|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
111-659 |
5.66e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 5.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 111 ESDLEAALVALLKREEDLHDAERKLLSDKNKLNRAKEELEKREKTISEASLKHESLQEELKRANVELASQAREIEELKHK 190
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 191 LRERDEERAALQSSLTLKEEELEKMRQEIANRSKEVSMAISEFESKSQLLSKANEVVKRQEGEIYALQRALEEKEEE--- 267
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEElee 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 268 -------LEISKATKKLEQEKLRETEANLKKQTEEWLIAQDEVNKLKEETVKRLGEANETMEDFMKVKKLLTDVRFELIS 340
Cdd:COG1196 384 laeelleALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 341 SREALVFSREQmeekeLLLEKQLEELEEQRKSVLSYMQSLRDAHTEVESERVKLRVVEAKNFALEREISVQKELLEDLRE 420
Cdd:COG1196 464 LLAELLEEAAL-----LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 421 ELQkekPLLELAMHDISVIQDELYKKANAFQVSQN--------LLQEKESSLVEAKLEIQHLKSEQASLELLLQEKDEEL 492
Cdd:COG1196 539 ALE---AALAAALQNIVVEDDEVAAAAIEYLKAAKagratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARY 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 493 AEARNKLGEVNQEVTELKALMISREDQLMEATEMLKEKDVHLHRIEGELGSSKLKVTEAEMVVERIAELTNRLLMSTTNG 572
Cdd:COG1196 616 YVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 573 QNQNAMRINNEISIDSMQQPLEkphddygmENKRLVMELSFTRENLRMKEMEVLAVQRALTFKDEEINV-VMGRLEAKEQ 651
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERL--------EEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELpEPPDLEELER 767
|
....*...
gi 18417960 652 ELKKLKEE 659
Cdd:COG1196 768 ELERLERE 775
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
121-409 |
9.87e-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: 68.94 E-value: 9.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 121 LLKREEDLHDAERKLLSDKNKLNRAKEELEKREKTISEASLKHESLQEELKRANVELASQAREIEELKHKLRERDEERAA 200
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 201 LQSSLTLKEEELEKMRQEIANRSKEV-----SMAISEFESKSQLLSKANEVVKRQEGEIYALQRALEEKEEELEISKATK 275
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 276 KLEQEKLRETEANLKKQTEEwliaQDEVNKLKEETVKRLGEANETMEDFMKVKKLLTDVRFELISSREALVFSREQMEEK 355
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKE----IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 18417960 356 ELLLEKQLEELEEQRKSVLSYMQSLRDAHTEVES---ERVKLRVVEAKNFALEREIS 409
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeEELSLEDVQAELQRVEEEIR 968
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
146-712 |
4.61e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 146 KEELEKREktISEASLKHESLQEELKRANVELASQAREIEELKHKLRERDEERAALQSSLTLKEEELEKMRQEIANRSKE 225
Cdd:COG1196 219 KEELKELE--AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 226 VSMAISEFESKSQLLSKANEVVKRQEGEIYALQRALEEKEEELEISKATKKLEQEKLRETEANLKKQTEEWLIAQDEVNK 305
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 306 LKEETVKRLGEANETMEDFMKVKKLLTDVRFELISSREALVFSREQMEEKELLLEKQLEELEEQRKSVLSYMQSLRDAHT 385
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 386 EVESERVKLRVVEAKNFALEREISVQKELLEDLREELQKEKPLLELAMHDISVIQdELYKKANAFQVSQNLLQEkesSLV 465
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK-AALLLAGLRGLAGAVAVL---IGV 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 466 EAKLEIQHLKSEQASLELLLQEKDEELAEARNKLGEVNQEVTELKALMISREDQLMEATEMLKEKDVHLHRIEGELGSSK 545
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 546 LKVTEAEMVVERIAELTNRLLMSttngqNQNAMRINNEISIDSMQQPLEKPHDDYGMENKRLVMELSFTRENLRMKEMEV 625
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAA-----LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 626 LAVQRALTFKDEEINVVMGRLEAKEQELKKLKEETINDSEDLKVLYALAQERVGEKTMGDLAIEMLQLEAANLEVEAATS 705
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
....*..
gi 18417960 706 ALQKLAK 712
Cdd:COG1196 768 ELERLER 774
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
110-319 |
5.43e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 5.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 110 LESDLEAALVALLKREEDLHDAERKLLSDKNKLNRAKEELEKREKTISEASLKHESLQEELKRANVELASQAREIEELKH 189
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 190 KLRERDEERAALQSSLTLKEEELEKMRQEIANRSKEVSMAISEFESKSQLLSKANEVVKRQEGEIYALQRALEEKEEELE 269
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 18417960 270 ISKATKKLEQEKLRETEANLKKQTEEWLIAQDEVNKLKEETVKRLGEANE 319
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
105-726 |
9.40e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.85 E-value: 9.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 105 SNLGVLESDLEAALVALLKREEDLHDAERKLLSDKNKLNR-------AKEELEKREKTISEASL-------KHESLQEEL 170
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRleqqkqiLRERLANLERQLEELEAqleelesKLDELAEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 171 KRANVELASQAREIEELKHKLRERDEERAALQSSLTLKEEELEKMRQEIANRSKEVSMAISEFESKSQLLSKANEVVKRQ 250
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 251 EGEIYALQRALEEKEEELEISK-ATKKLEQEKLRETEANLKKQTEEwliAQDEVNKLKEETVKRLGEANETMEDFMKVKK 329
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEE---LREELEEAEQALDAAERELAQLQARLDSLER 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 330 LLTDVRFELISSReALVFSREQMEEKELLLEKQLEELEEQRKSVLSYMQSLRDAHTEVESERVKL--------------- 394
Cdd:TIGR02168 497 LQENLEGFSEGVK-ALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAAKKaiaflkqnelgrvtf 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 395 ----RVVEAKNFALEREISVQKELLEDLREELQKEKPLLELAMHDI---SVIQDELykkANAFQVSQNLLQ--------- 458
Cdd:TIGR02168 576 lpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggVLVVDDL---DNALELAKKLRPgyrivtldg 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 459 --------------EKESSLVEAKLEIQHLKSEQASLELLLQEKDEELAEARNKLGEVNQEVTELKALMISREDQLMEAT 524
Cdd:TIGR02168 653 dlvrpggvitggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 525 EMLKEKDVHLHRIEGELGSSKLKVTEAEmvvERIAELTNRLLMSTTNGQNQNAMRINNEISIDSMQ---QPLEKPHDDYG 601
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELE---AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKeelKALREALDELR 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 602 MENKRLVMELSFTRENLRMKEMEVLAVQRALTFKDEEINVVMGRLEAKEQELKKLKEETINDSEDLKVLyaLAQERVGEK 681
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL--LNERASLEE 887
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 18417960 682 TMGDLAIEMLQLEAANLEVEAATSALQKLAKMSTELLTQADMSIE 726
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-352 |
2.82e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 110 LESDLEAALVALLKREEDLHDAERKLLSDKNKLNRAKEELEKREKTISEASLKHESLQEELKRANVELASQAREIEELKH 189
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 190 KLRERDEERAALQSSLTLKEEELEKMRQEIANRSKEVSMAISEFESKSQLLSKANEVVKRQEGEIYALQRALEEKEEELE 269
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 270 ISKAtkklEQEKLRETEANLKKQTEEWLIAQDEVNKLKEETVKRLGEANETMEDFMKVKKLLTDVRFELISSREALVFSR 349
Cdd:TIGR02168 856 SLAA----EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
...
gi 18417960 350 EQM 352
Cdd:TIGR02168 932 EGL 934
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
110-503 |
1.61e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 110 LESDLEAALVALLKREEDLHDAERKLLSDKNKLNRAKEELEKREKTISEASLKHESLQEELKRANVELASQAREIEELKH 189
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 190 KLRERDEERAALQSSLTLKEEELEKMRQEIANRSKEVSMAISEFESKSQLLSKANEVVKRQEGEIYALQRALEEKEEELE 269
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 270 ISKATKKLEQEKL---------------------RETEANLKKQTEEWLIAQDEVNKLKEetvKRLGEANETMEDFMKVK 328
Cdd:COG1196 509 GVKAALLLAGLRGlagavavligveaayeaaleaALAAALQNIVVEDDEVAAAAIEYLKA---AKAGRATFLPLDKIRAR 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 329 KLLTDVRFELISSREALVFSREQMEEKELLLEKQLEELEEQRKSVLSYMQSLRDAHTEVESERVKLRVVEAKNFALEREI 408
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 409 SVQKELLEDLREELQKEKPLLELAMHDISVIQDELYKKANAFQVSQNLLQEKESSLVEAKLEIQHLKSEQASLELLLQEK 488
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
410 420 430
....*....|....*....|....*....|....*...
gi 18417960 489 DEELAEA-----------------------RNKLGEVN 503
Cdd:COG1196 746 ELLEEEAleelpeppdleelerelerlereIEALGPVN 783
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
131-344 |
2.86e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 131 AERKLLSDKNKLNRAKEELEKREKTISEASLKHESLQEELKRANVELASQAREIEELKHKLRERDEERAALQSSLTLKEE 210
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 211 ELEKMRQEIANRSKEVSMA--------------ISEFESKSQLLSKANEVVKRQEGEIYALQRALEEKEEELEISKATKK 276
Cdd:COG4942 98 ELEAQKEELAELLRALYRLgrqpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18417960 277 LEQEKLRETEANLKKQTEEwliAQDEVNKLKEETVKRLGEANETMEDFMKVKKLLTDVRFELISSREA 344
Cdd:COG4942 178 ALLAELEEERAALEALKAE---RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
169-508 |
2.90e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 169 ELKRANVELASQAREIEELKHKLRERDEERAALQSSLTLKEEELEKMRQEIANRSKEVSMAISEFESKSQLLSKANEVVK 248
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 249 RQEGEIYALQRALEEKEEELEISKATKKLEQEKLRETEANLKKQTEEWLIAQDEVNKLKEE-TVKRLGEANETMEDFMKv 327
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaANLRERLESLERRIAAT- 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 328 KKLLTDVRFELISSREALVFSREQMEEKELLLEKQLEELEEQRKSVLSYMQSLRDAHTEVESERVKLRVVEAKNFALERE 407
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 408 ISVQKELLEDLREELQK----EKPLLELAMHDISVIQDELYKKANAFQVSQNLLQEKESSLvEAKLE---------IQHL 474
Cdd:TIGR02168 917 LEELREKLAQLELRLEGlevrIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRL-ENKIKelgpvnlaaIEEY 995
|
330 340 350
....*....|....*....|....*....|....
gi 18417960 475 KSEQASLELLLQEKdEELAEARNKLGEVNQEVTE 508
Cdd:TIGR02168 996 EELKERYDFLTAQK-EDLTEAKETLEEAIEEIDR 1028
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
112-309 |
1.44e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 112 SDLEAALVALLKREEDLHDAERKLLSD-----KNKLNRAKEELEKREKTISEASLKHESLQEELKRANVELASQAREIEE 186
Cdd:TIGR02169 261 SELEKRLEEIEQLLEELNKKIKDLGEEeqlrvKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 187 LKHKLRERDEERAALQSSLTLKEEELEKMRQEI--------------ANRSKEVSMAISEFESKSQLLSKANEVVKRQEG 252
Cdd:TIGR02169 341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELeevdkefaetrdelKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 18417960 253 EIYALQRALEEKEEELEISKATKKLEQEKLRETEANLKKQTEEWLIAQDEVNKLKEE 309
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
115-722 |
3.10e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 115 EAALVALLKREEdlHDAERKLLSDKNKLNRAK---EELEKREKTI---SEASLKHESLQEELKRanvelasqaREIEELK 188
Cdd:COG1196 163 EAAGISKYKERK--EEAERKLEATEENLERLEdilGELERQLEPLerqAEKAERYRELKEELKE---------LEAELLL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 189 HKLRERDEERAALQSSLTLKEEELEKMRQEIANRSKEVSMAISEFESKSQLLSKANEVVKRQEGEIYALQRAleekeeel 268
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD-------- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 269 eiskatKKLEQEKLRETEANLKKQTEEWLIAQDEVNKLKEETVKRLGEANETMEDfmkvkklltdvrfelissREALVFS 348
Cdd:COG1196 304 ------IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE------------------LEEAEAE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 349 REQMEEKELLLEKQLEELEEQRKSVLsymQSLRDAHTEVESERVKLRVVEAKNFALEREISVQKELLEDLREELQKEKPL 428
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELA---EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 429 LELAmhdisviqdelykkanafqvsQNLLQEKESSLVEAKLEIQHLKSEQASLELLLQEKDEELAEARNKLGEVNQEVTE 508
Cdd:COG1196 437 EEEE---------------------EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 509 LKALMISREDQLMEATEMLKEKDVHLHRIEGELGSSKLKVTEAEMVVERIAELTNRLLMSTTNGQNQNAMRINNEISIDS 588
Cdd:COG1196 496 LLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 589 mQQPLEKPHDDYGMENKRLVMELSFTRENLrmkemEVLAVQRALTFKDEEINVVMGRLEAKEQELKKLKEETINDSEDLK 668
Cdd:COG1196 576 -FLPLDKIRARAALAAALARGAIGAAVDLV-----ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 18417960 669 VLYALAQERVGEKTMGDLAIEMLQLEAANLEVEAATSALQKLAKMSTELLTQAD 722
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
129-352 |
4.74e-07 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 53.62 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 129 HDAERKLLSDKNKLNRAKEELEKRektiSEASLKHESLQEELKRANVELASQAREIEELKHKLRERDEERAALQSSLTLK 208
Cdd:pfam18971 609 YDEVKKAQKDLEKSLRKREHLEKE----VEKKLESKSGNKNKMEAKAQANSQKDEIFALINKEANRDARAIAYTQNLKGI 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 209 EEELEKMRQEIANRSKEVSMAISEFES-KSQLLSKANEVVKRQEGEIYALQRALEEKEEELEISKATKKLEQ------EK 281
Cdd:pfam18971 685 KRELSDKLEKISKDLKDFSKSFDEFKNgKNKDFSKAEETLKALKGSVKDLGINPEWISKVENLNAALNEFKNgknkdfSK 764
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18417960 282 LRETEANLKKQTEEWLIAQDEVNKLkeETVKRLGEANETMEDFMKVKKLLTDVRfelissrealVFSREQM 352
Cdd:pfam18971 765 VTQAKSDLENSVKDVIINQKVTDKV--DNLNQAVSVAKAMGDFSRVEQVLADLK----------NFSKEQL 823
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
103-530 |
4.96e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 103 PYSNLGVLEsDLEAALVALLKREEDLHDAERKLLSDKNKLNRAKEELEKREKTIS--EASLKHESLQEELKRANVELASQ 180
Cdd:COG4717 66 PELNLKELK-ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 181 AREIEELKHKLRERDEERAALQSsltlKEEELEKMRQEIANRSKEVSmaisefESKSQLLSKANEVVKRQEGEIYALQRA 260
Cdd:COG4717 145 PERLEELEERLEELRELEEELEE----LEAELAELQEELEELLEQLS------LATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 261 -LEEKEEELEISKATKKLEQEKLRETEANLKKQTEEWLIAQDEVNKLkeetvkrLGEANETMEDFMKVKKLLTDVRFELI 339
Cdd:COG4717 215 lEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLAL-------LGLGGSLLSLILTIAGVLFLVLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 340 SSREALVFSREQMEEKELLLEKQLEELEEQRKSVLSYMQSLRDAHTEVESERVKLRVVEAKNFALEREISVQKELLEDLR 419
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 420 EELQKEKPLLELAMHDIsviqDELYKKANAFQVSQNLLQEK---ESSLVEAKLEIQHL--KSEQASLELLLQEKDEELAE 494
Cdd:COG4717 368 LEQEIAALLAEAGVEDE----EELRAALEQAEEYQELKEELeelEEQLEELLGELEELleALDEEELEEELEELEEELEE 443
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 18417960 495 ARNKLGEVNQEVTELKALMISRE-----DQLMEATEMLKEK 530
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEedgelAELLQELEELKAE 484
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
141-478 |
7.28e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 7.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 141 KLNRAKEELEKREKTISEASLKHESLQEELKRANVE---------LASQAREIE--ELKHKLRERDEERAALQSSLTLKE 209
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRRErekaeryqaLLKEKREYEgyELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 210 EELEKMRQEIANRSKEVsmaisefESKSQLLSKANEVVKRQ-EGEIYALQRALEEKEEELEISKATKKLEQEKLRETEAN 288
Cdd:TIGR02169 251 EELEKLTEEISELEKRL-------EEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 289 LKKQTEEWLIAQDEVNKLKEETVKRLGEANETMEDFMKVKKLLTDVRFELISSREALVFSREQMEEKELLLEKQLEELEE 368
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 369 QRKSVLSYMQSLRDAHTEVESERVKLRVVEAKNFALEREisvqkeLLEDLREELQKEKPLLELAmHDISVIQDELYKKAN 448
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE------KEDKALEIKKQEWKLEQLA-ADLSKYEQELYDLKE 476
|
330 340 350
....*....|....*....|....*....|
gi 18417960 449 AFQVSQNLLQEKESSLVEAKLEIQHLKSEQ 478
Cdd:TIGR02169 477 EYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
179-558 |
8.79e-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: 52.75 E-value: 8.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 179 SQAREIEELKhklrerdEERAALQSSLTLKEEELEKMRQEIANRSKEVSMAISEFESKSQLLSKANEVVKRQEGEIYALQ 258
Cdd:TIGR02168 674 ERRREIEELE-------EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 259 RALEEKEEELEISKATKKLEQEKLRETEANLKKQTEEWLIAQDEVNKLKEETvkrlgEANETMedfmkvkklltdvrfel 338
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-----KALREA----------------- 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 339 issrealvfsreqmeekelllekqleeleeqrksvlsymqsLRDAHTEVESERVKLRVVEAKNFALEREISVQKELLEDL 418
Cdd:TIGR02168 805 -----------------------------------------LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 419 REELQKEKPLLELAMHDISVIQDELYKKANAFQVSQNLLQEKESSLVEAKLEIQHLKSEQASLELLLQEKDEELAEARNK 498
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18417960 499 LGEVNQEVTELKALMISREDQLMEATEMLKEKDVHLHR-IEGELGSSKLKVTEAEMVVERI 558
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENkIEDDEEEARRRLKRLENKIKEL 984
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
145-319 |
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: 50.60 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 145 AKEELEKREKTISEASLKHESLQEELKRANVELASQAREIEELKHKLRERDEERAALQSSLTLKEEELEKMRQEIANRSK 224
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 225 EVSMA---------------ISEFESKSQLLSKANEVVKRQEGEIYALQRALEEKEEELEISKATKKLEQEKLRETEANL 289
Cdd:COG3883 94 ALYRSggsvsyldvllgsesFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190
....*....|....*....|....*....|
gi 18417960 290 KKQTEEwliAQDEVNKLKEETVKRLGEANE 319
Cdd:COG3883 174 EAQQAE---QEALLAQLSAEEAAAEAQLAE 200
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
140-497 |
3.64e-06 |
|
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: 50.83 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 140 NKLNRAKEELEKREKTISEASLKHESLQEELKRAN--VELASQAREIEE--LKHKLRERDEERAALQSSLTLKEEELEKM 215
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSLERQAEKAEryKELKAELRELELalLVLRLEELREELEELQEELKEAEEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 216 RQEIANRSKEVSMAISEFESKSQLLSKANEVVKRQEGEIYALQRaleekeeeleiskaTKKLEQEKLRETEANLKKQTEE 295
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ--------------QKQILRERLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 296 WLIAQDEVNKLKEETVKRLGEANETMEDFMKVKKLLTDVRFELISSREALVFSREQMEEKELLLEKQLEELEEQRKSVLS 375
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 376 YmqslrdahtEVESERVKLRVVEAKNFALEREISVQKELLEDLREELQKEKPLLELAMHDISVIQDELYKKanafqvsQN 455
Cdd:TIGR02168 405 L---------EARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL-------RE 468
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 18417960 456 LLQEKESSLVEAKLEIQHLKSEQASLELLLQEKDEELAEARN 497
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
120-676 |
4.51e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 120 ALLKREEDLHDAERKLLSDKNKLNRAKEELEKREKTISEASLKHESLQEELKRANVELASQAREIEELKHKLRERDEERA 199
Cdd:PTZ00121 1228 AVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEA 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 200 ALQSSLTLKEEELEKMRQEIANRSKEVSMAISEFESKSQlLSKANEVVKRQEGEIYALQRALEEKEEELEISKA--TKKL 277
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE-AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAdaAKKK 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 278 EQEKLRETEAnlKKQTEEWLIAQDEVNKlKEETVKRLGEANETMEDFMKVKKLLTDVRfELISSREALVFSREQMEEKEL 357
Cdd:PTZ00121 1387 AEEKKKADEA--KKKAEEDKKKADELKK-AAAAKKKADEAKKKAEEKKKADEAKKKAE-EAKKADEAKKKAEEAKKAEEA 1462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 358 LLEKQLEELEEQRKsvlsymqslRDAHTEVESERVKLRVVEAKNFALEREISVQKELLEDLREELQKEKPLLELAMHDIS 437
Cdd:PTZ00121 1463 KKKAEEAKKADEAK---------KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEA 1533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 438 VIQDELyKKANAFQVSQNLLQEKESSLVEAKLEIQHLKSEQASLELLLQeKDEELAEARNKLGE----VNQEVTELKALM 513
Cdd:PTZ00121 1534 KKADEA-KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEevmkLYEEEKKMKAEE 1611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 514 ISREDQLMEATEMLKEKDVHLHRIEGELGSSKLKVTEAEMVveRIAELTNRLLMSTTNGQNQNAMRINNEISIDSMQQPL 593
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL--KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK 1689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 594 EKPHDDYGMENKRLVmelsftrENLRMKEMEVLAVQRALTFKDEEINVVMGRLEAKEQELKKLKEETINDSEDLKVLYAL 673
Cdd:PTZ00121 1690 AAEALKKEAEEAKKA-------EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHL 1762
|
...
gi 18417960 674 AQE 676
Cdd:PTZ00121 1763 KKE 1765
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-351 |
6.16e-06 |
|
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: 50.06 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 110 LESDLEAALVALLKRE-EDLHDAERKLLSDKNKLNRAKEELEKREKT----ISEASLKHESLQEELKRANVELASQAREI 184
Cdd:TIGR02168 218 LKAELRELELALLVLRlEELREELEELQEELKEAEEELEELTAELQEleekLEELRLEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 185 EELKHKLRERDEERAALQSSLTLKEEELEKMRQEIANRSKEVSMAISEFESKSQLLSKANEVVKRQEGEIYALQRALEEK 264
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 265 EEELEISK---ATKKLEQEKLRETEANLKKQTEEwliAQDEVNKLKEETVKRL-----GEANETMEDFMKVKKLLTDVRF 336
Cdd:TIGR02168 378 EEQLETLRskvAQLELQIASLNNEIERLEARLER---LEDRRERLQQEIEELLkkleeAELKELQAELEELEEELEELQE 454
|
250
....*....|....*
gi 18417960 337 ELISSREALVFSREQ 351
Cdd:TIGR02168 455 ELERLEEALEELREE 469
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
124-259 |
7.21e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 7.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 124 REEDLHDAERKLLSDKNKLNRAKEELEKREKTIseaslkhESLQEELKRANVELASQAREIEELKHKLRERDEERAALQS 203
Cdd:PRK12704 80 RRNELQKLEKRLLQKEENLDRKLELLEKREEEL-------EKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTA 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 18417960 204 SlTLKEEELEKMRQEIanrSKEVSMAISEFESKSQLLS--KANEVVkrqegeIYALQR 259
Cdd:PRK12704 153 E-EAKEILLEKVEEEA---RHEAAVLIKEIEEEAKEEAdkKAKEIL------AQAIQR 200
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
113-257 |
1.95e-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: 46.84 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 113 DLEAALVALLKREEDLHDAERKLLSDKNKLNRAKEELEKREKTiSEASLKHESLQEELKRANVELASQAREIEELKHKLR 192
Cdd:COG1579 35 ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-YEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEIL 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18417960 193 ERDEERAALQSSLTLKEEELEKMRQEIANRSKEVSMAISEFESK-SQLLSKANEVVKRQEGEIYAL 257
Cdd:COG1579 114 ELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAElEELEAEREELAAKIPPELLAL 179
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
115-407 |
4.78e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 115 EAALVALLKREEDLhdaERKLLSDKNKLNRAKEELEKREKTISEASLKHESLQEELKRANVEL-ASQAREIEELKHKLRE 193
Cdd:TIGR02169 222 EYEGYELLKEKEAL---ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkDLGEEEQLRVKEKIGE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 194 RDEERAALQSSLTLKEEELEKMRQEIANrskevsmAISEFESKSQLLSKANEVVKRQEGEIYALQRALEEKEEELEISKA 273
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEDAEERLAK-------LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 274 TKKLEQEKLRETEANLKKQTEEWLIAQDEVNKLKEETVKRLGEANETMEDFMKVKKLLTDVRFELISSREALVFSREQME 353
Cdd:TIGR02169 372 ELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK 451
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 18417960 354 EKELLLEKQLEELEEQRKSVLSYMQSLRDAHTEVESERVKLRVVEAKNFALERE 407
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
112-552 |
4.95e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 112 SDLEAALVALLKREEDLHDAERKLLSDKNKLNRAKEELEKREKTISEASLKHESLQEELKRANVELASQAREIEELKHKL 191
Cdd:PRK03918 196 KEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 192 RERDEERAALQSSLTLKEE----------------ELEKMRQEIANRSKEVSMAISEFESKSQLLSKANEVVK------- 248
Cdd:PRK03918 276 EELEEKVKELKELKEKAEEyiklsefyeeyldelrEIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKelekrle 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 249 RQEGEIYALQRALEEKEEELEISKATKKLEQEKLRETEANLKKQTEEWLIAQDEVNKLKEETVKRLGEANETMEDFMKVK 328
Cdd:PRK03918 356 ELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 329 KLLTDVRFELissrealvfSREQMEEKELLLEKQLEELEEQRKSVLSYMQSLRDAHTEVESERVKLRVVEAKNFALEREI 408
Cdd:PRK03918 436 GKCPVCGREL---------TEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 409 SVQKELLEDLREELQKEKPLLELAMH-------DISVIQDELyKKANAFQVSQNLLQEKESSLVEAKLEIQH-LKSEQAS 480
Cdd:PRK03918 507 ELEEKLKKYNLEELEKKAEEYEKLKEkliklkgEIKSLKKEL-EKLEELKKKLAELEKKLDELEEELAELLKeLEELGFE 585
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18417960 481 LELLLQEKDEELAEARNK---LGEVNQEVTELKALMISREDQLMEATEMLKEKDVHLHRIEGELGSSKLKVTEAE 552
Cdd:PRK03918 586 SVEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE 660
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
123-563 |
6.07e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 123 KREEDLHDAERKLLSDKNKLNRAKEELEKREKTISEASLKHESLQEELKRANVELASQAREIEELKHKLRERDEERAALQ 202
Cdd:PRK02224 199 KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 203 SSLTLKEEELEKMRQEIANRskevsMAISEFESKSQllskanEVVKRQEGEIYALQRALEEKEEELEISKATKKLEQEKL 282
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDL-----LAEAGLDDADA------EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 283 RETEANLKKQTEEwliaqdevnkLKEETVKRLGEANETMEDFMKVKKLLTDVRFELISSREALVFSREQMEEKELLLEKQ 362
Cdd:PRK02224 348 REDADDLEERAEE----------LREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 363 LEELEEQRKSVLSYMQSLRDAHTEVESERVKLRvvEAKNFALEREISVQKELLEDLREELQKEKplLELAMHDISVIQDE 442
Cdd:PRK02224 418 REERDELREREAELEATLRTARERVEEAEALLE--AGKCPECGQPVEGSPHVETIEEDRERVEE--LEAELEDLEEEVEE 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 443 LYKKAnafqvsqnllqEKESSLVEAKLEIQHLKSEQASLELLLQEKDEELAEARNKLGEVNQEVTELKALMISREDQLME 522
Cdd:PRK02224 494 VEERL-----------ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 18417960 523 ATEMLKEKDVHLHRIEGELGSSKLKVTEAEMVVERIAELTN 563
Cdd:PRK02224 563 AEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAD 603
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
139-318 |
8.95e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.00 E-value: 8.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 139 KNKLNRAKEELEKREKTISEASLkhESLQEELKRANVELASQAREIEELKHKLRERDEERAALqssltlkEEELEKMRQE 218
Cdd:COG2433 386 IEKELPEEEPEAEREKEHEEREL--TEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERL-------ERELSEARSE 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 219 I---ANRSKEVSMAISEFESKSQLLSKANEVVKRQEGEIYALQRALEEKEEELEIS-KATKKLEQEKLRETEANLKKQTE 294
Cdd:COG2433 457 ErreIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELVPvKVVEKFTKEAIRRLEEEYGLKEG 536
|
170 180
....*....|....*....|....
gi 18417960 295 EWLIAQDeVNKLKEETVKRLGEAN 318
Cdd:COG2433 537 DVVYLRD-ASGAGRSTAELLAEAG 559
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
130-681 |
9.54e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 130 DAERKLLSDKNKLNRAKEELEKREKT-ISEASLKHEslqEELKRANVELASQAREIEELKHKLRERDEERAALQSSLTLK 208
Cdd:PTZ00121 1174 DAKKAEAARKAEEVRKAEELRKAEDArKAEAARKAE---EERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERN 1250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 209 EEELEKMRQEIANRSKEVSMAI-SEFESKSQLLSKANEVVKRQEG----EIYALQRALEEKEEELEISKATKKLEQEKLR 283
Cdd:PTZ00121 1251 NEEIRKFEEARMAHFARRQAAIkAEEARKADELKKAEEKKKADEAkkaeEKKKADEAKKKAEEAKKADEAKKKAEEAKKK 1330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 284 ETEAnlKKQTEEWLIAqDEVNKLKEETVKRLGEANETMEDFMKVKKLLTDVRFELISSREALVFSREQMEEKELLLEKQL 363
Cdd:PTZ00121 1331 ADAA--KKKAEEAKKA-AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA 1407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 364 EELEEQRKSVLSYMQSLRDAHTEVESERVKLRVVEAKNFALEREISVQKELLEDLREELQKEKPllelamhdisviQDEL 443
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK------------ADEA 1475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 444 YKKANAFQVSQNLLQEKESSLVEAKlEIQHLKSEQASLELLLQEKDEELAEARNKLGEVNQEVTELKALMISREDQLMEA 523
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKAD-EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKA 1554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 524 TEMLKEKDVhlhriegELGSSKLKVTEAEMVVERIAELTNRLlmstTNGQNQNAMRINNEISIDSMQQPLEKPHDDYGME 603
Cdd:PTZ00121 1555 EELKKAEEK-------KKAEEAKKAEEDKNMALRKAEEAKKA----EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE 1623
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18417960 604 NKRLVMELSFTRENLRMKEMEVLAVQRALTfKDEEINVVMGRLEAKEQELKKLKEETINDSEDLKVLYALAQERVGEK 681
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELK-KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
122-668 |
2.11e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 122 LKREEDLHDAER-KLLSDKNKLNRAKEELEKREKTISEASLKHESLQEELKRANVELASQAREIEELK--HKLRERDEER 198
Cdd:PTZ00121 1121 KKKAEDARKAEEaRKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRkaEELRKAEDAR 1200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 199 AALQSSLTLKEEELEKMRQEIANRSKEVSMAISEFESKSQLLSKANEVVKRQEGEIYALQRALEEKEEELEIsKATKKLE 278
Cdd:PTZ00121 1201 KAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAI-KAEEARK 1279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 279 QEKLRETEAnlKKQTEEWLIAQD----EVNKLKEETVKRLGEANETMEDFMKVKKLLTDVRFELISSREALVFSREQMEE 354
Cdd:PTZ00121 1280 ADELKKAEE--KKKADEAKKAEEkkkaDEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD 1357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 355 KELLLEKQLEELEEQRKSVLSYMQSLRDAHTEV-ESERVKLRVVEAKNFA--LEREISVQKELLEDLREELQKEKPLLEL 431
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkKADEAKKKAEEDKKKAdeLKKAAAAKKKADEAKKKAEEKKKADEAK 1437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 432 AMHDISVIQDELYKKANAFQVSQNLLQEKESSlveAKLEIQHLKSEQASLELLLQEKDEEL----------AEARNKLGE 501
Cdd:PTZ00121 1438 KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA---KKADEAKKKAEEAKKADEAKKKAEEAkkkadeakkaAEAKKKADE 1514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 502 VNQEVTELKALMISREDQLMEATEMLKEKDV----HLHRIEG-ELGSSKLKVTEAEMVVERIAELTNR--LLMSTTNGQN 574
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADEAKKAEEKkkadELKKAEElKKAEEKKKAEEAKKAEEDKNMALRKaeEAKKAEEARI 1594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 575 QNAMRINNEISIDSMQQPLEKPHDDYGMENKRLVMELSFTRENLRMKEMEVLAVQRALTFKDEEINVVMGRLEAKEQELK 654
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
570
....*....|....
gi 18417960 655 KLKEETINDSEDLK 668
Cdd:PTZ00121 1675 KKAEEAKKAEEDEK 1688
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
121-310 |
2.53e-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: 44.63 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 121 LLKREEDLHDAERKLLSDKNKLNRAKEELEKREKTISEASLKHESLQEELKRANVELASQAREIEELKHKLRERDEERAA 200
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 201 LQSSLTLKEEELEKMRQEIANRSKEVSMAISEFESKSQLLSKANEVVKRQEGEIYALQRALEEKEEELEISKATKKLEQE 280
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475
|
170 180 190
....*....|....*....|....*....|
gi 18417960 281 KLRETEANLKKQTEEWLIAQDEVNKLKEET 310
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
126-344 |
2.90e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 126 EDLHDAERKLLSDKNKLNRAKEELEKREKTISE-ASLKHESLQEELKRANVELASQAREIEELKHKLRERDEERAALQSs 204
Cdd:PRK05771 43 ERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEkKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQ- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 205 ltlKEEELEKMRQ-----EIANRSKEVS-----MAISEFESKSQLLSKANEVVKRQ-EGEIYALqrALEEKEEELEISKA 273
Cdd:PRK05771 122 ---EIERLEPWGNfdldlSLLLGFKYVSvfvgtVPEDKLEELKLESDVENVEYISTdKGYVYVV--VVVLKELSDEVEEE 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18417960 274 TKKLEQEKLR-ETEANLKKQTEEWLIAQDEVNKLKEETVKRLGEANETMEDFMKV--KKLLTDVRFELISSREA 344
Cdd:PRK05771 197 LKKLGFERLElEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLAlyEYLEIELERAEALSKFL 270
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
111-307 |
3.15e-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: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 111 ESDLEAALVALLKREEDLHDAERKLLSDKNKLnRAKEELEKREKTISEASLKHESLQEELKRANVELASQA-----REIE 185
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQI-ELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRlelleAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 186 ELKHKLRERDEERAALQSSLTLKEEELEKMRQEIANRS--------KEVSMAISEFESKSQLLSKANEVVKRQEGEIY-- 255
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGgdrleqleREIERLERELEERERRRARLEALLAALGLPLPas 378
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 18417960 256 --ALQRALEEKEEELEISKATKKLEQEKLRETEANLKKQTEEWLIAQDEVNKLK 307
Cdd:COG4913 379 aeEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-659 |
3.21e-04 |
|
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: 44.28 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 107 LGVLESDLEAALVALLKREEDLHDAERKLLSDKNKLNRAKEELEKREKTISEASLKHESLQEELKRANVELASQAREIEE 186
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 187 LKHKLRErdEERAALQSSLTLKEEELEKMRQEIANRSKEVSMAISEFESKSQLLSKANEVVKRQEGEIYALQRaleEKEE 266
Cdd:TIGR02168 426 LLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER---LQEN 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 267 ELEISKATKKLEQEKLR------------ETEANLKKQTEEWL-------------IAQDEVNKLKEETVKRL------- 314
Cdd:TIGR02168 501 LEGFSEGVKALLKNQSGlsgilgvlseliSVDEGYEAAIEAALggrlqavvvenlnAAKKAIAFLKQNELGRVtflplds 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 315 ----------GEANETMEDFMKV-----------------------------------KKLLTDVRF-----ELISSREA 344
Cdd:TIGR02168 581 ikgteiqgndREILKNIEGFLGVakdlvkfdpklrkalsyllggvlvvddldnalelaKKLRPGYRIvtldgDLVRPGGV 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 345 LVFSREQMEEKELLLEKQLEELEEQRKSVLS-------YMQSLRDAHTEVESERVKLRVVEaknFALEREISVQKELLED 417
Cdd:TIGR02168 661 ITGGSAKTNSSILERRREIEELEEKIEELEEkiaelekALAELRKELEELEEELEQLRKEL---EELSRQISALRKDLAR 737
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 418 LREELQKEKPLLELAMHDISVIQDELYKKANAFQVSQNLLQEKESSLVEAKLEIQHLKSEQASLELLLQEKDEELAEARN 497
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 498 KLGEVNQEVTELKALMISREDQLMEATEMLKEKDVHLHRIEGELGSSKLKVTEAEmvvERIAELTNRL-----LMSTTNG 572
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE---SELEALLNERasleeALALLRS 894
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 573 QNQNAMRINNEISIDSMQ-----QPLEKPHDDYGMENKRLVMELSFTRENLRMKEMEVLAVQRALTFKDEEinvvmgRLE 647
Cdd:TIGR02168 895 ELEELSEELRELESKRSElrrelEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIED------DEE 968
|
650
....*....|..
gi 18417960 648 AKEQELKKLKEE 659
Cdd:TIGR02168 969 EARRRLKRLENK 980
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
107-712 |
4.71e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 107 LGVLESDLEAALVALLKREEDLHDAERKLLSDKNKLNRAKEELEKREKTISEAS----------LKHESLQEELKRANVE 176
Cdd:pfam02463 288 LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEkelkeleikrEAEEEEEEELEKLQEK 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 177 LASQAREIEELKHKLRERDEERAALQSSLTLKEEELEKMRQEIANRSKEVSMAISEFESKSQLLSKANEVVKRQEGEIYA 256
Cdd:pfam02463 368 LEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLT 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 257 LQRALEEKEEELEISKATKKLEQEKLRETEANLKKQT--EEWLIAQDEVNKLKEETVKRLGEANETMEDFMKVKKLLTDV 334
Cdd:pfam02463 448 EEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEqlELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISA 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 335 RFELISSREALVFSREQMEEKELLLEKQLEELEEQRKSVLSYMQSLRDAHTEVESERVKLRVVEAKNFALEREISVQKEL 414
Cdd:pfam02463 528 HGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQ 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 415 LEDLREELQ-KEKPLLELAMHDISVIQDELYKKANAFQVS---QNLLQEKESSLVEAKLEIQHLKSEQASLELLLQEKDE 490
Cdd:pfam02463 608 LDKATLEADeDDKRAKVVEGILKDTELTKLKESAKAKESGlrkGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAES 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 491 ELAEARNKLGEVNQEVTELKALMISREDQLMEATEMLKEKDVHLHRIEGELGSSKLKVTEAEMVVERIAELTNRLLMSTT 570
Cdd:pfam02463 688 ELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKS 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 571 NGQNQNAMRINNEISIDSMQQPLEKPHDDYGMENKRLVMELSFTRENLRMKEMEVLAVQRALTfKDEEINVVMGRLEAKE 650
Cdd:pfam02463 768 ELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKI-KEEELEELALELKEEQ 846
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18417960 651 QELKKLKEETINDSEDLKVLYALAQERVGEKTMGDLAIEMLQLEAANLEVEAATSALQKLAK 712
Cdd:pfam02463 847 KLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQK 908
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
110-232 |
6.97e-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: 41.83 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 110 LESDLEAALVALLKREEDLHDAERKLLSDKNKLNRAK--EELEKREKTISEASLKHESLQEELKRANVELASQAREIEEL 187
Cdd:COG1579 50 AKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAEL 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 18417960 188 KHKLRERDEERAALQSSLTLKEEELEKMRQEIANRSKEVSMAISE 232
Cdd:COG1579 130 EAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
130-324 |
7.90e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 130 DAERKLLSDKNKLNRAKEELEKREKTISEASLKHESLQE---------ELKRANVELASQAREIEELKHKLRERDE---E 197
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQErrealqrlaEYSWDEIDVASAEREIAELEAELERLDAssdD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 198 RAALQSSLTLKEEELEKMRQEIANRSKEVSMAISEFESKSQLLSKANEVVKRQEGEIYALQRALeekeeeleiskATKKL 277
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL-----------LEERF 755
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 18417960 278 EQEKLRETEANLKKQteewliAQDEVNKLKEETVKRLGEANETMEDF 324
Cdd:COG4913 756 AAALGDAVERELREN------LEERIDALRARLNRAEEELERAMRAF 796
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
110-296 |
9.59e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 110 LESDLEAALVALLKREEDLHDAERKLLSDKNKLNRAKEELEKREKTISEASLKHESLQEELKRANVELASQ--------- 180
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlralyrlgr 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 181 --------------------------AREIEELKHKLRERDEERAALQSSLTLKEEELEKMRQEIANRSKEVSMAISEfe 234
Cdd:COG4942 119 qpplalllspedfldavrrlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE-- 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18417960 235 sKSQLLSKANEVVKRQEGEIYALQRAleEKEEELEISKATKKLEQEKLRETEANLKKQTEEW 296
Cdd:COG4942 197 -RQKLLARLEKELAELAAELAELQQE--AEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
117-285 |
9.75e-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: 41.45 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 117 ALVALLKREEDLHDAERKLLSDKNKLNRAKEELEKREKTISEASLKHESLQEELKRANVELASQAREIEELKHKLrERDE 196
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI-KKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 197 ERaaLQSSLTLKE-----EELEKMRQEIANRSKEVSMAISEFESKSQLLSKANEVVKRQEGEIYALQRALEEKEEELEIS 271
Cdd:COG1579 80 EQ--LGNVRNNKEyealqKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170
....*....|....
gi 18417960 272 KATKKLEQEKLRET 285
Cdd:COG1579 158 LEELEAEREELAAK 171
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
461-695 |
1.13e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 461 ESSLVEAKLEIQHLKSEQASLELLLQEKDEELAEARNKLGEVNQEVTELKALMISREDQLMEATEMLKEKDVHLHRIEGE 540
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 541 LGSsklkvteaemVVERIAELTNRLlmsttngqnqnamrinneisidsmqQPLEKPHDDYGMENKRLVMELSFTRENLRM 620
Cdd:TIGR02169 387 LKD----------YREKLEKLKREI-------------------------NELKRELDRLQEELQRLSEELADLNAAIAG 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18417960 621 KEMEVLAVQRALTFKDEEINVVMGRLEAKEQELKKLKEETINDSEDLKVLyalaqervgEKTMGDLAIEMLQLEA 695
Cdd:TIGR02169 432 IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV---------EKELSKLQRELAEAEA 497
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
168-709 |
1.31e-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: 42.26 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 168 EELKRANVELASQAREIEELKHKLRERDEERaaLQSSLTLKEEELEKMRQEIANRSKEVSMAISEFESKSQLLSKANEVV 247
Cdd:TIGR00618 112 EQKKGRGRILAAKKSETEEVIHDLLKLDYKT--FTRVVLLPQGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKK 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 248 KRQEGEIYALQRALEEKEEELEISKATKKLEQEKLRETEANLK------KQTEEWLIAQDEVNKLKEETVKRLGEANETM 321
Cdd:TIGR00618 190 KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLRealqqtQQSHAYLTQKREAQEEQLKKQQLLKQLRARI 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 322 EDFMKVKKLLTDVRFELISSREALVFSRE-----QMEEKELLLEKQLEELEEQRKSVLSYMQSLRDAHTEVESERVKLRV 396
Cdd:TIGR00618 270 EELRAQEAVLEETQERINRARKAAPLAAHikavtQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQT 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 397 VEAKNFALEREISVQKELLEDLREELQKEKPLLELAMhdisviqdelyKKANAFQVSQNLLQEKESSLVE-AKLEIQHLK 475
Cdd:TIGR00618 350 LHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQ-----------QKTTLTQKLQSLCKELDILQREqATIDTRTSA 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 476 SEQASLELLLQEKDEELAEARNKLGEvnQEVTELKALMISREDQLMEATEMLKEKDVHLHRIEGELGSSKLKVTEAEMVV 555
Cdd:TIGR00618 419 FRDLQGQLAHAKKQQELQQRYAELCA--AAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARL 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 556 ERIAELtNRLLMSTTNGQNQNAMRINNEISIDSMQQPLEKPHDDYGMENKRLVMELSFTRENL-RMKEMEVLAVQ--RAL 632
Cdd:TIGR00618 497 LELQEE-PCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRaSLKEQMQEIQQsfSIL 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 633 TFKDEEINVVMGRLEAKEQELKKLKEETiNDSEDLKVLYALAQERVGEKTMGDLAI--------EMLQLEAANLEVEAAT 704
Cdd:TIGR00618 576 TQCDNRSKEDIPNLQNITVRLQDLTEKL-SEAEDMLACEQHALLRKLQPEQDLQDVrlhlqqcsQELALKLTALHALQLT 654
|
....*
gi 18417960 705 SALQK 709
Cdd:TIGR00618 655 LTQER 659
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
110-258 |
1.92e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 110 LESDLEAALVALLKREEDLHDAERKLLSDKNKLNRAKEELEKREKTISEASLKHESLQEELKRANVELASQAREIEELKH 189
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18417960 190 KLRERDEERAALQSSLTLKEEELEKMRQEIANRSKEVSMAISEFESKSQLLSKANEVVKRQEGEIYALQ 258
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK 475
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
172-302 |
2.06e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 172 RANVELASQAREIEELKHKLRERDEERAAL-QSSLTLKEEELEKMRQEIANRSKEVSMAISEFESKSQLLSKANEVVKR- 249
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALkKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEl 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 250 --QEGEIYALQRALEEKEEELE------------------ISKAT----KKL---EQEKLRETEANLKKQteewLIAQDE 302
Cdd:COG0542 481 eqRYGKIPELEKELAELEEELAelapllreevteediaevVSRWTgipvGKLlegEREKLLNLEEELHER----VIGQDE 556
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
116-554 |
2.82e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 116 AALVALLKREEDLHDAERKLLSDKNKLNRAKEELEKREKTISEASLKHESLQEELKRANVELASQAREIEELKHKLRERD 195
Cdd:PTZ00121 1266 ARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 196 EERAALQSSLTLKEEELEKMRQEIANRSKEVSMAISEFESKSQLLSKANEVVKRQE------GEIYALQRALEEKEEELE 269
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEedkkkaDELKKAAAAKKKADEAKK 1425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 270 ISKATKKLEQEKLRETEA----NLKKQTEEWLIAQDEVNKLKE----ETVKRLGEANETMEDFMKVKKLLTDVRFELISS 341
Cdd:PTZ00121 1426 KAEEKKKADEAKKKAEEAkkadEAKKKAEEAKKAEEAKKKAEEakkaDEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 342 REALVFSREQMEEKELLLEKQLEELEEQRKS-VLSYMQSLRDAHTEVESERVK----LRVVEAKNFALEREISVQKELLE 416
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKAdEAKKAEEKKKADELKKAEELKkaeeKKKAEEAKKAEEDKNMALRKAEE 1585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 417 DLREELQKEKPLLELAMHDISVIQDELYKKANAFQVSQNLLQEKESSLVEAKLEIQHLKSEQASLELLLQEKDEEL--AE 494
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIkaAE 1665
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 495 ARNKLGEVNQEVTELKalmiSREDQLMEATEMLKEKDVHLHRIEGELGSSKLKVTEAEMV 554
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAK----KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
123-226 |
3.00e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 123 KREEDLHDAERKLLSDKNKLNRAKEELEKREKTISEaslKHESLQEELKRANVELASQAREIeelkhkLRERDEERAALQ 202
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEE---LIEEQLQELERISGLTAEEAKEI------LLEKVEEEARHE 170
|
90 100
....*....|....*....|....
gi 18417960 203 SSLTLKEEElEKMRQEIANRSKEV 226
Cdd:PRK12704 171 AAVLIKEIE-EEAKEEADKKAKEI 193
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
104-221 |
3.21e-03 |
|
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: 41.20 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 104 YSNLGVLESDLEAALVALLKREEDLHDAERKLLSDKNKLNRAKEELEKREKTISEASLKH----ESLQEELKRANVELAS 179
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlnerASLEEALALLRSELEE 898
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 18417960 180 QAREIEELKHKLRERDEERAALQSSLTLKEEELEKMRQEIAN 221
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
178-598 |
3.29e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 178 ASQAREIEELKHKLRERDEERAALQSSLTLKEEELEKMRQEIANRSKEVSMAISEFESKSQLLSKANEVVKRQEGEIYAL 257
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 258 QRALEEkeeeleiskatkklEQEKLRETEANLKKQTEEWLIAQDEVNKLkeetvkrlgEANETMEDFMKVKKLLTDVRFE 337
Cdd:TIGR02169 750 EQEIEN--------------VKSELKELEARIEELEEDLHKLEEALNDL---------EARLSHSRIPEIQAELSKLEEE 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 338 LISSREALvfsreqmeekelllekqlEELEEQRKSVLSYMQSLRDAHTEVESERVKLRVVEAKNFALEREISVQKELLED 417
Cdd:TIGR02169 807 VSRIEARL------------------REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 418 LREELQKEKPLLELAMHDISVIQDELYKKANAFQVSQNLL----QEKESSLVEAKLEIQHLKSEQASLELLLQEkDEELA 493
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELeaqiEKKRKRLSELKAKLEALEEELSEIEDPKGE-DEEIP 947
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 494 EARNKLGEVNQEVTELKALMISREDQLMEATEMLKEKDVHLHRIEGELgsSKLKvTEAEMVVERIAELTNR---LLMSTT 570
Cdd:TIGR02169 948 EEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKR--AKLE-EERKAILERIEEYEKKkreVFMEAF 1024
|
410 420
....*....|....*....|....*...
gi 18417960 571 NGQNQNAMRINNEISIDSMQQPLEKPHD 598
Cdd:TIGR02169 1025 EAINENFNEIFAELSGGTGELILENPDD 1052
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
191-733 |
3.36e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 191 LRERDEERAALQSSLTLKEEELEKMRQEIANR--------SKEVSMAISEFE--------SKSQLLSKAN------EVVK 248
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKielllqqhQDRIEQLISEHEveitglteKASSARSQANsiqsqlEIIQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 249 ---RQEGEIYALQRALEEKEEELEIS--KATKKLEQEKLRETEANLKKQTEEWLIAQDEVNKLKEETVKRLGEANETMED 323
Cdd:pfam15921 306 eqaRNQNSMYMRQLSDLESTVSQLRSelREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLAD 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 324 FMKVKKLLTdvrfeLISSREALVFSREQMEEKELLLEKQLEELEEQRKSVLSYMQSLRDAHTEVESERvKLRVVEAKNFA 403
Cdd:pfam15921 386 LHKREKELS-----LEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMER-QMAAIQGKNES 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 404 LER------EISVQKELLEDLREELQKEKPLLELAMHDISVIQDELYKKANAFQVSqNLLQEKESSLVEAKL-EIQHLKS 476
Cdd:pfam15921 460 LEKvssltaQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAT-NAEITKLRSRVDLKLqELQHLKN 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 477 EQ----------ASLELLLQEKDEELAEARNKLGEVNQ--------------EVTELKALMISREDQLMEATEMLKEKDV 532
Cdd:pfam15921 539 EGdhlrnvqtecEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagamqvEKAQLEKEINDRRLELQEFKILKDKKDA 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 533 HLHRIEGELGSSKLKV-------TEAEMVVERIAELTNRLLMSTTNGQNQ-NAMRINNEI---SIDSMQQPLEKPHDDYG 601
Cdd:pfam15921 619 KIRELEARVSDLELEKvklvnagSERLRAVKDIKQERDQLLNEVKTSRNElNSLSEDYEVlkrNFRNKSEEMETTTNKLK 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 602 MENKRLVMELSFTRENLRMKE------MEV-LAVQRALTFKDEEINVVMGRLEAKEQELKK-------LKEETINDSEDL 667
Cdd:pfam15921 699 MQLKSAQSELEQTRNTLKSMEgsdghaMKVaMGMQKQITAKRGQIDALQSKIQFLEEAMTNankekhfLKEEKNKLSQEL 778
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18417960 668 KVLYALAQERVGEKTMGDLAIEMLQLEAANLEVEAATSALQkLAKMSTELLTQADMSIEADTTHTV 733
Cdd:pfam15921 779 STVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQ-FAECQDIIQRQEQESVRLKLQHTL 843
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
98-220 |
3.62e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 98 DDDDLPYSNLgVLESDLEAALVALLKREEDLHDAERKLLSDKNKLNRAKEELEKREKTI------SEASLKHESLQEE-- 169
Cdd:COG4913 593 DDRRRIRSRY-VLGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeySWDEIDVASAEREia 671
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 18417960 170 --------LKRANVELASQAREIEELKHKLRERDEERAALQSSLTLKEEELEKMRQEIA 220
Cdd:COG4913 672 eleaelerLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
139-250 |
5.62e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 139 KNKLNRAKEELEKrektiseasLKHEsLQEELKRANVELASQAREIEELKHKLRERDEERAALQSSLTLKEEELEKMRQE 218
Cdd:PRK12704 56 KEALLEAKEEIHK---------LRNE-FEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQE 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 18417960 219 IANRSKEVS-------------MAISEFESKSQLLSKANEVVKRQ 250
Cdd:PRK12704 126 LEKKEEELEelieeqlqeleriSGLTAEEAKEILLEKVEEEARHE 170
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
138-248 |
8.74e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.42 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 138 DKNKLNRAKEELEKREKTISEASLKHESLQEELKRANVELASQAREIEELKHKLRERDEERAalQSSLTLKEEELEKMRQ 217
Cdd:PRK00409 514 DKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEA--QQAIKEAKKEADEIIK 591
|
90 100 110
....*....|....*....|....*....|...
gi 18417960 218 EIANRSKEVSMAISEFESKS--QLLSKANEVVK 248
Cdd:PRK00409 592 ELRQLQKGGYASVKAHELIEarKRLNKANEKKE 624
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
110-406 |
8.94e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 110 LESDLEAALVALLKREEDLHDAERKLLSDKNKLNRAKEELEKREKTISEASLKHESLQEELKRANVELASQAREIEELKH 189
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 190 KLRERDEERAALQSSLTLKEEELEKMRQEIANRSKEVSMAISEFESKSQLLSKANEVVKRQEGEIYALQRALEEKEEELE 269
Cdd:COG4372 123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEEL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 270 ISKATKKLEQEKLRETEANLKKQTEEWLIAQDEVNKLKEETVKRLGEANETMEDFMKVKKLLTDVRFELISSREALVFSR 349
Cdd:COG4372 203 AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAA 282
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 18417960 350 EQMEEKELLLEKQLEELEEQRKSVLSYMQSLRDAHTEVESERVKLRVVEAKNFALER 406
Cdd:COG4372 283 LELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
456-716 |
9.24e-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: 39.82 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 456 LLQEKESSLVEAKLEIQHLKSEQASLELLLQEKDEELAEARNKLG-EVNQEVTELKALMISREDQLMEATEMLKEKDVHL 534
Cdd:pfam12128 245 KLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNqLLRTLDDQWKEKRDELNGELSAADAAVAKDRSEL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 535 HRIEgelgsSKLKVTEAEMVVERIAELTNRLLMStTNGQNQNAMRINNEISIDSMQQPLEKPHDDYGMENKRLVMELSFT 614
Cdd:pfam12128 325 EALE-----DQHGAFLDADIETAAADQEQLPSWQ-SELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 615 RENLRMKEMEVLAVQRALTFKDEeiNVVMGRLEAKEQELKKLKEETINDSEDLKVLYALAQ---ERVGEKTMGDLAIEML 691
Cdd:pfam12128 399 LAKIREARDRQLAVAEDDLQALE--SELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATatpELLLQLENFDERIERA 476
|
250 260
....*....|....*....|....*..
gi 18417960 692 Q--LEAANLEVEAATSALQKLAKMSTE 716
Cdd:pfam12128 477 ReeQEAANAEVERLQSELRQARKRRDQ 503
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
141-323 |
9.83e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 141 KLNRAKEELEKREKTISEASLKHESLQEELKRANVELASQAREIEELKHKLRERDEERAALQSSLTLKEEELEKMRQEIA 220
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18417960 221 NRSKEVSMAISEFESKSQLLSKANEVVKRQEGEIYALQ-RALEEKEEELEISKATKKLEQEKLRETEANLKKQTEEWLIA 299
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEeQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEK 198
|
170 180
....*....|....*....|....
gi 18417960 300 QDEVNKLKEETVKRLGEANETMED 323
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEELLE 222
|
|
| |
