|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
100-764 |
7.08e-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: 85.49 E-value: 7.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 100 KMNRYDKKIDSLMNAVGCLKSEVKMQKGERQMAKRFLEERKEELEEVAHELAETEHENTVLRHNIERIKEEKDFTMLQKK 179
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 180 HLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETNRTLRDLLREQH 259
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 260 CKEDSERLmeqqGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQ-AQLRCKE 338
Cdd:TIGR02168 435 LKELQAEL----EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgFSEGVKA 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 339 AENSRLCM-----QIKNLERSGNQHKAEVEA---------IMEQLKELKQKGDRDKETLK--------KAIRAQKERAEK 396
Cdd:TIGR02168 511 LLKNQSGLsgilgVLSELISVDEGYEAAIEAalggrlqavVVENLNAAKKAIAFLKQNELgrvtflplDSIKGTEIQGND 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 397 SEEYAEQLHVQLADKDL--YVAEALSTLESWRSRYnqVVKDKGDLELEIIVLNDR----VT---DLVNQQQSLEEKMRED 467
Cdd:TIGR02168 591 REILKNIEGFLGVAKDLvkFDPKLRKALSYLLGGV--LVVDDLDNALELAKKLRPgyriVTldgDLVRPGGVITGGSAKT 668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 468 RDSLVERlhrqtaeysafKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDnyksqvmktrlEADEVAAQLER 547
Cdd:TIGR02168 669 NSSILER-----------RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE-----------QLRKELEELSR 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 548 CDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLE 627
Cdd:TIGR02168 727 QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 628 MAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAiEDARRQV 707
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL-LNERASL 885
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 708 EQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQS---RLQDLKDRL 764
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGlevRIDNLQERL 945
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
208-766 |
1.42e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 208 ALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETNRTLRDLLREQhcKEDSERLMEQQGTLLKRLAEADSEKAR 287
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL--LAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 288 LllllqdkDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIME 367
Cdd:COG1196 321 L-------EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 368 QLKELKQKgdrdKETLKKAIRAQKERAEKSEEYAEQLHVQLadkdlyvAEALSTLESWRSRYNQVVKDKGDLELEIIVLN 447
Cdd:COG1196 394 AAAELAAQ----LEELEEAEEALLERLERLEEELEELEEAL-------AELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 448 DRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAP-MEDKLNQAHLEVQQLKASVKNYEGMIDN 526
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAlLLAGLRGLAGAVAVLIGVEAAYEAALEA 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 527 YKSQVMKTRL-EADEVAAQLERCDKENKMLKDE---MNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYE 602
Cdd:COG1196 543 ALAAALQNIVvEDDEVAAAAIEYLKAAKAGRATflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 603 RKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRL 682
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 683 EEktrecgslARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKD 762
Cdd:COG1196 703 EE--------EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
....
gi 1039759465 763 RLEQ 766
Cdd:COG1196 775 EIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
350-723 |
4.54e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 350 NLERsgnqhkaeVEAIMEQLkelkqkgDRDKETLKKairaQKERAEKSEEYAEQLhvQLADKDLYVAealstleswrsRY 429
Cdd:COG1196 187 NLER--------LEDILGEL-------ERQLEPLER----QAEKAERYRELKEEL--KELEAELLLL-----------KL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 430 NQVVKDKGDLELEIIVLNDRVTDLVNQQQSLE---EKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQA 506
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEaelEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 507 HLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLErcdkenkmlkdemnkEIEAARRQFQSQLADLqqlpdilki 586
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELE---------------EAEAELAEAEEALLEA--------- 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 587 tEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQ 666
Cdd:COG1196 371 -EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039759465 667 VIAKREEAIHQAQLRLEEKTREcgslARQLESAIEDARRQVEQTKEQALSKERAAQS 723
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEE----AALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
446-769 |
1.90e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 446 LNDRVTDLVNQQQSLEEKMR--EDRDSLVERLHRQTAEYSAFKLEneRLKASFAPMEDKLNQAHLEVQQLKASVKNYEGM 523
Cdd:COG1196 191 LEDILGELERQLEPLERQAEkaERYRELKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 524 IDNYKSQVMKTRLEADEVAAQLERCDKEnkmlKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYER 603
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAE----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 604 KNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQnvefLQVIAKREEAIHQAQLRLE 683
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ----LEELEEAEEALLERLERLE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 684 EKTRECGSLARQLESAIEDARRQVEQTKE---QALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDL 760
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEeeaELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
....*....
gi 1039759465 761 KDRLEQSES 769
Cdd:COG1196 501 ADYEGFLEG 509
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
233-788 |
5.10e-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: 66.62 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 233 QKELLLQKLSTFEETNRTLRDLLREQhcKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQcekaq 312
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEA--EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS----- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 313 aktaselskSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKE 392
Cdd:TIGR02168 299 ---------RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 393 RAEKSEEYAEQLHvQLADKdlyVAEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLE-EKMREDRDSL 471
Cdd:TIGR02168 370 LESRLEELEEQLE-TLRSK---VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEEL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 472 VERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKS------QVMKTRLEAD------ 539
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegvkALLKNQSGLSgilgvl 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 540 ----EVAAQLERC---------------DKENKMLKDEMNKEIEAARRQF------------QSQLADLQQLPDILKITe 588
Cdd:TIGR02168 526 seliSVDEGYEAAieaalggrlqavvveNLNAAKKAIAFLKQNELGRVTFlpldsikgteiqGNDREILKNIEGFLGVA- 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 589 AKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQ-------------GDKL----------EMAREKHQASQKENKQLSQ 645
Cdd:TIGR02168 605 KDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAkklrpgyrivtldGDLVrpggvitggsAKTNSSILERRREIEELEE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 646 KVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESA------IEDARRQVEQTKEQALSKER 719
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeveqLEERIAQLSKELTELEAEIE 764
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039759465 720 AAQSKILDLETQLSRTKTELGQLrrtrddadrryQSRLQDLKDRLEQSESTNRSMQNYVQFLKASYANV 788
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEEL-----------EAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
233-684 |
1.10e-10 |
|
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: 65.52 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 233 QKELLLQKLSTFEETNRTLRDLLRE-QHCKEDSERLMEQQGTLLK-RLAEADSEKARLLLLLQDKDKEVEELL------- 303
Cdd:pfam15921 311 QNSMYMRQLSDLESTVSQLRSELREaKRMYEDKIEELEKQLVLANsELTEARTERDQFSQESGNLDDQLQKLLadlhkre 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 304 QEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERS-GNQHKAEVEAI------MEQLKELKQKG 376
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIqgknesLEKVSSLTAQL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 377 DRDKETLKKAIR---AQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYN------QVVKDKGD------LEL 441
Cdd:pfam15921 471 ESTKEMLRKVVEeltAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDlklqelQHLKNEGDhlrnvqTEC 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 442 EIIVLN---------------DRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQA 506
Cdd:pfam15921 551 EALKLQmaekdkvieilrqqiENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 507 HLEVQQLK-------ASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQQ 579
Cdd:pfam15921 631 ELEKVKLVnagserlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 580 LPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKV-------DELER 652
Cdd:pfam15921 711 TRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELstvatekNKMAG 790
|
490 500 510
....*....|....*....|....*....|..
gi 1039759465 653 KLEATSAQNVEFLQVIAKREEAIHQAQLRLEE 684
Cdd:pfam15921 791 ELEVLRSQERRLKEKVANMEVALDKASLQFAE 822
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
339-709 |
2.57e-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: 64.31 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 339 AENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEA 418
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 419 LSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMredrDSLVERLHRQTAEYSAFKLENERLKASFAP 498
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL----DELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 499 MEDKLNQAHLEVQQLKASVKNYEGMIDNYksqvmktRLEADEVAAQLERCDKEnkmlKDEMNKEIEAARRQFQSQLADLQ 578
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEEL-------EELIEELESELEALLNE----RASLEEALALLRSELEELSEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 579 QLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRI-EHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEAT 657
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1039759465 658 SAQNVEFLQVIAKREEaihqaqlRLEEKTRECGSLAR---QLESAIEDARRQVEQ 709
Cdd:TIGR02168 985 GPVNLAAIEEYEELKE-------RYDFLTAQKEDLTEakeTLEEAIEEIDREARE 1032
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
534-772 |
7.86e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 7.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 534 TRLEA--DEVAAQLERCDKE------NKMLKDEMN-KEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERK 604
Cdd:COG1196 189 ERLEDilGELERQLEPLERQaekaerYRELKEELKeLEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 605 NIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEE 684
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 685 KTRECGSLARQLESAiEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRL 764
Cdd:COG1196 349 AEEELEEAEAELAEA-EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
....*...
gi 1039759465 765 EQSESTNR 772
Cdd:COG1196 428 EALAELEE 435
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
179-519 |
1.58e-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: 61.61 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 179 KHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQmtctdinTLTRQKELLLQKLSTFEETNRTLRDLLREQ 258
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-------ELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 259 HckEDSERLMEQQGTLLKRLAEADSEKArlllllqdkdkeveELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKE 338
Cdd:TIGR02168 753 S--KELTELEAEIEELEERLEEAEEELA--------------EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 339 AENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQkgdrDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEA 418
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSE----DIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 419 LSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKmredRDSLVERLhrqTAEYSafkLENERLKASFAP 498
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR----IDNLQERL---SEEYS---LTLEEAEALENK 962
|
330 340
....*....|....*....|.
gi 1039759465 499 MEDKLNQAHLEVQQLKASVKN 519
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
154-791 |
2.05e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.24 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 154 EHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTC-TDINTLTR 232
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVkEKIGELEA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 233 QKELLLQKLstfEETNRTLRDLL-REQHCKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKA 311
Cdd:TIGR02169 302 EIASLERSI---AEKERELEDAEeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 312 QAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELkqkgDRDKETLKKAIRAQK 391
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL----EEEKEDKALEIKKQE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 392 ERAEKSEEYAEQLHVQLADKdlyvaealstleswRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQ---SLEEKMREDR 468
Cdd:TIGR02169 455 WKLEQLAADLSKYEQELYDL--------------KEEYDRVEKELSKLQRELAEAEAQARASEERVRggrAVEEVLKASI 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 469 DS---LVERLHRQTAEYsAFKLE---NERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEV- 541
Cdd:TIGR02169 521 QGvhgTVAQLGSVGERY-ATAIEvaaGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVi 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 542 --AAQLERCDKENK-----MLKDEMNKE-IEAARRQF---------------------------------QSQLADLQQL 580
Cdd:TIGR02169 600 gfAVDLVEFDPKYEpafkyVFGDTLVVEdIEAARRLMgkyrmvtlegelfeksgamtggsraprggilfsRSEPAELQRL 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 581 PDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQ 660
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 661 NVEFLQVIAKREEAIHQAQLRLEE-KTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLEtQLSRTKTEL 739
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE-YLEKEIQEL 838
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1039759465 740 GQLRRTRDDADRRYQSRLQDLKDRLEQSESTNRSMQNYVQFLKASYANVFGD 791
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
267-766 |
3.88e-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: 60.62 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 267 LMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTA-----SELSKSMESMRGHLQAQLRCKEAEN 341
Cdd:pfam12128 267 YKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAvakdrSELEALEDQHGAFLDADIETAAADQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 342 SRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADkdlyvaeALST 421
Cdd:pfam12128 347 EQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAED-------DLQA 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 422 LES-WRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKM--REDRDSLVER----LHRQTAEYSAFKLENERLKA 494
Cdd:pfam12128 420 LESeLREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLlqLENFDERIERareeQEAANAEVERLQSELRQARK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 495 SFAPMEDKLNQAHLEVQQLKASVKNYEGMID----------NYKSQVMKTRLEADEVAAQLERCDkenkmLKDEMNKEIE 564
Cdd:pfam12128 500 RRDQASEALRQASRRLEERQSALDELELQLFpqagtllhflRKEAPDWEQSIGKVISPELLHRTD-----LDPEVWDGSV 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 565 AARRQFQSQLADLQQL--PDILKITEAklaecqdqlqgyerknidltaiisdLRSRIEHQGDKLEMAREKHQASQKENKQ 642
Cdd:pfam12128 575 GGELNLYGVKLDLKRIdvPEWAASEEE-------------------------LRERLDKAEEALQSAREKQAAAEEQLVQ 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 643 LSQKVDELERKLEatsaqnveflqvIAKReeAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQAlskerAAQ 722
Cdd:pfam12128 630 ANGELEKASREET------------FART--ALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSL-----EAQ 690
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1039759465 723 SKILDLETQLSRTKTElGQLRRTRDDADRRYQSRLQDLKDRLEQ 766
Cdd:pfam12128 691 LKQLDKKHQAWLEEQK-EQKREARTEKQAYWQVVEGALDAQLAL 733
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
189-706 |
6.37e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 6.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 189 MSKLVEAEMDGAAAAKQVMALKDTIGKlktekqmtCTDINTLTRQKELLLQKLSTFE-ETNRTLRDLLREQ--HCKEDSE 265
Cdd:COG4913 234 FDDLERAHEALEDAREQIELLEPIREL--------AERYAAARERLAELEYLRAALRlWFAQRRLELLEAEleELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 266 RLMEQQGTLLKRLAEADSEKAR-LLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRL 344
Cdd:COG4913 306 RLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 345 CMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQL------HVQLADKDL-YVAE 417
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALrdalaeALGLDEAELpFVGE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 418 AL---STLESWRS------------------RYNQVVK--DKGDLELEIivlndrVTDLVNQQQSLEEKMREDRDSLVER 474
Cdd:COG4913 466 LIevrPEEERWRGaiervlggfaltllvppeHYAAALRwvNRLHLRGRL------VYERVRTGLPDPERPRLDPDSLAGK 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 475 LHRQTAEYSAFkLENErLKASFAPM----EDKLNQAHLEVQQlkasvknyEGMI-DNYKSQVMKTRLEADEV-------A 542
Cdd:COG4913 540 LDFKPHPFRAW-LEAE-LGRRFDYVcvdsPEELRRHPRAITR--------AGQVkGNGTRHEKDDRRRIRSRyvlgfdnR 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 543 AQLERCDKENKMLKDEMN------KEIEAARRQFQSQLADLQQLPDI------LKITEAKLAECQDQLQGYERKNIDLTA 610
Cdd:COG4913 610 AKLAALEAELAELEEELAeaeerlEALEAELDALQERREALQRLAEYswdeidVASAEREIAELEAELERLDASSDDLAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 611 I---ISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATS--AQNVEFLQVIAKREEAI---HQAQLR- 681
Cdd:COG4913 690 LeeqLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEdlARLELRALLEERFAAALgdaVERELRe 769
|
570 580
....*....|....*....|....*.
gi 1039759465 682 -LEEKTRECGSLARQLESAIEDARRQ 706
Cdd:COG4913 770 nLEERIDALRARLNRAEEELERAMRA 795
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
149-655 |
8.90e-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: 59.26 E-value: 8.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 149 ELAETEHENTVLRHNIERIKEE---KDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCT 225
Cdd:TIGR04523 174 ELNLLEKEKLNIQKNIDKIKNKllkLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQT 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 226 DINTLTRQ----KELLLQKLSTFEETNRTLRDLlreqhckedserlMEQQGTLLKRLAEADSEKArlllllQDKDKEVEE 301
Cdd:TIGR04523 254 QLNQLKDEqnkiKKQLSEKQKELEQNNKKIKEL-------------EKQLNQLKSEISDLNNQKE------QDWNKELKS 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 302 LLQEIQCEKAQAKTasELSKSMESMrghlqaqlrckeaenSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKgdrdKE 381
Cdd:TIGR04523 315 ELKNQEKKLEEIQN--QISQNNKII---------------SQLNEQISQLKKELTNSESENSEKQRELEEKQNE----IE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 382 TLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLE 461
Cdd:TIGR04523 374 KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 462 ---EKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEA 538
Cdd:TIGR04523 454 liiKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEK 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 539 DEVAAQLErcDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKnidltaiISDLRSR 618
Cdd:TIGR04523 534 KEKESKIS--DLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE-------KKDLIKE 604
|
490 500 510
....*....|....*....|....*....|....*..
gi 1039759465 619 IEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLE 655
Cdd:TIGR04523 605 IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKN 641
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
448-772 |
1.54e-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: 58.53 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 448 DRVTDLVN----QQQSLEEKMRedrdsLVERLHRQTAEYSAfkLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGM 523
Cdd:TIGR02168 189 DRLEDILNelerQLKSLERQAE-----KAERYKELKAELRE--LELALLVLRLEELREELEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 524 IDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNkEIEAARRQFQSQLADLQQlpdilkiteaKLAECQDQLQGYER 603
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEIS-RLEQQKQILRERLANLER----------QLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 604 KNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATS---AQNVEFLQVIAKR----EEAIH 676
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRskvAQLELQIASLNNEierlEARLE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 677 QAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSR 756
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
330
....*....|....*.
gi 1039759465 757 LQDLKDRLEQSESTNR 772
Cdd:TIGR02168 491 LDSLERLQENLEGFSE 506
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
202-788 |
2.47e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 202 AAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETnrtlrdLLREQHCKEDSERLMEQQGTLLKRLAEA 281
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEV------LEEHEERREELETLEAEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 282 DSEKARLLLLLQDKDKEVEELLQEIQ-------CEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERS 354
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDdllaeagLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 355 GNQHKAEVEAIMEQLKELkqkgDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVK 434
Cdd:PRK02224 351 ADDLEERAEELREEAAEL----ESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 435 DKGDLELEIIVLNDRVTDlvNQQ-----------QSLEEKMR----EDRDSLVERLhrqTAEYSAFKLENERLKASFAPM 499
Cdd:PRK02224 427 REAELEATLRTARERVEE--AEAlleagkcpecgQPVEGSPHvetiEEDRERVEEL---EAELEDLEEEVEEVEERLERA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 500 EDkLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQlercdkenkmlKDEMNKEIEAARRQFQSQLADLQQ 579
Cdd:PRK02224 502 ED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER-----------AAELEAEAEEKREAAAEAEEEAEE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 580 LPDILKITEAKLAECQDQLQGYERknidltaiISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDEL-ERKLEATS 658
Cdd:PRK02224 570 AREEVAELNSKLAELKERIESLER--------IRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKrERKRELEA 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 659 AQNveflqviakrEEAIHQAQLRLEektrecgslarQLESAIEDARRQVEQTKEqalsKERAAQSKILDLETQLSRtkte 738
Cdd:PRK02224 642 EFD----------EARIEEAREDKE-----------RAEEYLEQVEEKLDELRE----ERDDLQAEIGAVENELEE---- 692
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1039759465 739 lgqlrrtrddadrryqsrLQDLKDRLEQSESTnrsmqnyVQFLKASYANV 788
Cdd:PRK02224 693 ------------------LEELRERREALENR-------VEALEALYDEA 717
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
267-779 |
3.29e-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: 57.36 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 267 LMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLR-CKEAENSRLC 345
Cdd:TIGR00606 417 LQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAEReLSKAEKNSLT 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 346 MQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEE-------YAEQLHVQLADKDlYVAEA 418
Cdd:TIGR00606 497 ETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQirkiksrHSDELTSLLGYFP-NKKQL 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 419 LSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMR------------EDRDSLVERLHRQ-------- 478
Cdd:TIGR00606 576 EDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSsyedklfdvcgsQDEESDLERLKEEieksskqr 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 479 ------TAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKN----YEGMIDNYKSQVMKTRLEADEVAAQLERC 548
Cdd:TIGR00606 656 amlagaTAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSklrlAPDKLKSTESELKKKEKRRDEMLGLAPGR 735
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 549 DKEnkmlKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTaIISDLRSRIEHQGDKLEM 628
Cdd:TIGR00606 736 QSI----IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVT-IMERFQMELKDVERKIAQ 810
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 629 AREKHQAS--QKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQ 706
Cdd:TIGR00606 811 QAAKLQGSdlDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQL 890
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039759465 707 VEQTKE-QALSKE-RAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQSESTNRSMQNYVQ 779
Cdd:TIGR00606 891 VELSTEvQSLIREiKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ 965
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
295-632 |
3.35e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 295 KDKEVEELLQEI--------QCEKAQAKTASELSkSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIM 366
Cdd:TIGR02168 675 RRREIEELEEKIeeleekiaELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 367 EQLKELKQKgdrdketlkkaIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIVL 446
Cdd:TIGR02168 754 KELTELEAE-----------IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 447 NDRVTDLVNQQQSLEEKMREdrdsLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDN 526
Cdd:TIGR02168 823 RERLESLERRIAATERRLED----LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 527 YKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKeIEAARRQFQSQLADLQQ--LPDILK---ITEAKLAECQDQLQGY 601
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSltLEEAEAlenKIEDDEEEARRRLKRL 977
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1039759465 602 ERK-----NIDLTAI--ISDLRSR---IEHQGDKLEMAREK 632
Cdd:TIGR02168 978 ENKikelgPVNLAAIeeYEELKERydfLTAQKEDLTEAKET 1018
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
274-718 |
7.95e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 7.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 274 LLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLE- 352
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 353 -RSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQ 431
Cdd:COG4717 131 yQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 432 VVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPM------------ 499
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlflvlgllallf 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 500 ------EDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVM-KTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQS 572
Cdd:COG4717 291 lllareKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 573 QLADLQQLPDIlkITEAKLAECQDQLQGYErkniDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENK--QLSQKVDEL 650
Cdd:COG4717 371 EIAALLAEAGV--EDEEELRAALEQAEEYQ----ELKEELEELEEQLEELLGELEELLEALDEEELEEEleELEEELEEL 444
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039759465 651 ERKLEATSAQNVEFLQVI--AKREEAIHQAQLRLEEKTRECGSLARQ------LESAIEDARRQVEQTKEQALSKE 718
Cdd:COG4717 445 EEELEELREELAELEAELeqLEEDGELAELLQELEELKAELRELAEEwaalklALELLEEAREEYREERLPPVLER 520
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
478-719 |
8.03e-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: 55.16 E-value: 8.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 478 QTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLercdKENKMLKD 557
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL----AELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 558 EMNKEIEAARRQFQSQLADLQQLPdilKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQ 637
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLG---RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 638 KENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSK 717
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
..
gi 1039759465 718 ER 719
Cdd:COG4942 251 LK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
541-773 |
1.90e-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: 54.00 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 541 VAAQLERCDKENKMLKdEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIE 620
Cdd:COG4942 15 AAAQADAAAEAEAELE-QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 621 HQGDKLEmAREKHQASQKENKQLSQKVDELERKLEATSAQNV--------EFLQVIAKREEAIHQAQLRLEEKTRECGSL 692
Cdd:COG4942 94 ELRAELE-AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAvrrlqylkYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 693 ARQLESAIEDARRQveqtkEQALSKERAAQSKIL-DLETQLSRTKTELGQLRRTrddadrryQSRLQDLKDRLEQSESTN 771
Cdd:COG4942 173 RAELEALLAELEEE-----RAALEALKAERQKLLaRLEKELAELAAELAELQQE--------AEELEALIARLEAEAAAA 239
|
..
gi 1039759465 772 RS 773
Cdd:COG4942 240 AE 241
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
446-765 |
3.15e-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: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 446 LNDRVTDLVNQQQSLEEKMRE---DRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEG 522
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRienRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 523 MIDNYKSQVMKTRLEADEVAAQLERC-DKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGY 601
Cdd:TIGR02169 759 ELKELEARIEELEEDLHKLEEALNDLeARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 602 ERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLR 681
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 682 LEEKTRECGSLARQLeSAIEDARRQVEQTKEQALSKERaAQSKILDLETQLSRtkteLGQLRRTRDDADRRYQSRLQDLK 761
Cdd:TIGR02169 919 LSELKAKLEALEEEL-SEIEDPKGEDEEIPEEELSLED-VQAELQRVEEEIRA----LEPVNMLAIQEYEEVLKRLDELK 992
|
....
gi 1039759465 762 DRLE 765
Cdd:TIGR02169 993 EKRA 996
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
350-764 |
3.31e-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: 54.19 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 350 NLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKA----IRAQkERAEKSEEYAEQLHVQLADkdlyVAEALSTLESW 425
Cdd:COG3096 337 NLVQTALRQQEKIERYQEDLEELTERLEEQEEVVEEAaeqlAEAE-ARLEAAEEEVDSLKSQLAD----YQQALDVQQTR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 426 RSRYNQVVKDKGDL-------ELEIIVLNDRVTDLVNQQQSLEEKMR--EDRDSLVERLHRQTAEysAFKLenerlkasf 496
Cdd:COG3096 412 AIQYQQAVQALEKAralcglpDLTPENAEDYLAAFRAKEQQATEEVLelEQKLSVADAARRQFEK--AYEL--------- 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 497 apmedklnqahleVQQLKASVknyegmidnyksqvmkTRLEADEVAAQLERCDKENKMLkdemnkeieAARR-QFQSQLA 575
Cdd:COG3096 481 -------------VCKIAGEV----------------ERSQAWQTARELLRRYRSQQAL---------AQRLqQLRAQLA 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 576 DLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELerkle 655
Cdd:COG3096 523 ELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKEL----- 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 656 atsaqnveflqviAKREEAIHQAQLRLEektrecgSLARQLESAIEDArRQVEQTKEQALSKERAAQSkildLETQLSRT 735
Cdd:COG3096 598 -------------AARAPAWLAAQDALE-------RLREQSGEALADS-QEVTAAMQQLLEREREATV----ERDELAAR 652
|
410 420
....*....|....*....|....*....
gi 1039759465 736 KTELGQLRRTRDDADRRYQSRLQDLKDRL 764
Cdd:COG3096 653 KQALESQIERLSQPGGAEDPRLLALAERL 681
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
357-656 |
5.43e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 357 QHKAEVEAIMEQLKELKQKGDRdKETLKKAIRAQKERAEKSEEYAEQLHVQLADK-DLYVAEALSTLESWRSRYNQVVKD 435
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIER-LDLIIDEKRQQLERLRREREKAERYQALLKEKrEYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 436 KGDLELEIIVLNDRVTDLVNQQQSLEEKMREdrdsLVERLHRQTA-EYSAFKLENERLKASFAPMEDKLNQAHLEVQQLK 514
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEE----LNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 515 ASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMN------------------------KEIEAARRQF 570
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEdlraeleevdkefaetrdelkdyrEKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 571 QSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMA--------------REKHQAS 636
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLaadlskyeqelydlKEEYDRV 481
|
330 340
....*....|....*....|
gi 1039759465 637 QKENKQLSQKVDELERKLEA 656
Cdd:TIGR02169 482 EKELSKLQRELAEAEAQARA 501
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
557-766 |
1.15e-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: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 557 DEMNKEIEAARRQfQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTaiISDLRSRIEHQGDKLEMAREKHQAS 636
Cdd:COG4913 238 ERAHEALEDAREQ-IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR--LELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 637 QKENKQLSQKVDELERKLEATSAQNVEFLqviakrEEAIHQAQLRLEEKTRECGSLARQL----------ESAIEDARRQ 706
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQL------EREIERLERELEERERRRARLEALLaalglplpasAEEFAALRAE 388
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039759465 707 VEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRR---TRDDADRRYQSRLQDLKDRLEQ 766
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAeiaSLERRKSNIPARLLALRDALAE 451
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
244-779 |
2.02e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 244 FEETNRTLRDLLREQHCKEDSERLMEQQGTLLK---RLAEADSEKA-----RLLLLLQDKDKEVEELLQEIQCEKAQAKT 315
Cdd:COG4913 234 FDDLERAHEALEDAREQIELLEPIRELAERYAAareRLAELEYLRAalrlwFAQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 316 ASELSKSMESMRGHLQAQLRCKEAEN-SRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERA 394
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 395 EKSEEYAEQLHVQLADkdlyvaealstlesWRSRYNQVVKDKGDLELEIIVLNDRVT----DLVNQQQSLEEKMREDRDS 470
Cdd:COG4913 394 EALEEELEALEEALAE--------------AEAALRDLRRELRELEAEIASLERRKSnipaRLLALRDALAEALGLDEAE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 471 L-------------------VER-LHRQtaeysAFKL--ENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYK 528
Cdd:COG4913 460 LpfvgelievrpeeerwrgaIERvLGGF-----ALTLlvPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 529 SQVMKTRLEADEVAA-------------------QLERCDK---ENKMLKD-----EMNKEIEAARRQF-----QSQLAD 576
Cdd:COG4913 535 SLAGKLDFKPHPFRAwleaelgrrfdyvcvdspeELRRHPRaitRAGQVKGngtrhEKDDRRRIRSRYVlgfdnRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 577 LqqlpdilkitEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGdklemAREKHQASQKENKQLSQKVDELERKLEA 656
Cdd:COG4913 615 L----------EAELAELEEELAEAEERLEALEAELDALQERREALQ-----RLAEYSWDEIDVASAEREIAELEAELER 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 657 TSAQNVEfLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQAlskERAAQSKILDLETQLSRTK 736
Cdd:COG4913 680 LDASSDD-LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL---EAAEDLARLELRALLEERF 755
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1039759465 737 TELGQlRRTRDDADRRYQSRLQDLKDRLEQSEST-NRSMQNYVQ 779
Cdd:COG4913 756 AAALG-DAVERELRENLEERIDALRARLNRAEEElERAMRAFNR 798
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
103-708 |
2.29e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 103 RYDKKIDSLMNAVGCLKSEVKMQKGERQMAKRFLEERKEELEEVAHELAETEHEntvlrhnIERIKEEKDFTMLQKKHLQ 182
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE-------LARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 183 QEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMtctdintltrQKELLLQKLSTFEETNRTLRDLLREQhcke 262
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE----------AEAELAEAEEALLEAEAELAEAEEEL---- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 263 dsERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASElsksmesmrghLQAQLRCKEAENS 342
Cdd:COG1196 382 --EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE-----------EEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 343 RLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQ-LHVQLADKDLYVAEALST 421
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvKAALLLAGLRGLAGAVAV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 422 LESWRSRYNQVVkdkgdLELEIIVLNDRVTDLVNQQQSLEEKMREDRDSLVERlhrqtaeysafkLENERLKASFAPMED 501
Cdd:COG1196 529 LIGVEAAYEAAL-----EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATF------------LPLDKIRARAALAAA 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 502 KLNQAHLEVQQLKASVKNYEgmiDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQQLP 581
Cdd:COG1196 592 LARGAIGAAVDLVASDLREA---DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 582 DILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQN 661
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1039759465 662 VEFLQVIAKREEAIHQAQLRLEEktrecgsLARQLES-------AIEDARRQVE 708
Cdd:COG1196 749 EEEALEELPEPPDLEELERELER-------LEREIEAlgpvnllAIEEYEELEE 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
295-618 |
2.92e-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: 51.22 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 295 KDKEVEELLQEIQCEKAQAKtASELSKSMESMRghlqAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKEL-- 372
Cdd:TIGR02169 205 REREKAERYQALLKEKREYE-GYELLKEKEALE----RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnk 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 373 --KQKGDRDKETLKKAIR---AQKERAEKS----EEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEI 443
Cdd:TIGR02169 280 kiKDLGEEEQLRVKEKIGeleAEIASLERSiaekERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 444 IVLNDRVTDLVNQQQSLEEKMREDRDSLVERlhrqTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGM 523
Cdd:TIGR02169 360 AELKEELEDLRAELEEVDKEFAETRDELKDY----REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 524 IdnyksqvmkTRLEADevaaqlercdkenkmlKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYER 603
Cdd:TIGR02169 436 I---------NELEEE----------------KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
330
....*....|....*
gi 1039759465 604 KNIDLTAIISDLRSR 618
Cdd:TIGR02169 491 ELAEAEAQARASEER 505
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
200-758 |
4.66e-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: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 200 AAAAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETNRTLRDLLREQhckEDSERLMEQQGTLLKRLA 279
Cdd:TIGR00618 296 AAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQE---IHIRDAHEVATSIREISC 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 280 EADSEKARLLLLLQDK--DKEVEELL-QEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQ---IKNLER 353
Cdd:TIGR00618 373 QQHTLTQHIHTLQQQKttLTQKLQSLcKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCaaaITCTAQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 354 SGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQ--------LHVQLADKDLYVAEALStlesw 425
Cdd:TIGR00618 453 CEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcplcgscIHPNPARQDIDNPGPLT----- 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 426 rSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDS---LVERLHRQTAEYSAFKLENERLKaSFAPMEDK 502
Cdd:TIGR00618 528 -RRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSfsiLTQCDNRSKEDIPNLQNITVRLQ-DLTEKLSE 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 503 L-------NQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRqfQSQLA 575
Cdd:TIGR00618 606 AedmlaceQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASR--QLALQ 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 576 DLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKE-NKQLSQKVDELERKL 654
Cdd:TIGR00618 684 KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKElMHQARTVLKARTEAH 763
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 655 EATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLArQLESAIEDARRQVEQTK----EQALSKERAAQSKILDLET 730
Cdd:TIGR00618 764 FNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLK-TLEAEIGQEIPSDEDILnlqcETLVQEEEQFLSRLEEKSA 842
|
570 580
....*....|....*....|....*...
gi 1039759465 731 QLSRTKTELGQLRRTRDDADRRYQSRLQ 758
Cdd:TIGR00618 843 TLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
165-775 |
5.36e-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: 50.12 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 165 ERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTF 244
Cdd:pfam15921 92 RRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 245 EETNRTLRdLLREQHCKEDSERLMEQQGTLLKRLAEADSekaRLLLLLQDKDKEVEELLQEIQCEkaqaktASELSKSME 324
Cdd:pfam15921 172 IEQLRKMM-LSHEGVLQEIRSILVDFEEASGKKIYEHDS---MSTMHFRSLGSAISKILRELDTE------ISYLKGRIF 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 325 SMRGHLQAqLRCKEAENSRLCMQIKN--LERSGNQHKAEVEAIMEQLKELKQKGDrdketlkkAIRAQKERAEKSEEYAE 402
Cdd:pfam15921 242 PVEDQLEA-LKSESQNKIELLLQQHQdrIEQLISEHEVEITGLTEKASSARSQAN--------SIQSQLEIIQEQARNQN 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 403 QLHV-QLADKDLYVAEALSTLESWRSRYNQVVKDkgdLELEIIVLNDRVTDLVNQQQSLEEK---MREDRDSLVERLHRQ 478
Cdd:pfam15921 313 SMYMrQLSDLESTVSQLRSELREAKRMYEDKIEE---LEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLHKR 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 479 TAEYSAFKLENERL-------KASFAPMEDKLNQAHLEVQQLKASVKnyegmidnyksqVMKTRLEAdEVAAQLERCDKE 551
Cdd:pfam15921 390 EKELSLEKEQNKRLwdrdtgnSITIDHLRRELDDRNMEVQRLEALLK------------AMKSECQG-QMERQMAAIQGK 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 552 NKMLK--DEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMA 629
Cdd:pfam15921 457 NESLEkvSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 630 R---EKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVI--------------AKREEAIHQAQLRLEE----KTRE 688
Cdd:pfam15921 537 KnegDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVgqhgrtagamqvekAQLEKEINDRRLELQEfkilKDKK 616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 689 CGSLaRQLESAIED-----------------ARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADR 751
Cdd:pfam15921 617 DAKI-RELEARVSDlelekvklvnagserlrAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTN 695
|
650 660
....*....|....*....|....
gi 1039759465 752 RYQSRLQDLKDRLEQSESTNRSMQ 775
Cdd:pfam15921 696 KLKMQLKSAQSELEQTRNTLKSME 719
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
154-709 |
8.45e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 8.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 154 EHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEmdgaaaaKQVMALK-DTIGKLKTEkqmtctdINTLTR 232
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELE-------AQIRGNGgDRLEQLERE-------IERLER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 233 QKELLLQKLSTFEETNRTL-------RDLLREQHckedsERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQE 305
Cdd:COG4913 353 ELEERERRRARLEALLAALglplpasAEEFAALR-----AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 306 IQcekAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLC--MQIKNLERS---------GNQ---------HKAEVEAI 365
Cdd:COG4913 428 IA---SLERRKSNIPARLLALRDALAEALGLDEAELPFVGelIEVRPEEERwrgaiervlGGFaltllvppeHYAAALRW 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 366 MEQLKeLKQK--GDRDKETLKKAIRAQKER---AEKSE----EYAEQLHVQLADKDLYV----AEALS------TLE--- 423
Cdd:COG4913 505 VNRLH-LRGRlvYERVRTGLPDPERPRLDPdslAGKLDfkphPFRAWLEAELGRRFDYVcvdsPEELRrhpraiTRAgqv 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 424 -SWRSRYnqvVKDKGDLELEIIVLN----DRVTDLVNQQQSLEEKMREdRDSLVERLHRQTAEYSAFKLENERLkASFAP 498
Cdd:COG4913 584 kGNGTRH---EKDDRRRIRSRYVLGfdnrAKLAALEAELAELEEELAE-AEERLEALEAELDALQERREALQRL-AEYSW 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 499 MEDKLNQAHLEVQQLKASVKNyegmIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEM---NKEIEAARRQFQSQLA 575
Cdd:COG4913 659 DEIDVASAEREIAELEAELER----LDASSDDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEELDELQD 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 576 DLQQLPDILKITEAKLAE------CQDQLQGYERKNidLTAIISDLRSRIEHQGDKLEMAREKHQASQKENkqlsqkVDE 649
Cdd:COG4913 735 RLEAAEDLARLELRALLEerfaaaLGDAVERELREN--LEERIDALRARLNRAEEELERAMRAFNREWPAE------TAD 806
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039759465 650 LERKLEAtsaqNVEFLQVIAK-REEAIHQ-----AQLRLEEKTRECGSLARQLESAIEDARRQVEQ 709
Cdd:COG4913 807 LDADLES----LPEYLALLDRlEEDGLPEyeerfKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
524-787 |
9.21e-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: 49.30 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 524 IDNYKSQVMKTRLEADEVAAQLERCD-------KENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQD 596
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDliidekrQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 597 QLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQA-SQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAI 675
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 676 HQAQLRLEEKTREcgslARQLESAIEDARRQVEQTKE--QALSKERAA-QSKILDLETQLSRTKTELGQlrrtrddadrr 752
Cdd:TIGR02169 325 AKLEAEIDKLLAE----IEELEREIEEERKRRDKLTEeyAELKEELEDlRAELEEVDKEFAETRDELKD----------- 389
|
250 260 270
....*....|....*....|....*....|....*
gi 1039759465 753 YQSRLQDLKDRLEQSESTNRSMQNYVQFLKASYAN 787
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
275-685 |
1.52e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 275 LKRLAEADSEKARLLLLLQDKDKEVEEL---------LQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLC 345
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAkkkaeekkkADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 346 MQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDK--ETLKKAIRAQK-ERAEKSEEYAEQLHVQLADKDLYVAEALSTL 422
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkaDEAKKAEEAKKaDEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 423 ESWRSRYNQVVKDKGDLELEIIVLNDRVTDLvnqqQSLEEKMREDRDSLVERLHRQTAEySAFKLENERLKASfapmedk 502
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEA----KKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIKAE------- 1623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 503 lnqahlEVQQLKASVKNYEGMIDNYKSQVMKtrleadevAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQqlpd 582
Cdd:PTZ00121 1624 ------ELKKAEEEKKKVEQLKKKEAEEKKK--------AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE---- 1685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 583 ilkitEAKLAECQDQLQGYERKNIDltaiisDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNV 662
Cdd:PTZ00121 1686 -----DEKKAAEALKKEAEEAKKAE------ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754
|
410 420
....*....|....*....|...
gi 1039759465 663 EFLQVIAKREEAIHQAQLRLEEK 685
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEK 1777
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
494-723 |
1.61e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 494 ASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLK---DEMNKEIEAARRQF 570
Cdd:COG3883 9 PTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQaeiAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 571 QSQLADLQQLPDILKITEAKLAecQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDEL 650
Cdd:COG3883 89 GERARALYRSGGSVSYLDVLLG--SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039759465 651 ERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQS 723
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
554-739 |
1.97e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 554 MLKDEMNKEIEAARRQ-------FQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQgDKL 626
Cdd:COG4717 46 MLLERLEKEADELFKPqgrkpelNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 627 EMAREKHQASQKENKQLSQKVDELErKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQ 706
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190
....*....|....*....|....*....|...
gi 1039759465 707 VEQTKEQALSKERAAQSKILDLETQLSRTKTEL 739
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
618-773 |
2.77e-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: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 618 RIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQnveflqvIAKREEAIHQAQLRLEEKTRECGSLARQLE 697
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE-------LEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039759465 698 SAIEDaRRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQSESTNRS 773
Cdd:COG1196 306 RLEER-RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
427-658 |
2.86e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.70 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 427 SRYNQVVKDKgdleleIIVLNDRVTDLVNQQQSLEEKMREDRDsLVERLHRQTAEysafklENERLKASFAPMEDKLNQA 506
Cdd:PHA02562 166 SEMDKLNKDK------IRELNQQIQTLDMKIDHIQQQIKTYNK-NIEEQRKKNGE------NIARKQNKYDELVEEAKTI 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 507 HLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKD------------EMNKEIEAARrqfqSQL 574
Cdd:PHA02562 233 KAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqqisEGPDRITKIK----DKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 575 ADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLR---SRIEHQGDKLEMAREKHQASQKENK-QLSQKVDEL 650
Cdd:PHA02562 309 KELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKqslITLVDKAKKVKAAIEELQAEFVDNAeELAKLQDEL 388
|
....*...
gi 1039759465 651 ERKLEATS 658
Cdd:PHA02562 389 DKIVKTKS 396
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
367-739 |
4.04e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.36 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 367 EQLK-ELKQ----KGDRDKET---LKKAIRA---QKERAEKSEEY----------AEQLHVQLADKDLYVAEALSTLESw 425
Cdd:PRK10929 26 KQITqELEQakaaKTPAQAEIveaLQSALNWleeRKGSLERAKQYqqvidnfpklSAELRQQLNNERDEPRSVPPNMST- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 426 rsrynqvvkdkGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPmEDKLNQ 505
Cdd:PRK10929 105 -----------DALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTP-NTPLAQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 506 AHL-----EVQQLKASVKNYE--GMIDNYKSQVmkTRLEADEVAAQLERCDKENKMLKDEMNkeieaARRQFQSQLAdlq 578
Cdd:PRK10929 173 AQLtalqaESAALKALVDELElaQLSANNRQEL--ARLRSELAKKRSQQLDAYLQALRNQLN-----SQRQREAERA--- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 579 qlpdiLKITEaKLAECQDqlqgyerkniDLTAIISdlrsriehqgDKLEMAREkhqASQKENKQlSQKVDELERKLEATS 658
Cdd:PRK10929 243 -----LESTE-LLAEQSG----------DLPKSIV----------AQFKINRE---LSQALNQQ-AQRMDLIASQQRQAA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 659 AQNVEFLQVI-AKREEA-----------IHQAQL-RLEEKTRecgslARQLESAIEDAR----------------RQVEQ 709
Cdd:PRK10929 293 SQTLQVRQALnTLREQSqwlgvsnalgeALRAQVaRLPEMPK-----PQQLDTEMAQLRvqrlryedllnkqpqlRQIRQ 367
|
410 420 430
....*....|....*....|....*....|
gi 1039759465 710 TKEQALSkerAAQSKILDleTQLsRTKTEL 739
Cdd:PRK10929 368 ADGQPLT---AEQNRILD--AQL-RTQREL 391
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
330-719 |
4.33e-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: 47.32 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 330 LQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLH-VQL 408
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqLKS 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 409 ADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMRE---DRDSLVERLHRQTAEYSAF 485
Cdd:TIGR04523 296 EISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNsesENSEKQRELEEKQNEIEKL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 486 KLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDE---MNKE 562
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvKELI 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 563 IEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQ 642
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 643 LSQKVDELERKLEA-----TSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSK 717
Cdd:TIGR04523 536 KESKISDLEDELNKddfelKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSL 615
|
..
gi 1039759465 718 ER 719
Cdd:TIGR04523 616 EK 617
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
562-727 |
9.87e-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: 44.53 E-value: 9.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 562 EIEAARRQFQSQLADLQQLpdiLKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMARekhqaSQKENK 641
Cdd:COG1579 21 RLEHRLKELPAELAELEDE---LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-----NNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 642 QLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQveqtkEQALSKERAA 721
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE-----LEELEAEREE 167
|
....*.
gi 1039759465 722 QSKILD 727
Cdd:COG1579 168 LAAKIP 173
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
357-764 |
1.04e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 357 QHKAEVEAIMEQLKELKQKgdrdKETLKKAIRAQKERAEKSEEYAEQLHVQLADkdlyVAEALSTLESWRSRYNQVVK-- 434
Cdd:PRK04863 352 RYQADLEELEERLEEQNEV----VEEADEQQEENEARAEAAEEEVDELKSQLAD----YQQALDVQQTRAIQYQQAVQal 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 435 DK-----GDLELEIIVLNDRVTDLVNQQQSLEEKMR--EDRDSLVERLHRQTAEysAFKLenerlkasfapmedklnqah 507
Cdd:PRK04863 424 ERakqlcGLPDLTADNAEDWLEEFQAKEQEATEELLslEQKLSVAQAAHSQFEQ--AYQL-------------------- 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 508 leVQQLKASVknyegmidnyksqvmkTRLEADEVAAQLERCDKENKMLkdemnkeieAARR-QFQSQLADLQQLPDILKI 586
Cdd:PRK04863 482 --VRKIAGEV----------------SRSEAWDVARELLRRLREQRHL---------AEQLqQLRMRLSELEQRLRQQQR 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 587 TEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELErkleatsaqnveflq 666
Cdd:PRK04863 535 AERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLA--------------- 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 667 viaKREEAIHQAQLRLEEktrecgsLARQLESAIEDArRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTR 746
Cdd:PRK04863 600 ---ARAPAWLAAQDALAR-------LREQSGEEFEDS-QDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPG 668
|
410
....*....|....*...
gi 1039759465 747 DDADrryqSRLQDLKDRL 764
Cdd:PRK04863 669 GSED----PRLNALAERF 682
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
538-737 |
1.19e-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: 45.14 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 538 ADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRS 617
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 618 RIEHQGDKL--------------------------------EMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFL 665
Cdd:COG4942 98 ELEAQKEELaellralyrlgrqpplalllspedfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039759465 666 QVIAKREEAihQAQLRLEEKTREcgSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKT 737
Cdd:COG4942 178 ALLAELEEE--RAALEALKAERQ--KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
76-738 |
2.02e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 76 SSEKLV-SVMRLSDLSTEDDDSGHCK--MNRYDKKIDSLMNAVGCLKSEVKMQKGERQMAKRFLEERKEELEEVAHELAE 152
Cdd:PRK03918 146 SREKVVrQILGLDDYENAYKNLGEVIkeIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 153 TEHENTVLRHNIERIKEEKdftmLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTekqmtctdintlTR 232
Cdd:PRK03918 226 LEKEVKELEELKEEIEELE----KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE------------LK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 233 QKELLLQKLSTF-EETNRTLRDLlreqhcKEDSERLMEQQGTLLKRLAEADSEKARLLLLLqdkdKEVEELLQEIQCEKA 311
Cdd:PRK03918 290 EKAEEYIKLSEFyEEYLDELREI------EKRLSRLEEEINGIEERIKELEEKEERLEELK----KKLKELEKRLEELEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 312 QAKTASELSKSMESMRGhLQAQLRCKEAEnsRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQK 391
Cdd:PRK03918 360 RHELYEEAKAKKEELER-LKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 392 E----RAEKSEEYAEQLhvqLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIVLND--RVTDLVNQQQSLEEKMR 465
Cdd:PRK03918 437 KcpvcGRELTEEHRKEL---LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 466 EDRdslVERLHRQTAEYSAFKLENERLKASFAPMEDKLNqahlEVQQLKASVKNYEGMIDNYKSqvmktrlEADEVAAQL 545
Cdd:PRK03918 514 KYN---LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE----KLEELKKKLAELEKKLDELEE-------ELAELLKEL 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 546 ERCDKENKMLKDEMNKEIEAARRQFQSqladLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQG-- 623
Cdd:PRK03918 580 EELGFESVEELEERLKELEPFYNEYLE----LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEkk 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 624 ---DKLEMAREKHQASQKENKQLSQKVDELERKLEaTSAQNVEFLQviaKREEAIHQAQLRLEektrecgslarQLESAI 700
Cdd:PRK03918 656 yseEEYEELREEYLELSRELAGLRAELEELEKRRE-EIKKTLEKLK---EELEEREKAKKELE-----------KLEKAL 720
|
650 660 670
....*....|....*....|....*....|....*...
gi 1039759465 701 EDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTE 738
Cdd:PRK03918 721 ERVEELREKVKKYKALLKERALSKVGEIASEIFEELTE 758
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
488-742 |
2.22e-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: 44.29 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 488 ENERLKASFAPMEDKLNqahlEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENkmlkdemnkeiEAAR 567
Cdd:pfam19220 4 RNELLRVRLGEMADRLE----DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAY-----------GKLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 568 RQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKV 647
Cdd:pfam19220 69 RELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 648 DELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLAR---QLESAIEDARRQVEQTkEQALSKERAAQSK 724
Cdd:pfam19220 149 QAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRrlaELETQLDATRARLRAL-EGQLAAEQAERER 227
|
250
....*....|....*....
gi 1039759465 725 IL-DLETQLSRTKTELGQL 742
Cdd:pfam19220 228 AEaQLEEAVEAHRAERASL 246
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
560-781 |
2.74e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 560 NKEIEAARRQFQSQLADLQQlpdilkiteaKLAECQDQLQGYERKN--IDLTAIISDLRSRIEHQGDKLEMAREKHQASQ 637
Cdd:COG3206 170 REEARKALEFLEEQLPELRK----------ELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 638 kenkqlsQKVDELERKLEATSAQNVEFLQ--VIAKREEAIHQAQLRLEEKTRECG--------------SLARQLESAIE 701
Cdd:COG3206 240 -------ARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTpnhpdvialraqiaALRAQLQQEAQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 702 DARRQVEQTKEQALSKERAAQSKILDLETQ---LSRTKTELGQLRRTRDDADRRYQSrlqdLKDRLEQSESTNRSMQNYV 778
Cdd:COG3206 313 RILASLEAELEALQAREASLQAQLAQLEARlaeLPELEAELRRLEREVEVARELYES----LLQRLEEARLAEALTVGNV 388
|
...
gi 1039759465 779 QFL 781
Cdd:COG3206 389 RVI 391
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
262-724 |
2.95e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 262 EDSERLMEQQGTLLKRLAEaDSEKARLLLLLQDKdKEVEELLQEIQCEKAQAKTASELSKSMESMRGHlQAQLRCKEAEN 341
Cdd:PTZ00121 1143 EEARKAEDAKRVEIARKAE-DARKAEEARKAEDA-KKAEAARKAEEVRKAEELRKAEDARKAEAARKA-EEERKAEEARK 1219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 342 SRLCMQIKNLERSGNQHKAEVEAIMEQlKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKdlyVAEALST 421
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEAKKDAEEAKKAE-EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE---KKKADEA 1295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 422 LESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDSlvERLHRQTAEYSAFKLENERLKASFAPME- 500
Cdd:PTZ00121 1296 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA--AEAAKAEAEAAADEAEAAEEKAEAAEKKk 1373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 501 -------DKLNQAHLEVQQLKASVKNYEGmiDNYKSQVMKTRLEADEVAAQLERcDKENKMLKDEMNKEIEAARR--QFQ 571
Cdd:PTZ00121 1374 eeakkkaDAAKKKAEEKKKADEAKKKAEE--DKKKADELKKAAAAKKKADEAKK-KAEEKKKADEAKKKAEEAKKadEAK 1450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 572 SQLADLQQLPDILKITE--------AKLAECQDQLQGYERKNIDLTAIISDLRSRIE--HQGDKLEMAREKHQASQKENK 641
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEeakkadeaKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEakKKADEAKKAEEAKKADEAKKA 1530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 642 QLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAA 721
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
...
gi 1039759465 722 QSK 724
Cdd:PTZ00121 1611 EAK 1613
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
446-774 |
2.97e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.76 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 446 LNDRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAE----YSAFKLENERLKASF-------APMEDKLNQAHLEVQQLK 514
Cdd:pfam00038 9 LNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpsrlYSLYEKEIEDLRRQLdtltverARLQLELDNLRLAAEDFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 515 ASVKNYEGMIDNYKSQVMKTRLEADEvaAQLERCDKENKMlkDEMNKEIEAARRQFQSQLADLQqlpdilkiteAKLAEC 594
Cdd:pfam00038 89 QKYEDELNLRTSAENDLVGLRKDLDE--ATLARVDLEAKI--ESLKEELAFLKKNHEEEVRELQ----------AQVSDT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 595 QDQLQGYERKNIDLTAIISDLRSRIEHQgdkleMAREKHQASQkenkQLSQKVDELERkleaTSAQNVEFLQviAKREEa 674
Cdd:pfam00038 155 QVNVEMDAARKLDLTSALAEIRAQYEEI-----AAKNREEAEE----WYQSKLEELQQ----AAARNGDALR--SAKEE- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 675 IHQAQLRLEEKTRECGSLARQLESaIEDARRQVEQTKEQALSKeraAQSKILDLETQLSRTKTELGQLrrtrddaDRRYQ 754
Cdd:pfam00038 219 ITELRRTIQSLEIELQSLKKQKAS-LERQLAETEERYELQLAD---YQELISELEAELQETRQEMARQ-------LREYQ 287
|
330 340
....*....|....*....|
gi 1039759465 755 SrLQDLKDRLEQSESTNRSM 774
Cdd:pfam00038 288 E-LLNVKLALDIEIATYRKL 306
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
147-397 |
2.99e-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: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 147 AHELAETEHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTD 226
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 227 INTLTRQKELLLQKLSTFEETNRtLRDLLREQHCKEDSERLMeqqgtLLKRLAEADSEKARlllllqdkdkEVEELLQEI 306
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPP-LALLLSPEDFLDAVRRLQ-----YLKYLAPARREQAE----------ELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 307 QcekaqaktasELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKA 386
Cdd:COG4942 163 A----------ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
250
....*....|.
gi 1039759465 387 IRAQKERAEKS 397
Cdd:COG4942 233 EAEAAAAAERT 243
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
279-777 |
4.70e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 279 AEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKS-MESMRGHLQAQLRCKEAENSRLCMQIKNLERSgnQ 357
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAeAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA--K 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 358 HKAEVEAIMEQLKELKQKGDRDKETLKKAiRAQKERAEKSEEYAEQlhVQLADKDLYVAEALSTLESWRSRYNQVVKDKg 437
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKAEEDKKKADELKKA-AAAKKKADEAKKKAEE--KKKADEAKKKAEEAKKADEAKKKAEEAKKAE- 1460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 438 dlELEIIVLNDRVTDlvNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASV 517
Cdd:PTZ00121 1461 --EAKKKAEEAKKAD--EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 518 KNYEGMIDNYKSQVMKTRLE---ADEV----AAQLERCDKENKMLKDEMNKEIEAARRQfqsQLADLQQLPDILKITEAK 590
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEElkkAEEKkkaeEAKKAEEDKNMALRKAEEAKKAEEARIE---EVMKLYEEEKKMKAEEAK 1613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 591 LAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLE----ATSAQNVEFLQ 666
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEeakkAEEDEKKAAEA 1693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 667 VIAKREEAIHQAQLRleEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLE-----TQLSRTKTELGQ 741
Cdd:PTZ00121 1694 LKKEAEEAKKAEELK--KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEekkkiAHLKKEEEKKAE 1771
|
490 500 510
....*....|....*....|....*....|....*.
gi 1039759465 742 LRRTRDDADRRYQSRLQDLKDRLEQSESTNRSMQNY 777
Cdd:PTZ00121 1772 EIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNF 1807
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
571-770 |
7.28e-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: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 571 QSQLAD-LQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDE 649
Cdd:pfam07888 33 QNRLEEcLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 650 LERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTREcgslarqLESAIEDARRQVEQTKEQAlSKERAAQSKILDLE 729
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETE-------LERMKERAKKAGAQRKEEE-AERKQLQAKLQQTE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039759465 730 TQLSRTKTELGQLRRTRDDADRRYQsRLQDLKDRLEQSEST 770
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVL-QLQDTITTLTQKLTT 224
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
457-768 |
1.27e-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: 42.36 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 457 QQSLEE----KMREDRDSLVERLHRQTAEysafKLENERLKAsfapmedklnqahLEVQQLKASVKNYEGMIDNYKSQVM 532
Cdd:TIGR02169 173 EKALEEleevEENIERLDLIIDEKRQQLE----RLRREREKA-------------ERYQALLKEKREYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 533 KTRLEAdeVAAQLERCDKENKMLK---DEMNKEIEAARrqfqsqladlQQLPDILKITEAKLAECQDQLQgyeRKNIDLT 609
Cdd:TIGR02169 236 ERQKEA--IERQLASLEEELEKLTeeiSELEKRLEEIE----------QLLEELNKKIKDLGEEEQLRVK---EKIGELE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 610 AIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTREc 689
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE- 379
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039759465 690 gslARQLESAIEDARRQVEQTKEQALSKERaAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQSE 768
Cdd:TIGR02169 380 ---FAETRDELKDYREKLEKLKREINELKR-ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE 454
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
293-484 |
1.28e-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: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 293 QDKDKEVEELLQEIQcekAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKEL 372
Cdd:COG4942 19 ADAAAEAEAELEQLQ---QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 373 KQKGDRDKETLKKAIRAQKERAEKSE-------EYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIV 445
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039759465 446 LNDRVTDLVNQQQSLEEKMREdRDSLVERLHRQTAEYSA 484
Cdd:COG4942 176 LEALLAELEEERAALEALKAE-RQKLLARLEKELAELAA 213
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
590-738 |
2.04e-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: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 590 KLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQ-----NVEF 664
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrNNKE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039759465 665 LQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTE 738
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
577-768 |
2.10e-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: 40.40 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 577 LQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEA 656
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 657 TSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLesaiedarRQVEQTKEQALSKERAAQSKILDLETQLSRTK 736
Cdd:pfam00261 83 LENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKL--------VVVEGDLERAEERAELAESKIVELEEELKVVG 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1039759465 737 TELGQL---RRTRDDADRRYQSRLQDLKDRLEQSE 768
Cdd:pfam00261 155 NNLKSLeasEEKASEREDKYEEQIRFLTEKLKEAE 189
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
149-466 |
2.59e-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: 41.59 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 149 ELAETEHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTctDIN 228
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS--RIP 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 229 TLTRQKELLLQKLSTFEETNRTLRDLLREQHCKEDSERlmEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIqc 308
Cdd:TIGR02169 795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE--KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL-- 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 309 EKAQAKTaselsKSMESMRGHLqaqlrckEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIR 388
Cdd:TIGR02169 871 EELEAAL-----RDLESRLGDL-------KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED 938
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 389 AQKERAEKSEEYAEQLHVQLadKDLYVAEALSTLESWRSR----YNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKM 464
Cdd:TIGR02169 939 PKGEDEEIPEEELSLEDVQA--ELQRVEEEIRALEPVNMLaiqeYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
..
gi 1039759465 465 RE 466
Cdd:TIGR02169 1017 RE 1018
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
446-652 |
2.67e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 446 LNDRVTDLvNQQQSLEEKMREDRDSLVERLhrqTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGmid 525
Cdd:PRK09039 58 LNSQIAEL-ADLLSLERQGNQDLQDSVANL---RASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQ--- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 526 nyksqvmktrlEADEVAAQLERcdkenkmlkdeMNKEIEAARRqfqsQLADLQQLpdiLKITEAKLAECQDQlqgyerkn 605
Cdd:PRK09039 131 -----------VSARALAQVEL-----------LNQQIAALRR----QLAALEAA---LDASEKRDRESQAK-------- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1039759465 606 idltaiISDLRSRIehqgdklemarekhqasqkeNKQLSQKVDELER 652
Cdd:PRK09039 174 ------IADLGRRL--------------------NVALAQRVQELNR 194
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
146-547 |
2.76e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 146 VAHELAETEHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCT 225
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 226 DINTLTRQKELLL-------QKLSTFEETNRTLRDLLREqhckedSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKE 298
Cdd:PRK02224 406 DLGNAEDFLEELReerdelrEREAELEATLRTARERVEE------AEALLEAGKCPECGQPVEGSPHVETIEEDRERVEE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 299 VEELLQEIQCEKAqaktasELSKSMESMRghlqaQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQkgdr 378
Cdd:PRK02224 480 LEAELEDLEEEVE------EVEERLERAE-----DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE---- 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 379 DKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDlyvaEALSTLESWRSRYNQVVkdkgDLELEIIVLNDRVTDLVNQQQ 458
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELN----SKLAELKERIESLERIR----TLLAAIADAEDEIERLREKRE 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 459 SLEEKMREDRDSLVERLHRQTAEYSAFKLEN-ERLKASFAPMEDKLNQAHLEVQQL---KASVKNYEGMIDNYKSQVMKT 534
Cdd:PRK02224 617 ALAELNDERRERLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELreeRDDLQAEIGAVENELEELEEL 696
|
410
....*....|...
gi 1039759465 535 RLEADEVAAQLER 547
Cdd:PRK02224 697 RERREALENRVEA 709
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
473-742 |
2.93e-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: 41.10 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 473 ERLHRQTAEYSAFKLENERlkASFAPMEDKLNQAHLEVQQLKASVKNYEGMID-----NYKSQVMKTRLEADEVAAQLER 547
Cdd:COG5185 256 EKLVEQNTDLRLEKLGENA--ESSKRLNENANNLIKQFENTKEKIAEYTKSIDikkatESLEEQLAAAEAEQELEESKRE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 548 CDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKIT--EAKLAECQDQLqgyERKNIDLTAIISDLRSRIEhqgDK 625
Cdd:COG5185 334 TETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSksSEELDSFKDTI---ESTKESLDEIPQNQRGYAQ---EI 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 626 LEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKRE-EAIHQAQLRLEEKTREcgsLARQLESAIEDAR 704
Cdd:COG5185 408 LATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMrEADEESQSRLEEAYDE---INRSVRSKKEDLN 484
|
250 260 270
....*....|....*....|....*....|....*...
gi 1039759465 705 RQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQL 742
Cdd:COG5185 485 EELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQV 522
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
200-386 |
3.05e-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: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 200 AAAAKQVMALKDTIGKLKTEKQmtctdINTLTRQKELLLQKLSTFEETNRTLRDLLREQhckedsERLMEQQGTLL--KR 277
Cdd:COG4192 68 VAALPEFAAATNTTERSQLRNQ-----LNTQLADIEELLAELEQLTQDAGDLRAAVADL------RNLLQQLDSLLtqRI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 278 LAEADSEKA--RLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENsrlcmQIKNL--ER 353
Cdd:COG4192 137 ALRRRLQELleQINWLHQDFNSELTPLLQEASWQQTRLLDSVETTESLRNLQNELQLLLRLLAIEN-----QIVSLlrEV 211
|
170 180 190
....*....|....*....|....*....|...
gi 1039759465 354 SGNQHKAEVEAIMEQLKELKQKGDRDKETLKKA 386
Cdd:COG4192 212 AAARDQADVDNLFDRLQYLKDELDRNLQALKNY 244
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
584-811 |
3.16e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 584 LKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEA------T 657
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralyR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 658 SAQNVEFLQVIAKRE---EAIHQAQL--RLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQL 732
Cdd:COG3883 98 SGGSVSYLDVLLGSEsfsDFLDRLSAlsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 733 SRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQ----SESTNRSMQNYVQFLKASYANVFGDAPYTSSYLTSSPIRSRS 808
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAaaaaAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
...
gi 1039759465 809 PPA 811
Cdd:COG3883 258 AAG 260
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
500-739 |
3.80e-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: 40.93 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 500 EDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAArrqfqsqladlqq 579
Cdd:pfam01576 88 EERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKER------------- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 580 lpdilKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSA 659
Cdd:pfam01576 155 -----KLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 660 QNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLA---RQLESAIEDARRQVEQTKEQALSKERAAQskilDLETQLSRTK 736
Cdd:pfam01576 230 QIAELRAQLAKKEEELQAALARLEEETAQKNNALkkiRELEAQISELQEDLESERAARNKAEKQRR----DLGEELEALK 305
|
...
gi 1039759465 737 TEL 739
Cdd:pfam01576 306 TEL 308
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
143-782 |
4.44e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.73 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 143 LEEVAHELAETEHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMdgaaaAKQVMALKDTIGKLKTEKQM 222
Cdd:pfam02463 178 LIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL-----KLNEERIDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 223 TCTDINTLTRQKELLLQKLSTFEETNRTLRDLLREQHCKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEEL 302
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 303 LQEIQCEKAQAKTASELSKSM--ESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDK 380
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAeeEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLE 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 381 ETLKKAIRAQKERAEKSEEYAEQLHVQLAD--KDLYVAEALSTLESWRSRYNQVVKDKGDLELEIivlndrvtdlVNQQQ 458
Cdd:pfam02463 413 LARQLEDLLKEEKKEELEILEEEEESIELKqgKLTEEKEELEKQELKLLKDELELKKSEDLLKET----------QLVKL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 459 SLEEKMREDRDSLVERLHRQTAeysafklENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEA 538
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQKESK-------ARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSA 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 539 DEVAaqlerCDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTA----IISD 614
Cdd:pfam02463 556 TADE-----VEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAkvveGILK 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 615 LRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLAR 694
Cdd:pfam02463 631 DTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 695 QLESAIEDARRQVEQTKEQALSKeraAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQSESTNRSM 774
Cdd:pfam02463 711 ELKKLKLEAEELLADRVQEAQDK---INEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLK 787
|
....*...
gi 1039759465 775 QNYVQFLK 782
Cdd:pfam02463 788 VEEEKEEK 795
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
293-651 |
4.45e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 293 QDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLErsgnQHKAEVEAIMEQLKEL 372
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ----QEKELLEKEIERLKET 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 373 KQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLE-------SWRSRYNQVVKDKGDLELEIIV 445
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEqkqkelkSKEKELKKLNEEKKELEEKVKD 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 446 LNDRVTDLVNQQQSLEEKMREDRDSLVERlhRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMID 525
Cdd:TIGR04523 515 LTKKISSLKEKIEKLESEKKEKESKISDL--EDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 526 NYKSQVMKTRLEADEVAAQLERCDKENKMLKDEmNKEIEAARRQFQSQLADLQQL----PDILKITEAKLAECQDQLQGY 601
Cdd:TIGR04523 593 QKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE-NEKLSSIIKNIKSKKNKLKQEvkqiKETIKEIRNKWPEIIKKIKES 671
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039759465 602 ERKNIDLTAIISD------------LRSRIEHQgdKLEMAREKHQASQKENKQLSQKVDELE 651
Cdd:TIGR04523 672 KTKIDDIIELMKDwlkelslhykkyITRMIRIK--DLPKLEEKYKEIEKELKKLDEFSKELE 731
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
100-399 |
4.54e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 100 KMNRYDKKIDSLMNAVGCLKSEVKMQKGERqmAKRFLEERKEELEEVAHEL--AETEHENTVLRHNIERIKEEKDFTMLQ 177
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEE--AKKADEAKKAEEAKKADEAkkAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 178 KKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTDintlTRQKELLLQKLSTFEETNRTLRDLLRE 257
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE----AKIKAEELKKAEEEKKKVEQLKKKEAE 1644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 258 QHCKEDSERLMEQQGTL----LKRLAEADSEKARLLLLLQDKDKEVEELLQEiqcEKAQAKTASELSKSMESMRGHLQaQ 333
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIkaaeEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK---EAEEAKKAEELKKKEAEEKKKAE-E 1720
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039759465 334 LRCKEAENSrlcMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEE 399
Cdd:PTZ00121 1721 LKKAEEENK---IKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
388-785 |
5.03e-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: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 388 RAQKERAEKSEEYAEQLHVQLADKDLYVAEaLSTLESWRSRY---NQVVKDKGDLELEIIVLNDRVTDL---VNQQQSLE 461
Cdd:COG3096 781 AAREKRLEELRAERDELAEQYAKASFDVQK-LQRLHQAFSQFvggHLAVAFAPDPEAELAALRQRRSELereLAQHRAQE 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 462 EKMREDRDSLVER---LHRQTAEYSAFKLE--NERLKASFAPMeDKLNQAHLEVQQLKASVKNYEGMIDNYKSqvmkTRL 536
Cdd:COG3096 860 QQLRQQLDQLKEQlqlLNKLLPQANLLADEtlADRLEELREEL-DAAQEAQAFIQQHGKALAQLEPLVAVLQS----DPE 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 537 EADEVAAQLERCDKENKMLKdemnKEIEA-----ARR---------QFQSQLADL-QQLPDILKITEAKLAECQDQLQGY 601
Cdd:COG3096 935 QFEQLQADYLQAKEQQRRLK----QQIFAlsevvQRRphfsyedavGLLGENSDLnEKLRARLEQAEEARREAREQLRQA 1010
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 602 ERKNIDLTAIISDLRSRiehqgdkLEMAREKHQASQKENKQLS------------QKVDELERKLEATSAQNVEFLQVIA 669
Cdd:COG3096 1011 QAQYSQYNQVLASLKSS-------RDAKQQTLQELEQELEELGvqadaeaeerarIRRDELHEELSQNRSRRSQLEKQLT 1083
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 670 KREEAIHQAQLRLeektrecgslaRQLESAIEDARRQVEQTKE-----QALSKERaaqskilDLETQLSRTK------TE 738
Cdd:COG3096 1084 RCEAEMDSLQKRL-----------RKAERDYKQEREQVVQAKAgwcavLRLARDN-------DVERRLHRRElaylsaDE 1145
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1039759465 739 LGQLRRTRDDADRRYQSRLQDLKDRLEQSEStNRSMQNYVQFLKASY 785
Cdd:COG3096 1146 LRSMSDKALGALRLAVADNEHLRDALRLSED-PRRPERKVQFYIAVY 1191
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
174-456 |
5.51e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.45 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 174 TMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKT----EKQMTCTDINTLTRQKELLLQKLSTFEETNR 249
Cdd:COG5022 780 GFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKtikrEKKLRETEEVEFSLKAEVLIQKFGRSLKAKK 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 250 TLRDLLREQhCKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQC---EKAQAKTA--SELSKSME 324
Cdd:COG5022 860 RFSLLKKET-IYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSdliENLEFKTEliARLKKLLN 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 325 SMRGHLQAQL-RCKEAENSRLCMQIKNLERSGNQHKAEV---EAIMEQLKELKQKGDRDKETLKKaIRAQKERAEKSEEY 400
Cdd:COG5022 939 NIDLEEGPSIeYVKLPELNKLHEVESKLKETSEEYEDLLkksTILVREGNKANSELKNFKKELAE-LSKQYGALQESTKQ 1017
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039759465 401 AEQLHVQLADKDlYVAEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQ 456
Cdd:COG5022 1018 LKELPVEVAELQ-SASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLR 1072
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
160-785 |
7.62e-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: 39.77 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 160 LRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDgaaaakqVMALKDTIGKLKTEKQMTCTDINTLTRQ------ 233
Cdd:pfam01576 101 MQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEED-------ILLLEDQNSKLSKERKLLEERISEFTSNlaeeee 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 234 KELLLQKLSTFEETNRT-LRDLLRE-----QHCKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQ 307
Cdd:pfam01576 174 KAKSLSKLKNKHEAMISdLEERLKKeekgrQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 308 CEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQL---KELKQKGDRDKETLK 384
Cdd:pfam01576 254 EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTaaqQELRSKREQEVTELK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 385 KAIRAQKERAEKSEEYAEQLHVQladkdlyvaealsTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKm 464
Cdd:pfam01576 334 KALEEETRSHEAQLQEMRQKHTQ-------------ALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQA- 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 465 REDRDSLVERLHRQTAEYSAFKLENERLKASFApmeDKLNQAHLEVQQLKASVKNYEGM-------IDNYKSQVMKTRLE 537
Cdd:pfam01576 400 KQDSEHKRKKLEGQLQELQARLSESERQRAELA---EKLSKLQSELESVSSLLNEAEGKniklskdVSSLESQLQDTQEL 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 538 ADEVAAQLERCDKENKMLKDEMN------KEIEAARRQFQSQLADLQ-QLPDILKITEAKLAECQDQLQGYERKNIDLTA 610
Cdd:pfam01576 477 LQEETRQKLNLSTRLRQLEDERNslqeqlEEEEEAKRNVERQLSTLQaQLSDMKKKLEEDAGTLEALEEGKKRLQRELEA 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 611 IISDLRSRIEhQGDKLEMAREKHQASQK----ENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKT 686
Cdd:pfam01576 557 LTQQLEEKAA-AYDKLEKTKNRLQQELDdllvDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKE 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 687 RECGSLARQLESAIEdARRQVEQTKEQAlskeRAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQ 766
Cdd:pfam01576 636 TRALSLARALEEALE-AKEELERTNKQL----RAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQA 710
|
650
....*....|....*....
gi 1039759465 767 SESTNRSMQNYVQFLKASY 785
Cdd:pfam01576 711 TEDAKLRLEVNMQALKAQF 729
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
416-737 |
9.31e-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: 39.29 E-value: 9.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 416 AEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRD--SLVERLHRQTAEYSAfKLENERLK 493
Cdd:pfam05622 127 SDKVKKLEATVETYKKKLEDLGDLRRQVKLLEERNAEYMQRTLQLEEELKKANAlrGQLETYKRQVQELHG-KLSEESKK 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 494 ASFAPMEDKLNQAHLE---------------------------VQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLE 546
Cdd:pfam05622 206 ADKLEFEYKKLEEKLEalqkekerliierdtlretneelrcaqLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 547 RCDKENKMLKdemnkeiEAARRQFQSQLADLQQLpdiLKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGD-- 624
Cdd:pfam05622 286 RLQHENKMLR-------LGQEGSYRERLTELQQL---LEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSka 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039759465 625 --------KLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAqlrLEEKTRECGSLARQL 696
Cdd:pfam05622 356 edssllkqKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEALRKKDEDMKA---MEERYKKYVEKAKSV 432
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1039759465 697 ESAIEDARRQVEQTKEQALSKERAAQSK-ILDLETQLSRTKT 737
Cdd:pfam05622 433 IKTLDPKQNPASPPEIQALKNQLLEKDKkIEHLERDFEKSKL 474
|
|
| |
