|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
95-759 |
1.66e-16 |
|
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: 84.34 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 95 KMNRYDKKIDSLMNAVGCLKSEVKMQKGERQMAKRFLEERKEELEEVAHELAETEHENTVLRHNIERIKEEKDFTMLQKK 174
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 175 HLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETNRTLRDLLREQH 254
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 255 CKEDSERLmeqqGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQ-AQLRCKE 333
Cdd:TIGR02168 435 LKELQAEL----EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgFSEGVKA 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 334 AENSRLCM-----QIKNLERSGNQHKAEVEA---------IMEQLKELKQKGDRDKETLK--------KAIRAQKERAEK 391
Cdd:TIGR02168 511 LLKNQSGLsgilgVLSELISVDEGYEAAIEAalggrlqavVVENLNAAKKAIAFLKQNELgrvtflplDSIKGTEIQGND 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 392 SEEYAEQLHVQLADKDL--YVAEALSTLESWRSRYnqVVKDKGDLELEIIVLNDR----VT---DLVNQQQSLEEKMRED 462
Cdd:TIGR02168 591 REILKNIEGFLGVAKDLvkFDPKLRKALSYLLGGV--LVVDDLDNALELAKKLRPgyriVTldgDLVRPGGVITGGSAKT 668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 463 RDSLVERlhrqtaeysafKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDnyksqvmktrlEADEVAAQLER 542
Cdd:TIGR02168 669 NSSILER-----------RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE-----------QLRKELEELSR 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 543 CDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLE 622
Cdd:TIGR02168 727 QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 623 MAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAiEDARRQV 702
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL-LNERASL 885
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 703 EQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQS---RLQDLKDRL 759
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGlevRIDNLQERL 945
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
203-761 |
2.51e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 203 ALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETNRTLRDLLREQhcKEDSERLMEQQGTLLKRLAEADSEKAR 282
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL--LAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 283 LllllqdkDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIME 362
Cdd:COG1196 321 L-------EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 363 QLKELKQKgdrdKETLKKAIRAQKERAEKSEEYAEQLHVQLadkdlyvAEALSTLESWRSRYNQVVKDKGDLELEIIVLN 442
Cdd:COG1196 394 AAAELAAQ----LEELEEAEEALLERLERLEEELEELEEAL-------AELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 443 DRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAP-MEDKLNQAHLEVQQLKASVKNYEGMIDN 521
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAlLLAGLRGLAGAVAVLIGVEAAYEAALEA 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 522 YKSQVMKTRL-EADEVAAQLERCDKENKMLKDE---MNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYE 597
Cdd:COG1196 543 ALAAALQNIVvEDDEVAAAAIEYLKAAKAGRATflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 598 RKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRL 677
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 678 EEktrecgslARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKD 757
Cdd:COG1196 703 EE--------EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
....
gi 1907136624 758 RLEQ 761
Cdd:COG1196 775 EIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
345-718 |
9.53e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 9.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 345 NLERsgnqhkaeVEAIMEQLkelkqkgDRDKETLKKairaQKERAEKSEEYAEQLhvQLADKDLYVAealstleswrsRY 424
Cdd:COG1196 187 NLER--------LEDILGEL-------ERQLEPLER----QAEKAERYRELKEEL--KELEAELLLL-----------KL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 425 NQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDSLVE---RLHRQTAEYSAFKLENERLKASFAPMEDKLNQA 501
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEElelELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 502 HLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLErcdkenkmlkdemnkEIEAARRQFQSQLADLqqlpdilki 581
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELE---------------EAEAELAEAEEALLEA--------- 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 582 tEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQ 661
Cdd:COG1196 371 -EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907136624 662 VIAKREEAIHQAQLRLEEKTREcgslARQLESAIEDARRQVEQTKEQALSKERAAQS 718
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEE----AALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
441-764 |
3.20e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 441 LNDRVTDLVNQQQSLEEKMR--EDRDSLVERLHRQTAEYSAFKLEneRLKASFAPMEDKLNQAHLEVQQLKASVKNYEGM 518
Cdd:COG1196 191 LEDILGELERQLEPLERQAEkaERYRELKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 519 IDNYKSQVMKTRLEADEVAAQLERCDKEnkmlKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYER 598
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAE----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 599 KNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQnvefLQVIAKREEAIHQAQLRLE 678
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ----LEELEEAEEALLERLERLE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 679 EKTRECGSLARQLESAIEDARRQVEQTKE---QALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDL 755
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEeeaELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
....*....
gi 1907136624 756 KDRLEQSES 764
Cdd:COG1196 501 ADYEGFLEG 509
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
228-783 |
1.30e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 228 QKELLLQKLSTFEETNRTLRDLLREQhcKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQcekaq 307
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEA--EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS----- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 308 aktaselskSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKE 387
Cdd:TIGR02168 299 ---------RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 388 RAEKSEEYAEQLHvQLADKdlyVAEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLE-EKMREDRDSL 466
Cdd:TIGR02168 370 LESRLEELEEQLE-TLRSK---VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEEL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 467 VERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKS------QVMKTRLEAD------ 534
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegvkALLKNQSGLSgilgvl 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 535 ----EVAAQLERC---------------DKENKMLKDEMNKEIEAARRQF------------QSQLADLQQLPDILKITe 583
Cdd:TIGR02168 526 seliSVDEGYEAAieaalggrlqavvveNLNAAKKAIAFLKQNELGRVTFlpldsikgteiqGNDREILKNIEGFLGVA- 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 584 AKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQ-------------GDKL----------EMAREKHQASQKENKQLSQ 640
Cdd:TIGR02168 605 KDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAkklrpgyrivtldGDLVrpggvitggsAKTNSSILERRREIEELEE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 641 KVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESA------IEDARRQVEQTKEQALSKER 714
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeveqLEERIAQLSKELTELEAEIE 764
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907136624 715 AAQSKILDLETQLSRTKTELGQLrrtrddadrryQSRLQDLKDRLEQSESTNRSMQNYVQFLKASYANV 783
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEEL-----------EAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
228-679 |
2.58e-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: 64.37 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 228 QKELLLQKLSTFEETNRTLRDLLRE-QHCKEDSERLMEQQGTLLK-RLAEADSEKARLLLLLQDKDKEVEELL------- 298
Cdd:pfam15921 311 QNSMYMRQLSDLESTVSQLRSELREaKRMYEDKIEELEKQLVLANsELTEARTERDQFSQESGNLDDQLQKLLadlhkre 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 299 QEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERS-GNQHKAEVEAI------MEQLKELKQKG 371
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIqgknesLEKVSSLTAQL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 372 DRDKETLKKAIR---AQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYN------QVVKDKGD------LEL 436
Cdd:pfam15921 471 ESTKEMLRKVVEeltAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDlklqelQHLKNEGDhlrnvqTEC 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 437 EIIVLN---------------DRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQA 501
Cdd:pfam15921 551 EALKLQmaekdkvieilrqqiENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 502 HLEVQQLK-------ASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQQ 574
Cdd:pfam15921 631 ELEKVKLVnagserlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 575 LPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKV-------DELER 647
Cdd:pfam15921 711 TRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELstvatekNKMAG 790
|
490 500 510
....*....|....*....|....*....|..
gi 1907136624 648 KLEATSAQNVEFLQVIAKREEAIHQAQLRLEE 679
Cdd:pfam15921 791 ELEVLRSQERRLKEKVANMEVALDKASLQFAE 822
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
334-704 |
4.51e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.54 E-value: 4.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 334 AENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEA 413
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 414 LSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMredrDSLVERLHRQTAEYSAFKLENERLKASFAP 493
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL----DELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 494 MEDKLNQAHLEVQQLKASVKNYEGMIDNYksqvmktRLEADEVAAQLERCDKEnkmlKDEMNKEIEAARRQFQSQLADLQ 573
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEEL-------EELIEELESELEALLNE----RASLEEALALLRSELEELSEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 574 QLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRI-EHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEAT 652
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907136624 653 SAQNVEFLQVIAKREEaihqaqlRLEEKTRECGSLAR---QLESAIEDARRQVEQ 704
Cdd:TIGR02168 985 GPVNLAAIEEYEELKE-------RYDFLTAQKEDLTEakeTLEEAIEEIDREARE 1032
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
529-767 |
1.16e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 529 TRLEA--DEVAAQLERCDKE------NKMLKDEMN-KEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERK 599
Cdd:COG1196 189 ERLEDilGELERQLEPLERQaekaerYRELKEELKeLEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 600 NIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEE 679
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 680 KTRECGSLARQLESAiEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRL 759
Cdd:COG1196 349 AEEELEEAEAELAEA-EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
....*...
gi 1907136624 760 EQSESTNR 767
Cdd:COG1196 428 EALAELEE 435
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-514 |
2.72e-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: 60.84 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 174 KHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQmtctdinTLTRQKELLLQKLSTFEETNRTLRDLLREQ 253
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-------ELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 254 HckEDSERLMEQQGTLLKRLAEADSEKArlllllqdkdkeveELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKE 333
Cdd:TIGR02168 753 S--KELTELEAEIEELEERLEEAEEELA--------------EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 334 AENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQkgdrDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEA 413
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSE----DIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 414 LSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKmredRDSLVERLhrqTAEYSafkLENERLKASFAP 493
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR----IDNLQERL---SEEYS---LTLEEAEALENK 962
|
330 340
....*....|....*....|.
gi 1907136624 494 MEDKLNQAHLEVQQLKASVKN 514
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
149-786 |
4.52e-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: 60.08 E-value: 4.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 149 EHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTC-TDINTLTR 227
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVkEKIGELEA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 228 QKELLLQKLstfEETNRTLRDLL-REQHCKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKA 306
Cdd:TIGR02169 302 EIASLERSI---AEKERELEDAEeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 307 QAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELkqkgDRDKETLKKAIRAQK 386
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL----EEEKEDKALEIKKQE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 387 ERAEKSEEYAEQLHVQLADKdlyvaealstleswRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQ---SLEEKMREDR 463
Cdd:TIGR02169 455 WKLEQLAADLSKYEQELYDL--------------KEEYDRVEKELSKLQRELAEAEAQARASEERVRggrAVEEVLKASI 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 464 DS---LVERLHRQTAEYsAFKLE---NERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEV- 536
Cdd:TIGR02169 521 QGvhgTVAQLGSVGERY-ATAIEvaaGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVi 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 537 --AAQLERCDKENK-----MLKDEMNKE-IEAARRQF---------------------------------QSQLADLQQL 575
Cdd:TIGR02169 600 gfAVDLVEFDPKYEpafkyVFGDTLVVEdIEAARRLMgkyrmvtlegelfeksgamtggsraprggilfsRSEPAELQRL 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 576 PDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQ 655
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 656 NVEFLQVIAKREEAIHQAQLRLEE-KTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLEtQLSRTKTEL 734
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE-YLEKEIQEL 838
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1907136624 735 GQLRRTRDDADRRYQSRLQDLKDRLEQSESTNRSMQNYVQFLKASYANVFGD 786
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
262-761 |
9.63e-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: 59.08 E-value: 9.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 262 LMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTA-----SELSKSMESMRGHLQAQLRCKEAEN 336
Cdd:pfam12128 267 YKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAvakdrSELEALEDQHGAFLDADIETAAADQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 337 SRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADkdlyvaeALST 416
Cdd:pfam12128 347 EQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAED-------DLQA 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 417 LES-WRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKM--REDRDSLVER----LHRQTAEYSAFKLENERLKA 489
Cdd:pfam12128 420 LESeLREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLlqLENFDERIERareeQEAANAEVERLQSELRQARK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 490 SFAPMEDKLNQAHLEVQQLKASVKNYEGMID----------NYKSQVMKTRLEADEVAAQLERCDkenkmLKDEMNKEIE 559
Cdd:pfam12128 500 RRDQASEALRQASRRLEERQSALDELELQLFpqagtllhflRKEAPDWEQSIGKVISPELLHRTD-----LDPEVWDGSV 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 560 AARRQFQSQLADLQQL--PDILKITEAklaecqdqlqgyerknidltaiisdLRSRIEHQGDKLEMAREKHQASQKENKQ 637
Cdd:pfam12128 575 GGELNLYGVKLDLKRIdvPEWAASEEE-------------------------LRERLDKAEEALQSAREKQAAAEEQLVQ 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 638 LSQKVDELERKLEatsaqnveflqvIAKReeAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQAlskerAAQ 717
Cdd:pfam12128 630 ANGELEKASREET------------FART--ALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSL-----EAQ 690
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1907136624 718 SKILDLETQLSRTKTElGQLRRTRDDADRRYQSRLQDLKDRLEQ 761
Cdd:pfam12128 691 LKQLDKKHQAWLEEQK-EQKREARTEKQAYWQVVEGALDAQLAL 733
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
184-701 |
1.75e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 184 MSKLVEAEMDGAAAAKQVMALKDTIGKlktekqmtCTDINTLTRQKELLLQKLSTFE-ETNRTLRDLLREQ--HCKEDSE 260
Cdd:COG4913 234 FDDLERAHEALEDAREQIELLEPIREL--------AERYAAARERLAELEYLRAALRlWFAQRRLELLEAEleELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 261 RLMEQQGTLLKRLAEADSEKAR-LLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRL 339
Cdd:COG4913 306 RLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 340 CMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQL------HVQLADKDL-YVAE 412
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALrdalaeALGLDEAELpFVGE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 413 AL---STLESWRS------------------RYNQVVK--DKGDLELEIivlndrVTDLVNQQQSLEEKMREDRDSLVER 469
Cdd:COG4913 466 LIevrPEEERWRGaiervlggfaltllvppeHYAAALRwvNRLHLRGRL------VYERVRTGLPDPERPRLDPDSLAGK 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 470 LHRQTAEYSAFkLENErLKASFAPM----EDKLNQAHLEVQQlkasvknyEGMI-DNYKSQVMKTRLEADEV-------A 537
Cdd:COG4913 540 LDFKPHPFRAW-LEAE-LGRRFDYVcvdsPEELRRHPRAITR--------AGQVkGNGTRHEKDDRRRIRSRyvlgfdnR 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 538 AQLERCDKENKMLKDEMN------KEIEAARRQFQSQLADLQQLPDI------LKITEAKLAECQDQLQGYERKNIDLTA 605
Cdd:COG4913 610 AKLAALEAELAELEEELAeaeerlEALEAELDALQERREALQRLAEYswdeidVASAEREIAELEAELERLDASSDDLAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 606 I---ISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATS--AQNVEFLQVIAKREEAI---HQAQLR- 676
Cdd:COG4913 690 LeeqLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEdlARLELRALLEERFAAALgdaVERELRe 769
|
570 580
....*....|....*....|....*.
gi 1907136624 677 -LEEKTRECGSLARQLESAIEDARRQ 701
Cdd:COG4913 770 nLEERIDALRARLNRAEEELERAMRA 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
443-767 |
2.57e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 443 DRVTDLVN----QQQSLEEKMRedrdsLVERLHRQTAEYSAfkLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGM 518
Cdd:TIGR02168 189 DRLEDILNelerQLKSLERQAE-----KAERYKELKAELRE--LELALLVLRLEELREELEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 519 IDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNkEIEAARRQFQSQLADLQQlpdilkiteaKLAECQDQLQGYER 598
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEIS-RLEQQKQILRERLANLER----------QLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 599 KNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATS---AQNVEFLQVIAKR----EEAIH 671
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRskvAQLELQIASLNNEierlEARLE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 672 QAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSR 751
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
330
....*....|....*.
gi 1907136624 752 LQDLKDRLEQSESTNR 767
Cdd:TIGR02168 491 LDSLERLQENLEGFSE 506
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
144-651 |
4.60e-08 |
|
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: 56.95 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 144 ELAETEHENTVLRHNIERIKEE---KDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCT 220
Cdd:TIGR04523 174 ELNLLEKEKLNIQKNIDKIKNKllkLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQT 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 221 DINTLTRQ----KELLLQKLSTFEETNRTLRDLlreqhckedserlMEQQGTLLKRLAEADSEKArlllllQDKDKEVEE 296
Cdd:TIGR04523 254 QLNQLKDEqnkiKKQLSEKQKELEQNNKKIKEL-------------EKQLNQLKSEISDLNNQKE------QDWNKELKS 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 297 LLQEIQCEKAQAKTasELSKSMESMrghlqaqlrckeaenSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKgdrdKE 376
Cdd:TIGR04523 315 ELKNQEKKLEEIQN--QISQNNKII---------------SQLNEQISQLKKELTNSESENSEKQRELEEKQNE----IE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 377 TLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLE 456
Cdd:TIGR04523 374 KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 457 ---EKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEA 533
Cdd:TIGR04523 454 liiKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEK 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 534 DEVAAQLErcDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSR 613
Cdd:TIGR04523 534 KEKESKIS--DLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKK 611
|
490 500 510
....*....|....*....|....*....|....*...
gi 1907136624 614 IEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEA 651
Cdd:TIGR04523 612 ISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
290-627 |
6.02e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 290 KDKEVEELLQEI--------QCEKAQAKTASELSkSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIM 361
Cdd:TIGR02168 675 RRREIEELEEKIeeleekiaELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 362 EQLKELKQKgdrdketlkkaIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIVL 441
Cdd:TIGR02168 754 KELTELEAE-----------IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 442 NDRVTDLVNQQQSLEEKMREdrdsLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDN 521
Cdd:TIGR02168 823 RERLESLERRIAATERRLED----LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 522 YKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKeIEAARRQFQSQLADLQQ--LPDILK---ITEAKLAECQDQLQGY 596
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSltLEEAEAlenKIEDDEEEARRRLKRL 977
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1907136624 597 ERK-----NIDLTAI--ISDLRSR---IEHQGDKLEMAREK 627
Cdd:TIGR02168 978 ENKikelgPVNLAAIeeYEELKERydfLTAQKEDLTEAKET 1018
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
197-783 |
7.17e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 7.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 197 AAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETnrtlrdLLREQHCKEDSERLMEQQGTLLKRLAEA 276
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEV------LEEHEERREELETLEAEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 277 DSEKARLLLLLQDKDKEVEELLQEIQ-------CEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERS 349
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDdllaeagLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 350 GNQHKAEVEAIMEQLKELkqkgDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVK 429
Cdd:PRK02224 351 ADDLEERAEELREEAAEL----ESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 430 DKGDLELEIIVLNDRVTDlvNQQ-----------QSLEEKMR----EDRDSLVERLhrqTAEYSAFKLENERLKASFAPM 494
Cdd:PRK02224 427 REAELEATLRTARERVEE--AEAlleagkcpecgQPVEGSPHvetiEEDRERVEEL---EAELEDLEEEVEEVEERLERA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 495 EDkLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQlercdkenkmlKDEMNKEIEAARRQFQSQLADLQQ 574
Cdd:PRK02224 502 ED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER-----------AAELEAEAEEKREAAAEAEEEAEE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 575 LPDILKITEAKLAECQDQLQGYERknidltaiISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDEL-ERKLEATS 653
Cdd:PRK02224 570 AREEVAELNSKLAELKERIESLER--------IRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKrERKRELEA 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 654 AQNveflqviakrEEAIHQAQLRLEektrecgslarQLESAIEDARRQVEQTKEqalsKERAAQSKILDLETQLSRtkte 733
Cdd:PRK02224 642 EFD----------EARIEEAREDKE-----------RAEEYLEQVEEKLDELRE----ERDDLQAEIGAVENELEE---- 692
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1907136624 734 lgqlrrtrddadrryqsrLQDLKDRLEQSESTnrsmqnyVQFLKASYANV 783
Cdd:PRK02224 693 ------------------LEELRERREALENR-------VEALEALYDEA 717
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
262-774 |
8.53e-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: 56.21 E-value: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 262 LMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLR-CKEAENSRLC 340
Cdd:TIGR00606 417 LQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAEReLSKAEKNSLT 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 341 MQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEE-------YAEQLHVQLADKDlYVAEA 413
Cdd:TIGR00606 497 ETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQirkiksrHSDELTSLLGYFP-NKKQL 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 414 LSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMR------------EDRDSLVERLHRQ-------- 473
Cdd:TIGR00606 576 EDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSsyedklfdvcgsQDEESDLERLKEEieksskqr 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 474 ------TAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKN----YEGMIDNYKSQVMKTRLEADEVAAQLERC 543
Cdd:TIGR00606 656 amlagaTAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSklrlAPDKLKSTESELKKKEKRRDEMLGLAPGR 735
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 544 DKEnkmlKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTaIISDLRSRIEHQGDKLEM 623
Cdd:TIGR00606 736 QSI----IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVT-IMERFQMELKDVERKIAQ 810
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 624 AREKHQAS--QKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQ 701
Cdd:TIGR00606 811 QAAKLQGSdlDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQL 890
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907136624 702 VEQTKE-QALSKE-RAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQSESTNRSMQNYVQ 774
Cdd:TIGR00606 891 VELSTEvQSLIREiKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ 965
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
473-714 |
1.04e-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: 54.77 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 473 QTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLercdKENKMLKD 552
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL----AELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 553 EMNKEIEAARRQFQSQLADLQQLPdilKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQ 632
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLG---RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 633 KENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSK 712
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
..
gi 1907136624 713 ER 714
Cdd:COG4942 251 LK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
536-768 |
2.54e-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: 53.61 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 536 VAAQLERCDKENKMLKdEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIE 615
Cdd:COG4942 15 AAAQADAAAEAEAELE-QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 616 HQGDKLEmAREKHQASQKENKQLSQKVDELERKLEATSAQNV--------EFLQVIAKREEAIHQAQLRLEEKTRECGSL 687
Cdd:COG4942 94 ELRAELE-AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAvrrlqylkYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 688 ARQLESAIEDARRQveqtkEQALSKERAAQSKIL-DLETQLSRTKTELGQLRRTrddadrryQSRLQDLKDRLEQSESTN 766
Cdd:COG4942 173 RAELEALLAELEEE-----RAALEALKAERQKLLaRLEKELAELAAELAELQQE--------AEELEALIARLEAEAAAA 239
|
..
gi 1907136624 767 RS 768
Cdd:COG4942 240 AE 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
269-713 |
2.58e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 269 LLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLE- 347
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 348 -RSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQ 426
Cdd:COG4717 131 yQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 427 VVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPM------------ 494
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlflvlgllallf 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 495 ------EDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVM-KTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQS 567
Cdd:COG4717 291 lllareKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 568 QLADLQQLPDIlkITEAKLAECQDQLQGYErkniDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENK--QLSQKVDEL 645
Cdd:COG4717 371 EIAALLAEAGV--EDEEELRAALEQAEEYQ----ELKEELEELEEQLEELLGELEELLEALDEEELEEEleELEEELEEL 444
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136624 646 ERKLEATSAQNVEFLQVI--AKREEAIHQAQLRLEEKTRECGSLARQ------LESAIEDARRQVEQTKEQALSKE 713
Cdd:COG4717 445 EEELEELREELAELEAELeqLEEDGELAELLQELEELKAELRELAEEwaalklALELLEEAREEYREERLPPVLER 520
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
441-760 |
4.91e-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: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 441 LNDRVTDLVNQQQSLEEKMRE---DRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEG 517
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRienRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 518 MIDNYKSQVMKTRLEADEVAAQLERC-DKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGY 596
Cdd:TIGR02169 759 ELKELEARIEELEEDLHKLEEALNDLeARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 597 ERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLR 676
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 677 LEEKTRECGSLARQLeSAIEDARRQVEQTKEQALSKERaAQSKILDLETQLSRtkteLGQLRRTRDDADRRYQSRLQDLK 756
Cdd:TIGR02169 919 LSELKAKLEALEEEL-SEIEDPKGEDEEIPEEELSLED-VQAELQRVEEEIRA----LEPVNMLAIQEYEEVLKRLDELK 992
|
....
gi 1907136624 757 DRLE 760
Cdd:TIGR02169 993 EKRA 996
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
345-759 |
5.85e-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: 53.42 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 345 NLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKA----IRAQkERAEKSEEYAEQLHVQLADkdlyVAEALSTLESW 420
Cdd:COG3096 337 NLVQTALRQQEKIERYQEDLEELTERLEEQEEVVEEAaeqlAEAE-ARLEAAEEEVDSLKSQLAD----YQQALDVQQTR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 421 RSRYNQVVKDKGDL-------ELEIIVLNDRVTDLVNQQQSLEEKMR--EDRDSLVERLHRQTAEysAFKLenerlkasf 491
Cdd:COG3096 412 AIQYQQAVQALEKAralcglpDLTPENAEDYLAAFRAKEQQATEEVLelEQKLSVADAARRQFEK--AYEL--------- 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 492 apmedklnqahleVQQLKASVknyegmidnyksqvmkTRLEADEVAAQLERCDKENKMLkdemnkeieAARR-QFQSQLA 570
Cdd:COG3096 481 -------------VCKIAGEV----------------ERSQAWQTARELLRRYRSQQAL---------AQRLqQLRAQLA 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 571 DLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELerkle 650
Cdd:COG3096 523 ELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKEL----- 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 651 atsaqnveflqviAKREEAIHQAQLRLEektrecgSLARQLESAIEDArRQVEQTKEQALSKERAAQSkildLETQLSRT 730
Cdd:COG3096 598 -------------AARAPAWLAAQDALE-------RLREQSGEALADS-QEVTAAMQQLLEREREATV----ERDELAAR 652
|
410 420
....*....|....*....|....*....
gi 1907136624 731 KTELGQLRRTRDDADRRYQSRLQDLKDRL 759
Cdd:COG3096 653 KQALESQIERLSQPGGAEDPRLLALAERL 681
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
352-651 |
9.69e-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: 52.76 E-value: 9.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 352 QHKAEVEAIMEQLKELKQKGDRdKETLKKAIRAQKERAEKSEEYAEQLHVQLADK-DLYVAEALSTLESWRSRYNQVVKD 430
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIER-LDLIIDEKRQQLERLRREREKAERYQALLKEKrEYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 431 KGDLELEIIVLNDRVTDLVNQQQSLEEKMREdrdsLVERLHRQTA-EYSAFKLENERLKASFAPMEDKLNQAHLEVQQLK 509
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEE----LNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 510 ASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMN------------------------KEIEAARRQF 565
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEdlraeleevdkefaetrdelkdyrEKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 566 QSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMA--------------REKHQAS 631
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLaadlskyeqelydlKEEYDRV 481
|
330 340
....*....|....*....|
gi 1907136624 632 QKENKQLSQKVDELERKLEA 651
Cdd:TIGR02169 482 EKELSKLQRELAEAEAQARA 501
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
552-761 |
1.72e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 552 DEMNKEIEAARRQfQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTaiISDLRSRIEHQGDKLEMAREKHQAS 631
Cdd:COG4913 238 ERAHEALEDAREQ-IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR--LELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 632 QKENKQLSQKVDELERKLEATSAQNVEFLqviakrEEAIHQAQLRLEEKTRECGSLARQL----------ESAIEDARRQ 701
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQL------EREIERLERELEERERRRARLEALLaalglplpasAEEFAALRAE 388
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907136624 702 VEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRR---TRDDADRRYQSRLQDLKDRLEQ 761
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAeiaSLERRKSNIPARLLALRDALAE 451
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
98-703 |
3.62e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 98 RYDKKIDSLMNAVGCLKSEVKMQKGERQMAKRFLEERKEELEEVAHELAETEHEntvlrhnIERIKEEKDFTMLQKKHLQ 177
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE-------LARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 178 QEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMtctdintltrQKELLLQKLSTFEETNRTLRDLLREQhcke 257
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE----------AEAELAEAEEALLEAEAELAEAEEEL---- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 258 dsERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASElsksmesmrghLQAQLRCKEAENS 337
Cdd:COG1196 382 --EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE-----------EEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 338 RLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQ-LHVQLADKDLYVAEALST 416
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvKAALLLAGLRGLAGAVAV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 417 LESWRSRYNQVVkdkgdLELEIIVLNDRVTDLVNQQQSLEEKMREDRDSLVERlhrqtaeysafkLENERLKASFAPMED 496
Cdd:COG1196 529 LIGVEAAYEAAL-----EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATF------------LPLDKIRARAALAAA 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 497 KLNQAHLEVQQLKASVKNYEGMIDnykSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQQLP 576
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARY---YVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 577 DILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQN 656
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1907136624 657 VEFLQVIAKREEAIHQAQLRLEEktrecgsLARQLES-------AIEDARRQVE 703
Cdd:COG1196 749 EEEALEELPEPPDLEELERELER-------LEREIEAlgpvnllAIEEYEELEE 795
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
239-774 |
4.24e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 239 FEETNRTLRDLLREQHCKEDSERLMEQQGTLLK---RLAEADSEKA-----RLLLLLQDKDKEVEELLQEIQCEKAQAKT 310
Cdd:COG4913 234 FDDLERAHEALEDAREQIELLEPIRELAERYAAareRLAELEYLRAalrlwFAQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 311 ASELSKSMESMRGHLQAQLRCKEAEN-SRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERA 389
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 390 EKSEEYAEQLHVQLADkdlyvaealstlesWRSRYNQVVKDKGDLELEIIVLNDRVT----DLVNQQQSLEEKMREDRDS 465
Cdd:COG4913 394 EALEEELEALEEALAE--------------AEAALRDLRRELRELEAEIASLERRKSnipaRLLALRDALAEALGLDEAE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 466 L-------------------VER-LHRQtaeysAFKL--ENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYK 523
Cdd:COG4913 460 LpfvgelievrpeeerwrgaIERvLGGF-----ALTLlvPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 524 SQVMKTRLEADEVAA-------------------QLERCDK---ENKMLKD-----EMNKEIEAARRQF-----QSQLAD 571
Cdd:COG4913 535 SLAGKLDFKPHPFRAwleaelgrrfdyvcvdspeELRRHPRaitRAGQVKGngtrhEKDDRRRIRSRYVlgfdnRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 572 LqqlpdilkitEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGdklemAREKHQASQKENKQLSQKVDELERKLEA 651
Cdd:COG4913 615 L----------EAELAELEEELAEAEERLEALEAELDALQERREALQ-----RLAEYSWDEIDVASAEREIAELEAELER 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 652 TSAQNVEfLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQAlskERAAQSKILDLETQLSRTK 731
Cdd:COG4913 680 LDASSDD-LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL---EAAEDLARLELRALLEERF 755
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1907136624 732 TELGQlRRTRDDADRRYQSRLQDLKDRLEQSEST-NRSMQNYVQ 774
Cdd:COG4913 756 AAALG-DAVERELRENLEERIDALRARLNRAEEElERAMRAFNR 798
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
290-613 |
5.92e-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: 50.07 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 290 KDKEVEELLQEIQCEKAQAKtASELSKSMESMRghlqAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKEL-- 367
Cdd:TIGR02169 205 REREKAERYQALLKEKREYE-GYELLKEKEALE----RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnk 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 368 --KQKGDRDKETLKKAIR---AQKERAEKS----EEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEI 438
Cdd:TIGR02169 280 kiKDLGEEEQLRVKEKIGeleAEIASLERSiaekERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 439 IVLNDRVTDLVNQQQSLEEKMREDRDSLVERlhrqTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGM 518
Cdd:TIGR02169 360 AELKEELEDLRAELEEVDKEFAETRDELKDY----REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 519 IdnyksqvmkTRLEADevaaqlercdkenkmlKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYER 598
Cdd:TIGR02169 436 I---------NELEEE----------------KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
330
....*....|....*
gi 1907136624 599 KNIDLTAIISDLRSR 613
Cdd:TIGR02169 491 ELAEAEAQARASEER 505
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
160-770 |
1.38e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.96 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 160 ERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTF 239
Cdd:pfam15921 92 RRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 240 EETNRTLRdLLREQHCKEDSERLMEQQGTLLKRLAEADSekaRLLLLLQDKDKEVEELLQEIQCEkaqaktASELSKSME 319
Cdd:pfam15921 172 IEQLRKMM-LSHEGVLQEIRSILVDFEEASGKKIYEHDS---MSTMHFRSLGSAISKILRELDTE------ISYLKGRIF 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 320 SMRGHLQAqLRCKEAENSRLCMQIKN--LERSGNQHKAEVEAIMEQLKELKQKGDrdketlkkAIRAQKERAEKSEEYAE 397
Cdd:pfam15921 242 PVEDQLEA-LKSESQNKIELLLQQHQdrIEQLISEHEVEITGLTEKASSARSQAN--------SIQSQLEIIQEQARNQN 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 398 QLHV-QLADKDLYVAEALSTLESWRSRYNQVVKDkgdLELEIIVLNDRVTDLVNQQQSLEEK---MREDRDSLVERLHRQ 473
Cdd:pfam15921 313 SMYMrQLSDLESTVSQLRSELREAKRMYEDKIEE---LEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLHKR 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 474 TAEYSAFKLENERL-------KASFAPMEDKLNQAHLEVQQLKASVKnyegmidnyksqVMKTRLEAdEVAAQLERCDKE 546
Cdd:pfam15921 390 EKELSLEKEQNKRLwdrdtgnSITIDHLRRELDDRNMEVQRLEALLK------------AMKSECQG-QMERQMAAIQGK 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 547 NKMLK--DEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMA 624
Cdd:pfam15921 457 NESLEkvSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 625 R---EKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVI--------------AKREEAIHQAQLRLEE----KTRE 683
Cdd:pfam15921 537 KnegDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVgqhgrtagamqvekAQLEKEINDRRLELQEfkilKDKK 616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 684 CGSLaRQLESAIED-----------------ARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADR 746
Cdd:pfam15921 617 DAKI-RELEARVSDlelekvklvnagserlrAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTN 695
|
650 660
....*....|....*....|....
gi 1907136624 747 RYQSRLQDLKDRLEQSESTNRSMQ 770
Cdd:pfam15921 696 KLKMQLKSAQSELEQTRNTLKSME 719
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
519-782 |
1.56e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 519 IDNYKSQVMKTRLEADEVAAQLERCD-------KENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQD 591
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDliidekrQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 592 QLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQA-SQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAI 670
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 671 HQAQLRLEEKTREcgslARQLESAIEDARRQVEQTKEQALSKE---RAAQSKILDLETQLSRTKTELGQlrrtrddadrr 747
Cdd:TIGR02169 325 AKLEAEIDKLLAE----IEELEREIEEERKRRDKLTEEYAELKeelEDLRAELEEVDKEFAETRDELKD----------- 389
|
250 260 270
....*....|....*....|....*....|....*
gi 1907136624 748 YQSRLQDLKDRLEQSESTNRSMQNYVQFLKASYAN 782
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
195-753 |
1.69e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.43 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 195 AAAAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETNRTLRDLLREQhckEDSERLMEQQGTLLKRLA 274
Cdd:TIGR00618 296 AAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQE---IHIRDAHEVATSIREISC 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 275 EADSEKARLLLLLQDK--DKEVEELL-QEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQ---IKNLER 348
Cdd:TIGR00618 373 QQHTLTQHIHTLQQQKttLTQKLQSLcKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCaaaITCTAQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 349 SGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQ--------LHVQLADKDLYVAEALStlesw 420
Cdd:TIGR00618 453 CEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcplcgscIHPNPARQDIDNPGPLT----- 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 421 rSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDS---LVERLHRQTAEYSAFKLENERLKaSFAPMEDK 497
Cdd:TIGR00618 528 -RRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSfsiLTQCDNRSKEDIPNLQNITVRLQ-DLTEKLSE 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 498 L-------NQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRqfQSQLA 570
Cdd:TIGR00618 606 AedmlaceQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASR--QLALQ 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 571 DLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKE-NKQLSQKVDELERKL 649
Cdd:TIGR00618 684 KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKElMHQARTVLKARTEAH 763
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 650 EATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLArQLESAIEDARRQVEQTK----EQALSKERAAQSKILDLET 725
Cdd:TIGR00618 764 FNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLK-TLEAEIGQEIPSDEDILnlqcETLVQEEEQFLSRLEEKSA 842
|
570 580
....*....|....*....|....*...
gi 1907136624 726 QLSRTKTELGQLRRTRDDADRRYQSRLQ 753
Cdd:TIGR00618 843 TLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
489-718 |
1.83e-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: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 489 ASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLK---DEMNKEIEAARRQF 565
Cdd:COG3883 9 PTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQaeiAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 566 QSQLADLQQLPDILKITEAKLAecQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDEL 645
Cdd:COG3883 89 GERARALYRSGGSVSYLDVLLG--SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907136624 646 ERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQS 718
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
149-704 |
2.41e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 149 EHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEmdgaaaaKQVMALK-DTIGKLKTEkqmtctdINTLTR 227
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELE-------AQIRGNGgDRLEQLERE-------IERLER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 228 QKELLLQKLSTFEETNRTL--RDLLREQHCKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQcek 305
Cdd:COG4913 353 ELEERERRRARLEALLAALglPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA--- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 306 AQAKTASELSKSMESMRGHLQAQLRCKEAENSRLC--MQIKNLERS---------GNQ---------HKAEVEAIMEQLK 365
Cdd:COG4913 430 SLERRKSNIPARLLALRDALAEALGLDEAELPFVGelIEVRPEEERwrgaiervlGGFaltllvppeHYAAALRWVNRLH 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 366 eLKQK--GDRDKETLKKAIRAQKER---AEKSE----EYAEQLHVQLADKDLYV----AEALS------TLE----SWRS 422
Cdd:COG4913 510 -LRGRlvYERVRTGLPDPERPRLDPdslAGKLDfkphPFRAWLEAELGRRFDYVcvdsPEELRrhpraiTRAgqvkGNGT 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 423 RYnqvVKDKGDLELEIIVLN----DRVTDLVNQQQSLEEKMREdRDSLVERLHRQTAEYSAFKLENERLkASFAPMEDKL 498
Cdd:COG4913 589 RH---EKDDRRRIRSRYVLGfdnrAKLAALEAELAELEEELAE-AEERLEALEAELDALQERREALQRL-AEYSWDEIDV 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 499 NQAHLEVQQLKASVKNyegmIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEM---NKEIEAARRQFQSQLADLQQL 575
Cdd:COG4913 664 ASAEREIAELEAELER----LDASSDDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEELDELQDRLEAA 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 576 PDILKITEAKLAE------CQDQLQGYERKNidLTAIISDLRSRIEHQGDKLEMAREKHQASQKENkqlsqkVDELERKL 649
Cdd:COG4913 740 EDLARLELRALLEerfaaaLGDAVERELREN--LEERIDALRARLNRAEEELERAMRAFNREWPAE------TADLDADL 811
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907136624 650 EAtsaqNVEFLQVIAK-REEAIHQ-----AQLRLEEKTRECGSLARQLESAIEDARRQVEQ 704
Cdd:COG4913 812 ES----LPEYLALLDRlEEDGLPEyeerfKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
613-768 |
3.40e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 613 RIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQnveflqvIAKREEAIHQAQLRLEEKTRECGSLARQLE 692
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE-------LEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136624 693 SAIEDaRRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQSESTNRS 768
Cdd:COG1196 306 RLEER-RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
270-680 |
3.64e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 270 LKRLAEADSEKARLLLLLQDKDKEVEEL---------LQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLC 340
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAkkkaeekkkADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 341 MQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDK--ETLKKAIRAQK-ERAEKSEEYAEQLHVQLADKDLYVAEALSTL 417
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkaDEAKKAEEAKKaDEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 418 ESWRSRYNQVVKDKGDLELEIIVLNDRVTDLvnqqQSLEEKMREDRDSLVERLHRQTAEySAFKLENERLKASfapmedk 497
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEA----KKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIKAE------- 1623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 498 lnqahlEVQQLKASVKNYEGMIDNYKSQVMKtrleadevAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQqlpd 577
Cdd:PTZ00121 1624 ------ELKKAEEEKKKVEQLKKKEAEEKKK--------AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE---- 1685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 578 ilkitEAKLAECQDQLQGYERKNIDltaiisDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNV 657
Cdd:PTZ00121 1686 -----DEKKAAEALKKEAEEAKKAE------ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754
|
410 420
....*....|....*....|...
gi 1907136624 658 EFLQVIAKREEAIHQAQLRLEEK 680
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEK 1777
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
422-653 |
3.76e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.32 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 422 SRYNQVVKDKgdleleIIVLNDRVTDLVNQQQSLEEKMREDRDsLVERLHRQTAEysafklENERLKASFAPMEDKLNQA 501
Cdd:PHA02562 166 SEMDKLNKDK------IRELNQQIQTLDMKIDHIQQQIKTYNK-NIEEQRKKNGE------NIARKQNKYDELVEEAKTI 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 502 HLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKD------------EMNKEIEAARrqfqSQL 569
Cdd:PHA02562 233 KAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqqisEGPDRITKIK----DKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 570 ADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLR---SRIEHQGDKLEMAREKHQASQKENK-QLSQKVDEL 645
Cdd:PHA02562 309 KELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKqslITLVDKAKKVKAAIEELQAEFVDNAeELAKLQDEL 388
|
....*...
gi 1907136624 646 ERKLEATS 653
Cdd:PHA02562 389 DKIVKTKS 396
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
549-734 |
3.98e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 549 MLKDEMNKEIEAARRQ-------FQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQgDKL 621
Cdd:COG4717 46 MLLERLEKEADELFKPqgrkpelNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 622 EMAREKHQASQKENKQLSQKVDELERkLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQ 701
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEE-LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190
....*....|....*....|....*....|...
gi 1907136624 702 VEQTKEQALSKERAAQSKILDLETQLSRTKTEL 734
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
362-734 |
5.40e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.97 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 362 EQLK-ELKQ----KGDRDKET---LKKAIRA---QKERAEKSEEY----------AEQLHVQLADKDLYVAEALSTLESw 420
Cdd:PRK10929 26 KQITqELEQakaaKTPAQAEIveaLQSALNWleeRKGSLERAKQYqqvidnfpklSAELRQQLNNERDEPRSVPPNMST- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 421 rsrynqvvkdkGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPmEDKLNQ 500
Cdd:PRK10929 105 -----------DALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTP-NTPLAQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 501 AHL-----EVQQLKASVKNYE--GMIDNYKSQVmkTRLEADEVAAQLERCDKENKMLKDEMNkeieaARRQFQSQLAdlq 573
Cdd:PRK10929 173 AQLtalqaESAALKALVDELElaQLSANNRQEL--ARLRSELAKKRSQQLDAYLQALRNQLN-----SQRQREAERA--- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 574 qlpdiLKITEaKLAECQDqlqgyerkniDLTAIISdlrsriehqgDKLEMAREkhqASQKENKQlSQKVDELERKLEATS 653
Cdd:PRK10929 243 -----LESTE-LLAEQSG----------DLPKSIV----------AQFKINRE---LSQALNQQ-AQRMDLIASQQRQAA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 654 AQNVEFLQVI-AKREEA-----------IHQAQL-RLEEKTRecgslARQLESAIEDAR----------------RQVEQ 704
Cdd:PRK10929 293 SQTLQVRQALnTLREQSqwlgvsnalgeALRAQVaRLPEMPK-----PQQLDTEMAQLRvqrlryedllnkqpqlRQIRQ 367
|
410 420 430
....*....|....*....|....*....|
gi 1907136624 705 TKEQALSkerAAQSKILDleTQLsRTKTEL 734
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 ... |
325-714 |
1.03e-04 |
|
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: 45.78 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 325 LQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLH-VQL 403
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqLKS 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 404 ADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMRE---DRDSLVERLHRQTAEYSAF 480
Cdd:TIGR04523 296 EISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNsesENSEKQRELEEKQNEIEKL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 481 KLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDE---MNKE 557
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvKELI 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 558 IEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQ 637
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 638 LSQKVDELERKLEA-----TSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSK 712
Cdd:TIGR04523 536 KESKISDLEDELNKddfelKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSL 615
|
..
gi 1907136624 713 ER 714
Cdd:TIGR04523 616 EK 617
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
533-732 |
1.64e-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: 44.75 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 533 ADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRS 612
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 613 RIEHQGDKL--------------------------------EMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFL 660
Cdd:COG4942 98 ELEAQKEELaellralyrlgrqpplalllspedfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907136624 661 QVIAKREEAihQAQLRLEEKTREcgSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKT 732
Cdd:COG4942 178 ALLAELEEE--RAALEALKAERQ--KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
352-759 |
1.87e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 352 QHKAEVEAIMEQLKELKQKgdrdKETLKKAIRAQKERAEKSEEYAEQLHVQLADkdlyVAEALSTLESWRSRYNQVVK-- 429
Cdd:PRK04863 352 RYQADLEELEERLEEQNEV----VEEADEQQEENEARAEAAEEEVDELKSQLAD----YQQALDVQQTRAIQYQQAVQal 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 430 DK-----GDLELEIIVLNDRVTDLVNQQQSLEEKMR--EDRDSLVERLHRQTAEysAFKLenerlkasfapmedklnqah 502
Cdd:PRK04863 424 ERakqlcGLPDLTADNAEDWLEEFQAKEQEATEELLslEQKLSVAQAAHSQFEQ--AYQL-------------------- 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 503 leVQQLKASVknyegmidnyksqvmkTRLEADEVAAQLERCDKENKMLkdemnkeieAARR-QFQSQLADLQQLPDILKI 581
Cdd:PRK04863 482 --VRKIAGEV----------------SRSEAWDVARELLRRLREQRHL---------AEQLqQLRMRLSELEQRLRQQQR 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 582 TEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELErkleatsaqnveflq 661
Cdd:PRK04863 535 AERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLA--------------- 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 662 viaKREEAIHQAQLRLEEktrecgsLARQLESAIEDArRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTR 741
Cdd:PRK04863 600 ---ARAPAWLAAQDALAR-------LREQSGEEFEDS-QDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPG 668
|
410
....*....|....*...
gi 1907136624 742 DDADrryqSRLQDLKDRL 759
Cdd:PRK04863 669 GSED----PRLNALAERF 682
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
557-722 |
2.06e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 557 EIEAARRQFQSQLADLQQLpdiLKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMARekhqaSQKENK 636
Cdd:COG1579 21 RLEHRLKELPAELAELEDE---LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-----NNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 637 QLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQveqtkEQALSKERAA 716
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE-----LEELEAEREE 167
|
....*.
gi 1907136624 717 QSKILD 722
Cdd:COG1579 168 LAAKIP 173
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
483-737 |
3.61e-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: 43.90 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 483 ENERLKASFAPMEDKLNqahlEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENkmlkdemnkeiEAAR 562
Cdd:pfam19220 4 RNELLRVRLGEMADRLE----DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAY-----------GKLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 563 RQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKV 642
Cdd:pfam19220 69 RELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 643 DELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLAR---QLESAIEDARRQVEQTkEQALSKERAAQSK 719
Cdd:pfam19220 149 QAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRrlaELETQLDATRARLRAL-EGQLAAEQAERER 227
|
250
....*....|....*....
gi 1907136624 720 IL-DLETQLSRTKTELGQL 737
Cdd:pfam19220 228 AEaQLEEAVEAHRAERASL 246
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
555-776 |
3.73e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 555 NKEIEAARRQFQSQLADLQQlpdilkiteaKLAECQDQLQGYERKN--IDLTAIISDLRSRIEHQGDKLEMAREKHQASQ 632
Cdd:COG3206 170 REEARKALEFLEEQLPELRK----------ELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 633 kenkqlsQKVDELERKLEATSAQNVEFLQ--VIAKREEAIHQAQLRLEEKTRECG--------------SLARQLESAIE 696
Cdd:COG3206 240 -------ARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTpnhpdvialraqiaALRAQLQQEAQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 697 DARRQVEQTKEQALSKERAAQSKILDLETQ---LSRTKTELGQLRRTRDDADRRYQSrlqdLKDRLEQSESTNRSMQNYV 773
Cdd:COG3206 313 RILASLEAELEALQAREASLQAQLAQLEARlaeLPELEAELRRLEREVEVARELYES----LLQRLEEARLAEALTVGNV 388
|
...
gi 1907136624 774 QFL 776
Cdd:COG3206 389 RVI 391
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
142-392 |
3.75e-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: 43.60 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 142 AHELAETEHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTD 221
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 222 INTLTRQKELLLQKLSTFEETNRtLRDLLREQHCKEDSERLMeqqgtLLKRLAEADSEKARlllllqdkdkEVEELLQEI 301
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPP-LALLLSPEDFLDAVRRLQ-----YLKYLAPARREQAE----------ELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 302 QcekaqaktasELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKA 381
Cdd:COG4942 163 A----------ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
250
....*....|.
gi 1907136624 382 IRAQKERAEKS 392
Cdd:COG4942 233 EAEAAAAAERT 243
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
257-719 |
6.82e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 257 EDSERLMEQQGTLLKRLAEaDSEKARLLLLLQDKdKEVEELLQEIQCEKAQAKTASELSKSMESMRGHlQAQLRCKEAEN 336
Cdd:PTZ00121 1143 EEARKAEDAKRVEIARKAE-DARKAEEARKAEDA-KKAEAARKAEEVRKAEELRKAEDARKAEAARKA-EEERKAEEARK 1219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 337 SRLCMQIKNLERSGNQHKAEVEAIMEQlKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKdlyVAEALST 416
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEAKKDAEEAKKAE-EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE---KKKADEA 1295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 417 LESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDSlvERLHRQTAEYSAFKLENERLKASFAPME- 495
Cdd:PTZ00121 1296 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA--AEAAKAEAEAAADEAEAAEEKAEAAEKKk 1373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 496 -------DKLNQAHLEVQQLKASVKNYEGmiDNYKSQVMKTRLEADEVAAQLERcDKENKMLKDEMNKEIEAARR--QFQ 566
Cdd:PTZ00121 1374 eeakkkaDAAKKKAEEKKKADEAKKKAEE--DKKKADELKKAAAAKKKADEAKK-KAEEKKKADEAKKKAEEAKKadEAK 1450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 567 SQLADLQQLPDILKITE--------AKLAECQDQLQGYERKNIDLTAIISDLRSRIE--HQGDKLEMAREKHQASQKENK 636
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEeakkadeaKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEakKKADEAKKAEEAKKADEAKKA 1530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 637 QLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAA 716
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
...
gi 1907136624 717 QSK 719
Cdd:PTZ00121 1611 EAK 1613
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
441-769 |
7.84e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.21 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 441 LNDRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAE----YSAFKLENERLKASF-------APMEDKLNQAHLEVQQLK 509
Cdd:pfam00038 9 LNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpsrlYSLYEKEIEDLRRQLdtltverARLQLELDNLRLAAEDFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 510 ASVKNYEGMIDNYKSQVMKTRLEADEvaAQLERCDKENKMlkDEMNKEIEAARRQFQSQLADLQqlpdilkiteAKLAEC 589
Cdd:pfam00038 89 QKYEDELNLRTSAENDLVGLRKDLDE--ATLARVDLEAKI--ESLKEELAFLKKNHEEEVRELQ----------AQVSDT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 590 QDQLQGYERKNIDLTAIISDLRSRIEHQgdkleMAREKHQASQkenkQLSQKVDELERkleaTSAQNVEFLQviAKREEa 669
Cdd:pfam00038 155 QVNVEMDAARKLDLTSALAEIRAQYEEI-----AAKNREEAEE----WYQSKLEELQQ----AAARNGDALR--SAKEE- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 670 IHQAQLRLEEKTRECGSLARQLESaIEDARRQVEQTKEQALSKeraAQSKILDLETQLSRTKTELGQLrrtrddaDRRYQ 749
Cdd:pfam00038 219 ITELRRTIQSLEIELQSLKKQKAS-LERQLAETEERYELQLAD---YQELISELEAELQETRQEMARQ-------LREYQ 287
|
330 340
....*....|....*....|
gi 1907136624 750 SrLQDLKDRLEQSESTNRSM 769
Cdd:pfam00038 288 E-LLNVKLALDIEIATYRKL 306
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
71-733 |
8.99e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 71 SSEKLV-SVMRLSDLSTEDDDSGHCK--MNRYDKKIDSLMNAVGCLKSEVKMQKGERQMAKRFLEERKEELEEVAHELAE 147
Cdd:PRK03918 146 SREKVVrQILGLDDYENAYKNLGEVIkeIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 148 TEHENTVLRHNIERIKEEKdftmLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTekqmtctdintlTR 227
Cdd:PRK03918 226 LEKEVKELEELKEEIEELE----KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE------------LK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 228 QKELLLQKLSTF-EETNRTLRDLlreqhcKEDSERLMEQQGTLLKRLAEADSEKARLLLLLqdkdKEVEELLQEIQCEKA 306
Cdd:PRK03918 290 EKAEEYIKLSEFyEEYLDELREI------EKRLSRLEEEINGIEERIKELEEKEERLEELK----KKLKELEKRLEELEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 307 QAKTASELSKSMESMRGhLQAQLRCKEAEnsRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQK 386
Cdd:PRK03918 360 RHELYEEAKAKKEELER-LKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 387 E----RAEKSEEYAEQLhvqLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIVLND--RVTDLVNQQQSLEEKMR 460
Cdd:PRK03918 437 KcpvcGRELTEEHRKEL---LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 461 EDRdslVERLHRQTAEYSAFKLENERLKASFAPMEDKLNqahlEVQQLKASVKNYEGMIDNYKSqvmktrlEADEVAAQL 540
Cdd:PRK03918 514 KYN---LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE----KLEELKKKLAELEKKLDELEE-------ELAELLKEL 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 541 ERCDKENKMLKDEMNKEIEAARRQFQSqladLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQG-- 618
Cdd:PRK03918 580 EELGFESVEELEERLKELEPFYNEYLE----LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEkk 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 619 ---DKLEMAREKHQASQKENKQLSQKVDELERKLEaTSAQNVEFLQviaKREEAIHQAQLRLEektrecgslarQLESAI 695
Cdd:PRK03918 656 yseEEYEELREEYLELSRELAGLRAELEELEKRRE-EIKKTLEKLK---EELEEREKAKKELE-----------KLEKAL 720
|
650 660 670
....*....|....*....|....*....|....*...
gi 1907136624 696 EDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTE 733
Cdd:PRK03918 721 ERVEELREKVKKYKALLKERALSKVGEIASEIFEELTE 758
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
274-772 |
1.16e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 274 AEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKS-MESMRGHLQAQLRCKEAENSRLCMQIKNLERSgnQ 352
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAeAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA--K 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 353 HKAEVEAIMEQLKELKQKGDRDKETLKKAiRAQKERAEKSEEYAEQlhVQLADKDLYVAEALSTLESWRSRYNQVVKDKg 432
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKAEEDKKKADELKKA-AAAKKKADEAKKKAEE--KKKADEAKKKAEEAKKADEAKKKAEEAKKAE- 1460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 433 dlELEIIVLNDRVTDlvNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASV 512
Cdd:PTZ00121 1461 --EAKKKAEEAKKAD--EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 513 KNYEGMIDNYKSQVMKTRLE---ADEV----AAQLERCDKENKMLKDEMNKEIEAARRQfqsQLADLQQLPDILKITEAK 585
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEElkkAEEKkkaeEAKKAEEDKNMALRKAEEAKKAEEARIE---EVMKLYEEEKKMKAEEAK 1613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 586 LAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLE----ATSAQNVEFLQ 661
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEeakkAEEDEKKAAEA 1693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 662 VIAKREEAIHQAQLRleEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLE-----TQLSRTKTELGQ 736
Cdd:PTZ00121 1694 LKKEAEEAKKAEELK--KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEekkkiAHLKKEEEKKAE 1771
|
490 500 510
....*....|....*....|....*....|....*.
gi 1907136624 737 LRRTRDDADRRYQSRLQDLKDRLEQSESTNRSMQNY 772
Cdd:PTZ00121 1772 EIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNF 1807
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
566-765 |
1.18e-03 |
|
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: 42.19 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 566 QSQLAD-LQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDE 644
Cdd:pfam07888 33 QNRLEEcLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 645 LERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTREcgslarqLESAIEDARRQVEQTKEQAlSKERAAQSKILDLE 724
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETE-------LERMKERAKKAGAQRKEEE-AERKQLQAKLQQTE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907136624 725 TQLSRTKTELGQLRRTRDDADRRYQsRLQDLKDRLEQSEST 765
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVL-QLQDTITTLTQKLTT 224
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
288-479 |
1.62e-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: 41.67 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 288 QDKDKEVEELLQEIQcekAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKEL 367
Cdd:COG4942 19 ADAAAEAEAELEQLQ---QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 368 KQKGDRDKETLKKAIRAQKERAEKSE-------EYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIV 440
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907136624 441 LNDRVTDLVNQQQSLEEKMREdRDSLVERLHRQTAEYSA 479
Cdd:COG4942 176 LEALLAELEEERAALEALKAE-RQKLLARLEKELAELAA 213
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
452-763 |
2.15e-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: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 452 QQSLEE----KMREDRDSLVERLHRQTAEysafKLENERLKAsfapmedklnqahLEVQQLKASVKNYEGMIDNYKSQVM 527
Cdd:TIGR02169 173 EKALEEleevEENIERLDLIIDEKRQQLE----RLRREREKA-------------ERYQALLKEKREYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 528 KTRLEAdeVAAQLERCDKENKMLK---DEMNKEIEAARrqfqsqladlQQLPDILKITEAKLAECQDQLQgyeRKNIDLT 604
Cdd:TIGR02169 236 ERQKEA--IERQLASLEEELEKLTeeiSELEKRLEEIE----------QLLEELNKKIKDLGEEEQLRVK---EKIGELE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 605 AIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTREc 684
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE- 379
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907136624 685 gslARQLESAIEDARRQVEQTKEQALSKERaAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQSE 763
Cdd:TIGR02169 380 ---FAETRDELKDYREKLEKLKREINELKR-ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE 454
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
441-647 |
2.84e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 441 LNDRVTDLvNQQQSLEEKMREDRDSLVERLhrqTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGmid 520
Cdd:PRK09039 58 LNSQIAEL-ADLLSLERQGNQDLQDSVANL---RASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQ--- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 521 nyksqvmktrlEADEVAAQLERcdkenkmlkdeMNKEIEAARRqfqsQLADLQQLpdiLKITEAKLAECQDQlqgyerkn 600
Cdd:PRK09039 131 -----------VSARALAQVEL-----------LNQQIAALRR----QLAALEAA---LDASEKRDRESQAK-------- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907136624 601 idltaiISDLRSRIehqgdklemarekhqasqkeNKQLSQKVDELER 647
Cdd:PRK09039 174 ------IADLGRRL--------------------NVALAQRVQELNR 194
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
585-733 |
3.48e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 585 KLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQ-----NVEF 659
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrNNKE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907136624 660 LQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTE 733
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
572-763 |
3.65e-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: 40.01 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 572 LQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEA 651
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 652 TSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLesaiedarRQVEQTKEQALSKERAAQSKILDLETQLSRTK 731
Cdd:pfam00261 83 LENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKL--------VVVEGDLERAEERAELAESKIVELEEELKVVG 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1907136624 732 TELGQL---RRTRDDADRRYQSRLQDLKDRLEQSE 763
Cdd:pfam00261 155 NNLKSLeasEEKASEREDKYEEQIRFLTEKLKEAE 189
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
579-806 |
3.67e-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: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 579 LKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEA------T 652
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralyR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 653 SAQNVEFLQVIAKRE---EAIHQAQL--RLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQL 727
Cdd:COG3883 98 SGGSVSYLDVLLGSEsfsDFLDRLSAlsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 728 SRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQ----SESTNRSMQNYVQFLKASYANVFGDAPYTSSYLTSSPIRSRS 803
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAaaaaAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
...
gi 1907136624 804 PPA 806
Cdd:COG3883 258 AAG 260
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
195-381 |
4.09e-03 |
|
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];
Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 40.83 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 195 AAAAKQVMALKDTIGKLKTEKQmtctdINTLTRQKELLLQKLSTFEETNRTLRDLLREQhckedsERLMEQQGTLL--KR 272
Cdd:COG4192 68 VAALPEFAAATNTTERSQLRNQ-----LNTQLADIEELLAELEQLTQDAGDLRAAVADL------RNLLQQLDSLLtqRI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 273 LAEADSEKA--RLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENsrlcmQIKNL--ER 348
Cdd:COG4192 137 ALRRRLQELleQINWLHQDFNSELTPLLQEASWQQTRLLDSVETTESLRNLQNELQLLLRLLAIEN-----QIVSLlrEV 211
|
170 180 190
....*....|....*....|....*....|...
gi 1907136624 349 SGNQHKAEVEAIMEQLKELKQKGDRDKETLKKA 381
Cdd:COG4192 212 AAARDQADVDNLFDRLQYLKDELDRNLQALKNY 244
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
141-542 |
4.53e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 141 VAHELAETEHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCT 220
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 221 DINTLTRQKELLL-------QKLSTFEETNRTLRDLLREqhckedSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKE 293
Cdd:PRK02224 406 DLGNAEDFLEELReerdelrEREAELEATLRTARERVEE------AEALLEAGKCPECGQPVEGSPHVETIEEDRERVEE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 294 VEELLQEIQCEKAqaktasELSKSMESMRghlqaQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQkgdr 373
Cdd:PRK02224 480 LEAELEDLEEEVE------EVEERLERAE-----DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE---- 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 374 DKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDlyvaEALSTLESWRSRYNQVVkdkgDLELEIIVLNDRVTDLVNQQQ 453
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELN----SKLAELKERIESLERIR----TLLAAIADAEDEIERLREKRE 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 454 SLEEKMREDRDSLVERLHRQTAEYSAFKLEN-ERLKASFAPMEDKLNQAHLEVQQL---KASVKNYEGMIDNYKSQVMKT 529
Cdd:PRK02224 617 ALAELNDERRERLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELreeRDDLQAEIGAVENELEELEEL 696
|
410
....*....|...
gi 1907136624 530 RLEADEVAAQLER 542
Cdd:PRK02224 697 RERREALENRVEA 709
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
144-461 |
4.79e-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: 40.44 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 144 ELAETEHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTctDIN 223
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS--RIP 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 224 TLTRQKELLLQKLSTFEETNRTLRDLLREQHCKEDSERlmEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIqc 303
Cdd:TIGR02169 795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE--KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL-- 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 304 EKAQAKTaselsKSMESMRGHLqaqlrckEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIR 383
Cdd:TIGR02169 871 EELEAAL-----RDLESRLGDL-------KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED 938
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 384 AQKERAEKSEEYAEQLHVQLadKDLYVAEALSTLESWRSR----YNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKM 459
Cdd:TIGR02169 939 PKGEDEEIPEEELSLEDVQA--ELQRVEEEIRALEPVNMLaiqeYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
..
gi 1907136624 460 RE 461
Cdd:TIGR02169 1017 RE 1018
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
468-737 |
5.58e-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: 40.33 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 468 ERLHRQTAEYSAFKLENERlkASFAPMEDKLNQAHLEVQQLKASVKNYEGMID-----NYKSQVMKTRLEADEVAAQLER 542
Cdd:COG5185 256 EKLVEQNTDLRLEKLGENA--ESSKRLNENANNLIKQFENTKEKIAEYTKSIDikkatESLEEQLAAAEAEQELEESKRE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 543 CDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKIT--EAKLAECQDQLqgyERKNIDLTAIISDLRSRIEhqgDK 620
Cdd:COG5185 334 TETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSksSEELDSFKDTI---ESTKESLDEIPQNQRGYAQ---EI 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 621 LEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKRE-EAIHQAQLRLEEKTREcgsLARQLESAIEDAR 699
Cdd:COG5185 408 LATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMrEADEESQSRLEEAYDE---INRSVRSKKEDLN 484
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907136624 700 RQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQL 737
Cdd:COG5185 485 EELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQV 522
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
495-734 |
6.22e-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: 40.16 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 495 EDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAArrqfqsqladlqq 574
Cdd:pfam01576 88 EERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKER------------- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 575 lpdilKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSA 654
Cdd:pfam01576 155 -----KLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 655 QNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLA---RQLESAIEDARRQVEQTKEQALSKERAAQskilDLETQLSRTK 731
Cdd:pfam01576 230 QIAELRAQLAKKEEELQAALARLEEETAQKNNALkkiRELEAQISELQEDLESERAARNKAEKQRR----DLGEELEALK 305
|
...
gi 1907136624 732 TEL 734
Cdd:pfam01576 306 TEL 308
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
169-451 |
8.35e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 39.68 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 169 TMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKT----EKQMTCTDINTLTRQKELLLQKLSTFEETNR 244
Cdd:COG5022 780 GFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKtikrEKKLRETEEVEFSLKAEVLIQKFGRSLKAKK 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 245 TLRDLLREQhCKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQC---EKAQAKTA--SELSKSME 319
Cdd:COG5022 860 RFSLLKKET-IYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSdliENLEFKTEliARLKKLLN 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 320 SMRGHLQAQL-RCKEAENSRLCMQIKNLERSGNQHKAEV---EAIMEQLKELKQKGDRDKETLKKaIRAQKERAEKSEEY 395
Cdd:COG5022 939 NIDLEEGPSIeYVKLPELNKLHEVESKLKETSEEYEDLLkksTILVREGNKANSELKNFKKELAE-LSKQYGALQESTKQ 1017
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136624 396 AEQLHVQLADKDlYVAEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQ 451
Cdd:COG5022 1018 LKELPVEVAELQ-SASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLR 1072
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
383-780 |
9.19e-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: 39.55 E-value: 9.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 383 RAQKERAEKSEEYAEQLHVQLADKDLYVAEaLSTLESWRSRY---NQVVKDKGDLELEIIVLNDRVTDL---VNQQQSLE 456
Cdd:COG3096 781 AAREKRLEELRAERDELAEQYAKASFDVQK-LQRLHQAFSQFvggHLAVAFAPDPEAELAALRQRRSELereLAQHRAQE 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 457 EKMREDRDSLVER---LHRQTAEYSAFKLE--NERLKASFAPMeDKLNQAHLEVQQLKASVKNYEGMIDNYKSqvmkTRL 531
Cdd:COG3096 860 QQLRQQLDQLKEQlqlLNKLLPQANLLADEtlADRLEELREEL-DAAQEAQAFIQQHGKALAQLEPLVAVLQS----DPE 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 532 EADEVAAQLERCDKENKMLKdemnKEIEA-----ARR---------QFQSQLADL-QQLPDILKITEAKLAECQDQLQGY 596
Cdd:COG3096 935 QFEQLQADYLQAKEQQRRLK----QQIFAlsevvQRRphfsyedavGLLGENSDLnEKLRARLEQAEEARREAREQLRQA 1010
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 597 ERKNIDLTAIISDLRSRiehqgdkLEMAREKHQASQKENKQLS------------QKVDELERKLEATSAQNVEFLQVIA 664
Cdd:COG3096 1011 QAQYSQYNQVLASLKSS-------RDAKQQTLQELEQELEELGvqadaeaeerarIRRDELHEELSQNRSRRSQLEKQLT 1083
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 665 KREEAIHQAQLRLeektrecgslaRQLESAIEDARRQVEQTKE-----QALSKERaaqskilDLETQLSRTK------TE 733
Cdd:COG3096 1084 RCEAEMDSLQKRL-----------RKAERDYKQEREQVVQAKAgwcavLRLARDN-------DVERRLHRRElaylsaDE 1145
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1907136624 734 LGQLRRTRDDADRRYQSRLQDLKDRLEQSEStNRSMQNYVQFLKASY 780
Cdd:COG3096 1146 LRSMSDKALGALRLAVADNEHLRDALRLSED-PRRPERKVQFYIAVY 1191
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
95-394 |
9.33e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 95 KMNRYDKKIDSLMNAVGCLKSEVKMQKGERqmAKRFLEERKEELEEVAHEL--AETEHENTVLRHNIERIKEEKDFTMLQ 172
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEE--AKKADEAKKAEEAKKADEAkkAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 173 KKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTDintlTRQKELLLQKLSTFEETNRTLRDLLRE 252
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE----AKIKAEELKKAEEEKKKVEQLKKKEAE 1644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136624 253 QHCKEDSERLMEQQGTL----LKRLAEADSEKARLLLLLQDKDKEVEELLQEiqcEKAQAKTASELSKSMESMRGHLQaQ 328
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIkaaeEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK---EAEEAKKAEELKKKEAEEKKKAE-E 1720
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136624 329 LRCKEAENSrlcMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEE 394
Cdd:PTZ00121 1721 LKKAEEENK---IKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| |
