|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
259-618 |
5.70e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.69 E-value: 5.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 259 YEKLKAQFEQDENKLRAdleKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQAEnrklledknthdfeLDEAKVQGE 338
Cdd:COG1196 215 YRELKEELKELEAELLL---LKLRELEAELEELEAELEELEAELEELEAELAELEAE--------------LEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 339 HLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEH---EGQMAELEKRLEKVSEKEKEAIEQLEKIQ 415
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELaelEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 416 KENKTIVKENVYLSESKQVLLESEINLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQNQKLLREA 495
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 496 QDSAELLEEVQKGKREIDHLRQQLAHQSSEAGSVGQLQQKLAESEHREYL-LQLELERVMKMERDLDGRIEGYIRSEAAA 574
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAeAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 71990528 575 NNELERLRKDTAEQKEKLEAMEMEARSKDLELADLTRKLAKARE 618
Cdd:COG1196 518 GLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAA 561
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
338-920 |
2.37e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.77 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 338 EHLEKQRKEAwEKVEQLQEMLGELEAELdRQKELKlQLEKDMEDLRKEHEGQMAELEKRLEKVSEKEKEAIEQLEKIQKE 417
Cdd:COG1196 203 EPLERQAEKA-ERYRELKEELKELEAEL-LLLKLR-ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 418 NKTIVKenvyLSESKQVLLESEINLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQNQKLLREAQD 497
Cdd:COG1196 280 ELELEE----AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 498 SAELLEEVQKGKREIDHLRQQLAHQSSEAgsvgqlQQKLAESEHREYLLQLELERVMKMERDLDGRIEGYIRSEAAANNE 577
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEEL------AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 578 LERLRKDTAEQKEKLEAMEMEARSKDLELADLTRKLAKAREEHETfeinARNQFYAVTGQMHEDIESYKQRLLELEPYPG 657
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL----LEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 658 KIISGSFRDFPSQTDPSPATTDAWMQTDVEEQLmVSPEVSLVSEAPSSLQDSRRSSHLDEKLRRT---------IEKIGE 728
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA-ALEAALAAALQNIVVEDDEVAAAAIEYLKAAkagratflpLDKIRA 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 729 LLAEHESFQESLRDPEFHTAEA----FRKISQLLKSILSGANSEEMLERIWTWLTLKTKALVEQQDEQMKKVQKAGEMLL 804
Cdd:COG1196 585 RAALAAALARGAIGAAVDLVASdlreADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 805 SQLREKESDNEVLTKKSLEMEAAAEEFRTYYNDMLTENDELRHRIVQLDEIREVESSNstkiEKGLREQLEQAQHELEKK 884
Cdd:COG1196 665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELE----EEALEEQLEAEREELLEE 740
|
570 580 590
....*....|....*....|....*....|....*.
gi 71990528 885 KREYMWKLQQKDEFYEIMDRNVKETEKENKRLLRKR 920
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
258-938 |
1.07e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 88.96 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 258 DYEKLKAQFEQDENKLrADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQAENRKLLEDKNTHDFELDEAKVQG 337
Cdd:TIGR02168 233 RLEELREELEELQEEL-KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 338 EHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEHEGQMAELEKRLEKVSEKEKEAIEQlekiqke 417
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL------- 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 418 nktivkenvylsESKQVLLESEIN-LKNELDEMAVKLRNSQHQVAGLNEKISEEkrRRKKQDADVTRLDEQNQKLLREAQ 496
Cdd:TIGR02168 385 ------------RSKVAQLELQIAsLNNEIERLEARLERLEDRRERLQQEIEEL--LKKLEEAELKELQAELEELEEELE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 497 DSAELLEEVQKGKREIDHLRQQLAHQsseagsVGQLQQKLAESEHREYLLQlelervmkmerDLDGRIEGYIRSEAAANN 576
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQA------LDAAERELAQLQARLDSLE-----------RLQENLEGFSEGVKALLK 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 577 ELERLRKDTAEQKEKLEAMEMEARSKDLELAD-----LTRKLAKAREEHETFEINA--RNQFYAVTGQMHEDIESYKQRL 649
Cdd:TIGR02168 514 NQSGLSGILGVLSELISVDEGYEAAIEAALGGrlqavVVENLNAAKKAIAFLKQNElgRVTFLPLDSIKGTEIQGNDREI 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 650 LELEPYPGKIISgSFRDFPSQTDP-------------SPATTDAWMQTDVEEQLMVSPEVSLVS-----------EAPSS 705
Cdd:TIGR02168 594 LKNIEGFLGVAK-DLVKFDPKLRKalsyllggvlvvdDLDNALELAKKLRPGYRIVTLDGDLVRpggvitggsakTNSSI 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 706 LQDSRRSSHLDEKLRRTIEKIGELLAE-------HESFQESLRDPEFHTAEAFRKISQLLKSILSGANSEEMLERIWTWL 778
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKAlaelrkeLEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 779 TLKTKALVEQQDEQMKKVQKAGEMLLSQLREKESDNEVLTKKSLEMEAAAEEF-----------------RTYYNDMLTE 841
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelraeltllneeaanlRERLESLERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 842 NDELRHRIVQLDEIREVESSNSTKIEK---GLREQLEQAQHELEKKKREYMWKLQQKDEF---YEIMDRNVKETEKENKR 915
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAeieELEELIEELESELEALLNERASLEEALALLrseLEELSEELRELESKRSE 912
|
730 740
....*....|....*....|...
gi 71990528 916 LLRKRTEDKERMDDFMLNIRKAQ 938
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLE 935
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
230-520 |
2.00e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 84.72 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 230 NLQIEVDQLHSEIEVIGKKKSDLENRLFDYEKLKAQFEQDENKLRA---DLEKKLKTSQEKLVKYEGKIEELQSRLNKKR 306
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKeleELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 307 KELEEVQAENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEH 386
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 387 ---EGQMAELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENVYLSESKQVLLESEINLKNELDEMAVKLRNSQHQVAGL 463
Cdd:TIGR02168 834 aatERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 464 NEKISE-----EKRRRKKQDADVtRLDEQNQKLLREAQDSAELLE--------EVQKGKREIDHLRQQLA 520
Cdd:TIGR02168 914 RRELEElreklAQLELRLEGLEV-RIDNLQERLSEEYSLTLEEAEalenkiedDEEEARRRLKRLENKIK 982
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
278-581 |
2.50e-14 |
|
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: 77.79 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 278 EKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQAENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQEM 357
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 358 LGELEAELdrqKELKLQLEKdMEDLRKEHEGQMAELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENVYLSESKQVLLE 437
Cdd:TIGR02168 756 LTELEAEI---EELEERLEE-AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 438 SEINLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQNQKLLREAQDSAELLEEVQKGKREIDHLRQ 517
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71990528 518 QLAHQSSEAG-SVGQLQQKLAESEHREY--------LLQLELERVMKMERDLDGRIEGYIRSEAAANNELERL 581
Cdd:TIGR02168 912 ELRRELEELReKLAQLELRLEGLEVRIDnlqerlseEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
247-634 |
4.48e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.90 E-value: 4.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 247 KKKSDLENRLFDYEKLKAQFEQDENKLrADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQAENRKLLEDKNTH 326
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAEL-EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 327 DFELDEAKVQGEHLEKQRKEA------WEKV-----EQLQEMLGELEAELDRQKELKLQLEKDmEDLRKEHEGQMAELEK 395
Cdd:COG1196 301 EQDIARLEERRRELEERLEELeeelaeLEEEleeleEELEELEEELEEAEEELEEAEAELAEA-EEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 396 RLEKVSEKEKEAIEQLEKIQKENKTIVKENVYLSESKQVLLESEINLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRK 475
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 476 KQDAdvtRLDEQNQKLLREAQDSAELLEEVQKGKREIDHLRQQLAHQSSEAGSVGQLQQKLAESEHREYLLQL---ELER 552
Cdd:COG1196 460 ALLE---LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLigvEAAY 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 553 VMKMERDLDGRIEGYIRSEAAANNELERLRKDTAEQKEKLEAMEMEARSKDLELADLTRKLAKAREEHETFEINARNQFY 632
Cdd:COG1196 537 EAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYY 616
|
..
gi 71990528 633 AV 634
Cdd:COG1196 617 VL 618
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
274-612 |
5.39e-12 |
|
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: 70.10 E-value: 5.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 274 RADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQAENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQ 353
Cdd:TIGR02169 697 LRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 354 LQEMLGELEAELDRQKELKLQLEKD-MEDLRKEHEGQMAELEKRLEKVSEKEkeaieqlEKIQKENKTIVKENVYLSESK 432
Cdd:TIGR02169 777 LEEALNDLEARLSHSRIPEIQAELSkLEEEVSRIEARLREIEQKLNRLTLEK-------EYLEKEIQELQEQRIDLKEQI 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 433 QVLLESEINLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADvtrldeqnqklLREAQDSAELLE-EVQKGKRE 511
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ-----------LRELERKIEELEaQIEKKRKR 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 512 IDHLRQQLAHQSSEAGSVGQLQQKLAESEHREyllqLELERVMKMERDLDGRIEGYIRSEAAANNELERLRKDTAEQKEK 591
Cdd:TIGR02169 919 LSELKAKLEALEEELSEIEDPKGEDEEIPEEE----LSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEK 994
|
330 340
....*....|....*....|.
gi 71990528 592 LEAMEMEARSKDLELADLTRK 612
Cdd:TIGR02169 995 RAKLEEERKAILERIEEYEKK 1015
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
229-887 |
5.70e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 5.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 229 ANLQIEVDQLHSEIEVIGKKKSDLENRLFDYEKLKAQFEQDENKLRAdlekKLKTSQEKLVKYEGKIEELQSRLNKKRKE 308
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE----RLANLERQLEELEAQLEELESKLDELAEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 309 LEEVQAENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEHEG 388
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 389 QMAELEKRLEKVSEKEKEAI--------EQLEKIQKENKTIVKENVYLSESKQVLLESEINLKNELDEMAVK---LRNSQ 457
Cdd:TIGR02168 419 LQQEIEELLKKLEEAELKELqaeleeleEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARldsLERLQ 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 458 HQVAGLNEKISEEKRRRKKQDADVTRLDEQ------------------NQKLLREAQDSA----ELLEEVQKGKR---EI 512
Cdd:TIGR02168 499 ENLEGFSEGVKALLKNQSGLSGILGVLSELisvdegyeaaieaalggrLQAVVVENLNAAkkaiAFLKQNELGRVtflPL 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 513 DHLRQQLAHQSSEAGSVGQLQQKLAESEHREYLLQLEL----------------------------ERVMKMERDL---D 561
Cdd:TIGR02168 579 DSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllggvlvvddldnalelakklrpgYRIVTLDGDLvrpG 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 562 GRIEGYIRSEAAA----NNELERLRKDTAEQKEKLEAMEME---ARSKDLELADLTRKLAKAREEHETFEINARNQFYAV 634
Cdd:TIGR02168 659 GVITGGSAKTNSSilerRREIEELEEKIEELEEKIAELEKAlaeLRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 635 TGQMHEDIESYKQRLLELEPYPGKIIsgSFRDFPSQTDPSPATTDAWMQTDVEEQLMVSPEVSLVSEAPSSLQDsrRSSH 714
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIE--ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA--ELTL 814
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 715 LDEKLRRTIEKIGELLAEHESFQESLRDPEFHTAEAFRKISQLLKSIlsgANSEEMLERIWTWLTLKTKaLVEQQDEQMK 794
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI---EELEELIEELESELEALLN-ERASLEEALA 890
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 795 KVQKAGEMLLSQLREKESDNEVLTKKSLEMEAAAEEFRTYYNDMLTENDELRHRIVQLDEIREVESSNSTKIEKGLREQL 874
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEA 970
|
730
....*....|...
gi 71990528 875 EQAQHELEKKKRE 887
Cdd:TIGR02168 971 RRRLKRLENKIKE 983
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
284-500 |
7.50e-12 |
|
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: 68.25 E-value: 7.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 284 SQEKLVKYEGKIEELQSRLNKKRKELEEVQAENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEA 363
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 364 ELDRQKELKLQLEKDMEDLRKEHEGQM-------AELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENVYLSESKQVLL 436
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71990528 437 ESEINLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQNQKLLREAQDSAE 500
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
234-653 |
8.55e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 8.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 234 EVDQLHSEIEVIGKKKSDLENRLfdyEKLKAQFEQDENKLR------ADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRK 307
Cdd:COG1196 233 KLRELEAELEELEAELEELEAEL---EELEAELAELEAELEelrlelEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 308 ELEEVQAENRKLLEdknthdfELDEAKVQGEHLEKQRKEAwekVEQLQEM---LGELEAELDRQKELKLQLEKDMEDLRK 384
Cdd:COG1196 310 RRRELEERLEELEE-------ELAELEEELEELEEELEEL---EEELEEAeeeLEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 385 EHEG---QMAELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENVYLSESKQVLLESEINLKNELDEMAVKLRNSQHQVA 461
Cdd:COG1196 380 ELEElaeELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 462 GLNEKISEEKRRRKKQDADVTRLDEQNQKLLREAQDSAELLEEVQkGKREIDHLRQQLAHQSSEAGSVGQLQQKLAESEH 541
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE-GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 542 --REYLLQLELERVMKMERDLDGRIEGYIRSEAAANNEL--ERLRKDTAEQKEKLEAMEMEARSKDLELADLTRKLAKAR 617
Cdd:COG1196 539 alEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL 618
|
410 420 430
....*....|....*....|....*....|....*.
gi 71990528 618 EEHETFEINARNQFYAVTGQMHEDIESYKQRLLELE 653
Cdd:COG1196 619 GDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGE 654
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
229-620 |
1.73e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 229 ANLQIEVDQLHSEIEVIGKKKSDLENRLFDYEKLKAQFEQDEnkLRADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKE 308
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ--ELEALEAELAELPERLEELEERLEELRELEEELEEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 309 LEEVQAENRKLLEDKNTHDFELDEakvQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEHE- 387
Cdd:COG4717 169 EAELAELQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERl 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 388 -----------------GQMAELEKRLEKV---------------SEKEKEAIEQLEKIQKENKTIVKENVYLSESKQVL 435
Cdd:COG4717 246 kearlllliaaallallGLGGSLLSLILTIagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 436 LESEINLKNELDEmAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTR---LDEQNQKLLREAQDSAELLEEVQKGKREI 512
Cdd:COG4717 326 AALGLPPDLSPEE-LLELLDRIEELQELLREAEELEEELQLEELEQEIaalLAEAGVEDEEELRAALEQAEEYQELKEEL 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 513 DHLRQQLA------HQSSEAGSVGQLQQKLAESEHREYLLQLELERVMKMERDLDGRIEgyirsEAAANNELERLRKDTA 586
Cdd:COG4717 405 EELEEQLEellgelEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELE-----QLEEDGELAELLQELE 479
|
410 420 430
....*....|....*....|....*....|....
gi 71990528 587 EQKEKLEAMEMEARSKDLELADLTRKLAKAREEH 620
Cdd:COG4717 480 ELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
252-653 |
1.43e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 252 LENRLFDYEKLKAQFEQDENKLRADLEKKLKTSQEKLVKYEGKIEELQS---RLNKKRKELEEVQAENRKLLEDKNTHDF 328
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEEleeELEELEAELEELREELEKLEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 329 --ELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEHEGQMAELEKRLEKVSEKEKE 406
Cdd:COG4717 131 yqELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 407 AIEQLEKIQKENKTIVKENVYLSESKQVLLESEINLKNE-----------LDEMAVKLRNSQHQVAGL------------ 463
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGVlflvlgllallf 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 464 -----NEKISEEKRRRKKQDADVTRLDEQNQKLLR------------EAQDSAELLEEVQKGKREIDHLRQQLAHQSSEA 526
Cdd:COG4717 291 lllarEKASLGKEAEELQALPALEELEEEELEELLaalglppdlspeELLELLDRIEELQELLREAEELEEELQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 527 GSVGQLQQKLAESEHREYLLQLELERVMKMERDLDgRIEGYIRSEAAANNELERlRKDTAEQKEKLEAMEMEARSKDLEL 606
Cdd:COG4717 371 EIAALLAEAGVEDEEELRAALEQAEEYQELKEELE-ELEEQLEELLGELEELLE-ALDEEELEEELEELEEELEELEEEL 448
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 71990528 607 ADLTRKLAKAREEHETFEINARNQfyavtgQMHEDIESYKQRLLELE 653
Cdd:COG4717 449 EELREELAELEAELEQLEEDGELA------ELLQELEELKAELRELA 489
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
286-621 |
1.83e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.09 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 286 EKLVKYEGKIEELQSRLNKKRKELEEVQAENRKLLEDKNthdfelDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEael 365
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERE------KAERYQALLKEKREYEGYELLKEKEALERQKE--- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 366 drqkelklQLEKDMEDLRKehegqmaELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKenvyLSESKQvlleseINLKNE 445
Cdd:TIGR02169 241 --------AIERQLASLEE-------ELEKLTEEISELEKRLEEIEQLLEELNKKIKD----LGEEEQ------LRVKEK 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 446 LDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQNQKLLRE----AQDSAELLEEVQKGKREIDHLRQQLAH 521
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREieeeRKRRDKLTEEYAELKEELEDLRAELEE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 522 QSSEAGS----VGQLQQKLAESEHREYLLQLELERVMKMERDLDGRIegyirseAAANNELERLRKDTAEQKEKLEAMEM 597
Cdd:TIGR02169 376 VDKEFAEtrdeLKDYREKLEKLKREINELKRELDRLQEELQRLSEEL-------ADLNAAIAGIEAKINELEEEKEDKAL 448
|
330 340
....*....|....*....|....
gi 71990528 598 EARSKDLELADLTRKLAKAREEHE 621
Cdd:TIGR02169 449 EIKKQEWKLEQLAADLSKYEQELY 472
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
251-944 |
2.28e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.09 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 251 DLENRLFDYE-KLKAQFEQDENKLRADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQAENRKLLEDK-NTHDF 328
Cdd:TIGR02169 215 ALLKEKREYEgYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqLRVKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 329 ELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEHEGQMAELEKRLEKVSEKEKEai 408
Cdd:TIGR02169 295 KIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE-- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 409 eqLEKIQKENKTIVKENVYLSESKQVLLESEINLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVT----RL 484
Cdd:TIGR02169 373 --LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEdkalEI 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 485 DEQNQKLLREAQDSAELLEEVQKGKREIDHLRQQLAHQSSE----AGSVGQLQQKLAESEHREYLLQLELERVMKMERDL 560
Cdd:TIGR02169 451 KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRElaeaEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 561 DGRIEGYIRS-EAAANNELERLRKDT----AEQKEKLEAM-----------EMEARSKDLELADLTRKLAKAREEHEtFE 624
Cdd:TIGR02169 531 GSVGERYATAiEVAAGNRLNNVVVEDdavaKEAIELLKRRkagratflplnKMRDERRDLSILSEDGVIGFAVDLVE-FD 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 625 INARNQFYAVTGQ--MHEDIESYKQ-----RLLELE----PYPGKIISGSFRDFPSQTDPSpattdawmqTDVEEQLMVS 693
Cdd:TIGR02169 610 PKYEPAFKYVFGDtlVVEDIEAARRlmgkyRMVTLEgelfEKSGAMTGGSRAPRGGILFSR---------SEPAELQRLR 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 694 PEVSLVSEAPSSLQDSRRS--SHLDE---KLRRTIEKIGELLAEHESFQESLRDPEFHTAEAFRKISQLLKSIlsgANSE 768
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRieNRLDElsqELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI---ENVK 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 769 EMLERIWTWLTLKTKALVEQQDEQMKKVQKAGEmllSQLREKESDNEVLTKKSLEMEAAAEEFRTYYNDMLTENDELRHR 848
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEALNDLEARLSH---SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 849 IVQLDEIREVESSNstkiekglREQLEQAQHELEKKKREYMWKLQQKDEFYEIMDRNVKETEKENKRLLRKRTEDKERMD 928
Cdd:TIGR02169 835 IQELQEQRIDLKEQ--------IKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
730
....*....|....*.
gi 71990528 929 DFMLNIRKAQEQWKYL 944
Cdd:TIGR02169 907 ELEAQIEKKRKRLSEL 922
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
234-434 |
3.08e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 63.31 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 234 EVDQLHSEIEVIGKKKSDLENRLFDYEKLKAQFEQDENKLRADLEkklkTSQEKLVKYEGKIEELQSRLNKKRKELEEVQ 313
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE----ALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 314 AENRK----------LLEDKNTHDFeLDEAKVQgEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLR 383
Cdd:COG3883 93 RALYRsggsvsyldvLLGSESFSDF-LDRLSAL-SKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 71990528 384 KEHEGQMAELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENVYLSESKQV 434
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
231-440 |
3.09e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.32 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 231 LQIEVDQLHSEIEVIGKKKSDLENRLFDYEKLKAQFEQDENKLRAD---LEKKLKTSQEKLVKYEGKIEELQSRLNKKRK 307
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEieeLEREIEEERKRRDKLTEEYAELKEELEDLRA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 308 ELEEVQAENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLR---K 384
Cdd:TIGR02169 372 ELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAleiK 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 71990528 385 EHEGQMAELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENVYLSESKQVLLESEI 440
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
234-512 |
4.13e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.93 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 234 EVDQLHSEIEVIGKKKSDLENRLFDYEKLKAQFEQDENKLRADLEK-KLKTSQEKLVKYEGKIEELQSRLNKKRKELEEV 312
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREI 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 313 QAENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDL---RKEHEGQ 389
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLkkeRDELEAQ 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 390 MAELEKRLEKVSEK-------EKEAIEQLEKIQKENKTIVKENVYLSESKQVLLESEiNLKNELDEMAVKLRNSQHQVAG 462
Cdd:TIGR02169 898 LRELERKIEELEAQiekkrkrLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE-DVQAELQRVEEEIRALEPVNML 976
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 71990528 463 LNEKISEEKRRRKKqdadvtrLDEQNQKLLREAQDSAELLEEVQKGKREI 512
Cdd:TIGR02169 977 AIQEYEEVLKRLDE-------LKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
106-634 |
5.45e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 5.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 106 ESLRGENESLREENCSLREESRRMDLVDKENvipviprlvfDEKPDLDPITVKSSEQIKKELLSFIKNDEDRTIMEA-KM 184
Cdd:PTZ00121 1281 DELKKAEEKKKADEAKKAEEKKKADEAKKKA----------EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAaKA 1350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 185 ENMLISDSKPPAKVFTATATIQVDTEKMDANIQTDKDDHVNvvnanlqiEVDQLHSEIEVIGKKKSDLENRLFDYEKLKA 264
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK--------KADEAKKKAEEDKKKADELKKAAAAKKKADE 1422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 265 QFEQDENKLRADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQAENrklLEDKNTHDFELDEAKVQGEHLEKQR 344
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE---AKKKAEEAKKADEAKKKAEEAKKKA 1499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 345 KEAWEKVEQLQEMLGELEAELDRQKE--LKLQLEKDMEDLRKEHEGQMAELEKRLEKVSE-KEKEAIEQLEKIQKENKTI 421
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADeaKKAEEAKKADEAKKAEEKKKADELKKAEELKKaEEKKKAEEAKKAEEDKNMA 1579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 422 VKENVYLSESKQVLLESEINLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQNQKL--LREAQDSA 499
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAeeLKKAEEEN 1659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 500 ELLEEVQKGKREIDHLRQQLAHQSSEAgsvgqlQQKLAESEHREYLLQLELERVMKMERDLDGRIEGYIRSEAAANNELE 579
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDKKKAEEAKKAEED------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 71990528 580 RLRKDTAEQKEKLEAMEMEARSKdleladltRKLAKAREEHETFEINARNQFYAV 634
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAKKDEEEK--------KKIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
197-544 |
1.55e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 61.96 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 197 KVFTATATIQVDTEKMDANIQTdkDDHVNVVNANLQIEVDQLHSEiEVIGK--KKSDLENRLFDYEKlkaqfeqDENKLR 274
Cdd:COG3206 51 PVYEASATLLVEPQSSDVLLSG--LSSLSASDSPLETQIEILKSR-PVLERvvDKLNLDEDPLGEEA-------SREAAI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 275 ADLEKKLKTSQEKL-----VKYEGKI-EELQSRLNKKRKELEEVQAENRKlledknthdfelDEAKVQGEHLEKQRKEAW 348
Cdd:COG3206 121 ERLRKNLTVEPVKGsnvieISYTSPDpELAAAVANALAEAYLEQNLELRR------------EEARKALEFLEEQLPELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 349 EKVEQLQEMLGELeaeldRQKELKLQLEKDMEDLrkehEGQMAELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENVYL 428
Cdd:COG3206 189 KELEEAEAALEEF-----RQKNGLVDLSEEAKLL----LQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 429 SESKQV--LLESEINLKNELDEMAVKLRNSQHQVAGLNEKISEEKRrrkkqdadvtRLDEQNQKLLREAQdsaellEEVQ 506
Cdd:COG3206 260 LQSPVIqqLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA----------QLQQEAQRILASLE------AELE 323
|
330 340 350
....*....|....*....|....*....|....*...
gi 71990528 507 KGKREIDHLRQQLAHQSSEAGSVGQLQQKLAESEhREY 544
Cdd:COG3206 324 ALQAREASLQAQLAQLEARLAELPELEAELRRLE-REV 360
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
275-413 |
4.33e-09 |
|
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: 58.01 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 275 ADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQAE----NRKLLEDKNTHDF-----ELDEAKVQGEHLEKQRK 345
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyEEQLGNVRNNKEYealqkEIESLKRRISDLEDEIL 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71990528 346 EAWEKVEQLQEMLGELEAELDrqkelklQLEKDMEDLRKEHEGQMAELEKRLEKVSEKEKEAIEQLEK 413
Cdd:COG1579 114 ELMERIEELEEELAELEAELA-------ELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
218-629 |
9.15e-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: 9.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 218 TDKDDHVNVVNANLQIEVDQLHSEIEVIGKKKSDLENRLFDYEKLKAQFEQDENKLRaDLEKKLKTSQEKLVKYEGKIEE 297
Cdd:TIGR04523 92 KKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIK-KKEKELEKLNNKYNDLKKQKEE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 298 LQSRLNKKRKELEEVQAENRK----------LLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDR 367
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKNIDKiknkllklelLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 368 QKELKLQLEKDMEDLRKEHEGQMAELEKRLEKVSEKEKEAIEQLEKIQKENKtiVKENVYLSESKQVLLeseiNLKNELD 447
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN--QKEQDWNKELKSELK----NQEKKLE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 448 EMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQ----NQKLLREAQDSAELLEEVQKGKREIDHLRQQLAHQS 523
Cdd:TIGR04523 325 EIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREleekQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 524 SEAgsvGQLQQKLAESEHREYLLQLELERVMKMERDLDGRIEGYIRSEAAANNELERLRKDTAEQKEKLEAMEMEARSKD 603
Cdd:TIGR04523 405 KLN---QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
410 420
....*....|....*....|....*.
gi 71990528 604 LELADLTRKLAKAREEHETFEINARN 629
Cdd:TIGR04523 482 QNLEQKQKELKSKEKELKKLNEEKKE 507
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
267-973 |
1.22e-08 |
|
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: 59.21 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 267 EQDENKLRADLEKKLKTSQEKLVKYEGKIEELQSRLNK--KRKELEEVQAENRKLLEDKNTHDFELDEAKVQGEHLEKQR 344
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKlkEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 345 KEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEHEGQmAELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKE 424
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEEL-KLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 425 NVYLSESKQVLLESEINLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQNQKLLREAQDSAELLEE 504
Cdd:pfam02463 323 KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 505 VQKGKREIDHLRQQLAHQSSEAGSVGQLQQKLAESEHREYLLQLELERVMKMERDLDGRIEGYIRSEAAANNELERLRKD 584
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 585 TAEQKEKLEAM-EMEARSKDLELADLTRKLAKAREEHETFEINARNQFYAVTGQMHEDIESYKQRLLELEPYPGKIISGS 663
Cdd:pfam02463 483 QEQLELLLSRQkLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 664 FRDFPSQTDPSPATtdawMQTDVEEQLMVSPEVSLVSEAPSSLQDSRRSSHLDEKLRRTIEKIGELLAEHESFQESLRDP 743
Cdd:pfam02463 563 RQKLVRALTELPLG----ARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLK 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 744 EFHTAeafrkISQLLKSILSGANSEEMLERIWTWLTLKTKALVEQQDEQMKKVQKAGEMLLSQLREKESDNEVLTKKSLE 823
Cdd:pfam02463 639 ESAKA-----KESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELK 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 824 MEAAAEEFRTYYNDMLTENDELRHRIVQLDEIREVESSNSTKIEKGLREQLEQAQHELEKKKREYMWKLQQKDEFYEIMD 903
Cdd:pfam02463 714 KLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKE 793
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 904 RNVKETEKENKRLLRKRTEDKERMDDFMLNIRKAQEQWKYLRMRNCQRHTSMMNMLESVKKKKHESRDMN 973
Cdd:pfam02463 794 EKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEI 863
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
282-426 |
3.21e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 57.48 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 282 KTSQEKLVKYEgkiEELQSRLNKKRKELEEVQAEnrKLLEDKnthdfelDEAKVQGEHLEKQRKEAWEKVEQLQEMLGEL 361
Cdd:PRK12704 27 KIAEAKIKEAE---EEAKRILEEAKKEAEAIKKE--ALLEAK-------EEIHKLRNEFEKELRERRNELQKLEKRLLQK 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71990528 362 EAELDRQKELKLQLEKDMEDLRKEHEGQMAELEKRLEKVSEKEKEAIEQLEKI----QKENKTIVKENV 426
Cdd:PRK12704 95 EENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsgltAEEAKEILLEKV 163
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
231-624 |
4.12e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 231 LQIEVDQLHSEIEVIGKKKSDLENRLFDYEKLKAQFEQDENKLrADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELE 310
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL-ETLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 311 EVQAENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEhegqM 390
Cdd:PRK02224 290 ELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREE----A 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 391 AELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENVY-------LSESKQVLLESEINLKNELDEMAVKLRNSQH----- 458
Cdd:PRK02224 366 AELESELEEAREAVEDRREEIEELEEEIEELRERFGDapvdlgnAEDFLEELREERDELREREAELEATLRTARErveea 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 459 ------------------------------QVAGLNEKISEEKRRRKKQDADVTRLDE------QNQKLLREAQDSAELL 502
Cdd:PRK02224 446 ealleagkcpecgqpvegsphvetieedreRVEELEAELEDLEEEVEEVEERLERAEDlveaedRIERLEERREDLEELI 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 503 EEVQKGKRE----IDHLRQQLAHQSSEAGSVGQLQQKLAES--EHREYLLQLELERV-MKMERDLDGRIEGYIRSEAAAN 575
Cdd:PRK02224 526 AERRETIEEkrerAEELRERAAELEAEAEEKREAAAEAEEEaeEAREEVAELNSKLAeLKERIESLERIRTLLAAIADAE 605
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 71990528 576 NELERLRkdtaEQKEKLEAMEMEARSKDLELADLTRKLA---------KAREEHETFE 624
Cdd:PRK02224 606 DEIERLR----EKREALAELNDERRERLAEKRERKRELEaefdearieEAREDKERAE 659
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
229-519 |
4.74e-08 |
|
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: 57.39 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 229 ANLQIEVDQLHSEIEVIGKKKSDLENRlfdYEKLKAQFEQDENKLRADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKE 308
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKR---LEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 309 LEEVQAENRKLLEdknthdfELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAEldrqkelklqlekdMEDLRKEHEg 388
Cdd:TIGR02169 317 LEDAEERLAKLEA-------EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE--------------LEDLRAELE- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 389 qmaELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENVYLSESKQVLLESEINLKNELDEMAVKLRNSQHQVAGLNEKIS 468
Cdd:TIGR02169 375 ---EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK 451
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 71990528 469 EEKRRRKKQDADvtrLDEQNQKLLREAQDSAELLEEVQKGKREIDHLRQQL 519
Cdd:TIGR02169 452 KQEWKLEQLAAD---LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
230-925 |
6.61e-08 |
|
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: 56.90 E-value: 6.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 230 NLQIEVDQLHSEIEVIGKKKSDLENRLFDYEKLKAQFEQDENKL----RADLEKKLKTSQEKLVKYEGKIEELQSRLNKK 305
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEeekeKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 306 RKELEEVQAENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQEmLGELEAELDRQKELKLQLEKDMEDLRKE 385
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEK-LQEKLEQLEEELLAKKKLESERLSSAAK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 386 HEGQMAELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENVYLSESKQVLLESEINLKNELDEMAVKLRNSQHQVAGLNE 465
Cdd:pfam02463 392 LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 466 KISEEKRRRKKQDADVTRLDEQNQKLLREAQDSAELLEEV-QKGKREIDHLRQQLAHQSSEAGSVGQLQQKLAES----- 539
Cdd:pfam02463 472 DLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVlLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIStaviv 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 540 ----EHREYLLQLELERVMKMERDLDGRIEGYIRSEAAANNELERLRKDTAEQKEKLEAMEMEARSKDLELADLTRKLAK 615
Cdd:pfam02463 552 evsaTADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKD 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 616 AREEHETFEINARNQFYAVTGQMHEDIESYKQRLLELEPYPGKIISGSFRDFPSQTDPSPATTDAWMQTDVEEQLMVSPE 695
Cdd:pfam02463 632 TELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEE 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 696 VSLVSEAPSSLQDSRRSSHLDEKLRRTIEKIGELLAEHESFQESLRDPEFHTAEAFRKISQLLKSILSGANSEEMLERIW 775
Cdd:pfam02463 712 LKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEE 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 776 TWLTLKTKALVEQQDEQMKKVQKAGEMLLSQLREKESDNEVLTKKSLEMEAAAEEFRTYYNDMLTENDELrhRIVQLDEI 855
Cdd:pfam02463 792 KEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEE--EITKEELL 869
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 856 REVESSNSTKIEKGLREQLEQAQHELEKKKREYMWKLQQKDEFYEIMDRNVKETEKENKRLLRKRTEDKE 925
Cdd:pfam02463 870 QELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEE 939
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
272-571 |
8.43e-08 |
|
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: 56.61 E-value: 8.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 272 KLRADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQAENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKV 351
Cdd:TIGR02169 202 RLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 352 E--------QLQEMLGELEAELDRQKELKLQLEKDMEDLrkehEGQMAELEKRLEKVSEKEKEAIEQLEKIQKEnKTIVK 423
Cdd:TIGR02169 282 KdlgeeeqlRVKEKIGELEAEIASLERSIAEKERELEDA----EERLAKLEAEIDKLLAEIEELEREIEEERKR-RDKLT 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 424 ENVYLSESKQVLLESEI-NLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQ----NQKLLREAQDS 498
Cdd:TIGR02169 357 EEYAELKEELEDLRAELeEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEladlNAAIAGIEAKI 436
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71990528 499 AELLEEVQKGKREIDHLRQQL----AHQSSEAGSVGQLQQKLAESEHREYLLQLELERVMKMERDLDGRIEGYIRSE 571
Cdd:TIGR02169 437 NELEEEKEDKALEIKKQEWKLeqlaADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVE 513
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
245-627 |
8.56e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 8.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 245 IGKKKSDLENRLfdyEKLKAQFEQdenKLRAD-------LEKKLKTSQEKLVKYEGKIEELQSRlnkkRKELEEVQAENR 317
Cdd:PRK02224 178 VERVLSDQRGSL---DQLKAQIEE---KEEKDlherlngLESELAELDEEIERYEEQREQARET----RDEADEVLEEHE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 318 KLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDR---QKELKLQLEKDMEDLRKEHEGQMAELE 394
Cdd:PRK02224 248 ERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDllaEAGLDDADAEAVEARREELEDRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 395 KRLEKVSEKEKEAIEQLEKIQKENKTivkenvyLSESKQVLLESEINLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRR 474
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADD-------LEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 475 KKQDADVTRLDEQNQKLLREAQDSAELLEEVQKGKREIDHLRQQlAHQSSEAGSVGQLQQKLAESEHREYL--------- 545
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEE-AEALLEAGKCPECGQPVEGSPHVETIeedrervee 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 546 LQLELERVMKMERDLDGRIEgyiRSEAA--ANNELERLR-------KDTAEQKEKLEAMEMEARSKDLELADLTRKLAKA 616
Cdd:PRK02224 480 LEAELEDLEEEVEEVEERLE---RAEDLveAEDRIERLEerredleELIAERRETIEEKRERAEELRERAAELEAEAEEK 556
|
410
....*....|.
gi 71990528 617 REEHETFEINA 627
Cdd:PRK02224 557 REAAAEAEEEA 567
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
307-998 |
1.06e-07 |
|
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: 56.13 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 307 KELEEVQAENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQEmlgELEAELDRQKELKLQLEKDMEDLRKEH 386
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEK---LELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 387 EGQMAELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENVYLSESKQVLLESEINLKNELDEMAV----KLRNSQHQVAG 462
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVddeeKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 463 LNEKISEEKRRRKKQDADVTRLDEQNQKLLREAQDSAELLEEVQKGKREIDHLRQQLAHQSSEAGSVGQLQQKLAESEHR 542
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 543 EYLLQLELERVMKMERDLDGRIEGYIRSEAAANNELERLRKDTAEQKEKLEAMEMEARSKDLELADLTRKLAKAREEHET 622
Cdd:pfam02463 406 EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 623 FEINARNQFYAVTGQMHEDIESYKQRLLELEPYPGKIISGSFrdFPSQTDPSPATTDAWMQTDVEEQLMVSPEVSLVSEA 702
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISA--HGRLGDLGVAVENYKVAISTAVIVEVSATADEVEER 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 703 PSSLQDSRRSSHLDEKLRRTIEKIGELLAEHESFQESLRDPEFHTAEAFRKISQLLKSILSGANSEEMLERIWTWLTLKT 782
Cdd:pfam02463 564 QKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKA 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 783 KALVEQQDEQMKKVQKAGEMLLSQLREKESDNEVLTKKSLEMEAAAEEFRTYYNDMLTENDELR----------HRIVQL 852
Cdd:pfam02463 644 KESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRekeelkklklEAEELL 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 853 DEIREVESSNSTKIEKGLREQLEQAQHELEKKKREYMWKLQQKDEFYEIMDRNVKETEKENKRLLRKRTEDKERMDDFML 932
Cdd:pfam02463 724 ADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL 803
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71990528 933 NIRKAQEQWKYLRMRNCQRHTSMMNMLESVKKKKHESRDMNWLLQRFEDSIRKYGVAELTTEEILE 998
Cdd:pfam02463 804 RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELL 869
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
234-606 |
1.18e-07 |
|
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: 55.89 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 234 EVDQLHSEIEVIGKKKsdlENRLFDYEKLKAQFEQDENKLRADLEKKLKTsqeklvkYEGKIEELQSRLNKKRKELEEVQ 313
Cdd:pfam15921 293 QANSIQSQLEIIQEQA---RNQNSMYMRQLSDLESTVSQLRSELREAKRM-------YEDKIEELEKQLVLANSELTEAR 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 314 AENRKLLEDKNTHDFEL-----DEAKVQGE-HLEK-QRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEH 386
Cdd:pfam15921 363 TERDQFSQESGNLDDQLqkllaDLHKREKElSLEKeQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEC 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 387 EGQMaelEKRLEKVSEKEkeaiEQLEKIQKENKTIvkenvylsESKQVLLESEINlknELDEMAVKLRNSQHQVAGLNEK 466
Cdd:pfam15921 443 QGQM---ERQMAAIQGKN----ESLEKVSSLTAQL--------ESTKEMLRKVVE---ELTAKKMTLESSERTVSDLTAS 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 467 ISEEKRRRKKQDADVTRLDEQNQKLLREAQDSAELLEEVQKGKREIDHLRQQLAHQSseagsvgqlqqKLAEsehreyLL 546
Cdd:pfam15921 505 LQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKD-----------KVIE------IL 567
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71990528 547 QLELERVMKMERDlDGRIEGYIRSEAAA------NNELERLRKDTAEQKEKLEAMEMEARSKDLEL 606
Cdd:pfam15921 568 RQQIENMTQLVGQ-HGRTAGAMQVEKAQlekeinDRRLELQEFKILKDKKDAKIRELEARVSDLEL 632
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
259-998 |
1.43e-07 |
|
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: 55.75 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 259 YEKLKAQFEQDENKLRADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQAENRKLLEDKNTHDFELDEAKVQGE 338
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 339 HLEKQRKE---AWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEH----------EGQMAELEKRLEKVSEKEK 405
Cdd:pfam02463 252 EIESSKQEiekEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELlklerrkvddEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 406 EAIEQLEKIQKENKTIVK---ENVYLSESKQVLLESEINLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVT 482
Cdd:pfam02463 332 KEKEEIEELEKELKELEIkreAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 483 RLDEQNQKLLREAQDSAELLEEVQKGKREID--HLRQQLAHQSSEAGSVGQLQQKLAESEHREYLLQLELERVMKMERDL 560
Cdd:pfam02463 412 ELARQLEDLLKEEKKEELEILEEEEESIELKqgKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLS 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 561 DGRIEGYIRSEAAANNELERLRKdTAEQKEKLEAMEMEARSKDLELADLTRKLAK-------------AREEHETFEINA 627
Cdd:pfam02463 492 RQKLEERSQKESKARSGLKVLLA-LIKDGVGGRIISAHGRLGDLGVAVENYKVAIstavivevsatadEVEERQKLVRAL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 628 RNQFYAVTGQMHEDIESYKQRLLELEPYPGKIISGSFRDFPSQTDPSPATTDAWMQTDVEEQLMVSPEVSLVSEAPSSLQ 707
Cdd:pfam02463 571 TELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRK 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 708 DSRRSSHLDEKLRRTIE-----KIGELLAEHESFQESLRDPEFHTAEAFRKISQLLKSILSGANSEEMLERIWTWLTLKT 782
Cdd:pfam02463 651 GVSLEEGLAEKSEVKASlseltKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEA 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 783 KALVEQQDEQMKKVQKAGEMLLSQLREKESDNEVLTKKSLEMEAAAEEFRTYYNDMLTENDELRHRIVQLDEIREVESSN 862
Cdd:pfam02463 731 QDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEEL 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 863 STKIEKGLREQLEQAQHELEK----KKREYMWKLQQKDEFYEIMDRNVKETEKENKRLLRKRTEDKERMDDFMLNIRKAQ 938
Cdd:pfam02463 811 KEEAELLEEEQLLIEQEEKIKeeelEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELES 890
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71990528 939 EQWKYLRMRN--CQRHTSMMNMLESVKKKKHESRDMNWLLQRFEDSIRKYGVAELTTEEILE 998
Cdd:pfam02463 891 KEEKEKEEKKelEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEE 952
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
264-653 |
2.49e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.96 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 264 AQFEQDENKLRADLEKKLKTSQEKLVKyEGKIEELQSRLNKKRKELEEvQAENRKLLEDknthdfELDEAKvqgEHLEKQ 343
Cdd:PRK04863 272 ADYMRHANERRVHLEEALELRRELYTS-RRQLAAEQYRLVEMARELAE-LNEAESDLEQ------DYQAAS---DHLNLV 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 344 RK--EAWEKVEQLQEMLGELEAELDRQKELklqlekdmedlRKEHEGQMAELEKRLEKVSEKEKEAIEQLEKIQK----- 416
Cdd:PRK04863 341 QTalRQQEKIERYQADLEELEERLEEQNEV-----------VEEADEQQEENEARAEAAEEEVDELKSQLADYQQaldvq 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 417 ENKTIVKENVY--LSESKQVLLESEINLKNeLDEMAVKLRNSQHQVAglnEKISEEKRRRKKQDADVTRLdEQNQKLLRE 494
Cdd:PRK04863 410 QTRAIQYQQAVqaLERAKQLCGLPDLTADN-AEDWLEEFQAKEQEAT---EELLSLEQKLSVAQAAHSQF-EQAYQLVRK 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 495 AQDSAELLEEVQKGKREIDHLRQQLAHqsseAGSVGQLQQKLAESEhREYLLQLELERvmkMERDLDGRIEGYIRSEAAA 574
Cdd:PRK04863 485 IAGEVSRSEAWDVARELLRRLREQRHL----AEQLQQLRMRLSELE-QRLRQQQRAER---LLAEFCKRLGKNLDDEDEL 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 575 NN---ELERLRKDTAEQKEKLEAMEMEARSKDLELADLTRKLAKAREEHETFEiNARNQFYAVTGQMHED---IESYKQR 648
Cdd:PRK04863 557 EQlqeELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQ-DALARLREQSGEEFEDsqdVTEYMQQ 635
|
....*
gi 71990528 649 LLELE 653
Cdd:PRK04863 636 LLERE 640
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
294-948 |
2.72e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 294 KIEELQSRLNKKRKELEEVQAENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEA--WEKVEQLQEMLGELEAEL----DR 367
Cdd:PTZ00121 1189 KAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAkkAEEERNNEEIRKFEEARMahfaRR 1268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 368 QKELKLQLEKDMEDLRKEHEGQMAELEKRLEKVSE--------KEKEAIEQLEKIQKENKTIVKENVYLSESKQVLLESE 439
Cdd:PTZ00121 1269 QAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKadeakkkaEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAA 1348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 440 inlKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRK--KQDADVTRLDEQNQKLLREAQDSAELLEEVQKGKREIDHLRQ 517
Cdd:PTZ00121 1349 ---KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADaaKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKK 1425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 518 ---------QLAHQSSEAGSVGQLQQKLAESEHREYLLQLELERvmKMERDLDGRIEGYIRSEAA------ANNELERLR 582
Cdd:PTZ00121 1426 kaeekkkadEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA--KKADEAKKKAEEAKKADEAkkkaeeAKKKADEAK 1503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 583 KDTAEQKEKLEAMEMEARSKdlelADLTRKLAKAREEHETFEINARNQFYAVTgQMHEDIESYKQRLLELEPYPGKIISG 662
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKK----ADEAKKAEEAKKADEAKKAEEKKKADELK-KAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 663 SFRDFPSQTDPSPATTDAWMQTDVEEQLMVSPEVSLVSEAPSSLQDSRRSSHLDEKLRRTIEKIGELLAEHESFQESLRD 742
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 743 PEFHTAEAFRKISQLLKSILSGANSEEmlERIWTWLTLKTKALVEQQDEQMKKVQKAGEMLLSQLREKESDN----EVLT 818
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEE--DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENkikaEEAK 1736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 819 KKSLEMEAAAEEFRTyyndmlteNDELRHRIVQLDEIREVESSNSTK-----IEKGLREQLEQAQHELEKKKREYmwklq 893
Cdd:PTZ00121 1737 KEAEEDKKKAEEAKK--------DEEEKKKIAHLKKEEEKKAEEIRKekeavIEEELDEEDEKRRMEVDKKIKDI----- 1803
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 71990528 894 qKDEFYEIMDRNVKETEKENKRLLRKRTEDKERMDDFMLNIRKAQEQWKYLRMRN 948
Cdd:PTZ00121 1804 -FDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKN 1857
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
234-836 |
3.40e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 234 EVDQLHSEIEVIGKKKSDLENRLFDYEKLKAQFEQDENKLRaDLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQ 313
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEIS-SELPELREELEKLEKEVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 314 AENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAwEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEHEGqmaeL 393
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING----I 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 394 EKRLEKVSEKEKEaieqLEKIQKENKTIVKENVYLSESKQvLLESEINLKNELDEMavKLRNSQHQVAGLNEKISEEKRR 473
Cdd:PRK03918 327 EERIKELEEKEER----LEELKKKLKELEKRLEELEERHE-LYEEAKAKKEELERL--KKRLTGLTPEKLEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 474 RKKQDADVTRLDEQNQKLLREAQDSAELLEEVQKGK-------REID--HLRQQLAHQSSEAGSVGQLQQKLAESEHREY 544
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgRELTeeHRKELLEEYTAELKRIEKELKEIEEKERKLR 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 545 LLQLELERVMKMERDLDGRIEGYIRSEAAANN-------ELERLRKDTAEQKEKLEAMEMEARS--KDLE-LADLTRKLA 614
Cdd:PRK03918 480 KELRELEKVLKKESELIKLKELAEQLKELEEKlkkynleELEKKAEEYEKLKEKLIKLKGEIKSlkKELEkLEELKKKLA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 615 KAREEHETFEINARNQFYAVTGQMHEDIESYKQRLLELEPYPGKIIsgsfrdfpsqtdpspattdawmqtdveeqlmvsp 694
Cdd:PRK03918 560 ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYL---------------------------------- 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 695 evslvsEAPSSLQDSRRSSHLDEKLRRTIEKIGELLAEHESFQESLRDP-----EFHTAEAFRKISQLLKSilsgansee 769
Cdd:PRK03918 606 ------ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEleeleKKYSEEEYEELREEYLE--------- 670
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71990528 770 mLERIWTWLTLKTKALVEQQDEQMKKVQKAGEMlLSQLREKESDNEVLTKKSLEMEAAAEEFRTYYN 836
Cdd:PRK03918 671 -LSRELAGLRAELEELEKRREEIKKTLEKLKEE-LEEREKAKKELEKLEKALERVEELREKVKKYKA 735
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
305-596 |
4.30e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 305 KRKELEEVQAENRKLLEDKNthdfELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAEL----DRQKELKLQLEKDME 380
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKR----ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIeqleQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 381 DLRK------EHEGQMAELEKRLEKVSE---KEKEAIEQLE------KIQKENKTIVKENVYLSESKQVLLESEINLKNE 445
Cdd:TIGR02169 745 DLSSleqeieNVKSELKELEARIEELEEdlhKLEEALNDLEarlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 446 LDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQNQKLLREAQDSAELLEEVQKGKREIDHLRQQLAHQSSE 525
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71990528 526 agsVGQLQQKLAESEHREYLLQLELERVMKMERDLDgRIEGYIRSEAAANNELERLRKDTAEQKEKLEAME 596
Cdd:TIGR02169 905 ---IEELEAQIEKKRKRLSELKAKLEALEEELSEIE-DPKGEDEEIPEEELSLEDVQAELQRVEEEIRALE 971
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
293-624 |
5.11e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 293 GKIEELQSRLNKKRKELEEVQAENRKLLEDK----------------NTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQE 356
Cdd:PRK02224 162 GKLEEYRERASDARLGVERVLSDQRGSLDQLkaqieekeekdlherlNGLESELAELDEEIERYEEQREQARETRDEADE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 357 MLGELEaelDRQKELKlQLEKDMEDLRKEhegqMAELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENVYLSESKQVLL 436
Cdd:PRK02224 242 VLEEHE---ERREELE-TLEAEIEDLRET----IAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 437 ESEINLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQNQKLLREAQDSAellEEVQKGKREIDHLR 516
Cdd:PRK02224 314 ARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAR---EAVEDRREEIEELE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 517 QQLAhqsSEAGSVGQLQQKLAESEHREYLLQLELERVMKMERDLdgriEGYIRSEAAANNELERLRKD----TAEQKEKL 592
Cdd:PRK02224 391 EEIE---ELRERFGDAPVDLGNAEDFLEELREERDELREREAEL----EATLRTARERVEEAEALLEAgkcpECGQPVEG 463
|
330 340 350
....*....|....*....|....*....|..
gi 71990528 593 EAMEMEARSKDLELADLTRKLAKAREEHETFE 624
Cdd:PRK02224 464 SPHVETIEEDRERVEELEAELEDLEEEVEEVE 495
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
342-630 |
5.51e-07 |
|
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: 53.91 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 342 KQRKEAWEKVEQLQEMLGELE---AELDRQKE-LKLQLEK-----DMEDLRKEHE-----GQMAELEKRLEKVSEKEKEA 407
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEdilNELERQLKsLERQAEKaerykELKAELRELElallvLRLEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 408 IEQLEKIQKENKTivkenvylSESKQVLLESEIN-LKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDE 486
Cdd:TIGR02168 252 EEELEELTAELQE--------LEEKLEELRLEVSeLEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 487 QNQKLLREAQDSAELLEEVQKgkrEIDHLRQQLAhqsSEAGSVGQLQQKLAESEHREYLLQLELERVMKMERDLDgrieg 566
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEE---KLEELKEELE---SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE----- 392
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71990528 567 yiRSEAAANNELERLRKD----------TAEQKEKLEAMEMEARSKDL--ELADLTRKLAKAREEHETFEINARNQ 630
Cdd:TIGR02168 393 --LQIASLNNEIERLEARlerledrrerLQQEIEELLKKLEEAELKELqaELEELEEELEELQEELERLEEALEEL 466
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
237-651 |
6.25e-07 |
|
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: 53.58 E-value: 6.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 237 QLHSEIEVIGKKKSDLENrlfdYEKLKAQFEQDENKLRADLEKkLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQAEN 316
Cdd:pfam15921 445 QMERQMAAIQGKNESLEK----VSSLTAQLESTKEMLRKVVEE-LTAKKMTLESSERTVSDLTASLQEKERAIEATNAEI 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 317 RKLLEDKNTHDFELDEAKVQGEHLEKQRKEA-----------------WEKVEQLQEMLGELEAELDRQKELKLQLEKDM 379
Cdd:pfam15921 520 TKLRSRVDLKLQELQHLKNEGDHLRNVQTECealklqmaekdkvieilRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEI 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 380 EDLRKEHEGQMAELEKRLEKVSEKEKEAIE-QLEKIQkenktivkenvyLSESKQVLLESEINLKNELDEMAVKLRNSQH 458
Cdd:pfam15921 600 NDRRLELQEFKILKDKKDAKIRELEARVSDlELEKVK------------LVNAGSERLRAVKDIKQERDQLLNEVKTSRN 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 459 QVAGLNEKISEEKRRRKKQDADVTRLDEQNQKLLREAQDSAELLEEVQKGKREIDHLRQQLA-----HQSSEAGSVGQLQ 533
Cdd:pfam15921 668 ELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAmgmqkQITAKRGQIDALQ 747
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 534 QKLAESEHREYLLQLELERVMKMERDLDGRIEGYIRSEAAANNELERLRKDTAEQKEKLEAMEMEARSKDLELADLTRKL 613
Cdd:pfam15921 748 SKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDII 827
|
410 420 430
....*....|....*....|....*....|....*...
gi 71990528 614 AKAREEHETFEINARNQFYAVTGQMHEDIESYKQRLLE 651
Cdd:pfam15921 828 QRQEQESVRLKLQHTLDVKELQGPGYTSNSSMKPRLLQ 865
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
229-421 |
6.38e-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: 52.84 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 229 ANLQIEVDQLHSEIEVIGKKKSDLENRLFDYEKLKAQFEQDENKLRADLEKKlktsqeklvkyEGKIEELQSRLNKKRKE 308
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL-----------EKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 309 LEEVQAENRK---------LLEDKNTHDFELDEAKVQgeHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDM 379
Cdd:COG4942 106 LAELLRALYRlgrqpplalLLSPEDFLDAVRRLQYLK--YLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 71990528 380 EDLRKEHEGQMAELEKRLEKVSEKEKEAIEQLEKIQKENKTI 421
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
294-926 |
6.82e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 6.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 294 KIEELQSRLNKKRKELEEVQAENRKLLEDKNTHDFELDEAKVQGEHLEK-QRKEAWEKVEQLQEMLGELEAELDRQKELK 372
Cdd:PTZ00121 1165 KAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKaEEARKAEDAKKAEAVKKAEEAKKDAEEAKK 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 373 LQLEKDMEDLRKEHEGQMAELEKRLEKVSEKEKEAIEQLEKIQKenktiVKENVYLSESKQVLLESEINLKNELDEMAVK 452
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE-----KKKADEAKKAEEKKKADEAKKKAEEAKKADE 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 453 LRNSQHQVAGLNEKIsEEKRRRKKQDADVTRLDEQNQKllREAQDSAELLEEVQKGKREIDHLRQQLAHQSSEAGSVGQL 532
Cdd:PTZ00121 1320 AKKKAEEAKKKADAA-KKKAEEAKKAAEAAKAEAEAAA--DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEA 1396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 533 QQKLAESEHREYLLQLELERVMKMErDLDGRIEGYIRSEAAANNELERLRKDTAEQK--EKLEAMEMEARSKDLELADLT 610
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKKADEAKKKAEEAKKADEAKKKaeEAKKAEEAKKKAEEAKKADEA 1475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 611 RKlaKAREEHETFEINARNQFYAVTGQMHEDIESYKQRLLELEPYPGKIISGSFRDFPSQTDPSPATTDAWMQTDVE--- 687
Cdd:PTZ00121 1476 KK--KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADElkk 1553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 688 -EQLMVSPEVSLVSEAPSSLQDSRRSSHLDEKLRRTIEKIGELLAEHESFQESLRDPEFHTAEAFRKISQLLKsilsgan 766
Cdd:PTZ00121 1554 aEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK------- 1626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 767 sEEMLERIWTWLTLKTKALVEQQDEQMKKVQKAGEMLLSQLREKESDNEvltKKSLEMEAAAEEFRTYYNDMLTENDELR 846
Cdd:PTZ00121 1627 -KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK---KKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 847 ----------HRIVQLDEIREVESSNSTKIEKGLRE------QLEQAQHELEKKKREYMWKLQQKDEFYEIMDRNVKETE 910
Cdd:PTZ00121 1703 kaeelkkkeaEEKKKAEELKKAEEENKIKAEEAKKEaeedkkKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
650
....*....|....*.
gi 71990528 911 KENKRLLRKRTEDKER 926
Cdd:PTZ00121 1783 EELDEEDEKRRMEVDK 1798
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
444-630 |
1.01e-06 |
|
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: 52.07 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 444 NELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQ---NQKLLREAQDSAELLE-EVQKGKREIDHLRQQL 519
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiaaLARRIRALEQELAALEaELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 520 AHQSSEAGSVGQLQQKLAESEHREYLLQ----LELERVMKMERDLDGRIEGYIRSEAAANNELERLRKDTAEQKEKLEAM 595
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSpedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190
....*....|....*....|....*....|....*
gi 71990528 596 EMEARSKDLELADLTRKLAKAREEHETFEINARNQ 630
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
349-652 |
1.04e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 349 EKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEhegqmAELEKRLEKVSEKEKEAIEQLEKIQKenktivkenvyl 428
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQER-----REALQRLAEYSWDEIDVASAEREIAE------------ 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 429 seskqvlLESEInlkNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQNQKLLREAQDSAELLEEVQKG 508
Cdd:COG4913 673 -------LEAEL---ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 509 KREidHLRQQLAhqsseagsvgqlqqklaesEHREYLLQLELERvmKMERDLDGRIEGYIRSEAAANNELERLRK----- 583
Cdd:COG4913 743 ARL--ELRALLE-------------------ERFAAALGDAVER--ELRENLEERIDALRARLNRAEEELERAMRafnre 799
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71990528 584 ---DTAEQKEKLEAMEM-EARSKDLELADLTRKLAKAREEHETFEINARNQFYAvtgQMHEDIESYKQRLLEL 652
Cdd:COG4913 800 wpaETADLDADLESLPEyLALLDRLEEDGLPEYEERFKELLNENSIEFVADLLS---KLRRAIREIKERIDPL 869
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
368-602 |
1.08e-06 |
|
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: 52.07 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 368 QKELKLQLEKDMEDLRKehegQMAELEKRLEKVSEKEKEAIEQLEKIQKEnktivkenvyLSESKQVLLEseinLKNELD 447
Cdd:COG4942 18 QADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERR----------IAALARRIRA----LEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 448 EMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQNQ-KLLREAQDSA-----------------ELLEEVQKGK 509
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlALLLSPEDFLdavrrlqylkylaparrEQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 510 REIDHLRQQLAHQSSeagsvgQLQQKLAESEHReyllQLELERVMKMERDLDGRIEGYIRSEAAANNELERLRKDTAEQK 589
Cdd:COG4942 160 AELAALRAELEAERA------ELEALLAELEEE----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|...
gi 71990528 590 EKLEAMEMEARSK 602
Cdd:COG4942 230 ARLEAEAAAAAER 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
333-549 |
1.43e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 333 AKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEhegqMAELEKRLEKVSEKEKEAIEQLE 412
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE----IDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 413 KIQKENKTIVKENVYLSeskqVLLESEiNLKNELDEMAVKLRNSQHQvaglNEKISEEKRRRKKQDADVTRLDEQNQKLL 492
Cdd:COG3883 90 ERARALYRSGGSVSYLD----VLLGSE-SFSDFLDRLSALSKIADAD----ADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 71990528 493 REAQDSAELLEEVQKGKREIDHLRQQL-AHQSSEAGSVGQLQQKLAESEHREYLLQLE 549
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLsAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
237-620 |
1.71e-06 |
|
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: 52.36 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 237 QLHSEIEVIGKKKSDLENRLFDYEKLKAQFEQDENKLRADLEKKlktsQEKLVKYEGKI------EELQSRLNKKRKELE 310
Cdd:TIGR00606 574 QLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESK----EEQLSSYEDKLfdvcgsQDEESDLERLKEEIE 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 311 EVQAENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEHEGQM 390
Cdd:TIGR00606 650 KSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEML 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 391 AELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENVYLSESKQVL--LESEINLKNELDEMAVKLRNSQHQVAGLNEKIS 468
Cdd:TIGR00606 730 GLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLgtIMPEEESAKVCLTDVTIMERFQMELKDVERKIA 809
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 469 EEKRRRKKQDADVT------RLDEQNQKLLREAQDSAELLEEVQKGKREIDHLRQQLAHQSSEAGSVGQ-LQQKLAESEH 541
Cdd:TIGR00606 810 QQAAKLQGSDLDRTvqqvnqEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTnLQRRQQFEEQ 889
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 542 REYLLQ--LELERVMKMERDLDGRIEGYIRSEAAANNELERLRKDTAEQKE-KLEAMEMEARSKDLELADLTRKLAKARE 618
Cdd:TIGR00606 890 LVELSTevQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQdKVNDIKEKVKNIHGYMKDIENKIQDGKD 969
|
..
gi 71990528 619 EH 620
Cdd:TIGR00606 970 DY 971
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
329-534 |
2.70e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 329 ELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEHEGQMAELEKRLEKVSEKEKEA- 407
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVs 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 408 -----------------IEQLEKIQKENKTIVKEnvyLSESKQVLLESEINLKNELDEMAVKLRNSQHQVAGLNEKISEE 470
Cdd:COG3883 104 yldvllgsesfsdfldrLSALSKIADADADLLEE---LKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71990528 471 KRRRKKQDADVTRLDEQNQKLLREAQDSAELLEEVQKGKREIDHLRQQLAHQSSEAGSVGQLQQ 534
Cdd:COG3883 181 EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
375-623 |
3.16e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 375 LEKDMEDLRKEHEGQMAELEKRLEKVSEKEKEAIEQLEKIQKENKTIVkenvyLSESKQVLLESEINLKNELDEMAVKLR 454
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 455 NSQHQVAGLNEKISeekrrrkkqdadvtrLDEQNQKLLREAQDSAELLEEVQKGKREIDHLRQQLAHQSSEagsVGQLQQ 534
Cdd:COG3206 237 EAEARLAALRAQLG---------------SGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPD---VIALRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 535 KLAESEHReylLQLELERVMkmeRDLDGRIEGYIRSEAAANNELERLRKDTAEQKEKLeamemearskdLELADLTRKLA 614
Cdd:COG3206 299 QIAALRAQ---LQQEAQRIL---ASLEAELEALQAREASLQAQLAQLEARLAELPELE-----------AELRRLEREVE 361
|
....*....
gi 71990528 615 KAREEHETF 623
Cdd:COG3206 362 VARELYESL 370
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
250-628 |
3.41e-06 |
|
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: 51.33 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 250 SDLENRLFDYEKLKaqfeQDENKLRADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQAENRKLLEDKNTHDFE 329
Cdd:pfam01576 190 SDLEERLKKEEKGR----QELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKK 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 330 LDEAKVQGEHL--------------EKQRKEAWEKVEQLQemlGELEAELDR---QKELKLQ-------LEKDMEDLRKE 385
Cdd:pfam01576 266 IRELEAQISELqedleseraarnkaEKQRRDLGEELEALK---TELEDTLDTtaaQQELRSKreqevteLKKALEEETRS 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 386 HEGQMAELEKRLEKVSEKEKEAIEQ-------LEK----IQKENKTIVKENVYLSESKQVLLESEINLKNELDEMAVKLR 454
Cdd:pfam01576 343 HEAQLQEMRQKHTQALEELTEQLEQakrnkanLEKakqaLESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLS 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 455 NSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQNQKLLREA-------QDSAELLEEVQKGKREIDH-----------LR 516
Cdd:pfam01576 423 ESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVsslesqlQDTQELLQEETRQKLNLSTrlrqledernsLQ 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 517 QQLAHQSSEAGSVGQ----LQQKLAESEHR--EYLLQLEL--ERVMKMERDLDGRIEGYIRSEAAAN----------NEL 578
Cdd:pfam01576 503 EQLEEEEEAKRNVERqlstLQAQLSDMKKKleEDAGTLEAleEGKKRLQRELEALTQQLEEKAAAYDklektknrlqQEL 582
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 71990528 579 ERLRKDTAEQKEKLEAMEMEARSKDLELADLTRKLAKAREEHETFEINAR 628
Cdd:pfam01576 583 DDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAR 632
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
234-424 |
3.54e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 234 EVDQLHSEIEVIGKKKSDLENRLFDYEKLKAQFEQDE--NKLRADL-----EKKLKTSQEKLVKYEGKIEELQSRLNKKR 306
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIRELAERYAAARERLAelEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 307 KELEEVQAENRKLLEDKNTHDFE-LDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDrqkelklQLEKDMEDLRKE 385
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLP-------ASAEEFAALRAE 388
|
170 180 190
....*....|....*....|....*....|....*....
gi 71990528 386 HEGQMAELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKE 424
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
292-514 |
5.76e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 292 EGKIEELQSRLNKKRKELEEVQAENRKLLEdknthdfELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKEl 371
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQA-------ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 372 klQLEKDMEDLRKEhEGQMAELE---------------KRLEKVSEKEKEAIEQLEKIQKEnktivkenvyLSESKQVLL 436
Cdd:COG3883 87 --ELGERARALYRS-GGSVSYLDvllgsesfsdfldrlSALSKIADADADLLEELKADKAE----------LEAKKAELE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71990528 437 ESEINLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQNQKLLREAQDSAELLEEVQKGKREIDH 514
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
349-613 |
7.07e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 7.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 349 EKVEQLQEMLGELEAELDRQKELK---LQLEKDMEDLRKEHEGQMAELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKEN 425
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLekfIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 426 VYLSESKQVLLESEINLKneldEMAVKLRNSQHQVAGLNEKISEEKRRRKKQdadvtrldeqnQKLLREAQDSAELLEEV 505
Cdd:PRK03918 238 EEIEELEKELESLEGSKR----KLEEKIRELEERIEELKKEIEELEEKVKEL-----------KELKEKAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 506 QKGKREIDHLRQQLAHQSSEAGSVGQLQQKLAESEHREYLLQLELERVMKMERDLDGRIEGYIRSEAAANNeLERLRKD- 584
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE-LERLKKRl 381
|
250 260
....*....|....*....|....*....
gi 71990528 585 TAEQKEKLEAMEMEARSKDLELADLTRKL 613
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKI 410
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
257-942 |
7.27e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 257 FDYEKLKAQFEQDENKLRADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQAEN-RKLLEDKNTHDFELDEAKV 335
Cdd:PTZ00121 1079 FDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDaRKAEEARKAEDAKRVEIAR 1158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 336 QGEhlEKQRKEAWEKVEQLQEMLGELEAELDRQKElklQLEKdMEDLRKEHEGQMAELEKRLEKVSEKEKEA-IEQLEKI 414
Cdd:PTZ00121 1159 KAE--DARKAEEARKAEDAKKAEAARKAEEVRKAE---ELRK-AEDARKAEAARKAEEERKAEEARKAEDAKkAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 415 QKenktiVKENVYLSESKQVLLESEINLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQNQKL--L 492
Cdd:PTZ00121 1233 EE-----AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAdeA 1307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 493 REAQDSAELLEEVQKGKREIDHLRQQLAHQSSEAGSVGQLQQKLAESEHREYLLQLELERVMKMERDLDGRIEGYIRSEA 572
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA 1387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 573 AANNELERLRKDTAEQKEKLEAMEMEARSKdlELADLTRKLAKAREEHETFEINARNQFYAVTGQMHEDiESYKQRLLEL 652
Cdd:PTZ00121 1388 EEKKKADEAKKKAEEDKKKADELKKAAAAK--KKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE-EAKKAEEAKK 1464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 653 EPYPGKIISGSFRDFPSQTDPSPATTDAWMQTDVEEQLMVSPEVSLVSEAPSSLQDSRRSshldEKLRRTIEKigELLAE 732
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA----DEAKKAEEA--KKADE 1538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 733 HESFQESLRDPEFHTAEAFRKISQLLKSILSGANSEEmleriwtwltlktKALVEQQDEQMKKVQKAGEMLLSQLREKES 812
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED-------------KNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 813 DNEV-LTKKSLEMEAAAEEFRtyyndmltENDELRHRIVQL-----DEIREVESSNSTKIEKGLREQLEQAQHELEKKKR 886
Cdd:PTZ00121 1606 KMKAeEAKKAEEAKIKAEELK--------KAEEEKKKVEQLkkkeaEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 71990528 887 EYMWKLQQKDEFYEIMDRNVKETEKENKRLLRKRTEDKERMDDfmlnIRKAQEQWK 942
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE----LKKAEEENK 1729
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
86-624 |
8.24e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 86 EASKELKKKDRANSLLRDQNESLRGENESLREENCSLREESRRMDLVDKENvipviprlvfdekpdldpitvKSSEQIKK 165
Cdd:PRK03918 197 EKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKEL---------------------ESLEGSKR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 166 ELLSFIKNDEDRtIMEAKMEnmlISDSKppakvftatatiqvDTEKMDANIQTDKDDHVnvvnaNLQIEVDQLHSEIEVI 245
Cdd:PRK03918 256 KLEEKIRELEER-IEELKKE---IEELE--------------EKVKELKELKEKAEEYI-----KLSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 246 GKKKSDLENRLFDYEKLKAQFEQDENKLRaDLEKKLKTSQEKLVKYEGKIEELQsRLNKKRKELEEVQAENRklledknt 325
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLT-------- 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 326 hDFELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDM-------EDLRKEHEGQ-MAELEKRL 397
Cdd:PRK03918 383 -GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgRELTEEHRKElLEEYTAEL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 398 EKVSEKEKEAIEQLEKIQKENKTIvkENVYLSESKQVLLEseinlkneldEMAVKLRNSQHQVAGLN-EKISEEKRRRKK 476
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELREL--EKVLKKESELIKLK----------ELAEQLKELEEKLKKYNlEELEKKAEEYEK 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 477 QDADVTRLDEQNQKLLREAQDSAEL---LEEVQKGKREIDHLRQQLAHQSSEAG--SVGQLQQKLAESE--HREYL---- 545
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEKLEELkkkLAELEKKLDELEEELAELLKELEELGfeSVEELEERLKELEpfYNEYLelkd 609
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71990528 546 LQLELERVMKMERDLDGRIEGYIRSEAAANNELERLRKDTAEQKEKLEamEMEARSKDLELADLTRKLAKAREEHETFE 624
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAELEELE 686
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
282-598 |
1.00e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.74 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 282 KTSQEKLVKYEgkieelQSRLNKKRKELEEVQAENRKLLEDKNTHDFELD-EAKVQGEHlEKQRKEAWEKVEQLQEMLGE 360
Cdd:pfam17380 287 RQQQEKFEKME------QERLRQEKEEKAREVERRRKLEEAEKARQAEMDrQAAIYAEQ-ERMAMERERELERIRQEERK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 361 LEAELDRQKELKLQLEK--DMEDLRKEHEGQMAELEKRLE---KVSEKEKEAIEQLEKIQKENKTIVKENVYLSESKQVL 435
Cdd:pfam17380 360 RELERIRQEEIAMEISRmrELERLQMERQQKNERVRQELEaarKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 436 LESEinLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRR---KKQDADVTRLDEQNQKLLREAqdsaelLEEVQKGKREI 512
Cdd:pfam17380 440 LEEE--RAREMERVRLEEQERQQQVERLRQQEEERKRKKlelEKEKRDRKRAEEQRRKILEKE------LEERKQAMIEE 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 513 DHLRQQLAHQSSEAgsvgqlQQKLAESEHREyllQLELERVMKMERDLDGRIEgyirseaaannelERLRKDTaEQKEKL 592
Cdd:pfam17380 512 ERKRKLLEKEMEER------QKAIYEEERRR---EAEEERRKQQEMEERRRIQ-------------EQMRKAT-EERSRL 568
|
....*.
gi 71990528 593 EAMEME 598
Cdd:pfam17380 569 EAMERE 574
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
260-554 |
1.01e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.74 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 260 EKLKAQFEQDENKL--RADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQAENRKL-LEDKNTHDFELDEAKVQ 336
Cdd:pfam17380 299 ERLRQEKEEKAREVerRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKReLERIRQEEIAMEISRMR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 337 G-EHLEKQRKEAWEKVEQLQEMLGELE-AELDRQKELKLQLeKDMEDLRKEHEGQMAELEKRLEKVSEKEKEAIEQLEKI 414
Cdd:pfam17380 379 ElERLQMERQQKNERVRQELEAARKVKiLEEERQRKIQQQK-VEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 415 QKENKTIVKENVYLSESKQVLLESEINLKNELDEMAVKLrnSQHQVAGLNEKISEEKRRRKKQDADVtrldEQNQKLLRE 494
Cdd:pfam17380 458 RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI--LEKELEERKQAMIEEERKRKLLEKEM----EERQKAIYE 531
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 495 AQDSAELLEEVQKGKREIDHLRQQlahqsseagsvgqlQQKLAESEHREYLLQLELERVM 554
Cdd:pfam17380 532 EERRREAEEERRKQQEMEERRRIQ--------------EQMRKATEERSRLEAMEREREM 577
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
229-417 |
1.13e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 229 ANLQIEVDQLHSEIEVIGKKKSDLENRLFDYEKLKAQFEQDENKLRADLEkkLKTSQEKLvkyeGKIEELQSRLNKKRKE 308
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID--VASAEREI----AELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 309 LEEVQAENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEHEG 388
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE 766
|
170 180
....*....|....*....|....*....
gi 71990528 389 QMAELEKRLEKVSEKEKEAIEQLEKIQKE 417
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
228-600 |
1.48e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 228 NANLQIEVDQLHSEIE----VIGKKKSDLENRLFDYEKLKAQFEqDENKLRADLEKKLKTSQEKLVKYEGKIEELQSRLn 303
Cdd:PRK02224 358 AEELREEAAELESELEeareAVEDRREEIEELEEEIEELRERFG-DAPVDLGNAEDFLEELREERDELREREAELEATL- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 304 kkrKELEEVQAENRKLLEDKN-----------THDFELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELE--AELDRQKE 370
Cdd:PRK02224 436 ---RTARERVEEAEALLEAGKcpecgqpvegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEdlVEAEDRIE 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 371 LKLQLEKDMEDLRKEHEgqmAELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENVYLSESKQVLLESEINLKnELDEMA 450
Cdd:PRK02224 513 RLEERREDLEELIAERR---ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA-ELKERI 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 451 VKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQNQKLLREAQDSAELLEEVQKGKREidhlrqqlahqsseagsvg 530
Cdd:PRK02224 589 ESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIE------------------- 649
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71990528 531 QLQQKLAESEhrEYLLQLE--LERVMKMERDLDGRIeGYIRSEAAANNELERLRKDTAEQKEKLEAMEMEAR 600
Cdd:PRK02224 650 EAREDKERAE--EYLEQVEekLDELREERDDLQAEI-GAVENELEELEELRERREALENRVEALEALYDEAE 718
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
240-519 |
1.67e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.86 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 240 SEIEVIGKKKSDLENRLFDY----EKLKAQFEQDENK-LRADL---EKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEE 311
Cdd:TIGR04523 274 KELEQNNKKIKELEKQLNQLkseiSDLNNQKEQDWNKeLKSELknqEKKLEEIQNQISQNNKIISQLNEQISQLKKELTN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 312 VQAENRKLledknthDFELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEHEGQMA 391
Cdd:TIGR04523 354 SESENSEK-------QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 392 ELEKRLEKVsEKEKEAIEQLEKIQKENKTIVKENVYLSESkqvlleseinLKNELDEMAVKLRNSQHQVAGLNEKISEEK 471
Cdd:TIGR04523 427 EIERLKETI-IKNNSEIKDLTNQDSVKELIIKNLDNTRES----------LETQLKVLSRSINKIKQNLEQKQKELKSKE 495
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 71990528 472 RRRKKQDADVTRLDEQNQKLLREaqdSAELLEEVQKGKREIDHLRQQL 519
Cdd:TIGR04523 496 KELKKLNEEKKELEEKVKDLTKK---ISSLKEKIEKLESEKKEKESKI 540
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
218-469 |
1.81e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.86 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 218 TDKDDHVNVVNANLQIEVDQLHSEIEVIGKKKSDLENRLfdyEKLKAQFEQDENKLRAdLEKKLKTSQEKLVKYEGKIEE 297
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL---EQKQKELKSKEKELKK-LNEEKKELEEKVKDLTKKISS 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 298 LQSRLNKKRKELEEVQAENRKLLEDKNTHDFELDEAKVQGEHLEKQrkeawEKVEQLQEMLGELEAELDRQKELKLQLEK 377
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKN-----KEIEELKQTQKSLKKKQEEKQELIDQKEK 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 378 DMEDLRKEhegqmaeLEKRLEKVSEKEKEaieqLEKIQKENKTIVKENVYLSESKQVLLESEINLKNELDEMAVKLRNSQ 457
Cdd:TIGR04523 597 EKKDLIKE-------IEEKEKKISSLEKE----LEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEII 665
|
250
....*....|..
gi 71990528 458 HQVAGLNEKISE 469
Cdd:TIGR04523 666 KKIKESKTKIDD 677
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
283-519 |
2.03e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 283 TSQEKLVKYEGKIEELQSRLNKKRKELEEVQAenrklledknthdfELDEAKVQGEHLEKQRKEAWE--KVEQLQEMLGE 360
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEA--------------ELDALQERREALQRLAEYSWDeiDVASAEREIAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 361 LEAELDRqkelklqLEKDMEDLRkehegqmaELEKRLEKVSEKEKEAIEQLEKIQKENKTivkenvylseskqvllesei 440
Cdd:COG4913 673 LEAELER-------LDASSDDLA--------ALEEQLEELEAELEELEEELDELKGEIGR-------------------- 717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 441 nLKNELDEMAVKLRNSQHQVAGLNEKISEEKRrrkkqdadvTRLDEQNQKLL---REAQDSAELLEEVQKGKREIDHLRQ 517
Cdd:COG4913 718 -LEKELEQAEEELDELQDRLEAAEDLARLELR---------ALLEERFAAALgdaVERELRENLEERIDALRARLNRAEE 787
|
..
gi 71990528 518 QL 519
Cdd:COG4913 788 EL 789
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
284-885 |
2.63e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.58 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 284 SQEKLVKYEGKiEELQSRLNKKRKELEEVQaenRKLLEDKNTHdfeldeakvqgehlEKQRKEAWEKVEQLQEMLGELEA 363
Cdd:pfam15921 63 SPRKIIAYPGK-EHIERVLEEYSHQVKDLQ---RRLNESNELH--------------EKQKFYLRQSVIDLQTKLQEMQM 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 364 ELDRQKELKLQLEKDMEDLRKEHEGQMAELEKRL---EKVSEKEKEAIEQLEKIQKENKTIvkenvyLSESKQVLLESEI 440
Cdd:pfam15921 125 ERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKclkEDMLEDSNTQIEQLRKMMLSHEGV------LQEIRSILVDFEE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 441 NLKNELDEM----AVKLRNSQHQVAGLNEKISEEKRRRKKQdadVTRLDEQNQKLLREAQDSAELLEEVQKgkreiDHLR 516
Cdd:pfam15921 199 ASGKKIYEHdsmsTMHFRSLGSAISKILRELDTEISYLKGR---IFPVEDQLEALKSESQNKIELLLQQHQ-----DRIE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 517 QQLAHQSSEagsVGQLQQKLAESEHREYLLQLELERVMKMERDLDGRiegYIRSEAAANNELERLRKDTAEQKEKLEAmE 596
Cdd:pfam15921 271 QLISEHEVE---ITGLTEKASSARSQANSIQSQLEIIQEQARNQNSM---YMRQLSDLESTVSQLRSELREAKRMYED-K 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 597 MEARSKDLELADltRKLAKAREEHETFEINARN---QFYAVTGQMHEdiesyKQRLLELEPYPGKIIsgsfrdfpSQTDP 673
Cdd:pfam15921 344 IEELEKQLVLAN--SELTEARTERDQFSQESGNlddQLQKLLADLHK-----REKELSLEKEQNKRL--------WDRDT 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 674 SPATTDAWMQTDVEEQLMVSPEVSLVSEAPSSL---QDSRRSSHLDEKlRRTIEKIGELLAEHESFQESLRD-PEFHTAE 749
Cdd:pfam15921 409 GNSITIDHLRRELDDRNMEVQRLEALLKAMKSEcqgQMERQMAAIQGK-NESLEKVSSLTAQLESTKEMLRKvVEELTAK 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 750 AF------RKISQLLKSI------LSGANSEEMLERIWTWLTLKTKALVEQQDEQMKKVQKAGEMLLSQLREKESDNEVL 817
Cdd:pfam15921 488 KMtlesseRTVSDLTASLqekeraIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEIL 567
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71990528 818 TKKSLEMEAAAEEFRTYYNDMLTENDELRHRI----VQLDEIREVESSNSTKIekglrEQLEQAQHELEKKK 885
Cdd:pfam15921 568 RQQIENMTQLVGQHGRTAGAMQVEKAQLEKEIndrrLELQEFKILKDKKDAKI-----RELEARVSDLELEK 634
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
243-593 |
2.72e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.93 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 243 EVIGKKKSDLENRLFDYEKLKAQFE-QDENKLRADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQAENRKLLE 321
Cdd:pfam06160 56 DIVTKSLPDIEELLFEAEELNDKYRfKKAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 322 DKNTHDFELDEAkvqGEHLEKQRKEAWEKVEQLQEMLGE---LEAE--LDRQKELKLQLEKDMEDLRKEHEGQMAELEKR 396
Cdd:pfam06160 136 TLLANRFSYGPA---IDELEKQLAEIEEEFSQFEELTESgdyLEARevLEKLEEETDALEELMEDIPPLYEELKTELPDQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 397 LEKVSEKEKEAIEQleKIQKENKTIVKEnvyLSESKQVLLESEINLKN-ELDEMAVKLRNSQHQVAGLNEKISEEKRRR- 474
Cdd:pfam06160 213 LEELKEGYREMEEE--GYALEHLNVDKE---IQQLEEQLEENLALLENlELDEAEEALEEIEERIDQLYDLLEKEVDAKk 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 475 ---KKQDA---DVTRLDEQNQKLLREA---QDSAEL----LEEVQKGKREIDHLRQQLAhqsseagsvgQLQQKLAE--- 538
Cdd:pfam06160 288 yveKNLPEiedYLEHAEEQNKELKEELervQQSYTLneneLERVRGLEKQLEELEKRYD----------EIVERLEEkev 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 71990528 539 --SEHREYLLQLE--LERVMKMERDLDGRIEGYIRSEAAANNELERLRKDTAEQKEKLE 593
Cdd:pfam06160 358 aySELQEELEEILeqLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVE 416
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
287-424 |
3.03e-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: 46.46 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 287 KLVKYEGKIEELQSRLNKKRKELEEVQAENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGE------ 360
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnke 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71990528 361 ---LEAELDRQKELKLQLEKDMEDLRKEHEgqmaELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKE 424
Cdd:COG1579 91 yeaLQKEIESLKRRISDLEDEILELMERIE----ELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
229-630 |
3.77e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 229 ANLQIEVDQLHSEIEVIGKKKSDLENRLFDYEKLKAQFEQDE----NKLRADLEKKLKTSQEKLVKYEGKIEELQSRLNK 304
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRleqlEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 305 KRKELEEVQAENRKLLEDKNTHDFELDEakvqgehlekQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRK 384
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEALEE----------ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 385 EHEGQMAELEKRLE------KVSEKEKE---AIE---------------------------------QLEKIQKE----- 417
Cdd:COG4913 448 ALAEALGLDEAELPfvgeliEVRPEEERwrgAIErvlggfaltllvppehyaaalrwvnrlhlrgrlVYERVRTGlpdpe 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 418 ----------NKTIVKENVYLSESKQVL--------LESEINLKNEldEMAV---------------------------- 451
Cdd:COG4913 528 rprldpdslaGKLDFKPHPFRAWLEAELgrrfdyvcVDSPEELRRH--PRAItragqvkgngtrhekddrrrirsryvlg 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 452 -----KLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQnQKLLREAQDSAELLEEVQKGKREIDHLRQQLAHQSSEA 526
Cdd:COG4913 606 fdnraKLAALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVASAEREIAELEAELERLDASS 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 527 GSVGQLQQKLAEsehreylLQLELErvmkmerDLDGRIEGYIRSEAAANNELERLRKDTAEQKEKLEAMEMEARSKDLEL 606
Cdd:COG4913 685 DDLAALEEQLEE-------LEAELE-------ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
490 500
....*....|....*....|....
gi 71990528 607 ADLTRKLAKAREEHETFEINARNQ 630
Cdd:COG4913 751 LEERFAAALGDAVERELRENLEER 774
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
230-520 |
5.43e-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: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 230 NLQIEVDQLHSEIEVIGKKKSDLENRLFDYEKLKAQFEQDENKLRA---DLEKKLKTSQEKLVKYEGKIEELQSRLNKKR 306
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQqikDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 307 KELEEVQAENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEH 386
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 387 ---EGQMAELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENVYLSESKQVLLESE---INLKNELDEMAVKLRNSQHQV 460
Cdd:TIGR04523 197 lklELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQtqlNQLKDEQNKIKKQLSEKQKEL 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 461 AGLNEKISEEKRRRKKQDADVTRLDEQNQKLLreaqdSAELLEEVQKGKREIDHLRQQLA 520
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKEQDW-----NKELKSELKNQEKKLEEIQNQIS 331
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
249-468 |
5.66e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.21 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 249 KSDLENRLFDYEKLKAQfEQDENKLRADLE---KKLKTSQEKLVKYEGK-------------IEELQSRLNKKRKELEEV 312
Cdd:PRK11281 62 QQDLEQTLALLDKIDRQ-KEETEQLKQQLAqapAKLRQAQAELEALKDDndeetretlstlsLRQLESRLAQTLDQLQNA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 313 QaenrkllEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQEML---------------GELEAELD--------RQK 369
Cdd:PRK11281 141 Q-------NDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLkggkvggkalrpsqrVLLQAEQAllnaqndlQRK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 370 ELK----LQ-LEKDMEDLRKEH----EGQMAEL-----EKRLEKVSEKEKEAIEQlEKIQK--ENKTIVKE---NVYLSe 430
Cdd:PRK11281 214 SLEgntqLQdLLQKQRDYLTARiqrlEHQLQLLqeainSKRLTLSEKTVQEAQSQ-DEAARiqANPLVAQEleiNLQLS- 291
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 71990528 431 skQVLLESEINLkNEL--DEMAVK--LRNSQHQVAGLNEKIS 468
Cdd:PRK11281 292 --QRLLKATEKL-NTLtqQNLRVKnwLDRLTQSERNIKEQIS 330
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
295-522 |
5.72e-05 |
|
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: 47.25 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 295 IEELQSRLNKKRKELEEVQAENRKLLEDKNTHDFELDEA-----KVQGEhleKQRKEAWEKVEQLQEMLGELEAELDRQK 369
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAyelvcKIAGE---VERSQAWQTARELLRRYRSQQALAQRLQ 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 370 ELKLQLekdmedlrkehegqmAELEKRLEKvsekEKEAIEQLEKIQKENKTIVKENVYLSESKQVLLESEINLKNELDEM 449
Cdd:COG3096 516 QLRAQL---------------AELEQRLRQ----QQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEA 576
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71990528 450 AVKLRNSQHQVAGLNEKISEEKRR----RKKQDAdVTRLDEQNQKLLREAQDSAELLEEVQKGKREIDHLRQQLAHQ 522
Cdd:COG3096 577 VEQRSELRQQLEQLRARIKELAARapawLAAQDA-LERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAAR 652
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
235-454 |
7.54e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.84 E-value: 7.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 235 VDQLHSEIEVIGKKKsdlenrlfdyEKLKAQFEQDENKLRADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVqa 314
Cdd:PRK05771 59 LDKLRSYLPKLNPLR----------EEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERL-- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 315 enrKLLEdknthDFELDEAKVQGEHLEKQR-----KEAWEKVEQLQEMLGELEAELDRQKE--LKLQLEKDMEDLRKEhe 387
Cdd:PRK05771 127 ---EPWG-----NFDLDLSLLLGFKYVSVFvgtvpEDKLEELKLESDVENVEYISTDKGYVyvVVVVLKELSDEVEEE-- 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71990528 388 gqMAELEKRLEKVSEKE--KEAI----EQLEKIQKENKTIVKE-NVYLSESKQVLLESEINLKNELDEMAVKLR 454
Cdd:PRK05771 197 --LKKLGFERLELEEEGtpSELIreikEELEEIEKERESLLEElKELAKKYLEELLALYEYLEIELERAEALSK 268
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
294-470 |
7.68e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 294 KIEELQSRLNKKRKELEEVQAENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKElkl 373
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 374 qlEKDMEDLRKEhegqMAELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKEnvyLSESKQVLLESEINLKNELDEMAVKL 453
Cdd:COG1579 88 --NKEYEALQKE----IESLKRRISDLEDEILELMERIEELEEELAELEAE---LAELEAELEEKKAELDEELAELEAEL 158
|
170
....*....|....*..
gi 71990528 454 RNSQHQVAGLNEKISEE 470
Cdd:COG1579 159 EELEAEREELAAKIPPE 175
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
236-620 |
1.11e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 236 DQLHSEIEVIGKKKSDLENRLFDYEKLKAQFEQDENK-----LRADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKEL- 309
Cdd:PRK04863 789 EQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGShlavaFEADPEAELRQLNRRRVELERALADHESQEQQQRSQLe 868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 310 ---EEVQAENR-----KLLEDkNTHDFELDEAKVQGEHLE------KQRKEAWEKVEQLQEMLGELEAELDRQKELKLQL 375
Cdd:PRK04863 869 qakEGLSALNRllprlNLLAD-ETLADRVEEIREQLDEAEeakrfvQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQA 947
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 376 EKDMEDL------------RKEHEGqMAELEKRLEK---VSEKEKEAIEQLEKIQKENKTIVKENV-YLSESKQVL--LE 437
Cdd:PRK04863 948 QQTQRDAkqqafaltevvqRRAHFS-YEDAAEMLAKnsdLNEKLRQRLEQAEQERTRAREQLRQAQaQLAQYNQVLasLK 1026
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 438 SEIN--------LKNELDEMAV--------KLRNSQHQvagLNEKISEEKRRRKKQDADVTR----LDEQNQKLLREAQD 497
Cdd:PRK04863 1027 SSYDakrqmlqeLKQELQDLGVpadsgaeeRARARRDE---LHARLSANRSRRNQLEKQLTFceaeMDNLTKKLRKLERD 1103
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 498 SAELLEEVQKGKREIDHL--------------RQQLAHQSS-EAGSV-----GQLQQKLAESEH-REYLLQLElervmkm 556
Cdd:PRK04863 1104 YHEMREQVVNAKAGWCAVlrlvkdngverrlhRRELAYLSAdELRSMsdkalGALRLAVADNEHlRDVLRLSE------- 1176
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71990528 557 erdlDGRI-EGYIRSEAAANNEL-ERLRKD---TAEQKEKLEAMEmearskdLELADLTRKLAkAREEH 620
Cdd:PRK04863 1177 ----DPKRpERKVQFYIAVYQHLrERIRQDiirTDDPVEAIEQME-------IELSRLTEELT-SREQK 1233
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
243-595 |
1.17e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.98 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 243 EVIGKKKSDLENRLFDYEKLKAQFeqdeNKLRAdlEKKLKTSQEKLVKYEGKIEELQSRLNkkrkELEEVQAENRKlled 322
Cdd:PRK04778 75 EIVTNSLPDIEEQLFEAEELNDKF----RFRKA--KHEINEIESLLDLIEEDIEQILEELQ----ELLESEEKNRE---- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 323 knthdfELDEAKVQGEHLEK----QRKEAWEKVEQLQEMLGELEAELDRQKELK------------LQLEKDMEDLRKeh 386
Cdd:PRK04778 141 ------EVEQLKDLYRELRKsllaNRFSFGPALDELEKQLENLEEEFSQFVELTesgdyveareilDQLEEELAALEQ-- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 387 egQMAELEKRLEKVsekEKEAIEQLEKIQKENKTIVKENVYL---------SESKQVLLESEINLKN-ELDEMAVKLRNS 456
Cdd:PRK04778 213 --IMEEIPELLKEL---QTELPDQLQELKAGYRELVEEGYHLdhldiekeiQDLKEQIDENLALLEElDLDEAEEKNEEI 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 457 QHQVAGLNEKISEE-------KRRRKKQDADVTRLDEQNQKLLREAQD-------SAELLEEVQKGKREIDHLRQQLAHQ 522
Cdd:PRK04778 288 QERIDQLYDILEREvkarkyvEKNSDTLPDFLEHAKEQNKELKEEIDRvkqsytlNESELESVRQLEKQLESLEKQYDEI 367
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71990528 523 SSEAGSvgqlqQKLAESEHREYLLQLE--LERVMKMERDLDGRIEGYIRSEAAANNELERLRKDTAEQKEKLEAM 595
Cdd:PRK04778 368 TERIAE-----QEIAYSELQEELEEILkqLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEKS 437
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
277-543 |
1.25e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.25 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 277 LEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQaenrKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQL-- 354
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMT----KFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELkg 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 355 --QEMLGELEAELDRQKELKLQLEKdMEDLRKEHEGQMAELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENVYLSESK 432
Cdd:pfam05483 437 keQELIFLLQAREKEIHDLEIQLTA-IKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLEL 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 433 QVLLESEINLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVT-RLDEQNQKLLREAQDSAELLEEVQKGKRE 511
Cdd:pfam05483 516 KKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKcKLDKSEENARSIEYEVLKKEKQMKILENK 595
|
250 260 270
....*....|....*....|....*....|..
gi 71990528 512 IDHLRQQLAHQSSEAGSVGQLQQKLAESEHRE 543
Cdd:pfam05483 596 CNNLKKQIENKNKNIEELHQENKALKKKGSAE 627
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
276-464 |
1.51e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.60 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 276 DLEKKLKTSQEKLVKYEGKIEELqsrlnkkrkELEEVQAENRKLlEDKNTHDFELDEAKVQGEH-LEKQRKEAWEKVEQL 354
Cdd:PRK04778 253 DIEKEIQDLKEQIDENLALLEEL---------DLDEAEEKNEEI-QERIDQLYDILEREVKARKyVEKNSDTLPDFLEHA 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 355 QEMLGELEAELDRQKElKLQLEKDMEDLRKEHEGQMAELEKRL----EKVSEKEK---EAIEQLEKIQKENKTIVKENVY 427
Cdd:PRK04778 323 KEQNKELKEEIDRVKQ-SYTLNESELESVRQLEKQLESLEKQYdeitERIAEQEIaysELQEELEEILKQLEEIEKEQEK 401
|
170 180 190
....*....|....*....|....*....|....*..
gi 71990528 428 LSESKQVLLESEINLKNELDEMAVKLRNSQHQVAGLN 464
Cdd:PRK04778 402 LSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEKSN 438
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
362-613 |
1.56e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.50 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 362 EAELDRQKELKLQLEKDMEDLRKEHEGQMAELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENVYLSESKQVLLESEIN 441
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 442 LKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQNQKLLREAQDSAELLEEVQKGKREIDHLRQQLAH 521
Cdd:pfam05557 81 KKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 522 QSSEAGSVGQ----LQQKLAESEHREYLL---QLELERVMKMERDLDGRIE--GYIRSEAAANNELERLRKDTAEQKEKL 592
Cdd:pfam05557 161 QQSSLAEAEQrikeLEFEIQSQEQDSEIVknsKSELARIPELEKELERLREhnKHLNENIENKLLLKEEVEDLKRKLERE 240
|
250 260
....*....|....*....|.
gi 71990528 593 EAMEMEARSKDLELADLTRKL 613
Cdd:pfam05557 241 EKYREEAATLELEKEKLEQEL 261
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
231-457 |
1.82e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.30 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 231 LQIEVDQLHSEIEVIGKKKSDLENRLFDYEKLKAQFEQDENklrADLEKKLKTSQEKLVKYEGKIeelqsrlNKKRKELE 310
Cdd:PRK05771 91 VEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPWGN---FDLDLSLLLGFKYVSVFVGTV-------PEDKLEEL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 311 EVQAENRKLLEDKNTHDFE----LDEAKVQGEHLEKQRKEAWEKVE-----QLQEMLGELEAELDRQKELKLQLEKDMED 381
Cdd:PRK05771 161 KLESDVENVEYISTDKGYVyvvvVVLKELSDEVEEELKKLGFERLEleeegTPSELIREIKEELEEIEKERESLLEELKE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 382 LRKEHEGQMAELEKRLEKVSEKEKE-----------AIE------QLEKIQKENKTIVKENVYLseskqvlleSEINLKN 444
Cdd:PRK05771 241 LAKKYLEELLALYEYLEIELERAEAlskflktdktfAIEgwvpedRVKKLKELIDKATGGSAYV---------EFVEPDE 311
|
250
....*....|...
gi 71990528 445 ELDEMAVKLRNSQ 457
Cdd:PRK05771 312 EEEEVPTKLKNPK 324
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
240-500 |
1.84e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 240 SEIEVIGKKKSDLENRLFDYEKLKAQFEQDENKLRAdlekKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQAENRKL 319
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNE----ELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 320 LEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKehegqMAELEKRLEK 399
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEK-----IKELEKELEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 400 ------VSEKEKEAIEQLEKIQKENKTIVKENVYLSESKQVLLESEINLKNELDEMAVKLRNSQHQVAGLNEKISEEKRR 473
Cdd:COG1340 152 akkaleKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEE 231
|
250 260
....*....|....*....|....*..
gi 71990528 474 RKKQDADVTRLDEQNQKLLREAQDSAE 500
Cdd:COG1340 232 IIELQKELRELRKELKKLRKKQRALKR 258
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
225-621 |
1.97e-04 |
|
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: 45.34 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 225 NVVNANLQIEVDQLHSEIEVIGKKKSDLENRLFDYEKLKAQFEQDENKLRADLE------------KKLKTSQEKLVKYE 292
Cdd:TIGR00618 197 ELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREaqeeqlkkqqllKQLRARIEELRAQE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 293 GKIEELQSRLNKKRK---------ELEEVQAENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGE--- 360
Cdd:TIGR00618 277 AVLEETQERINRARKaaplaahikAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQeih 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 361 LEAELDRQKELKLQLEKDMEDLRKEHegqmaELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENVYLSESKQVLLESEI 440
Cdd:TIGR00618 357 IRDAHEVATSIREISCQQHTLTQHIH-----TLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKK 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 441 NLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQNQKLLREAQDSAE---LLEEVQKGKREIDHLRQ 517
Cdd:TIGR00618 432 QQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVvlaRLLELQEEPCPLCGSCI 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 518 QLAHQSSEAGSVGQLQQKLAESEHREYLLQLELERV---MKMERDLDGRIEGYIRSEAAANNELERLRKDTAEQKEKLEA 594
Cdd:TIGR00618 512 HPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVyhqLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN 591
|
410 420
....*....|....*....|....*..
gi 71990528 595 MEMEARSKDLELADLTRKLAKAREEHE 621
Cdd:TIGR00618 592 ITVRLQDLTEKLSEAEDMLACEQHALL 618
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
243-493 |
2.20e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.23 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 243 EVIGKKKSDLENRLfdyEKLKAQFEQDENKLRADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQAENRKLLED 322
Cdd:COG2433 380 EALEELIEKELPEE---EPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 323 KNTHDFELDEAKVQGEHLEKQRKEawekVEQLQEMLGELEAELDRQKEL-KLQLEKDM------EDLRKEHegqMAELEK 395
Cdd:COG2433 457 ERREIRKDREISRLDREIERLERE----LEEERERIEELKRKLERLKELwKLEHSGELvpvkvvEKFTKEA---IRRLEE 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 396 R----------LEKVSEKEKEAIEQLekIQKENKTIVKENVYLSESKQVLLESEINLKNElDEMAVKLRNSQhqvAGLNE 465
Cdd:COG2433 530 EyglkegdvvyLRDASGAGRSTAELL--AEAGPRAVIVPGELSEAADEVLFEEGIPVLPA-EDVTIQEVDDL---AVVDE 603
|
250 260
....*....|....*....|....*...
gi 71990528 466 KISEEKRRRKKQDADVTRLDEQNQKLLR 493
Cdd:COG2433 604 EELEAAIEDWEERAEERRREKKAEMLER 631
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
235-504 |
2.31e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 235 VDQLHSEIEVIGKKKSDLENrlfDYEKLKAQFEQDENKLRA-------------DLEKKLKTSQEKLVKYEGKIEELQSR 301
Cdd:TIGR04523 337 ISQLNEQISQLKKELTNSES---ENSEKQRELEEKQNEIEKlkkenqsykqeikNLESQINDLESKIQNQEKLNQQKDEQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 302 LNKKRKELEEVQAENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMED 381
Cdd:TIGR04523 414 IKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 382 LRKEHEGQMAELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENVYLSESKQVLLESEINLKNELDEmavklrnsqHQVA 461
Cdd:TIGR04523 494 KEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLE---------KEID 564
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 71990528 462 GLNEKISEEKRRRKKQDADVTRLDEQNQKLLREAQDSAELLEE 504
Cdd:TIGR04523 565 EKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE 607
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
229-413 |
2.32e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 229 ANLQIEVDQLHSEIEVIGKKKSDLENRLfdyEKLKAQFEQDENKLrADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKE 308
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEE---KALLKQLAALERRI-AALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 309 LEEVQAENRK----------------LLEDKNTHDF-----------------------ELDEAKVQGEHLEKQRKEAWE 349
Cdd:COG4942 99 LEAQKEELAEllralyrlgrqpplalLLSPEDFLDAvrrlqylkylaparreqaeelraDLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71990528 350 KVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEHEgQMAELEKRLEKVSEKEKEAIEQLEK 413
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELA-ELQQEAEELEALIARLEAEAAAAAE 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
440-887 |
2.61e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 440 INLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQNQKL--LREAQDSAELLEEVQKGKREIDHLRQ 517
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELekLEKLLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 518 QLAHQSSEAGSVGQLQQKLAESEHREYLLQLELERVMkmeRDLDGRIEGYIRSeaaANNELERLRKDTAEQKEKLEAMEM 597
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELL---EQLSLATEEELQD---LAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 598 EARSKDLELADLTRKLAKAREEHetfEINARNQFYAVTGQMHEDIESYKQRLLELEPYPGKIISGSfrdfpsqtdpSPAT 677
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEE---RLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVL----------GLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 678 TDAWMQTDVEEQLMVSPEVSLVSEAPSSLQDSRRSSHLDE-------------KLRRTIEKIGELLAEHESFQESLRdpe 744
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAlglppdlspeellELLDRIEELQELLREAEELEEELQ--- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 745 fhTAEAFRKISQLLKSIlsGANSEEMLERIWTwltlktkaLVEQQDEQMKKVQKAGEMLLSQLREKESDNEVLTKKSLem 824
Cdd:COG4717 365 --LEELEQEIAALLAEA--GVEDEEELRAALE--------QAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL-- 430
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71990528 825 EAAAEEFRTYYNDMLTENDELRHRIVQLD-EIREVESSnstkiekglrEQLEQAQHELEKKKRE 887
Cdd:COG4717 431 EEELEELEEELEELEEELEELREELAELEaELEQLEED----------GELAELLQELEELKAE 484
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
232-434 |
2.65e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 232 QIEVDQLHSEIEVigKKKSDLENRLFDYEKLKAQ---FEQDENKLRADLEKKlKTSQEKLVKYEGKIEELQSRlnKKRKE 308
Cdd:PTZ00121 1619 KIKAEELKKAEEE--KKKVEQLKKKEAEEKKKAEelkKAEEENKIKAAEEAK-KAEEDKKKAEEAKKAEEDEK--KAAEA 1693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 309 LEEVQAENRKLLEDKNTHdfelDEAKVQGEHLEKQRKEAWEKVEQLQ----------EMLGELEAELDRQKELKLQLEKD 378
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKE----AEEKKKAEELKKAEEENKIKAEEAKkeaeedkkkaEEAKKDEEEKKKIAHLKKEEEKK 1769
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71990528 379 MEDLRKEH-----EGQMAELEKRLEKVSEKEKEAIEQLEKIQKENKtivKENVYLSESKQV 434
Cdd:PTZ00121 1770 AEEIRKEKeavieEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGK---EGNLVINDSKEM 1827
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
341-640 |
2.79e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.73 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 341 EKQRKEAWEKVEQlqEMLGELEAELDRQKELKLQLEKdmedlrkEHEGQMAELEKRLEKVSEKEKEAIE---QLEKIQKE 417
Cdd:pfam17380 286 ERQQQEKFEKMEQ--ERLRQEKEEKAREVERRRKLEE-------AEKARQAEMDRQAAIYAEQERMAMErerELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 418 NKTIVKENVylsesKQVLLESEINLKNELDEMAVKlrnsqhqvaglnekiSEEKRRRKKQDADVTRldeqNQKLLREaqd 497
Cdd:pfam17380 357 ERKRELERI-----RQEEIAMEISRMRELERLQME---------------RQQKNERVRQELEAAR----KVKILEE--- 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 498 saELLEEVQKGKREIDHLRQQlahqsseagsvgqlqqklAESEHREYLLQLELERVMKMERdldgriegYIRSEAAANNE 577
Cdd:pfam17380 410 --ERQRKIQQQKVEMEQIRAE------------------QEEARQREVRRLEEERAREMER--------VRLEEQERQQQ 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71990528 578 LERLRKDTAEQKEKLEAMEMEARSKDLELADLTRKLAKAREEHETFEINARNQFYAVTGQMHE 640
Cdd:pfam17380 462 VERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEE 524
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
243-423 |
2.84e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 243 EVIGKKKSDLENRLFDYEKLKAQFEQDenklRADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEevQAENRKLLED 322
Cdd:PRK00409 509 KLIGEDKEKLNELIASLEELERELEQK----AEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAE--KEAQQAIKEA 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 323 KNTHDFELDEAKV--QGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEdLRKEHEGQMAELekrLEKV 400
Cdd:PRK00409 583 KKEADEIIKELRQlqKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDE-VKYLSLGQKGEV---LSIP 658
|
170 180 190
....*....|....*....|....*....|...
gi 71990528 401 SEKE----------KEAIEQLEKIQKENKTIVK 423
Cdd:PRK00409 659 DDKEaivqagimkmKVPLSDLEKIQKPKKKKKK 691
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
445-653 |
3.42e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 445 ELDEMAVKLRNSQHQVAGLnEKISEEKRRRKKQDADVTRLDEqnqklLREAQDSAELLEEVQKGKREIDHLRQQLAhqss 524
Cdd:COG4913 236 DLERAHEALEDAREQIELL-EPIRELAERYAAARERLAELEY-----LRAALRLWFAQRRLELLEAELEELRAELA---- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 525 eagsvgQLQQKLAESEHREYLLQLELERVMKMERDLDG-RIEGYIRSEAAANNELERLRKDTAEQKEKLEAMEMEARSKD 603
Cdd:COG4913 306 ------RLEAELERLEARLDALREELDELEAQIRGNGGdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 71990528 604 LELADLTRKLAKAREEHETFEINARNQFYAVTGQMHEDIESYKQRLLELE 653
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
231-543 |
3.44e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 231 LQIEVDQLHSEIEVIGKKKSDLENRLfdyEKLKAQFEQDENKLRaDLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELE 310
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEEL---EQARSELEQLEEELE-ELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 311 EVQAENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELdrQKELKLQLEKDMEDLRKEHEgQM 390
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL--QALSEAEAEQALDELLKEAN-RN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 391 AELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENVYLSESKQVLLESEINLKNELDEMAVKLRNSQHQVAGLNEKISEE 470
Cdd:COG4372 196 AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEE 275
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71990528 471 KRRRKKQDADVTRLDEQNQKLLREAQDSAELLEEVQKGKREIDHLRQQLAHQSSEAGSVGQLQQKLAESEHRE 543
Cdd:COG4372 276 EELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
285-594 |
3.61e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 285 QEKLVKYEGKIEELQSRL---NKKRKELEEVQAENRKLLEDKNThdfELDEAKVQ----GEHLE---------KQRKEAW 348
Cdd:PRK04863 347 QEKIERYQADLEELEERLeeqNEVVEEADEQQEENEARAEAAEE---EVDELKSQladyQQALDvqqtraiqyQQAVQAL 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 349 EKVEQLQEmLGELEAE--LDRQKELKLQLEKDMEDLRkehegqmaELEKRLeKVSEkekEAIEQLEKIQKENKTIVKEnV 426
Cdd:PRK04863 424 ERAKQLCG-LPDLTADnaEDWLEEFQAKEQEATEELL--------SLEQKL-SVAQ---AAHSQFEQAYQLVRKIAGE-V 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 427 YLSESKQVLleseinlkNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQNQKLLREAQDSAELLEEVQ 506
Cdd:PRK04863 490 SRSEAWDVA--------RELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQE 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 507 KGKREIDHLRQQLAHQSSEAGSVGQLQQKLaESEHREYL--------LQLELERVMKM--ERDLDG-RIEGYIRSEAAAN 575
Cdd:PRK04863 562 ELEARLESLSESVSEARERRMALRQQLEQL-QARIQRLAarapawlaAQDALARLREQsgEEFEDSqDVTEYMQQLLERE 640
|
330
....*....|....*....
gi 71990528 576 NELERLRKDTAEQKEKLEA 594
Cdd:PRK04863 641 RELTVERDELAARKQALDE 659
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
286-417 |
4.13e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.30 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 286 EKLVKYEGKIEELQSRLNKKRKELEEVQAENRKLLEDknthdFELDEAKVqgEHLEkQRKEAWEK--------VEQLQEM 357
Cdd:COG0497 254 ERLAEYDPSLAELAERLESALIELEEAASELRRYLDS-----LEFDPERL--EEVE-ERLALLRRlarkygvtVEELLAY 325
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71990528 358 LGELEAELDRQKelklQLEKDMEDLRKEHEGQMAELEKRLEKVSEKEKEAIEQLEK-IQKE 417
Cdd:COG0497 326 AEELRAELAELE----NSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLEKaVTAE 382
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
268-605 |
4.20e-04 |
|
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: 44.57 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 268 QDENKLRADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQAENRKLLEDKNTHDFELDEAKVQGEH-LEKQRKE 346
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPeQDLQDVR 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 347 AWEKveQLQEmlgeleaeldRQKELKLQLEKDMEDLRKEHEGQMAELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENV 426
Cdd:TIGR00618 632 LHLQ--QCSQ----------ELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 427 YLSESK-QVLLESEINLKNELDEMAVKLRNSQHQVAG----LNEKISEEKRRRKKQDADVTRLDEQNqkllreaqdSAEL 501
Cdd:TIGR00618 700 AQCQTLlRELETHIEEYDREFNEIENASSSLGSDLAAredaLNQSLKELMHQARTVLKARTEAHFNN---------NEEV 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 502 LEEVQKGKREIDHLRQQLAHQSSEAGSVGQLQQKLAESE----HREYLLQLELERVMKMERDLDGRIEGYIRSEAAANNE 577
Cdd:TIGR00618 771 TAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGqeipSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQ 850
|
330 340 350
....*....|....*....|....*....|
gi 71990528 578 LERLrKDTAEQKEKL--EAMEMEARSKDLE 605
Cdd:TIGR00618 851 LLKY-EECSKQLAQLtqEQAKIIQLSDKLN 879
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
329-888 |
4.52e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 329 ELDEAKVQGEHLE------KQRKEAWEKVEQLQEMLGELEAELDRQKelKLQLEKDMEDLRKEHEGQMAELEkRLEKVSE 402
Cdd:COG4913 243 ALEDAREQIELLEpirelaERYAAARERLAELEYLRAALRLWFAQRR--LELLEAELEELRAELARLEAELE-RLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 403 KEKEAIEQLEKIQKENKTIVKENvylseskqvlLESEI-NLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADV 481
Cdd:COG4913 320 ALREELDELEAQIRGNGGDRLEQ----------LEREIeRLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 482 TRLDEQNQKLLREAQDS-AELLEEVQKGKREIDHLRQQLAHQSSEAGSVGQ--------LQQKLAESEHR-----EyLLQ 547
Cdd:COG4913 390 AALLEALEEELEALEEAlAEAEAALRDLRRELRELEAEIASLERRKSNIPArllalrdaLAEALGLDEAElpfvgE-LIE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 548 LELErvmkmERDLDGRIEGYIRS-----------EAAANNELERLRKDTAEQKEKLEAMEMEARSKDLELADLTRKLAKA 616
Cdd:COG4913 469 VRPE-----EERWRGAIERVLGGfaltllvppehYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFK 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 617 REEHETF---EINARNQFYAVtgqmhEDIEsykqrllELEPYPGKI-----ISGSFRDFpsQTDPSPATTDAW-MQTDVE 687
Cdd:COG4913 544 PHPFRAWleaELGRRFDYVCV-----DSPE-------ELRRHPRAItragqVKGNGTRH--EKDDRRRIRSRYvLGFDNR 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 688 EQL-MVSPEVSLVSEAPSSLQDSRRSShldEKLRRTIEKIGELLAEHESFQESLRDpefhTAEAFRKISQL---LKSILS 763
Cdd:COG4913 610 AKLaALEAELAELEEELAEAEERLEAL---EAELDALQERREALQRLAEYSWDEID----VASAEREIAELeaeLERLDA 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 764 GANSEEMLERIWTWLTLKTKALVEQQDEQMKKVQKAGEmllsqlrEKESDNEVLTKKSLEMEAAAEEFRTYYNDMLtenD 843
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEK-------ELEQAEEELDELQDRLEAAEDLARLELRALL---E 752
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 71990528 844 ELRHRIVQLDEIREVESSNSTKIEKgLREQLEQAQHELEKKKREY 888
Cdd:COG4913 753 ERFAAALGDAVERELRENLEERIDA-LRARLNRAEEELERAMRAF 796
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
349-510 |
4.66e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 349 EKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKehegqmaELEKRLEKVSEKEKEAIEQLEkiqKENKTIVKEnvyl 428
Cdd:PRK00409 516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKE-------ELEEKKEKLQEEEDKLLEEAE---KEAQQAIKE---- 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 429 seskqvlleseinLKNELDEMAVKLRNSQ-HQVAGLNEKISEEKRRrkkqdadvtRLDEQNQKLLREAQDSAELLEEVQK 507
Cdd:PRK00409 582 -------------AKKEADEIIKELRQLQkGGYASVKAHELIEARK---------RLNKANEKKEKKKKKQKEKQEELKV 639
|
...
gi 71990528 508 GKR 510
Cdd:PRK00409 640 GDE 642
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
327-504 |
4.99e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 327 DFELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKehegQMAELEKRLEKV-SEKEK 405
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA----RIKKYEEQLGNVrNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 406 EAIEqlekiqkenktivKENVYLSESKQVLLESEINLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRkkqDADVTRLD 485
Cdd:COG1579 92 EALQ-------------KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELE 155
|
170
....*....|....*....
gi 71990528 486 EQNQKLLREAQDSAELLEE 504
Cdd:COG1579 156 AELEELEAEREELAAKIPP 174
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
232-592 |
5.21e-04 |
|
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: 44.06 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 232 QIEVDQLHSEIEVIGKKKSDLENRLFDYEKLKAQFEQDENKLRADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEE 311
Cdd:pfam12128 589 RIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDK 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 312 VQ----AENRKLLEDKNTHDFELD----EAKVQGEHLEKQRKEA-WEKVEQLQEMLGELEAELDRQKELKL----QLEKD 378
Cdd:pfam12128 669 KNkalaERKDSANERLNSLEAQLKqldkKHQAWLEEQKEQKREArTEKQAYWQVVEGALDAQLALLKAAIAarrsGAKAE 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 379 MEDLRKEHEGQMAEL---EKRLEKVSEKEKEAIEQLEKIQKENKTIVKENVYLSEskQVLLESEiNLKNELDEMAVKLRN 455
Cdd:pfam12128 749 LKALETWYKRDLASLgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQE--TWLQRRP-RLATQLSNIERAISE 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 456 SQHQvagLNEKISEEKRRRKKQdadvtrldEQNQKLLREAQDsaELLEEVQKGKREIDHLRQQLAHQSSEAGSvGQLQQK 535
Cdd:pfam12128 826 LQQQ---LARLIADTKLRRAKL--------EMERKASEKQQV--RLSENLRGLRCEMSKLATLKEDANSEQAQ-GSIGER 891
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 71990528 536 LAESEHREYLLQLELERVMKMERDLDGRIEGYIRSEAAANneLERLRKDTAEQKEKL 592
Cdd:pfam12128 892 LAQLEDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLAET--WESLREEDHYQNDKG 946
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
249-619 |
5.22e-04 |
|
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: 43.91 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 249 KSDLENRLFDYEKLKAQFEQDENKLRADLeKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQAENRKLLEDKnthdf 328
Cdd:pfam05622 9 KDELAQRCHELDQQVSLLQEEKNSLQQEN-KKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETAR----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 329 elDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKdmedlRKEHEGQMAELEKRLEKVSEKEKeai 408
Cdd:pfam05622 83 --DDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDK-----VKKLEATVETYKKKLEDLGDLRR--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 409 eQLEKIQKENKTIVKENVYLSESkqvlLESEINLKNELDemavklrNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQN 488
Cdd:pfam05622 153 -QVKLLEERNAEYMQRTLQLEEE----LKKANALRGQLE-------TYKRQVQELHGKLSEESKKADKLEFEYKKLEEKL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 489 QKLLREAQ------DS-AELLEEVQKGKREIDHLRQQLAHQSSEAGSVGQLQQKLAESEHREYLLQLELERVMkmerdLD 561
Cdd:pfam05622 221 EALQKEKErliierDTlRETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKM-----LR 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 71990528 562 GRIEGYIRSEAAannELERLRKDTAEQKEKLEAMEMEARSKDLELADLTRKLAKAREE 619
Cdd:pfam05622 296 LGQEGSYRERLT---ELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQE 350
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
241-619 |
5.81e-04 |
|
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: 44.01 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 241 EIEVIGKKKSDLENRLFDYEKLKAQFEQDENKLRADLEKKLKTSQEKlvkyegkiEELQSRLNKKRKELEEVqaenrkll 320
Cdd:pfam01576 13 ELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEA--------EEMRARLAARKQELEEI-------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 321 edknTHDFE--LDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAEldRQkelKLQLEKdmedlrkehegqmAELEKRLE 398
Cdd:pfam01576 77 ----LHELEsrLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAA--RQ---KLQLEK-------------VTTEAKIK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 399 KVSEKEKEAIEQLEKIQKENKtivkenvyLSESKQVLLESEINLKNELDEMAVKLRNSQHQV-AGLNEKISEEKRRRKKQ 477
Cdd:pfam01576 135 KLEEDILLLEDQNSKLSKERK--------LLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMiSDLEERLKKEEKGRQEL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 478 DADVTRLDEQNQKLLREAQDSAELLEE--VQKGKREiDHLRQQLAHQSSEAGSVGQLQQKLAESEHREYLLQ--LELERV 553
Cdd:pfam01576 207 EKAKRKLEGESTDLQEQIAELQAQIAElrAQLAKKE-EELQAALARLEEETAQKNNALKKIRELEAQISELQedLESERA 285
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71990528 554 M-----KMERDLDGRIEGyIRSE-------AAANNELERLRKDTAEQKEKleAMEMEARSKDLELADLTRKLAKAREE 619
Cdd:pfam01576 286 ArnkaeKQRRDLGEELEA-LKTEledtldtTAAQQELRSKREQEVTELKK--ALEEETRSHEAQLQEMRQKHTQALEE 360
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
353-617 |
7.17e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 353 QLQEMLGELEAELDRQKELKLQLEKDMEDL---RKEHEGQMAELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENVYLS 429
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYkrdREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 430 ESKQVLLESEINLKNELDEMAVKLRnSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQNQKLLREAQDSAEllEEVQKGK 509
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIK-TLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTE--EELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 510 REIDHLRQQLAHQSSEA----GSVGQLQQKLAESEHREyllqLELERVMKMERDLDGRIEGYIRSEAAANNELErlrkDT 585
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVlqlqDTITTLTQKLTTAHRKE----AENEALLEELRSLQERLNASERKVEGLGEELS----SM 263
|
250 260 270
....*....|....*....|....*....|..
gi 71990528 586 AEQKEKLEAMEMEARskdLELADLTRKLAKAR 617
Cdd:pfam07888 264 AAQRDRTQAELHQAR---LQAAQLTLQLADAS 292
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
252-496 |
9.41e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.19 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 252 LENRLFDYEKLKAQFEQDENKLRADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQAENRKLLEDKNTHDFELD 331
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 332 EAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQ------KELKLQLEKDMEDLRKEHEGQMAELEKRLEKVSEKEK 405
Cdd:pfam05557 87 ALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAelelqsTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 406 EAIEQLEKIQKENKTIVKENVYLSESKQVL-----LESEInlkNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQD-- 478
Cdd:pfam05557 167 EAEQRIKELEFEIQSQEQDSEIVKNSKSELaripeLEKEL---ERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEky 243
|
250
....*....|....*....
gi 71990528 479 -ADVTRLDEQNQKLLREAQ 496
Cdd:pfam05557 244 rEEAATLELEKEKLEQELQ 262
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
234-619 |
9.82e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 9.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 234 EVDQLHSEIEVIGKKKSDLENRLFDyEKLKAQFEQDENKLRAdlEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQ 313
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFE-EARMAHFARRQAAIKA--EEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 314 AENRKlledknthdfELDEAKVQGEHLEKQ----RKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDmeDLRKEHEGQ 389
Cdd:PTZ00121 1311 AEEAK----------KADEAKKKAEEAKKKadaaKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA--EKKKEEAKK 1378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 390 MAELEKRlekvSEKEKEAIEQLEKIQKENKTIVKENVYLSESKQVLLESEINLKNELDEMAVKLRNSQHQVAGLNEKISE 469
Cdd:PTZ00121 1379 KADAAKK----KAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 470 EKRRRK--KQDADVTRLDEQNQKLLREAQDSAELLEEVQKGKREIDHLRQQlAHQSSEAGSVGQLQQKLAESEHREYLLQ 547
Cdd:PTZ00121 1455 EAKKAEeaKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA-AEAKKKADEAKKAEEAKKADEAKKAEEA 1533
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71990528 548 LELERVMKMERdldgriegyiRSEAAANNELERLRKDTAEQKEKLEAMEMEARSKDLELADLTRKLAKAREE 619
Cdd:PTZ00121 1534 KKADEAKKAEE----------KKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE 1595
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
321-630 |
9.94e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 321 EDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEhegqMAELEKRLEKV 400
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAE----LAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 401 SEKEKEAIEQLEKIQKENKTIVKENVYLSESKQVLLESEINLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQdad 480
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ--- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 481 vtRLDEQNQKLLREAQDSAELLEEVQKGKREIDHLRQQLAHQSSEAGSVGQLQQKLAESEHREYLLQLELERVMKMERDL 560
Cdd:COG4372 184 --ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 561 DGRIEGYIRSEAAANNELERLRKDTAEQKEKLEAMEMEARSKDLELADLTRKLAKAREEHETFEINARNQ 630
Cdd:COG4372 262 ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELA 331
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
334-538 |
1.03e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 334 KVQGEHLEKQRKEAWEKVEQLQEMLGELEAEldrQKELKLQLEKDMEDLrKEHEGQMAELEKRLEKVSEKEKEAIEQLEK 413
Cdd:PHA02562 198 KTYNKNIEEQRKKNGENIARKQNKYDELVEE---AKTIKAEIEELTDEL-LNLVMDIEDPSAALNKLNTAAAKIKSKIEQ 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 414 IQKENKtIVKENVYLSESKQVLLESEinlkNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQNQKLLR 493
Cdd:PHA02562 274 FQKVIK-MYEKGGVCPTCTQQISEGP----DRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKIST 348
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 71990528 494 EAQDSAELLEEVQKGKREIDHLRQQLAHQSSEagsVGQLQQKLAE 538
Cdd:PHA02562 349 NKQSLITLVDKAKKVKAAIEELQAEFVDNAEE---LAKLQDELDK 390
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
229-407 |
1.12e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 229 ANLQIEVDQLHSEIEVIGKKKSDLENRLFDYEKLKAQFEQDENKLRADLEKKLKTSQeKLVKYEG--------------K 294
Cdd:COG4942 58 AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALY-RLGRQPPlalllspedfldavR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 295 IEELQSRLNKKRKELEEVQAENRKLLEDKNThdfELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQ 374
Cdd:COG4942 137 RLQYLKYLAPARREQAEELRADLAELAALRA---ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
|
170 180 190
....*....|....*....|....*....|...
gi 71990528 375 LEKDMEDLRKEHEGQMAELEKRLEKVSEKEKEA 407
Cdd:COG4942 214 ELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
336-618 |
1.41e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.53 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 336 QGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKD------------MEDLRKEHEGQMAE------LEKRL 397
Cdd:PLN03229 409 EGVPVDPERKVNMKKREAVKTPVRELEGEVEKLKEQILKAKESsskpselalnemIEKLKKEIDLEYTEaviamgLQERL 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 398 EKVSEKEKEA-----------IEQLEKIQKE-NKTIVKENVYLS-ESKQVLLE--SEINLKNELDEMAVKLRnsqhqvAG 462
Cdd:PLN03229 489 ENLREEFSKAnsqdqlmhpvlMEKIEKLKDEfNKRLSRAPNYLSlKYKLDMLNefSRAKALSEKKSKAEKLK------AE 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 463 LNEKISEEKRRRK-KQDADVTRLDEQNQKLLREAQDSAELLEEVQKGKREID-HLRQQLAHQSSEAGSVGQLQQKLAESE 540
Cdd:PLN03229 563 INKKFKEVMDRPEiKEKMEALKAEVASSGASSGDELDDDLKEKVEKMKKEIElELAGVLKSMGLEVIGVTKKNKDTAEQT 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 541 HREYLLqlelERVMKMERDLDGRIEGYIRSeAAANNELERLRKDTA--------EQKEKLEAMEMEARSKDLELADLTRK 612
Cdd:PLN03229 643 PPPNLQ----EKIESLNEEINKKIERVIRS-SDLKSKIELLKLEVAkasktpdvTEKEKIEALEQQIKQKIAEALNSSEL 717
|
....*.
gi 71990528 613 LAKARE 618
Cdd:PLN03229 718 KEKFEE 723
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
466-619 |
1.69e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 466 KISEEKRRRKKQDADvTRLDEQNQKLLREAQDSA-----ELLEEVQKGKREIDHLRQQLAHQSSeagsvgQLQQKLAESE 540
Cdd:PRK12704 34 KEAEEEAKRILEEAK-KEAEAIKKEALLEAKEEIhklrnEFEKELRERRNELQKLEKRLLQKEE------NLDRKLELLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 541 HREYLLQLELERVMKMERDLDGRIEGYIRSEAAANNELERLRKDTAEQ--KEKLEAMEMEARskdLELADLTRKL-AKAR 617
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEakEILLEKVEEEAR---HEAAVLIKEIeEEAK 183
|
..
gi 71990528 618 EE 619
Cdd:PRK12704 184 EE 185
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
340-424 |
1.76e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 340 LEKQRKEAWEKVEqlqemlgELEAELDRQKELKLQLEKDMEDLRKEHEGQMAELEKRLEKVSEKEKEAIEQ----LEKIQ 415
Cdd:PRK00409 525 LEELERELEQKAE-------EAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEiikeLRQLQ 597
|
....*....
gi 71990528 416 KENKTIVKE 424
Cdd:PRK00409 598 KGGYASVKA 606
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
218-514 |
1.87e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.20 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 218 TDKDDHVNVVNANLQIEVDQLHSEIEVIGKKKSDLENrlFDYEKLKAQFEQDE------NKLRA----DLEKKLkTSQEK 287
Cdd:PLN02939 91 TSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSD--FQLEDLVGMIQNAEknilllNQARLqaleDLEKIL-TEKEA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 288 LvkyEGKIEELQSRLNKKRKELeevqaenrKLLEDKNTHdfeldeAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDR 367
Cdd:PLN02939 168 L---QGKINILEMRLSETDARI--------KLAAQEKIH------VEILEEQLEKLRNELLIRGATEGLCVHSLSKELDV 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 368 QKELKLQLEKDMEDLRKEHEgQMAELEKRLEKVsEKEKEAIEQLEKiQKENKTIVKENVYLS-------------ESKQV 434
Cdd:PLN02939 231 LKEENMLLKDDIQFLKAELI-EVAETEERVFKL-EKERSLLDASLR-ELESKFIVAQEDVSKlsplqydcwwekvENLQD 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 435 LLESEIN--------------LKNELDEMAVKLRN------SQHQVAGLNEKISEEKRRRKKQDADVTRLDEQNQKLLRE 494
Cdd:PLN02939 308 LLDRATNqvekaalvldqnqdLRDKVDKLEASLKEanvskfSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKE 387
|
330 340
....*....|....*....|
gi 71990528 495 AQDSAELLEEvQKGKREIDH 514
Cdd:PLN02939 388 FQDTLSKLKE-ESKKRSLEH 406
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
360-654 |
1.92e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 360 ELEAEldrQKELKLQLEK--DMEDLRKEHEGQMAELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENvYLSES-KQvll 436
Cdd:PRK11281 53 LLEAE---DKLVQQDLEQtlALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRET-LSTLSlRQ--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 437 eseinLKNELDEMAVKLRNSQHQVAGLNEKI----SEEKRRRKKQDADVTRLDEQNQkLLREAQDSAELLEEVQKGKR-- 510
Cdd:PRK11281 126 -----LESRLAQTLDQLQNAQNDLAEYNSQLvslqTQPERAQAALYANSQRLQQIRN-LLKGGKVGGKALRPSQRVLLqa 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 511 EIDHLRQQLAHQSSEAGSVGQLQ-----------QKLAESEHREYLLQ-------LEL-ERVMK--MERDLDGRIEG--Y 567
Cdd:PRK11281 200 EQALLNAQNDLQRKSLEGNTQLQdllqkqrdyltARIQRLEHQLQLLQeainskrLTLsEKTVQeaQSQDEAARIQAnpL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 568 IRSEAAANNEL-ERLRKDT----------------------AEQ--KEKLEAM------------EMEARSKDLELADLT 610
Cdd:PRK11281 280 VAQELEINLQLsQRLLKATeklntltqqnlrvknwldrltqSERniKEQISVLkgslllsrilyqQQQALPSADLIEGLA 359
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 71990528 611 RKLAKAREEHetFEIN-ARNQFYavtgqmheDIESYKQRLLELEP 654
Cdd:PRK11281 360 DRIADLRLEQ--FEINqQRDALF--------QPDAYIDKLEAGHK 394
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
291-423 |
1.93e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 291 YEGKIEELQSRLnKKRKELEEVQA---------------ENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQ 355
Cdd:COG2433 348 YKNKFERVEKKV-PPDVDRDEVKArvirglsieealeelIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE 426
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71990528 356 EMLGELEAELDRQKELKLQLEKDMEDLRKEHEGQMAELEK---------RLEKVSEKEKEAIEQLEKIQKENKTIVK 423
Cdd:COG2433 427 AEVEELEAELEEKDERIERLERELSEARSEERREIRKDREisrldreieRLERELEEERERIEELKRKLERLKELWK 503
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
352-914 |
2.17e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 352 EQLQEMLGELEAELDRQKElklqleKDMEDLRKEHEGQMAELEKRLEKVSEKEKEAIEQLEKIQKenktivkenvylses 431
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEE------KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADE--------------- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 432 kqvLLESEINLKNELDEMAVKLRNSQhqvaglnEKISEEKRRRkkqDADVTRLDEQNQKLLREAQDSAELLEEVQKGKRE 511
Cdd:PRK02224 242 ---VLEEHEERREELETLEAEIEDLR-------ETIAETERER---EELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 512 IDHLRQQLAHQSSEAGSVGQ--LQQKLAESEHREyllqlELERVMKMERDLDGRIEGyIRSEAAA-NNELERLRKDTAEQ 588
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDrlEECRVAAQAHNE-----EAESLREDADDLEERAEE-LREEAAElESELEEAREAVEDR 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 589 KEKLEAMEMEARSKDLELADLTRKLAKAREEHETFEinarnqfyavtgqmhEDIESYKQRLLELEpypgkiisgsfrdfp 668
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR---------------EERDELREREAELE--------------- 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 669 sqtdpspattdAWMQTdVEEQLMVSPEVSLVSEAPSSLQDSRRSSHLD--EKLRRTIEKIGELLAEHESFQESLrDPEFH 746
Cdd:PRK02224 433 -----------ATLRT-ARERVEEAEALLEAGKCPECGQPVEGSPHVEtiEEDRERVEELEAELEDLEEEVEEV-EERLE 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 747 TAEAFRKISQLLKSILSGA-NSEEMLEriwtwltlKTKALVEQQDEQMKKVQKAGEMLLSQLREKEsdnEVLTKKSLEME 825
Cdd:PRK02224 500 RAEDLVEAEDRIERLEERReDLEELIA--------ERRETIEEKRERAEELRERAAELEAEAEEKR---EAAAEAEEEAE 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 826 AAAEEFRTYyNDMLTENDElrhRIVQLDEIREVESSNSTKIEK--GLREQLEQAQhELEKKKREYMW-KLQQKDEFYEIM 902
Cdd:PRK02224 569 EAREEVAEL-NSKLAELKE---RIESLERIRTLLAAIADAEDEieRLREKREALA-ELNDERRERLAeKRERKRELEAEF 643
|
570
....*....|..
gi 71990528 903 DRNVKETEKENK 914
Cdd:PRK02224 644 DEARIEEAREDK 655
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
328-900 |
2.51e-03 |
|
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: 41.88 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 328 FELDEAKVQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEHEGQMAELEKRLEKVSEKEKEA 407
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 408 IEQLEKIQKENKTIVKENVYLSESKQVlleSEINLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQ 487
Cdd:TIGR00618 253 EEQLKKQQLLKQLRARIEELRAQEAVL---EETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 488 NQKLLREAQDSAELLEEVQKGKREIDHLRQ----------QLAHQSSEAGSVGQLQQKLAESEHREYLLQLELERvmkmE 557
Cdd:TIGR00618 330 RAAHVKQQSSIEEQRRLLQTLHSQEIHIRDahevatsireISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDI----L 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 558 RDLDGRIEGYIRSEAAANNELERLRKDTAEQKEKLE----AMEMEARSKDLELADLTRKLAKAREehETFEINARNQFYA 633
Cdd:TIGR00618 406 QREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAElcaaAITCTAQCEKLEKIHLQESAQSLKE--REQQLQTKEQIHL 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 634 VTGQMHEDIESYKQRLLElEPYPGKIISGSFRDFPSQTDPSPATTDAWMQTDVEEQLMVSPEVSLVSEAPSSLQDSRRSS 713
Cdd:TIGR00618 484 QETRKKAVVLARLLELQE-EPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLK 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 714 HLDEKLRRTIEKIGELLAEHESFQESLRDPEFHTAEAFRKISQLLKSILsgANSEEMLERIWTWLTLKTKALVEQQ---D 790
Cdd:TIGR00618 563 EQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLA--CEQHALLRKLQPEQDLQDVRLHLQQcsqE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 791 EQMKKVQKAGEML--------LSQLREKESDNEVLTKKSLEMEAAAEEFR--TYYNDMLTENDELRHRIVQ----LDEIR 856
Cdd:TIGR00618 641 LALKLTALHALQLtltqervrEHALSIRVLPKELLASRQLALQKMQSEKEqlTYWKEMLAQCQTLLRELEThieeYDREF 720
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 71990528 857 EVESSNSTKIEKGLREQLEQAQHELEKKKREYMWKLQQKDEFYE 900
Cdd:TIGR00618 721 NEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHF 764
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
336-441 |
2.60e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 41.18 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 336 QGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEHEgqmaELEKRLEKVsEKEKEAIEQL-EKI 414
Cdd:smart00435 278 SMEKLQEKIKALKYQLKRLKKMILLFEMISDLKRKLKSKFERDNEKLDAEVK----EKKKEKKKE-EKKKKQIERLeERI 352
|
90 100
....*....|....*....|....*....
gi 71990528 415 QK-ENKTIVKEnvylsESKQVLL-ESEIN 441
Cdd:smart00435 353 EKlEVQATDKE-----ENKTVALgTSKIN 376
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
274-504 |
3.09e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 274 RADLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQAENRKlledknthdfELDEAKVQGEHLEKQRKEawekVEQ 353
Cdd:pfam07888 43 RAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKE----------ELRQSREKHEELEEKYKE----LSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 354 LQEMLGELEAELDRQKELKLQLEKDMEDLRKEHEGQMAELEKRLEKVSEKEKEAIEQLEKIQKENKTIVKENVYLSESKQ 433
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71990528 434 VLLESEINLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVTRLdEQNQKLLREAQDSAELLEE 504
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEEL-RSLQERLNASERKVEGLGE 258
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
433-621 |
3.32e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 433 QVLLESEINLKN-ELDEMAvklrnsqHQVAGLNEKISEEKRRRKKQDADVTRLdeqnqkllREAQDSAELLEEvqkgkrE 511
Cdd:PRK09039 41 QFFLSREISGKDsALDRLN-------SQIAELADLLSLERQGNQDLQDSVANL--------RASLSAAEAERS------R 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 512 IDHLRQQLAHQSSEA-GSVGQLQQKLAESEH--REYLLQLELervmkmerdldgriegyirseaaANNELERLRKDTAEQ 588
Cdd:PRK09039 100 LQALLAELAGAGAAAeGRAGELAQELDSEKQvsARALAQVEL-----------------------LNQQIAALRRQLAAL 156
|
170 180 190
....*....|....*....|....*....|....*
gi 71990528 589 KEKLEAMEMEARSKDLELADLTRKL--AKAREEHE 621
Cdd:PRK09039 157 EAALDASEKRDRESQAKIADLGRRLnvALAQRVQE 191
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
229-506 |
4.49e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 40.77 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 229 ANLQIEVDQLHSEIEVIGKKKSDLENRLFDYE-KLKAQFEQDENKL-----------RADLEKKLKTSQEKLVKYEGKIE 296
Cdd:NF033838 121 KELDAAFEQFKKDTLEPGKKVAEATKKVEEAEkKAKDQKEEDRRNYptntyktleleIAESDVEVKKAELELVKEEAKEP 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 297 ELQSRLNKKRKELEEVQAENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQE--------MLGELEAELDRQ 368
Cdd:NF033838 201 RDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKpkrrakrgVLGEPATPDKKE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 369 KELKLQL----EKDMEDLRKEHEGQMAELEKrleKVSEKEKEAIEQLEKIQKENKTIVKENVYL--SESKQVLLESEINL 442
Cdd:NF033838 281 NDAKSSDssvgEETLPSPSLKPEKKVAEAEK---KVEEAKKKAKDQKEEDRRNYPTNTYKTLELeiAESDVKVKEAELEL 357
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71990528 443 kneLDEMAVKLRNSqhqvaglnEKISEEKRRRKKQDADVTRLDE---QNQKLLREAQDSAELLEEVQ 506
Cdd:NF033838 358 ---VKEEAKEPRNE--------EKIKQAKAKVESKKAEATRLEKiktDRKKAEEEAKRKAAEEDKVK 413
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
276-532 |
4.59e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 276 DLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQAENRKLLEDkntHDFELDEAKVQGEHLEKQRKEAWEKVEQLQ 355
Cdd:PHA02562 185 TLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKT---IKAEIEELTDELLNLVMDIEDPSAALNKLN 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 356 EMLGELEAELDrqkelklQLEKDMEDLRKEHE-----GQMAELEKRLEKVSEKEKEAIEQLEKIqkeNKTIVKENVylse 430
Cdd:PHA02562 262 TAAAKIKSKIE-------QFQKVIKMYEKGGVcptctQQISEGPDRITKIKDKLKELQHSLEKL---DTAIDELEE---- 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 431 skqvlleseinLKNELDEMAVKLRnsqhqvaGLNEKISEEKRRRKKQDADVTRLDEQNQKLLREAQDSAELLEEVQKGKR 510
Cdd:PHA02562 328 -----------IMDEFNEQSKKLL-------ELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELD 389
|
250 260
....*....|....*....|..
gi 71990528 511 EIDHLRQQLAHQSSEAGSVGQL 532
Cdd:PHA02562 390 KIVKTKSELVKEKYHRGIVTDL 411
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
223-394 |
5.24e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 223 HVNVVNANLQIE----VDQLHSEIEvigkkKSDLENRLFDYEKLKAQFEQDENKLRAdLEKKLKTSQEKLVKYEGKIEEL 298
Cdd:COG4913 241 HEALEDAREQIEllepIRELAERYA-----AARERLAELEYLRAALRLWFAQRRLEL-LEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 299 QSRLNKKRKELEEVQAENRK--------LLEDKNTHDFELDEAKVQGEHLEKQ-----------RKEAWEKVEQLQEMLG 359
Cdd:COG4913 315 EARLDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRARLEALlaalglplpasAEEFAALRAEAAALLE 394
|
170 180 190
....*....|....*....|....*....|....*
gi 71990528 360 ELEAELDRQKELKLQLEKDMEDLRKEHEGQMAELE 394
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
340-621 |
5.31e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 340 LEKQRKEAWEKVEQLQEMLGELEAELDRQKELKLQLEKDMEDLRKEHEgqmAELEKRLEKVSEKEKEAIEQLEKIQKENK 419
Cdd:pfam01576 683 LERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFE---RDLQARDEQGEEKRRQLVKQVRELEAELE 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 420 TIVKENVYLSESKQVL------LESEINLKNELDEMAVK-LRNSQHQVAGLNEKISEEKRRRKKQDADVTRLDEQNQKLL 492
Cdd:pfam01576 760 DERKQRAQAVAAKKKLeldlkeLEAQIDAANKGREEAVKqLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLE 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 493 REAQDSAELLEEVQKGKREIDHLRQQLAHQSSEAGS---------------VGQLQQKLAESEHREYLLQLELERVMKME 557
Cdd:pfam01576 840 AELLQLQEDLAASERARRQAQQERDELADEIASGASgksalqdekrrlearIAQLEEELEEEQSNTELLNDRLRKSTLQV 919
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71990528 558 RDLDGRIEGYIRSEAAANNELERLRKDTAEQKEKLEAMEMEARSK-DLELADLTRKLAKAREEHE 621
Cdd:pfam01576 920 EQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKfKSSIAALEAKIAQLEEQLE 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
229-424 |
6.19e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 229 ANLQIEVDQLHSEIEVIGKKKSDLENRLfdyEKLKAQfeqdenklRADLEKKLKTSQEKLVKYEGKIEELQSRLnKKRKE 308
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEAALRDLESRL---GDLKKE--------RDELEAQLRELERKIEELEAQIEKKRKRL-SELKA 924
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 309 LEEVQAENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEKVEQLQEM----LGELEAELDRQKELKLQLEKDMEDLRk 384
Cdd:TIGR02169 925 KLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVnmlaIQEYEEVLKRLDELKEKRAKLEEERK- 1003
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 71990528 385 ehegqmaELEKRLEKVSEKEKEA-IEQLEKIQKENKTIVKE 424
Cdd:TIGR02169 1004 -------AILERIEEYEKKKREVfMEAFEAINENFNEIFAE 1037
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
276-411 |
6.49e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 276 DLEKKLKTSQEKLVKYEGKIEELQSRLNKKRKELEEVQA-----ENRKLLEDKNTHDFELDEAKVQGEHLEKQRKEAWEK 350
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkyseeEYEELREEYLELSRELAGLRAELEELEKRREEIKKT 695
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71990528 351 VEQLQEMLGELEAELDRQKELKLQLEkDMEDLRKEHEGQMAELEKR-LEKVSEKEKEAIEQL 411
Cdd:PRK03918 696 LEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALLKERaLSKVGEIASEIFEEL 756
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
275-596 |
6.92e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.71 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 275 ADLEKKLKTSQEKLVkyegkieELQSRLNKKRKELEEVQAENRKLLEDKNT--------------------HDFELDEAK 334
Cdd:COG3096 288 LELRRELFGARRQLA-------EEQYRLVEMARELEELSARESDLEQDYQAasdhlnlvqtalrqqekierYQEDLEELT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 335 VQGEHLEKQRKEAWEKVEQLQEMLGELEAELDRQKelklqlekdmedlrkeheGQMAELEKRLEkvsEKEKEAIEQLEKI 414
Cdd:COG3096 361 ERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLK------------------SQLADYQQALD---VQQTRAIQYQQAV 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 415 QKenktivkenvyLSESKQVLLESEI---NLKNELDEMAVKLRNSQHQVAGLNEK--ISEEKRRR--------KKQDADV 481
Cdd:COG3096 420 QA-----------LEKARALCGLPDLtpeNAEDYLAAFRAKEQQATEEVLELEQKlsVADAARRQfekayelvCKIAGEV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 482 TRLD--EQNQKLLREAQDSAELLEEVQKGKREIDHLRQQLAHQSseagSVGQLQQKLAESEHREYLLQLELERVMKMERD 559
Cdd:COG3096 489 ERSQawQTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQ----NAERLLEEFCQRIGQQLDAAEELEELLAELEA 564
|
330 340 350
....*....|....*....|....*....|....*..
gi 71990528 560 LDGRIEGYIRSEAAANNELERLRKDTAEQKEKLEAME 596
Cdd:COG3096 565 QLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARA 601
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
290-417 |
9.15e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 38.73 E-value: 9.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 290 KYEGKIEELQSRLNKKRKELEEVQAENRKLLEdknthdfELDEAKVQGEHLEKQRKEAwekvEQLQEMLGELEAELDrqk 369
Cdd:pfam13851 30 SLKEEIAELKKKEERNEKLMSEIQQENKRLTE-------PLQKAQEEVEELRKQLENY----EKDKQSLKNLKARLK--- 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 71990528 370 elklQLEKDMEDLRKEHEgqmaELEKRLEKVSEKEKEAIEQLEKIQKE 417
Cdd:pfam13851 96 ----VLEKELKDLKWEHE----VLEQRFEKVERERDELYDKFEAAIQD 135
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
250-628 |
9.43e-03 |
|
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: 40.21 E-value: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 250 SDLENRLFDYEKLKAQFEQDENKLRADLEKKLKTS----QEKLVKYEGKIEELQSRLNKKRKELEEVQAENRKLL-EDKN 324
Cdd:pfam12128 261 SHLHFGYKSDETLIASRQEERQETSAELNQLLRTLddqwKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLdADIE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 325 THDFELDEAKVQGEHLEKQRKEawekVEQLQEMLGELEAELDRQKEL-KLQLEKDMEDLRKEHEGQMAELEKRLEkVSEK 403
Cdd:pfam12128 341 TAAADQEQLPSWQSELENLEER----LKALTGKHQDVTAKYNRRRSKiKEQNNRDIAGIKDKLAKIREARDRQLA-VAED 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 404 EKEAIEQLEKIQKE-NKTIVKENVYLSESKQVLLESEINLKNELDEMAVKLRNSQHQVAGLNEKISEEKRRRKKQDADVT 482
Cdd:pfam12128 416 DLQALESELREQLEaGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELR 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 483 RLDEQNQKLLREAQDSAELLEEVQKgkrEIDHLRQQLAHQS--------SEAGSVGQLQQKLAESE--HREYLLQLELER 552
Cdd:pfam12128 496 QARKRRDQASEALRQASRRLEERQS---ALDELELQLFPQAgtllhflrKEAPDWEQSIGKVISPEllHRTDLDPEVWDG 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71990528 553 VMKMERDLDG------RIE--GYIRSEAAANNELERLRKDTAEQKEKLEAMEMEARSKDLELADLTRKLAKAREEHETFE 624
Cdd:pfam12128 573 SVGGELNLYGvkldlkRIDvpEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNAR 652
|
....
gi 71990528 625 INAR 628
Cdd:pfam12128 653 LDLR 656
|
|
|