|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
119-783 |
1.30e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 88.19 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 119 KMNRYDKKIDSLMNAVGCLKSEVKMQKGERQMAKRFLEERKEELEEVAHELAETEHENTVLRHNIERIKEEKDFTMLQKK 198
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 199 HLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETNRTLRDLLREQH 278
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 279 CKEDSERLmeqqGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQ-AQLRCKE 357
Cdd:TIGR02168 435 LKELQAEL----EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgFSEGVKA 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 358 AENSRLCM-----QIKNLERSGNQHKAEVEA---------IMEQLKELKQKGDRDKETLK--------KAIRAQKERAEK 415
Cdd:TIGR02168 511 LLKNQSGLsgilgVLSELISVDEGYEAAIEAalggrlqavVVENLNAAKKAIAFLKQNELgrvtflplDSIKGTEIQGND 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 416 SEEYAEQLHVQLADKDL--YVAEALSTLESWRSRYnqVVKDKGDLELEIIVLNDR----VT---DLVNQQQSLEEKMRED 486
Cdd:TIGR02168 591 REILKNIEGFLGVAKDLvkFDPKLRKALSYLLGGV--LVVDDLDNALELAKKLRPgyriVTldgDLVRPGGVITGGSAKT 668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 487 RDSLVERlhrqtaeysafKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDnyksqvmktrlEADEVAAQLER 566
Cdd:TIGR02168 669 NSSILER-----------RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE-----------QLRKELEELSR 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 567 CDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLE 646
Cdd:TIGR02168 727 QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 647 MAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAiEDARRQV 726
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL-LNERASL 885
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 727 EQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQS---RLQDLKDRL 783
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGlevRIDNLQERL 945
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
227-785 |
4.61e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 4.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 227 ALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETNRTLRDLLREQhcKEDSERLMEQQGTLLKRLAEADSEKAR 306
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL--LAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 307 LllllqdkDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIME 386
Cdd:COG1196 321 L-------EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 387 QLKELKQKgdrdKETLKKAIRAQKERAEKSEEYAEQLHVQLadkdlyvAEALSTLESWRSRYNQVVKDKGDLELEIIVLN 466
Cdd:COG1196 394 AAAELAAQ----LEELEEAEEALLERLERLEEELEELEEAL-------AELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 467 DRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAP-MEDKLNQAHLEVQQLKASVKNYEGMIDN 545
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAlLLAGLRGLAGAVAVLIGVEAAYEAALEA 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 546 YKSQVMKTRL-EADEVAAQLERCDKENKMLKDE---MNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYE 621
Cdd:COG1196 543 ALAAALQNIVvEDDEVAAAAIEYLKAAKAGRATflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 622 RKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRL 701
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 702 EEktrecgslARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKD 781
Cdd:COG1196 703 EE--------EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
....
gi 1907136592 782 RLEQ 785
Cdd:COG1196 775 EIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
369-742 |
1.14e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 369 NLERsgnqhkaeVEAIMEQLkelkqkgDRDKETLKKairaQKERAEKSEEYAEQLhvQLADKDLYVAealstleswrsRY 448
Cdd:COG1196 187 NLER--------LEDILGEL-------ERQLEPLER----QAEKAERYRELKEEL--KELEAELLLL-----------KL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 449 NQVVKDKGDLELEIIVLNDRVTDLVNQQQSLE---EKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQA 525
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEaelEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 526 HLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLErcdkenkmlkdemnkEIEAARRQFQSQLADLqqlpdilki 605
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELE---------------EAEAELAEAEEALLEA--------- 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 606 tEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQ 685
Cdd:COG1196 371 -EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907136592 686 VIAKREEAIHQAQLRLEEKTREcgslARQLESAIEDARRQVEQTKEQALSKERAAQS 742
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEE----AALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
252-807 |
8.18e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 8.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 252 QKELLLQKLSTFEETNRTLRDLLREQhcKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQcekaq 331
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEA--EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS----- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 332 aktaselskSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKE 411
Cdd:TIGR02168 299 ---------RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 412 RAEKSEEYAEQLHvQLADKdlyVAEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLE-EKMREDRDSL 490
Cdd:TIGR02168 370 LESRLEELEEQLE-TLRSK---VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEEL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 491 VERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKS------QVMKTRLEAD------ 558
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegvkALLKNQSGLSgilgvl 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 559 ----EVAAQLERC---------------DKENKMLKDEMNKEIEAARRQF------------QSQLADLQQLPDILKITe 607
Cdd:TIGR02168 526 seliSVDEGYEAAieaalggrlqavvveNLNAAKKAIAFLKQNELGRVTFlpldsikgteiqGNDREILKNIEGFLGVA- 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 608 AKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQ-------------GDKL----------EMAREKHQASQKENKQLSQ 664
Cdd:TIGR02168 605 KDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAkklrpgyrivtldGDLVrpggvitggsAKTNSSILERRREIEELEE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 665 KVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESA------IEDARRQVEQTKEQALSKER 738
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeveqLEERIAQLSKELTELEAEIE 764
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907136592 739 AAQSKILDLETQLSRTKTELGQLrrtrddadrryQSRLQDLKDRLEQSESTNRSMQNYVQFLKASYANV 807
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEEL-----------EAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
465-788 |
8.26e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 8.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 465 LNDRVTDLVNQQQSLEEKMR--EDRDSLVERLHRQTAEYSAFKLEneRLKASFAPMEDKLNQAHLEVQQLKASVKNYEGM 542
Cdd:COG1196 191 LEDILGELERQLEPLERQAEkaERYRELKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 543 IDNYKSQVMKTRLEADEVAAQLERCDKEnkmlKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYER 622
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAE----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 623 KNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQnvefLQVIAKREEAIHQAQLRLE 702
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ----LEELEEAEEALLERLERLE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 703 EKTRECGSLARQLESAIEDARRQVEQTKE---QALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDL 779
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEeeaELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
....*....
gi 1907136592 780 KDRLEQSES 788
Cdd:COG1196 501 ADYEGFLEG 509
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
252-703 |
3.81e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 67.07 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 252 QKELLLQKLSTFEETNRTLRDLLRE-QHCKEDSERLMEQQGTLLK-RLAEADSEKARLLLLLQDKDKEVEELL------- 322
Cdd:pfam15921 311 QNSMYMRQLSDLESTVSQLRSELREaKRMYEDKIEELEKQLVLANsELTEARTERDQFSQESGNLDDQLQKLLadlhkre 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 323 QEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERS-GNQHKAEVEAI------MEQLKELKQKG 395
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIqgknesLEKVSSLTAQL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 396 DRDKETLKKAIR---AQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYN------QVVKDKGD------LEL 460
Cdd:pfam15921 471 ESTKEMLRKVVEeltAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDlklqelQHLKNEGDhlrnvqTEC 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 461 EIIVLN---------------DRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQA 525
Cdd:pfam15921 551 EALKLQmaekdkvieilrqqiENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 526 HLE--------VQQLKAsVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQ 597
Cdd:pfam15921 631 ELEkvklvnagSERLRA-VKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELE 709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 598 QLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKV-------DELE 670
Cdd:pfam15921 710 QTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELstvatekNKMA 789
|
490 500 510
....*....|....*....|....*....|...
gi 1907136592 671 RKLEATSAQNVEFLQVIAKREEAIHQAQLRLEE 703
Cdd:pfam15921 790 GELEVLRSQERRLKEKVANMEVALDKASLQFAE 822
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
358-721 |
1.03e-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: 65.85 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 358 AENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEA 437
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 438 LSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMredrDSLVERLHRQTAEYSAFKLENERLKASFAP 517
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL----DELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 518 MEDKLNQAHLEVQQLKASVKNYEGMIDNYksqvmktRLEADEVAAQLERCDKEnkmlKDEMNKEIEAARRQFQSQLADLQ 597
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEEL-------EELIEELESELEALLNE----RASLEEALALLRSELEELSEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 598 QLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRI-EHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEAT 676
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1907136592 677 SAQNVEFLQVIAKREEaihqaqlRLEEKTRECGSLAR---QLESAIED 721
Cdd:TIGR02168 985 GPVNLAAIEEYEELKE-------RYDFLTAQKEDLTEakeTLEEAIEE 1025
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-810 |
3.96e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.93 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 173 EHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTC-TDINTLTR 251
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVkEKIGELEA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 252 QKELLLQKLstfEETNRTLRDLL-REQHCKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKA 330
Cdd:TIGR02169 302 EIASLERSI---AEKERELEDAEeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 331 QAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELkqkgDRDKETLKKAIRAQK 410
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL----EEEKEDKALEIKKQE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 411 ERAEKSEEYAEQLHVQLADKdlyvaealstleswRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQ---SLEEKMREDR 487
Cdd:TIGR02169 455 WKLEQLAADLSKYEQELYDL--------------KEEYDRVEKELSKLQRELAEAEAQARASEERVRggrAVEEVLKASI 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 488 DS---LVERLHRQTAEYsAFKLE---NERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEV- 560
Cdd:TIGR02169 521 QGvhgTVAQLGSVGERY-ATAIEvaaGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVi 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 561 --AAQLERCDKENK-----MLKDEMNKE-IEAARRQF---------------------------------QSQLADLQQL 599
Cdd:TIGR02169 600 gfAVDLVEFDPKYEpafkyVFGDTLVVEdIEAARRLMgkyrmvtlegelfeksgamtggsraprggilfsRSEPAELQRL 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 600 PDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQ 679
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 680 NVEFLQVIAKREEAIHQAQLRLEE-KTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLEtQLSRTKTEL 758
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE-YLEKEIQEL 838
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1907136592 759 GQLRRTRDDADRRYQSRLQDLKDRLEQSESTNRSMQNYVQFLKASYANVFGD 810
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
553-791 |
4.04e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 553 TRLEA--DEVAAQLERCDKE------NKMLKDEMN-KEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERK 623
Cdd:COG1196 189 ERLEDilGELERQLEPLERQaekaerYRELKEELKeLEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 624 NIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEE 703
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 704 KTRECGSLARQLESAiEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRL 783
Cdd:COG1196 349 AEEELEEAEAELAEA-EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
....*...
gi 1907136592 784 EQSESTNR 791
Cdd:COG1196 428 EALAELEE 435
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
198-538 |
5.17e-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: 5.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 198 KHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQmtctdinTLTRQKELLLQKLSTFEETNRTLRDLLREQ 277
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-------ELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 278 HckEDSERLMEQQGTLLKRLAEADSEKArlllllqdkdkeveELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKE 357
Cdd:TIGR02168 753 S--KELTELEAEIEELEERLEEAEEELA--------------EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 358 AENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQkgdrDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEA 437
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSE----DIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 438 LSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKmredRDSLVERLhrqTAEYSafkLENERLKASFAP 517
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR----IDNLQERL---SEEYS---LTLEEAEALENK 962
|
330 340
....*....|....*....|.
gi 1907136592 518 MEDKLNQAHLEVQQLKASVKN 538
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKE 983
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
167-674 |
1.10e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.96 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 167 HELAETEHENTVLRHniERIKEEKDFTMLQKKhlQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTDI 246
Cdd:TIGR04523 180 KEKLNIQKNIDKIKN--KLLKLELLLSNLKKK--IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 247 NTLTRQ----KELLLQKLSTFEETNRTLRDLlreqhckedserlMEQQGTLLKRLAEADSEKArlllllQDKDKEVEELL 322
Cdd:TIGR04523 256 NQLKDEqnkiKKQLSEKQKELEQNNKKIKEL-------------EKQLNQLKSEISDLNNQKE------QDWNKELKSEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 323 QEIQCEKAQAKTasELSKSMESMrghlqaqlrckeaenSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKgdrdKETL 402
Cdd:TIGR04523 317 KNQEKKLEEIQN--QISQNNKII---------------SQLNEQISQLKKELTNSESENSEKQRELEEKQNE----IEKL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 403 KKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLE-- 480
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEli 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 481 -EKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADE 559
Cdd:TIGR04523 456 iKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 560 VAAQLErcDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKnidltaiISDLRSRIE 639
Cdd:TIGR04523 536 KESKIS--DLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE-------KKDLIKEIE 606
|
490 500 510
....*....|....*....|....*....|....*
gi 1907136592 640 HQGDKLEMAREKHQASQKENKQLSQKVDELERKLE 674
Cdd:TIGR04523 607 EKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKN 641
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
286-785 |
1.15e-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: 62.16 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 286 LMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTA-----SELSKSMESMRGHLQAQLRCKEAEN 360
Cdd:pfam12128 267 YKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAvakdrSELEALEDQHGAFLDADIETAAADQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 361 SRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADkdlyvaeALST 440
Cdd:pfam12128 347 EQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAED-------DLQA 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 441 LES-WRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKM--REDRDSLVER----LHRQTAEYSAFKLENERLKA 513
Cdd:pfam12128 420 LESeLREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLlqLENFDERIERareeQEAANAEVERLQSELRQARK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 514 SFAPMEDKLNQAHLEVQQLKASVKNYEGMID----------NYKSQVMKTRLEADEVAAQLERCDkenkmLKDEMNKEIE 583
Cdd:pfam12128 500 RRDQASEALRQASRRLEERQSALDELELQLFpqagtllhflRKEAPDWEQSIGKVISPELLHRTD-----LDPEVWDGSV 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 584 AARRQFQSQLADLQQL--PDILKITEAklaecqdqlqgyerknidltaiisdLRSRIEHQGDKLEMAREKHQASQKENKQ 661
Cdd:pfam12128 575 GGELNLYGVKLDLKRIdvPEWAASEEE-------------------------LRERLDKAEEALQSAREKQAAAEEQLVQ 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 662 LSQKVDELERKLEatsaqnveflqvIAKReeAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQAlskerAAQ 741
Cdd:pfam12128 630 ANGELEKASREET------------FART--ALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSL-----EAQ 690
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1907136592 742 SKILDLETQLSRTKTElGQLRRTRDDADRRYQSRLQDLKDRLEQ 785
Cdd:pfam12128 691 LKQLDKKHQAWLEEQK-EQKREARTEKQAYWQVVEGALDAQLAL 733
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
208-725 |
1.84e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 208 MSKLVEAEMDGAAAAKQVMALKDTIGKlktekqmtCTDINTLTRQKELLLQKLSTFE-ETNRTLRDLLREQ--HCKEDSE 284
Cdd:COG4913 234 FDDLERAHEALEDAREQIELLEPIREL--------AERYAAARERLAELEYLRAALRlWFAQRRLELLEAEleELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 285 RLMEQQGTLLKRLAEADSEKAR-LLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRL 363
Cdd:COG4913 306 RLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 364 CMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQL------HVQLADKDL-YVAE 436
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALrdalaeALGLDEAELpFVGE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 437 AL---STLESWRS------------------RYNQVVK--DKGDLELEIivlndrVTDLVNQQQSLEEKMREDRDSLVER 493
Cdd:COG4913 466 LIevrPEEERWRGaiervlggfaltllvppeHYAAALRwvNRLHLRGRL------VYERVRTGLPDPERPRLDPDSLAGK 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 494 LHRQTAEYSAFkLENErLKASFAPM----EDKLNQAHLEVQQlkasvknyEGMI-DNYKSQVMKTRLEADEV-------A 561
Cdd:COG4913 540 LDFKPHPFRAW-LEAE-LGRRFDYVcvdsPEELRRHPRAITR--------AGQVkGNGTRHEKDDRRRIRSRyvlgfdnR 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 562 AQLERCDKENKMLKDEMN------KEIEAARRQFQSQLADLQQLPDI------LKITEAKLAECQDQLQGYERKNIDLTA 629
Cdd:COG4913 610 AKLAALEAELAELEEELAeaeerlEALEAELDALQERREALQRLAEYswdeidVASAEREIAELEAELERLDASSDDLAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 630 I---ISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATS--AQNVEFLQVIAKREEAI---HQAQLR- 700
Cdd:COG4913 690 LeeqLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEdlARLELRALLEERFAAALgdaVERELRe 769
|
570 580
....*....|....*....|....*.
gi 1907136592 701 -LEEKTRECGSLARQLESAIEDARRQ 725
Cdd:COG4913 770 nLEERIDALRARLNRAEEELERAMRA 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
467-802 |
4.26e-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: 60.46 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 467 DRVTDLVN----QQQSLEEKMRedrdsLVERLHRQTAEYSAfkLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGM 542
Cdd:TIGR02168 189 DRLEDILNelerQLKSLERQAE-----KAERYKELKAELRE--LELALLVLRLEELREELEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 543 IDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNkEIEAARRQFQSQLADLQQlpdilkiteaKLAECQDQLQGYER 622
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEIS-RLEQQKQILRERLANLER----------QLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 623 KNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEAtsaqnveflqviAKREEAIHQAQLRLE 702
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET------------LRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 703 EKTREcgslarQLESAIEDARRQVEQTKEQALSKERAAQS-KILDLETQLSRTKTELGQLRRTRDDAdrryQSRLQDLKD 781
Cdd:TIGR02168 399 NNEIE------RLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERL----EEALEELRE 468
|
330 340
....*....|....*....|.
gi 1907136592 782 RLEQSESTNRSMQNYVQFLKA 802
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQA 489
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
221-807 |
5.39e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.05 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 221 AAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETnrtlrdLLREQHCKEDSERLMEQQGTLLKRLAEA 300
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEV------LEEHEERREELETLEAEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 301 DSEKARLLLLLQDKDKEVEELLQEIQ-------CEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERS 373
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDdllaeagLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 374 GNQHKAEVEAIMEQLKELkqkgDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVK 453
Cdd:PRK02224 351 ADDLEERAEELREEAAEL----ESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 454 DKGDLELEIIVLNDRVTDlvNQQ-----------QSLEEKMR----EDRDSLVERLhrqTAEYSAFKLENERLKASFAPM 518
Cdd:PRK02224 427 REAELEATLRTARERVEE--AEAlleagkcpecgQPVEGSPHvetiEEDRERVEEL---EAELEDLEEEVEEVEERLERA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 519 EDkLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQlercdkenkmlKDEMNKEIEAARRQFQSQLADLQQ 598
Cdd:PRK02224 502 ED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER-----------AAELEAEAEEKREAAAEAEEEAEE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 599 LPDILKITEAKLAECQDQLQGYERknidltaiISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDEL-ERKLEATS 677
Cdd:PRK02224 570 AREEVAELNSKLAELKERIESLER--------IRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKrERKRELEA 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 678 AQNveflqviakrEEAIHQAQLRLEektrecgslarQLESAIEDARRQVEQTKEqalsKERAAQSKILDLETQLSRtkte 757
Cdd:PRK02224 642 EFD----------EARIEEAREDKE-----------RAEEYLEQVEEKLDELRE----ERDDLQAEIGAVENELEE---- 692
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1907136592 758 lgqlrrtrddadrryqsrLQDLKDRLEQSESTnrsmqnyVQFLKASYANV 807
Cdd:PRK02224 693 ------------------LEELRERREALENR-------VEALEALYDEA 717
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
286-798 |
9.27e-09 |
|
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: 59.29 E-value: 9.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 286 LMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLR-CKEAENSRLC 364
Cdd:TIGR00606 417 LQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAEReLSKAEKNSLT 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 365 MQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEE-------YAEQLHVQLADKDlYVAEA 437
Cdd:TIGR00606 497 ETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQirkiksrHSDELTSLLGYFP-NKKQL 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 438 LSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMR------------EDRDSLVERLHRQ-------- 497
Cdd:TIGR00606 576 EDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSsyedklfdvcgsQDEESDLERLKEEieksskqr 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 498 ------TAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKN----YEGMIDNYKSQVMKTRLEADEVAAQLERC 567
Cdd:TIGR00606 656 amlagaTAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSklrlAPDKLKSTESELKKKEKRRDEMLGLAPGR 735
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 568 DKEnkmlKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTaIISDLRSRIEHQGDKLEM 647
Cdd:TIGR00606 736 QSI----IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVT-IMERFQMELKDVERKIAQ 810
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 648 AREKHQAS--QKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQ 725
Cdd:TIGR00606 811 QAAKLQGSdlDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQL 890
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907136592 726 VEQTKE-QALSKE-RAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQSESTNRSMQNYVQ 798
Cdd:TIGR00606 891 VELSTEvQSLIREiKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ 965
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
314-651 |
1.02e-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: 59.30 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 314 KDKEVEELLQEI--------QCEKAQAKTASELSkSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIM 385
Cdd:TIGR02168 675 RRREIEELEEKIeeleekiaELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 386 EQLKELKQKgdrdketlkkaIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIVL 465
Cdd:TIGR02168 754 KELTELEAE-----------IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 466 NDRVTDLVNQQQSLEEKMREdrdsLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDN 545
Cdd:TIGR02168 823 RERLESLERRIAATERRLED----LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 546 YKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKeIEAARRQFQSQLADLQQ--LPDILK---ITEAKLAECQDQLQGY 620
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSltLEEAEAlenKIEDDEEEARRRLKRL 977
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1907136592 621 ERK-----NIDLTAI--ISDLRSR---IEHQGDKLEMAREK 651
Cdd:TIGR02168 978 ENKikelgPVNLAAIeeYEELKERydfLTAQKEDLTEAKET 1018
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
293-737 |
1.86e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 293 LLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLE- 371
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 372 -RSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQ 450
Cdd:COG4717 131 yQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 451 VVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPM------------ 518
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlflvlgllallf 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 519 ------EDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVM-KTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQS 591
Cdd:COG4717 291 lllareKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 592 QLADLQQLPDIlkITEAKLAECQDQLQGYErkniDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENK--QLSQKVDEL 669
Cdd:COG4717 371 EIAALLAEAGV--EDEEELRAALEQAEEYQ----ELKEELEELEEQLEELLGELEELLEALDEEELEEEleELEEELEEL 444
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136592 670 ERKLEATSAQNVEFLQVI--AKREEAIHQAQLRLEEKTRECGSLARQ------LESAIEDARRQVEQTKEQALSKE 737
Cdd:COG4717 445 EEELEELREELAELEAELeqLEEDGELAELLQELEELKAELRELAEEwaalklALELLEEAREEYREERLPPVLER 520
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
497-738 |
4.03e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 497 QTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLercdKENKMLKD 576
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL----AELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 577 EMNKEIEAARRQFQSQLADLQQLPdilKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQ 656
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLG---RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 657 KENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSK 736
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
..
gi 1907136592 737 ER 738
Cdd:COG4942 251 LK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
560-792 |
8.21e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 8.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 560 VAAQLERCDKENKMLKdEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIE 639
Cdd:COG4942 15 AAAQADAAAEAEAELE-QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 640 HQGDKLEmAREKHQASQKENKQLSQKVDELERKLEATSAQNV--------EFLQVIAKREEAIHQAQLRLEEKTRECGSL 711
Cdd:COG4942 94 ELRAELE-AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAvrrlqylkYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 712 ARQLESAIEDARRQveqtkEQALSKERAAQSKIL-DLETQLSRTKTELGQLRRTrddadrryQSRLQDLKDRLEQSESTN 790
Cdd:COG4942 173 RAELEALLAELEEE-----RAALEALKAERQKLLaRLEKELAELAAELAELQQE--------AEELEALIARLEAEAAAA 239
|
..
gi 1907136592 791 RS 792
Cdd:COG4942 240 AE 241
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
316-783 |
1.13e-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: 55.73 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 316 KEVEELLQEiqcEKAQAKTASELSKsMESMRGHLQAQLrckEAENSRLcmqikNLERSGNQHKAEVEAIMEQLKELKQKG 395
Cdd:COG3096 296 GARRQLAEE---QYRLVEMARELEE-LSARESDLEQDY---QAASDHL-----NLVQTALRQQEKIERYQEDLEELTERL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 396 DRDKETLKKA----IRAQkERAEKSEEYAEQLHVQLADkdlyVAEALSTLESWRSRYNQVVKDKGDL-------ELEIIV 464
Cdd:COG3096 364 EEQEEVVEEAaeqlAEAE-ARLEAAEEEVDSLKSQLAD----YQQALDVQQTRAIQYQQAVQALEKAralcglpDLTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 465 LNDRVTDLVNQQQSLEEKMR--EDRDSLVERLHRQTAEysAFKLenerlkasfapmedklnqahleVQQLKASVknyegm 542
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLelEQKLSVADAARRQFEK--AYEL----------------------VCKIAGEV------ 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 543 idnyksqvmkTRLEADEVAAQLERCDKENKMLkdemnkeieAARR-QFQSQLADLQQLPDILKITEAKLAECQDQLQGYE 621
Cdd:COG3096 489 ----------ERSQAWQTARELLRRYRSQQAL---------AQRLqQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQL 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 622 RKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELerkleatsaqnveflqviAKREEAIHQAQLRL 701
Cdd:COG3096 550 DAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKEL------------------AARAPAWLAAQDAL 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 702 EektrecgSLARQLESAIEDArRQVEQTKEQALSKERAAQSkildLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKD 781
Cdd:COG3096 612 E-------RLREQSGEALADS-QEVTAAMQQLLEREREATV----ERDELAARKQALESQIERLSQPGGAEDPRLLALAE 679
|
..
gi 1907136592 782 RL 783
Cdd:COG3096 680 RL 681
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
465-784 |
1.49e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 465 LNDRVTDLVNQQQSLEEKMRE---DRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEG 541
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRienRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 542 MIDNYKSQVMKTRLEADEVAAQLERC-DKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGY 620
Cdd:TIGR02169 759 ELKELEARIEELEEDLHKLEEALNDLeARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 621 ERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLR 700
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 701 LEEKTRECGSLARQLeSAIEDARRQVEQTKEQALSKERaAQSKILDLETQLSRtkteLGQLRRTRDDADRRYQSRLQDLK 780
Cdd:TIGR02169 919 LSELKAKLEALEEEL-SEIEDPKGEDEEIPEEELSLED-VQAELQRVEEEIRA----LEPVNMLAIQEYEEVLKRLDELK 992
|
....
gi 1907136592 781 DRLE 784
Cdd:TIGR02169 993 EKRA 996
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
376-675 |
2.11e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 376 QHKAEVEAIMEQLKELKQKGDRdKETLKKAIRAQKERAEKSEEYAEQLHVQLADK-DLYVAEALSTLESWRSRYNQVVKD 454
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIER-LDLIIDEKRQQLERLRREREKAERYQALLKEKrEYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 455 KGDLELEIIVLNDRVTDLVNQQQSLEEKMREdrdsLVERLHRQTA-EYSAFKLENERLKASFAPMEDKLNQAHLEVQQLK 533
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEE----LNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 534 ASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMN------------------------KEIEAARRQF 589
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEdlraeleevdkefaetrdelkdyrEKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 590 QSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMA--------------REKHQAS 655
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLaadlskyeqelydlKEEYDRV 481
|
330 340
....*....|....*....|
gi 1907136592 656 QKENKQLSQKVDELERKLEA 675
Cdd:TIGR02169 482 EKELSKLQRELAEAEAQARA 501
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
263-798 |
6.08e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 6.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 263 FEETNRTLRDLLREQHCKEDSERLMEQQGTLLK---RLAEADSEKA-----RLLLLLQDKDKEVEELLQEIQCEKAQAKT 334
Cdd:COG4913 234 FDDLERAHEALEDAREQIELLEPIRELAERYAAareRLAELEYLRAalrlwFAQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 335 ASELSKSMESMRGHLQAQLRCKEAEN-SRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERA 413
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 414 EKSEEYAEQLHVQLADkdlyvaealstlesWRSRYNQVVKDKGDLELEIIVLNDRVT----DLVNQQQSLEEKMREDRDS 489
Cdd:COG4913 394 EALEEELEALEEALAE--------------AEAALRDLRRELRELEAEIASLERRKSnipaRLLALRDALAEALGLDEAE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 490 L-------------------VER-LHRQtaeysAFKL--ENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYK 547
Cdd:COG4913 460 LpfvgelievrpeeerwrgaIERvLGGF-----ALTLlvPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 548 SQVMKTRLEADEVAA-------------------QLERCDK---ENKMLKD-----EMNKEIEAARRQF-----QSQLAD 595
Cdd:COG4913 535 SLAGKLDFKPHPFRAwleaelgrrfdyvcvdspeELRRHPRaitRAGQVKGngtrhEKDDRRRIRSRYVlgfdnRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 596 LqqlpdilkitEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGdklemAREKHQASQKENKQLSQKVDELERKLEA 675
Cdd:COG4913 615 L----------EAELAELEEELAEAEERLEALEAELDALQERREALQ-----RLAEYSWDEIDVASAEREIAELEAELER 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 676 TSAQNVEfLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQAlskERAAQSKILDLETQLSRTK 755
Cdd:COG4913 680 LDASSDD-LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL---EAAEDLARLELRALLEERF 755
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1907136592 756 TELGQlRRTRDDADRRYQSRLQDLKDRLEQSEST-NRSMQNYVQ 798
Cdd:COG4913 756 AAALG-DAVERELRENLEERIDALRARLNRAEEElERAMRAFNR 798
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
122-727 |
7.67e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 7.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 122 RYDKKIDSLMNAVGCLKSEVKMQKGERQMAKRFLEERKEELEEVAHELAETEHEntvlrhnIERIKEEKDFTMLQKKHLQ 201
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE-------LARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 202 QEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMtctdintltrQKELLLQKLSTFEETNRTLRDLLREQhcke 281
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE----------AEAELAEAEEALLEAEAELAEAEEEL---- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 282 dsERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASElsksmesmrghLQAQLRCKEAENS 361
Cdd:COG1196 382 --EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE-----------EEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 362 RLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQ-LHVQLADKDLYVAEALST 440
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvKAALLLAGLRGLAGAVAV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 441 LESWRSRYNQVVkdkgdLELEIIVLNDRVTDLVNQQQSLEEKMREdrdslvERLHRQTAeysafkLENERLKASFAPMED 520
Cdd:COG1196 529 LIGVEAAYEAAL-----EAALAAALQNIVVEDDEVAAAAIEYLKA------AKAGRATF------LPLDKIRARAALAAA 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 521 KLNQAHLEVQQLKASVKNYEGMIDnykSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQQLP 600
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARY---YVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 601 DILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQN 680
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1907136592 681 VEFLQVIAKREEAIHQAQLRLEEktrecgsLARQLES-------AIEDARRQVE 727
Cdd:COG1196 749 EEEALEELPEPPDLEELERELER-------LEREIEAlgpvnllAIEEYEELEE 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
314-637 |
1.06e-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: 52.76 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 314 KDKEVEELLQEIQCEKAQAKtASELSKSMESMRghlqAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKEL-- 391
Cdd:TIGR02169 205 REREKAERYQALLKEKREYE-GYELLKEKEALE----RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnk 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 392 --KQKGDRDKETLKKAIR---AQKERAEKS----EEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEI 462
Cdd:TIGR02169 280 kiKDLGEEEQLRVKEKIGeleAEIASLERSiaekERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 463 IVLNDRVTDLVNQQQSLEEKMREDRDSLVERlhrqTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGM 542
Cdd:TIGR02169 360 AELKEELEDLRAELEEVDKEFAETRDELKDY----REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 543 IdnyksqvmkTRLEADevaaqlercdkenkmlKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYER 622
Cdd:TIGR02169 436 I---------NELEEE----------------KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
330
....*....|....*
gi 1907136592 623 KNIDLTAIISDLRSR 637
Cdd:TIGR02169 491 ELAEAEAQARASEER 505
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
219-777 |
1.10e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.66 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 219 AAAAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETNRTLRDLLREQhckEDSERLMEQQGTLLKRLA 298
Cdd:TIGR00618 296 AAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQE---IHIRDAHEVATSIREISC 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 299 EADSEKARLLLLLQDK--DKEVEELL-QEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQ---IKNLER 372
Cdd:TIGR00618 373 QQHTLTQHIHTLQQQKttLTQKLQSLcKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCaaaITCTAQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 373 SGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQ--------LHVQLADKDLYVAEALStlesw 444
Cdd:TIGR00618 453 CEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcplcgscIHPNPARQDIDNPGPLT----- 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 445 rSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDS---LVERLHRQTAEYSAFKLENERLKaSFAPMEDK 521
Cdd:TIGR00618 528 -RRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSfsiLTQCDNRSKEDIPNLQNITVRLQ-DLTEKLSE 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 522 L-------NQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRqfQSQLA 594
Cdd:TIGR00618 606 AedmlaceQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASR--QLALQ 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 595 DLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKE-NKQLSQKVDELERKL 673
Cdd:TIGR00618 684 KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKElMHQARTVLKARTEAH 763
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 674 EATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLArQLESAIEDARRQVEQTK----EQALSKERAAQSKILDLET 749
Cdd:TIGR00618 764 FNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLK-TLEAEIGQEIPSDEDILnlqcETLVQEEEQFLSRLEEKSA 842
|
570 580
....*....|....*....|....*...
gi 1907136592 750 QLSRTKTELGQLRRTRDDADRRYQSRLQ 777
Cdd:TIGR00618 843 TLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
184-794 |
1.53e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.04 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 184 ERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTF 263
Cdd:pfam15921 92 RRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 264 EETNRTLRdLLREQHCKEDSERLMEQQGTLLKRLAEADSekaRLLLLLQDKDKEVEELLQEIQCEkaqaktASELSKSME 343
Cdd:pfam15921 172 IEQLRKMM-LSHEGVLQEIRSILVDFEEASGKKIYEHDS---MSTMHFRSLGSAISKILRELDTE------ISYLKGRIF 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 344 SMRGHLQAqLRCKEAENSRLCMQIKN--LERSGNQHKAEVEAIMEQLKELKQKGDrdketlkkAIRAQKERAEKSEEYAE 421
Cdd:pfam15921 242 PVEDQLEA-LKSESQNKIELLLQQHQdrIEQLISEHEVEITGLTEKASSARSQAN--------SIQSQLEIIQEQARNQN 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 422 QLHV-QLADKDLYVAEALSTLESWRSRYNQVVKDkgdLELEIIVLNDRVTDLVNQQQSLEEK---MREDRDSLVERLHRQ 497
Cdd:pfam15921 313 SMYMrQLSDLESTVSQLRSELREAKRMYEDKIEE---LEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLHKR 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 498 TAEYSAFKLENERL-------KASFAPMEDKLNQAHLEVQQLKASVKnyegmidnyksqVMKTRLEAdEVAAQLERCDKE 570
Cdd:pfam15921 390 EKELSLEKEQNKRLwdrdtgnSITIDHLRRELDDRNMEVQRLEALLK------------AMKSECQG-QMERQMAAIQGK 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 571 NKMLK--DEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMA 648
Cdd:pfam15921 457 NESLEkvSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 649 R---EKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVI--------------AKREEAIHQAQLRLEE----KTRE 707
Cdd:pfam15921 537 KnegDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVgqhgrtagamqvekAQLEKEINDRRLELQEfkilKDKK 616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 708 CGSLaRQLESAIED-----------------ARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADR 770
Cdd:pfam15921 617 DAKI-RELEARVSDlelekvklvnagserlrAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTN 695
|
650 660
....*....|....*....|....
gi 1907136592 771 RYQSRLQDLKDRLEQSESTNRSMQ 794
Cdd:pfam15921 696 KLKMQLKSAQSELEQTRNTLKSME 719
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
173-728 |
1.67e-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: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 173 EHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEmdgaaaaKQVMALK-DTIGKLKTEkqmtctdINTLTR 251
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELE-------AQIRGNGgDRLEQLERE-------IERLER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 252 QKELLLQKLSTFEETNRTL-------RDLLREQHckedsERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQE 324
Cdd:COG4913 353 ELEERERRRARLEALLAALglplpasAEEFAALR-----AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 325 IQcekAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLC--MQIKNLERS---------GNQ---------HKAEVEAI 384
Cdd:COG4913 428 IA---SLERRKSNIPARLLALRDALAEALGLDEAELPFVGelIEVRPEEERwrgaiervlGGFaltllvppeHYAAALRW 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 385 MEQLKeLKQK--GDRDKETLKKAIRAQKER---AEKSE----EYAEQLHVQLADKDLYV----AEALS------TLE--- 442
Cdd:COG4913 505 VNRLH-LRGRlvYERVRTGLPDPERPRLDPdslAGKLDfkphPFRAWLEAELGRRFDYVcvdsPEELRrhpraiTRAgqv 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 443 -SWRSRYnqvVKDKGDLELEIIVLN----DRVTDLVNQQQSLEEKMREdRDSLVERLHRQTAEYSAFKLENERLkASFAP 517
Cdd:COG4913 584 kGNGTRH---EKDDRRRIRSRYVLGfdnrAKLAALEAELAELEEELAE-AEERLEALEAELDALQERREALQRL-AEYSW 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 518 MEDKLNQAHLEVQQLKASVKNyegmIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEM---NKEIEAARRQFQSQLA 594
Cdd:COG4913 659 DEIDVASAEREIAELEAELER----LDASSDDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEELDELQD 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 595 DLQQLPDILKITEAKLAE------CQDQLQGYERKNidLTAIISDLRSRIEHQGDKLEMAREKHQASQKENkqlsqkVDE 668
Cdd:COG4913 735 RLEAAEDLARLELRALLEerfaaaLGDAVERELREN--LEERIDALRARLNRAEEELERAMRAFNREWPAE------TAD 806
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136592 669 LERKLEAtsaqNVEFLQVIAK-REEAIHQ-----AQLRLEEKTRECGSLARQLESAIEDARRQVEQ 728
Cdd:COG4913 807 LDADLES----LPEYLALLDRlEEDGLPEyeerfKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
543-806 |
3.99e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 543 IDNYKSQVMKTRLEADEVAAQLERCD-------KENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQD 615
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDliidekrQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 616 QLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQA-SQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAI 694
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 695 HQAQLRLEEKTREcgslARQLESAIEDARRQVEQTKE--QALSKERAA-QSKILDLETQLSRTKTELGQlrrtrddadrr 771
Cdd:TIGR02169 325 AKLEAEIDKLLAE----IEELEREIEEERKRRDKLTEeyAELKEELEDlRAELEEVDKEFAETRDELKD----------- 389
|
250 260 270
....*....|....*....|....*....|....*
gi 1907136592 772 YQSRLQDLKDRLEQSESTNRSMQNYVQFLKASYAN 806
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
513-742 |
7.74e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 7.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 513 ASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLK---DEMNKEIEAARRQF 589
Cdd:COG3883 9 PTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQaeiAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 590 QSQLADLQQLPDILKITEAKLAecQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDEL 669
Cdd:COG3883 89 GERARALYRSGGSVSYLDVLLG--SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907136592 670 ERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQS 742
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
573-758 |
8.25e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 573 MLKDEMNKEIEAARRQ-------FQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQgDKL 645
Cdd:COG4717 46 MLLERLEKEADELFKPqgrkpelNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 646 EMAREKHQASQKENKQLSQKVDELErKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQ 725
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190
....*....|....*....|....*....|...
gi 1907136592 726 VEQTKEQALSKERAAQSKILDLETQLSRTKTEL 758
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
294-729 |
8.90e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 8.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 294 LKRLAEADSEKARLLLLLQDKDKEVEEL---------LQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLC 364
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAkkkaeekkkADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 365 MQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDK--ETLKKAIRAQK-ERAEKSEEYAEQLHVQLADKDLYVAEALSTL 441
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkaDEAKKAEEAKKaDEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 442 ESWRSRYNQVVKDKGDLELEIIVLNDRVTDLvnqqQSLEEKMREDRDSLVERLHRQTAEySAFKLENERLKASfapmedk 521
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEA----KKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIKAE------- 1623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 522 lnqahlEVQQLKASVKNYEGMIDNYKSQVMKtrleadevAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQqlpd 601
Cdd:PTZ00121 1624 ------ELKKAEEEKKKVEQLKKKEAEEKKK--------AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE---- 1685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 602 ilkitEAKLAECQDQLQGYERKNIDltaiisDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNV 681
Cdd:PTZ00121 1686 -----DEKKAAEALKKEAEEAKKAE------ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1907136592 682 EFLQVIAKREEAIHQAQLRLEEKTrecGSLARQLESAIEDARRQVEQT 729
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKE---AVIEEELDEEDEKRRMEVDKK 1799
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
349-738 |
1.41e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.86 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 349 LQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLH-VQL 427
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqLKS 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 428 ADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMRE---DRDSLVERLHRQTAEYSAF 504
Cdd:TIGR04523 296 EISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNsesENSEKQRELEEKQNEIEKL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 505 KLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDE---MNKE 581
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvKELI 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 582 IEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQ 661
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 662 LSQKVDELERKLEA-----TSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSK 736
Cdd:TIGR04523 536 KESKISDLEDELNKddfelKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSL 615
|
..
gi 1907136592 737 ER 738
Cdd:TIGR04523 616 EK 617
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
637-792 |
1.68e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 637 RIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQnveflqvIAKREEAIHQAQLRLEEKTRECGSLARQLE 716
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE-------LEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136592 717 SAIEDaRRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQSESTNRS 792
Cdd:COG1196 306 RLEER-RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
446-677 |
1.73e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.47 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 446 SRYNQVVKDKgdleleIIVLNDRVTDLVNQQQSLEEKMREDRDsLVERLHRQTAEysafklENERLKASFAPMEDKLNQA 525
Cdd:PHA02562 166 SEMDKLNKDK------IRELNQQIQTLDMKIDHIQQQIKTYNK-NIEEQRKKNGE------NIARKQNKYDELVEEAKTI 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 526 HLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKD------------EMNKEIEAARrqfqSQL 593
Cdd:PHA02562 233 KAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqqisEGPDRITKIK----DKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 594 ADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLR---SRIEHQGDKLEMAREKHQASQKENK-QLSQKVDEL 669
Cdd:PHA02562 309 KELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKqslITLVDKAKKVKAAIEELQAEFVDNAeELAKLQDEL 388
|
....*...
gi 1907136592 670 ERKLEATS 677
Cdd:PHA02562 389 DKIVKTKS 396
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
386-758 |
2.28e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.13 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 386 EQLK-ELKQ----KGDRDKET---LKKAIRA---QKERAEKSEEY----------AEQLHVQLADKDLYVAEALSTLESw 444
Cdd:PRK10929 26 KQITqELEQakaaKTPAQAEIveaLQSALNWleeRKGSLERAKQYqqvidnfpklSAELRQQLNNERDEPRSVPPNMST- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 445 rsrynqvvkdkGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPmEDKLNQ 524
Cdd:PRK10929 105 -----------DALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTP-NTPLAQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 525 AHL-----EVQQLKASVKNYE--GMIDNYKSQVmkTRLEADEVAAQLERCDKENKMLKDEMNkeieaARRQFQSQLAdlq 597
Cdd:PRK10929 173 AQLtalqaESAALKALVDELElaQLSANNRQEL--ARLRSELAKKRSQQLDAYLQALRNQLN-----SQRQREAERA--- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 598 qlpdiLKITEaKLAECQDqlqgyerkniDLTAIISdlrsriehqgDKLEMAREkhqASQKENKQlSQKVDELERKLEATS 677
Cdd:PRK10929 243 -----LESTE-LLAEQSG----------DLPKSIV----------AQFKINRE---LSQALNQQ-AQRMDLIASQQRQAA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 678 AQNVEFLQVI-AKREEA-----------IHQAQL-RLEEKTRecgslARQLESAIEDAR----------------RQVEQ 728
Cdd:PRK10929 293 SQTLQVRQALnTLREQSqwlgvsnalgeALRAQVaRLPEMPK-----PQQLDTEMAQLRvqrlryedllnkqpqlRQIRQ 367
|
410 420 430
....*....|....*....|....*....|
gi 1907136592 729 TKEQALSkerAAQSKILDleTQLsRTKTEL 758
Cdd:PRK10929 368 ADGQPLT---AEQNRILD--AQL-RTQREL 391
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
376-783 |
3.98e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 376 QHKAEVEAIMEQLKELKQKgdrdKETLKKAIRAQKERAEKSEEYAEQLHVQLADkdlyVAEALSTLESWRSRYNQVVK-- 453
Cdd:PRK04863 352 RYQADLEELEERLEEQNEV----VEEADEQQEENEARAEAAEEEVDELKSQLAD----YQQALDVQQTRAIQYQQAVQal 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 454 DK-----GDLELEIIVLNDRVTDLVNQQQSLEEKMR--EDRDSLVERLHRQTAEysAFKLenerlkasfapmedklnqah 526
Cdd:PRK04863 424 ERakqlcGLPDLTADNAEDWLEEFQAKEQEATEELLslEQKLSVAQAAHSQFEQ--AYQL-------------------- 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 527 leVQQLKASVknyegmidnyksqvmkTRLEADEVAAQLERCDKENKMLkdemnkeieAARR-QFQSQLADLQQLPDILKI 605
Cdd:PRK04863 482 --VRKIAGEV----------------SRSEAWDVARELLRRLREQRHL---------AEQLqQLRMRLSELEQRLRQQQR 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 606 TEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELErkleatsaqnveflq 685
Cdd:PRK04863 535 AERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLA--------------- 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 686 viaKREEAIHQAQLRLEEktrecgsLARQLESAIEDArRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTR 765
Cdd:PRK04863 600 ---ARAPAWLAAQDALAR-------LREQSGEEFEDS-QDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPG 668
|
410
....*....|....*...
gi 1907136592 766 DDADrryqSRLQDLKDRL 783
Cdd:PRK04863 669 GSED----PRLNALAERF 682
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
581-746 |
4.35e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 581 EIEAARRQFQSQLADLQQLpdiLKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMARekhqaSQKENK 660
Cdd:COG1579 21 RLEHRLKELPAELAELEDE---LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-----NNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 661 QLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQveqtkEQALSKERAA 740
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE-----LEELEAEREE 167
|
....*.
gi 1907136592 741 QSKILD 746
Cdd:COG1579 168 LAAKIP 173
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
95-757 |
4.65e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 95 SSEKLV-SVMRLSDLSTEDDDSGHCK--MNRYDKKIDSLMNAVGCLKSEVKMQKGERQMAKRFLEERKEELEEVAHELAE 171
Cdd:PRK03918 146 SREKVVrQILGLDDYENAYKNLGEVIkeIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 172 TEHENTVLRHNIERIKEEKdftmLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTekqmtctdintlTR 251
Cdd:PRK03918 226 LEKEVKELEELKEEIEELE----KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE------------LK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 252 QKELLLQKLSTF-EETNRTLRDLlreqhcKEDSERLMEQQGTLLKRLAEADSEKARLLLLLqdkdKEVEELLQEIQCEKA 330
Cdd:PRK03918 290 EKAEEYIKLSEFyEEYLDELREI------EKRLSRLEEEINGIEERIKELEEKEERLEELK----KKLKELEKRLEELEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 331 QAKTASELSKSMESMRGhLQAQLRCKEAEnsRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQK 410
Cdd:PRK03918 360 RHELYEEAKAKKEELER-LKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 411 E----RAEKSEEYAEQLhvqLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIVLND--RVTDLVNQQQSLEEKMR 484
Cdd:PRK03918 437 KcpvcGRELTEEHRKEL---LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 485 EDRdslVERLHRQTAEYSAFKLENERLKASFAPMEDKLNqahlEVQQLKASVKNYEGMIDNYKSqvmktrlEADEVAAQL 564
Cdd:PRK03918 514 KYN---LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE----KLEELKKKLAELEKKLDELEE-------ELAELLKEL 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 565 ERCDKENKMLKDEMNKEIEAARRQFQSqladLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQG-- 642
Cdd:PRK03918 580 EELGFESVEELEERLKELEPFYNEYLE----LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEkk 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 643 ---DKLEMAREKHQASQKENKQLSQKVDELERKLEaTSAQNVEFLQviaKREEAIHQAQLRLEektrecgslarQLESAI 719
Cdd:PRK03918 656 yseEEYEELREEYLELSRELAGLRAELEELEKRRE-EIKKTLEKLK---EELEEREKAKKELE-----------KLEKAL 720
|
650 660 670
....*....|....*....|....*....|....*...
gi 1907136592 720 EDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTE 757
Cdd:PRK03918 721 ERVEELREKVKKYKALLKERALSKVGEIASEIFEELTE 758
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
557-756 |
6.30e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 557 ADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRS 636
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 637 RIEHQGDKL--------------------------------EMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFL 684
Cdd:COG4942 98 ELEAQKEELaellralyrlgrqpplalllspedfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907136592 685 QVIAKREEAihQAQLRLEEKTREcgSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKT 756
Cdd:COG4942 178 ALLAELEEE--RAALEALKAERQ--KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
465-793 |
8.43e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.30 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 465 LNDRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAE----YSAFKLENERLKASF-------APMEDKLNQAHLEVQQLK 533
Cdd:pfam00038 9 LNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpsrlYSLYEKEIEDLRRQLdtltverARLQLELDNLRLAAEDFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 534 ASVKNYEGMIDNYKSQVMKTRLEADEvaAQLERCDKENKMlkDEMNKEIEAARRQFQSQLADLQqlpdilkiteAKLAEC 613
Cdd:pfam00038 89 QKYEDELNLRTSAENDLVGLRKDLDE--ATLARVDLEAKI--ESLKEELAFLKKNHEEEVRELQ----------AQVSDT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 614 QDQLQGYERKNIDLTAIISDLRSRIEHQgdkleMAREKHQASQkenkQLSQKVDELERkleaTSAQNVEFLQviAKREEa 693
Cdd:pfam00038 155 QVNVEMDAARKLDLTSALAEIRAQYEEI-----AAKNREEAEE----WYQSKLEELQQ----AAARNGDALR--SAKEE- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 694 IHQAQLRLEEKTRECGSLARQLESaIEDARRQVEQTKEQALSKeraAQSKILDLETQLSRTKTELGQLrrtrddaDRRYQ 773
Cdd:pfam00038 219 ITELRRTIQSLEIELQSLKKQKAS-LERQLAETEERYELQLAD---YQELISELEAELQETRQEMARQ-------LREYQ 287
|
330 340
....*....|....*....|
gi 1907136592 774 SrLQDLKDRLEQSESTNRSM 793
Cdd:pfam00038 288 E-LLNVKLALDIEIATYRKL 306
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
507-761 |
8.79e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 45.83 E-value: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 507 ENERLKASFAPMEDKLNqahlEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENkmlkdemnkeiEAAR 586
Cdd:pfam19220 4 RNELLRVRLGEMADRLE----DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAY-----------GKLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 587 RQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKV 666
Cdd:pfam19220 69 RELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 667 DELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLAR---QLESAIEDARRQVEQTkEQALSKERAAQSK 743
Cdd:pfam19220 149 QAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRrlaELETQLDATRARLRAL-EGQLAAEQAERER 227
|
250
....*....|....*....
gi 1907136592 744 IL-DLETQLSRTKTELGQL 761
Cdd:pfam19220 228 AEaQLEEAVEAHRAERASL 246
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
579-800 |
1.25e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 579 NKEIEAARRQFQSQLADLQQlpdilkiteaKLAECQDQLQGYERKN--IDLTAIISDLRSRIEHQGDKLEMAREKHQASQ 656
Cdd:COG3206 170 REEARKALEFLEEQLPELRK----------ELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 657 kenkqlsQKVDELERKLEATSAQNVEFLQ--VIAKREEAIHQAQLRLEEKTRECG--------------SLARQLESAIE 720
Cdd:COG3206 240 -------ARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTpnhpdvialraqiaALRAQLQQEAQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 721 DARRQVEQTKEQALSKERAAQSKILDLETQ---LSRTKTELGQLRRTRDDADRRYQSrlqdLKDRLEQSESTNRSMQNYV 797
Cdd:COG3206 313 RILASLEAELEALQAREASLQAQLAQLEARlaeLPELEAELRRLEREVEVARELYES----LLQRLEEARLAEALTVGNV 388
|
...
gi 1907136592 798 QFL 800
Cdd:COG3206 389 RVI 391
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
166-416 |
1.47e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 166 AHELAETEHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTD 245
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 246 INTLTRQKELLLQKLSTFEETNRtLRDLLREQHCKEDSERLMeqqgtLLKRLAEADSEKARlllllqdkdkEVEELLQEI 325
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPP-LALLLSPEDFLDAVRRLQ-----YLKYLAPARREQAE----------ELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 326 QcekaqaktasELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKA 405
Cdd:COG4942 163 A----------ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
250
....*....|.
gi 1907136592 406 IRAQKERAEKS 416
Cdd:COG4942 233 EAEAAAAAERT 243
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
281-743 |
1.64e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 281 EDSERLMEQQGTLLKRLAEaDSEKARLLLLLQDKdKEVEELLQEIQCEKAQAKTASELSKSMESMRGHlQAQLRCKEAEN 360
Cdd:PTZ00121 1143 EEARKAEDAKRVEIARKAE-DARKAEEARKAEDA-KKAEAARKAEEVRKAEELRKAEDARKAEAARKA-EEERKAEEARK 1219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 361 SRLCMQIKNLERSGNQHKAEVEAIMEQlKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKdlyVAEALST 440
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEAKKDAEEAKKAE-EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE---KKKADEA 1295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 441 LESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDSlvERLHRQTAEYSAFKLENERLKASFAPME- 519
Cdd:PTZ00121 1296 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA--AEAAKAEAEAAADEAEAAEEKAEAAEKKk 1373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 520 -------DKLNQAHLEVQQLKASVKNYEGmiDNYKSQVMKTRLEADEVAAQLERcDKENKMLKDEMNKEIEAARR--QFQ 590
Cdd:PTZ00121 1374 eeakkkaDAAKKKAEEKKKADEAKKKAEE--DKKKADELKKAAAAKKKADEAKK-KAEEKKKADEAKKKAEEAKKadEAK 1450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 591 SQLADLQQLPDILKITE--------AKLAECQDQLQGYERKNIDLTAIISDLRSRIE--HQGDKLEMAREKHQASQKENK 660
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEeakkadeaKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEakKKADEAKKAEEAKKADEAKKA 1530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 661 QLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAA 740
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
...
gi 1907136592 741 QSK 743
Cdd:PTZ00121 1611 EAK 1613
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
298-796 |
2.81e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 298 AEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSmesmrghlQAQLRCKEAENSRLCMQIKNLERSGNQH 377
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKA--------EAEAAADEAEAAEEKAEAAEKKKEEAKK 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 378 KAE-VEAIMEQLK---ELKQKGDRDK---ETLKKAiRAQKERAEKSEEYAEQlhVQLADKDLYVAEALSTLESWRSRYNQ 450
Cdd:PTZ00121 1379 KADaAKKKAEEKKkadEAKKKAEEDKkkaDELKKA-AAAKKKADEAKKKAEE--KKKADEAKKKAEEAKKADEAKKKAEE 1455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 451 VVKDKgdlELEIIVLNDRVTDlvNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQ 530
Cdd:PTZ00121 1456 AKKAE---EAKKKAEEAKKAD--EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA 1530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 531 QLKASVKNYEGMIDNYKSQVMKTRLE---ADEV----AAQLERCDKENKMLKDEMNKEIEAARRQfqsQLADLQQLPDIL 603
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADELKKAEElkkAEEKkkaeEAKKAEEDKNMALRKAEEAKKAEEARIE---EVMKLYEEEKKM 1607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 604 KITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLE----ATSAQ 679
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEeakkAEEDE 1687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 680 NVEFLQVIAKREEAIHQAQLRleEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLE-----TQLSRT 754
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELK--KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEekkkiAHLKKE 1765
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1907136592 755 KTELGQLRRTRDDADRRYQSRLQDLKDRLEQSESTNRSMQNY 796
Cdd:PTZ00121 1766 EEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNF 1807
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
590-789 |
4.17e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 590 QSQLAD-LQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDE 668
Cdd:pfam07888 33 QNRLEEcLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 669 LERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTREcgslarqLESAIEDARRQVEQTKEQAlSKERAAQSKILDLE 748
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETE-------LERMKERAKKAGAQRKEEE-AERKQLQAKLQQTE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907136592 749 TQLSRTKTELGQLRRTRDDADRRYQsRLQDLKDRLEQSEST 789
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVL-QLQDTITTLTQKLTT 224
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
476-802 |
4.23e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 476 QQSLEE----KMREDRDSLVERLHRQTAEysafKLENERLKAsfapmedklnqahLEVQQLKASVKNYEGMIDNYKSQVM 551
Cdd:TIGR02169 173 EKALEEleevEENIERLDLIIDEKRQQLE----RLRREREKA-------------ERYQALLKEKREYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 552 KTRLEAdeVAAQLERCDKENKMLK---DEMNKEIEAARrqfqsqladlQQLPDILKITEAKLAECQDQLQgyeRKNIDLT 628
Cdd:TIGR02169 236 ERQKEA--IERQLASLEEELEKLTeeiSELEKRLEEIE----------QLLEELNKKIKDLGEEEQLRVK---EKIGELE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 629 AIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREE---------------- 692
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEeledlraeleevdkef 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 693 -----AIHQAQLRLEEKTRECGSL----------ARQLESAIEDARRQVEQTKEQALSKERAAQSKILDL---ETQLSRT 754
Cdd:TIGR02169 381 aetrdELKDYREKLEKLKREINELkreldrlqeeLQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIkkqEWKLEQL 460
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1907136592 755 KTELGQLRRTRDDADRRY---QSRLQDLKDRLEQSESTNRSMQNYVQFLKA 802
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYdrvEKELSKLQRELAEAEAQARASEERVRGGRA 511
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
312-503 |
7.34e-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: 42.83 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 312 QDKDKEVEELLQEIQcekAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKEL 391
Cdd:COG4942 19 ADAAAEAEAELEQLQ---QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 392 KQKGDRDKETLKKAIRAQKERAEKSE-------EYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIV 464
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907136592 465 LNDRVTDLVNQQQSLEEKMREdRDSLVERLHRQTAEYSA 503
Cdd:COG4942 176 LEALLAELEEERAALEALKAE-RQKLLARLEKELAELAA 213
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
162-801 |
8.09e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.04 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 162 LEEVAHELAETEHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMdgaaaAKQVMALKDTIGKLKTEKQM 241
Cdd:pfam02463 178 LIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL-----KLNEERIDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 242 TCTDINTLTRQKELLLQKLSTFEETNRTLRDLLREQHCKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEEL 321
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 322 LQEIQCEKAQAKTASELSKSM--ESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDK 399
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAeeEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLE 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 400 ETLKKAIRAQKERAEKSEEYAEQLHVQLAD--KDLYVAEALSTLESWRSRYNQVVKDKGDLELEIivlndrvtdlVNQQQ 477
Cdd:pfam02463 413 LARQLEDLLKEEKKEELEILEEEEESIELKqgKLTEEKEELEKQELKLLKDELELKKSEDLLKET----------QLVKL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 478 SLEEKMREDRDSLVERLHRQTAeysafklENERLKASFAPMEDKLNQAHLEVQQLKasvKNYEGMIDNYKSQVMKTRLEA 557
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQKESK-------ARSGLKVLLALIKDGVGGRIISAHGRL---GDLGVAVENYKVAISTAVIVE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 558 DEVAAQLerCDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTA----IISD 633
Cdd:pfam02463 553 VSATADE--VEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAkvveGILK 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 634 LRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLAR 713
Cdd:pfam02463 631 DTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 714 QLESAIEDARRQVEQTKEQALSKeraAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQSESTNRSM 793
Cdd:pfam02463 711 ELKKLKLEAEELLADRVQEAQDK---INEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLK 787
|
....*...
gi 1907136592 794 QNYVQFLK 801
Cdd:pfam02463 788 VEEEKEEK 795
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
492-761 |
8.28e-04 |
|
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: 43.02 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 492 ERLHRQTAEYSAFKLENERlkASFAPMEDKLNQAHLEVQQLKASVKNYEGMID-----NYKSQVMKTRLEADEVAAQLER 566
Cdd:COG5185 256 EKLVEQNTDLRLEKLGENA--ESSKRLNENANNLIKQFENTKEKIAEYTKSIDikkatESLEEQLAAAEAEQELEESKRE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 567 CDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKIT--EAKLAECQDQLqgyERKNIDLTAIISDLRSRIEhqgDK 644
Cdd:COG5185 334 TETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSksSEELDSFKDTI---ESTKESLDEIPQNQRGYAQ---EI 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 645 LEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKRE-EAIHQAQLRLEEKTREcgsLARQLESAIEDAR 723
Cdd:COG5185 408 LATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMrEADEESQSRLEEAYDE---INRSVRSKKEDLN 484
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907136592 724 RQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQL 761
Cdd:COG5185 485 EELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQV 522
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
609-757 |
1.12e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 609 KLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQ-----NVEF 683
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrNNKE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907136592 684 LQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTE 757
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
596-787 |
1.18e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.55 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 596 LQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEA 675
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 676 TSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLesaiedarRQVEQTKEQALSKERAAQSKILDLETQLSRTK 755
Cdd:pfam00261 83 LENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKL--------VVVEGDLERAEERAELAESKIVELEEELKVVG 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1907136592 756 TELGQL---RRTRDDADRRYQSRLQDLKDRLEQSE 787
Cdd:pfam00261 155 NNLKSLeasEEKASEREDKYEEQIRFLTEKLKEAE 189
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
312-670 |
1.20e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 312 QDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLErsgnQHKAEVEAIMEQLKEL 391
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ----QEKELLEKEIERLKET 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 392 KQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLE-------SWRSRYNQVVKDKGDLELEIIV 464
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEqkqkelkSKEKELKKLNEEKKELEEKVKD 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 465 LNDRVTDLVNQQQSLEEKMREDRDSLVERlhRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMID 544
Cdd:TIGR04523 515 LTKKISSLKEKIEKLESEKKEKESKISDL--EDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 545 NYKSQVMKTRLEADEVAAQLERCDKENKMLKDEmNKEIEAARRQFQSQLADLQQL----PDILKITEAKLAECQDQLQGY 620
Cdd:TIGR04523 593 QKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE-NEKLSSIIKNIKSKKNKLKQEvkqiKETIKEIRNKWPEIIKKIKES 671
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907136592 621 ERKNIDLTAIISD------------LRSRIEHQgdKLEMAREKHQASQKENKQLSQKVDELE 670
Cdd:TIGR04523 672 KTKIDDIIELMKDwlkelslhykkyITRMIRIK--DLPKLEEKYKEIEKELKKLDEFSKELE 731
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
165-566 |
1.20e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 165 VAHELAETEHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCT 244
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 245 DINTLTRQKELLL-------QKLSTFEETNRTLRDLLREqhckedSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKE 317
Cdd:PRK02224 406 DLGNAEDFLEELReerdelrEREAELEATLRTARERVEE------AEALLEAGKCPECGQPVEGSPHVETIEEDRERVEE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 318 VEELLQEIQCEKAqaktasELSKSMESMRghlqaQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQkgdr 397
Cdd:PRK02224 480 LEAELEDLEEEVE------EVEERLERAE-----DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE---- 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 398 DKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDlyvaEALSTLESWRSRYNQVVkdkgDLELEIIVLNDRVTDLVNQQQ 477
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELN----SKLAELKERIESLERIR----TLLAAIADAEDEIERLREKRE 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 478 SLEEKMREDRDSLVERLHRQTAEYSAFKLEN-ERLKASFAPMEDKLNQAHLEVQQL---KASVKNYEGMIDNYKSQVMKT 553
Cdd:PRK02224 617 ALAELNDERRERLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELreeRDDLQAEIGAVENELEELEEL 696
|
410
....*....|...
gi 1907136592 554 RLEADEVAAQLER 566
Cdd:PRK02224 697 RERREALENRVEA 709
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
168-485 |
1.32e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 168 ELAETEHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTctDIN 247
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS--RIP 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 248 TLTRQKELLLQKLSTFEETNRTLRDLLREQHCKEDSERlmEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIqc 327
Cdd:TIGR02169 795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE--KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL-- 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 328 EKAQAKTaselsKSMESMRGHLqaqlrckEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIR 407
Cdd:TIGR02169 871 EELEAAL-----RDLESRLGDL-------KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED 938
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 408 AQKERAEKSEEYAEQLHVQLadKDLYVAEALSTLESWRSR----YNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKM 483
Cdd:TIGR02169 939 PKGEDEEIPEEELSLEDVQA--ELQRVEEEIRALEPVNMLaiqeYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
..
gi 1907136592 484 RE 485
Cdd:TIGR02169 1017 RE 1018
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
603-830 |
1.46e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 603 LKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEA------T 676
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralyR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 677 SAQNVEFLQVIAKRE---EAIHQAQL--RLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQL 751
Cdd:COG3883 98 SGGSVSYLDVLLGSEsfsDFLDRLSAlsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 752 SRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQ----SESTNRSMQNYVQFLKASYANVFGDAPYTSSYLTSSPIRSRS 827
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAaaaaAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
...
gi 1907136592 828 PPA 830
Cdd:COG3883 258 AAG 260
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
179-804 |
1.66e-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: 42.08 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 179 LRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDgaaaakqVMALKDTIGKLKTEKQMTCTDINTLTRQ------ 252
Cdd:pfam01576 101 MQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEED-------ILLLEDQNSKLSKERKLLEERISEFTSNlaeeee 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 253 KELLLQKLSTFEETNRT-LRDLLRE-----QHCKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQ 326
Cdd:pfam01576 174 KAKSLSKLKNKHEAMISdLEERLKKeekgrQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 327 CEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQL---KELKQKGDRDKETLK 403
Cdd:pfam01576 254 EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTaaqQELRSKREQEVTELK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 404 KAIRAQKERAEKSEEYAEQLHVQladkdlyvaealsTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKm 483
Cdd:pfam01576 334 KALEEETRSHEAQLQEMRQKHTQ-------------ALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQA- 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 484 REDRDSLVERLHRQTAEYSAFKLENERLKASFApmeDKLNQAHLEVQQLKASVKNYEGM-------IDNYKSQVMKTR-L 555
Cdd:pfam01576 400 KQDSEHKRKKLEGQLQELQARLSESERQRAELA---EKLSKLQSELESVSSLLNEAEGKniklskdVSSLESQLQDTQeL 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 556 EADEVAAQLE-----RCDKENKMLKDEMNKEIEAARRQFQSQLADLQ-QLPDILKITEAKLAECQDQLQGYERKNIDLTA 629
Cdd:pfam01576 477 LQEETRQKLNlstrlRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQaQLSDMKKKLEEDAGTLEALEEGKKRLQRELEA 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 630 IISDLRSRIEhQGDKLEMAREKHQASQK----ENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKT 705
Cdd:pfam01576 557 LTQQLEEKAA-AYDKLEKTKNRLQQELDdllvDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKE 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 706 RECGSLARQLESAIEdARRQVEQTKEQAlskeRAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQ 785
Cdd:pfam01576 636 TRALSLARALEEALE-AKEELERTNKQL----RAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQA 710
|
650
....*....|....*....
gi 1907136592 786 SESTNRSMQNYVQFLKASY 804
Cdd:pfam01576 711 TEDAKLRLEVNMQALKAQF 729
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
465-671 |
1.67e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 465 LNDRVTDLvNQQQSLEEKMREDRDSLVERLhrqTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGmid 544
Cdd:PRK09039 58 LNSQIAEL-ADLLSLERQGNQDLQDSVANL---RASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQ--- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 545 nyksqvmktrlEADEVAAQLERcdkenkmlkdeMNKEIEAARRqfqsQLADLQQLpdiLKITEAKLAECQDQlqgyerkn 624
Cdd:PRK09039 131 -----------VSARALAQVEL-----------LNQQIAALRR----QLAALEAA---LDASEKRDRESQAK-------- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907136592 625 idltaiISDLRSRIehqgdklemarekhqasqkeNKQLSQKVDELER 671
Cdd:PRK09039 174 ------IADLGRRL--------------------NVALAQRVQELNR 194
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
519-758 |
1.77e-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: 42.08 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 519 EDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAArrqfqsqladlqq 598
Cdd:pfam01576 88 EERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKER------------- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 599 lpdilKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSA 678
Cdd:pfam01576 155 -----KLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 679 QNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLA---RQLESAIEDARRQVEQTKEQALSKERAAQskilDLETQLSRTK 755
Cdd:pfam01576 230 QIAELRAQLAKKEEELQAALARLEEETAQKNNALkkiRELEAQISELQEDLESERAARNKAEKQRR----DLGEELEALK 305
|
...
gi 1907136592 756 TEL 758
Cdd:pfam01576 306 TEL 308
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
219-405 |
2.03e-03 |
|
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];
Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 41.60 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 219 AAAAKQVMALKDTIGKLKTEKQmtctdINTLTRQKELLLQKLSTFEETNRTLRDLLREQhckedsERLMEQQGTLL--KR 296
Cdd:COG4192 68 VAALPEFAAATNTTERSQLRNQ-----LNTQLADIEELLAELEQLTQDAGDLRAAVADL------RNLLQQLDSLLtqRI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 297 LAEADSEKA--RLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENsrlcmQIKNL--ER 372
Cdd:COG4192 137 ALRRRLQELleQINWLHQDFNSELTPLLQEASWQQTRLLDSVETTESLRNLQNELQLLLRLLAIEN-----QIVSLlrEV 211
|
170 180 190
....*....|....*....|....*....|...
gi 1907136592 373 SGNQHKAEVEAIMEQLKELKQKGDRDKETLKKA 405
Cdd:COG4192 212 AAARDQADVDNLFDRLQYLKDELDRNLQALKNY 244
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
407-804 |
2.07e-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: 41.86 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 407 RAQKERAEKSEEYAEQLHVQLADKDLYVAEaLSTLESWRSRY---NQVVKDKGDLELEIIVLNDRVTDL---VNQQQSLE 480
Cdd:COG3096 781 AAREKRLEELRAERDELAEQYAKASFDVQK-LQRLHQAFSQFvggHLAVAFAPDPEAELAALRQRRSELereLAQHRAQE 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 481 EKMREDRDSLVER---LHRQTAEYSAFKLE--NERLKASFAPMeDKLNQAHLEVQQLKASVKNYEGMIDNYKSqvmkTRL 555
Cdd:COG3096 860 QQLRQQLDQLKEQlqlLNKLLPQANLLADEtlADRLEELREEL-DAAQEAQAFIQQHGKALAQLEPLVAVLQS----DPE 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 556 EADEVAAQLERCDKENKMLKdemnKEIEA-----ARR---------QFQSQLADL-QQLPDILKITEAKLAECQDQLQGY 620
Cdd:COG3096 935 QFEQLQADYLQAKEQQRRLK----QQIFAlsevvQRRphfsyedavGLLGENSDLnEKLRARLEQAEEARREAREQLRQA 1010
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 621 ERKNIDLTAIISDLRSRiehqgdkLEMAREKHQASQKENKQLS------------QKVDELERKLEATSAQNVEFLQVIA 688
Cdd:COG3096 1011 QAQYSQYNQVLASLKSS-------RDAKQQTLQELEQELEELGvqadaeaeerarIRRDELHEELSQNRSRRSQLEKQLT 1083
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 689 KREEAIHQAQLRLeektrecgslaRQLESAIEDARRQVEQTKE-----QALSKERaaqskilDLETQLSRTKT------E 757
Cdd:COG3096 1084 RCEAEMDSLQKRL-----------RKAERDYKQEREQVVQAKAgwcavLRLARDN-------DVERRLHRRELaylsadE 1145
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1907136592 758 LGQLRRTRDDADRRYQSRLQDLKDRLEQSEStNRSMQNYVQFLKASY 804
Cdd:COG3096 1146 LRSMSDKALGALRLAVADNEHLRDALRLSED-PRRPERKVQFYIAVY 1191
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
367-731 |
3.19e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.99 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 367 IKNLERSGNQHKAEVEAIMEQLKElkqkgdrdketLKKAIRAQKERAEKSEEYAEqlhvqladkdlyvaEALSTLESWRS 446
Cdd:pfam06160 109 LDELLESEEKNREEVEELKDKYRE-----------LRKTLLANRFSYGPAIDELE--------------KQLAEIEEEFS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 447 RYNQVVKDkGD-LELEIIVLNdrvtdLVNQQQSLEEKMrEDRDSLVERLHrqtaeySAFKLENERLKASFAPMEDKlnQA 525
Cdd:pfam06160 164 QFEELTES-GDyLEAREVLEK-----LEEETDALEELM-EDIPPLYEELK------TELPDQLEELKEGYREMEEE--GY 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 526 HLEVQQLKASVKNYEGMIDNYKSQVmkTRLEADEVAAQLERCDKENKMLKDEMNKEIEaARRQFQSQLA----DLQQLPD 601
Cdd:pfam06160 229 ALEHLNVDKEIQQLEEQLEENLALL--ENLELDEAEEALEEIEERIDQLYDLLEKEVD-AKKYVEKNLPeiedYLEHAEE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 602 ILKITEAKLAECQD-----------------QLQGYERKNIDLTAII-------SDLRSRIEHQGDKLEMAREKH----- 652
Cdd:pfam06160 306 QNKELKEELERVQQsytlnenelervrglekQLEELEKRYDEIVERLeekevaySELQEELEEILEQLEEIEEEQeefke 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 653 --QASQKENKQLSQKVDELERKLEAT----SAQNV-----EFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIED 721
Cdd:pfam06160 386 slQSLRKDELEAREKLDEFKLELREIkrlvEKSNLpglpeSYLDYFFDVSDEIEDLADELNEVPLNMDEVNRLLDEAQDD 465
|
410
....*....|
gi 1907136592 722 ARRQVEQTKE 731
Cdd:pfam06160 466 VDTLYEKTEE 475
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
435-756 |
3.54e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.83 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 435 AEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRD--SLVERLHRQTAEYSAfKLENERLK 512
Cdd:pfam05622 127 SDKVKKLEATVETYKKKLEDLGDLRRQVKLLEERNAEYMQRTLQLEEELKKANAlrGQLETYKRQVQELHG-KLSEESKK 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 513 ASFAPMEDKLNQAHLE---------------------------VQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLE 565
Cdd:pfam05622 206 ADKLEFEYKKLEEKLEalqkekerliierdtlretneelrcaqLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 566 RCDKENKMLKdemnkeiEAARRQFQSQLADLQQLpdiLKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGD-- 643
Cdd:pfam05622 286 RLQHENKMLR-------LGQEGSYRERLTELQQL---LEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSka 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 644 --------KLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAqlrLEEKTRECGSLARQL 715
Cdd:pfam05622 356 edssllkqKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEALRKKDEDMKA---MEERYKKYVEKAKSV 432
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1907136592 716 ESAIEDARRQVEQTKEQALSKERAAQSK-ILDLETQLSRTKT 756
Cdd:pfam05622 433 IKTLDPKQNPASPPEIQALKNQLLEKDKkIEHLERDFEKSKL 474
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
193-475 |
3.77e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.22 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 193 TMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKT----EKQMTCTDINTLTRQKELLLQKLSTFEETNR 268
Cdd:COG5022 780 GFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKtikrEKKLRETEEVEFSLKAEVLIQKFGRSLKAKK 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 269 TLRDLLREQhCKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQC---EKAQAKTA--SELSKSME 343
Cdd:COG5022 860 RFSLLKKET-IYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSdliENLEFKTEliARLKKLLN 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 344 SMRGHLQAQL-RCKEAENSRLCMQIKNLERSGNQHKAEV---EAIMEQLKELKQKGDRDKETLKKaIRAQKERAEKSEEY 419
Cdd:COG5022 939 NIDLEEGPSIeYVKLPELNKLHEVESKLKETSEEYEDLLkksTILVREGNKANSELKNFKKELAE-LSKQYGALQESTKQ 1017
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136592 420 AEQLHVQLADKDlYVAEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQ 475
Cdd:COG5022 1018 LKELPVEVAELQ-SASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLR 1072
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
119-418 |
3.85e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 119 KMNRYDKKIDSLMNAVGCLKSEVKMQKGERqmAKRFLEERKEELEEVAHEL--AETEHENTVLRHNIERIKEEKDFTMLQ 196
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEE--AKKADEAKKAEEAKKADEAkkAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 197 KKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTDintlTRQKELLLQKLSTFEETNRTLRDLLRE 276
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE----AKIKAEELKKAEEEKKKVEQLKKKEAE 1644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 277 QHCKEDSERLMEQQGTL----LKRLAEADSEKARLLLLLQDKDKEVEELLQEiqcEKAQAKTASELSKSMESMRGHLQaQ 352
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIkaaeEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK---EAEEAKKAEELKKKEAEEKKKAE-E 1720
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136592 353 LRCKEAENSrlcMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEE 418
Cdd:PTZ00121 1721 LKKAEEENK---IKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
175-627 |
5.15e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 40.59 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 175 ENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAE---MDGAAAAKQVMALKDTIgkLKTEKQMTcTDINTLTR 251
Cdd:PTZ00440 729 KYNDLKSSIEEYKEEEEKLEVYKHQIINRKNEFILHLYENDkdlPDGKNTYEEFLQYKDTI--LNKENKIS-NDINILKE 805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 252 QKELLLQKLSTFEETNRTLRDLLREQHckEDSERLMEQQGTLLKRLAEADSEKarlllLLQDKDKEVEELLQEIQCEKAQ 331
Cdd:PTZ00440 806 NKKNNQDLLNSYNILIQKLEAHTEKND--EELKQLLQKFPTEDENLNLKELEK-----EFNENNQIVDNIIKDIENMNKN 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 332 AKTASELSKSMESMRGHLQAqlrckeaensrlcmqIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKE 411
Cdd:PTZ00440 879 INIIKTLNIAINRSNSNKQL---------------VEHLLNNKIDLKNKLEQHMKIINTDNIIQKNEKLNLLNNLNKEKE 943
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 412 RAEK--SEEYAEQLHVQLADKDLYVAEALSTLESW-RSRYNQVVKDKGD----------LELEIIVLNDRVTDLVNQQQs 478
Cdd:PTZ00440 944 KIEKqlSDTKINNLKMQIEKTLEYYDKSKENINGNdGTHLEKLDKEKDEwehfkseidkLNVNYNILNKKIDDLIKKQH- 1022
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 479 leEKMREDRDSLVERLHRQTAEYSAFKLEN-ERLKASFAPME-------DKLNQAHLEVQQLKASVKNYEGMIDNYKSQV 550
Cdd:PTZ00440 1023 --DDIIELIDKLIKEKGKEIEEKVDQYISLlEKMKTKLSSFHfnidikkYKNPKIKEEIKLLEEKVEALLKKIDENKNKL 1100
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907136592 551 MKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDIL-KITEAKLAECQdqlqgYERKNIDL 627
Cdd:PTZ00440 1101 IEIKNKSHEHVVNADKEKNKQTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDiTLNEVNEIEIE-----YERILIDH 1173
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
276-778 |
6.56e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.09 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 276 EQHCKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASE----LSKSMESMRGHLQA 351
Cdd:pfam05483 228 EEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEkkdhLTKELEDIKMSLQR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 352 QLRCKEAENSRLCMQIKNLersgNQHKAEVEAIMEQLKELK-------QKGDRDKETLKKAIRAQKERAEKSEEYAEQLH 424
Cdd:pfam05483 308 SMSTQKALEEDLQIATKTI----CQLTEEKEAQMEELNKAKaahsfvvTEFEATTCSLEELLRTEQQRLEKNEDQLKIIT 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 425 VQLADKDLYVAE----------ALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDSLV--- 491
Cdd:pfam05483 384 MELQKKSSELEEmtkfknnkevELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTaik 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 492 --ERLHRQTAEYSAFKLENERLKASfaPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDK 569
Cdd:pfam05483 464 tsEEHYLKEVEDLKTELEKEKLKNI--ELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 570 ENKMLKDEMnkeiEAARRQFQSQLADLQQLpdiLKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAR 649
Cdd:pfam05483 542 KEMNLRDEL----ESVREEFIQKGDEVKCK---LDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELH 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 650 EKHQASQK----ENKQLSQ---KVDELERKLEATSaqnveflqviAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDA 722
Cdd:pfam05483 615 QENKALKKkgsaENKQLNAyeiKVNKLELELASAK----------QKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIA 684
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136592 723 RRQVEQTKEqalsKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQD 778
Cdd:pfam05483 685 DEAVKLQKE----IDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQE 736
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
125-540 |
7.89e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.10 E-value: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 125 KKIDSLMNAvgcLKSEVKMQKgERQMAKrfLEERKEELEEVAHELAETEHENTVLRHNIERIKEEKdftmLQKKHLQQEK 204
Cdd:pfam15921 429 QRLEALLKA---MKSECQGQM-ERQMAA--IQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKK----MTLESSERTV 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 205 ECLMSKLVEAEMDGAAAAKQVMALKDTIG-KLKTEKQMTCTDINTLTRQKELLLQKLSTFEETNrtLRDLLREQhcKEDS 283
Cdd:pfam15921 499 SDLTASLQEKERAIEATNAEITKLRSRVDlKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDK--VIEILRQQ--IENM 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 284 ERLMEQQGtllkRLAEA-DSEKARLLLLLQDKDKEVEELlqEIQCEKAQAKTaselsKSMESMRGHLQ-AQLRCKEAENS 361
Cdd:pfam15921 575 TQLVGQHG----RTAGAmQVEKAQLEKEINDRRLELQEF--KILKDKKDAKI-----RELEARVSDLElEKVKLVNAGSE 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 362 RLcMQIKNLERSGNQHKAEVEAIMEQLKELKQkgdrDKETLKKAIRaqkERAEKSEEYAEQLHVQLADKDLYVAEALSTL 441
Cdd:pfam15921 644 RL-RAVKDIKQERDQLLNEVKTSRNELNSLSE----DYEVLKRNFR---NKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 442 ESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKM----------REDRDSLVERL-------HRQTAEYSAF 504
Cdd:pfam15921 716 KSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMtnankekhflKEEKNKLSQELstvatekNKMAGELEVL 795
|
410 420 430
....*....|....*....|....*....|....*.
gi 1907136592 505 KLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYE 540
Cdd:pfam15921 796 RSQERRLKEKVANMEVALDKASLQFAECQDIIQRQE 831
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
456-805 |
8.30e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 456 GDLELEIIVLNDR-------VTDLVNQQQSLEEKMREDRD--SLVERLhrqtaEYSAFKLENERLKASFAPMEDKLNQAh 526
Cdd:PRK04863 833 ADPEAELRQLNRRrveleraLADHESQEQQQRSQLEQAKEglSALNRL-----LPRLNLLADETLADRVEEIREQLDEA- 906
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 527 levQQLKASVKNYEGMIDNYKSQVMKTR--------LEAD--EVAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADL 596
Cdd:PRK04863 907 ---EEAKRFVQQHGNALAQLEPIVSVLQsdpeqfeqLKQDyqQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMLAKN 983
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 597 QQLPDIL----KITEAKLAECQDQLQGYERKNIDLTAIISDLRSRI-----EHQGDKLEMAREKHQASQKENKQLSQKVD 667
Cdd:PRK04863 984 SDLNEKLrqrlEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYdakrqMLQELKQELQDLGVPADSGAEERARARRD 1063
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 668 ELERKLEATSAqnveflqviakREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKilDL 747
Cdd:PRK04863 1064 ELHARLSANRS-----------RRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDN--GV 1130
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907136592 748 ETQLSR------TKTELGQLRRTRDDADRRYQSRLQDLKDRLEQSEsTNRSMQNYVQFLKASYA 805
Cdd:PRK04863 1131 ERRLHRrelaylSADELRSMSDKALGALRLAVADNEHLRDVLRLSE-DPKRPERKVQFYIAVYQ 1193
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
184-426 |
9.17e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 39.72 E-value: 9.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 184 ERIKEEKdFTMLQKKHLQQEKECLMS------KLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKEL-- 255
Cdd:pfam17380 286 ERQQQEK-FEKMEQERLRQEKEEKAReverrrKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELer 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 256 -LLQKLSTFEETNRTLRDLLREQHCKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKT 334
Cdd:pfam17380 365 iRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136592 335 ASELS--KSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQ-LKELKQKG----------DRDKET 401
Cdd:pfam17380 445 AREMErvRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKeLEERKQAMieeerkrkllEKEMEE 524
|
250 260
....*....|....*....|....*
gi 1907136592 402 LKKAIRAQKERAEKSEEYAEQLHVQ 426
Cdd:pfam17380 525 RQKAIYEEERRREAEEERRKQQEME 549
|
|
| |
