|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
132-686 |
1.99e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 132 ERFRNLDEEVEKYRAVYNKLRYEHtfLKSEFEHQKEEYARILDEgKIKYESEIARLEEDKEELRNQLLNVDLTKD----- 206
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRE--LEAELEELEAELEELEAE-LEELEAELAELEAELEELRLELEELELELEeaqae 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 207 ----SKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRIQVRQLAEMQATVRSLEAEKQSANLRAERLEK 282
Cdd:COG1196 290 eyelLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 283 ELQSSSEQNTFLINKLHKAEREINTLSSKVKELKHsNKLEITDIKLETARAKSELERERNKIQSELDGLQSDNEILKAAV 362
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEE-LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 363 EHHKVLLVEKDRELIRKVQAAKE--EGYQKLVVLQDEKLELENRLADLEKMKVEH-----DVWRQSEKDQYEEKLRASQM 435
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEaaLLEAALAELLEELAEAAARLLLLLEAEADYegfleGVKAALLLAGLRGLAGAVAV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 436 A---EEITRKELQSVRLKLQQQIVTiENAEKEKNENSDLKQQISSLQIQVTSLAQSENDLLNSNQMLKEMVERLKQECRN 512
Cdd:COG1196 529 LigvEAAYEAALEAALAAALQNIVV-EDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 513 FRSQAEKAQLEAEKTLEEKQIQWLEEKHKLHERITDREEKY--------NQAKEKLQRAAIAQKKRKSLHENKLKRLQEK 584
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREvtlegeggSAGGSLTGGSRRELLAALLEAEAELEELAER 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 585 VEVLEAKKEELETENQVLNRQNVPFEDYTRLQKRLKDIQRRHNEFRSLILVPNMPPTASINPVSFqssamvpsmELPFPP 664
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA---------LEELPE 758
|
570 580
....*....|....*....|..
gi 109134347 665 HMQEEQHQRELSLLRKRLEELE 686
Cdd:COG1196 759 PPDLEELERELERLEREIEALG 780
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
229-600 |
1.09e-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: 71.63 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 229 AEVAELKAEKENSEAQVENAQRIQVR---QLAEMQATVRSLEAEKQSAN----LRAERLEKELQSSSEQNTFLINKLHKA 301
Cdd:TIGR02168 165 AGISKYKERRKETERKLERTRENLDRledILNELERQLKSLERQAEKAErykeLKAELRELELALLVLRLEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 302 EREINTLSSKVKELkhSNKLEITDIKLETAR-AKSELERERNKIQSELDGLQsdneILKAAVEHHKVLLVEKDRELIRK- 379
Cdd:TIGR02168 245 QEELKEAEEELEEL--TAELQELEEKLEELRlEVSELEEEIEELQKELYALA----NEISRLEQQKQILRERLANLERQl 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 380 --VQAAKEEGYQKLVVLQDEKLELENRLADLEKMKvehdvwrQSEKDQYEEKLRASQMAEEItRKELQsvrlklqqqivt 457
Cdd:TIGR02168 319 eeLEAQLEELESKLDELAEELAELEEKLEELKEEL-------ESLEAELEELEAELEELESR-LEELE------------ 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 458 iENAEKEKNENSDLKQQISSLQIQVTSLAQSENDLlnsnqmlKEMVERLKQECRNFRSQAEKAQLEAEKTLEEKQIQWLE 537
Cdd:TIGR02168 379 -EQLETLRSKVAQLELQIASLNNEIERLEARLERL-------EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE 450
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109134347 538 EKHKLHERITDREEKYNQAKEKLQRAAIAQKkrkslheNKLKRLQEKVEVLEAKKEELETENQ 600
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAE-------RELAQLQARLDSLERLQENLEGFSE 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
29-633 |
8.62e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 8.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 29 SEFQKMLIDERLRCEHHKANYQTLKAEHTRLQNEHVKLQ---NELKHLFNEKQTQQEKLQLLLEELRGELVEKTKDLEEM 105
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEeeiEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 106 KLQILT-PQKLELLRAQI--QQELETPMRERFRNLDEEVEKYRAVYNKLRYEHTFLKSEFEHQKEEYARILDEGKiKYES 182
Cdd:TIGR02168 322 EAQLEElESKLDELAEELaeLEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA-SLNN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 183 EIARLEEDKEELRNQLLNVDLTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRiqvrQLAEMQAT 262
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE----ELEEAEQA 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 263 VRSLEAEKQSANLRA---ERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVK-------------------------- 313
Cdd:TIGR02168 477 LDAAERELAQLQARLdslERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISvdegyeaaieaalggrlqavvvenln 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 314 -------ELKHSNKLEITDIKLETARAKSELERERNKIQSELDGLQSDNEILKAAVEHHK--------VLLVEKDRELIR 378
Cdd:TIGR02168 557 aakkaiaFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllggVLVVDDLDNALE 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 379 kvQAAKEEGYQKLVVLQDEKLELENRLADLEKMKVEHDVWRQSEKDQYEEKLRASQMAEEITRKELQSVRLKLQQQIVTI 458
Cdd:TIGR02168 637 --LAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEL 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 459 ENAEKEKNEnsdLKQQISSLQIQVTSLAQSENDLLNSNQMLKEMVERLKQECRNFRSQAEKAQLEAE------KTLEEKQ 532
Cdd:TIGR02168 715 EQLRKELEE---LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAeaeaeiEELEAQI 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 533 IQWLEEKHKLHERITDREEKYNQAKEKLQRAAIAQKKRKSLHENKLKRLQEKVEVLEAKKEELETENQVLNRQNVPFEDY 612
Cdd:TIGR02168 792 EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
650 660
....*....|....*....|.
gi 109134347 613 TRLQKRLKDIQRRHNEFRSLI 633
Cdd:TIGR02168 872 ESELEALLNERASLEEALALL 892
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
43-685 |
1.14e-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: 62.00 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 43 EHHKANYQTLKAEHTRLQNEHVKLQNELKHLFNEKQTQQEKLQLLLEELRGELVEKTkDLEEMKLQILTPQKLELLRAQI 122
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA-ELEEKLEELKEELESLEAELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 123 QQELETPMRERFRNLDEEVEKYRAVYNKLRYEHTFLKSEFEHQKEEYARIldegkikyESEIARLEEDKEELRNQLLNVD 202
Cdd:TIGR02168 363 LEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL--------EDRRERLQQEIEELLKKLEEAE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 203 LTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKEnseaQVENAQRIQVRQLAEMQATVRSLEAEKQSANLRAERLEK 282
Cdd:TIGR02168 435 LKELQAELEELEEELEELQEELERLEEALEELREELE----EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 283 ELQSSSEQNTF------LINKLHKAEREINTL------------SSKVKE----LKHSNKLEITDIKLETARAKSELERE 340
Cdd:TIGR02168 511 LLKNQSGLSGIlgvlseLISVDEGYEAAIEAAlggrlqavvvenLNAAKKaiafLKQNELGRVTFLPLDSIKGTEIQGND 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 341 RNKIQSELDGLQSDNEILKAAVEHHKVL---------------------------------------------------- 368
Cdd:TIGR02168 591 REILKNIEGFLGVAKDLVKFDPKLRKALsyllggvlvvddldnalelakklrpgyrivtldgdlvrpggvitggsaktns 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 369 -LVEKDRElIRKVQAAKEEGYQKLVVLQDEKLELENRLADLEKMKVEhdvwRQSEKDQYEEKLRASQMAEEITRKELQSV 447
Cdd:TIGR02168 671 sILERRRE-IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ----LRKELEELSRQISALRKDLARLEAEVEQL 745
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 448 RLKLQQQIVTIENAEKEKNENSDLKQQISSLQIQV--------TSLAQSENDLLNSNQMLKEMVERLKQECRNFRSQAEK 519
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAeaeieeleAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 520 -AQLEAEKTLEEKQIQWLEEKhklHERITDREEKYNQAKEKLQRAAIAQKKRKSLHENKLKRLQEKVEVLEAKKEELETE 598
Cdd:TIGR02168 826 lESLERRIAATERRLEDLEEQ---IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 599 NQVLNRQNVPFED-YTRLQKRLKDIQRRHNEFRSLILvpnmpPTASINPVSFQSSAMVPsMELPFPPHMQEEQHQRELSL 677
Cdd:TIGR02168 903 LRELESKRSELRReLEELREKLAQLELRLEGLEVRID-----NLQERLSEEYSLTLEEA-EALENKIEDDEEEARRRLKR 976
|
....*...
gi 109134347 678 LRKRLEEL 685
Cdd:TIGR02168 977 LENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
38-599 |
3.76e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 38 ERLRCEHHKANYQTLKAEHTRLQNEHVKLQNELKHLfnekQTQQEKLQLLLEELRGELVEKTKDLEEMKlqiltpQKLEL 117
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELEAELEEL----EAELAELEAELEELRLELEELELELEEAQ------AEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 118 LRAQIQQELE--TPMRERFRNLDEEVEKYRAVYNKLRYEHTFLKSEFEHQKEEYARILDEGKIKyESEIARLEEDKEELR 195
Cdd:COG1196 293 LLAELARLEQdiARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA-EAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 196 NQLLNVDLTKDSKRVEQLA--REKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRiQVRQLAEMQATVRSLEAEKQSA 273
Cdd:COG1196 372 AELAEAEEELEELAEELLEalRAAAELAAQLEELEEAEEALLERLERLEEELEELEE-ALAELEEEEEEEEEALEEAAEE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 274 NLRAERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKHSNKLEITDIKLETARAKS-ELERERNKIQSELDGLQ 352
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAaLLLAGLRGLAGAVAVLI 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 353 SDNEILKAAVEH-----HKVLLVEKDRELIRKVQAAKEEGYQKLVVLQDEKLELENRLADLEKMKVEHDVWRQSEKDQYE 427
Cdd:COG1196 531 GVEAAYEAALEAalaaaLQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLRE 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 428 EKLRASQMAEEItrKELQSVRLKLQQQIVTIENAEKEKNENSDLKQQISSLQIQVTSLAQSENDLLNSNQMLKEMVERLK 507
Cdd:COG1196 611 ADARYYVLGDTL--LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERL 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 508 QECRNFRSQAEKAQLEAEKTLEEKQIQWLEEKHKLHERITDREEKYNQAKEKLQRAAIAQKKRKSLHEN---KLKRLQEK 584
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPeppDLEELERE 768
|
570
....*....|....*
gi 109134347 585 VEVLEAKKEELETEN 599
Cdd:COG1196 769 LERLEREIEALGPVN 783
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
328-625 |
3.07e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 328 LETARAKSELERERNKIQSELDGLQSDNEILKAAVE--HHKVLLVEKDRELI----RKVQAAKEEGYQKLVVLQDEKLEL 401
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSdaSRKIGEIEKEIEQLeqeeEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 402 ENRLADLEKmkvehdvwrqsEKDQYEEKLRASQMA-EEITRKELQSVRLKLQQQIVTIENAEKEKNEN-SDLKQQISSLQ 479
Cdd:TIGR02169 757 KSELKELEA-----------RIEELEEDLHKLEEAlNDLEARLSHSRIPEIQAELSKLEEEVSRIEARlREIEQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 480 IQVTSLAQSENDLLNSNQMLKEMVERLKQECRNFRSQAEKAQLEAEKTleEKQIQWLEEKHK-LHERITDREEKYNQAKE 558
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL--EAALRDLESRLGdLKKERDELEAQLRELER 903
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109134347 559 KLQRAAIAQKKRKSLhenkLKRLQEKVEVLEAKKEELETENQVLNRQNVPFEDYTRLQKRLKDIQRR 625
Cdd:TIGR02169 904 KIEELEAQIEKKRKR----LSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEE 966
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
115-632 |
4.55e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 4.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 115 LELLRAQIQQELETPMRERFRNLDEEVEKYRAVYNKLRYEhtflKSEFEHQKEEYARILDEGKIKYEsEIARLEEDKEEL 194
Cdd:PRK02224 189 LDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQ----REQARETRDEADEVLEEHEERRE-ELETLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 195 RNqllnvDLTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVE---------NAQRIQVRQ-LAEMQATVR 264
Cdd:PRK02224 264 RE-----TIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEavearreelEDRDEELRDrLEECRVAAQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 265 SLEAEKQSANLRAERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKH-----SNKLEITDIKLETARAKSE-LE 338
Cdd:PRK02224 339 AHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEeieelRERFGDAPVDLGNAEDFLEeLR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 339 RERNKIQSELDGLQSDNEILKAAVEHHKVLL--------------------VEKDRELIRKVQAAKEEgyqklvvLQDEK 398
Cdd:PRK02224 419 EERDELREREAELEATLRTARERVEEAEALLeagkcpecgqpvegsphvetIEEDRERVEELEAELED-------LEEEV 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 399 LELENRLADLEKM-KVEHDVWRQSEKDQYEEKLRASQmAEEITRKELQSVRLKLQQQIVTIENAEKEKnENSDLKQQISS 477
Cdd:PRK02224 492 EEVEERLERAEDLvEAEDRIERLEERREDLEELIAER-RETIEEKRERAEELRERAAELEAEAEEKRE-AAAEAEEEAEE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 478 LQIQVTSLaqsendllnsNQMLKEMVERLKQECRNFRSQAEKAQLEAE-KTLEEKQIQWLEEKHKLHERITDREEKYNQA 556
Cdd:PRK02224 570 AREEVAEL----------NSKLAELKERIESLERIRTLLAAIADAEDEiERLREKREALAELNDERRERLAEKRERKREL 639
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109134347 557 KEKLQRAAIAQ-KKRKSLHENKLKRLQEKVEVLEAKKEELETENQVLNRQnvpFEDYTRLQKRLKDIQRRHNEFRSL 632
Cdd:PRK02224 640 EAEFDEARIEEaREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENE---LEELEELRERREALENRVEALEAL 713
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
123-630 |
1.09e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 123 QQELETPMRERFRNLDEEVEKYRAVYNKLRYEHTFLKSEfEHQKEEYARILDEGKIKYESEIARLEEDKEELRNQLLNVD 202
Cdd:PTZ00121 1237 KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE-EARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAK 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 203 LTKDSKRVEQLAREKVYLCQKlKGLEAEVAELKAEKENSEAQVENAQRIQVRQLAEMQATVRSLEAEKQSANLRAERLEK 282
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKK-KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD 1394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 283 ELQSSSEQNTFLINKLHKAEREINTLSSKVKELKHSNKLEITDIKLETARAKSELERERNKIQSELDGLQSDNEILKAAV 362
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE 1474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 363 EHHKVLLVEKDRELIRKVQAAKEEGYQKLVVLQDEKLELENRLADLEKMKVEHDVWRQSEKDQYEEKLRASQMAEEITRK 442
Cdd:PTZ00121 1475 AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKA 1554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 443 ElqsvRLKLQQQIVTIENAEKEKNEN------SDLKQQISSLQIQVTSLAQSENDLLNSNQMLKEMVERLKQEcRNFRSQ 516
Cdd:PTZ00121 1555 E----ELKKAEEKKKAEEAKKAEEDKnmalrkAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE-ELKKAE 1629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 517 AEKAQLEAEKTLEEKQIQWLEEKHKLHERITDREE----KYNQAKEKLQRAAIAQKKRKSLHENKLKRLQEKVEVLEAKK 592
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAeeakKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 109134347 593 ---EELETENQVLNRQNVPFEDYTRLQKRLKDIQRRHNEFR 630
Cdd:PTZ00121 1710 keaEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
99-475 |
1.96e-07 |
|
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: 54.74 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 99 TKDLEEMKLQILTPQKLELLRAQ-IQQELETPMRERFRnldeEVEKYRAVYNKLRYEHTFLKSEFEHQKEEYARILDegk 177
Cdd:pfam15921 473 TKEMLRKVVEELTAKKMTLESSErTVSDLTASLQEKER----AIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRN--- 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 178 IKYESEIARL---EEDK--EELRNQLLNVD--LTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVEnaqr 250
Cdd:pfam15921 546 VQTECEALKLqmaEKDKviEILRQQIENMTqlVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIR---- 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 251 iqvrqlaEMQATVRSLEAEK-QSANLRAERLeKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKH-----SNKLEIT 324
Cdd:pfam15921 622 -------ELEARVSDLELEKvKLVNAGSERL-RAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRnfrnkSEEMETT 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 325 --DIKLETARAKSELERERNKIQSeLDGlqSDNEILKAAVEHHKVLLVEKDR-----ELIRKVQAAKEEGYQKLVVLQDE 397
Cdd:pfam15921 694 tnKLKMQLKSAQSELEQTRNTLKS-MEG--SDGHAMKVAMGMQKQITAKRGQidalqSKIQFLEEAMTNANKEKHFLKEE 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 398 KLELENRLADL----EKMKVEHDVWRQSEKDQYEE-----------KLRASQMAEEITRKELQSVRLKLQQQIVTIENAE 462
Cdd:pfam15921 771 KNKLSQELSTVatekNKMAGELEVLRSQERRLKEKvanmevaldkaSLQFAECQDIIQRQEQESVRLKLQHTLDVKELQG 850
|
410
....*....|...
gi 109134347 463 KEKNENSDLKQQI 475
Cdd:pfam15921 851 PGYTSNSSMKPRL 863
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
49-605 |
2.23e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 49 YQTLKAEHTRLQ--------NEHVKLQNELKHLFNEKQTQQEKLQLLLEELRGELVEKTKDLEEMKLQILTPQKLELLRA 120
Cdd:TIGR02168 215 YKELKAELRELElallvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 121 QIQQELEtpmrERFRNLDEEVEKYRAVYNKLRYEHTFLKSEFEHQKEEYARI---LDEGKIKYESEIARLEEDKEELRNq 197
Cdd:TIGR02168 295 NEISRLE----QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELeekLEELKEELESLEAELEELEAELEE- 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 198 lLNVDLTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQ--------RIQVRQLAEMQATVRSLEAE 269
Cdd:TIGR02168 370 -LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQqeieellkKLEEAELKELQAELEELEEE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 270 KQSANLRAERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKH--SNKLEITDIKLETARAKSELERERNKIQSE 347
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERlqENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 348 L---------------DGLQS----DNEILKAAVEH------HKVLLVEKDRELIRKVQAAKEE---------GYQKLVV 393
Cdd:TIGR02168 529 IsvdegyeaaieaalgGRLQAvvveNLNAAKKAIAFlkqnelGRVTFLPLDSIKGTEIQGNDREilkniegflGVAKDLV 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 394 LQDEKLE---------------LENRLADLEKMK-------VEHDVWRQSEKDQYEEKLRASQMAEeiTRKELQSVRLKL 451
Cdd:TIGR02168 609 KFDPKLRkalsyllggvlvvddLDNALELAKKLRpgyrivtLDGDLVRPGGVITGGSAKTNSSILE--RRREIEELEEKI 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 452 QQQIVTIENAEKE----KNENSDLKQQISSLQIQVTSLAQSENDLLNSNQMLKEMVERLKQecRNFRSQAEKAQLEAEKT 527
Cdd:TIGR02168 687 EELEEKIAELEKAlaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE--RIAQLSKELTELEAEIE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 528 LEEKQIQWLEEKHKLHER-ITDREEKYNQAKEKLQ---RAAIAQKKRKSLHENKLKRLQEKVEVLEAKKEELETENQVLN 603
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAeIEELEAQIEQLKEELKalrEALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
..
gi 109134347 604 RQ 605
Cdd:TIGR02168 845 EQ 846
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
37-630 |
2.56e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 37 DERLRCEHHKANYQTLKAEHTRLQNEHVKLQNELKHLFNEKQTQQEKLQLLLEELRGELVEKTKDLEEMKLQILTPQKLE 116
Cdd:PTZ00121 1113 EARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEE 1192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 117 LLRAQIQQELETPMRERFRNLDEEVEKYRavynKLRYEHTFLKSEFEHQKEEYARILDEgkIKYESEIARLEEDKEELRN 196
Cdd:PTZ00121 1193 LRKAEDARKAEAARKAEEERKAEEARKAE----DAKKAEAVKKAEEAKKDAEEAKKAEE--ERNNEEIRKFEEARMAHFA 1266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 197 QLLNVDLTKDSKRVEQLAREKvylcQKLKGLEAEVAELKAEKENSEAQVENAQRIQVRQLAEMQATVRSLEAEKQS---- 272
Cdd:PTZ00121 1267 RRQAAIKAEEARKADELKKAE----EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAeeak 1342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 273 -----ANLRAERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKHSN----KLEITDIKLETARAKSELERERNK 343
Cdd:PTZ00121 1343 kaaeaAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADeakkKAEEDKKKADELKKAAAAKKKADE 1422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 344 IQSELDGLQSDNEILKAAVEHHKVLLVEKDRELIRKVQAAKEEGYQKLVVLQDEKLELENRLADLEKMKVEHDVWRQSE- 422
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEa 1502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 423 KDQYEEKLRASQMAE-EITRKELQSVRLKLQQQIVTIENAEKEKNENSDLKQQISSLQIQVTSLAQSENDLLNSNQML-- 499
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKaEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALrk 1582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 500 ---------KEMVERLKQECRNFRSQAEKAQLEAEKTLEEKQIQWLEEKHKLHERITDREEKYNQAKEKLQRAAIAQKKR 570
Cdd:PTZ00121 1583 aeeakkaeeARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK 1662
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 571 KSLHENKLKRLQEKVEVLEAKKEELETENQVLNRQNVPFEDYTRLQKRLKDIQRRHNEFR 630
Cdd:PTZ00121 1663 AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELK 1722
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
180-565 |
2.89e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 180 YESEIARLEEDKEELRNQLLNVDLTKDSKRvEQLARekvylcqklkgleaevaeLKAEKENSEAQVENAQRIQVRQLAEM 259
Cdd:TIGR02169 168 FDRKKEKALEELEEVEENIERLDLIIDEKR-QQLER------------------LRREREKAERYQALLKEKREYEGYEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 260 QATVRSLEAEKQSANLRAERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKHSnklEITDIKLETARAKSELER 339
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE---EQLRVKEKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 340 ERNKIQSELDGLQ-SDNEILKAAVEHHKVLL-VEKDRELIRKVQAAKEEGYQKLVVLQDEKLELENRLADLEKmkvEHDV 417
Cdd:TIGR02169 306 LERSIAEKERELEdAEERLAKLEAEIDKLLAeIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK---EFAE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 418 WRQsEKDQYEEKLrasqmaEEITRK--ELQSVRLKLQQQIVTIENAEKE-KNENSDLKQQISSLQIQVTSLAQSENDLLN 494
Cdd:TIGR02169 383 TRD-ELKDYREKL------EKLKREinELKRELDRLQEELQRLSEELADlNAAIAGIEAKINELEEEKEDKALEIKKQEW 455
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109134347 495 SNQMLKEMVERLKQECrnFRSQAEKAQLEAEKTLEEKQIQWLEEKhklhERITDREEKYNQAKEKLQRAAI 565
Cdd:TIGR02169 456 KLEQLAADLSKYEQEL--YDLKEEYDRVEKELSKLQRELAEAEAQ----ARASEERVRGGRAVEEVLKASI 520
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
114-615 |
6.33e-07 |
|
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: 53.05 E-value: 6.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 114 KLELLRAQIQ-QELETPMR-----ERFRNLDEEVEKYRAVYNKLRYEHTFLKSEFEHQKEEYARILDEGKI-----KYES 182
Cdd:TIGR00618 195 KAELLTLRSQlLTLCTPCMpdtyhERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLrarieELRA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 183 EIARLEEDKEELRNQLLNVDLTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRIQVRQLAEMQAT 262
Cdd:TIGR00618 275 QEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 263 VRSLEAEKQSANLRAER-----LEKELQSSSEQNTFLINKLHKAEREINTLSSKV-KELKHSNKLEITDIKLETARAKSE 336
Cdd:TIGR00618 355 IHIRDAHEVATSIREIScqqhtLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQaTIDTRTSAFRDLQGQLAHAKKQQE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 337 LERERNKIQSELDGLQSDNEILK--AAVEHHKVLLVEKDRE-----LIRKVQAAKEEGYQKLVVLQDEKLELENRLADLE 409
Cdd:TIGR00618 435 LQQRYAELCAAAITCTAQCEKLEkiHLQESAQSLKEREQQLqtkeqIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPN 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 410 KMKVEHDVW--RQSEKDQYEEKLRASQMAEEITRKELQSVRLKLQQqivTIENAEKEKNENSDLKQQISSLQIQVTSLAQ 487
Cdd:TIGR00618 515 PARQDIDNPgpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRAS---LKEQMQEIQQSFSILTQCDNRSKEDIPNLQN 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 488 SENDLLNSNQMLKEMVERLKQECRNFRSQAEKAQLEAEKTLEEKQIQWLEEKHKLHERITDREEKYNQAKEKLQRAAIAQ 567
Cdd:TIGR00618 592 ITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLP 671
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 109134347 568 KKRKSLHENKLKRLQEKVEVLEAKKEELETENQVLNRQNVPFEDYTRL 615
Cdd:TIGR00618 672 KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDRE 719
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
36-604 |
6.98e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 36 IDERLRCEHHKANYQTLKAEHTRLQNEHVKLQNELKHLFNEKQTQQEKLQLLLEELRGELVEKTKDLEEMKLQILTPQKL 115
Cdd:PTZ00121 1166 AEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKA 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 116 ELLR--AQIQQELETPMRERFRNLDEEVEKYRAVYNKLRYEHTFLKSEfEHQKEEYARILDEGKIKYEsEIARLEEDKEE 193
Cdd:PTZ00121 1246 EEERnnEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKADEAKKKAE-EAKKADEAKKK 1323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 194 LRNQLLNVDLTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRIQVRQLAEMQATVRSLEAEKQSA 273
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED 1403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 274 NLRAERLEK---------ELQSSSEQNTFLINKLHKAEREINTLSSKvKELKHSNKLEITDIKLETARAKSELERERNKI 344
Cdd:PTZ00121 1404 KKKADELKKaaaakkkadEAKKKAEEKKKADEAKKKAEEAKKADEAK-KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA 1482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 345 QSELDGLQSDNEILKAAVEHHKVLLVEKDRELIRKVQAAK--EEGYQKLVVLQDEKLELENRLADLEKMKVEHDVWRQSE 422
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKkaDEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 423 KDQYEEKLRASQMAEEITRKELQSVRLKLQQQIVTIENAEKEKNENSDLKQQISSLQIQVTSLAQSENDLLNSNQMLKEM 502
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE 1642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 503 VERLK--------QECRNFRSQAEKAQLEAEKTLEEKQIQWLEEKHKLHERITDREEKYNQAKEKLQRAAIAQKK----R 570
Cdd:PTZ00121 1643 AEEKKkaeelkkaEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKaeelK 1722
|
570 580 590
....*....|....*....|....*....|....*.
gi 109134347 571 KSLHENKLKRLQEKVEVLEAKK--EELETENQVLNR 604
Cdd:PTZ00121 1723 KAEEENKIKAEEAKKEAEEDKKkaEEAKKDEEEKKK 1758
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
243-469 |
7.41e-07 |
|
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: 52.07 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 243 AQVENAQRIQvRQLAEMQATVRSLEAEKQSANLRAERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKHsnklE 322
Cdd:COG4942 17 AQADAAAEAE-AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK----E 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 323 ITDIKLETARAKSELER-----ERNKIQSELDGLQSDNEILKAAVEHHKV-LLVEKDRELIRKVQAAKEEGYQKLVVLQD 396
Cdd:COG4942 92 IAELRAELEAQKEELAEllralYRLGRQPPLALLLSPEDFLDAVRRLQYLkYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109134347 397 EKLELENRLADLEKMKVEHDVwRQSEKDQYEEKLRASQMAEEITRKELQSVRLKLQQQIVTIENAEKEKNENS 469
Cdd:COG4942 172 ERAELEALLAELEEERAALEA-LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
117-567 |
1.07e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 117 LLRAQIQQELETPMRERFRNLDEEVEKYRAVYNKLRyehtflksEFEHQKEEYARILDEgKIKYESEIARLEEDKEELRN 196
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNLKELKELEEELK--------EAEEKEEEYAELQEE-LEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 197 QLlnvDLTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRIQVRQLAEMQATVRSLEAEKQSANLR 276
Cdd:COG4717 117 EL---EKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 277 AERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKHSNKLEITDIKLETARAKSELERERNKIQSELDGLQSDNE 356
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 357 ILKAAVEHHKVLLVEKDRELIRKVQAAKEEGYQKLVVLQDEKLELENRLADLEKMKVEHDVWRQSEKDQYEEKLRASQMA 436
Cdd:COG4717 274 TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 437 EEITRKELQSVRLKLQQQIV------------TIENAEKEKNENSDLKQQISSLQIQVTSLAQSENDLLNSNQ--MLKEM 502
Cdd:COG4717 354 REAEELEEELQLEELEQEIAallaeagvedeeELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEE 433
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109134347 503 VERLKQECRnfRSQAEKAQLEAEKTLEEKQIQWLEEKHKLHERITDREEKYNQAKEKLQRAAIAQ 567
Cdd:COG4717 434 LEELEEELE--ELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
36-633 |
1.69e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 36 IDERLRCEHHKANYQTLKAEHTRLQNEHVKLQNELKHLFNEKQTQQEKLQLLLEELRGELVEKTKDLEEMKLQILTPQKL 115
Cdd:PTZ00121 1214 AEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 116 ELLRAQIQQELETPMR--ERFRNLDE-----EVEKYRAVYNKLRYEHTFLKSEFEHQKEEYARI-LDEGKIKYESEIARL 187
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKkaEEAKKADEakkkaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADeAEAAEEKAEAAEKKK 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 188 EEDK---EELRNQLLNVDLTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRIQVRQLAEmqATVR 264
Cdd:PTZ00121 1374 EEAKkkaDAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAD--EAKK 1451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 265 SLEAEKQSANLRAERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKHSNKLEITDIKLETARAKSELERERNKI 344
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 345 QSELDGLQSDNEILKAAVEHHKVLLVEKDRELIRKVQAAKEEGYQKLVVLQDEKLEL--ENRLADLEKMKVEHDVWRQSE 422
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeEARIEEVMKLYEEEKKMKAEE 1611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 423 -KDQYEEKLRASQM-AEEITRKELQSVRLKLQQQIVTIENAEKEKNENSDLKQQISSlqiqvtslaQSENDllnsnqmlK 500
Cdd:PTZ00121 1612 aKKAEEAKIKAEELkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK---------KAEED--------K 1674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 501 EMVERLKQECRNFRSQAEKAQLEAEKTLEEKQIQWLEEKHKLHERITDREEKYNQAK-EKLQRAAIAQKKRKS---LHEN 576
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKaEEAKKEAEEDKKKAEeakKDEE 1754
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 109134347 577 KLKRLQEKVEVLEAKKEELETENQVLNRQNVPFEDYTRLQKRLKDIQRRHNEFRSLI 633
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANII 1811
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
171-632 |
3.33e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 171 RILDEGKIKYESEIARLEEDKEELRNQllNVDLTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVenaqr 250
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEK--EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELE----- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 251 iqvRQLAEMQATVRSLEAEKQSANLRAERLEKElqssseqntflINKLHKAEREINTLSSKVKELKHSNKL--EITDIKL 328
Cdd:PRK03918 245 ---KELESLEGSKRKLEEKIRELEERIEELKKE-----------IEELEEKVKELKELKEKAEEYIKLSEFyeEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 329 ETARAKSELERERNKIQSELDGLQSDNEILKAavehhkvlLVEKDRELIRKVQAAKE--EGYQKLVVLQDEKLELENRLA 406
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEE--------LKKKLKELEKRLEELEErhELYEEAKAKKEELERLKKRLT 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 407 DLEKMKVEHDVWR-QSEKDQYEEKL-----RASQMAEEITRKELQSVRLKLQQQIVTIENAEKEKNENSDLKQ----QIS 476
Cdd:PRK03918 383 GLTPEKLEKELEElEKAKEEIEEEIskitaRIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEeytaELK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 477 SLQIQVTSLAQSENDLLNSnqmLKEMVERLKQECRNFRSQAEKAQL-EAEKTLEEKQIQWLEEKHKLHERItdrEEKYNQ 555
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKE---LRELEKVLKKESELIKLKELAEQLkELEEKLKKYNLEELEKKAEEYEKL---KEKLIK 536
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109134347 556 AKEKLQRAAIAQKKRKSLhENKLKRLQEKVEVLEAKKEELETENQVLNrqnvpFEDYTRLQKRLKDIQRRHNEFRSL 632
Cdd:PRK03918 537 LKGEIKSLKKELEKLEEL-KKKLAELEKKLDELEEELAELLKELEELG-----FESVEELEERLKELEPFYNEYLEL 607
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
130-626 |
3.84e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 130 MRERFRNLDEEVEKYRAVYNKLRYehtfLKSEFEHQKEEYARILDEGKiKYESEIARLEEDKEELRNQLLNV-DLTKDSK 208
Cdd:PRK03918 212 ISSELPELREELEKLEKEVKELEE----LKEEIEELEKELESLEGSKR-KLEEKIRELEERIEELKKEIEELeEKVKELK 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 209 RVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRiQVRQLAEMQATVRSLEAEKQSANLRAERLEKELQsss 288
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE-RIKELEEKEERLEELKKKLKELEKRLEELEERHE--- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 289 eqntflinKLHKAEREINTLSSKVKELKHSNKLEITDIKLETARAKSELERERNKIQSELDGLQSDNEILKAAV------ 362
Cdd:PRK03918 363 --------LYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIeelkka 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 363 ------------EHHKVLLVEKDRELIRKVQAAKEEGYQKLVVLQDEKLELENRLADLEKMKVEHDVWRQSEkdQYEEKL 430
Cdd:PRK03918 435 kgkcpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLK--ELEEKL 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 431 RaSQMAEEITRKElqsvrlklqqqivtiENAEKEKNENSDLKQQISSLQiqvtSLAQSENDLLNSNQMLKEMVERLKQEC 510
Cdd:PRK03918 513 K-KYNLEELEKKA---------------EEYEKLKEKLIKLKGEIKSLK----KELEKLEELKKKLAELEKKLDELEEEL 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 511 RNFRSQAEKAQLEAEKTLEEKqIQWLEEKHKLHERITDreekynqAKEKLQRAAIAQKKRKSLHENKLKRLQEKVEVLEA 590
Cdd:PRK03918 573 AELLKELEELGFESVEELEER-LKELEPFYNEYLELKD-------AEKELEREEKELKKLEEELDKAFEELAETEKRLEE 644
|
490 500 510
....*....|....*....|....*....|....*.
gi 109134347 591 KKEELETENQVLNRqnvpfEDYTRLQKRLKDIQRRH 626
Cdd:PRK03918 645 LRKELEELEKKYSE-----EEYEELREEYLELSREL 675
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
158-610 |
4.87e-06 |
|
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: 49.74 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 158 LKSEFEHQKEEYARILDEGKIKYESEIARLEEDKEELRNQLLNVD-LTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKA 236
Cdd:pfam05557 14 LQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRlLEKREAEAEEALREQAELNRLKKKYLEALNKKLN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 237 EKENSEAQVENAQRIQVRQLAEMQATVRSLEAEKQSANLRAERLE---KELQSSSEQNTFLINKLHKAEREINTLSSKVK 313
Cdd:pfam05557 94 EKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQerlDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 314 ELKHSNKLEITDiKLETARAKSELEReRNKIQSELDGLQSDNEILKAAVEHhKVLLVEKDRELIRKVQaaKEEGYQ-KLV 392
Cdd:pfam05557 174 ELEFEIQSQEQD-SEIVKNSKSELAR-IPELEKELERLREHNKHLNENIEN-KLLLKEEVEDLKRKLE--REEKYReEAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 393 VLQDEKLELENRLADLEKMKVEH--------DVWRQSEKDQYEEK-LRASQMAEEITRKELQSVRLKLQQQI-VTIENAE 462
Cdd:pfam05557 249 TLELEKEKLEQELQSWVKLAQDTglnlrspeDLSRRIEQLQQREIvLKEENSSLTSSARQLEKARRELEQELaQYLKKIE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 463 KEKNENSDLKQQISSLQIQVtSLAQSENDLLNsnQMLKEMVERLKQEcrNFRSQAEKAQLEAEKTLEEKQIQWLEEKHKL 542
Cdd:pfam05557 329 DLNKKLKRHKALVRRLQRRV-LLLTKERDGYR--AILESYDKELTMS--NYSPQLLERIEEAEDMTQKMQAHNEEMEAQL 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109134347 543 hERITDREEKYNQAKEKLQRAAIAQKKRKSLHENKLKRlqEKVEVLEAKKEELETENQVLNRQNVPFE 610
Cdd:pfam05557 404 -SVAEEELGGYKQQAQTLERELQALRQQESLADPSYSK--EEVDSLRRKLETLELERQRLREQKNELE 468
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
207-605 |
8.28e-06 |
|
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: 49.35 E-value: 8.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 207 SKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRIQVRQL-AEMQATVRSLEAEKQSANLRAERLEKELQ 285
Cdd:pfam15921 223 SKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLiSEHEVEITGLTEKASSARSQANSIQSQLE 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 286 SSSEQ----NTFLINKLHKAEREINTLSSKVKELKHSNKLEITDIKLETARAKSELER---ERNKIQSELDGLqsDNEIL 358
Cdd:pfam15921 303 IIQEQarnqNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEartERDQFSQESGNL--DDQLQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 359 KAAVEHHK-----VLLVEKDRELIRKVQAAKEEGYQKLVVLQDEKLELENRLADLEKMK------VEHDVWRQSEKDQYE 427
Cdd:pfam15921 381 KLLADLHKrekelSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKsecqgqMERQMAAIQGKNESL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 428 EKLRASQMAEEITRKELQSVRLKLQQQIVTIENAEKEKNE---------------NSDLKQQISSLQIQVTSL------- 485
Cdd:pfam15921 461 EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDltaslqekeraieatNAEITKLRSRVDLKLQELqhlkneg 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 486 -----AQSENDLLNSNQMLKE-MVERLKQECRNFRS------------QAEKAQLEAE---KTLEEKQIQWLEEK----- 539
Cdd:pfam15921 541 dhlrnVQTECEALKLQMAEKDkVIEILRQQIENMTQlvgqhgrtagamQVEKAQLEKEindRRLELQEFKILKDKkdaki 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 540 HKLHERITDRE----EKYNQAKEKLQRAA-IAQKKRKSLHE-----NKLKRLQEKVEVLEA----KKEELETENQVLNRQ 605
Cdd:pfam15921 621 RELEARVSDLElekvKLVNAGSERLRAVKdIKQERDQLLNEvktsrNELNSLSEDYEVLKRnfrnKSEEMETTTNKLKMQ 700
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
113-308 |
1.15e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 113 QKLELLRAQIQQeletpMRERFRNLDEEVEKYRAVYNKLRyehtFLKSEFEHQKEEYARILDEGKIkyESEIARLEEDKE 192
Cdd:COG4913 610 AKLAALEAELAE-----LEEELAEAEERLEALEAELDALQ----ERREALQRLAEYSWDEIDVASA--EREIAELEAELE 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 193 ELRNQllNVDLTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRiQVRQLAEMQATVRSLEAEKQS 272
Cdd:COG4913 679 RLDAS--SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD-RLEAAEDLARLELRALLEERF 755
|
170 180 190
....*....|....*....|....*....|....*..
gi 109134347 273 ANLRAERLEKELQSS-SEQNTFLINKLHKAEREINTL 308
Cdd:COG4913 756 AAALGDAVERELRENlEERIDALRARLNRAEEELERA 792
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
339-631 |
1.36e-05 |
|
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: 48.53 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 339 RERNKIQSELDGL-QSDNEILKAAVEhhkvllVEKDRELIRKVQAAKEEGYQKLVVLQDEKLELEnRLADLEKMKVEHDV 417
Cdd:TIGR02169 153 VERRKIIDEIAGVaEFDRKKEKALEE------LEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 418 W-RQSEKDQYEEKLRASQMAEEITRKELQSVRLKLQQQIVTIENAEKE------------KNENSDLKQQISSLQIQVTS 484
Cdd:TIGR02169 226 YeLLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLleelnkkikdlgEEEQLRVKEKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 485 LAQSENDLlnsnqmlKEMVERLKQECRNFRSQAEKAQLEAEKtLEEKQIQWLEEKHKLHERITDREEKYNqakEKLQRAA 564
Cdd:TIGR02169 306 LERSIAEK-------ERELEDAEERLAKLEAEIDKLLAEIEE-LEREIEEERKRRDKLTEEYAELKEELE---DLRAELE 374
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109134347 565 IAQKKRKSLHEnKLKRLQEKVEVLEAKKEELETE-NQVLNRQNVPFEDYTRLQKRLKDIQRRHNEFRS 631
Cdd:TIGR02169 375 EVDKEFAETRD-ELKDYREKLEKLKREINELKRElDRLQEELQRLSEELADLNAAIAGIEAKINELEE 441
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
167-353 |
1.53e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 167 EEYARILDE-GKIKYESEIARLEEDKEELrnQLLNvdltkdsKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQV 245
Cdd:COG4913 262 ERYAAARERlAELEYLRAALRLWFAQRRL--ELLE-------AELEELRAELARLEAELERLEARLDALREELDELEAQI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 246 ENAqriQVRQLAEMQATVRSLEAEKQSANLRAERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKHSNKLEITD 325
Cdd:COG4913 333 RGN---GGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAE 409
|
170 180
....*....|....*....|....*...
gi 109134347 326 IKletaRAKSELERERNKIQSELDGLQS 353
Cdd:COG4913 410 AE----AALRDLRRELRELEAEIASLER 433
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
30-598 |
1.88e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 30 EFQKMLIDERLRCEHHKANYQTLKAEHTRLQNEHVKLQNELKHLFNEKQTQQEKLQLLLEELRGELVEKTKDLEEMKLQI 109
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 110 LTPQKLELLRAQIQQELETPMRERFRNLDEEVEKYRAVYNKLRYEHTFLKSEFEHQKEEYARILDEGKIkyESEIARLEE 189
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL--EEAEEALLE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 190 DKEELRNQLLNVDLTKDSKRVEQLAREkvylcQKLKGLEAEVAELKAEKENSEAQVENAQRIQVRQLAEMQATVRSLEAE 269
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEE-----EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 270 KQSANLRAERLEK-ELQSSSEQNTFLINKLHKAEREINTLSSKVKELK-----HSNKLEITDIKLETARAKSELERERNK 343
Cdd:COG1196 490 AARLLLLLEAEADyEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEaaleaALAAALQNIVVEDDEVAAAAIEYLKAA 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 344 IQSELDGLQSDN-EILKAAVEHHKVLLVEKDRELIRKVQAAKEEGYQKLVVLQDEKLELENRLADLEKMKVEHDVwrqse 422
Cdd:COG1196 570 KAGRATFLPLDKiRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG----- 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 423 kdQYEEKLRASQMAEEITRKELQSVRLKLQQQIVTIENAEKEKNENSDLKQQISSLQIQVTSLAQSENDLLNSNQMLKEM 502
Cdd:COG1196 645 --RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELE 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 503 VERLKQECRNFRSQAEKAQLEAEKTLEEKqiqwLEEKHKLHERITDREEKYNQAKEKLQR------AAIAQkkrkslhen 576
Cdd:COG1196 723 EEALEEQLEAEREELLEELLEEEELLEEE----ALEELPEPPDLEELERELERLEREIEAlgpvnlLAIEE--------- 789
|
570 580
....*....|....*....|..
gi 109134347 577 kLKRLQEKVEVLEAKKEELETE 598
Cdd:COG1196 790 -YEELEERYDFLSEQREDLEEA 810
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
222-385 |
1.91e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 222 QKLKGLEAEVAELKAEkeNSEAQVENAQRIQVRQLAEMQATVRSLEAEKQSANLRAERLEKELQSSSEQNTFLIN----- 296
Cdd:COG3206 189 KELEEAEAALEEFRQK--NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspviq 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 297 ----KLHKAEREINTLSSK-------VKELKHSNKLEITDIKLETARAKSELERERNKIQSELDGLQSDNEILKAAVEHH 365
Cdd:COG3206 267 qlraQLAELEAELAELSARytpnhpdVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL 346
|
170 180
....*....|....*....|
gi 109134347 366 KVLLVEkDRELIRKVQAAKE 385
Cdd:COG3206 347 PELEAE-LRRLEREVEVARE 365
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
116-628 |
2.05e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 116 ELLRAQIQQELETPMRERFRNLDEEVEKYRAvynkLRYEHTFLKSEFEHQKeeyARILDEGKIKYESEIARLEEDKEELR 195
Cdd:COG4913 243 ALEDAREQIELLEPIRELAERYAAARERLAE----LEYLRAALRLWFAQRR---LELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 196 NQLLNVDLTKDSKRvEQLAREKVylcQKLKGLEAEVAELKAEKENSEAQVENAQRiQVRQL-AEMQATVRSLEAEKQSAN 274
Cdd:COG4913 316 ARLDALREELDELE-AQIRGNGG---DRLEQLEREIERLERELEERERRRARLEA-LLAALgLPLPASAEEFAALRAEAA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 275 LRAERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKHSNKleitDIKLETARAKSELERERNKIQSELDGL--- 351
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS----NIPARLLALRDALAEALGLDEAELPFVgel 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 352 ---QSDNEILKAAVEhhKVL-------LVEKD--RELIRKVQAAKEEG---YQKlVVLQDEKLELENRLAD--LEKMKVE 414
Cdd:COG4913 467 ievRPEEERWRGAIE--RVLggfaltlLVPPEhyAAALRWVNRLHLRGrlvYER-VRTGLPDPERPRLDPDslAGKLDFK 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 415 HDVWRQSEKDQY-----------EEKLR--------ASQMAEEITRKELQSVRLKLQQQIVTIENAEKEKnensDLKQQI 475
Cdd:COG4913 544 PHPFRAWLEAELgrrfdyvcvdsPEELRrhpraitrAGQVKGNGTRHEKDDRRRIRSRYVLGFDNRAKLA----ALEAEL 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 476 SSLQIQVTSLAQSENDLlnsnQMLKEMVERLKQECRNFRSQ--AEKAQLEAEKTLE--EKQIQWLEEKHKLHERITDREE 551
Cdd:COG4913 620 AELEEELAEAEERLEAL----EAELDALQERREALQRLAEYswDEIDVASAEREIAelEAELERLDASSDDLAALEEQLE 695
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109134347 552 KYNQAKEKLQRAAIAQKKRKSLHENKLKRLQEKVEVLEAKKEELETENQVlnrqnvpfEDYTRLQKRLKDIQRRHNE 628
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--------ELRALLEERFAAALGDAVE 764
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
48-412 |
3.19e-05 |
|
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: 47.37 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 48 NYQTLKAEHTRLQNEHVKLQNELKHLFNEKQTQQEKLQLLLEELrgelVEKTKDLEEMKLQIltpQKLELLRAQIQQELE 127
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL----SDASRKIGEIEKEI---EQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 128 TpMRERFRNLDEEVEKYRAVYNKLRYEHTFLKSEFEHQKEE----YARILDEGKIKYESEIARLEEDKEELRNQL--LNV 201
Cdd:TIGR02169 741 E-LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlndlEARLSHSRIPEIQAELSKLEEEVSRIEARLreIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 202 DLTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQriqvRQLAEMQATVRSLEAEKqsANLRAERLE 281
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE----EELEELEAALRDLESRL--GDLKKERDE 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 282 kelqssseqntfLINKLHKAEREINTLSSKVKELKHsnKLEITDIKLETARAK-SELERERNKIQSELDGLQSDNEILKa 360
Cdd:TIGR02169 894 ------------LEAQLRELERKIEELEAQIEKKRK--RLSELKAKLEALEEElSEIEDPKGEDEEIPEEELSLEDVQA- 958
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109134347 361 avehhKVLLVEKDRELIRKVQAAKEEGYQ-----------KLVVLQDEKLELENRLADLEKMK 412
Cdd:TIGR02169 959 -----ELQRVEEEIRALEPVNMLAIQEYEevlkrldelkeKRAKLEEERKAILERIEEYEKKK 1016
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
155-632 |
8.73e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 8.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 155 HTFLKSEFEHQKEEYARILDEGKIKYESEIARLEEDKEELRNQllnvdltkdskrVEQLAREKvylcQKLKGLEAEVAEL 234
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEK------------EEEYAELQ----EELEELEEELEEL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 235 KAEKENSEAQVENAQRIQvrQLAEMQATVRSLEAEKQSANLRAERLEKELQSSSEqntfLINKLHKAEREINTLSSKVKE 314
Cdd:COG4717 108 EAELEELREELEKLEKLL--QLLPLYQELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 315 LKHSNKLEITDIKLETARAKSELERERNKIQSELDGLQSDNEILKAAVEHHKV-LLVEKDRELIRKVQAAKEEGYQKLVV 393
Cdd:COG4717 182 LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENeLEAAALEERLKEARLLLLIAAALLAL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 394 LQDEKLELENRLADLEKMKVE----HDVWRQSEKDQYEEKLRASQMAEEITRKELQSVRLKLQQQIVTIENaEKEKNENS 469
Cdd:COG4717 262 LGLGGSLLSLILTIAGVLFLVlgllALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPP-DLSPEELL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 470 DLKQQISSLQIQVTSLAQSENDLlnsnqmlkemveRLKQECRNFRSQAEKAQLEAEKTLEEKQIQWlEEKHKLHERITDR 549
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEEL------------QLEELEQEIAALLAEAGVEDEEELRAALEQA-EEYQELKEELEEL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 550 EEKYNQAKEKLQraAIAQKKRKSLHENKLKRLQEKVEVLEAKKEELETENQVLNRQNVPFEDYTRLQKRLKDIQRRHNEF 629
Cdd:COG4717 408 EEQLEELLGELE--ELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAEL 485
|
...
gi 109134347 630 RSL 632
Cdd:COG4717 486 REL 488
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
381-598 |
9.29e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 9.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 381 QAAKEEGYQKLVVLQDEKLELENRLADLEKMKVEhdvwRQSEKDQYEEKLRASQMAEEITRKELQSVRLKLQQQIVTIEN 460
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 461 AEKEKNENSD-LKQQISSLQ-------IQVTSLAQSENDLLNSNQMLKEMVERLKQECRNFRsqAEKAQLEAEKTLEEKQ 532
Cdd:COG4942 95 LRAELEAQKEeLAELLRALYrlgrqppLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR--ADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109134347 533 IQWLEEkhkLHERITDREEKYNQAKEKLQRAAIAQKKRKSLHENKLKRLQEKVEVLEAKKEELETE 598
Cdd:COG4942 173 RAELEA---LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
179-596 |
1.03e-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: 45.83 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 179 KYESEIARLEEDKEELRNQLlnVDLTKDSKRVEQLAREkvyLCQKLKGLEAEVAELKAEKEnseaQVENAQRIQVRQLAE 258
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKREL--SSLQSELRRIENRLDE---LSQELSDASRKIGEIEKEIE----QLEQEEEKLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 259 MQATVRSLEAEKQSANLRAERLEKELQSSSEqntflinKLHKAEREINTLSSKvkeLKHSNKLEITDIKLETARAKSELE 338
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEE-------DLHKLEEALNDLEAR---LSHSRIPEIQAELSKLEEEVSRIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 339 RERNKIQSELDGLQSDNEILKAAVEHHKVLLVEKDrELIRKVQAAKEEGYQKLVVLQDEKLELENRLADLEKMKVEhdvw 418
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK-EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD---- 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 419 RQSEKDQYEEKLRASQMAEEITRKELQSVRLKLQQQIVTIENAEKEKNENSDLKQQISSLQIQVTSLAQsendllnsnqm 498
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED----------- 955
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 499 LKEMVERLKQECRNFRSQAEKAQLEAEKTLEekqiqwleekhklheritdreekynqakeklqraaiaqkkrkslhenKL 578
Cdd:TIGR02169 956 VQAELQRVEEEIRALEPVNMLAIQEYEEVLK-----------------------------------------------RL 988
|
410
....*....|....*...
gi 109134347 579 KRLQEKVEVLEAKKEELE 596
Cdd:TIGR02169 989 DELKEKRAKLEEERKAIL 1006
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
202-603 |
1.34e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 202 DLTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRIQvrQLAEMQATVRSLEAEKQSANLRAERLE 281
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL--QLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 282 KELQSSSEqntfLINKLHKAEREINTLSSKVKELKHSNKLEITDIKLETARAKSELERERNKIQSELDGLQSDNEILKAA 361
Cdd:COG4717 153 ERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 362 VEHHKV-LLVEKDRELIRKVQAAKEEGYQKLVVLQDEKLELENRLADLEKMKV---------EHDVWRQSEKDQYEEKLR 431
Cdd:COG4717 229 LEQLENeLEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLvlgllallfLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 432 ASQMAEEITRKELQSVRLKLQ-QQIVTIENAEKEKNENSDLKQQISSL-----QIQVTSLAQSENDLLNSNQM--LKEMV 503
Cdd:COG4717 309 ALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAeeleeELQLEELEQEIAALLAEAGVedEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 504 ERLKQECRNFRSQAEKAQLEA---EKTLEEKQIQWLEEKHKLHERITDREEKYNQAKEKL-----QRAAIAQKKRKSLHE 575
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEqleELLGELEELLEALDEEELEEELEELEEELEELEEELeelreELAELEAELEQLEED 468
|
410 420
....*....|....*....|....*...
gi 109134347 576 NKLKRLQEKVEVLEAKKEELETENQVLN 603
Cdd:COG4717 469 GELAELLQELEELKAELRELAEEWAALK 496
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
290-596 |
1.43e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.11 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 290 QNTFLINKLHKAEREiNTLSSKVKELKHSnKLEITDIKLETARAKSELERERNKIQSElDGLQSDNEILKAAVEHHKVLL 369
Cdd:pfam17380 267 ENEFLNQLLHIVQHQ-KAVSERQQQEKFE-KMEQERLRQEKEEKAREVERRRKLEEAE-KARQAEMDRQAAIYAEQERMA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 370 VEKDRELIRKVQaakEEGYQKLVVLQDEKLELE-NRLADLEKMKVEHDvwRQSEKDQYE-EKLRASQMAEEITRKELQSV 447
Cdd:pfam17380 344 MERERELERIRQ---EERKRELERIRQEEIAMEiSRMRELERLQMERQ--QKNERVRQElEAARKVKILEEERQRKIQQQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 448 RLKLQQQIVTIENA---------EKEKNENSDLKQQISSLQIQVTSLAQSENDLlnsnqmlKEMVERLKQECRNFRSQAE 518
Cdd:pfam17380 419 KVEMEQIRAEQEEArqrevrrleEERAREMERVRLEEQERQQQVERLRQQEEER-------KRKKLELEKEKRDRKRAEE 491
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109134347 519 KAQLEAEKTLEEKQIQWLEEKHKLHERITDREEKYNQAKEKLQRAAIAQKKRKSLHENKLKRLQEKVEVLEAKKEELE 596
Cdd:pfam17380 492 QRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE 569
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
312-622 |
1.65e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.92 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 312 VKELKHSNKLEITDIKLETARAK-SELERERNKIQSELDGLQSDNEILKAAVEHHKVLLVEKDRELIRKVQAAKEEGYQK 390
Cdd:PRK05771 22 LEALHELGVVHIEDLKEELSNERlRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 391 LVVLQDEKLELENRLADLEKMKVEHDVWRQSEKDqyEEKLRasqmaeeitRKELQSVRLKLqqqiVTIENAEKEKNENSD 470
Cdd:PRK05771 102 IKELEEEISELENEIKELEQEIERLEPWGNFDLD--LSLLL---------GFKYVSVFVGT----VPEDKLEELKLESDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 471 LKQQ-ISSLQIQVTSLAQSENDLLNsnqmlkemverlkqecrNFRSQAEKAQLEAEKTLEEKQIQwlEEKHKLHERITDR 549
Cdd:PRK05771 167 ENVEyISTDKGYVYVVVVVLKELSD-----------------EVEEELKKLGFERLELEEEGTPS--ELIREIKEELEEI 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109134347 550 EEKYNQAKEKLqrAAIAQKkrkslHENKLKRLQEK----VEVLEAKKEELETENQVLNRQNVPFEDYTRLQKRLKDI 622
Cdd:PRK05771 228 EKERESLLEEL--KELAKK-----YLEELLALYEYleieLERAEALSKFLKTDKTFAIEGWVPEDRVKKLKELIDKA 297
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
121-380 |
2.25e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.73 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 121 QIQQELETPMRERFRNLDEEVEKYRAVYNKLRYEHTFLKSEFEHQKEEYARiLDEGKIKYESEIARLEEDK-----EELR 195
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAE-QERMAMERERELERIRQEErkrelERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 196 NQLLNVDLTK---------DSKRVEQLAREKVYLCQKLKGLEAE----VAELKAEKENSEAQVENAQRIQVRQLAEMQA- 261
Cdd:pfam17380 367 QEEIAMEISRmrelerlqmERQQKNERVRQELEAARKVKILEEErqrkIQQQKVEMEQIRAEQEEARQREVRRLEEERAr 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 262 -----------------TVRSLEAEKQSANLRAERLEKELQSSSEQNTFLINK-LHKAEREINTLSSKVKELKHSNKLEI 323
Cdd:pfam17380 447 emervrleeqerqqqveRLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKeLEERKQAMIEEERKRKLLEKEMEERQ 526
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 109134347 324 TDIKLETARAKSELERERNKIQSELDGLQSdnEILKAAVEHHKVLLVEKDRELIRKV 380
Cdd:pfam17380 527 KAIYEEERRREAEEERRKQQEMEERRRIQE--QMRKATEERSRLEAMEREREMMRQI 581
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
188-323 |
2.59e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 188 EEDKEELRNQLLNVDLTKDSKRVEQLARekvylcqKLKGLEAEVAELKAEkenseaqvenaqriqvrqLAEMQATVRSLE 267
Cdd:COG2433 393 EEPEAEREKEHEERELTEEEEEIRRLEE-------QVERLEAEVEELEAE------------------LEEKDERIERLE 447
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 268 AE----KQSANLRAERlEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKHSNKLEI 323
Cdd:COG2433 448 RElseaRSEERREIRK-DREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEH 506
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
389-596 |
4.44e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 389 QKLVVLQDEKLELENRLADLekmkvehdvwrQSEKDQYEEKLRASQMAEEITRKELQsvrlKLQQQIVTIENAEKEKNEn 468
Cdd:COG3883 23 KELSELQAELEAAQAELDAL-----------QAELEELNEEYNELQAELEALQAEID----KLQAEIAEAEAEIEERRE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 469 sDLKQQISSLQIQ------VTSLAQSEN--DLLNSNQMLKEMVERLKQECRNFrsQAEKAQLEAEKTLEEKQIQWLEEKh 540
Cdd:COG3883 87 -ELGERARALYRSggsvsyLDVLLGSESfsDFLDRLSALSKIADADADLLEEL--KADKAELEAKKAELEAKLAELEAL- 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 109134347 541 klheritdrEEKYNQAKEKLQRAAIAQKKRKSLHENKLKRLQEKVEVLEAKKEELE 596
Cdd:COG3883 163 ---------KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
257-627 |
5.74e-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: 43.50 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 257 AEMQATVRSLEAEKQSANLRAERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKHSNKLEITDIkletARAKSE 336
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDI----QRLKND 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 337 LERERNKIQSELDGLQSDNEILKAAVEHHKVLLVEKDRELIRKVQAAKEEGYQKLVVLQDEKLELENRLADLEKMKVEHD 416
Cdd:TIGR00606 767 IEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIE 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 417 VWRQSEKDQYEEKLRASQMAEEITRKELQsVRLKLQQQIVTIENAEKEKNENSDLKQQISSLQIQVTSLAQSENDLLNSN 496
Cdd:TIGR00606 847 LNRKLIQDQQEQIQHLKSKTNELKSEKLQ-IGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 497 QML---------------KEMVERLKQECRNFRSQAEKAQLEAEKTLEEKQIQWLEEKHKLHERiTDREEKYNQAKEKLQ 561
Cdd:TIGR00606 926 EELissketsnkkaqdkvNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEEC-EKHQEKINEDMRLMR 1004
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109134347 562 RAAIAQKKRKSLHENKLKRLQEKVEVLEAKKEELETENQVLNRQNVPF-EDYTRLQKRLKDIQRRHN 627
Cdd:TIGR00606 1005 QDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMkQEHQKLEENIDLIKRNHV 1071
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
38-360 |
6.23e-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: 43.13 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 38 ERLRCEHHKA-NYQTLKAEhtrlqnehvKLQNELKHLFNEKQTQQEKLQLLLEELRGELVEKTKDLEEMKLQILTPQKLE 116
Cdd:TIGR02169 201 ERLRREREKAeRYQALLKE---------KREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 117 LLRAQIQQELETPMRERFRNLDEEVEKYRAVYNKLRYEHTFLKSEFEHQKEEYArildegkiKYESEIARLEEDKEELRn 196
Cdd:TIGR02169 272 QLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA--------KLEAEIDKLLAEIEELE- 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 197 qllnvdltkdsKRVEQLAREKVYLCQKLKGLEAEVAELKAEKEnseaQVENAQRIQVRQLAEMQATVRSLEAEKQSANLR 276
Cdd:TIGR02169 343 -----------REIEEERKRRDKLTEEYAELKEELEDLRAELE----EVDKEFAETRDELKDYREKLEKLKREINELKRE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 277 AERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKEL-----KHSNKLEITDIKLETARAK-SELERERNKIQSELDG 350
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKaleikKQEWKLEQLAADLSKYEQElYDLKEEYDRVEKELSK 487
|
330
....*....|
gi 109134347 351 LQSDNEILKA 360
Cdd:TIGR02169 488 LQRELAEAEA 497
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
514-628 |
6.88e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 514 RSQAEKAQLEAEKTLEE--------KQIQWLEEKHKLHERITDREEKYNQAKEKLQRaaiaQKKRKSLHENKLKRlqeKV 585
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEakkeaeaiKKEALLEAKEEIHKLRNEFEKELRERRNELQK----LEKRLLQKEENLDR---KL 102
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 109134347 586 EVLEAKKEELETENQVLNRQNvpfEDYTRLQKRLKDIQRRHNE 628
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQ---QELEKKEEELEELIEEQLQ 142
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
125-288 |
7.18e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.05 E-value: 7.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 125 ELETPMRERFRnLDEEVEKYRAVYNKLRYEHTFLKSEFEHQKEEYARILDEGKIKYESEIARLEEDKEELRNQLLNVDLT 204
Cdd:pfam09787 48 ELEELRQERDL-LREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 205 KdskrvEQLAREKVYLCQKLKGLEAEVAELKAEKEN------SEAQVENAQRIQVRQLAEMQATVRSLEAEKQSANLRAE 278
Cdd:pfam09787 127 E-----EELRRSKATLQSRIKDREAEIEKLRNQLTSksqsssSQSELENRLHQLTETLIQKQTMLEALSTEKNSLVLQLE 201
|
170
....*....|
gi 109134347 279 RLEKELQSSS 288
Cdd:pfam09787 202 RMEQQIKELQ 211
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
243-491 |
7.56e-04 |
|
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: 7.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 243 AQVENAQRIQVRQLAEMQATVRSLEAEKQSANLRAERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKhsNKLE 322
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR--EELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 323 itdiklETARAKSELERERNKIQSELDGlQSDNEILK--AAVEHhkvlLVEKDRELIRKVQAAKEEGYQKLVVLQDEKLE 400
Cdd:COG3883 90 ------ERARALYRSGGSVSYLDVLLGS-ESFSDFLDrlSALSK----IADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 401 LENRLADLEKMKVEHDVwRQSEKDQYEEKLRASQMAEEITRKELQSVRLKLQQQIVTIENAEKEKNENSDLKQQISSLQI 480
Cdd:COG3883 159 LEALKAELEAAKAELEA-QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
250
....*....|.
gi 109134347 481 QVTSLAQSEND 491
Cdd:COG3883 238 AAAAAAASAAG 248
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
158-523 |
7.62e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 158 LKSEFEHQKEEYARIL---DEGKIKYESEIARLEEDKEELRnqllnvdltkdsKRVEQLAREKVylcqKLKGLEAEVAEL 234
Cdd:pfam15921 438 MKSECQGQMERQMAAIqgkNESLEKVSSLTAQLESTKEMLR------------KVVEELTAKKM----TLESSERTVSDL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 235 KAEKENSEAQVE--NAQRIQVR-----QLAEMQAT------VRSLEAEKQSANLRAERLEKELQSSSEQNTFLINKLHKA 301
Cdd:pfam15921 502 TASLQEKERAIEatNAEITKLRsrvdlKLQELQHLknegdhLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQH 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 302 EREINTLSSKVKELKHsnklEITDIKLETARAKSELERERNKIQsELDGLQSDNEIlkaavehHKVLLVEKDRELIRKVQ 381
Cdd:pfam15921 582 GRTAGAMQVEKAQLEK----EINDRRLELQEFKILKDKKDAKIR-ELEARVSDLEL-------EKVKLVNAGSERLRAVK 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 382 AAKEEGYQKLVVLQDEKLELENRLADLEKMKveHDVWRQSEK-----DQYEEKLRASQMAEEITRKELQS---------- 446
Cdd:pfam15921 650 DIKQERDQLLNEVKTSRNELNSLSEDYEVLK--RNFRNKSEEmetttNKLKMQLKSAQSELEQTRNTLKSmegsdghamk 727
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 447 VRLKLQQQIVT------------------IENAEKEKNEnsdLKQQISSLQIQVTSLAQSENDLLNSNQMLKEMVERLKQ 508
Cdd:pfam15921 728 VAMGMQKQITAkrgqidalqskiqfleeaMTNANKEKHF---LKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
|
410
....*....|....*
gi 109134347 509 ECRNFRSQAEKAQLE 523
Cdd:pfam15921 805 KVANMEVALDKASLQ 819
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
35-508 |
9.23e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 9.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 35 LIDERLRCEHHKANYQTLKAEHTRLQNEHVKLQNELKHLfNEKQTQQEKLQLLLEELRGELVEKTKDLEEMKLQILTPQK 114
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKL-EEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 115 LELLRAQIQQELETPMRE--RFRNLDEEVEKYRAVYNKLRYEHTFLKSEFEHQKEEYARIldEGKIKYESEIARLEEDKE 192
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRlsRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEL--EERHELYEEAKAKKEELE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 193 ELRNQLLNVDLTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRIQVR-QLAEMQATVRSLEAEKQ 271
Cdd:PRK03918 376 RLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcPVCGRELTEEHRKELLE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 272 SANLRAERLEKELQSSSEQNTFLINKLHKAEREINTLSSKVKELKHSNKLEITDIKLETARAK--SELERERNKIQSELD 349
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEelEKKAEEYEKLKEKLI 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 350 GLQSDNEILKAAVEHHKVLLVEKdRELIRKVQAAKEEGYQKLVVLQDEKL----ELENRLADLEKMKVEHDVWRQSEKDQ 425
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEELKKKL-AELEKKLDELEEELAELLKELEELGFesveELEERLKELEPFYNEYLELKDAEKEL 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 426 YEEKLRASQMAEEI---------TRKELQSVRLKLQQ--QIVTIENAEKEKNENSDLKQQISSLQIQVTSLAQSENDLLN 494
Cdd:PRK03918 615 EREEKELKKLEEELdkafeelaeTEKRLEELRKELEEleKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKK 694
|
490
....*....|....
gi 109134347 495 SNQMLKEMVERLKQ 508
Cdd:PRK03918 695 TLEKLKEELEEREK 708
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
43-509 |
1.20e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 43 EHHKANYQTLKAEHTRLQNEHVKLQNELKHLfnekqtqqeklqllleelrgelvektKDLEEMKLQILTPQKLELLRAQI 122
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELEAELEEL--------------------------REELEKLEKLLQLLPLYQELEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 123 QQELEtPMRERFRNLDEEVEKYRAVYNKLRyehtFLKSEFEHQKEEYARILDEGKIKYESEIARLEEDKEELRnqllnvd 202
Cdd:COG4717 138 EAELA-ELPERLEELEERLEELRELEEELE----ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 203 ltkdsKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRiqvRQLAEMQATVRSLEAEKQSANLRAERLEK 282
Cdd:COG4717 206 -----QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA---RLLLLIAAALLALLGLGGSLLSLILTIAG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 283 ELQSSSEQNTFLINKLHKAEREINTLSSKVKELKHSNKLEITDIKLETARAKSELERERNKIQSELDGLQSDNEILKAAV 362
Cdd:COG4717 278 VLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 363 EHHKVLLVE----KDRELIRKVQAAKEEGYQKLVVLQDEKLELENRLADLE-----KMKVEHDVWRQSEKDQYEEKLRAS 433
Cdd:COG4717 358 ELEEELQLEeleqEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEeqleeLLGELEELLEALDEEELEEELEEL 437
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109134347 434 QMAEEITRKELQSVRLKLQQQIVTIENAEKEkNENSDLKQQISSLQIQVTSLAQSendlLNSNQMLKEMVERLKQE 509
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEED-GELAELLQELEELKAELRELAEE----WAALKLALELLEEAREE 508
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
113-304 |
1.98e-03 |
|
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: 40.90 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 113 QKLELLRAQIQQeletpMRERFRNLDEEVEKYRAVYNKLRYEHTFLKSEFEHQKEEYARILDE----GKIKYESEIARLE 188
Cdd:COG4942 55 KQLAALERRIAA-----LARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAlyrlGRQPPLALLLSPE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 189 EDKEELRN-QLLNVDLTKDSKRVEQLAREKvylcQKLKGLEAEVAELKAEKENSEAQVENAQRIQVRQLAEMQATVRSLE 267
Cdd:COG4942 130 DFLDAVRRlQYLKYLAPARREQAEELRADL----AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE 205
|
170 180 190
....*....|....*....|....*....|....*..
gi 109134347 268 AEKQSANLRAERLEKELQSSSEqntfLINKLHKAERE 304
Cdd:COG4942 206 KELAELAAELAELQQEAEELEA----LIARLEAEAAA 238
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
161-610 |
2.55e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.19 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 161 EFEHQKEEYARILDEGKIKYE------SEIARLEEDK---EELRNQLLNVDLTKDSKRVEQLAREKVYLCQKLKGLEAEV 231
Cdd:TIGR01612 1170 EIEKKIENIVTKIDKKKNIYDeikkllNEIAEIEKDKtslEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYI 1249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 232 AELKAEKENSEaQVENAQRIQVRQLAEMQAT-----------VRSLEAEKQSANLRAERLE---------------KELQ 285
Cdd:TIGR01612 1250 EDLDEIKEKSP-EIENEMGIEMDIKAEMETFnishdddkdhhIISKKHDENISDIREKSLKiiedfseesdindikKELQ 1328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 286 S--------SSEQNTFL--------INKLHKAEREINTLSSKVKELKHSNK-----LEITDIKLETARAKSELERERNKI 344
Cdd:TIGR01612 1329 KnlldaqkhNSDINLYLneianiynILKLNKIKKIIDEVKEYTKEIEENNKnikdeLDKSEKLIKKIKDDINLEECKSKI 1408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 345 QSELDGLQSDNEILKAAVEHHKVLLVEKDRELIRKvqAAKEegYQKLVVLQDEKLELENRLA-----------------D 407
Cdd:TIGR01612 1409 ESTLDDKDIDECIKKIKELKNHILSEESNIDTYFK--NADE--NNENVLLLFKNIEMADNKSqhilkikkdnatndhdfN 1484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 408 LEKMKvEHDVWRQSEKDQYEEKLRASQMAEEITRKELQSVRLKLQQ--QIVTIENAEKEKNENSDLKQQISSLQIQVTSL 485
Cdd:TIGR01612 1485 INELK-EHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKysALAIKNKFAKTKKDSEIIIKEIKDAHKKFILE 1563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 486 AQSENDLLNSnqmLKEMVERLKQECRNfRSQAEKAQLEAEKTLEEKQIQWLEEKHkLHERITDREEKYNQAKEKLQRAAI 565
Cdd:TIGR01612 1564 AEKSEQKIKE---IKKEKFRIEDDAAK-NDKSNKAAIDIQLSLENFENKFLKISD-IKKKINDCLKETESIEKKISSFSI 1638
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 109134347 566 -AQKKRKSLHENKLKRLQEKVEVLEAKKEELETENQVLNRQNVPFE 610
Cdd:TIGR01612 1639 dSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIE 1684
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
191-516 |
2.60e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 191 KEELRNQLLNV----DLTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQriqvRQLAEMQATVRSl 266
Cdd:PRK11281 38 EADVQAQLDALnkqkLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQ----AELEALKDDNDE- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 267 EAEKQSANLRAERLEKELQSSSEQntflinkLHKAEREINTLSSKVkelkhsnkleitdIKLETArakseLERERNKIQS 346
Cdd:PRK11281 113 ETRETLSTLSLRQLESRLAQTLDQ-------LQNAQNDLAEYNSQL-------------VSLQTQ-----PERAQAALYA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 347 ELDGLQSDNEILKAavehhkvllVEKDRELIRKVQAAKEEGYQKLVVLQDE--KLELEN--RLADLEKMKVEHDVWRQse 422
Cdd:PRK11281 168 NSQRLQQIRNLLKG---------GKVGGKALRPSQRVLLQAEQALLNAQNDlqRKSLEGntQLQDLLQKQRDYLTARI-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 423 kDQYEEKLRASQmaEEITRKelqsvRLKLQQQIVT-IENAEK--EKNENSDLKQQIS-SLQIQVTSLAQSE--NDLLNSN 496
Cdd:PRK11281 237 -QRLEHQLQLLQ--EAINSK-----RLTLSEKTVQeAQSQDEaaRIQANPLVAQELEiNLQLSQRLLKATEklNTLTQQN 308
|
330 340
....*....|....*....|
gi 109134347 497 QMLKEMVERLKQECRNFRSQ 516
Cdd:PRK11281 309 LRVKNWLDRLTQSERNIKEQ 328
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
230-605 |
2.85e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 230 EVAELKAEKENSEAQVENAQRIQV---RQLAEMQATVRSLEAEKQSANlraERLEKELQSSSEQNtflinKLHKAEREIN 306
Cdd:PRK04863 287 EALELRRELYTSRRQLAAEQYRLVemaRELAELNEAESDLEQDYQAAS---DHLNLVQTALRQQE-----KIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 307 TLSSKVKELKHSNKlEITDIKLETARAKSELERERNKIQSELDGLQSDNEIL--KAAVEHHKVLLVEKDREL-------I 377
Cdd:PRK04863 359 ELEERLEEQNEVVE-EADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQqtRAIQYQQAVQALERAKQLcglpdltA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 378 RKVQAAKEEGYQKLVVLQDEKLELENRLADlekmkvehdvwRQSEKDQYEEKLRA-SQMAEEITRKELQsvrlklQQQIV 456
Cdd:PRK04863 438 DNAEDWLEEFQAKEQEATEELLSLEQKLSV-----------AQAAHSQFEQAYQLvRKIAGEVSRSEAW------DVARE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 457 TIENAEKEKNensdLKQQISSLQIQVTSLAQSENDLLNSNQMLKEMVERLKQECRN------FRSQAEKAQLEAEKTLEE 530
Cdd:PRK04863 501 LLRRLREQRH----LAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDedeleqLQEELEARLESLSESVSE 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 531 KQIQWLEEKHKLHERITDREEKYNQAKEKLQRAAIAQKKRKSLHE---------NKLKRLQEKVEVLEAKKEELETENQV 601
Cdd:PRK04863 577 ARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEefedsqdvtEYMQQLLERERELTVERDELAARKQA 656
|
....
gi 109134347 602 LNRQ 605
Cdd:PRK04863 657 LDEE 660
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
222-408 |
3.31e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 222 QKLKGLEAEVAELKAEKENSEAQVENAQRI-----QVRQLAEMQATVRSLEAEKQSANLRAERLEKELQSSSEQNtfliN 296
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAEldalqERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASS----D 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 297 KLHKAEREINTLSSKVKELKHsnklEITDIKletaRAKSELERERNKIQSELDGLQSDNEILKAAVEHHKVLLVEK--DR 374
Cdd:COG4913 686 DLAALEEQLEELEAELEELEE----ELDELK----GEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErfAA 757
|
170 180 190
....*....|....*....|....*....|....*
gi 109134347 375 ELIRKVQAAKEEGYQK-LVVLQDEKLELENRLADL 408
Cdd:COG4913 758 ALGDAVERELRENLEErIDALRARLNRAEEELERA 792
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
37-474 |
3.88e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 37 DERLRCEHHKANYQTLKAEHTRLQNEHVKLQNELKHLFNEKQTQQEKLQLLLEELRGELVEKTKDLEEMKLQILTPQKLE 116
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE 1442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 117 LLRAQIQQELETPMRERFRNLDEEVEKYRAVYNKLRYEHTFLKSEFEHQKEEYARILDEGKIKYESEIARLEEDKEELRN 196
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 197 QLLNVDLTKDSKRVEQLAR-EKVYLCQKLKGLEA--------EVAELKAEKENSEA---------QVENAQRIQVRQLAE 258
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKaEEKKKADELKKAEElkkaeekkKAEEAKKAEEDKNMalrkaeeakKAEEARIEEVMKLYE 1602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 259 MQATVRSLEAEK-QSANLRAERLEKElqsssEQNTFLINKLHKAEREINTLSSKVKELKHSNKLEITDIKLETARAKSEL 337
Cdd:PTZ00121 1603 EEKKMKAEEAKKaEEAKIKAEELKKA-----EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 338 ERERnkiQSELDGLQSDNEILKAAVEHHKVLLVEK-DRELIRKVQAAKEEGYQKLVVLQDEKLELENRLADLEKMKVEHD 416
Cdd:PTZ00121 1678 EEAK---KAEEDEKKAAEALKKEAEEAKKAEELKKkEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 109134347 417 VWRQSEKDQYEEKLRASQMAEEITRKELQSVRLKLQQQIVTIENAEKEKNENSDLKQQ 474
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
195-290 |
4.74e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 195 RNQLLNVDLTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRiqvrQLAEMQATVRSLEAEKQSAN 274
Cdd:COG3883 120 RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA----QQAEQEALLAQLSAEEAAAE 195
|
90
....*....|....*.
gi 109134347 275 LRAERLEKELQSSSEQ 290
Cdd:COG3883 196 AQLAELEAELAAAEAA 211
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
179-520 |
4.84e-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: 40.39 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 179 KYESEIARLEEDKEELRNQLLNVDLTKDSKRVEQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQRiqvrQLAE 258
Cdd:TIGR04523 292 QLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQR----ELEE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 259 MQATVRSLEAEKQSANLRAERLEK-------ELQSSSEQNTFLINKLHKAEREINTLSSKVKELKHSNKLEITDIKlETA 331
Cdd:TIGR04523 368 KQNEIEKLKKENQSYKQEIKNLESqindlesKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK-DLT 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 332 RAKSELERERNKIQSELDGLQSDNEILKAAVEHHKVLLVEKDRELIRKVQ------AAKEEGYQKLVVLQDEKLELENRL 405
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKelkklnEEKKELEEKVKDLTKKISSLKEKI 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 406 ADLEKMKVEHDVWRQSEKDQYEEK---LRASQMAEEITRKELQSVRLKLQQQIVTIENAEKEK------NENSDLKQQIS 476
Cdd:TIGR04523 527 EKLESEKKEKESKISDLEDELNKDdfeLKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQElidqkeKEKKDLIKEIE 606
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 109134347 477 SLQIQVTSL------AQSENDLLNSNQM-LKEMVERLKQECRNFRSQAEKA 520
Cdd:TIGR04523 607 EKEKKISSLekelekAKKENEKLSSIIKnIKSKKNKLKQEVKQIKETIKEI 657
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
444-594 |
5.32e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 444 LQSVRLKLQQQIVTIENAEKE-KNENSDLKQQISSLQiqvtslaqsendllnsnQMLKEMVERLKQECRNFRSQAEKAQL 522
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEaEKLKEELEEKKEKLQ-----------------EEEDKLLEEAEKEAQQAIKEAKKEAD 587
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109134347 523 EAEKTLEEKQIQWLEEKhKLHErITDREEKYNQAKEKLQRAAIAQKKR-KSLHEN---KLKRLQEKVEVLEAKKEE 594
Cdd:PRK00409 588 EIIKELRQLQKGGYASV-KAHE-LIEARKRLNKANEKKEKKKKKQKEKqEELKVGdevKYLSLGQKGEVLSIPDDK 661
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
131-290 |
6.12e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.75 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 131 RERFRNLDEEVEKYRAVYNKLRYEHTFLKSEFEHQKEEYARIldegkikyESEIARLEEDKEELRNQLLNVdltKDSKRV 210
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL--------ELEIEEVEARIKKYEEQLGNV---RNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 211 EQLAREKVYLCQKLKGLEAEVAELKAEKENSEAQVENAQriqvRQLAEMQATVRSLEAEKQSANLRAERLEKELQSSSEQ 290
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELE----AELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
278-596 |
6.86e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 39.61 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 278 ERLEKELQSSSE-----QNTFLINKLHKAEREintLSSKVKELKHSNKLEITdikletARAKSELERERNKIQSELDGLQ 352
Cdd:NF033838 68 EKILSEIQKSLDkrkhtQNVALNKKLSDIKTE---YLYELNVLKEKSEAELT------SKTKKELDAAFEQFKKDTLEPG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 353 SDNEILKAAVEHHKvllvekdreliRKVQAAKEEGYQKLVVLQDEKLELEN-------RLADLEKMKVEHDVWRQSEKDQ 425
Cdd:NF033838 139 KKVAEATKKVEEAE-----------KKAKDQKEEDRRNYPTNTYKTLELEIaesdvevKKAELELVKEEAKEPRDEEKIK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 426 YEEKLRASQMAEEITRKELQSVRLKLQQQIVTIENAEKEK--NENSDLKQQ--------ISSLQIQVTSlAQSENDLLNS 495
Cdd:NF033838 208 QAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEavEKNVATSEQdkpkrrakRGVLGEPATP-DKKENDAKSS 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 496 NQMLKEMV---ERLKQECRnfRSQAEKAQLEAEKTLEEKQiqwlEEKHK---------LHERITDREEKYNQAKEKLqra 563
Cdd:NF033838 287 DSSVGEETlpsPSLKPEKK--VAEAEKKVEEAKKKAKDQK----EEDRRnyptntyktLELEIAESDVKVKEAELEL--- 357
|
330 340 350
....*....|....*....|....*....|...
gi 109134347 564 aIAQKKRKSLHENKLKRLQEKVEVLEAKKEELE 596
Cdd:NF033838 358 -VKEEAKEPRNEEKIKQAKAKVESKKAEATRLE 389
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
226-587 |
7.44e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.57 E-value: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 226 GLEAEVAELKAEKENSEAQVENAQRIQVRQLAEMQATVRSLEAEKQSANLRAERLEKELQSSSEQNTFLINKLHKAEREI 305
Cdd:pfam02463 654 LEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDK 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 306 NTLSSKVKELKHSNKLEITDIKLETARAKSELERERNKIQSELDGLQSDNEILKAAVEHHKVLLVEKDRELIRKVQAAKE 385
Cdd:pfam02463 734 INEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEE 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 386 EGYQKLVVLQDEKLELENRLADLEKMKVEHDVWRQSEKDQYEEKLRASQMAEEITRKELQSVRLKLQQQIVTIENAEKEK 465
Cdd:pfam02463 814 AELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEE 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 466 NENSDLKQQISSLQIQVTSLAQSENDLLNSNQMLKEMVERLKQECRNFRSQAEKAQLEAEKTLEEKQIQWLEEKHKLHER 545
Cdd:pfam02463 894 KEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELG 973
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 109134347 546 ------ITDREEKYNQAKEKLQRAAIAQKKRKSLHENKLKRLQEKVEV 587
Cdd:pfam02463 974 kvnlmaIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
297-470 |
9.58e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.99 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 297 KLHKAEREI-NTLSSKVKELKHSNKLEITDIKLETARAKSELERERNKIQSELDGLQSDNEILKAAVEHHKVLLVEKDRE 375
Cdd:PRK12704 32 KIKEAEEEAkRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109134347 376 lirkvqaakeegyqklvvLQDEKLELENRLADLEKMKVEHDVWRQSEKDQYEeklRASQM-AEEITRKELQSVRLKLQQQ 454
Cdd:PRK12704 112 ------------------LEKKEKELEQKQQELEKKEEELEELIEEQLQELE---RISGLtAEEAKEILLEKVEEEARHE 170
|
170
....*....|....*..
gi 109134347 455 I-VTIENAEKEKNENSD 470
Cdd:PRK12704 171 AaVLIKEIEEEAKEEAD 187
|
|
|