|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
114-778 |
3.11e-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: 87.03 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 114 KMNRYDKKIDSLMNAVGCLKSEVKMQKGERQMAKRFLEERKEELEEVAHELAETEHENTVLRHNIERIKEEKDFTMLQKK 193
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 194 HLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETNRTLRDLLREQH 273
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 274 CKEDSERLmeqqGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQ-AQLRCKE 352
Cdd:TIGR02168 435 LKELQAEL----EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgFSEGVKA 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 353 AENSRLCM-----QIKNLERSGNQHKAEVEA---------IMEQLKELKQKGDRDKETLK--------KAIRAQKERAEK 410
Cdd:TIGR02168 511 LLKNQSGLsgilgVLSELISVDEGYEAAIEAalggrlqavVVENLNAAKKAIAFLKQNELgrvtflplDSIKGTEIQGND 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 411 SEEYAEQLHVQLADKDL--YVAEALSTLESWRSRYnqVVKDKGDLELEIIVLNDR----VT---DLVNQQQSLEEKMRED 481
Cdd:TIGR02168 591 REILKNIEGFLGVAKDLvkFDPKLRKALSYLLGGV--LVVDDLDNALELAKKLRPgyriVTldgDLVRPGGVITGGSAKT 668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 482 RDSLVERlhrqtaeysafKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDnyksqvmktrlEADEVAAQLER 561
Cdd:TIGR02168 669 NSSILER-----------RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE-----------QLRKELEELSR 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 562 CDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLE 641
Cdd:TIGR02168 727 QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 642 MAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAiEDARRQV 721
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL-LNERASL 885
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 722 EQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQS---RLQDLKDRL 778
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGlevRIDNLQERL 945
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
222-780 |
8.30e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 8.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 222 ALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETNRTLRDLLREQhcKEDSERLMEQQGTLLKRLAEADSEKAR 301
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL--LAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 302 LllllqdkDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIME 381
Cdd:COG1196 321 L-------EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 382 QLKELKQKgdrdKETLKKAIRAQKERAEKSEEYAEQLHVQLadkdlyvAEALSTLESWRSRYNQVVKDKGDLELEIIVLN 461
Cdd:COG1196 394 AAAELAAQ----LEELEEAEEALLERLERLEEELEELEEAL-------AELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 462 DRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAP-MEDKLNQAHLEVQQLKASVKNYEGMIDN 540
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAlLLAGLRGLAGAVAVLIGVEAAYEAALEA 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 541 YKSQVMKTRL-EADEVAAQLERCDKENKMLKDE---MNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYE 616
Cdd:COG1196 543 ALAAALQNIVvEDDEVAAAAIEYLKAAKAGRATflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 617 RKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRL 696
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 697 EEktrecgslARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKD 776
Cdd:COG1196 703 EE--------EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
....
gi 1907136608 777 RLEQ 780
Cdd:COG1196 775 EIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
364-737 |
2.37e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 364 NLERsgnqhkaeVEAIMEQLkelkqkgDRDKETLKKairaQKERAEKSEEYAEQLhvQLADKDLYVAealstleswrsRY 443
Cdd:COG1196 187 NLER--------LEDILGEL-------ERQLEPLER----QAEKAERYRELKEEL--KELEAELLLL-----------KL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 444 NQVVKDKGDLELEIIVLNDRVTDLVNQQQSLE---EKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQA 520
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEaelEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 521 HLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLErcdkenkmlkdemnkEIEAARRQFQSQLADLqqlpdilki 600
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELE---------------EAEAELAEAEEALLEA--------- 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 601 tEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQ 680
Cdd:COG1196 371 -EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907136608 681 VIAKREEAIHQAQLRLEEKTREcgslARQLESAIEDARRQVEQTKEQALSKERAAQS 737
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEE----AALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
460-783 |
1.31e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 460 LNDRVTDLVNQQQSLEEKMR--EDRDSLVERLHRQTAEYSAFKLEneRLKASFAPMEDKLNQAHLEVQQLKASVKNYEGM 537
Cdd:COG1196 191 LEDILGELERQLEPLERQAEkaERYRELKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 538 IDNYKSQVMKTRLEADEVAAQLERCDKEnkmlKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYER 617
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAE----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 618 KNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQnvefLQVIAKREEAIHQAQLRLE 697
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ----LEELEEAEEALLERLERLE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 698 EKTRECGSLARQLESAIEDARRQVEQTKE---QALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDL 774
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEeeaELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
....*....
gi 1907136608 775 KDRLEQSES 783
Cdd:COG1196 501 ADYEGFLEG 509
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
247-802 |
2.52e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 247 QKELLLQKLSTFEETNRTLRDLLREQhcKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQcekaq 326
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEA--EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS----- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 327 aktaselskSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKE 406
Cdd:TIGR02168 299 ---------RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 407 RAEKSEEYAEQLHvQLADKdlyVAEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLE-EKMREDRDSL 485
Cdd:TIGR02168 370 LESRLEELEEQLE-TLRSK---VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEEL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 486 VERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKS------QVMKTRLEAD------ 553
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegvkALLKNQSGLSgilgvl 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 554 ----EVAAQLERC---------------DKENKMLKDEMNKEIEAARRQF------------QSQLADLQQLPDILKITe 602
Cdd:TIGR02168 526 seliSVDEGYEAAieaalggrlqavvveNLNAAKKAIAFLKQNELGRVTFlpldsikgteiqGNDREILKNIEGFLGVA- 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 603 AKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQ-------------GDKL----------EMAREKHQASQKENKQLSQ 659
Cdd:TIGR02168 605 KDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAkklrpgyrivtldGDLVrpggvitggsAKTNSSILERRREIEELEE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 660 KVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESA------IEDARRQVEQTKEQALSKER 733
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeveqLEERIAQLSKELTELEAEIE 764
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907136608 734 AAQSKILDLETQLSRTKTELGQLrrtrddadrryQSRLQDLKDRLEQSESTNRSMQNYVQFLKASYANV 802
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEEL-----------EAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
247-698 |
7.65e-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: 65.91 E-value: 7.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 247 QKELLLQKLSTFEETNRTLRDLLRE-QHCKEDSERLMEQQGTLLK-RLAEADSEKARLLLLLQDKDKEVEELL------- 317
Cdd:pfam15921 311 QNSMYMRQLSDLESTVSQLRSELREaKRMYEDKIEELEKQLVLANsELTEARTERDQFSQESGNLDDQLQKLLadlhkre 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 318 QEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERS-GNQHKAEVEAI------MEQLKELKQKG 390
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIqgknesLEKVSSLTAQL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 391 DRDKETLKKAIR---AQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYN------QVVKDKGD------LEL 455
Cdd:pfam15921 471 ESTKEMLRKVVEeltAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDlklqelQHLKNEGDhlrnvqTEC 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 456 EIIVLN---------------DRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQA 520
Cdd:pfam15921 551 EALKLQmaekdkvieilrqqiENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 521 HLEVQQLK-------ASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQQ 593
Cdd:pfam15921 631 ELEKVKLVnagserlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 594 LPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKV-------DELER 666
Cdd:pfam15921 711 TRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELstvatekNKMAG 790
|
490 500 510
....*....|....*....|....*....|..
gi 1907136608 667 KLEATSAQNVEFLQVIAKREEAIHQAQLRLEE 698
Cdd:pfam15921 791 ELEVLRSQERRLKEKVANMEVALDKASLQFAE 822
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
353-716 |
1.49e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 353 AENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEA 432
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 433 LSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMredrDSLVERLHRQTAEYSAFKLENERLKASFAP 512
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL----DELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 513 MEDKLNQAHLEVQQLKASVKNYEGMIDNYksqvmktRLEADEVAAQLERCDKEnkmlKDEMNKEIEAARRQFQSQLADLQ 592
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEEL-------EELIEELESELEALLNE----RASLEEALALLRSELEELSEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 593 QLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRI-EHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEAT 671
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1907136608 672 SAQNVEFLQVIAKREEaihqaqlRLEEKTRECGSLAR---QLESAIED 716
Cdd:TIGR02168 985 GPVNLAAIEEYEELKE-------RYDFLTAQKEDLTEakeTLEEAIEE 1025
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
548-786 |
5.49e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 548 TRLEA--DEVAAQLERCDKE------NKMLKDEMN-KEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERK 618
Cdd:COG1196 189 ERLEDilGELERQLEPLERQaekaerYRELKEELKeLEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 619 NIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEE 698
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 699 KTRECGSLARQLESAiEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRL 778
Cdd:COG1196 349 AEEELEEAEAELAEA-EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
....*...
gi 1907136608 779 EQSESTNR 786
Cdd:COG1196 428 EALAELEE 435
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
193-533 |
9.46e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 9.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 193 KHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQmtctdinTLTRQKELLLQKLSTFEETNRTLRDLLREQ 272
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-------ELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 273 HckEDSERLMEQQGTLLKRLAEADSEKArlllllqdkdkeveELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKE 352
Cdd:TIGR02168 753 S--KELTELEAEIEELEERLEEAEEELA--------------EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 353 AENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQkgdrDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEA 432
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSE----DIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 433 LSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKmredRDSLVERLhrqTAEYSafkLENERLKASFAP 512
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR----IDNLQERL---SEEYS---LTLEEAEALENK 962
|
330 340
....*....|....*....|.
gi 1907136608 513 MEDKLNQAHLEVQQLKASVKN 533
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
168-805 |
1.04e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.39 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 168 EHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTC-TDINTLTR 246
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVkEKIGELEA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 247 QKELLLQKLstfEETNRTLRDLL-REQHCKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKA 325
Cdd:TIGR02169 302 EIASLERSI---AEKERELEDAEeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 326 QAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELkqkgDRDKETLKKAIRAQK 405
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL----EEEKEDKALEIKKQE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 406 ERAEKSEEYAEQLHVQLADKdlyvaealstleswRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQ---SLEEKMREDR 482
Cdd:TIGR02169 455 WKLEQLAADLSKYEQELYDL--------------KEEYDRVEKELSKLQRELAEAEAQARASEERVRggrAVEEVLKASI 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 483 DS---LVERLHRQTAEYsAFKLE---NERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEV- 555
Cdd:TIGR02169 521 QGvhgTVAQLGSVGERY-ATAIEvaaGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVi 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 556 --AAQLERCDKENK-----MLKDEMNKE-IEAARRQF---------------------------------QSQLADLQQL 594
Cdd:TIGR02169 600 gfAVDLVEFDPKYEpafkyVFGDTLVVEdIEAARRLMgkyrmvtlegelfeksgamtggsraprggilfsRSEPAELQRL 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 595 PDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQ 674
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 675 NVEFLQVIAKREEAIHQAQLRLEE-KTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLEtQLSRTKTEL 753
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE-YLEKEIQEL 838
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1907136608 754 GQLRRTRDDADRRYQSRLQDLKDRLEQSESTNRSMQNYVQFLKASYANVFGD 805
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
281-780 |
2.76e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 61.01 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 281 LMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTA-----SELSKSMESMRGHLQAQLRCKEAEN 355
Cdd:pfam12128 267 YKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAvakdrSELEALEDQHGAFLDADIETAAADQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 356 SRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADkdlyvaeALST 435
Cdd:pfam12128 347 EQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAED-------DLQA 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 436 LES-WRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKM--REDRDSLVER----LHRQTAEYSAFKLENERLKA 508
Cdd:pfam12128 420 LESeLREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLlqLENFDERIERareeQEAANAEVERLQSELRQARK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 509 SFAPMEDKLNQAHLEVQQLKASVKNYEGMID----------NYKSQVMKTRLEADEVAAQLERCDkenkmLKDEMNKEIE 578
Cdd:pfam12128 500 RRDQASEALRQASRRLEERQSALDELELQLFpqagtllhflRKEAPDWEQSIGKVISPELLHRTD-----LDPEVWDGSV 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 579 AARRQFQSQLADLQQL--PDILKITEAklaecqdqlqgyerknidltaiisdLRSRIEHQGDKLEMAREKHQASQKENKQ 656
Cdd:pfam12128 575 GGELNLYGVKLDLKRIdvPEWAASEEE-------------------------LRERLDKAEEALQSAREKQAAAEEQLVQ 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 657 LSQKVDELERKLEatsaqnveflqvIAKReeAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQAlskerAAQ 736
Cdd:pfam12128 630 ANGELEKASREET------------FART--ALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSL-----EAQ 690
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1907136608 737 SKILDLETQLSRTKTElGQLRRTRDDADRRYQSRLQDLKDRLEQ 780
Cdd:pfam12128 691 LKQLDKKHQAWLEEQK-EQKREARTEKQAYWQVVEGALDAQLAL 733
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
203-720 |
4.23e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 203 MSKLVEAEMDGAAAAKQVMALKDTIGKlktekqmtCTDINTLTRQKELLLQKLSTFE-ETNRTLRDLLREQ--HCKEDSE 279
Cdd:COG4913 234 FDDLERAHEALEDAREQIELLEPIREL--------AERYAAARERLAELEYLRAALRlWFAQRRLELLEAEleELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 280 RLMEQQGTLLKRLAEADSEKAR-LLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRL 358
Cdd:COG4913 306 RLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 359 CMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQL------HVQLADKDL-YVAE 431
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALrdalaeALGLDEAELpFVGE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 432 AL---STLESWRS------------------RYNQVVK--DKGDLELEIivlndrVTDLVNQQQSLEEKMREDRDSLVER 488
Cdd:COG4913 466 LIevrPEEERWRGaiervlggfaltllvppeHYAAALRwvNRLHLRGRL------VYERVRTGLPDPERPRLDPDSLAGK 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 489 LHRQTAEYSAFkLENErLKASFAPM----EDKLNQAHLEVQQlkasvknyEGMI-DNYKSQVMKTRLEADEV-------A 556
Cdd:COG4913 540 LDFKPHPFRAW-LEAE-LGRRFDYVcvdsPEELRRHPRAITR--------AGQVkGNGTRHEKDDRRRIRSRyvlgfdnR 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 557 AQLERCDKENKMLKDEMN------KEIEAARRQFQSQLADLQQLPDI------LKITEAKLAECQDQLQGYERKNIDLTA 624
Cdd:COG4913 610 AKLAALEAELAELEEELAeaeerlEALEAELDALQERREALQRLAEYswdeidVASAEREIAELEAELERLDASSDDLAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 625 I---ISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATS--AQNVEFLQVIAKREEAI---HQAQLR- 695
Cdd:COG4913 690 LeeqLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEdlARLELRALLEERFAAALgdaVERELRe 769
|
570 580
....*....|....*....|....*.
gi 1907136608 696 -LEEKTRECGSLARQLESAIEDARRQ 720
Cdd:COG4913 770 nLEERIDALRARLNRAEEELERAMRA 795
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
163-669 |
6.15e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 59.65 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 163 ELAETEHENTVLRHNIERIKEE---KDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCT 239
Cdd:TIGR04523 174 ELNLLEKEKLNIQKNIDKIKNKllkLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQT 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 240 DINTLTRQ----KELLLQKLSTFEETNRTLRDLlreqhckedserlMEQQGTLLKRLAEADSEKArlllllQDKDKEVEE 315
Cdd:TIGR04523 254 QLNQLKDEqnkiKKQLSEKQKELEQNNKKIKEL-------------EKQLNQLKSEISDLNNQKE------QDWNKELKS 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 316 LLQEIQCEKAQAKTasELSKSMESMrghlqaqlrckeaenSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKgdrdKE 395
Cdd:TIGR04523 315 ELKNQEKKLEEIQN--QISQNNKII---------------SQLNEQISQLKKELTNSESENSEKQRELEEKQNE----IE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 396 TLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLE 475
Cdd:TIGR04523 374 KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 476 ---EKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEA 552
Cdd:TIGR04523 454 liiKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEK 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 553 DEVAAQLErcDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKnidltaiISDLRSR 632
Cdd:TIGR04523 534 KEKESKIS--DLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE-------KKDLIKE 604
|
490 500 510
....*....|....*....|....*....|....*..
gi 1907136608 633 IEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLE 669
Cdd:TIGR04523 605 IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKN 641
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
462-797 |
8.71e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 8.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 462 DRVTDLVN----QQQSLEEKMRedrdsLVERLHRQTAEYSAfkLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGM 537
Cdd:TIGR02168 189 DRLEDILNelerQLKSLERQAE-----KAERYKELKAELRE--LELALLVLRLEELREELEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 538 IDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNkEIEAARRQFQSQLADLQQlpdilkiteaKLAECQDQLQGYER 617
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEIS-RLEQQKQILRERLANLER----------QLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 618 KNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEAtsaqnveflqviAKREEAIHQAQLRLE 697
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET------------LRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 698 EKTREcgslarQLESAIEDARRQVEQTKEQALSKERAAQS-KILDLETQLSRTKTELGQLRRTRDDAdrryQSRLQDLKD 776
Cdd:TIGR02168 399 NNEIE------RLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERL----EEALEELRE 468
|
330 340
....*....|....*....|.
gi 1907136608 777 RLEQSESTNRSMQNYVQFLKA 797
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQA 489
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
216-802 |
1.23e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 216 AAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETnrtlrdLLREQHCKEDSERLMEQQGTLLKRLAEA 295
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEV------LEEHEERREELETLEAEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 296 DSEKARLLLLLQDKDKEVEELLQEIQ-------CEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERS 368
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDdllaeagLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 369 GNQHKAEVEAIMEQLKELkqkgDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVK 448
Cdd:PRK02224 351 ADDLEERAEELREEAAEL----ESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 449 DKGDLELEIIVLNDRVTDlvNQQ-----------QSLEEKMR----EDRDSLVERLhrqTAEYSAFKLENERLKASFAPM 513
Cdd:PRK02224 427 REAELEATLRTARERVEE--AEAlleagkcpecgQPVEGSPHvetiEEDRERVEEL---EAELEDLEEEVEEVEERLERA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 514 EDkLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQlercdkenkmlKDEMNKEIEAARRQFQSQLADLQQ 593
Cdd:PRK02224 502 ED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER-----------AAELEAEAEEKREAAAEAEEEAEE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 594 LPDILKITEAKLAECQDQLQGYERknidltaiISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDEL-ERKLEATS 672
Cdd:PRK02224 570 AREEVAELNSKLAELKERIESLER--------IRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKrERKRELEA 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 673 AQNveflqviakrEEAIHQAQLRLEektrecgslarQLESAIEDARRQVEQTKEqalsKERAAQSKILDLETQLSRtkte 752
Cdd:PRK02224 642 EFD----------EARIEEAREDKE-----------RAEEYLEQVEEKLDELRE----ERDDLQAEIGAVENELEE---- 692
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1907136608 753 lgqlrrtrddadrryqsrLQDLKDRLEQSESTnrsmqnyVQFLKASYANV 802
Cdd:PRK02224 693 ------------------LEELRERREALENR-------VEALEALYDEA 717
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
309-646 |
1.87e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 309 KDKEVEELLQEI--------QCEKAQAKTASELSkSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIM 380
Cdd:TIGR02168 675 RRREIEELEEKIeeleekiaELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 381 EQLKELKQKgdrdketlkkaIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIVL 460
Cdd:TIGR02168 754 KELTELEAE-----------IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 461 NDRVTDLVNQQQSLEEKMREdrdsLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDN 540
Cdd:TIGR02168 823 RERLESLERRIAATERRLED----LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 541 YKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKeIEAARRQFQSQLADLQQ--LPDILK---ITEAKLAECQDQLQGY 615
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSltLEEAEAlenKIEDDEEEARRRLKRL 977
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1907136608 616 ERK-----NIDLTAI--ISDLRSR---IEHQGDKLEMAREK 646
Cdd:TIGR02168 978 ENKikelgPVNLAAIeeYEELKERydfLTAQKEDLTEAKET 1018
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
281-793 |
2.59e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 57.75 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 281 LMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLR-CKEAENSRLC 359
Cdd:TIGR00606 417 LQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAEReLSKAEKNSLT 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 360 MQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEE-------YAEQLHVQLADKDlYVAEA 432
Cdd:TIGR00606 497 ETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQirkiksrHSDELTSLLGYFP-NKKQL 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 433 LSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMR------------EDRDSLVERLHRQ-------- 492
Cdd:TIGR00606 576 EDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSsyedklfdvcgsQDEESDLERLKEEieksskqr 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 493 ------TAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKN----YEGMIDNYKSQVMKTRLEADEVAAQLERC 562
Cdd:TIGR00606 656 amlagaTAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSklrlAPDKLKSTESELKKKEKRRDEMLGLAPGR 735
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 563 DKEnkmlKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTaIISDLRSRIEHQGDKLEM 642
Cdd:TIGR00606 736 QSI----IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVT-IMERFQMELKDVERKIAQ 810
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 643 AREKHQAS--QKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQ 720
Cdd:TIGR00606 811 QAAKLQGSdlDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQL 890
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907136608 721 VEQTKE-QALSKE-RAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQSESTNRSMQNYVQ 793
Cdd:TIGR00606 891 VELSTEvQSLIREiKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ 965
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
492-733 |
5.48e-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: 55.93 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 492 QTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLercdKENKMLKD 571
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL----AELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 572 EMNKEIEAARRQFQSQLADLQQLPdilKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQ 651
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLG---RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 652 KENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSK 731
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
..
gi 1907136608 732 ER 733
Cdd:COG4942 251 LK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
288-732 |
6.63e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 6.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 288 LLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLE- 366
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 367 -RSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQ 445
Cdd:COG4717 131 yQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 446 VVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPM------------ 513
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlflvlgllallf 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 514 ------EDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVM-KTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQS 586
Cdd:COG4717 291 lllareKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 587 QLADLQQLPDIlkITEAKLAECQDQLQGYErkniDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENK--QLSQKVDEL 664
Cdd:COG4717 371 EIAALLAEAGV--EDEEELRAALEQAEEYQ----ELKEELEELEEQLEELLGELEELLEALDEEELEEEleELEEELEEL 444
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136608 665 ERKLEATSAQNVEFLQVI--AKREEAIHQAQLRLEEKTRECGSLARQ------LESAIEDARRQVEQTKEQALSKE 732
Cdd:COG4717 445 EEELEELREELAELEAELeqLEEDGELAELLQELEELKAELRELAEEwaalklALELLEEAREEYREERLPPVLER 520
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
555-787 |
1.19e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 555 VAAQLERCDKENKMLKdEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIE 634
Cdd:COG4942 15 AAAQADAAAEAEAELE-QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 635 HQGDKLEmAREKHQASQKENKQLSQKVDELERKLEATSAQNV--------EFLQVIAKREEAIHQAQLRLEEKTRECGSL 706
Cdd:COG4942 94 ELRAELE-AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAvrrlqylkYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 707 ARQLESAIEDARRQveqtkEQALSKERAAQSKIL-DLETQLSRTKTELGQLRRTrddadrryQSRLQDLKDRLEQSESTN 785
Cdd:COG4942 173 RAELEALLAELEEE-----RAALEALKAERQKLLaRLEKELAELAAELAELQQE--------AEELEALIARLEAEAAAA 239
|
..
gi 1907136608 786 RS 787
Cdd:COG4942 240 AE 241
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
460-779 |
2.18e-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: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 460 LNDRVTDLVNQQQSLEEKMRE---DRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEG 536
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRienRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 537 MIDNYKSQVMKTRLEADEVAAQLERC-DKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGY 615
Cdd:TIGR02169 759 ELKELEARIEELEEDLHKLEEALNDLeARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 616 ERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLR 695
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 696 LEEKTRECGSLARQLeSAIEDARRQVEQTKEQALSKERaAQSKILDLETQLSRtkteLGQLRRTRDDADRRYQSRLQDLK 775
Cdd:TIGR02169 919 LSELKAKLEALEEEL-SEIEDPKGEDEEIPEEELSLED-VQAELQRVEEEIRA----LEPVNMLAIQEYEEVLKRLDELK 992
|
....
gi 1907136608 776 DRLE 779
Cdd:TIGR02169 993 EKRA 996
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
364-778 |
2.26e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.96 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 364 NLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKA----IRAQkERAEKSEEYAEQLHVQLADkdlyVAEALSTLESW 439
Cdd:COG3096 337 NLVQTALRQQEKIERYQEDLEELTERLEEQEEVVEEAaeqlAEAE-ARLEAAEEEVDSLKSQLAD----YQQALDVQQTR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 440 RSRYNQVVKDKGDL-------ELEIIVLNDRVTDLVNQQQSLEEKMR--EDRDSLVERLHRQTAEysAFKLenerlkasf 510
Cdd:COG3096 412 AIQYQQAVQALEKAralcglpDLTPENAEDYLAAFRAKEQQATEEVLelEQKLSVADAARRQFEK--AYEL--------- 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 511 apmedklnqahleVQQLKASVknyegmidnyksqvmkTRLEADEVAAQLERCDKENKMLkdemnkeieAARR-QFQSQLA 589
Cdd:COG3096 481 -------------VCKIAGEV----------------ERSQAWQTARELLRRYRSQQAL---------AQRLqQLRAQLA 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 590 DLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELerkle 669
Cdd:COG3096 523 ELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKEL----- 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 670 atsaqnveflqviAKREEAIHQAQLRLEektrecgSLARQLESAIEDArRQVEQTKEQALSKERAAQSkildLETQLSRT 749
Cdd:COG3096 598 -------------AARAPAWLAAQDALE-------RLREQSGEALADS-QEVTAAMQQLLEREREATV----ERDELAAR 652
|
410 420
....*....|....*....|....*....
gi 1907136608 750 KTELGQLRRTRDDADRRYQSRLQDLKDRL 778
Cdd:COG3096 653 KQALESQIERLSQPGGAEDPRLLALAERL 681
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
371-670 |
3.96e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 371 QHKAEVEAIMEQLKELKQKGDRdKETLKKAIRAQKERAEKSEEYAEQLHVQLADK-DLYVAEALSTLESWRSRYNQVVKD 449
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIER-LDLIIDEKRQQLERLRREREKAERYQALLKEKrEYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 450 KGDLELEIIVLNDRVTDLVNQQQSLEEKMREdrdsLVERLHRQTA-EYSAFKLENERLKASFAPMEDKLNQAHLEVQQLK 528
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEE----LNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 529 ASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMN------------------------KEIEAARRQF 584
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEdlraeleevdkefaetrdelkdyrEKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 585 QSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMA--------------REKHQAS 650
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLaadlskyeqelydlKEEYDRV 481
|
330 340
....*....|....*....|
gi 1907136608 651 QKENKQLSQKVDELERKLEA 670
Cdd:TIGR02169 482 EKELSKLQRELAEAEAQARA 501
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
571-780 |
1.02e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 571 DEMNKEIEAARRQfQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTaiISDLRSRIEHQGDKLEMAREKHQAS 650
Cdd:COG4913 238 ERAHEALEDAREQ-IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR--LELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 651 QKENKQLSQKVDELERKLEATSAQNVEFLqviakrEEAIHQAQLRLEEKTRECGSLARQL----------ESAIEDARRQ 720
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQL------EREIERLERELEERERRRARLEALLaalglplpasAEEFAALRAE 388
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907136608 721 VEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRR---TRDDADRRYQSRLQDLKDRLEQ 780
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAeiaSLERRKSNIPARLLALRDALAE 451
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
117-722 |
1.35e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 117 RYDKKIDSLMNAVGCLKSEVKMQKGERQMAKRFLEERKEELEEVAHELAETEHEntvlrhnIERIKEEKDFTMLQKKHLQ 196
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE-------LARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 197 QEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMtctdintltrQKELLLQKLSTFEETNRTLRDLLREQhcke 276
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE----------AEAELAEAEEALLEAEAELAEAEEEL---- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 277 dsERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASElsksmesmrghLQAQLRCKEAENS 356
Cdd:COG1196 382 --EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE-----------EEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 357 RLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQ-LHVQLADKDLYVAEALST 435
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvKAALLLAGLRGLAGAVAV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 436 LESWRSRYNQVVkdkgdLELEIIVLNDRVTDLVNQQQSLEEKMREDRDSLVERlhrqtaeysafkLENERLKASFAPMED 515
Cdd:COG1196 529 LIGVEAAYEAAL-----EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATF------------LPLDKIRARAALAAA 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 516 KLNQAHLEVQQLKASVKNYEGMIDnykSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQQLP 595
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARY---YVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 596 DILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQN 675
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1907136608 676 VEFLQVIAKREEAIHQAQLRLEEktrecgsLARQLES-------AIEDARRQVE 722
Cdd:COG1196 749 EEEALEELPEPPDLEELERELER-------LEREIEAlgpvnllAIEEYEELEE 795
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
258-793 |
1.51e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 258 FEETNRTLRDLLREQHCKEDSERLMEQQGTLLK---RLAEADSEKA-----RLLLLLQDKDKEVEELLQEIQCEKAQAKT 329
Cdd:COG4913 234 FDDLERAHEALEDAREQIELLEPIRELAERYAAareRLAELEYLRAalrlwFAQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 330 ASELSKSMESMRGHLQAQLRCKEAEN-SRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERA 408
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 409 EKSEEYAEQLHVQLADkdlyvaealstlesWRSRYNQVVKDKGDLELEIIVLNDRVT----DLVNQQQSLEEKMREDRDS 484
Cdd:COG4913 394 EALEEELEALEEALAE--------------AEAALRDLRRELRELEAEIASLERRKSnipaRLLALRDALAEALGLDEAE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 485 L-------------------VER-LHRQtaeysAFKL--ENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYK 542
Cdd:COG4913 460 LpfvgelievrpeeerwrgaIERvLGGF-----ALTLlvPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 543 SQVMKTRLEADEVAA-------------------QLERCDK---ENKMLKD-----EMNKEIEAARRQF-----QSQLAD 590
Cdd:COG4913 535 SLAGKLDFKPHPFRAwleaelgrrfdyvcvdspeELRRHPRaitRAGQVKGngtrhEKDDRRRIRSRYVlgfdnRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 591 LqqlpdilkitEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGdklemAREKHQASQKENKQLSQKVDELERKLEA 670
Cdd:COG4913 615 L----------EAELAELEEELAEAEERLEALEAELDALQERREALQ-----RLAEYSWDEIDVASAEREIAELEAELER 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 671 TSAQNVEfLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQAlskERAAQSKILDLETQLSRTK 750
Cdd:COG4913 680 LDASSDD-LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL---EAAEDLARLELRALLEERF 755
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1907136608 751 TELGQlRRTRDDADRRYQSRLQDLKDRLEQSEST-NRSMQNYVQ 793
Cdd:COG4913 756 AAALG-DAVERELRENLEERIDALRARLNRAEEElERAMRAFNR 798
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
309-632 |
2.20e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 309 KDKEVEELLQEIQCEKAQAKtASELSKSMESMRghlqAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKEL-- 386
Cdd:TIGR02169 205 REREKAERYQALLKEKREYE-GYELLKEKEALE----RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnk 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 387 --KQKGDRDKETLKKAIR---AQKERAEKS----EEYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEI 457
Cdd:TIGR02169 280 kiKDLGEEEQLRVKEKIGeleAEIASLERSiaekERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 458 IVLNDRVTDLVNQQQSLEEKMREDRDSLVERlhrqTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGM 537
Cdd:TIGR02169 360 AELKEELEDLRAELEEVDKEFAETRDELKDY----REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 538 IdnyksqvmkTRLEADevaaqlercdkenkmlKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYER 617
Cdd:TIGR02169 436 I---------NELEEE----------------KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
330
....*....|....*
gi 1907136608 618 KNIDLTAIISDLRSR 632
Cdd:TIGR02169 491 ELAEAEAQARASEER 505
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
214-772 |
3.31e-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: 51.12 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 214 AAAAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTFEETNRTLRDLLREQhckEDSERLMEQQGTLLKRLA 293
Cdd:TIGR00618 296 AAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQE---IHIRDAHEVATSIREISC 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 294 EADSEKARLLLLLQDK--DKEVEELL-QEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQ---IKNLER 367
Cdd:TIGR00618 373 QQHTLTQHIHTLQQQKttLTQKLQSLcKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCaaaITCTAQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 368 SGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQ--------LHVQLADKDLYVAEALStlesw 439
Cdd:TIGR00618 453 CEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcplcgscIHPNPARQDIDNPGPLT----- 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 440 rSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDS---LVERLHRQTAEYSAFKLENERLKaSFAPMEDK 516
Cdd:TIGR00618 528 -RRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSfsiLTQCDNRSKEDIPNLQNITVRLQ-DLTEKLSE 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 517 L-------NQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAARRqfQSQLA 589
Cdd:TIGR00618 606 AedmlaceQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASR--QLALQ 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 590 DLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKE-NKQLSQKVDELERKL 668
Cdd:TIGR00618 684 KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKElMHQARTVLKARTEAH 763
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 669 EATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLArQLESAIEDARRQVEQTK----EQALSKERAAQSKILDLET 744
Cdd:TIGR00618 764 FNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLK-TLEAEIGQEIPSDEDILnlqcETLVQEEEQFLSRLEEKSA 842
|
570 580
....*....|....*....|....*...
gi 1907136608 745 QLSRTKTELGQLRRTRDDADRRYQSRLQ 772
Cdd:TIGR00618 843 TLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
179-789 |
3.62e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.89 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 179 ERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTDINTLTRQKELLLQKLSTF 258
Cdd:pfam15921 92 RRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 259 EETNRTLRdLLREQHCKEDSERLMEQQGTLLKRLAEADSekaRLLLLLQDKDKEVEELLQEIQCEkaqaktASELSKSME 338
Cdd:pfam15921 172 IEQLRKMM-LSHEGVLQEIRSILVDFEEASGKKIYEHDS---MSTMHFRSLGSAISKILRELDTE------ISYLKGRIF 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 339 SMRGHLQAqLRCKEAENSRLCMQIKN--LERSGNQHKAEVEAIMEQLKELKQKGDrdketlkkAIRAQKERAEKSEEYAE 416
Cdd:pfam15921 242 PVEDQLEA-LKSESQNKIELLLQQHQdrIEQLISEHEVEITGLTEKASSARSQAN--------SIQSQLEIIQEQARNQN 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 417 QLHV-QLADKDLYVAEALSTLESWRSRYNQVVKDkgdLELEIIVLNDRVTDLVNQQQSLEEK---MREDRDSLVERLHRQ 492
Cdd:pfam15921 313 SMYMrQLSDLESTVSQLRSELREAKRMYEDKIEE---LEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLHKR 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 493 TAEYSAFKLENERL-------KASFAPMEDKLNQAHLEVQQLKASVKnyegmidnyksqVMKTRLEAdEVAAQLERCDKE 565
Cdd:pfam15921 390 EKELSLEKEQNKRLwdrdtgnSITIDHLRRELDDRNMEVQRLEALLK------------AMKSECQG-QMERQMAAIQGK 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 566 NKMLK--DEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMA 643
Cdd:pfam15921 457 NESLEkvSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 644 R---EKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVI--------------AKREEAIHQAQLRLEE----KTRE 702
Cdd:pfam15921 537 KnegDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVgqhgrtagamqvekAQLEKEINDRRLELQEfkilKDKK 616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 703 CGSLaRQLESAIED-----------------ARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADR 765
Cdd:pfam15921 617 DAKI-RELEARVSDlelekvklvnagserlrAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTN 695
|
650 660
....*....|....*....|....
gi 1907136608 766 RYQSRLQDLKDRLEQSESTNRSMQ 789
Cdd:pfam15921 696 KLKMQLKSAQSELEQTRNTLKSME 719
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
168-723 |
5.46e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 168 EHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEmdgaaaaKQVMALK-DTIGKLKTEkqmtctdINTLTR 246
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELE-------AQIRGNGgDRLEQLERE-------IERLER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 247 QKELLLQKLSTFEETNRTL-------RDLLREQHckedsERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQE 319
Cdd:COG4913 353 ELEERERRRARLEALLAALglplpasAEEFAALR-----AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 320 IQcekAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLC--MQIKNLERS---------GNQ---------HKAEVEAI 379
Cdd:COG4913 428 IA---SLERRKSNIPARLLALRDALAEALGLDEAELPFVGelIEVRPEEERwrgaiervlGGFaltllvppeHYAAALRW 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 380 MEQLKeLKQK--GDRDKETLKKAIRAQKER---AEKSE----EYAEQLHVQLADKDLYV----AEALS------TLE--- 437
Cdd:COG4913 505 VNRLH-LRGRlvYERVRTGLPDPERPRLDPdslAGKLDfkphPFRAWLEAELGRRFDYVcvdsPEELRrhpraiTRAgqv 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 438 -SWRSRYnqvVKDKGDLELEIIVLN----DRVTDLVNQQQSLEEKMREdRDSLVERLHRQTAEYSAFKLENERLkASFAP 512
Cdd:COG4913 584 kGNGTRH---EKDDRRRIRSRYVLGfdnrAKLAALEAELAELEEELAE-AEERLEALEAELDALQERREALQRL-AEYSW 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 513 MEDKLNQAHLEVQQLKASVKNyegmIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEM---NKEIEAARRQFQSQLA 589
Cdd:COG4913 659 DEIDVASAEREIAELEAELER----LDASSDDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEELDELQD 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 590 DLQQLPDILKITEAKLAE------CQDQLQGYERKNidLTAIISDLRSRIEHQGDKLEMAREKHQASQKENkqlsqkVDE 663
Cdd:COG4913 735 RLEAAEDLARLELRALLEerfaaaLGDAVERELREN--LEERIDALRARLNRAEEELERAMRAFNREWPAE------TAD 806
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136608 664 LERKLEAtsaqNVEFLQVIAK-REEAIHQ-----AQLRLEEKTRECGSLARQLESAIEDARRQVEQ 723
Cdd:COG4913 807 LDADLES----LPEYLALLDRlEEDGLPEyeerfKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
538-801 |
7.12e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 538 IDNYKSQVMKTRLEADEVAAQLERCD-------KENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQD 610
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDliidekrQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 611 QLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQA-SQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAI 689
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 690 HQAQLRLEEKTREcgslARQLESAIEDARRQVEQTKE--QALSKERAA-QSKILDLETQLSRTKTELGQlrrtrddadrr 766
Cdd:TIGR02169 325 AKLEAEIDKLLAE----IEELEREIEEERKRRDKLTEeyAELKEELEDlRAELEEVDKEFAETRDELKD----------- 389
|
250 260 270
....*....|....*....|....*....|....*
gi 1907136608 767 YQSRLQDLKDRLEQSESTNRSMQNYVQFLKASYAN 801
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
508-737 |
8.76e-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: 8.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 508 ASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLK---DEMNKEIEAARRQF 584
Cdd:COG3883 9 PTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQaeiAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 585 QSQLADLQQLPDILKITEAKLAecQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDEL 664
Cdd:COG3883 89 GERARALYRSGGSVSYLDVLLG--SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907136608 665 ERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQS 737
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
289-699 |
1.57e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 289 LKRLAEADSEKARLLLLLQDKDKEVEEL---------LQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLC 359
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAkkkaeekkkADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 360 MQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDK--ETLKKAIRAQK-ERAEKSEEYAEQLHVQLADKDLYVAEALSTL 436
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkaDEAKKAEEAKKaDEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 437 ESWRSRYNQVVKDKGDLELEIIVLNDRVTDLvnqqQSLEEKMREDRDSLVERLHRQTAEySAFKLENERLKASfapmedk 516
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEA----KKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIKAE------- 1623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 517 lnqahlEVQQLKASVKNYEGMIDNYKSQVMKtrleadevAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQqlpd 596
Cdd:PTZ00121 1624 ------ELKKAEEEKKKVEQLKKKEAEEKKK--------AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE---- 1685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 597 ilkitEAKLAECQDQLQGYERKNIDltaiisDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNV 676
Cdd:PTZ00121 1686 -----DEKKAAEALKKEAEEAKKAE------ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754
|
410 420
....*....|....*....|...
gi 1907136608 677 EFLQVIAKREEAIHQAQLRLEEK 699
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEK 1777
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
568-753 |
1.65e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 568 MLKDEMNKEIEAARRQ-------FQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQgDKL 640
Cdd:COG4717 46 MLLERLEKEADELFKPqgrkpelNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 641 EMAREKHQASQKENKQLSQKVDELERkLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQ 720
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEE-LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190
....*....|....*....|....*....|...
gi 1907136608 721 VEQTKEQALSKERAAQSKILDLETQLSRTKTEL 753
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
632-787 |
2.14e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 632 RIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQnveflqvIAKREEAIHQAQLRLEEKTRECGSLARQLE 711
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE-------LEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136608 712 SAIEDaRRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQSESTNRS 787
Cdd:COG1196 306 RLEER-RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
441-672 |
2.36e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.70 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 441 SRYNQVVKDKgdleleIIVLNDRVTDLVNQQQSLEEKMREDRDsLVERLHRQTAEysafklENERLKASFAPMEDKLNQA 520
Cdd:PHA02562 166 SEMDKLNKDK------IRELNQQIQTLDMKIDHIQQQIKTYNK-NIEEQRKKNGE------NIARKQNKYDELVEEAKTI 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 521 HLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKD------------EMNKEIEAARrqfqSQL 588
Cdd:PHA02562 233 KAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqqisEGPDRITKIK----DKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 589 ADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLR---SRIEHQGDKLEMAREKHQASQKENK-QLSQKVDEL 664
Cdd:PHA02562 309 KELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKqslITLVDKAKKVKAAIEELQAEFVDNAeELAKLQDEL 388
|
....*...
gi 1907136608 665 ERKLEATS 672
Cdd:PHA02562 389 DKIVKTKS 396
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
381-753 |
3.26e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.74 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 381 EQLK-ELKQ----KGDRDKET---LKKAIRA---QKERAEKSEEY----------AEQLHVQLADKDLYVAEALSTLESw 439
Cdd:PRK10929 26 KQITqELEQakaaKTPAQAEIveaLQSALNWleeRKGSLERAKQYqqvidnfpklSAELRQQLNNERDEPRSVPPNMST- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 440 rsrynqvvkdkGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPmEDKLNQ 519
Cdd:PRK10929 105 -----------DALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTP-NTPLAQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 520 AHL-----EVQQLKASVKNYE--GMIDNYKSQVmkTRLEADEVAAQLERCDKENKMLKDEMNkeieaARRQFQSQLAdlq 592
Cdd:PRK10929 173 AQLtalqaESAALKALVDELElaQLSANNRQEL--ARLRSELAKKRSQQLDAYLQALRNQLN-----SQRQREAERA--- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 593 qlpdiLKITEaKLAECQDqlqgyerkniDLTAIISdlrsriehqgDKLEMAREkhqASQKENKQlSQKVDELERKLEATS 672
Cdd:PRK10929 243 -----LESTE-LLAEQSG----------DLPKSIV----------AQFKINRE---LSQALNQQ-AQRMDLIASQQRQAA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 673 AQNVEFLQVI-AKREEA-----------IHQAQL-RLEEKTRecgslARQLESAIEDAR----------------RQVEQ 723
Cdd:PRK10929 293 SQTLQVRQALnTLREQSqwlgvsnalgeALRAQVaRLPEMPK-----PQQLDTEMAQLRvqrlryedllnkqpqlRQIRQ 367
|
410 420 430
....*....|....*....|....*....|
gi 1907136608 724 TKEQALSkerAAQSKILDleTQLsRTKTEL 753
Cdd:PRK10929 368 ADGQPLT---AEQNRILD--AQL-RTQREL 391
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
344-733 |
3.73e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.32 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 344 LQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLH-VQL 422
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqLKS 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 423 ADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMRE---DRDSLVERLHRQTAEYSAF 499
Cdd:TIGR04523 296 EISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNsesENSEKQRELEEKQNEIEKL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 500 KLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDE---MNKE 576
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvKELI 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 577 IEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQ 656
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 657 LSQKVDELERKLEA-----TSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSK 731
Cdd:TIGR04523 536 KESKISDLEDELNKddfelKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSL 615
|
..
gi 1907136608 732 ER 733
Cdd:TIGR04523 616 EK 617
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
371-778 |
6.85e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 6.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 371 QHKAEVEAIMEQLKELKQKgdrdKETLKKAIRAQKERAEKSEEYAEQLHVQLADkdlyVAEALSTLESWRSRYNQVVK-- 448
Cdd:PRK04863 352 RYQADLEELEERLEEQNEV----VEEADEQQEENEARAEAAEEEVDELKSQLAD----YQQALDVQQTRAIQYQQAVQal 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 449 DK-----GDLELEIIVLNDRVTDLVNQQQSLEEKMR--EDRDSLVERLHRQTAEysAFKLenerlkasfapmedklnqah 521
Cdd:PRK04863 424 ERakqlcGLPDLTADNAEDWLEEFQAKEQEATEELLslEQKLSVAQAAHSQFEQ--AYQL-------------------- 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 522 leVQQLKASVknyegmidnyksqvmkTRLEADEVAAQLERCDKENKMLkdemnkeieAARR-QFQSQLADLQQLPDILKI 600
Cdd:PRK04863 482 --VRKIAGEV----------------SRSEAWDVARELLRRLREQRHL---------AEQLqQLRMRLSELEQRLRQQQR 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 601 TEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELErkleatsaqnveflq 680
Cdd:PRK04863 535 AERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLA--------------- 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 681 viaKREEAIHQAQLRLEEktrecgsLARQLESAIEDArRQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQLRRTR 760
Cdd:PRK04863 600 ---ARAPAWLAAQDALAR-------LREQSGEEFEDS-QDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPG 668
|
410
....*....|....*...
gi 1907136608 761 DDADrryqSRLQDLKDRL 778
Cdd:PRK04863 669 GSED----PRLNALAERF 682
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
552-751 |
8.41e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 552 ADEVAAQLERCDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRS 631
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 632 RIEHQGDKL--------------------------------EMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFL 679
Cdd:COG4942 98 ELEAQKEELaellralyrlgrqpplalllspedfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907136608 680 QVIAKREEAihQAQLRLEEKTREcgSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKT 751
Cdd:COG4942 178 ALLAELEEE--RAALEALKAERQ--KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
576-741 |
8.87e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 8.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 576 EIEAARRQFQSQLADLQQLpdiLKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMARekhqaSQKENK 655
Cdd:COG1579 21 RLEHRLKELPAELAELEDE---LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-----NNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 656 QLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQveqtkEQALSKERAA 735
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE-----LEELEAEREE 167
|
....*.
gi 1907136608 736 QSKILD 741
Cdd:COG1579 168 LAAKIP 173
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
502-756 |
1.37e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 45.06 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 502 ENERLKASFAPMEDKLNqahlEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENkmlkdemnkeiEAAR 581
Cdd:pfam19220 4 RNELLRVRLGEMADRLE----DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAY-----------GKLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 582 RQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKV 661
Cdd:pfam19220 69 RELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 662 DELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLAR---QLESAIEDARRQVEQTkEQALSKERAAQSK 738
Cdd:pfam19220 149 QAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRrlaELETQLDATRARLRAL-EGQLAAEQAERER 227
|
250
....*....|....*....
gi 1907136608 739 IL-DLETQLSRTKTELGQL 756
Cdd:pfam19220 228 AEaQLEEAVEAHRAERASL 246
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
574-795 |
1.62e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 574 NKEIEAARRQFQSQLADLQQlpdilkiteaKLAECQDQLQGYERKN--IDLTAIISDLRSRIEHQGDKLEMAREKHQASQ 651
Cdd:COG3206 170 REEARKALEFLEEQLPELRK----------ELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 652 kenkqlsQKVDELERKLEATSAQNVEFLQ--VIAKREEAIHQAQLRLEEKTRECG--------------SLARQLESAIE 715
Cdd:COG3206 240 -------ARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTpnhpdvialraqiaALRAQLQQEAQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 716 DARRQVEQTKEQALSKERAAQSKILDLETQ---LSRTKTELGQLRRTRDDADRRYQSrlqdLKDRLEQSESTNRSMQNYV 792
Cdd:COG3206 313 RILASLEAELEALQAREASLQAQLAQLEARlaeLPELEAELRRLEREVEVARELYES----LLQRLEEARLAEALTVGNV 388
|
...
gi 1907136608 793 QFL 795
Cdd:COG3206 389 RVI 391
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
90-752 |
1.74e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 90 SSEKLV-SVMRLSDLSTEDDDSGHCK--MNRYDKKIDSLMNAVGCLKSEVKMQKGERQMAKRFLEERKEELEEVAHELAE 166
Cdd:PRK03918 146 SREKVVrQILGLDDYENAYKNLGEVIkeIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 167 TEHENTVLRHNIERIKEEKdftmLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTekqmtctdintlTR 246
Cdd:PRK03918 226 LEKEVKELEELKEEIEELE----KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE------------LK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 247 QKELLLQKLSTF-EETNRTLRDLlreqhcKEDSERLMEQQGTLLKRLAEADSEKARLLLLLqdkdKEVEELLQEIQCEKA 325
Cdd:PRK03918 290 EKAEEYIKLSEFyEEYLDELREI------EKRLSRLEEEINGIEERIKELEEKEERLEELK----KKLKELEKRLEELEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 326 QAKTASELSKSMESMRGhLQAQLRCKEAEnsRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQK 405
Cdd:PRK03918 360 RHELYEEAKAKKEELER-LKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 406 E----RAEKSEEYAEQLhvqLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIVLND--RVTDLVNQQQSLEEKMR 479
Cdd:PRK03918 437 KcpvcGRELTEEHRKEL---LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 480 EDRdslVERLHRQTAEYSAFKLENERLKASFAPMEDKLNqahlEVQQLKASVKNYEGMIDNYKSqvmktrlEADEVAAQL 559
Cdd:PRK03918 514 KYN---LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE----KLEELKKKLAELEKKLDELEE-------ELAELLKEL 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 560 ERCDKENKMLKDEMNKEIEAARRQFQSqladLQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQG-- 637
Cdd:PRK03918 580 EELGFESVEELEERLKELEPFYNEYLE----LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEkk 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 638 ---DKLEMAREKHQASQKENKQLSQKVDELERKLEaTSAQNVEFLQviaKREEAIHQAQLRLEektrecgslarQLESAI 714
Cdd:PRK03918 656 yseEEYEELREEYLELSRELAGLRAELEELEKRRE-EIKKTLEKLK---EELEEREKAKKELE-----------KLEKAL 720
|
650 660 670
....*....|....*....|....*....|....*...
gi 1907136608 715 EDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTE 752
Cdd:PRK03918 721 ERVEELREKVKKYKALLKERALSKVGEIASEIFEELTE 758
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
161-411 |
2.01e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 161 AHELAETEHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTD 240
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 241 INTLTRQKELLLQKLSTFEETNRtLRDLLREQHCKEDSERLMeqqgtLLKRLAEADSEKARlllllqdkdkEVEELLQEI 320
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPP-LALLLSPEDFLDAVRRLQ-----YLKYLAPARREQAE----------ELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 321 QcekaqaktasELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKA 400
Cdd:COG4942 163 A----------ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
250
....*....|.
gi 1907136608 401 IRAQKERAEKS 411
Cdd:COG4942 233 EAEAAAAAERT 243
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
460-788 |
2.08e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.14 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 460 LNDRVTDLVNQQQSLEEKMREDRDSLVERLHRQTAE----YSAFKLENERLKASF-------APMEDKLNQAHLEVQQLK 528
Cdd:pfam00038 9 LNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpsrlYSLYEKEIEDLRRQLdtltverARLQLELDNLRLAAEDFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 529 ASVKNYEGMIDNYKSQVMKTRLEADEvaAQLERCDKENKMlkDEMNKEIEAARRQFQSQLADLQqlpdilkiteAKLAEC 608
Cdd:pfam00038 89 QKYEDELNLRTSAENDLVGLRKDLDE--ATLARVDLEAKI--ESLKEELAFLKKNHEEEVRELQ----------AQVSDT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 609 QDQLQGYERKNIDLTAIISDLRSRIEHQgdkleMAREKHQASQkenkQLSQKVDELERkleaTSAQNVEFLQviAKREEa 688
Cdd:pfam00038 155 QVNVEMDAARKLDLTSALAEIRAQYEEI-----AAKNREEAEE----WYQSKLEELQQ----AAARNGDALR--SAKEE- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 689 IHQAQLRLEEKTRECGSLARQLESaIEDARRQVEQTKEQALSKeraAQSKILDLETQLSRTKTELGQLrrtrddaDRRYQ 768
Cdd:pfam00038 219 ITELRRTIQSLEIELQSLKKQKAS-LERQLAETEERYELQLAD---YQELISELEAELQETRQEMARQ-------LREYQ 287
|
330 340
....*....|....*....|
gi 1907136608 769 SrLQDLKDRLEQSESTNRSM 788
Cdd:pfam00038 288 E-LLNVKLALDIEIATYRKL 306
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
276-738 |
2.99e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 276 EDSERLMEQQGTLLKRLAEaDSEKARLLLLLQDKdKEVEELLQEIQCEKAQAKTASELSKSMESMRGHlQAQLRCKEAEN 355
Cdd:PTZ00121 1143 EEARKAEDAKRVEIARKAE-DARKAEEARKAEDA-KKAEAARKAEEVRKAEELRKAEDARKAEAARKA-EEERKAEEARK 1219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 356 SRLCMQIKNLERSGNQHKAEVEAIMEQlKELKQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKdlyVAEALST 435
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEAKKDAEEAKKAE-EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE---KKKADEA 1295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 436 LESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRDSlvERLHRQTAEYSAFKLENERLKASFAPME- 514
Cdd:PTZ00121 1296 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA--AEAAKAEAEAAADEAEAAEEKAEAAEKKk 1373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 515 -------DKLNQAHLEVQQLKASVKNYEGmiDNYKSQVMKTRLEADEVAAQLERcDKENKMLKDEMNKEIEAARR--QFQ 585
Cdd:PTZ00121 1374 eeakkkaDAAKKKAEEKKKADEAKKKAEE--DKKKADELKKAAAAKKKADEAKK-KAEEKKKADEAKKKAEEAKKadEAK 1450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 586 SQLADLQQLPDILKITE--------AKLAECQDQLQGYERKNIDLTAIISDLRSRIE--HQGDKLEMAREKHQASQKENK 655
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEeakkadeaKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEakKKADEAKKAEEAKKADEAKKA 1530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 656 QLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAA 735
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
...
gi 1907136608 736 QSK 738
Cdd:PTZ00121 1611 EAK 1613
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
293-791 |
4.88e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 293 AEADSEKARLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKS-MESMRGHLQAQLRCKEAENSRLCMQIKNLERSgnQ 371
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAeAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA--K 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 372 HKAEVEAIMEQLKELKQKGDRDKETLKKAiRAQKERAEKSEEYAEQlhVQLADKDLYVAEALSTLESWRSRYNQVVKDKg 451
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKAEEDKKKADELKKA-AAAKKKADEAKKKAEE--KKKADEAKKKAEEAKKADEAKKKAEEAKKAE- 1460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 452 dlELEIIVLNDRVTDlvNQQQSLEEKMREDRDSLVERLHRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASV 531
Cdd:PTZ00121 1461 --EAKKKAEEAKKAD--EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 532 KNYEGMIDNYKSQVMKTRLE---ADEV----AAQLERCDKENKMLKDEMNKEIEAARRQfqsQLADLQQLPDILKITEAK 604
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEElkkAEEKkkaeEAKKAEEDKNMALRKAEEAKKAEEARIE---EVMKLYEEEKKMKAEEAK 1613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 605 LAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLE----ATSAQNVEFLQ 680
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEeakkAEEDEKKAAEA 1693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 681 VIAKREEAIHQAQLRleEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLE-----TQLSRTKTELGQ 755
Cdd:PTZ00121 1694 LKKEAEEAKKAEELK--KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEekkkiAHLKKEEEKKAE 1771
|
490 500 510
....*....|....*....|....*....|....*.
gi 1907136608 756 LRRTRDDADRRYQSRLQDLKDRLEQSESTNRSMQNY 791
Cdd:PTZ00121 1772 EIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNF 1807
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
585-784 |
6.76e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 585 QSQLAD-LQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDE 663
Cdd:pfam07888 33 QNRLEEcLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 664 LERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTREcgslarqLESAIEDARRQVEQTKEQAlSKERAAQSKILDLE 743
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETE-------LERMKERAKKAGAQRKEEE-AERKQLQAKLQQTE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907136608 744 TQLSRTKTELGQLRRTRDDADRRYQsRLQDLKDRLEQSEST 784
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVL-QLQDTITTLTQKLTT 224
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
471-797 |
8.14e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 471 QQSLEE----KMREDRDSLVERLHRQTAEysafKLENERLKAsfapmedklnqahLEVQQLKASVKNYEGMIDNYKSQVM 546
Cdd:TIGR02169 173 EKALEEleevEENIERLDLIIDEKRQQLE----RLRREREKA-------------ERYQALLKEKREYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 547 KTRLEAdeVAAQLERCDKENKMLK---DEMNKEIEAARrqfqsqladlQQLPDILKITEAKLAECQDQLQgyeRKNIDLT 623
Cdd:TIGR02169 236 ERQKEA--IERQLASLEEELEKLTeeiSELEKRLEEIE----------QLLEELNKKIKDLGEEEQLRVK---EKIGELE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 624 AIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREE---------------- 687
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEeledlraeleevdkef 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 688 -----AIHQAQLRLEEKTRECGSL----------ARQLESAIEDARRQVEQTKEQALSKERAAQSKILDL---ETQLSRT 749
Cdd:TIGR02169 381 aetrdELKDYREKLEKLKREINELkreldrlqeeLQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIkkqEWKLEQL 460
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1907136608 750 KTELGQLRRTRDDADRRY---QSRLQDLKDRLEQSESTNRSMQNYVQFLKA 797
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYdrvEKELSKLQRELAEAEAQARASEERVRGGRA 511
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
307-498 |
8.30e-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: 42.44 E-value: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 307 QDKDKEVEELLQEIQcekAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKEL 386
Cdd:COG4942 19 ADAAAEAEAELEQLQ---QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 387 KQKGDRDKETLKKAIRAQKERAEKSE-------EYAEQLHVQLADKDLYVAEALSTLESWRSRYNQVVKDKGDLELEIIV 459
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907136608 460 LNDRVTDLVNQQQSLEEKMREdRDSLVERLHRQTAEYSA 498
Cdd:COG4942 176 LEALLAELEEERAALEALKAE-RQKLLARLEKELAELAA 213
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
487-756 |
1.43e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.25 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 487 ERLHRQTAEYSAFKLENERlkASFAPMEDKLNQAHLEVQQLKASVKNYEGMID-----NYKSQVMKTRLEADEVAAQLER 561
Cdd:COG5185 256 EKLVEQNTDLRLEKLGENA--ESSKRLNENANNLIKQFENTKEKIAEYTKSIDikkatESLEEQLAAAEAEQELEESKRE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 562 CDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKIT--EAKLAECQDQLqgyERKNIDLTAIISDLRSRIEhqgDK 639
Cdd:COG5185 334 TETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSksSEELDSFKDTI---ESTKESLDEIPQNQRGYAQ---EI 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 640 LEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKRE-EAIHQAQLRLEEKTREcgsLARQLESAIEDAR 718
Cdd:COG5185 408 LATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMrEADEESQSRLEEAYDE---INRSVRSKKEDLN 484
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907136608 719 RQVEQTKEQALSKERAAQSKILDLETQLSRTKTELGQL 756
Cdd:COG5185 485 EELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQV 522
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
598-825 |
1.58e-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: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 598 LKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEA------T 671
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralyR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 672 SAQNVEFLQVIAKRE---EAIHQAQL--RLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQL 746
Cdd:COG3883 98 SGGSVSYLDVLLGSEsfsDFLDRLSAlsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 747 SRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQ----SESTNRSMQNYVQFLKASYANVFGDAPYTSSYLTSSPIRSRS 822
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAaaaaAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
...
gi 1907136608 823 PPA 825
Cdd:COG3883 258 AAG 260
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
460-666 |
1.70e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 460 LNDRVTDLvNQQQSLEEKMREDRDSLVERLhrqTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGmid 539
Cdd:PRK09039 58 LNSQIAEL-ADLLSLERQGNQDLQDSVANL---RASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQ--- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 540 nyksqvmktrlEADEVAAQLERcdkenkmlkdeMNKEIEAARRqfqsQLADLQQLpdiLKITEAKLAECQDQlqgyerkn 619
Cdd:PRK09039 131 -----------VSARALAQVEL-----------LNQQIAALRR----QLAALEAA---LDASEKRDRESQAK-------- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907136608 620 idltaiISDLRSRIehqgdklemarekhqasqkeNKQLSQKVDELER 666
Cdd:PRK09039 174 ------IADLGRRL--------------------NVALAQRVQELNR 194
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
160-561 |
1.78e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 160 VAHELAETEHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCT 239
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 240 DINTLTRQKELLL-------QKLSTFEETNRTLRDLLREqhckedSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKE 312
Cdd:PRK02224 406 DLGNAEDFLEELReerdelrEREAELEATLRTARERVEE------AEALLEAGKCPECGQPVEGSPHVETIEEDRERVEE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 313 VEELLQEIQCEKAqaktasELSKSMESMRghlqaQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQkgdr 392
Cdd:PRK02224 480 LEAELEDLEEEVE------EVEERLERAE-----DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE---- 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 393 DKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDlyvaEALSTLESWRSRYNQVVkdkgDLELEIIVLNDRVTDLVNQQQ 472
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELN----SKLAELKERIESLERIR----TLLAAIADAEDEIERLREKRE 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 473 SLEEKMREDRDSLVERLHRQTAEYSAFKLEN-ERLKASFAPMEDKLNQAHLEVQQL---KASVKNYEGMIDNYKSQVMKT 548
Cdd:PRK02224 617 ALAELNDERRERLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELreeRDDLQAEIGAVENELEELEEL 696
|
410
....*....|...
gi 1907136608 549 RLEADEVAAQLER 561
Cdd:PRK02224 697 RERREALENRVEA 709
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
604-752 |
1.82e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 604 KLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQ-----NVEF 678
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrNNKE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907136608 679 LQVIAKREEAIHQAQLRLEEKTRECGSLARQLESAIEDARRQVEQTKEQALSKERAAQSKILDLETQLSRTKTE 752
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
591-782 |
1.85e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.78 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 591 LQQLPDILKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEA 670
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 671 TSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLARQLesaiedarRQVEQTKEQALSKERAAQSKILDLETQLSRTK 750
Cdd:pfam00261 83 LENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKL--------VVVEGDLERAEERAELAESKIVELEEELKVVG 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1907136608 751 TELGQL---RRTRDDADRRYQSRLQDLKDRLEQSE 782
Cdd:pfam00261 155 NNLKSLeasEEKASEREDKYEEQIRFLTEKLKEAE 189
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
214-400 |
2.24e-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: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 214 AAAAKQVMALKDTIGKLKTEKQmtctdINTLTRQKELLLQKLSTFEETNRTLRDLLREQhckedsERLMEQQGTLL--KR 291
Cdd:COG4192 68 VAALPEFAAATNTTERSQLRNQ-----LNTQLADIEELLAELEQLTQDAGDLRAAVADL------RNLLQQLDSLLtqRI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 292 LAEADSEKA--RLLLLLQDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENsrlcmQIKNL--ER 367
Cdd:COG4192 137 ALRRRLQELleQINWLHQDFNSELTPLLQEASWQQTRLLDSVETTESLRNLQNELQLLLRLLAIEN-----QIVSLlrEV 211
|
170 180 190
....*....|....*....|....*....|...
gi 1907136608 368 SGNQHKAEVEAIMEQLKELKQKGDRDKETLKKA 400
Cdd:COG4192 212 AAARDQADVDNLFDRLQYLKDELDRNLQALKNY 244
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
163-480 |
2.35e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 163 ELAETEHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTctDIN 242
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS--RIP 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 243 TLTRQKELLLQKLSTFEETNRTLRDLLREQHCKEDSERlmEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIqc 322
Cdd:TIGR02169 795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE--KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL-- 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 323 EKAQAKTaselsKSMESMRGHLqaqlrckEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIR 402
Cdd:TIGR02169 871 EELEAAL-----RDLESRLGDL-------KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED 938
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 403 AQKERAEKSEEYAEQLHVQLadKDLYVAEALSTLESWRSR----YNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKM 478
Cdd:TIGR02169 939 PKGEDEEIPEEELSLEDVQA--ELQRVEEEIRALEPVNMLaiqeYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
..
gi 1907136608 479 RE 480
Cdd:TIGR02169 1017 RE 1018
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
157-796 |
2.68e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 157 LEEVAHELAETEHENTVLRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMdgaaaAKQVMALKDTIGKLKTEKQM 236
Cdd:pfam02463 178 LIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL-----KLNEERIDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 237 TCTDINTLTRQKELLLQKLSTFEETNRTLRDLLREQHCKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEEL 316
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 317 LQEIQCEKAQAKTASELSKSM--ESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDK 394
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAeeEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLE 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 395 ETLKKAIRAQKERAEKSEEYAEQLHVQLAD--KDLYVAEALSTLESWRSRYNQVVKDKGDLELEIivlndrvtdlVNQQQ 472
Cdd:pfam02463 413 LARQLEDLLKEEKKEELEILEEEEESIELKqgKLTEEKEELEKQELKLLKDELELKKSEDLLKET----------QLVKL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 473 SLEEKMREDRDSLVERLHRQTAeysafklENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEA 552
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQKESK-------ARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSA 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 553 DEVAaqlerCDKENKMLKDEMNKEIEAARRQFQSQLADLQQLPDILKITEAKLAECQDQLQGYERKNIDLTA----IISD 628
Cdd:pfam02463 556 TADE-----VEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAkvveGILK 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 629 LRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLAR 708
Cdd:pfam02463 631 DTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 709 QLESAIEDARRQVEQTKEQALSKeraAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQSESTNRSM 788
Cdd:pfam02463 711 ELKKLKLEAEELLADRVQEAQDK---INEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLK 787
|
....*...
gi 1907136608 789 QNYVQFLK 796
Cdd:pfam02463 788 VEEEKEEK 795
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
514-753 |
2.72e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 514 EDKLNQAHLEVQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLERCDKENKMLKDEMNKEIEAArrqfqsqladlqq 593
Cdd:pfam01576 88 EERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKER------------- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 594 lpdilKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGDKLEMAREKHQASQKENKQLSQKVDELERKLEATSA 673
Cdd:pfam01576 155 -----KLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 674 QNVEFLQVIAKREEAIHQAQLRLEEKTRECGSLA---RQLESAIEDARRQVEQTKEQALSKERAAQskilDLETQLSRTK 750
Cdd:pfam01576 230 QIAELRAQLAKKEEELQAALARLEEETAQKNNALkkiRELEAQISELQEDLESERAARNKAEKQRR----DLGEELEALK 305
|
...
gi 1907136608 751 TEL 753
Cdd:pfam01576 306 TEL 308
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
307-665 |
3.80e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 307 QDKDKEVEELLQEIQCEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLErsgnQHKAEVEAIMEQLKEL 386
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ----QEKELLEKEIERLKET 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 387 KQKGDRDKETLKKAIRAQKERAEKSEEYAEQLHVQLADKDLYVAEALSTLE-------SWRSRYNQVVKDKGDLELEIIV 459
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEqkqkelkSKEKELKKLNEEKKELEEKVKD 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 460 LNDRVTDLVNQQQSLEEKMREDRDSLVERlhRQTAEYSAFKLENERLKASFAPMEDKLNQAHLEVQQLKASVKNYEGMID 539
Cdd:TIGR04523 515 LTKKISSLKEKIEKLESEKKEKESKISDL--EDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 540 NYKSQVMKTRLEADEVAAQLERCDKENKMLKDEmNKEIEAARRQFQSQLADLQQL----PDILKITEAKLAECQDQLQGY 615
Cdd:TIGR04523 593 QKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE-NEKLSSIIKNIKSKKNKLKQEvkqiKETIKEIRNKWPEIIKKIKES 671
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907136608 616 ERKNIDLTAIISD------------LRSRIEHQgdKLEMAREKHQASQKENKQLSQKVDELE 665
Cdd:TIGR04523 672 KTKIDDIIELMKDwlkelslhykkyITRMIRIK--DLPKLEEKYKEIEKELKKLDEFSKELE 731
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
402-799 |
4.02e-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: 41.09 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 402 RAQKERAEKSEEYAEQLHVQLADKDLYVAEaLSTLESWRSRY---NQVVKDKGDLELEIIVLNDRVTDL---VNQQQSLE 475
Cdd:COG3096 781 AAREKRLEELRAERDELAEQYAKASFDVQK-LQRLHQAFSQFvggHLAVAFAPDPEAELAALRQRRSELereLAQHRAQE 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 476 EKMREDRDSLVER---LHRQTAEYSAFKLE--NERLKASFAPMeDKLNQAHLEVQQLKASVKNYEGMIDNYKSqvmkTRL 550
Cdd:COG3096 860 QQLRQQLDQLKEQlqlLNKLLPQANLLADEtlADRLEELREEL-DAAQEAQAFIQQHGKALAQLEPLVAVLQS----DPE 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 551 EADEVAAQLERCDKENKMLKdemnKEIEA-----ARR---------QFQSQLADL-QQLPDILKITEAKLAECQDQLQGY 615
Cdd:COG3096 935 QFEQLQADYLQAKEQQRRLK----QQIFAlsevvQRRphfsyedavGLLGENSDLnEKLRARLEQAEEARREAREQLRQA 1010
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 616 ERKNIDLTAIISDLRSRiehqgdkLEMAREKHQASQKENKQLS------------QKVDELERKLEATSAQNVEFLQVIA 683
Cdd:COG3096 1011 QAQYSQYNQVLASLKSS-------RDAKQQTLQELEQELEELGvqadaeaeerarIRRDELHEELSQNRSRRSQLEKQLT 1083
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 684 KREEAIHQAQLRLeektrecgslaRQLESAIEDARRQVEQTKE-----QALSKERaaqskilDLETQLSRTK------TE 752
Cdd:COG3096 1084 RCEAEMDSLQKRL-----------RKAERDYKQEREQVVQAKAgwcavLRLARDN-------DVERRLHRRElaylsaDE 1145
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1907136608 753 LGQLRRTRDDADRRYQSRLQDLKDRLEQSEStNRSMQNYVQFLKASY 799
Cdd:COG3096 1146 LRSMSDKALGALRLAVADNEHLRDALRLSED-PRRPERKVQFYIAVY 1191
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
114-413 |
4.72e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 114 KMNRYDKKIDSLMNAVGCLKSEVKMQKGERqmAKRFLEERKEELEEVAHEL--AETEHENTVLRHNIERIKEEKDFTMLQ 191
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEE--AKKADEAKKAEEAKKADEAkkAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 192 KKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKTEKQMTCTDintlTRQKELLLQKLSTFEETNRTLRDLLRE 271
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE----AKIKAEELKKAEEEKKKVEQLKKKEAE 1644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 272 QHCKEDSERLMEQQGTL----LKRLAEADSEKARLLLLLQDKDKEVEELLQEiqcEKAQAKTASELSKSMESMRGHLQaQ 347
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIkaaeEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK---EAEEAKKAEELKKKEAEEKKKAE-E 1720
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136608 348 LRCKEAENSrlcMQIKNLERSGNQHKAEVEAIMEQLKELKQKGDRDKETLKKAIRAQKERAEKSEE 413
Cdd:PTZ00121 1721 LKKAEEENK---IKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
174-799 |
4.96e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 174 LRHNIERIKEEKDFTMLQKKHLQQEKECLMSKLVEAEMDgaaaakqVMALKDTIGKLKTEKQMTCTDINTLTRQ------ 247
Cdd:pfam01576 101 MQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEED-------ILLLEDQNSKLSKERKLLEERISEFTSNlaeeee 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 248 KELLLQKLSTFEETNRT-LRDLLRE-----QHCKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQ 321
Cdd:pfam01576 174 KAKSLSKLKNKHEAMISdLEERLKKeekgrQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 322 CEKAQAKTASELSKSMESMRGHLQAQLRCKEAENSRLCMQIKNLERSGNQHKAEVEAIMEQL---KELKQKGDRDKETLK 398
Cdd:pfam01576 254 EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTaaqQELRSKREQEVTELK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 399 KAIRAQKERAEKSEEYAEQLHVQladkdlyvaealsTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKm 478
Cdd:pfam01576 334 KALEEETRSHEAQLQEMRQKHTQ-------------ALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQA- 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 479 REDRDSLVERLHRQTAEYSAFKLENERLKASFApmeDKLNQAHLEVQQLKASVKNYEGM-------IDNYKSQVMKTR-L 550
Cdd:pfam01576 400 KQDSEHKRKKLEGQLQELQARLSESERQRAELA---EKLSKLQSELESVSSLLNEAEGKniklskdVSSLESQLQDTQeL 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 551 EADEVAAQLE-----RCDKENKMLKDEMNKEIEAARRQFQSQLADLQ-QLPDILKITEAKLAECQDQLQGYERKNIDLTA 624
Cdd:pfam01576 477 LQEETRQKLNlstrlRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQaQLSDMKKKLEEDAGTLEALEEGKKRLQRELEA 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 625 IISDLRSRIEhQGDKLEMAREKHQASQK----ENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAQLRLEEKT 700
Cdd:pfam01576 557 LTQQLEEKAA-AYDKLEKTKNRLQQELDdllvDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKE 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 701 RECGSLARQLESAIEdARRQVEQTKEQAlskeRAAQSKILDLETQLSRTKTELGQLRRTRDDADRRYQSRLQDLKDRLEQ 780
Cdd:pfam01576 636 TRALSLARALEEALE-AKEELERTNKQL----RAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQA 710
|
650
....*....|....*....
gi 1907136608 781 SESTNRSMQNYVQFLKASY 799
Cdd:pfam01576 711 TEDAKLRLEVNMQALKAQF 729
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
188-470 |
5.12e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.45 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 188 TMLQKKHLQQEKECLMSKLVEAEMDGAAAAKQVMALKDTIGKLKT----EKQMTCTDINTLTRQKELLLQKLSTFEETNR 263
Cdd:COG5022 780 GFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKtikrEKKLRETEEVEFSLKAEVLIQKFGRSLKAKK 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 264 TLRDLLREQhCKEDSERLMEQQGTLLKRLAEADSEKARLLLLLQDKDKEVEELLQEIQC---EKAQAKTA--SELSKSME 338
Cdd:COG5022 860 RFSLLKKET-IYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSdliENLEFKTEliARLKKLLN 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 339 SMRGHLQAQL-RCKEAENSRLCMQIKNLERSGNQHKAEV---EAIMEQLKELKQKGDRDKETLKKaIRAQKERAEKSEEY 414
Cdd:COG5022 939 NIDLEEGPSIeYVKLPELNKLHEVESKLKETSEEYEDLLkksTILVREGNKANSELKNFKKELAE-LSKQYGALQESTKQ 1017
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907136608 415 AEQLHVQLADKDlYVAEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQ 470
Cdd:COG5022 1018 LKELPVEVAELQ-SASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLR 1072
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
430-751 |
7.04e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 39.67 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 430 AEALSTLESWRSRYNQVVKDKGDLELEIIVLNDRVTDLVNQQQSLEEKMREDRD--SLVERLHRQTAEYSAfKLENERLK 507
Cdd:pfam05622 127 SDKVKKLEATVETYKKKLEDLGDLRRQVKLLEERNAEYMQRTLQLEEELKKANAlrGQLETYKRQVQELHG-KLSEESKK 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 508 ASFAPMEDKLNQAHLE---------------------------VQQLKASVKNYEGMIDNYKSQVMKTRLEADEVAAQLE 560
Cdd:pfam05622 206 ADKLEFEYKKLEEKLEalqkekerliierdtlretneelrcaqLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 561 RCDKENKMLKdemnkeiEAARRQFQSQLADLQQLpdiLKITEAKLAECQDQLQGYERKNIDLTAIISDLRSRIEHQGD-- 638
Cdd:pfam05622 286 RLQHENKMLR-------LGQEGSYRERLTELQQL---LEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSka 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907136608 639 --------KLEMAREKHQASQKENKQLSQKVDELERKLEATSAQNVEFLQVIAKREEAIHQAqlrLEEKTRECGSLARQL 710
Cdd:pfam05622 356 edssllkqKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEALRKKDEDMKA---MEERYKKYVEKAKSV 432
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1907136608 711 ESAIEDARRQVEQTKEQALSKERAAQSK-ILDLETQLSRTKT 751
Cdd:pfam05622 433 IKTLDPKQNPASPPEIQALKNQLLEKDKkIEHLERDFEKSKL 474
|
|
| |
