRAALRLWFAQRRLELLEAELEELRAELA--------- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 264 lglsdysGLQEELQELRERYHFLNEEYRALQE---SNS-----SLTGQLADLESERTQRATERWLQSQTLSMTSAESQTS 335
Cdd:COG4913 306 -------RLEAELERLEARLDALREELDELEAqirGNGgdrleQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510765 336 EMDFLE-----------PDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQREL 395
Cdd:COG4913 379 AEEFAAlraeaaalleaLEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
107-415 |
6.05e-07 |
|
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: 53.15 E-value: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASaqqaevftkqiQQLQGELRSLREEISLLEhekeSEL 186
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAY-----------GKLRRELAGLTRRLSAAE----GEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 187 KEIEQELHLAQAEIQSLRQAAEDSATEhESDIASLQEDLcrmQNELEDMERIRGDYEMEIASLRAEMEMKSSepsgslgl 266
Cdd:pfam19220 86 EELVARLAKLEAALREAEAAKEELRIE-LRDKTAQAEAL---ERQLAAETEQNRALEEENKALREEAQAAEK-------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 267 sDYSGLQEELQELRERYHFLNEEYRALQ----ESN---SSLTGQLADLESER-TQRATERWLQSQtLSMTSAESQTSEMD 338
Cdd:pfam19220 154 -ALQRAEGELATARERLALLEQENRRLQalseEQAaelAELTRRLAELETQLdATRARLRALEGQ-LAAEQAERERAEAQ 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510765 339 FLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELcceLEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVTQNE 415
Cdd:pfam19220 232 LEEAVEAHRAERASLRMKLEALTARAAATEQL---LAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEAD 305
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
110-465 |
1.50e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 52.75 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 110 ELRAQvlqLVAELEETRELAGQHEDDSLElQGLLEderlASAQQAEVfTKQIQQLQGELRSLREEISLL---EHEKESEL 186
Cdd:PRK10929 83 ELRQQ---LNNERDEPRSVPPNMSTDALE-QEILQ----VSSQLLEK-SRQAQQEQDRAREISDSLSQLpqqQTEARRQL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 187 KEIEQELHLAQAEIQSLRQAAedsatehesdIASLQEDLCRMQ---NELEdMERIRGDYEMEIASLRAEMEMKSSEPsgs 263
Cdd:PRK10929 154 NEIERRLQTLGTPNTPLAQAQ----------LTALQAESAALKalvDELE-LAQLSANNRQELARLRSELAKKRSQQ--- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 264 lglsdysgLQEELQELRERYHFL--NEEYRALqESNSSLTGQLADL-ESERTQRATERWLqSQTLSmtsaeSQTSEMDFL 340
Cdd:PRK10929 220 --------LDAYLQALRNQLNSQrqREAERAL-ESTELLAEQSGDLpKSIVAQFKINREL-SQALN-----QQAQRMDLI 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 341 -----EPDPEMQLLRQQLRDAEEQMH--GMKN-----------------KCQELCCELEELQHHRQVSEEEQRRLQRELK 396
Cdd:PRK10929 285 asqqrQAASQTLQVRQALNTLREQSQwlGVSNalgealraqvarlpempKPQQLDTEMAQLRVQRLRYEDLLNKQPQLRQ 364
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510765 397 CAQNEvlrfqtSHSVTQNEelksrlctlQKKYDTSQDEQNELLKMQLQ----LQTELRQLKVMKSTLVENQSE 465
Cdd:PRK10929 365 IRQAD------GQPLTAEQ---------NRILDAQLRTQRELLNSLLSggdtLILELTKLKVANSQLEDALKE 422
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
158-395 |
2.00e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 158 TKQIQQLQGELRSLREEISLLEhekeSELKEIEQELHLAQAEIQSLRQAAEDSatEHESDIASLQEDLCRMQNELEDMER 237
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAE----ERLEALEAELDALQERREALQRLAEYS--WDEIDVASAEREIAELEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 238 irgdyemeiaslraememkssepsgslGLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQrate 317
Cdd:COG4913 683 ---------------------------SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE---- 731
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510765 318 rwLQSQTLSMTSAESQTSEMDFLEpdpemQLLRQQLRDAEEQMHgmknkcqelccelEELQHHRQVSEEEQRRLQREL 395
Cdd:COG4913 732 --LQDRLEAAEDLARLELRALLEE-----RFAAALGDAVERELR-------------ENLEERIDALRARLNRAEEEL 789
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
99-255 |
2.42e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.78 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 99 RGLSLtETELEELRAQVLqlvAELEETRELAGQHEDDSLELqgllEDERlasaqqaevftkqIQQLQGELRSLREEISLL 178
Cdd:COG2433 374 RGLSI-EEALEELIEKEL---PEEEPEAEREKEHEERELTE----EEEE-------------IRRLEEQVERLEAEVEEL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 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 ... |
346-1021 |
2.77e-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: 51.98 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 346 MQLLRQQLRDAEeqmhgmknKCQELCCELEELQHHRQVSEEEQrrLQRELKCAQNEVLRFQTSHsvtqnEELKSRLCTLQ 425
Cdd:TIGR02168 202 LKSLERQAEKAE--------RYKELKAELRELELALLVLRLEE--LREELEELQEELKEAEEEL-----EELTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 426 KKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLveNQSEKELLCRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCHEA 505
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRL--EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 506 ELQHLRDTVASFKESNEkdtETHAQLQEMKQLYQASKDELERQKHMYDQLEQDLLLCQLELKELKAShpIPEDKGKCANK 585
Cdd:TIGR02168 345 KLEELKEELESLEAELE---ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR--LERLEDRRERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 586 CDTLLSRLTELQE-KYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPKsgLLLKSQELLTKLEDLCEL 664
Cdd:TIGR02168 420 QQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA--AERELAQLQARLDSLERL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 665 QLLYQGMQEEQKKLIQNQDC------VLKEQLEIHEELRRFKE----SHFQEVL-ENPDDSKLA----KSSKCNRNKQSK 729
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNQSGlsgilgVLSELISVDEGYEAAIEaalgGRLQAVVvENLNAAKKAiaflKQNELGRVTFLP 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 730 LLMEQMQALQVMYDAGQAKQELLQQEQGRLLEERKRLQADLQLCLEemQLLQVQSPSIKMSLESY--------------- 794
Cdd:TIGR02168 578 LDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLG--GVLVVDDLDNALELAKKlrpgyrivtldgdlv 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 795 ---GKSYGSMVPSN----------ENCRKTYDTTVDDNES-------YYKSYTSTQTSSKSFLKSYDSSTSASEAYGKSY 854
Cdd:TIGR02168 656 rpgGVITGGSAKTNssilerrreiEELEEKIEELEEKIAElekalaeLRKELEELEEELEQLRKELEELSRQISALRKDL 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 855 CTTSNSSITYKKSYGSTSSSDT-------CQKSFVSSCTDEEPAEPEDMERFEEMVVKVLIKLQAVQAMYQISQEEHSQL 927
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTeleaeieELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 928 QEQMEKLLAKQKDLKEELDACEREFKECMECLEKPMAPQNDKN-EIKELQTKLRELQLQYQASMDEQGRLLVVQEQLEGQ 1006
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaEIEELEELIEELESELEALLNERASLEEALALLRSE 895
|
730
....*....|....*
gi 1370510765 1007 LQCCQEELRQLREKR 1021
Cdd:TIGR02168 896 LEELSEELRELESKR 910
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
105-469 |
3.59e-06 |
|
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: 51.17 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 105 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQaevfTKQIQQLQGELRSLREEISLLEHEKE- 183
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN----NKKIKELEKQLNQLKSEISDLNNQKEq 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 184 -------SELKEIEQELHLAQAEIQSLRQAA----------EDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEI 246
Cdd:TIGR04523 307 dwnkelkSELKNQEKKLEEIQNQISQNNKIIsqlneqisqlKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 247 ASLRA-----EMEMKSSEPSGSLGLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQ 321
Cdd:TIGR04523 387 KNLESqindlESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 322 SQTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNE 401
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510765 402 VLrfqTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELL 469
Cdd:TIGR04523 547 LN---KDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKK 611
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
101-237 |
3.72e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSlELQGLLEDERLASAQQAEV---FTK---QIQQLQGELRSLREE 174
Cdd:COG3206 228 LAEARAELAEAEARLAALRAQLGSGPDALPELLQSP-VIQQLRAQLAELEAELAELsarYTPnhpDVIALRAQIAALRAQ 306
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510765 175 IsllEHEKESELKEIEQELHLAQAEIQSLRQAAEdsatEHESDIASLQEDlcrmQNELEDMER 237
Cdd:COG3206 307 L---QQEAQRILASLEAELEALQAREASLQAQLA----QLEARLAELPEL----EAELRRLER 358
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
99-263 |
4.80e-06 |
|
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: 50.15 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 99 RGLSLTETELEELRAQVLQLVAELEETREL----------AGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGEL 168
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEElaellralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 169 RSLREEISLLEHEKESELKEIEQELHLAQAEIQSLRQAAEdsatEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIAS 248
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKA----ERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
170
....*....|....*
gi 1370510765 249 LRAEMEMKSSEPSGS 263
Cdd:COG4942 232 LEAEAAAAAERTPAA 246
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
140-453 |
7.26e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.51 E-value: 7.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 140 QGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQELHLAQAEiqSLRQAAEDSA----TEHE 215
Cdd:pfam17380 263 QTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAE--KARQAEMDRQaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 216 SDIASLQEDLCRMQNE--LEDMERIRG-DYEMEIASLRA------EMEMKSSEPSGSL-GLSDYSGLQEELQELRERYHF 285
Cdd:pfam17380 341 RMAMERERELERIRQEerKRELERIRQeEIAMEISRMRElerlqmERQQKNERVRQELeAARKVKILEEERQRKIQQQKV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 286 LNEEYRALQESNSSLTGQLADLESERT-----QRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQL--------LRQQ 352
Cdd:pfam17380 421 EMEQIRAEQEEARQREVRRLEEERAREmervrLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRaeeqrrkiLEKE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 353 LRDAEEQMHGMKNKCQELCCELEELQhhRQVSEEEQRRLQRELKCAQNEV-LRFQTSHSVTQNEELKSRLCTLQKKYD-T 430
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKEMEERQ--KAIYEEERRREAEEERRKQQEMeERRRIQEQMRKATEERSRLEAMEREREmM 578
|
330 340
....*....|....*....|...
gi 1370510765 431 SQDEQNELLKMQLQLQTELRQLK 453
Cdd:pfam17380 579 RQIVESEKARAEYEATTPITTIK 601
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
104-318 |
8.07e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 8.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 104 TETELEELRAQVLQLVAELEETRELAGQHEDdslelqglLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKE 183
Cdd:COG4913 666 AEREIAELEAELERLDASSDDLAALEEQLEE--------LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 184 S--ELKEIEQELHLAQAEIQSLRQAAEDSATEH-ESDIASLQEDLCRMQNELED-MERIRGDYEMEIASLRAEMEmksse 259
Cdd:COG4913 738 AaeDLARLELRALLEERFAAALGDAVERELRENlEERIDALRARLNRAEEELERaMRAFNREWPAETADLDADLE----- 812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370510765 260 psgslGLSDYsglQEELQELRER--YHFLNEEYRALQE-SNSSLTGQLADLESERtQRATER 318
Cdd:COG4913 813 -----SLPEY---LALLDRLEEDglPEYEERFKELLNEnSIEFVADLLSKLRRAI-REIKER 865
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-540 |
8.89e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 8.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 173 EEISLLEHEKESELKEIEQelhlaQAEIQSLRQAAEDSATEHESDIASLQEDlcRMQNELEDMERIRGDYEMEIASLRAE 252
Cdd:COG1196 189 ERLEDILGELERQLEPLER-----QAEKAERYRELKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 253 MEmkssepsgslglsdysGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERtQRATERWLQSQTlsmtsaes 332
Cdd:COG1196 262 LA----------------ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI-ARLEERRRELEE-------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 333 qtsemdflepdpEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTSHSVT 412
Cdd:COG1196 317 ------------RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 413 QNEELksrlcTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELLcrLQKLHLQHQNVTCEKEKLLER 492
Cdd:COG1196 385 AEELL-----EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE--EEEEEEALEEAAEEEAELEEE 457
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1370510765 493 QQQLQEELQCHEAELQHLRDTVASFKESNEKDTETHAQLQEMKQLYQA 540
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
106-251 |
1.56e-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: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 106 TELEELRAQVLQLVAELEETRELAGQHEDDSLE-LQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEIS-------- 176
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLELLEaELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggdrle 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 177 LLEHE---KESELKEIEQE----------LHLA----QAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIR 239
Cdd:COG4913 342 QLEREierLERELEERERRrarleallaaLGLPlpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
170
....*....|..
gi 1370510765 240 GDYEMEIASLRA 251
Cdd:COG4913 422 RELEAEIASLER 433
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
138-783 |
1.92e-05 |
|
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: 49.20 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 138 ELQGLLEDERLASAqqAEVFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESD 217
Cdd:pfam02463 161 EAAGSRLKRKKKEA--LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 218 IASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLGLSDYSGLQEELQE-----LRERYHFLNEEYRA 292
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKsellkLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 293 LQESNSSLTGQLADLESERTQRATERWLQS-QTLSMTSAESQTSEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELC 371
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEiKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 372 CELEELQHHRQVSEEEQRRL----------------QRELKCAQNEVLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQ 435
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEdllkeekkeeleileeEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 436 NELLKMQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCE-KEKLLERQQQLQEELQCHEAELQHLRDTV 514
Cdd:pfam02463 479 LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHgRLGDLGVAVENYKVAISTAVIVEVSATAD 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 515 ASFKESNEKDTETHAQLQEMKQLYQASKDELERQKHMYDQLEQDLLLCQLELKELKASHpipEDKGKCANKCDTLLSRLT 594
Cdd:pfam02463 559 EVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADE---DDKRAKVVEGILKDTELT 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 595 ELQEKYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELhrltlplpksgLLLKSQELLTKLEDLCELQLLYQGMQEE 674
Cdd:pfam02463 636 KLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELL-----------EIQELQEKAESELAKEEILRRQLEIKKK 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 675 QKKLIQNQDCVLKEQLEIHEELRRFKESHFQEVLENPDDSKLAKSSKCNRNKQSKLLMEQMQALQVMYDAGQAKQELLQQ 754
Cdd:pfam02463 705 EQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTE 784
|
650 660
....*....|....*....|....*....
gi 1370510765 755 EQGRLLEERKRLQADLQLCLEEMQLLQVQ 783
Cdd:pfam02463 785 KLKVEEEKEEKLKAQEEELRALEEELKEE 813
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
107-593 |
2.38e-05 |
|
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: 48.68 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLElQGLLEDERLASAQ-QAEVFTKQIQQLQGELRSLREEISLLEHEKESE 185
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQHGAFLDADIE-TAAADQEQLPSWQsELENLEERLKALTGKHQDVTAKYNRRRSKIKEQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 186 LKEIEQELHLAQAEIqslRQAAEDSATEHESDIASLQEDLcRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLg 265
Cdd:pfam12128 388 NNRDIAGIKDKLAKI---REARDRQLAVAEDDLQALESEL-REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPEL- 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 266 LSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGqLADLESERTQRATERWLQSQtlsmtSAESQTSEMDFLEPDPE 345
Cdd:pfam12128 463 LLQLENFDERIERAREEQEAANAEVERLQSELRQARK-RRDQASEALRQASRRLEERQ-----SALDELELQLFPQAGTL 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 346 MQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQrrlqreLKCAQNEVLRFQTSHSVTQNEELKSRLCTLQ 425
Cdd:pfam12128 537 LHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELN------LYGVKLDLKRIDVPEWAASEEELRERLDKAE 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 426 KKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELlcRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCH-E 504
Cdd:pfam12128 611 EALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARL--DLRRLFDEKQSEKDKKNKALAERKDSANERLNSlE 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 505 AELQHLRDTVASFKESNEKDTETH--AQLQEMKQLYQASKDELERQKH----MYDQLEQDLLLCQLELK-ELKASHPIPE 577
Cdd:pfam12128 689 AQLKQLDKKHQAWLEEQKEQKREArtEKQAYWQVVEGALDAQLALLKAaiaaRRSGAKAELKALETWYKrDLASLGVDPD 768
|
490
....*....|....*.
gi 1370510765 578 DKGKCANKCDTLLSRL 593
Cdd:pfam12128 769 VIAKLKREIRTLERKI 784
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
82-792 |
2.72e-05 |
|
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: 48.81 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 82 EQVQKggsvgslsvNKHRGLSLTETELEELRAQVLQLVaeleetrelaGQHEDDSLELQGLLEDERLASAQQAEVfTKQI 161
Cdd:pfam02463 278 EKEKK---------LQEEELKLLAKEEEELKSELLKLE----------RRKVDDEEKLKESEKEKKKAEKELKKE-KEEI 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 162 QQLQGELRSLREEISLLEHEKESELKEIEQELHLAQAEIQSLRQAAEDSATEhESDIASLQEDLCRMQNELEDMERIRGD 241
Cdd:pfam02463 338 EELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA-AKLKEEELELKSEEEKEAQLLLELARQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 242 YEMEiasLRAEMEMKSSEPSGSLGLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQ 321
Cdd:pfam02463 417 LEDL---LKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 322 SQTLSMTSAESQTSEMDFLEPdpemqLLRQQLRDAEEQMHGMKNKCQELccELEELQHHRQVSEEEQRRLQRELKCAQNE 401
Cdd:pfam02463 494 KLEERSQKESKARSGLKVLLA-----LIKDGVGGRIISAHGRLGDLGVA--VENYKVAISTAVIVEVSATADEVEERQKL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 402 VLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVmkstLVENQSEKELLCRLQKLHLQHQN 481
Cdd:pfam02463 567 VRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDD----KRAKVVEGILKDTELTKLKESAK 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 482 VTCEKEKLLERQQQLQEELQCHEAELQHLRDTVASFKESNEK---DTETHAQLQEMKQLYQASKDELERQKHMYDQLEQD 558
Cdd:pfam02463 643 AKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKaesELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 559 LLLCQLELKELKASHPIPEDKGKCANKCDTLLSRL-----------TELQEKYKASQKEMGQLQMEQCELLEDQRRMqEE 627
Cdd:pfam02463 723 LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLkkeekeeekseLSLKEKELAEEREKTEKLKVEEEKEEKLKAQ-EE 801
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 628 QGQLQEELHRLTLPLPKSGLLLKSQELLTKLEDLCELQLLYQGMQEEQKKLIQNQDCVLKEQLEIHEELRRFKESHFQEV 707
Cdd:pfam02463 802 ELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEE 881
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 708 LENPDD--SKLAKSSKCNRNKQSKLLMEQMQALQVMYDAGQAKQELLQQEQGRLLEERKRLQADLQLCLEEMQLLQVQSP 785
Cdd:pfam02463 882 QKLKDEleSKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEER 961
|
....*..
gi 1370510765 786 SIKMSLE 792
Cdd:pfam02463 962 NKRLLLA 968
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
105-623 |
3.46e-05 |
|
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: 48.43 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 105 ETELEELRAQVLQLVAELEETRELAGQHED--DSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEK 182
Cdd:TIGR00618 337 QSSIEEQRRLLQTLHSQEIHIRDAHEVATSirEISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRT 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 183 ESE------LKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQE----------DLCRMQNELEDMERI---RGDYE 243
Cdd:TIGR00618 417 SAFrdlqgqLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQEsaqslkereqQLQTKEQIHLQETRKkavVLARL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 244 MEIASLRAEMEMKSSEPSGSLGLSDYSG-LQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESE--RTQRATERWL 320
Cdd:TIGR00618 497 LELQEEPCPLCGSCIHPNPARQDIDNPGpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQmqEIQQSFSILT 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 321 QSQTLSMTSAESQTSEMDFLEPDPEMQllrqqlrDAEEQMHGMKNKCQELccELEELQHHRQVSEEEQRRLQRElkcAQN 400
Cdd:TIGR00618 577 QCDNRSKEDIPNLQNITVRLQDLTEKL-------SEAEDMLACEQHALLR--KLQPEQDLQDVRLHLQQCSQEL---ALK 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 401 EVLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQlqlqTELRQLKVMKSTLVENQSE-KELLCRLQKLHLQH 479
Cdd:TIGR00618 645 LTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQ----SEKEQLTYWKEMLAQCQTLlRELETHIEEYDREF 720
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 480 QNVTCEKEKLLERQQQLQEELQCHEAELQHLRDTV--ASFKESNEKDTETHAQLQEMKQLYQASKDELERQKhmydQLEQ 557
Cdd:TIGR00618 721 NEIENASSSLGSDLAAREDALNQSLKELMHQARTVlkARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNR----LREE 796
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510765 558 DlllcQLELKELKASHP--IPEDKGKCANKCDTLLSRLTELQEKYKASQKEMGQLQMEQCELLEDQRR 623
Cdd:TIGR00618 797 D----THLLKTLEAEIGqeIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
107-267 |
3.66e-05 |
|
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: 47.06 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 107 ELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEHEKESEL 186
Cdd:pfam09787 62 EIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 187 KEIEQELHLAQAEIQSlRQAAEDSATEHESDIASLQEDLCRMQNELEDM--ERIRGDYEMEiaslRAEMEMKSSEPSGSL 264
Cdd:pfam09787 142 KDREAEIEKLRNQLTS-KSQSSSSQSELENRLHQLTETLIQKQTMLEALstEKNSLVLQLE----RMEQQIKELQGEGSN 216
|
...
gi 1370510765 265 GLS 267
Cdd:pfam09787 217 GTS 219
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
101-252 |
3.91e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 101 LSLTETELEELRAQVLQLVAELEETRELAGQH-------EDDSLELQGLLEDERLASA-QQAEVFTKQIQQLQGELRSLR 172
Cdd:COG3883 60 LEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsGGSVSYLDVLLGSESFSDFlDRLSALSKIADADADLLEELK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 173 EEISLLEhEKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAE 252
Cdd:COG3883 140 ADKAELE-AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
105-616 |
4.67e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.81 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 105 ETELEELRAQVLQLVAELE----ETRELAGQHEDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLREEISLLEH 180
Cdd:pfam15921 259 ELLLQQHQDRIEQLISEHEveitGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 181 EKESELKEIEQELHLAQAEIQSLRQAAEDSATEH---ESDIASLQEDLCRMQNEL---------------------EDME 236
Cdd:pfam15921 339 MYEDKIEELEKQLVLANSELTEARTERDQFSQESgnlDDQLQKLLADLHKREKELslekeqnkrlwdrdtgnsitiDHLR 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 237 RIRGDYEMEIASLRAEMEMKSSEPSGSL--GLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLE-SERTQ 313
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSECQGQMerQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLEsSERTV 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 314 RATERWLQSQTLSMtsaESQTSEMDFLEPDPEMQLLR-QQLRDAEEQMHGMKNKCQELCCELEEL--------------- 377
Cdd:pfam15921 499 SDLTASLQEKERAI---EATNAEITKLRSRVDLKLQElQHLKNEGDHLRNVQTECEALKLQMAEKdkvieilrqqienmt 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 378 ----QHHRQVS--EEEQRRLQRELKCAQNEVLRFQT--SHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTE- 448
Cdd:pfam15921 576 qlvgQHGRTAGamQVEKAQLEKEINDRRLELQEFKIlkDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQEr 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 449 ---LRQLKVMKSTLVENQSEKELLCRlqklhlqhqNVTCEKEKLLERQQQLQEELQCHEAELQHLRDTVASFKESNEKDT 525
Cdd:pfam15921 656 dqlLNEVKTSRNELNSLSEDYEVLKR---------NFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAM 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 526 ETHAQLQEMKQLYQASKDELERQKHMYDQLEQDLLLCQLELKELKAS-----HPIPEDKGKCANKCDTLLSRLTELQEKY 600
Cdd:pfam15921 727 KVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKlsqelSTVATEKNKMAGELEVLRSQERRLKEKV 806
|
570
....*....|....*...
gi 1370510765 601 KASQKEM--GQLQMEQCE 616
Cdd:pfam15921 807 ANMEVALdkASLQFAECQ 824
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
101-296 |
5.65e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 101 LSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGL-------------LEDERLASAQQAEVFTKQIQQLQGE 167
Cdd:PRK02224 215 LAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLeaeiedlretiaeTEREREELAEEVRDLRERLEELEEE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 168 LRSLREE----------ISLLEHEKESELKEIEQELHLAQAEIQSLRQAAE---DSATEHESDIASLQEDLCRMQNELED 234
Cdd:PRK02224 295 RDDLLAEaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAEslrEDADDLEERAEELREEAAELESELEE 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510765 235 MERIRGDYEMEIASLRAEMEMKSSE----PSGSLGLSDYSG-LQEELQELRERYHFLNEEYRALQES 296
Cdd:PRK02224 375 AREAVEDRREEIEELEEEIEELRERfgdaPVDLGNAEDFLEeLREERDELREREAELEATLRTARER 441
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
101-698 |
7.94e-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: 7.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 101 LSLTETELEELRAQVLQLvaelEETRELAGQHEDDSLELQGLledERLASAQQAEVFTKQIQQLQGELRSLREEISLLEH 180
Cdd:COG4913 237 LERAHEALEDAREQIELL----EPIRELAERYAAARERLAEL---EYLRAALRLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 181 EKEselkEIEQELHLAQAEIQSLRQAAEDSATEhesDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEmkssep 260
Cdd:COG4913 310 ELE----RLEARLDALREELDELEAQIRGNGGD---RLEQLEREIERLERELEERERRRARLEALLAALGLPLP------ 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 261 sgsLGLSDYSGLQEELQELRERyhfLNEEYRALQESNSSLTGQLADLESERTQRATE-RWLQSQTLSMtsaesqtsemdf 339
Cdd:COG4913 377 ---ASAEEFAALRAEAAALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEiASLERRKSNI------------ 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 340 lepDPEMQLLRQQLRDAeeqmhgMKNKCQELC--CELEEL--------------------------QHHRQVSEE-EQRR 390
Cdd:COG4913 439 ---PARLLALRDALAEA------LGLDEAELPfvGELIEVrpeeerwrgaiervlggfaltllvppEHYAAALRWvNRLH 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 391 LQRELkcaqnEVLRFQTSHSVTQNEELKSRlcTLQKKYDTSQDEQNELLKMQLQlqtelRQLKVMKstlVENQSE----- 465
Cdd:COG4913 510 LRGRL-----VYERVRTGLPDPERPRLDPD--SLAGKLDFKPHPFRAWLEAELG-----RRFDYVC---VDSPEElrrhp 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 466 ---------KELLCRLQK---LHLQHQNVTCE--KEKLLERqqqlqeelqchEAELQHLRDTVASFKESNEKDTETHAQL 531
Cdd:COG4913 575 raitragqvKGNGTRHEKddrRRIRSRYVLGFdnRAKLAAL-----------EAELAELEEELAEAEERLEALEAELDAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 532 QEMKQLYQASKDELERQK------HMYDQLEQdlllcqlELKELKASHPipedkgkcankcdtllsRLTELQEKYKASQK 605
Cdd:COG4913 644 QERREALQRLAEYSWDEIdvasaeREIAELEA-------ELERLDASSD-----------------DLAALEEQLEELEA 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 606 EMGQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLpKSGLLLKSQELLTKLEDLCELQLLYQGMQEEQKKLIQNQDCV 685
Cdd:COG4913 700 ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL-EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDAL 778
|
650
....*....|...
gi 1370510765 686 LKEQLEIHEELRR 698
Cdd:COG4913 779 RARLNRAEEELER 791
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
96-606 |
1.02e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 96 NKHRGLSLTETELEELRAQVLQLVAELEETRELAGQHEddslELQGLLEDERlasaqqaevftKQIQQLQGELRSLREEI 175
Cdd:PRK03918 197 EKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELE-----------KELESLEGSKRKLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 176 SLLEhEKESELKEIEQELHLAQAEIQSLRQAAEDSATehesdiasLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEM 255
Cdd:PRK03918 262 RELE-ERIEELKKEIEELEEKVKELKELKEKAEEYIK--------LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 256 KSSEPSGSLGLSD-YSGLQEELQELRERyHFLNEEYRALQESNSSLTGQLADLESERTQRATERwlqsqtLSMTSAESQT 334
Cdd:PRK03918 333 LEEKEERLEELKKkLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTGLTPEKLEKELEE------LEKAKEEIEE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 335 SEMDFLEPDPEMQLLRQQLRDAEEQMHGMKNKC----------------QELCCELEELQHHRQVSEEEQRRLQRELKCA 398
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelteehrkellEEYTAELKRIEKELKEIEEKERKLRKELREL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 399 QNEVL---RFQTSHSVT-QNEELKSRLCTLQ--------KKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSE- 465
Cdd:PRK03918 486 EKVLKkesELIKLKELAeQLKELEEKLKKYNleelekkaEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKl 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 466 KELLCRLQKLH--LQHQNVTCEKE------------KLLERQQQLQEELQCHEAELQHLRDTV-ASFKESNEKDT---ET 527
Cdd:PRK03918 566 DELEEELAELLkeLEELGFESVEEleerlkelepfyNEYLELKDAEKELEREEKELKKLEEELdKAFEELAETEKrleEL 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 528 HAQLQEMKQLYqaSKDELERQKHMYDQLEQDL--LLCQLE------------LKELKASHPIPEDKGKCANKCDTLLSRL 593
Cdd:PRK03918 646 RKELEELEKKY--SEEEYEELREEYLELSRELagLRAELEelekrreeikktLEKLKEELEEREKAKKELEKLEKALERV 723
|
570
....*....|....*.
gi 1370510765 594 TELQEK---YKASQKE 606
Cdd:PRK03918 724 EELREKvkkYKALLKE 739
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
104-619 |
1.07e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 104 TETELEELRAQVLQLvaeleETRELAGQHEDDSLELQGLLEDERLASAQQaevFTKQIQQLQGELRSLREEISLLEHEKE 183
Cdd:PRK04863 584 LRQQLEQLQARIQRL-----AARAPAWLAAQDALARLREQSGEEFEDSQD---VTEYMQQLLERERELTVERDELAARKQ 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 184 SELKEIEQELHLAQAEIQSLRQAAED----SATEHESDIaSLQE------------------DLCRMQNELEDMERIRGD 241
Cdd:PRK04863 656 ALDEEIERLSQPGGSEDPRLNALAERfggvLLSEIYDDV-SLEDapyfsalygparhaivvpDLSDAAEQLAGLEDCPED 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 242 Y---EMEIASLR-AEMEMKSSEPSGSLGLSD----YSG------------------LQEELQELRERYHFLNEEYRALQE 295
Cdd:PRK04863 735 LyliEGDPDSFDdSVFSVEELEKAVVVKIADrqwrYSRfpevplfgraarekrieqLRAEREELAERYATLSFDVQKLQR 814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 296 SNSSLTGQLA-------DLESERTQRATERWLQSQTLSMTSAESQTsemdflepdpemQLLRQQLRDAEEQMHGMkNKCQ 368
Cdd:PRK04863 815 LHQAFSRFIGshlavafEADPEAELRQLNRRRVELERALADHESQE------------QQQRSQLEQAKEGLSAL-NRLL 881
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 369 ---------ELCCELEELQHHRQVSEEEQRRLQRElkcaQNEVLRFQTSHSVTQNEElkSRLCTLQKKYDTSQDEQnELL 439
Cdd:PRK04863 882 prlnlladeTLADRVEEIREQLDEAEEAKRFVQQH----GNALAQLEPIVSVLQSDP--EQFEQLKQDYQQAQQTQ-RDA 954
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 440 KMQLQLQTELRQLKVMKS------TLVENQSEKELLcrLQKLHLQHQNVTCEKEKLLErqqqlqeelqcHEAELQHLRDT 513
Cdd:PRK04863 955 KQQAFALTEVVQRRAHFSyedaaeMLAKNSDLNEKL--RQRLEQAEQERTRAREQLRQ-----------AQAQLAQYNQV 1021
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 514 VASFKESNEKDTETHAQL-QEMKQL-YQASKDELERQKHMYDQLEQDLLLCQLELKELKAshpipeDKGKCANKCDTLLS 591
Cdd:PRK04863 1022 LASLKSSYDAKRQMLQELkQELQDLgVPADSGAEERARARRDELHARLSANRSRRNQLEK------QLTFCEAEMDNLTK 1095
|
570 580
....*....|....*....|....*...
gi 1370510765 592 RLTELQEKYKASQKEMGQLQMEQCELLE 619
Cdd:PRK04863 1096 KLRKLERDYHEMREQVVNAKAGWCAVLR 1123
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
104-792 |
1.16e-04 |
|
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: 46.60 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 104 TETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLED-----ERLASAQQAEVfTKQIQQLQGELRSLREEISLL 178
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElnkkiKDLGEEEQLRV-KEKIGELEAEIASLERSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 179 EHEKE---SELKEIEQELHLAQAEIQSLRQAAEDSATEHES---DIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAE 252
Cdd:TIGR02169 314 ERELEdaeERLAKLEAEIDKLLAEIEELEREIEEERKRRDKlteEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 253 MEMKSSEPSGSLGLSDYsgLQEELQELRERYHFLNEEYRALQEsnssltgQLADLESERTQRATERWLQSQTLSMTSAEs 332
Cdd:TIGR02169 394 LEKLKREINELKRELDR--LQEELQRLSEELADLNAAIAGIEA-------KINELEEEKEDKALEIKKQEWKLEQLAAD- 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 333 qtsemdflepdpeMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQR--RLQRELKCAQNEVL------- 403
Cdd:TIGR02169 464 -------------LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRggRAVEEVLKASIQGVhgtvaql 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 404 -----RFQTS----------HSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQlQLQTELRQLK--------------- 453
Cdd:TIGR02169 531 gsvgeRYATAievaagnrlnNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMR-DERRDLSILSedgvigfavdlvefd 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 454 ---------VMKSTLVEN--------------------------------QSEKELLCRLQKLHLQHQNVTCEKEKLLER 492
Cdd:TIGR02169 610 pkyepafkyVFGDTLVVEdieaarrlmgkyrmvtlegelfeksgamtggsRAPRGGILFSRSEPAELQRLRERLEGLKRE 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 493 QQQLQEELQCHEAELQHLRDTVasfKESNEKDTETHAQLQEMKQLYQASKDELErqkhmydQLEQDLLLCQLELKELKAs 572
Cdd:TIGR02169 690 LSSLQSELRRIENRLDELSQEL---SDASRKIGEIEKEIEQLEQEEEKLKERLE-------ELEEDLSSLEQEIENVKS- 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 573 hpipedkgkcanKCDTLLSRLTELQEKYKASQKEMGQLqmEQCELLEDQRRMQEEQGQLQEELHRLTLPLpksglllksQ 652
Cdd:TIGR02169 759 ------------ELKELEARIEELEEDLHKLEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARL---------R 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 653 ELLTKLEDL-CELQLLYQGMQEEQKKLIQNQDCVLKEQLEIhEELRRFKESHFQEVLENPDDSKLAKSSKCNRNKQSKLL 731
Cdd:TIGR02169 816 EIEQKLNRLtLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI-ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510765 732 MEQMQALQVMYDAGQAKQELLQQEQGRLLEERKRLQADLQlCLEEMQLLQVQSPSIKMSLE 792
Cdd:TIGR02169 895 EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS-EIEDPKGEDEEIPEEELSLE 954
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
107-401 |
2.10e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.50 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 107 ELEELRAQVLQLVAELEETRELAGQHeDDSLELQGLLEDERLASAQQAEVFTKQIQQLQGELRSLrEEISLLEHEKESEL 186
Cdd:pfam05557 22 ELEHKRARIELEKKASALKRQLDRES-DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYL-EALNKKLNEKESQL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 187 KEIEQELHLAQAEIQSLRQAAEDSA---TEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLR-AEMEMKSSEPSG 262
Cdd:pfam05557 100 ADAREVISCLKNELSELRRQIQRAElelQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAeAEQRIKELEFEI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 263 SLGLSDYSGLQE---------ELQELRERYHFLNEEYRALQESNSSLTGQLADLES-------------------ERTQR 314
Cdd:pfam05557 180 QSQEQDSEIVKNskselaripELEKELERLREHNKHLNENIENKLLLKEEVEDLKRklereekyreeaatlelekEKLEQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 315 ATERWL---QSQTLSMTSAESQTSEMDFLEPD-----PEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEE 386
Cdd:pfam05557 260 ELQSWVklaQDTGLNLRSPEDLSRRIEQLQQReivlkEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKA 339
|
330
....*....|....*
gi 1370510765 387 EQRRLQRELKCAQNE 401
Cdd:pfam05557 340 LVRRLQRRVLLLTKE 354
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
71-767 |
2.18e-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: 45.73 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 71 EEEEEEV----EEEEEQVQKGGSVGSLSVNKHRGLSLTETELEEL------------------------RAQVLQLVAEL 122
Cdd:pfam02463 282 KLQEEELkllaKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAekelkkekeeieelekelkeleikREAEEEEEEEL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 123 EETRELAGQHEDDSLELQGLLEDERLASAQQAE------VFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQELHLA 196
Cdd:pfam02463 362 EKLQEKLEQLEEELLAKKKLESERLSSAAKLKEeelelkSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIEL 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 197 QAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLGLSDYSGLQEEL 276
Cdd:pfam02463 442 KQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 277 ------QELRERYHFLNEEYRALQESN----SSLTGQLADLESERTQRATERWLQSQTLS--MTSAESQTSEMDFLEPDP 344
Cdd:pfam02463 522 griisaHGRLGDLGVAVENYKVAISTAviveVSATADEVEERQKLVRALTELPLGARKLRllIPKLKLPLKSIAVLEIDP 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 345 EMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRqvsEEEQRRLQRELKCAQNEVLRFQTSHSVTQNEELKSRLCTL 424
Cdd:pfam02463 602 ILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLK---ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEI 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 425 QKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCHE 504
Cdd:pfam02463 679 QELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK 758
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 505 A--ELQHLRDTVASFKESNEKDTETHAQLQEMKQLYQASKDELERQKHMYDQLEQDLLLCQLELKELKASHPIPEDKGKC 582
Cdd:pfam02463 759 KeeKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEEL 838
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 583 ANKCDTLLSRLTELQEKYKASQKEMGQLQMEQCELLEdqrrmqeeqgqlqeeLHRLTLPLPKSGLLLKSQELLTKLEDLC 662
Cdd:pfam02463 839 ALELKEEQKLEKLAEEELERLEEEITKEELLQELLLK---------------EEELEEQKLKDELESKEEKEKEEKKELE 903
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 663 ELQLLYQgMQEEQKKLIQNQDCVLKEQLEI-HEELRRFKESHFQEVLENPDDSKLAKSSKCNRNKQSKLLMEQ--MQALQ 739
Cdd:pfam02463 904 EESQKLN-LLEEKENEIEERIKEEAEILLKyEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVnlMAIEE 982
|
730 740
....*....|....*....|....*...
gi 1370510765 740 VMYDAGQAKQELLQQEqgRLLEERKRLQ 767
Cdd:pfam02463 983 FEEKEERYNKDELEKE--RLEEEKKKLI 1008
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
191-317 |
2.41e-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: 44.15 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 191 QELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGSLGLSDYS 270
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYE 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1370510765 271 GLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATE 317
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE 139
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
244-460 |
2.64e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 244 MEIASLRAEMEM--KSSEPSGSLGLSDYSGLQEELQELRERyhflNEEYRALQESNSSLTGQLADLESERTQRATERWLQ 321
Cdd:COG4717 46 MLLERLEKEADElfKPQGRKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 322 SQTLsmtsaesqtsemDFLEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELKCAQNE 401
Cdd:COG4717 122 EKLL------------QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370510765 402 VLRfQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNEL------LKMQLQLQTELRQLKVMKSTLV 460
Cdd:COG4717 190 TEE-ELQDLAEELEELQQRLAELEEELEEAQEELEELeeeleqLENELEAAALEERLKEARLLLL 253
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
104-402 |
7.43e-04 |
|
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: 43.88 E-value: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 104 TETELEE----LRAQVLQLVAELEETRELAGQHEDDSLELQGLLEderlASAQQAEVFTKQIQQLQGELRSLREEISlle 179
Cdd:TIGR00606 689 TEAELQEfisdLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAP----GRQSIIDLKEKEIPELRNKLQKVNRDIQ--- 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 180 hEKESELKEIEQELHLAQAEiqslrqaaEDSATEHESDIASLQedlcRMQNELEDMERirgdyemeiaslraEMEMKSSE 259
Cdd:TIGR00606 762 -RLKNDIEEQETLLGTIMPE--------EESAKVCLTDVTIME----RFQMELKDVER--------------KIAQQAAK 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 260 PSGSLGLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWlqsqTLSMTSAESQTSEMDF 339
Cdd:TIGR00606 815 LQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKL----QIGTNLQRRQQFEEQL 890
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510765 340 LEPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRqvsEEEQRRLQRELKCAQNEV 402
Cdd:TIGR00606 891 VELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSK---ETSNKKAQDKVNDIKEKV 950
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
509-792 |
7.81e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.74 E-value: 7.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 509 HLRDTVASFKESNEKDTEthaQLQEMKQLYQASKDELERQKHMYDQLEQD-LLLCQLELKELKASHPIPEDKGKCANKCD 587
Cdd:PLN02939 97 HNRASMQRDEAIAAIDNE---QQTNSKDGEQLSDFQLEDLVGMIQNAEKNiLLLNQARLQALEDLEKILTEKEALQGKIN 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 588 TLLSRLTELQEKYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPksglLLKSQELLTKLEdlcelqll 667
Cdd:PLN02939 174 ILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELD----VLKEENMLLKDD-------- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 668 yqgMQEEQKKLIQNQDCvlKEQLEIHEELRRFKESHFQEVlenpdDSKLAkSSKCNRNKQSKL----LMEQMQALQVMYD 743
Cdd:PLN02939 242 ---IQFLKAELIEVAET--EERVFKLEKERSLLDASLREL-----ESKFI-VAQEDVSKLSPLqydcWWEKVENLQDLLD 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370510765 744 --AGQAKQELLQQEQGRLLEER-KRLQADL------QLCLEEMQLLQVQSPSIKMSLE 792
Cdd:PLN02939 311 raTNQVEKAALVLDQNQDLRDKvDKLEASLkeanvsKFSSYKVELLQQKLKLLEERLQ 368
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
159-317 |
7.97e-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: 42.60 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 159 KQIQQLQGELRSLREEISLLEHEK---ESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASL-----QEDLCRMQN 230
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELaalEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnNKEYEALQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 231 ELEDMERIRGDYEMEIASLRAEMEMKSSEpsgslglsdYSGLQEELQELRERyhfLNEEYRALQESNSSLTGQLADLESE 310
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEE---------LAELEAELAELEAE---LEEKKAELDEELAELEAELEELEAE 164
|
....*..
gi 1370510765 311 RTQRATE 317
Cdd:COG1579 165 REELAAK 171
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
909-1020 |
8.28e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 909 KLQAVQAMYQISQEEHSQLQEQMEKLLAKQKDLKEELDACEREFKECMECLEKPMAPQ-------------NDKNEIKEL 975
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEReiaeleaelerldASSDDLAAL 690
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1370510765 976 QTKLRELQLQYQASMDEQGRLLVVQEQLEGQLQCCQEELRQLREK 1020
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
158-739 |
8.53e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.56 E-value: 8.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 158 TKQIQQLQGELRSLREEISLLEHEKESELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMER 237
Cdd:pfam05483 73 SEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 238 IRgdyemEIASLRAEMEMKSSEPSgslglsdySGLQEELQELRERYHFLN----------EEYRaLQESNSSLT------ 301
Cdd:pfam05483 153 TR-----HLCNLLKETCARSAEKT--------KKYEYEREETRQVYMDLNnniekmilafEELR-VQAENARLEmhfklk 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 302 ---GQLADLESERTQRATERWLQSQTL--SMTSAESQTSEMDFL--EPDPEMQLLRQQLRDAEEQMHGMKNKCQELCCEL 374
Cdd:pfam05483 219 edhEKIQHLEEEYKKEINDKEKQVSLLliQITEKENKMKDLTFLleESRDKANQLEEKTKLQDENLKELIEKKDHLTKEL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 375 EELQHHRQVSEEEQRRLQRELKCAQNEVLRF--------------QTSHSVTQNEeLKSRLCTLQKKYDTSQ------DE 434
Cdd:pfam05483 299 EDIKMSLQRSMSTQKALEEDLQIATKTICQLteekeaqmeelnkaKAAHSFVVTE-FEATTCSLEELLRTEQqrleknED 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 435 QNELLKMQLQLQT-ELRQL-KVMKSTLVENQSEKELLCRLQKLHLQHQNVTCEKEKLLERQQQLQEELQCHEAELQHLRD 512
Cdd:pfam05483 378 QLKIITMELQKKSsELEEMtKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEI 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 513 TVASFKESNEKdtethaQLQEMKQLyqasKDELERQKHMYDQLEQDLLLCQLELKEL--KASHPI------PEDKGKCAN 584
Cdd:pfam05483 458 QLTAIKTSEEH------YLKEVEDL----KTELEKEKLKNIELTAHCDKLLLENKELtqEASDMTlelkkhQEDIINCKK 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 585 KCDTLLSRLTELQEKYKASQKEMGQLQME--------QCELLEDQRRMQEEQGQLQEELHRLTLPLPKSGLLLKSQELLT 656
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRDELESVREEfiqkgdevKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 657 K-LEDL-CELQLLYQGMQEEQKKLIQNQDCVLKEQLEIHEELRRFKE--SHFQEVLEnpdDSKLAKSSKCNRNKQSKLLM 732
Cdd:pfam05483 608 KnIEELhQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEiiDNYQKEIE---DKKISEEKLLEEVEKAKAIA 684
|
....*..
gi 1370510765 733 EQMQALQ 739
Cdd:pfam05483 685 DEAVKLQ 691
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
186-451 |
1.09e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 186 LKEIEQELHLAQAEIQSLRQAAE--DSATEHESDIASLQEDLCRMQNELEDMERirgdyemEIASLRAEMEMKSSEPSGS 263
Cdd:PRK11281 48 LNKQKLLEAEDKLVQQDLEQTLAllDKIDRQKEETEQLKQQLAQAPAKLRQAQA-------ELEALKDDNDEETRETLST 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 264 LGLSDysgLQEELQELRERyhfLNEEYRALQESNSSLTGQlaDLESERTQRA-TERWLQSQTLSMTSAESQTSEMDfLEP 342
Cdd:PRK11281 121 LSLRQ---LESRLAQTLDQ---LQNAQNDLAEYNSQLVSL--QTQPERAQAAlYANSQRLQQIRNLLKGGKVGGKA-LRP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 343 DpemqllRQQLRDAEEQMHGMKNKCQELccELEE-------LQHHRQVSEEEQRRLQRELKCAQ---NEVLRFQTSHSVT 412
Cdd:PRK11281 192 S------QRVLLQAEQALLNAQNDLQRK--SLEGntqlqdlLQKQRDYLTARIQRLEHQLQLLQeaiNSKRLTLSEKTVQ 263
|
250 260 270
....*....|....*....|....*....|....*....
gi 1370510765 413 QNEELKsrlctlqkkyDTSQDEQNELLKMQLQLQTELRQ 451
Cdd:PRK11281 264 EAQSQD----------EAARIQANPLVAQELEINLQLSQ 292
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
138-400 |
1.11e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.60 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 138 ELQGLleDERLASaqqaevFTKQIQQLQGELRSLREEISLLEHEKESELKEIEQelhLAQAEIQSLRQAAEDSATEH--- 214
Cdd:pfam00038 5 QLQEL--NDRLAS------YIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYS---LYEKEIEDLRRQLDTLTVERarl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 215 ESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLR----------AEMEMKssepsgslglsdYSGLQEELQELRERYh 284
Cdd:pfam00038 74 QLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRkdldeatlarVDLEAK------------IESLKEELAFLKKNH- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 285 flNEEYRALQESNSS--------------LTGQLADLE------SERTQRATERWLQSQTLSMTSAESQTSEMdflepdp 344
Cdd:pfam00038 141 --EEEVRELQAQVSDtqvnvemdaarkldLTSALAEIRaqyeeiAAKNREEAEEWYQSKLEELQQAAARNGDA------- 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510765 345 emqllrqqLRDAEEQMHGMKNKCQELCCELEELQH-----HRQVSEEEQrRLQRELKCAQN 400
Cdd:pfam00038 212 --------LRSAKEEITELRRTIQSLEIELQSLKKqkaslERQLAETEE-RYELQLADYQE 263
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
144-315 |
1.20e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 144 EDERLASAQQAEVFTKQIQQLQGELRSLREEISllehEKESELKEIEQELHLAQAEIQSLrqaaedsatehESDIASLQE 223
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELE----ELNEEYNELQAELEALQAEIDKL-----------QAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 224 DLCRMQNELEdmERIRGDYEMEIASLRAEMEMKSSEPSGSLG---------------LSDYSGLQEELQELRERyhfLNE 288
Cdd:COG3883 80 EIEERREELG--ERARALYRSGGSVSYLDVLLGSESFSDFLDrlsalskiadadadlLEELKADKAELEAKKAE---LEA 154
|
170 180
....*....|....*....|....*..
gi 1370510765 289 EYRALQESNSSLTGQLADLESERTQRA 315
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQE 181
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
209-471 |
1.30e-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: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 209 DSATEHESDIASLQEDLCRMQNELEDMERIRGDYEmEIASLRAEMEMKSSEpsgsLGLSDYSGLQEELQELRERYHFLNE 288
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEPIRELAE-RYAAARERLAELEYL----RAALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 289 EYRALQESNSSLTGQLADLESERtQRATERWLQSQTlsmtsaesqtsemdflepdPEMQLLRQQLRDAEEQMHGMKNKCQ 368
Cdd:COG4913 303 ELARLEAELERLEARLDALREEL-DELEAQIRGNGG-------------------DRLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 369 ELCCELEELQHHRQVSEEEQRRLQRELKCAQnevlrfqtshsvtqnEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTE 448
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRAEAAALL---------------EALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
250 260
....*....|....*....|....
gi 1370510765 449 LRQLKVMKSTLVENQSE-KELLCR 471
Cdd:COG4913 428 IASLERRKSNIPARLLAlRDALAE 451
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
109-295 |
1.34e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 109 EELRAQV--LQLVAELEETRELAGQHEDDSLELQGLLEDERlasaQQAEVFTKQIQQLQGELRSLREEISLLEHEKESEL 186
Cdd:PRK11281 39 ADVQAQLdaLNKQKLLEAEDKLVQQDLEQTLALLDKIDRQK----EETEQLKQQLAQAPAKLRQAQAELEALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 187 KEIEQELHLAQ-----AEIQSLRQAAEDSATEHESDIASLQEDLCRMQNEL-EDMERI---------------------R 239
Cdd:PRK11281 115 RETLSTLSLRQlesrlAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALyANSQRLqqirnllkggkvggkalrpsqR 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370510765 240 GDYEMEIASLRAEMEMKSSEPSGSLGLSDYsgLQEELQELRERYHFLNEEYRALQE 295
Cdd:PRK11281 195 VLLQAEQALLNAQNDLQRKSLEGNTQLQDL--LQKQRDYLTARIQRLEHQLQLLQE 248
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
99-249 |
1.37e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 99 RGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQgllederlASAQQAEVFTKQIQQLQGELRSLREEISLL 178
Cdd:PRK09039 46 REISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLR--------ASLSAAEAERSRLQALLAELAGAGAAAEGR 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370510765 179 EHEKESELKEIEQELHLAQAEIQSLRQaaedsatehesDIASLQEDLCRMQNELEDMERIRGDYEMEIASL 249
Cdd:PRK09039 118 AGELAQELDSEKQVSARALAQVELLNQ-----------QIAALRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
237-453 |
1.46e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.05 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 237 RIRGDYEMEIASLRaememkssEPSGSLGLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQrat 316
Cdd:pfam09787 18 RILQSKEKLIASLK--------EGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQE--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 317 erwlqsqtlsmtsaesqtsemdflepdpEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRR----LQ 392
Cdd:pfam09787 87 ----------------------------EAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRskatLQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370510765 393 RELKCAQNEV--LRFQ---TSHSVTQNEELKSRLCTL-------QKKYDTSQDEQNELlkmQLQLQTELRQLK 453
Cdd:pfam09787 139 SRIKDREAEIekLRNQltsKSQSSSSQSELENRLHQLtetliqkQTMLEALSTEKNSL---VLQLERMEQQIK 208
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
136-478 |
1.61e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 136 SLELQGLLEDERLASAQQAEVFTKQIQQLQGeLRSLREEISLLEHEKESeLKEIEQELHLAQAEIQslrqaaedsatEHE 215
Cdd:pfam12128 205 ILEDDGVVPPKSRLNRQQVEHWIRDIQAIAG-IMKIRPEFTKLQQEFNT-LESAELRLSHLHFGYK-----------SDE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 216 SDIASLQEDLCRMQNELEdmerirgdyeMEIASLRAEMEMKSSEPSGSLglsdySGLQEELQELRERYHFLNEEYRALQE 295
Cdd:pfam12128 272 TLIASRQEERQETSAELN----------QLLRTLDDQWKEKRDELNGEL-----SAADAAVAKDRSELEALEDQHGAFLD 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 296 SN-SSLTGQLADLESERTQ-RATERWLQSQTlsmTSAESQTSEMDFLEPDPEMQLLRQ----------QLRDAEEQMHGM 363
Cdd:pfam12128 337 ADiETAAADQEQLPSWQSElENLEERLKALT---GKHQDVTAKYNRRRSKIKEQNNRDiagikdklakIREARDRQLAVA 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 364 KNKCQELCCELEElQHHRQVSE--EEQRRLQRELkcaqnEVLRFQTShSVTQNEELKSRLCTLQKKYDTSQDEQNELLKM 441
Cdd:pfam12128 414 EDDLQALESELRE-QLEAGKLEfnEEEYRLKSRL-----GELKLRLN-QATATPELLLQLENFDERIERAREEQEAANAE 486
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1370510765 442 QLQLQTELRQLKvmksTLVENQSEK---------ELLCRLQKLHLQ 478
Cdd:pfam12128 487 VERLQSELRQAR----KRRDQASEAlrqasrrleERQSALDELELQ 528
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
96-452 |
1.96e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 96 NKHRGLSLTETELE-ELRAQVLQLVAE---LEETRELAGQHEDDSLELQGLLE--DERLASAQQAEVFTKQIQQLQGELR 169
Cdd:PRK04863 279 NERRVHLEEALELRrELYTSRRQLAAEqyrLVEMARELAELNEAESDLEQDYQaaSDHLNLVQTALRQQEKIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 170 SLREEislLEhekesELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQEDL-------CRMQNELEDMERIRG-- 240
Cdd:PRK04863 359 ELEER---LE-----EQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALdvqqtraIQYQQAVQALERAKQlc 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 241 ---DYEME-----IASLRAEME------------MKSSEPSGS------------LGLSDYSGLQEELQELRERYhflnE 288
Cdd:PRK04863 431 glpDLTADnaedwLEEFQAKEQeateellsleqkLSVAQAAHSqfeqayqlvrkiAGEVSRSEAWDVARELLRRL----R 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 289 EYRALQESNSSLTGQLADLESE-RTQRATERWLQSQTLSMTSAESQTSEMDFLEPDPEMQL--LRQQLRDAEEQMHGMKN 365
Cdd:PRK04863 507 EQRHLAEQLQQLRMRLSELEQRlRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLesLSESVSEARERRMALRQ 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 366 KCQELCCELEELQHHRQVSEEEQRRLQRelkcaqnevLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQL 445
Cdd:PRK04863 587 QLEQLQARIQRLAARAPAWLAAQDALAR---------LREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQAL 657
|
....*..
gi 1370510765 446 QTELRQL 452
Cdd:PRK04863 658 DEEIERL 664
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
465-788 |
2.17e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 465 EKELLCRLQKLHLQHQNVtcEKEKLLERQQQLQEELQCHEAELQHLRDTVASFKESNEKDTETHAQLQEMKQLYQASKDE 544
Cdd:COG1196 222 LKELEAELLLLKLRELEA--ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 545 LERQKHMYDQLEQDLLLCQLELKELKASHpipedkgkcANKCDTLLSRLTELQEKYKASQKEMGQLQMEQCELLEDQRRM 624
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAEL---------EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 625 QEEQGQLQEELHRLTlplpksglllksQELLTKLEDLCELQLLYQGMQEEQKKLIQNQDCVLKEQLEIHEELrrfkeshf 704
Cdd:COG1196 371 EAELAEAEEELEELA------------EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL-------- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 705 QEVLENPDDSKLAKSSkcnRNKQSKLLMEQMQALQVMYDAGQAKQELLQQEQGRLLEERKRLQADLQLCLEEMQLLQVQS 784
Cdd:COG1196 431 AELEEEEEEEEEALEE---AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
|
....
gi 1370510765 785 PSIK 788
Cdd:COG1196 508 EGVK 511
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
106-224 |
2.75e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 106 TELEELRAQVLQLVAELEEtrelagqheddslelqgLLEDERLASAQQAEVFTKQIQQLQGELRSLREEislLEHEKE-- 183
Cdd:COG0542 411 EELDELERRLEQLEIEKEA-----------------LKKEQDEASFERLAELRDELAELEEELEALKAR---WEAEKEli 470
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1370510765 184 SELKEIEQELHLAQAEIQSLRQAAEDSATEHESDIASLQED 224
Cdd:COG0542 471 EEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
105-781 |
3.24e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 105 ETELEELRAQVLQLVAELEETRELagqHEDDSLELQgllederlasaQQAEVFTKQIQQLQGElRSLREEISLLEHEKES 184
Cdd:pfam15921 77 ERVLEEYSHQVKDLQRRLNESNEL---HEKQKFYLR-----------QSVIDLQTKLQEMQME-RDAMADIRRRESQSQE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 185 ELK-EIEQELHlaqaEIQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGDYEMEIASLRAEMEMKSSEPSGS 263
Cdd:pfam15921 142 DLRnQLQNTVH----ELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRS 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 264 LGlsdySGLQEELQELRERYHFLNEEYRALQEsnssltgQLADLESErTQRATERWLQSQtlsmtsaesqtsemdflepd 343
Cdd:pfam15921 218 LG----SAISKILRELDTEISYLKGRIFPVED-------QLEALKSE-SQNKIELLLQQH-------------------- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 344 peMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRlqrelkcaQNEVLRFQTSHSVTQNEELKSRLCT 423
Cdd:pfam15921 266 --QDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARN--------QNSMYMRQLSDLESTVSQLRSELRE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 424 LQKKYdtsQDEQNELLKMQLQLQTELRQLKVMKSTLveNQSEKELLCRLQK----LHLQHQNVTCEKEKLLERQQQLQEe 499
Cdd:pfam15921 336 AKRMY---EDKIEELEKQLVLANSELTEARTERDQF--SQESGNLDDQLQKlladLHKREKELSLEKEQNKRLWDRDTG- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 500 lqcHEAELQHLRdtvasfKESNEKDTEthaqLQEMKQLYQASKDELErqkhmyDQLEQDLLLCQLELKELKASHPIPEDK 579
Cdd:pfam15921 410 ---NSITIDHLR------RELDDRNME----VQRLEALLKAMKSECQ------GQMERQMAAIQGKNESLEKVSSLTAQL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 580 GKCANKCDTLLSRLTELQEKYKASQKEMGQLqmeQCELLEDQRRMQEEQGQLQEELHRLTLPLPKSGLLLKSQELLTKLE 659
Cdd:pfam15921 471 ESTKEMLRKVVEELTAKKMTLESSERTVSDL---TASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 660 DLCE------------LQLLYQGMQEEQKKLIQNQDC-----VLKEQLEIHEELRRFKESHFQeVLENPDDSKLAKSSKc 722
Cdd:pfam15921 548 TECEalklqmaekdkvIEILRQQIENMTQLVGQHGRTagamqVEKAQLEKEINDRRLELQEFK-ILKDKKDAKIRELEA- 625
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370510765 723 nrnKQSKLLMEQMQALQVMYDAGQAKQElLQQEQGRLLEERKRLQADLQLCLEEMQLLQ 781
Cdd:pfam15921 626 ---RVSDLELEKVKLVNAGSERLRAVKD-IKQERDQLLNEVKTSRNELNSLSEDYEVLK 680
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
345-772 |
3.46e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 345 EMQLLRQQLRDAEEQMHgmknkcqelccELEELQHHRQVSEEEQRRLQRELKCAQNEVLRFQTshsVTQNEELKSRLCTL 424
Cdd:COG4717 72 ELKELEEELKEAEEKEE-----------EYAELQEELEELEEELEELEAELEELREELEKLEK---LLQLLPLYQELEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 425 QKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCEKEKLLerqqqlqeelqcHE 504
Cdd:COG4717 138 EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE------------LQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 505 AELQHLRDTVASFKESNEkdtETHAQLQEMKQLYQASKDELERQKHMYDQLEQDLLLCQLELKELKASHPIPEDKGKCAN 584
Cdd:COG4717 206 QRLAELEEELEEAQEELE---ELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 585 KCDTLLSRLTELQEKYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPKSGLLLKSQELLTKLEDLCEl 664
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE- 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 665 QLLYQGMQEEQKKLIQNQDCVLKEQL-EIHEELRRFKE-----SHFQEVLENPDDSKLAKSSKCNRNKqsklLMEQMQAL 738
Cdd:COG4717 362 ELQLEELEQEIAALLAEAGVEDEEELrAALEQAEEYQElkeelEELEEQLEELLGELEELLEALDEEE----LEEELEEL 437
|
410 420 430
....*....|....*....|....*....|....
gi 1370510765 739 QVMYDAGQAKQELLQQEQGRLLEERKRLQADLQL 772
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEEDGEL 471
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
112-795 |
4.32e-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: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 112 RAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERLASA-------QQAEVFTKQIQQLQGELRSLREEislLEHEKES 184
Cdd:TIGR00618 165 KKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQlltlctpCMPDTYHERKQVLEKELKHLREA---LQQTQQS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 185 ELKeIEQELHLAQAEIQSLRQAAEDSATEHEsdiASLQEDLCRMQNELEDMERIRGDYEMEIASLrAEMEMKSSEPsgsl 264
Cdd:TIGR00618 242 HAY-LTQKREAQEEQLKKQQLLKQLRARIEE---LRAQEAVLEETQERINRARKAAPLAAHIKAV-TQIEQQAQRI---- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 265 glsdYSGLQEELQELRERYHflneEYRALQESNSSLTGQladlesertQRATERWLQSQTLSMTSAESQTSEMDFLEPDP 344
Cdd:TIGR00618 313 ----HTELQSKMRSRAKLLM----KRAAHVKQQSSIEEQ---------RRLLQTLHSQEIHIRDAHEVATSIREISCQQH 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 345 EmqlLRQQLRDAEEQMHGMKNKCQELCCELE---ELQHHRQVSEEEQRRLQRELKCAQNEVlrfqtshsVTQNEELKSRL 421
Cdd:TIGR00618 376 T---LTQHIHTLQQQKTTLTQKLQSLCKELDilqREQATIDTRTSAFRDLQGQLAHAKKQQ--------ELQQRYAELCA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 422 CTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTLVENQSEKELLCRLQKLHLQHQNVTCEKEKLLERQQQLQEELQ 501
Cdd:TIGR00618 445 AAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPG 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 502 CHEAELQHLRDTVASFKESNEKdteTHAQLQEMKQLYQASKDELERQkhmyDQLEQDLLLCQLELKELKASHPIPEDkgk 581
Cdd:TIGR00618 525 PLTRRMQRGEQTYAQLETSEED---VYHQLTSERKQRASLKEQMQEI----QQSFSILTQCDNRSKEDIPNLQNITV--- 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 582 cankcdtLLSRLTELQEKYKASQKEMGQLQMEQCELLEDQRRMQEEQGQLQEELHRLTLPLPKSGLLLKSQELLTKLEDL 661
Cdd:TIGR00618 595 -------RLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSI 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 662 CELQLLYQGMQEEQKKLIQNqdcvLKEQLEIHEELRRFKESHFQEVLEnpddsKLAKSSKcNRNKQSKLLMEQMQALQVM 741
Cdd:TIGR00618 668 RVLPKELLASRQLALQKMQS----EKEQLTYWKEMLAQCQTLLRELET-----HIEEYDR-EFNEIENASSSLGSDLAAR 737
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370510765 742 YDAGQAKQELLQQEQGRLLEER--------KRLQADLQLCLEEMQLLQVQSPSIKMSLESYG 795
Cdd:TIGR00618 738 EDALNQSLKELMHQARTVLKARteahfnnnEEVTAALQTGAELSHLAAEIQFFNRLREEDTH 799
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
105-194 |
4.80e-03 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 38.75 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 105 ETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERlasaqqaEVFTKQIQQLQGELRSL-REEISLLEhEKE 183
Cdd:pfam09744 49 NVELEELREDNEQLETQYEREKALRKRAEEELEEIEDQWEQET-------KDLLSQVESLEEENRRLeADHVSRLE-EKE 120
|
90
....*....|.
gi 1370510765 184 SELKEIEQELH 194
Cdd:pfam09744 121 AELKKEYSKLH 131
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
96-462 |
6.06e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 96 NKHRGLSLTETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLLEDERlasaQQAEVFTKQIQQLQGELRSLREEI 175
Cdd:TIGR04523 318 NQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQ----NEIEKLKKENQSYKQEIKNLESQI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 176 SLLE----------HEKESELKEIEQELHLAQAEIQSLRQAAEDSATEhesdIASLQEDLCRMQNELEDMERIRGDYEME 245
Cdd:TIGR04523 394 NDLEskiqnqeklnQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE----IKDLTNQDSVKELIIKNLDNTRESLETQ 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 246 IASLraEMEMKSSEpsgslglSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERTQRATERWLQSQTL 325
Cdd:TIGR04523 470 LKVL--SRSINKIK-------QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 326 SmtSAESQTSEMDFlepDPEMQLLRQQLRDAEEQMHGMKNKCQELCCELEELQHHRQVSEEEQRRLQRELkcAQNEVLRF 405
Cdd:TIGR04523 541 S--DLEDELNKDDF---ELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI--EEKEKKIS 613
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370510765 406 QTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKmqlQLQTELRQLKVMKSTLVEN 462
Cdd:TIGR04523 614 SLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVK---QIKETIKEIRNKWPEIIKK 667
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
162-259 |
6.19e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.09 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 162 QQLQGELRSLREEISLLEHEKESELKEIEQElhlaqaeiQSLRQAAEDSATEHESDIASLQEDLCRMQNELEDMERIRGD 241
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQ--------QQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQ 216
|
90
....*....|....*...
gi 1370510765 242 YEMEIASlRAEMEMKSSE 259
Cdd:PRK11448 217 KRKEITD-QAAKRLELSE 233
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
894-1028 |
6.69e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 894 EDMERFEEMVVKVLIKLQAVQAMYQISQEEHSQLQEQMEKLLAKQKDLKEELDACEREFKEcmecLEKpmAPQNDKNEIK 973
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE----LES--RLEELEEQLE 382
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1370510765 974 ELQTKLRELQLQYQASMDEQGRLLVVQEQLEGQLQCCQEELRQLREKRPSVVKEA 1028
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
158-617 |
6.77e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 158 TKQIQQLQGELRSLREEISLLEHEKESELKEIEQELHLAQAEIQSLRqaaedsatEHESDIASLQEDLCRMQNELEDMER 237
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE--------ELKEEIEELEKELESLEGSKRKLEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 238 IRGDYEMEIASLRAEMEMkssepsgslgLSDYSGLQEELQELRERYHFLNEEYRALQESNSSLTGQLADLESERtqrate 317
Cdd:PRK03918 260 KIRELEERIEELKKEIEE----------LEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI------ 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 318 rwlqsqtlsmtsaesqtsemdflepdpemQLLRQQLRDAEEqmhgMKNKCQELCCELEELQHHRQVSEEEQRRLQrELKC 397
Cdd:PRK03918 324 -----------------------------NGIEERIKELEE----KEERLEELKKKLKELEKRLEELEERHELYE-EAKA 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 398 AQNEVLRFQTSHSVTQNEELKSRLCTLQKKYDTSQDEQNELLKMQLQLQTELRQLKVMKSTL-------------VENQS 464
Cdd:PRK03918 370 KKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELkkakgkcpvcgreLTEEH 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 465 EKELlcrLQKLHLQHQNV------TCEKEKLLERQQQLQEELQCHEAELQHLRDTVASFKESNEKdtethaqlqemkqLY 538
Cdd:PRK03918 450 RKEL---LEEYTAELKRIekelkeIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEK-------------LK 513
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370510765 539 QASKDELERQKHMYDQLEQDLLLCQLELKELKAShpipedkgkcANKCDTLLSRLTELQEKYKASQKEMGQLQMEQCEL 617
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE----------LEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
104-206 |
7.71e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.71 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370510765 104 TETELEELRAQVLQLVAELEETRELAGQHEDDSLELQGLlederlasAQQAEvftKQIQQLQGELRSLREEISLLEHEKE 183
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGL--------AAELE---EKQQELEAQLEQLQEKAAETSQERK 215
|
90 100 110
....*....|....*....|....*....|..
gi 1370510765 184 SELKEIEQE----LHLAQAEI-----QSLRQA 206
Cdd:PRK11448 216 QKRKEITDQaakrLELSEEETrilidQQLRKA 247
|
|
| |
