|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
120-784 |
3.29e-17 |
|
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: 86.65 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 120 KMNRYDKKIDSLMNAVGCLKSEVKMQKGERQMAKRFLEERKEELEEVAHELAETEHENTVLRHNIERIKEEKDFTMLQKK 199
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 200 HLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETNRTLRDLLREQH 279
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 280 CKEDSERLmeqqGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQ-AQLRCKE 358
Cdd:TIGR02168 435 LKELQAEL----EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgFSEGVKA 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 359 AENSRLCM-----QIKNLERSGNQHKAEVEA---------IMEQLKELKQKGDRDKETLK--------KAIRAQKERAEK 416
Cdd:TIGR02168 511 LLKNQSGLsgilgVLSELISVDEGYEAAIEAalggrlqavVVENLNAAKKAIAFLKQNELgrvtflplDSIKGTEIQGND 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 417 SEEYAEQLHVQLADKDL--YVAEALSTLESWRSRYnqVVKDKGDLELEIIVLNDR----VT---DLVNQQQSLEEKMRED 487
Cdd:TIGR02168 591 REILKNIEGFLGVAKDLvkFDPKLRKALSYLLGGV--LVVDDLDNALELAKKLRPgyriVTldgDLVRPGGVITGGSAKT 668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 488 RDSLVERlhrqtaeysafKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDnyksqvmktrlEADEVAAQLER 567
Cdd:TIGR02168 669 NSSILER-----------RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE-----------QLRKELEELSR 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 568 CDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLE 647
Cdd:TIGR02168 727 QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 648 MAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAiEDARRQV 727
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL-LNERASL 885
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 728 EQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQS---RLQDLKDRL 784
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGlevRIDNLQERL 945
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
228-786 |
1.04e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 228 ALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETNRTLRDLLREQhcKEDSERLMEQQGTLLKRLAEADSEKAR 307
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL--LAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 308 LllllqdkDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIME 387
Cdd:COG1196 321 L-------EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 388 QLKELKQKgdrdKETLKKAIRAQKERAEKSEEYAEQLHVQLadkdlyvAEALSTLESWRSRYNQVVKDKGDLELEIIVLN 467
Cdd:COG1196 394 AAAELAAQ----LEELEEAEEALLERLERLEEELEELEEAL-------AELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 468 DRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAP-MEDKLNQAHLEVQQLKASVKNYEGMIDN 546
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAlLLAGLRGLAGAVAVLIGVEAAYEAALEA 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 547 YKSQVMKTRL-EADEVAAQLERCDKENKMLKDE---MNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYE 622
Cdd:COG1196 543 ALAAALQNIVvEDDEVAAAAIEYLKAAKAGRATflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 623 RKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRL 702
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 703 EEktrecgslARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKD 782
Cdd:COG1196 703 EE--------EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
....
gi 1907136589 783 RLEQ 786
Cdd:COG1196 775 EIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
370-743 |
2.90e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 370 NLERsgnqhkaeVEAIMEQLkelkqkgDRDKETLKKairaQKERAEKSEEYAEQLhvQLADKDLYVAealstleswrsRY 449
Cdd:COG1196 187 NLER--------LEDILGEL-------ERQLEPLER----QAEKAERYRELKEEL--KELEAELLLL-----------KL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 450 NQVVKDKGDLELEIIVLNDRVTDLVNQQQSLE---EKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQA 526
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEaelEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 527 HLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLErcdkenkmlkdemnkEIEAARRQFQSQLADLqqlpdilki 606
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELE---------------EAEAELAEAEEALLEA--------- 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 607 tEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQ 686
Cdd:COG1196 371 -EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907136589 687 VIAKREEAIHQAQLRLEEKTREcgslARQLESAIEDARRQVEQTKEQALSKERAAQS 743
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEE----AALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
466-789 |
1.54e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 466 LNDRVTDLVNQQQSLEEKMR--EDRDSLVERLHRQTAEYSAFKLEneRLKASFAPMEDKLNQAHLEVQQLKASVKNYEGM 543
Cdd:COG1196 191 LEDILGELERQLEPLERQAEkaERYRELKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 544 IDNYKSQVMKTRLEADEVAAQLERCDKEnkmlKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYER 623
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAE----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 624 KNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQnvefLQVIAKREEAIHQAQLRLE 703
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ----LEELEEAEEALLERLERLE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 704 EKTRECGSLARQLESAIEDARRQVEQTKE---QALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDL 780
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEeeaELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
....*....
gi 1907136589 781 KDRLEQSES 789
Cdd:COG1196 501 ADYEGFLEG 509
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
253-808 |
2.75e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 253 QKELLLQKLSTFEETNRTLRDLLREQhcKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQcekaq 332
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEA--EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS----- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 333 aktaselskSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKE 412
Cdd:TIGR02168 299 ---------RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 413 RAEKSEEYAEQLHvQLADKdlyVAEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLE-EKMREDRDSL 491
Cdd:TIGR02168 370 LESRLEELEEQLE-TLRSK---VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEEL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 492 VERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKS------QVMKTRLEAD------ 559
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegvkALLKNQSGLSgilgvl 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 560 ----EVAAQLERC---------------DKENKMLKDEMNKEIEAARRQF------------QSQLADLQQLPDILKITe 608
Cdd:TIGR02168 526 seliSVDEGYEAAieaalggrlqavvveNLNAAKKAIAFLKQNELGRVTFlpldsikgteiqGNDREILKNIEGFLGVA- 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 609 AKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQ-------------GDKL----------EMAREKHQASQKENKQLSQ 665
Cdd:TIGR02168 605 KDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAkklrpgyrivtldGDLVrpggvitggsAKTNSSILERRREIEELEE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 666 KVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESA------IEDARRQVEQTKEQALSKER 739
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeveqLEERIAQLSKELTELEAEIE 764
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907136589 740 AAQSKILDLETQLSRTKTELGQLrrtrddadrryQSRLQDLKDRLEQSESTNRSMQNYVQFLKASYANV 808
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEEL-----------EAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
253-704 |
7.10e-11 |
|
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: 66.30 E-value: 7.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 253 QKELLLQKLSTFEETNRTLRDLLRE-QHCKEDSERLMEQQGTLLK-RLAEADSEKARLLLLLQDKDKEVEELL------- 323
Cdd:pfam15921 311 QNSMYMRQLSDLESTVSQLRSELREaKRMYEDKIEELEKQLVLANsELTEARTERDQFSQESGNLDDQLQKLLadlhkre 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 324 QEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERS-GNQHKAEVEAI------MEQLKELKQKG 396
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIqgknesLEKVSSLTAQL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 397 DRDKETLKKAIR---AQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYN------QVVKDKGD------LEL 461
Cdd:pfam15921 471 ESTKEMLRKVVEeltAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDlklqelQHLKNEGDhlrnvqTEC 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 462 EIIVLN---------------DRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQA 526
Cdd:pfam15921 551 EALKLQmaekdkvieilrqqiENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 527 HLEVQQLK-------ASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQQ 599
Cdd:pfam15921 631 ELEKVKLVnagserlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 600 LPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKV-------DELER 672
Cdd:pfam15921 711 TRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELstvatekNKMAG 790
|
490 500 510
....*....|....*....|....*....|..
gi 1907136589 673 KLEATSAQNVEFLQVIAKREEAIHQAQLRLEE 704
Cdd:pfam15921 791 ELEVLRSQERRLKEKVANMEVALDKASLQFAE 822
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
359-722 |
1.66e-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: 65.08 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 359 AENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEA 438
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 439 LSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMredrDSLVERLHRQTAEYSAFKLENERLKASFAP 518
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL----DELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 519 MEDKLNQAHLEVQQLKASVKNYEGMIDNYksqvmktRLEADEVAAQLERCDKEnkmlKDEMNKEIEAARRQFQSQLADLQ 598
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEEL-------EELIEELESELEALLNE----RASLEEALALLRSELEELSEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 599 QLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRI-EHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEAT 677
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1907136589 678 SAQNVEFLQVIAKREEaihqaqlRLEEKTRECGSLAR---QLESAIED 722
Cdd:TIGR02168 985 GPVNLAAIEEYEELKE-------RYDFLTAQKEDLTEakeTLEEAIEE 1025
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
554-792 |
6.36e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 6.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 554 TRLEA--DEVAAQLERCDKE------NKMLKDEMN-KEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERK 624
Cdd:COG1196 189 ERLEDilGELERQLEPLERQaekaerYRELKEELKeLEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 625 NIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEE 704
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 705 KTRECGSLARQLESAiEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRL 784
Cdd:COG1196 349 AEEELEEAEAELAEA-EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
....*...
gi 1907136589 785 EQSESTNR 792
Cdd:COG1196 428 EALAELEE 435
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
174-811 |
8.90e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 8.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 174 EHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTC-TDINTLTR 252
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVkEKIGELEA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 253 QKELLLQKLstfEETNRTLRDLL-REQHCKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKA 331
Cdd:TIGR02169 302 EIASLERSI---AEKERELEDAEeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 332 QAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELkqkgDRDKETLKKAIRAQK 411
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL----EEEKEDKALEIKKQE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 412 ERAEKSEEYAEQLHVQLADKdlyvaealstleswRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQ---SLEEKMREDR 488
Cdd:TIGR02169 455 WKLEQLAADLSKYEQELYDL--------------KEEYDRVEKELSKLQRELAEAEAQARASEERVRggrAVEEVLKASI 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 489 DS---LVERLHRQTAEYsAFKLE---NERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEV- 561
Cdd:TIGR02169 521 QGvhgTVAQLGSVGERY-ATAIEvaaGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVi 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 562 --AAQLERCDKENK-----MLKDEMNKE-IEAARRQF---------------------------------QSQLADLQQL 600
Cdd:TIGR02169 600 gfAVDLVEFDPKYEpafkyVFGDTLVVEdIEAARRLMgkyrmvtlegelfeksgamtggsraprggilfsRSEPAELQRL 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 601 PDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQ 680
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 681 NVEFLQVIAKREEAIHQAQLRLEE-KTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLEtQLSRTKTEL 759
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE-YLEKEIQEL 838
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1907136589 760 GQLRRTRDDADRRYQSRLQDLKDRLEQSESTNRSMQNYVQFLKASYANVFGD 811
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
199-539 |
9.81e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 9.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 199 KHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQmtctdinTLTRQKELLLQKLSTFEETNRTLRDLLREQ 278
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-------ELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 279 HckEDSERLMEQQGTLLKRLAEADSEKArlllllqdkdkeveELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKE 358
Cdd:TIGR02168 753 S--KELTELEAEIEELEERLEEAEEELA--------------EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 359 AENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQkgdrDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEA 438
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSE----DIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 439 LSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKmredRDSLVERLhrqTAEYSafkLENERLKASFAP 518
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR----IDNLQERL---SEEYS---LTLEEAEALENK 962
|
330 340
....*....|....*....|.
gi 1907136589 519 MEDKLNQAHLEVQQLKASVKN 539
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKE 983
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
168-675 |
2.47e-09 |
|
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: 60.80 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 168 HELAETEHENTVLRHniERIKEEKDFTMLQKKhlQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTDI 247
Cdd:TIGR04523 180 KEKLNIQKNIDKIKN--KLLKLELLLSNLKKK--IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 248 NTLTRQ----KELLLQKLSTFEETNRTLRDLlreqhckedserlMEQQGTLLKRLAEADSEKArlllllQDKDKEVEELL 323
Cdd:TIGR04523 256 NQLKDEqnkiKKQLSEKQKELEQNNKKIKEL-------------EKQLNQLKSEISDLNNQKE------QDWNKELKSEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 324 QEIQCEKAQAKTasELSKSMESMrghlqaqlrckeaenSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKgdrdKETL 403
Cdd:TIGR04523 317 KNQEKKLEEIQN--QISQNNKII---------------SQLNEQISQLKKELTNSESENSEKQRELEEKQNE----IEKL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 404 KKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLE-- 481
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEli 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 482 -EKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADE 560
Cdd:TIGR04523 456 iKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 561 VAAQLErcDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKnidltaiISDLRSRIE 640
Cdd:TIGR04523 536 KESKIS--DLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE-------KKDLIKEIE 606
|
490 500 510
....*....|....*....|....*....|....*
gi 1907136589 641 HQGDKLEMAREKHQASQKENKQLSQKVDELERKLE 675
Cdd:TIGR04523 607 EKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKN 641
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
287-786 |
2.62e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 61.01 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 287 LMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTA-----SELSKSMESMRGHLQAQLRCKEAEN 361
Cdd:pfam12128 267 YKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAvakdrSELEALEDQHGAFLDADIETAAADQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 362 SRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADkdlyvaeALST 441
Cdd:pfam12128 347 EQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAED-------DLQA 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 442 LES-WRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKM--REDRDSLVER----LHRQTAEYSAFKLENERLKA 514
Cdd:pfam12128 420 LESeLREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLlqLENFDERIERareeQEAANAEVERLQSELRQARK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 515 SFAPMEDKLNQAHLEVQQLKASVKNYEGMID----------NYKSQVMKTRLEADEVAAQLERCDkenkmLKDEMNKEIE 584
Cdd:pfam12128 500 RRDQASEALRQASRRLEERQSALDELELQLFpqagtllhflRKEAPDWEQSIGKVISPELLHRTD-----LDPEVWDGSV 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 585 AARRQFQSQLADLQQL--PDILKITEAklaecqdqlqgyerknidltaiisdLRSRIEHQGDKLEMAREKHQASQKENKQ 662
Cdd:pfam12128 575 GGELNLYGVKLDLKRIdvPEWAASEEE-------------------------LRERLDKAEEALQSAREKQAAAEEQLVQ 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 663 LSQKVDELERKLEatsaqnveflqvIAKReeAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQAlskerAAQ 742
Cdd:pfam12128 630 ANGELEKASREET------------FART--ALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSL-----EAQ 690
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1907136589 743 SKILDLETQLSRTKTElGQLRRTRDDADRRYQSRLQDLKDRLEQ 786
Cdd:pfam12128 691 LKQLDKKHQAWLEEQK-EQKREARTEKQAYWQVVEGALDAQLAL 733
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
209-726 |
4.49e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 4.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 209 MSKLVEAEMDGAAAAKQVMALKDTIGKlktekqmtCTDINTLTRQKELLLQKLSTFE-ETNRTLRDLLREQ--HCKEDSE 285
Cdd:COG4913 234 FDDLERAHEALEDAREQIELLEPIREL--------AERYAAARERLAELEYLRAALRlWFAQRRLELLEAEleELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 286 RLMEQQGTLLKRLAEADSEKAR-LLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRL 364
Cdd:COG4913 306 RLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 365 CMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQL------HVQLADKDL-YVAE 437
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALrdalaeALGLDEAELpFVGE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 438 AL---STLESWRS------------------RYNQVVK--DKGDLELEIivlndrVTDLVNQQQSLEEKMREDRDSLVER 494
Cdd:COG4913 466 LIevrPEEERWRGaiervlggfaltllvppeHYAAALRwvNRLHLRGRL------VYERVRTGLPDPERPRLDPDSLAGK 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 495 LHRQTAEYSAFkLENErLKASFAPM----EDKLNQAHLEVQQlkasvknyEGMI-DNYKSQVMKTRLEADEV-------A 562
Cdd:COG4913 540 LDFKPHPFRAW-LEAE-LGRRFDYVcvdsPEELRRHPRAITR--------AGQVkGNGTRHEKDDRRRIRSRyvlgfdnR 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 563 AQLERCDKENKMLKDEMN------KEIEAARRQFQSQLADLQQLPDI------LKITEAKLAECQDQLQGYERKNIDLTA 630
Cdd:COG4913 610 AKLAALEAELAELEEELAeaeerlEALEAELDALQERREALQRLAEYswdeidVASAEREIAELEAELERLDASSDDLAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 631 I---ISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATS--AQNVEFLQVIAKREEAI---HQAQLR- 701
Cdd:COG4913 690 LeeqLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEdlARLELRALLEERFAAALgdaVERELRe 769
|
570 580
....*....|....*....|....*.
gi 1907136589 702 -LEEKTRECGSLARQLESAIEDARRQ 726
Cdd:COG4913 770 nLEERIDALRARLNRAEEELERAMRA 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
468-803 |
9.58e-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: 59.30 E-value: 9.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 468 DRVTDLVN----QQQSLEEKMRedrdsLVERLHRQTAEYSAfkLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGM 543
Cdd:TIGR02168 189 DRLEDILNelerQLKSLERQAE-----KAERYKELKAELRE--LELALLVLRLEELREELEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 544 IDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNkEIEAARRQFQSQLADLQQlpdilkiteaKLAECQDQLQGYER 623
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEIS-RLEQQKQILRERLANLER----------QLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 624 KNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEAtsaqnveflqviAKREEAIHQAQLRLE 703
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET------------LRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 704 EKTREcgslarQLESAIEDARRQVEQTKEQALSKERAAQS-KILDLETQLSRTKTELGQLRRTRDDAdrryQSRLQDLKD 782
Cdd:TIGR02168 399 NNEIE------RLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERL----EEALEELRE 468
|
330 340
....*....|....*....|.
gi 1907136589 783 RLEQSESTNRSMQNYVQFLKA 803
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQA 489
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
222-808 |
1.05e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 222 AAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETnrtlrdLLREQHCKEDSERLMEQQGTLLKRLAEA 301
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEV------LEEHEERREELETLEAEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 302 DSEKARLLLLLQDKDKEVEELLQEIQ-------CEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERS 374
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDdllaeagLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 375 GNQHKAEVEAIMEQLKELkqkgDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVK 454
Cdd:PRK02224 351 ADDLEERAEELREEAAEL----ESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 455 DKGDLELEIIVLNDRVTDlvNQQ-----------QSLEEKMR----EDRDSLVERLhrqTAEYSAFKLENERLKASFAPM 519
Cdd:PRK02224 427 REAELEATLRTARERVEE--AEAlleagkcpecgQPVEGSPHvetiEEDRERVEEL---EAELEDLEEEVEEVEERLERA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 520 EDkLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQlercdkenkmlKDEMNKEIEAARRQFQSQLADLQQ 599
Cdd:PRK02224 502 ED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER-----------AAELEAEAEEKREAAAEAEEEAEE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 600 LPDILKITEAKLAECQDQLQGYERknidltaiISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDEL-ERKLEATS 678
Cdd:PRK02224 570 AREEVAELNSKLAELKERIESLER--------IRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKrERKRELEA 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 679 AQNveflqviakrEEAIHQAQLRLEektrecgslarQLESAIEDARRQVEQTKEqalsKERAAQSKILDLETQLSRtkte 758
Cdd:PRK02224 642 EFD----------EARIEEAREDKE-----------RAEEYLEQVEEKLDELRE----ERDDLQAEIGAVENELEE---- 692
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1907136589 759 lgqlrrtrddadrryqsrLQDLKDRLEQSESTnrsmqnyVQFLKASYANV 808
Cdd:PRK02224 693 ------------------LEELRERREALENR-------VEALEALYDEA 717
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
315-652 |
2.06e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 315 KDKEVEELLQEI--------QCEKAQAKTASELSkSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIM 386
Cdd:TIGR02168 675 RRREIEELEEKIeeleekiaELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 387 EQLKELKQKgdrdketlkkaIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIVL 466
Cdd:TIGR02168 754 KELTELEAE-----------IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 467 NDRVTDLVNQQQSLEEKMREdrdsLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDN 546
Cdd:TIGR02168 823 RERLESLERRIAATERRLED----LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 547 YKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKeIEAARRQFQSQLADLQQ--LPDILK---ITEAKLAECQDQLQGY 621
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSltLEEAEAlenKIEDDEEEARRRLKRL 977
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1907136589 622 ERK-----NIDLTAI--ISDLRSR---IEHQGDKLEMAREK 652
Cdd:TIGR02168 978 ENKikelgPVNLAAIeeYEELKERydfLTAQKEDLTEAKET 1018
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
287-799 |
2.10e-08 |
|
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: 58.13 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 287 LMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLR-CKEAENSRLC 365
Cdd:TIGR00606 417 LQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAEReLSKAEKNSLT 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 366 MQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEE-------YAEQLHVQLADKDlYVAEA 438
Cdd:TIGR00606 497 ETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQirkiksrHSDELTSLLGYFP-NKKQL 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 439 LSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMR------------EDRDSLVERLHRQ-------- 498
Cdd:TIGR00606 576 EDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSsyedklfdvcgsQDEESDLERLKEEieksskqr 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 499 ------TAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKN----YEGMIDNYKSQVMKTRLEADEVAAQLERC 568
Cdd:TIGR00606 656 amlagaTAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSklrlAPDKLKSTESELKKKEKRRDEMLGLAPGR 735
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 569 DKEnkmlKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTaIISDLRSRIEHQGDKLEM 648
Cdd:TIGR00606 736 QSI----IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVT-IMERFQMELKDVERKIAQ 810
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 649 AREKHQAS--QKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQ 726
Cdd:TIGR00606 811 QAAKLQGSdlDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQL 890
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907136589 727 VEQTKE-QALSKE-RAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQSESTNRSMQNYVQ 799
Cdd:TIGR00606 891 VELSTEvQSLIREiKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ 965
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
498-739 |
6.84e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 6.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 498 QTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLercdKENKMLKD 577
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL----AELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 578 EMNKEIEAARRQFQSQLADLQQLPdilKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQ 657
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLG---RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 658 KENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSK 737
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
..
gi 1907136589 738 ER 739
Cdd:COG4942 251 LK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
294-738 |
6.87e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 6.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 294 LLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLE- 372
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 373 -RSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQ 451
Cdd:COG4717 131 yQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 452 VVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPM------------ 519
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlflvlgllallf 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 520 ------EDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVM-KTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQS 592
Cdd:COG4717 291 lllareKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 593 QLADLQQLPDIlkITEAKLAECQDQLQGYErkniDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENK--QLSQKVDEL 670
Cdd:COG4717 371 EIAALLAEAGV--EDEEELRAALEQAEEYQ----ELKEELEELEEQLEELLGELEELLEALDEEELEEEleELEEELEEL 444
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136589 671 ERKLEATSAQNVEFLQVI--AKREEAIHQAQLRLEEKTRECGSLARQ------LESAIEDARRQVEQTKEQALSKE 738
Cdd:COG4717 445 EEELEELREELAELEAELeqLEEDGELAELLQELEELKAELRELAEEwaalklALELLEEAREEYREERLPPVLER 520
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
561-793 |
1.66e-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: 54.38 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 561 VAAQLERCDKENKMLKdEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIE 640
Cdd:COG4942 15 AAAQADAAAEAEAELE-QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 641 HQGDKLEmAREKHQASQKENKQLSQKVDELERKLEATSAQNV--------EFLQVIAKREEAIHQAQLRLEEKTRECGSL 712
Cdd:COG4942 94 ELRAELE-AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAvrrlqylkYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 713 ARQLESAIEDARRQveqtkEQALSKERAAQSKIL-DLETQLSRTKTELGQLRRTrddadrryQSRLQDLKDRLEQSESTN 791
Cdd:COG4942 173 RAELEALLAELEEE-----RAALEALKAERQKLLaRLEKELAELAAELAELQQE--------AEELEALIARLEAEAAAA 239
|
..
gi 1907136589 792 RS 793
Cdd:COG4942 240 AE 241
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
466-785 |
2.06e-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: 55.07 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 466 LNDRVTDLVNQQQSLEEKMRE---DRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEG 542
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRienRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 543 MIDNYKSQVMKTRLEADEVAAQLERC-DKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGY 621
Cdd:TIGR02169 759 ELKELEARIEELEEDLHKLEEALNDLeARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 622 ERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLR 701
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 702 LEEKTRECGSLARQLeSAIEDARRQVEQTKEQALSKERaAQSKILDLETQLSRtkteLGQLRRTRDDADRRYQSRLQDLK 781
Cdd:TIGR02169 919 LSELKAKLEALEEEL-SEIEDPKGEDEEIPEEELSLED-VQAELQRVEEEIRA----LEPVNMLAIQEYEEVLKRLDELK 992
|
....
gi 1907136589 782 DRLE 785
Cdd:TIGR02169 993 EKRA 996
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
370-784 |
2.82e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.57 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 370 NLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKA----IRAQkERAEKSEEYAEQLHVQLADkdlyVAEALSTLESW 445
Cdd:COG3096 337 NLVQTALRQQEKIERYQEDLEELTERLEEQEEVVEEAaeqlAEAE-ARLEAAEEEVDSLKSQLAD----YQQALDVQQTR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 446 RSRYNQVVKDKGDL-------ELEIIVLNDRVTDLVNQQQSLEEKMR--EDRDSLVERLHRQTAEysAFKLenerlkasf 516
Cdd:COG3096 412 AIQYQQAVQALEKAralcglpDLTPENAEDYLAAFRAKEQQATEEVLelEQKLSVADAARRQFEK--AYEL--------- 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 517 apmedklnqahleVQQLKASVknyegmidnyksqvmkTRLEADEVAAQLERCDKENKMLkdemnkeieAARR-QFQSQLA 595
Cdd:COG3096 481 -------------VCKIAGEV----------------ERSQAWQTARELLRRYRSQQAL---------AQRLqQLRAQLA 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 596 DLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELerkle 675
Cdd:COG3096 523 ELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKEL----- 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 676 atsaqnveflqviAKREEAIHQAQLRLEektrecgSLARQLESAIEDArRQVEQTKEQALSKERAAQSkildLETQLSRT 755
Cdd:COG3096 598 -------------AARAPAWLAAQDALE-------RLREQSGEALADS-QEVTAAMQQLLEREREATV----ERDELAAR 652
|
410 420
....*....|....*....|....*....
gi 1907136589 756 KTELGQLRRTRDDADRRYQSRLQDLKDRL 784
Cdd:COG3096 653 KQALESQIERLSQPGGAEDPRLLALAERL 681
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
377-676 |
3.29e-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: 54.30 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 377 QHKAEVEAIMEQLKELKQKGDRdKETLKKAIRAQKERAEKSEEYAEQLHVQLADK-DLYVAEALSTLESWRSRYNQVVKD 455
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIER-LDLIIDEKRQQLERLRREREKAERYQALLKEKrEYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 456 KGDLELEIIVLNDRVTDLVNQQQSLEEKMREdrdsLVERLHRQTA-EYSAFKLENERLKASFAPMEDKLNQAHLEVQQLK 534
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEE----LNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 535 ASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMN------------------------KEIEAARRQF 590
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEdlraeleevdkefaetrdelkdyrEKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 591 QSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMA--------------REKHQAS 656
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLaadlskyeqelydlKEEYDRV 481
|
330 340
....*....|....*....|
gi 1907136589 657 QKENKQLSQKVDELERKLEA 676
Cdd:TIGR02169 482 EKELSKLQRELAEAEAQARA 501
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
577-786 |
1.03e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 577 DEMNKEIEAARRQfQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTaiISDLRSRIEHQGDKLEMAREKHQAS 656
Cdd:COG4913 238 ERAHEALEDAREQ-IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR--LELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 657 QKENKQLSQKVDELERKLEATSAQNVEFLqviakrEEAIHQAQLRLEEKTRECGSLARQL----------ESAIEDARRQ 726
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQL------EREIERLERELEERERRRARLEALLaalglplpasAEEFAALRAE 388
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907136589 727 VEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRR---TRDDADRRYQSRLQDLKDRLEQ 786
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAeiaSLERRKSNIPARLLALRDALAE 451
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
264-799 |
1.53e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 264 FEETNRTLRDLLREQHCKEDSERLMEQQGTLLK---RLAEADSEKA-----RLLLLLQDKDKEVEELLQEIQCEKAQAKT 335
Cdd:COG4913 234 FDDLERAHEALEDAREQIELLEPIRELAERYAAareRLAELEYLRAalrlwFAQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 336 ASELSKSMESMRGHLQAQLRCKEAEN-SRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERA 414
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 415 EKSEEYAEQLHVQLADkdlyvaealstlesWRSRYNQVVKDKGDLELEIIVLNDRVT----DLVNQQQSLEEKMREDRDS 490
Cdd:COG4913 394 EALEEELEALEEALAE--------------AEAALRDLRRELRELEAEIASLERRKSnipaRLLALRDALAEALGLDEAE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 491 L-------------------VER-LHRQtaeysAFKL--ENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYK 548
Cdd:COG4913 460 LpfvgelievrpeeerwrgaIERvLGGF-----ALTLlvPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 549 SQVMKTRLEADEVAA-------------------QLERCDK---ENKMLKD-----EMNKEIEAARRQF-----QSQLAD 596
Cdd:COG4913 535 SLAGKLDFKPHPFRAwleaelgrrfdyvcvdspeELRRHPRaitRAGQVKGngtrhEKDDRRRIRSRYVlgfdnRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 597 LqqlpdilkitEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGdklemAREKHQASQKENKQLSQKVDELERKLEA 676
Cdd:COG4913 615 L----------EAELAELEEELAEAEERLEALEAELDALQERREALQ-----RLAEYSWDEIDVASAEREIAELEAELER 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 677 TSAQNVEfLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQAlskERAAQSKILDLETQLSRTK 756
Cdd:COG4913 680 LDASSDD-LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL---EAAEDLARLELRALLEERF 755
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1907136589 757 TELGQlRRTRDDADRRYQSRLQDLKDRLEQSEST-NRSMQNYVQ 799
Cdd:COG4913 756 AAALG-DAVERELRENLEERIDALRARLNRAEEElERAMRAFNR 798
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
123-728 |
1.61e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 123 RYDKKIDSLMNAVGCLKSEVKMQKGERQMAKRFLEERKEELEEVAHELAETEHEntvlrhnIERIKEEKDFTMLQKKHLQ 202
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE-------LARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 203 QEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMtctdintltrQKELLLQKLSTFEETNRTLRDLLREQhcke 282
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE----------AEAELAEAEEALLEAEAELAEAEEEL---- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 283 dsERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASElsksmesmrghLQAQLRCKEAENS 362
Cdd:COG1196 382 --EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE-----------EEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 363 RLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQ-LHVQLADKDLYVAEALST 441
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvKAALLLAGLRGLAGAVAV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 442 LESWRSRYNQVVkdkgdLELEIIVLNDRVTDLVNQQQSLEEKMREDRDSLVERlhrqtaeysafkLENERLKASFAPMED 521
Cdd:COG1196 529 LIGVEAAYEAAL-----EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATF------------LPLDKIRARAALAAA 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 522 KLNQAHLEVQQLKASVKNYEGMIDnykSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQQLP 601
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARY---YVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 602 DILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQN 681
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1907136589 682 VEFLQVIAKREEAIHQAQLRLEEktrecgsLARQLES-------AIEDARRQVE 728
Cdd:COG1196 749 EEEALEELPEPPDLEELERELER-------LEREIEAlgpvnllAIEEYEELEE 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
315-638 |
1.99e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 315 KDKEVEELLQEIQCEKAQAKtASELSKSMESMRghlqAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKEL-- 392
Cdd:TIGR02169 205 REREKAERYQALLKEKREYE-GYELLKEKEALE----RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnk 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 393 --KQKGDRDKETLKKAIR---AQKERAEKS----EEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEI 463
Cdd:TIGR02169 280 kiKDLGEEEQLRVKEKIGeleAEIASLERSiaekERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 464 IVLNDRVTDLVNQQQSLEEKMREDRDSLVERlhrqTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGM 543
Cdd:TIGR02169 360 AELKEELEDLRAELEEVDKEFAETRDELKDY----REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 544 IdnyksqvmkTRLEADevaaqlercdkenkmlKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYER 623
Cdd:TIGR02169 436 I---------NELEEE----------------KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
330
....*....|....*
gi 1907136589 624 KNIDLTAIISDLRSR 638
Cdd:TIGR02169 491 ELAEAEAQARASEER 505
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
185-795 |
3.35e-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: 50.89 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 185 ERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTF 264
Cdd:pfam15921 92 RRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 265 EETNRTLRdLLREQHCKEDSERLMEQQGTLLKRLAEADSekaRLLLLLQDKDKEVEELLQEIQCEkaqaktASELSKSME 344
Cdd:pfam15921 172 IEQLRKMM-LSHEGVLQEIRSILVDFEEASGKKIYEHDS---MSTMHFRSLGSAISKILRELDTE------ISYLKGRIF 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 345 SMRGHLQAqLRCKEAENSRLCMQIKN--LERSGNQHKAEVEAIMEQLKELKQKGDrdketlkkAIRAQKERAEKSEEYAE 422
Cdd:pfam15921 242 PVEDQLEA-LKSESQNKIELLLQQHQdrIEQLISEHEVEITGLTEKASSARSQAN--------SIQSQLEIIQEQARNQN 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 423 QLHV-QLADKDLYVAEALSTLESWRSRYNQVVKDkgdLELEIIVLNDRVTDLVNQQQSLEEK---MREDRDSLVERLHRQ 498
Cdd:pfam15921 313 SMYMrQLSDLESTVSQLRSELREAKRMYEDKIEE---LEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLHKR 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 499 TAEYSAFKLENERL-------KASFAPMEDKLNQAHLEVQQLKASVKnyegmidnyksqVMKTRLEAdEVAAQLERCDKE 571
Cdd:pfam15921 390 EKELSLEKEQNKRLwdrdtgnSITIDHLRRELDDRNMEVQRLEALLK------------AMKSECQG-QMERQMAAIQGK 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 572 NKMLK--DEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMA 649
Cdd:pfam15921 457 NESLEkvSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 650 R---EKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVI--------------AKREEAIHQAQLRLEE----KTRE 708
Cdd:pfam15921 537 KnegDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVgqhgrtagamqvekAQLEKEINDRRLELQEfkilKDKK 616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 709 CGSLaRQLESAIED-----------------ARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADR 771
Cdd:pfam15921 617 DAKI-RELEARVSDlelekvklvnagserlrAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTN 695
|
650 660
....*....|....*....|....
gi 1907136589 772 RYQSRLQDLKDRLEQSESTNRSMQ 795
Cdd:pfam15921 696 KLKMQLKSAQSELEQTRNTLKSME 719
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
220-778 |
4.57e-06 |
|
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: 50.35 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 220 AAAAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETNRTLRDLLREQhckEDSERLMEQQGTLLKRLA 299
Cdd:TIGR00618 296 AAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQE---IHIRDAHEVATSIREISC 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 300 EADSEKARLLLLLQDK--DKEVEELL-QEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQ---IKNLER 373
Cdd:TIGR00618 373 QQHTLTQHIHTLQQQKttLTQKLQSLcKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCaaaITCTAQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 374 SGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQ--------LHVQLADKDLYVAEALStlesw 445
Cdd:TIGR00618 453 CEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcplcgscIHPNPARQDIDNPGPLT----- 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 446 rSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDS---LVERLHRQTAEYSAFKLENERLKaSFAPMEDK 522
Cdd:TIGR00618 528 -RRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSfsiLTQCDNRSKEDIPNLQNITVRLQ-DLTEKLSE 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 523 L-------NQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRqfQSQLA 595
Cdd:TIGR00618 606 AedmlaceQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASR--QLALQ 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 596 DLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKE-NKQLSQKVDELERKL 674
Cdd:TIGR00618 684 KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKElMHQARTVLKARTEAH 763
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 675 EATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLArQLESAIEDARRQVEQTK----EQALSKERAAQSKILDLET 750
Cdd:TIGR00618 764 FNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLK-TLEAEIGQEIPSDEDILnlqcETLVQEEEQFLSRLEEKSA 842
|
570 580
....*....|....*....|....*...
gi 1907136589 751 QLSRTKTELGQLRRTRDDADRRYQSRLQ 778
Cdd:TIGR00618 843 TLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
174-729 |
6.00e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 174 EHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEmdgaaaaKQVMALK-DTIGKLKTEkqmtctdINTLTR 252
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELE-------AQIRGNGgDRLEQLERE-------IERLER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 253 QKELLLQKLSTFEETNRTL-------RDLLREQHckedsERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQE 325
Cdd:COG4913 353 ELEERERRRARLEALLAALglplpasAEEFAALR-----AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 326 IQcekAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLC--MQIKNLERS---------GNQ---------HKAEVEAI 385
Cdd:COG4913 428 IA---SLERRKSNIPARLLALRDALAEALGLDEAELPFVGelIEVRPEEERwrgaiervlGGFaltllvppeHYAAALRW 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 386 MEQLKeLKQK--GDRDKETLKKAIRAQKER---AEKSE----EYAEQLHVQLADKDLYV----AEALS------TLE--- 443
Cdd:COG4913 505 VNRLH-LRGRlvYERVRTGLPDPERPRLDPdslAGKLDfkphPFRAWLEAELGRRFDYVcvdsPEELRrhpraiTRAgqv 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 444 -SWRSRYnqvVKDKGDLELEIIVLN----DRVTDLVNQQQSLEEKMREdRDSLVERLHRQTAEYSAFKLENERLkASFAP 518
Cdd:COG4913 584 kGNGTRH---EKDDRRRIRSRYVLGfdnrAKLAALEAELAELEEELAE-AEERLEALEAELDALQERREALQRL-AEYSW 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 519 MEDKLNQAHLEVQQLKASVKNyegmIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEM---NKEIEAARRQFQSQLA 595
Cdd:COG4913 659 DEIDVASAEREIAELEAELER----LDASSDDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEELDELQD 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 596 DLQQLPDILKITEAKLAE------CQDQLQGYERKNidLTAIISDLRSRIEHQGDKLEMAREKHQASQKENkqlsqkVDE 669
Cdd:COG4913 735 RLEAAEDLARLELRALLEerfaaaLGDAVERELREN--LEERIDALRARLNRAEEELERAMRAFNREWPAE------TAD 806
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136589 670 LERKLEAtsaqNVEFLQVIAK-REEAIHQ-----AQLRLEEKTRECGSLARQLESAIEDARRQVEQ 729
Cdd:COG4913 807 LDADLES----LPEYLALLDRlEEDGLPEyeerfKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
544-807 |
6.60e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 6.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 544 IDNYKSQVMKTRLEADEVAAQLERCD-------KENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQD 616
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDliidekrQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 617 QLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQA-SQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAI 695
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 696 HQAQLRLEEKTREcgslARQLESAIEDARRQVEQTKE--QALSKERAA-QSKILDLETQLSRTKTELGQlrrtrddadrr 772
Cdd:TIGR02169 325 AKLEAEIDKLLAE----IEELEREIEEERKRRDKLTEeyAELKEELEDlRAELEEVDKEFAETRDELKD----------- 389
|
250 260 270
....*....|....*....|....*....|....*
gi 1907136589 773 YQSRLQDLKDRLEQSESTNRSMQNYVQFLKASYAN 807
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
295-730 |
1.02e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 295 LKRLAEADSEKARLLLLLQDKDKEVEEL---------LQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLC 365
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAkkkaeekkkADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 366 MQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDK--ETLKKAIRAQK-ERAEKSEEYAEQLHVQLADkDLYVAEALSTL 442
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkaDEAKKAEEAKKaDEAKKAEEAKKADEAKKAE-EKKKADELKKA 1554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 443 ESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQqqsLEEKMREDRDSLVERLHRQTAEySAFKLENERLKASfapmedk 522
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK---AEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIKAE------- 1623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 523 lnqahlEVQQLKASVKNYEGMIDNYKSQVMKtrleadevAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQqlpd 602
Cdd:PTZ00121 1624 ------ELKKAEEEKKKVEQLKKKEAEEKKK--------AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE---- 1685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 603 ilkitEAKLAECQDQLQGYERKNIDltaiisDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNV 682
Cdd:PTZ00121 1686 -----DEKKAAEALKKEAEEAKKAE------ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1907136589 683 EFLQVIAKREEAIHQAQLRLEEKTrecGSLARQLESAIEDARRQVEQT 730
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKE---AVIEEELDEEDEKRRMEVDKK 1799
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
514-743 |
1.29e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 514 ASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLK---DEMNKEIEAARRQF 590
Cdd:COG3883 9 PTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQaeiAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 591 QSQLADLQQLPDILKITEAKLAecQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDEL 670
Cdd:COG3883 89 GERARALYRSGGSVSYLDVLLG--SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907136589 671 ERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQS 743
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
574-759 |
1.71e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 574 MLKDEMNKEIEAARRQ-------FQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQgDKL 646
Cdd:COG4717 46 MLLERLEKEADELFKPqgrkpelNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 647 EMAREKHQASQKENKQLSQKVDELERkLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQ 726
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEE-LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190
....*....|....*....|....*....|...
gi 1907136589 727 VEQTKEQALSKERAAQSKILDLETQLSRTKTEL 759
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
447-678 |
1.99e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.09 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 447 SRYNQVVKDKgdleleIIVLNDRVTDLVNQQQSLEEKMREDRDsLVERLHRQTAEysafklENERLKASFAPMEDKLNQA 526
Cdd:PHA02562 166 SEMDKLNKDK------IRELNQQIQTLDMKIDHIQQQIKTYNK-NIEEQRKKNGE------NIARKQNKYDELVEEAKTI 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 527 HLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKD------------EMNKEIEAARrqfqSQL 594
Cdd:PHA02562 233 KAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqqisEGPDRITKIK----DKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 595 ADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLR---SRIEHQGDKLEMAREKHQASQKENK-QLSQKVDEL 670
Cdd:PHA02562 309 KELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKqslITLVDKAKKVKAAIEELQAEFVDNAeELAKLQDEL 388
|
....*...
gi 1907136589 671 ERKLEATS 678
Cdd:PHA02562 389 DKIVKTKS 396
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
350-739 |
2.20e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 350 LQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLH-VQL 428
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqLKS 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 429 ADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMRE---DRDSLVERLHRQTAEYSAF 505
Cdd:TIGR04523 296 EISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNsesENSEKQRELEEKQNEIEKL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 506 KLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDE---MNKE 582
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvKELI 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 583 IEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQ 662
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 663 LSQKVDELERKLEA-----TSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSK 737
Cdd:TIGR04523 536 KESKISDLEDELNKddfelKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSL 615
|
..
gi 1907136589 738 ER 739
Cdd:TIGR04523 616 EK 617
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
638-793 |
2.33e-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: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 638 RIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQnveflqvIAKREEAIHQAQLRLEEKTRECGSLARQLE 717
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE-------LEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136589 718 SAIEDaRRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQSESTNRS 793
Cdd:COG1196 306 RLEER-RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
387-759 |
3.96e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.36 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 387 EQLK-ELKQ----KGDRDKET---LKKAIRA---QKERAEKSEEY----------AEQLHVQLADKDLYVAEALSTLESw 445
Cdd:PRK10929 26 KQITqELEQakaaKTPAQAEIveaLQSALNWleeRKGSLERAKQYqqvidnfpklSAELRQQLNNERDEPRSVPPNMST- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 446 rsrynqvvkdkGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPmEDKLNQ 525
Cdd:PRK10929 105 -----------DALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTP-NTPLAQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 526 AHL-----EVQQLKASVKNYE--GMIDNYKSQVmkTRLEADEVAAQLERCDKENKMLKDEMNkeieaARRQFQSQLAdlq 598
Cdd:PRK10929 173 AQLtalqaESAALKALVDELElaQLSANNRQEL--ARLRSELAKKRSQQLDAYLQALRNQLN-----SQRQREAERA--- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 599 qlpdiLKITEaKLAECQDqlqgyerkniDLTAIISdlrsriehqgDKLEMAREkhqASQKENKQlSQKVDELERKLEATS 678
Cdd:PRK10929 243 -----LESTE-LLAEQSG----------DLPKSIV----------AQFKINRE---LSQALNQQ-AQRMDLIASQQRQAA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 679 AQNVEFLQVI-AKREEA-----------IHQAQL-RLEEKTRecgslARQLESAIEDAR----------------RQVEQ 729
Cdd:PRK10929 293 SQTLQVRQALnTLREQSqwlgvsnalgeALRAQVaRLPEMPK-----PQQLDTEMAQLRvqrlryedllnkqpqlRQIRQ 367
|
410 420 430
....*....|....*....|....*....|
gi 1907136589 730 TKEQALSkerAAQSKILDleTQLsRTKTEL 759
Cdd:PRK10929 368 ADGQPLT---AEQNRILD--AQL-RTQREL 391
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
582-747 |
7.87e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 582 EIEAARRQFQSQLADLQQLpdiLKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMARekhqaSQKENK 661
Cdd:COG1579 21 RLEHRLKELPAELAELEDE---LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-----NNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 662 QLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQveqtkEQALSKERAA 741
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE-----LEELEAEREE 167
|
....*.
gi 1907136589 742 QSKILD 747
Cdd:COG1579 168 LAAKIP 173
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
377-784 |
8.48e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 377 QHKAEVEAIMEQLKELKQKgdrdKETLKKAIRAQKERAEKSEEYAEQLHVQLADkdlyVAEALSTLESWRSRYNQVVK-- 454
Cdd:PRK04863 352 RYQADLEELEERLEEQNEV----VEEADEQQEENEARAEAAEEEVDELKSQLAD----YQQALDVQQTRAIQYQQAVQal 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 455 DK-----GDLELEIIVLNDRVTDLVNQQQSLEEKMR--EDRDSLVERLHRQTAEysAFKLenerlkasfapmedklnqah 527
Cdd:PRK04863 424 ERakqlcGLPDLTADNAEDWLEEFQAKEQEATEELLslEQKLSVAQAAHSQFEQ--AYQL-------------------- 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 528 leVQQLKASVknyegmidnyksqvmkTRLEADEVAAQLERCDKENKMLkdemnkeieAARR-QFQSQLADLQQLPDILKI 606
Cdd:PRK04863 482 --VRKIAGEV----------------SRSEAWDVARELLRRLREQRHL---------AEQLqQLRMRLSELEQRLRQQQR 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 607 TEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELErkleatsaqnveflq 686
Cdd:PRK04863 535 AERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLA--------------- 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 687 viaKREEAIHQAQLRLEEktrecgsLARQLESAIEDArRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTR 766
Cdd:PRK04863 600 ---ARAPAWLAAQDALAR-------LREQSGEEFEDS-QDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPG 668
|
410
....*....|....*...
gi 1907136589 767 DDADrryqSRLQDLKDRL 784
Cdd:PRK04863 669 GSED----PRLNALAERF 682
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
96-758 |
9.61e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 9.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 96 SSEKLV-SVMRLSDLSTEDDDSGHCK--MNRYDKKIDSLMNAVGCLKSEVKMQKGERQMAKRFLEERKEELEEVAHELAE 172
Cdd:PRK03918 146 SREKVVrQILGLDDYENAYKNLGEVIkeIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 173 TEHENTVLRHNIERIKEEKdftmLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTekqmtctdintlTR 252
Cdd:PRK03918 226 LEKEVKELEELKEEIEELE----KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE------------LK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 253 QKELLLQKLSTF-EETNRTLRDLlreqhcKEDSERLMEQQGTLLKRLAEADSEKARLLLLLqdkdKEVEELLQEIQCEKA 331
Cdd:PRK03918 290 EKAEEYIKLSEFyEEYLDELREI------EKRLSRLEEEINGIEERIKELEEKEERLEELK----KKLKELEKRLEELEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 332 QAKTASELSKSMESMRGhLQAQLRCKEAEnsRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQK 411
Cdd:PRK03918 360 RHELYEEAKAKKEELER-LKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 412 E----RAEKSEEYAEQLhvqLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIVLND--RVTDLVNQQQSLEEKMR 485
Cdd:PRK03918 437 KcpvcGRELTEEHRKEL---LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 486 EDRdslVERLHRQTAEYSAFKLENERLKASFAPMEDKLNqahlEVQQLKASVKNYEGMIDNYKSqvmktrlEADEVAAQL 565
Cdd:PRK03918 514 KYN---LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE----KLEELKKKLAELEKKLDELEE-------ELAELLKEL 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 566 ERCDKENKMLKDEMNKEIEAARRQFQSqladLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQG-- 643
Cdd:PRK03918 580 EELGFESVEELEERLKELEPFYNEYLE----LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEkk 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 644 ---DKLEMAREKHQASQKENKQLSQKVDELERKLEaTSAQNVEFLQviaKREEAIHQAQLRLEektrecgslarQLESAI 720
Cdd:PRK03918 656 yseEEYEELREEYLELSRELAGLRAELEELEKRRE-EIKKTLEKLK---EELEEREKAKKELE-----------KLEKAL 720
|
650 660 670
....*....|....*....|....*....|....*...
gi 1907136589 721 EDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTE 758
Cdd:PRK03918 721 ERVEELREKVKKYKALLKERALSKVGEIASEIFEELTE 758
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
558-757 |
1.12e-04 |
|
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: 45.53 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 558 ADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRS 637
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 638 RIEHQGDKL--------------------------------EMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFL 685
Cdd:COG4942 98 ELEAQKEELaellralyrlgrqpplalllspedfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907136589 686 QVIAKREEAihQAQLRLEEKTREcgSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKT 757
Cdd:COG4942 178 ALLAELEEE--RAALEALKAERQ--KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
508-762 |
1.56e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 45.06 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 508 ENERLKASFAPMEDKLNqahlEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENkmlkdemnkeiEAAR 587
Cdd:pfam19220 4 RNELLRVRLGEMADRLE----DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAY-----------GKLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 588 RQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKV 667
Cdd:pfam19220 69 RELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 668 DELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLAR---QLESAIEDARRQVEQTkEQALSKERAAQSK 744
Cdd:pfam19220 149 QAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRrlaELETQLDATRARLRAL-EGQLAAEQAERER 227
|
250
....*....|....*....
gi 1907136589 745 IL-DLETQLSRTKTELGQL 762
Cdd:pfam19220 228 AEaQLEEAVEAHRAERASL 246
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
580-801 |
1.89e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 580 NKEIEAARRQFQSQLADLQQlpdilkiteaKLAECQDQLQGYERKN--IDLTAIISDLRSRIEHQGDKLEMAREKHQASQ 657
Cdd:COG3206 170 REEARKALEFLEEQLPELRK----------ELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 658 kenkqlsQKVDELERKLEATSAQNVEFLQ--VIAKREEAIHQAQLRLEEKTRECG--------------SLARQLESAIE 721
Cdd:COG3206 240 -------ARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTpnhpdvialraqiaALRAQLQQEAQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 722 DARRQVEQTKEQALSKERAAQSKILDLETQ---LSRTKTELGQLRRTRDDADRRYQSrlqdLKDRLEQSESTNRSMQNYV 798
Cdd:COG3206 313 RILASLEAELEALQAREASLQAQLAQLEARlaeLPELEAELRRLEREVEVARELYES----LLQRLEEARLAEALTVGNV 388
|
...
gi 1907136589 799 QFL 801
Cdd:COG3206 389 RVI 391
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
282-744 |
1.93e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 282 EDSERLMEQQGTLLKRLAEaDSEKARLLLLLQDKdKEVEELLQEIQCEKAQAKTASELSKSMESMRGHlQAQLRCKEAEN 361
Cdd:PTZ00121 1143 EEARKAEDAKRVEIARKAE-DARKAEEARKAEDA-KKAEAARKAEEVRKAEELRKAEDARKAEAARKA-EEERKAEEARK 1219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 362 SRLCMQIKNLERSGNQHKAEVEAIMEQlKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKdlyVAEALST 441
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEAKKDAEEAKKAE-EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE---KKKADEA 1295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 442 LESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDSlvERLHRQTAEYSAFKLENERLKASFAPME- 520
Cdd:PTZ00121 1296 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA--AEAAKAEAEAAADEAEAAEEKAEAAEKKk 1373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 521 -------DKLNQAHLEVQQLKASVKNYEGmiDNYKSQVMKTRLEADEVAAQLERcDKENKMLKDEMNKEIEAARR--QFQ 591
Cdd:PTZ00121 1374 eeakkkaDAAKKKAEEKKKADEAKKKAEE--DKKKADELKKAAAAKKKADEAKK-KAEEKKKADEAKKKAEEAKKadEAK 1450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 592 SQLADLQQLPDILKITE--------AKLAECQDQLQGYERKNIDLTAIISDLRSRIE--HQGDKLEMAREKHQASQKENK 661
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEeakkadeaKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEakKKADEAKKAEEAKKADEAKKA 1530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 662 QLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAA 741
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
...
gi 1907136589 742 QSK 744
Cdd:PTZ00121 1611 EAK 1613
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
466-794 |
2.23e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.14 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 466 LNDRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAE----YSAFKLENERLKASF-------APMEDKLNQAHLEVQQLK 534
Cdd:pfam00038 9 LNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpsrlYSLYEKEIEDLRRQLdtltverARLQLELDNLRLAAEDFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 535 ASVKNYEGMIDNYKSQVMKTRLEADEvaAQLERCDKENKMlkDEMNKEIEAARRQFQSQLADLQqlpdilkiteAKLAEC 614
Cdd:pfam00038 89 QKYEDELNLRTSAENDLVGLRKDLDE--ATLARVDLEAKI--ESLKEELAFLKKNHEEEVRELQ----------AQVSDT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 615 QDQLQGYERKNIDLTAIISDLRSRIEHQgdkleMAREKHQASQkenkQLSQKVDELERkleaTSAQNVEFLQviAKREEa 694
Cdd:pfam00038 155 QVNVEMDAARKLDLTSALAEIRAQYEEI-----AAKNREEAEE----WYQSKLEELQQ----AAARNGDALR--SAKEE- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 695 IHQAQLRLEEKTRECGSLARQLESaIEDARRQVEQTKEQALSKeraAQSKILDLETQLSRTKTELGQLrrtrddaDRRYQ 774
Cdd:pfam00038 219 ITELRRTIQSLEIELQSLKKQKAS-LERQLAETEERYELQLAD---YQELISELEAELQETRQEMARQ-------LREYQ 287
|
330 340
....*....|....*....|
gi 1907136589 775 SrLQDLKDRLEQSESTNRSM 794
Cdd:pfam00038 288 E-LLNVKLALDIEIATYRKL 306
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
167-417 |
2.87e-04 |
|
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: 43.98 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 167 AHELAETEHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTD 246
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 247 INTLTRQKELLLQKLSTFEETNRtLRDLLREQHCKEDSERLMeqqgtLLKRLAEADSEKARlllllqdkdkEVEELLQEI 326
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPP-LALLLSPEDFLDAVRRLQ-----YLKYLAPARREQAE----------ELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 327 QcekaqaktasELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKA 406
Cdd:COG4942 163 A----------ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
250
....*....|.
gi 1907136589 407 IRAQKERAEKS 417
Cdd:COG4942 233 EAEAAAAAERT 243
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
299-797 |
2.97e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 299 AEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKS-MESMRGHLQAQLRCKEAENSRLCMQIKNLERSgnQ 377
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAeAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA--K 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 378 HKAEVEAIMEQLKELKQKGDRDKETLKKAiRAQKERAEKSEEYAEQlhVQLADKDLYVAEALSTLESWRSRYNQVVKDKg 457
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKAEEDKKKADELKKA-AAAKKKADEAKKKAEE--KKKADEAKKKAEEAKKADEAKKKAEEAKKAE- 1460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 458 dlELEIIVLNDRVTDlvNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASV 537
Cdd:PTZ00121 1461 --EAKKKAEEAKKAD--EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 538 KNYEGMIDNYKSQVMKTRLE---ADEV----AAQLERCDKENKMLKDEMNKEIEAARRQfqsQLADLQQLPDILKITEAK 610
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEElkkAEEKkkaeEAKKAEEDKNMALRKAEEAKKAEEARIE---EVMKLYEEEKKMKAEEAK 1613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 611 LAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLE----ATSAQNVEFLQ 686
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEeakkAEEDEKKAAEA 1693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 687 VIAKREEAIHQAQLRleEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLE-----TQLSRTKTELGQ 761
Cdd:PTZ00121 1694 LKKEAEEAKKAEELK--KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEekkkiAHLKKEEEKKAE 1771
|
490 500 510
....*....|....*....|....*....|....*.
gi 1907136589 762 LRRTRDDADRRYQSRLQDLKDRLEQSESTNRSMQNY 797
Cdd:PTZ00121 1772 EIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNF 1807
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
591-790 |
6.76e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 591 QSQLAD-LQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDE 669
Cdd:pfam07888 33 QNRLEEcLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 670 LERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTREcgslarqLESAIEDARRQVEQTKEQAlSKERAAQSKILDLE 749
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETE-------LERMKERAKKAGAQRKEEE-AERKQLQAKLQQTE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907136589 750 TQLSRTKTELGQLRRTRDDADRRYQsRLQDLKDRLEQSEST 790
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVL-QLQDTITTLTQKLTT 224
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
477-803 |
7.81e-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: 7.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 477 QQSLEE----KMREDRDSLVERLHRQTAEysafKLENERLKAsfapmedklnqahLEVQQLKASVKNYEGMIDNYKSQVM 552
Cdd:TIGR02169 173 EKALEEleevEENIERLDLIIDEKRQQLE----RLRREREKA-------------ERYQALLKEKREYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 553 KTRLEAdeVAAQLERCDKENKMLK---DEMNKEIEAARrqfqsqladlQQLPDILKITEAKLAECQDQLQgyeRKNIDLT 629
Cdd:TIGR02169 236 ERQKEA--IERQLASLEEELEKLTeeiSELEKRLEEIE----------QLLEELNKKIKDLGEEEQLRVK---EKIGELE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 630 AIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREE---------------- 693
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEeledlraeleevdkef 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 694 -----AIHQAQLRLEEKTRECGSL----------ARQLESAIEDARRQVEQTKEQALSKERAAQSKILDL---ETQLSRT 755
Cdd:TIGR02169 381 aetrdELKDYREKLEKLKREINELkreldrlqeeLQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIkkqEWKLEQL 460
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1907136589 756 KTELGQLRRTRDDADRRY---QSRLQDLKDRLEQSESTNRSMQNYVQFLKA 803
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYdrvEKELSKLQRELAEAEAQARASEERVRGGRA 511
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
313-504 |
1.14e-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: 42.06 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 313 QDKDKEVEELLQEIQcekAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKEL 392
Cdd:COG4942 19 ADAAAEAEAELEQLQ---QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 393 KQKGDRDKETLKKAIRAQKERAEKSE-------EYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIV 465
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907136589 466 LNDRVTDLVNQQQSLEEKMREdRDSLVERLHRQTAEYSA 504
Cdd:COG4942 176 LEALLAELEEERAALEALKAE-RQKLLARLEKELAELAA 213
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
493-762 |
1.39e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.25 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 493 ERLHRQTAEYSAFKLENERlkASFAPMEDKLNQAHLEVQQLKASVKNYEGMID-----NYKSQVMKTRLEADEVAAQLER 567
Cdd:COG5185 256 EKLVEQNTDLRLEKLGENA--ESSKRLNENANNLIKQFENTKEKIAEYTKSIDikkatESLEEQLAAAEAEQELEESKRE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 568 CDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKIT--EAKLAECQDQLqgyERKNIDLTAIISDLRSRIEhqgDK 645
Cdd:COG5185 334 TETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSksSEELDSFKDTI---ESTKESLDEIPQNQRGYAQ---EI 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 646 LEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKRE-EAIHQAQLRLEEKTREcgsLARQLESAIEDAR 724
Cdd:COG5185 408 LATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMrEADEESQSRLEEAYDE---INRSVRSKKEDLN 484
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907136589 725 RQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQL 762
Cdd:COG5185 485 EELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQV 522
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
597-788 |
1.59e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.17 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 597 LQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEA 676
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 677 TSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLesaiedarRQVEQTKEQALSKERAAQSKILDLETQLSRTK 756
Cdd:pfam00261 83 LENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKL--------VVVEGDLERAEERAELAESKIVELEEELKVVG 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1907136589 757 TELGQL---RRTRDDADRRYQSRLQDLKDRLEQSE 788
Cdd:pfam00261 155 NNLKSLeasEEKASEREDKYEEQIRFLTEKLKEAE 189
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
166-567 |
1.72e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 166 VAHELAETEHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCT 245
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 246 DINTLTRQKELLL-------QKLSTFEETNRTLRDLLREqhckedSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKE 318
Cdd:PRK02224 406 DLGNAEDFLEELReerdelrEREAELEATLRTARERVEE------AEALLEAGKCPECGQPVEGSPHVETIEEDRERVEE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 319 VEELLQEIQCEKAqaktasELSKSMESMRghlqaQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQkgdr 398
Cdd:PRK02224 480 LEAELEDLEEEVE------EVEERLERAE-----DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE---- 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 399 DKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDlyvaEALSTLESWRSRYNQVVkdkgDLELEIIVLNDRVTDLVNQQQ 478
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELN----SKLAELKERIESLERIR----TLLAAIADAEDEIERLREKRE 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 479 SLEEKMREDRDSLVERLHRQTAEYSAFKLEN-ERLKASFAPMEDKLNQAHLEVQQL---KASVKNYEGMIDNYKSQVMKT 554
Cdd:PRK02224 617 ALAELNDERRERLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELreeRDDLQAEIGAVENELEELEEL 696
|
410
....*....|...
gi 1907136589 555 RLEADEVAAQLER 567
Cdd:PRK02224 697 RERREALENRVEA 709
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
610-758 |
1.75e-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: 40.68 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 610 KLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQ-----NVEF 684
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrNNKE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907136589 685 LQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTE 758
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
163-802 |
1.93e-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: 41.88 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 163 LEEVAHELAETEHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMdgaaaAKQVMALKDTIGKLKTEKQM 242
Cdd:pfam02463 178 LIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL-----KLNEERIDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 243 TCTDINTLTRQKELLLQKLSTFEETNRTLRDLLREQHCKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEEL 322
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 323 LQEIQCEKAQAKTASELSKSM--ESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDK 400
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAeeEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLE 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 401 ETLKKAIRAQKERAEKSEEYAEQLHVQLAD--KDLYVAEALSTLESWRSRYNQVVKDKGDLELEIivlndrvtdlVNQQQ 478
Cdd:pfam02463 413 LARQLEDLLKEEKKEELEILEEEEESIELKqgKLTEEKEELEKQELKLLKDELELKKSEDLLKET----------QLVKL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 479 SLEEKMREDRDSLVERLHRQTAeysafklENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEA 558
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQKESK-------ARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSA 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 559 DEVAaqlerCDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTA----IISD 634
Cdd:pfam02463 556 TADE-----VEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAkvveGILK 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 635 LRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLAR 714
Cdd:pfam02463 631 DTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 715 QLESAIEDARRQVEQTKEQALSKeraAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQSESTNRSM 794
Cdd:pfam02463 711 ELKKLKLEAEELLADRVQEAQDK---INEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLK 787
|
....*...
gi 1907136589 795 QNYVQFLK 802
Cdd:pfam02463 788 VEEEKEEK 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
169-486 |
1.95e-03 |
|
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: 41.98 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 169 ELAETEHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTctDIN 248
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS--RIP 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 249 TLTRQKELLLQKLSTFEETNRTLRDLLREQHCKEDSERlmEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIqc 328
Cdd:TIGR02169 795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE--KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL-- 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 329 EKAQAKTaselsKSMESMRGHLqaqlrckEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIR 408
Cdd:TIGR02169 871 EELEAAL-----RDLESRLGDL-------KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED 938
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 409 AQKERAEKSEEYAEQLHVQLadKDLYVAEALSTLESWRSR----YNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKM 484
Cdd:TIGR02169 939 PKGEDEEIPEEELSLEDVQA--ELQRVEEEIRALEPVNMLaiqeYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
..
gi 1907136589 485 RE 486
Cdd:TIGR02169 1017 RE 1018
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
313-671 |
2.24e-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: 41.54 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 313 QDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLErsgnQHKAEVEAIMEQLKEL 392
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ----QEKELLEKEIERLKET 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 393 KQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLE-------SWRSRYNQVVKDKGDLELEIIV 465
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEqkqkelkSKEKELKKLNEEKKELEEKVKD 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 466 LNDRVTDLVNQQQSLEEKMREDRDSLVERlhRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMID 545
Cdd:TIGR04523 515 LTKKISSLKEKIEKLESEKKEKESKISDL--EDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 546 NYKSQVMKTRLEADEVAAQLERCDKENKMLKDEmNKEIEAARRQFQSQLADLQQL----PDILKITEAKLAECQDQLQGY 621
Cdd:TIGR04523 593 QKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE-NEKLSSIIKNIKSKKNKLKQEvkqiKETIKEIRNKWPEIIKKIKES 671
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907136589 622 ERKNIDLTAIISD------------LRSRIEHQgdKLEMAREKHQASQKENKQLSQKVDELE 671
Cdd:TIGR04523 672 KTKIDDIIELMKDwlkelslhykkyITRMIRIK--DLPKLEEKYKEIEKELKKLDEFSKELE 731
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
466-672 |
2.25e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 466 LNDRVTDLvNQQQSLEEKMREDRDSLVERLhrqTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGmid 545
Cdd:PRK09039 58 LNSQIAEL-ADLLSLERQGNQDLQDSVANL---RASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQ--- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 546 nyksqvmktrlEADEVAAQLERcdkenkmlkdeMNKEIEAARRqfqsQLADLQQLpdiLKITEAKLAECQDQlqgyerkn 625
Cdd:PRK09039 131 -----------VSARALAQVEL-----------LNQQIAALRR----QLAALEAA---LDASEKRDRESQAK-------- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907136589 626 idltaiISDLRSRIehqgdklemarekhqasqkeNKQLSQKVDELER 672
Cdd:PRK09039 174 ------IADLGRRL--------------------NVALAQRVQELNR 194
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
604-831 |
2.40e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 604 LKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEA------T 677
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralyR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 678 SAQNVEFLQVIAKRE---EAIHQAQL--RLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQL 752
Cdd:COG3883 98 SGGSVSYLDVLLGSEsfsDFLDRLSAlsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 753 SRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQ----SESTNRSMQNYVQFLKASYANVFGDAPYTSSYLTSSPIRSRS 828
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAaaaaAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
...
gi 1907136589 829 PPA 831
Cdd:COG3883 258 AAG 260
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
220-406 |
2.54e-03 |
|
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];
Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 41.21 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 220 AAAAKQVMALKDTIGKLKTEKQmtctdINTLTRQKELLLQKLSTFEETNRTLRDLLREQhckedsERLMEQQGTLL--KR 297
Cdd:COG4192 68 VAALPEFAAATNTTERSQLRNQ-----LNTQLADIEELLAELEQLTQDAGDLRAAVADL------RNLLQQLDSLLtqRI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 298 LAEADSEKA--RLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENsrlcmQIKNL--ER 373
Cdd:COG4192 137 ALRRRLQELleQINWLHQDFNSELTPLLQEASWQQTRLLDSVETTESLRNLQNELQLLLRLLAIEN-----QIVSLlrEV 211
|
170 180 190
....*....|....*....|....*....|...
gi 1907136589 374 SGNQHKAEVEAIMEQLKELKQKGDRDKETLKKA 406
Cdd:COG4192 212 AAARDQADVDNLFDRLQYLKDELDRNLQALKNY 244
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
520-759 |
3.01e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 520 EDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAArrqfqsqladlqq 599
Cdd:pfam01576 88 EERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKER------------- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 600 lpdilKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSA 679
Cdd:pfam01576 155 -----KLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 680 QNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLA---RQLESAIEDARRQVEQTKEQALSKERAAQskilDLETQLSRTK 756
Cdd:pfam01576 230 QIAELRAQLAKKEEELQAALARLEEETAQKNNALkkiRELEAQISELQEDLESERAARNKAEKQRR----DLGEELEALK 305
|
...
gi 1907136589 757 TEL 759
Cdd:pfam01576 306 TEL 308
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
120-419 |
3.82e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 120 KMNRYDKKIDSLMNAVGCLKSEVKMQKGERqmAKRFLEERKEELEEVAHEL--AETEHENTVLRHNIERIKEEKDFTMLQ 197
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEE--AKKADEAKKAEEAKKADEAkkAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 198 KKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTDintlTRQKELLLQKLSTFEETNRTLRDLLRE 277
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE----AKIKAEELKKAEEEKKKVEQLKKKEAE 1644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 278 QHCKEDSERLMEQQGTL----LKRLAEADSEKARLLLLLQDKDKEVEELLQEiqcEKAQAKTASELSKSMESMRGHLQaQ 353
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIkaaeEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK---EAEEAKKAEELKKKEAEEKKKAE-E 1720
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136589 354 LRCKEAENSrlcMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEE 419
Cdd:PTZ00121 1721 LKKAEEENK---IKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
194-476 |
4.25e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 194 TMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKT----EKQMTCTDINTLTRQKELLLQKLSTFEETNR 269
Cdd:COG5022 780 GFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKtikrEKKLRETEEVEFSLKAEVLIQKFGRSLKAKK 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 270 TLRDLLREQhCKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQC---EKAQAKTA--SELSKSME 344
Cdd:COG5022 860 RFSLLKKET-IYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSdliENLEFKTEliARLKKLLN 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 345 SMRGHLQAQL-RCKEAENSRLCMQIKNLERSGNQHKAEV---EAIMEQLKELKQKGDRDKETLKKaIRAQKERAEKSEEY 420
Cdd:COG5022 939 NIDLEEGPSIeYVKLPELNKLHEVESKLKETSEEYEDLLkksTILVREGNKANSELKNFKKELAE-LSKQYGALQESTKQ 1017
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136589 421 AEQLHVQLADKDlYVAEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQ 476
Cdd:COG5022 1018 LKELPVEVAELQ-SASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLR 1072
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
408-805 |
5.05e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.71 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 408 RAQKERAEKSEEYAEQLHVQLADKDLYVAEaLSTLESWRSRY---NQVVKDKGDLELEIIVLNDRVTDL---VNQQQSLE 481
Cdd:COG3096 781 AAREKRLEELRAERDELAEQYAKASFDVQK-LQRLHQAFSQFvggHLAVAFAPDPEAELAALRQRRSELereLAQHRAQE 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 482 EKMREDRDSLVER---LHRQTAEYSAFKLE--NERLKASFAPMeDKLNQAHLEVQQLKASVKNYEGMIDNYKSqvmkTRL 556
Cdd:COG3096 860 QQLRQQLDQLKEQlqlLNKLLPQANLLADEtlADRLEELREEL-DAAQEAQAFIQQHGKALAQLEPLVAVLQS----DPE 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 557 EADEVAAQLERCDKENKMLKdemnKEIEA-----ARR---------QFQSQLADL-QQLPDILKITEAKLAECQDQLQGY 621
Cdd:COG3096 935 QFEQLQADYLQAKEQQRRLK----QQIFAlsevvQRRphfsyedavGLLGENSDLnEKLRARLEQAEEARREAREQLRQA 1010
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 622 ERKNIDLTAIISDLRSRiehqgdkLEMAREKHQASQKENKQLS------------QKVDELERKLEATSAQNVEFLQVIA 689
Cdd:COG3096 1011 QAQYSQYNQVLASLKSS-------RDAKQQTLQELEQELEELGvqadaeaeerarIRRDELHEELSQNRSRRSQLEKQLT 1083
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 690 KREEAIHQAQLRLeektrecgslaRQLESAIEDARRQVEQTKE-----QALSKERaaqskilDLETQLSRTK------TE 758
Cdd:COG3096 1084 RCEAEMDSLQKRL-----------RKAERDYKQEREQVVQAKAgwcavLRLARDN-------DVERRLHRRElaylsaDE 1145
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1907136589 759 LGQLRRTRDDADRRYQSRLQDLKDRLEQSEStNRSMQNYVQFLKASY 805
Cdd:COG3096 1146 LRSMSDKALGALRLAVADNEHLRDALRLSED-PRRPERKVQFYIAVY 1191
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
180-805 |
5.45e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 180 LRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDgaaaakqVMALKDTIGKLKTEKQMTCTDINTLTRQ------ 253
Cdd:pfam01576 101 MQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEED-------ILLLEDQNSKLSKERKLLEERISEFTSNlaeeee 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 254 KELLLQKLSTFEETNRT-LRDLLRE-----QHCKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQ 327
Cdd:pfam01576 174 KAKSLSKLKNKHEAMISdLEERLKKeekgrQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 328 CEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQL---KELKQKGDRDKETLK 404
Cdd:pfam01576 254 EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTaaqQELRSKREQEVTELK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 405 KAIRAQKERAEKSEEYAEQLHVQladkdlyvaealsTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKm 484
Cdd:pfam01576 334 KALEEETRSHEAQLQEMRQKHTQ-------------ALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQA- 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 485 REDRDSLVERLHRQTAEYSAFKLENERLKASFApmeDKLNQAHLEVQQLKASVKNYEGM-------IDNYKSQVMKTR-L 556
Cdd:pfam01576 400 KQDSEHKRKKLEGQLQELQARLSESERQRAELA---EKLSKLQSELESVSSLLNEAEGKniklskdVSSLESQLQDTQeL 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 557 EADEVAAQLE-----RCDKENKMLKDEMNKEIEAARRQFQSQLADLQ-QLPDILKITEAKLAECQDQLQGYERKNIDLTA 630
Cdd:pfam01576 477 LQEETRQKLNlstrlRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQaQLSDMKKKLEEDAGTLEALEEGKKRLQRELEA 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 631 IISDLRSRIEhQGDKLEMAREKHQASQK----ENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKT 706
Cdd:pfam01576 557 LTQQLEEKAA-AYDKLEKTKNRLQQELDdllvDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKE 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 707 RECGSLARQLESAIEdARRQVEQTKEQAlskeRAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQ 786
Cdd:pfam01576 636 TRALSLARALEEALE-AKEELERTNKQL----RAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQA 710
|
650
....*....|....*....
gi 1907136589 787 SESTNRSMQNYVQFLKASY 805
Cdd:pfam01576 711 TEDAKLRLEVNMQALKAQF 729
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
176-628 |
6.65e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 40.20 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 176 ENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAE---MDGAAAAKQVMALKDTIgkLKTEKQMTcTDINTLTR 252
Cdd:PTZ00440 729 KYNDLKSSIEEYKEEEEKLEVYKHQIINRKNEFILHLYENDkdlPDGKNTYEEFLQYKDTI--LNKENKIS-NDINILKE 805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 253 QKELLLQKLSTFEETNRTLRDLLREQHckEDSERLMEQQGTLLKRLAEADSEKarlllLLQDKDKEVEELLQEIQCEKAQ 332
Cdd:PTZ00440 806 NKKNNQDLLNSYNILIQKLEAHTEKND--EELKQLLQKFPTEDENLNLKELEK-----EFNENNQIVDNIIKDIENMNKN 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 333 AKTASELSKSMESMRGHLQAqlrckeaensrlcmqIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKE 412
Cdd:PTZ00440 879 INIIKTLNIAINRSNSNKQL---------------VEHLLNNKIDLKNKLEQHMKIINTDNIIQKNEKLNLLNNLNKEKE 943
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 413 RAEK--SEEYAEQLHVQLADKDLYVAEALSTLESW-RSRYNQVVKDKGD----------LELEIIVLNDRVTDLVNQQQs 479
Cdd:PTZ00440 944 KIEKqlSDTKINNLKMQIEKTLEYYDKSKENINGNdGTHLEKLDKEKDEwehfkseidkLNVNYNILNKKIDDLIKKQH- 1022
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 480 leEKMREDRDSLVERLHRQTAEYSAFKLEN-ERLKASFAPME-------DKLNQAHLEVQQLKASVKNYEGMIDNYKSQV 551
Cdd:PTZ00440 1023 --DDIIELIDKLIKEKGKEIEEKVDQYISLlEKMKTKLSSFHfnidikkYKNPKIKEEIKLLEEKVEALLKKIDENKNKL 1100
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907136589 552 MKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDIL-KITEAKLAECQdqlqgYERKNIDL 628
Cdd:PTZ00440 1101 IEIKNKSHEHVVNADKEKNKQTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDiTLNEVNEIEIE-----YERILIDH 1173
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
436-757 |
6.80e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.06 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 436 AEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRD--SLVERLHRQTAEYSAfKLENERLK 513
Cdd:pfam05622 127 SDKVKKLEATVETYKKKLEDLGDLRRQVKLLEERNAEYMQRTLQLEEELKKANAlrGQLETYKRQVQELHG-KLSEESKK 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 514 ASFAPMEDKLNQAHLE---------------------------VQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLE 566
Cdd:pfam05622 206 ADKLEFEYKKLEEKLEalqkekerliierdtlretneelrcaqLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 567 RCDKENKMLKdemnkeiEAARRQFQSQLADLQQLpdiLKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGD-- 644
Cdd:pfam05622 286 RLQHENKMLR-------LGQEGSYRERLTELQQL---LEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSka 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 645 --------KLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAqlrLEEKTRECGSLARQL 716
Cdd:pfam05622 356 edssllkqKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEALRKKDEDMKA---MEERYKKYVEKAKSV 432
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1907136589 717 ESAIEDARRQVEQTKEQALSKERAAQSK-ILDLETQLSRTKT 757
Cdd:pfam05622 433 IKTLDPKQNPASPPEIQALKNQLLEKDKkIEHLERDFEKSKL 474
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
368-732 |
8.50e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.45 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 368 IKNLERSGNQHKAEVEAIMEQLKElkqkgdrdketLKKAIRAQKERAEKSEEYAEqlhvqladkdlyvaEALSTLESWRS 447
Cdd:pfam06160 109 LDELLESEEKNREEVEELKDKYRE-----------LRKTLLANRFSYGPAIDELE--------------KQLAEIEEEFS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 448 RYNQVVKDkGD-LELEIIVLNdrvtdLVNQQQSLEEKMrEDRDSLVERLHrqtaeySAFKLENERLKASFAPMEDKlnQA 526
Cdd:pfam06160 164 QFEELTES-GDyLEAREVLEK-----LEEETDALEELM-EDIPPLYEELK------TELPDQLEELKEGYREMEEE--GY 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 527 HLEVQQLKASVKNYEGMIDNYKSQVmkTRLEADEVAAQLERCDKENKMLKDEMNKEIEaARRQFQSQLA----DLQQLPD 602
Cdd:pfam06160 229 ALEHLNVDKEIQQLEEQLEENLALL--ENLELDEAEEALEEIEERIDQLYDLLEKEVD-AKKYVEKNLPeiedYLEHAEE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 603 ILKITEAKLAECQD-----------------QLQGYERKNIDLTAII-------SDLRSRIEHQGDKLEMAREKH----- 653
Cdd:pfam06160 306 QNKELKEELERVQQsytlnenelervrglekQLEELEKRYDEIVERLeekevaySELQEELEEILEQLEEIEEEQeefke 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136589 654 --QASQKENKQLSQKVDELERKLEAT----SAQNV-----EFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIED 722
Cdd:pfam06160 386 slQSLRKDELEAREKLDEFKLELREIkrlvEKSNLpglpeSYLDYFFDVSDEIEDLADELNEVPLNMDEVNRLLDEAQDD 465
|
410
....*....|
gi 1907136589 723 ARRQVEQTKE 732
Cdd:pfam06160 466 VDTLYEKTEE 475
|
|
| |
