|
Name |
Accession |
Description |
Interval |
E-value |
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
5-795 |
0e+00 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 907.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 5 QNVEEKISFTKIRELIKEECSGPLGIQFVDKMSFSKDLSLVSRLLEQTDEFKKIIGSGELFPSSNYTDANPYLDKARIeG 84
Cdd:COG1193 3 EKTLEKLEFDKILELLAEYAVSELGKELARKLRPSTDLEEVERLLAETAEARRLLRLEGGLPLGGIPDIRPLLKRAEE-G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 85 SFLDQEEFHEIRLSLFTLSRCIEFFKDHEEAYPSLFALLGLVALDNTVLRAIERILDEKGKIRNNASQELSLIRSQILYE 164
Cdd:COG1193 82 GVLSPEELLDIARTLRAARRLKRFLEELEEEYPALKELAERLPPLPELEKEIDRAIDEDGEVKDSASPELRRIRREIRSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 165 ENRLRKVLDRIFREAKSKGMTPDdASITVRGGRMVIPVLAENKRKIKGFIHDESATGQTVYLEPAEVLDINNELKDLEYM 244
Cdd:COG1193 162 EQRIREKLESILRSASYQKYLQD-AIITIRNGRYVIPVKAEYKGKIPGIVHDQSASGQTLFIEPMAVVELNNELRELEAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 245 ERREIQRILTKLTDTMRPFIPEMRKAYHFLGMVDFIRAKAKFAIKTNSHKPILKKERQLQWSDARHPLLEFalkqvgKKV 324
Cdd:COG1193 241 ERREIERILRELSALVREYAEELLENLEILAELDFIFAKARYALELKAVKPELNDEGYIKLKKARHPLLDL------KKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 325 VPLNLSLDHNRRLLVISGPNAGGKSVTLKTVALAQFMLQCGLLVPMDSHSVCTVFDDFFIDIGDEQNIENDLSTYSSHLM 404
Cdd:COG1193 315 VPIDIELGEDFRTLVITGPNTGGKTVTLKTVGLLTLMAQSGLPIPAAEGSELPVFDNIFADIGDEQSIEQSLSTFSSHMT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 405 SMKHFTQFADKKSIIFIDEFGTGTEPMFGGAIAEGILLALNSTGAYGVITTHYGNLKQVAAKNQGLVNGAMRYDVEKLEP 484
Cdd:COG1193 395 NIVEILEKADENSLVLLDELGAGTDPQEGAALAIAILEELLERGARVVATTHYSELKAYAYNTEGVENASVEFDVETLSP 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 485 LYQLDIGKPGSSFALEIASKIGIAKDIIDYAKEHIGEERVKYDKILTKLENQMAQQESLLLENKRKERILDQRMKEYAEM 564
Cdd:COG1193 475 TYRLLIGVPGRSNAFEIARRLGLPEEIIERARELLGEESIDVEKLIEELERERRELEEEREEAERLREELEKLREELEEK 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 565 KESLEQNKKKYIQEAKTEAKALLDDVNRKIENTISEIRRTQADKDKAKELRQEVEQLKAKVKPEKKTPAPEKTIKVISGE 644
Cdd:COG1193 555 LEELEEEKEEILEKAREEAEEILREARKEAEELIRELREAQAEEEELKEARKKLEELKQELEEKLEKPKKKAKPAKPPEE 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 645 IAVGDHVRLKDSGAIAEVMAL-KKNEAEISIGDLKSNVKLNRLEKISLGEMKKEKKslaRRVGFDTN-AKMMDFSPNLDI 722
Cdd:COG1193 635 LKVGDRVRVLSLGQKGEVLEIpKGGEAEVQVGILKMTVKLSDLEKVEKKKPKKPKK---RPAGVSVSvSKASTVSPELDL 711
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495902521 723 RGKRAEEIISLVQNFVDDGFMLGLKDLRIVHGKGDGILREITRNLLRSMNSVSKLEDEHADRGGAGVTLVTLK 795
Cdd:COG1193 712 RGMRVEEALPELDKYLDDALLAGLPEVRIIHGKGTGALRKGVREYLKRHPYVKSFRLGEPGEGGDGVTVVELK 784
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
5-795 |
2.27e-170 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 510.91 E-value: 2.27e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 5 QNVEEKISFTKIRELIKEECSGPLGIQFVDKMSFSKDLSLVSRLLEQTDEFKKIIGSGELFPSSNYTDANPYLDKARIeG 84
Cdd:PRK00409 3 EKTLRVLEFNKIKEQLKTFAASELGKEKVLQLDPETDFEEVEELLEETDEAAKLLRLKGLPPFEGVKDIDDALKRAEK-G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 85 SFLDQEEFHEI--RLSLF-TLSRCIEFFKDHEEaYPSLFALLGLVALDNTVLRAIERILDEKGKIRNNASQELSLIRSQI 161
Cdd:PRK00409 82 GVLSGDELLEIakTLRYFrQLKRFIEDLEEEEE-LPILEEWVAKIRTLPELEQEIHNCIDEEGEVKDSASEKLRGIRRQL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 162 LYEENRLRKVLDRIFReakSKGMTP--DDASITVRGGRMVIPVLAENKRKIKGFIHDESATGQTVYLEPAEVLDINNELK 239
Cdd:PRK00409 161 RRKKSRIREKLESIIR---SKSLQKylQDTIITIRNDRYVLPVKAEYKHAIKGIVHDQSSSGATLYIEPQSVVELNNEIR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 240 DLEYMERREIQRILTKLTDTMRPFIPEMRKAYHFLGMVDFIRAKAKFAIKTNSHKPILKKERQLQWSDARHPLLefalkq 319
Cdd:PRK00409 238 ELRNKEEQEIERILKELSAKVAKNLDFLKFLNKIFDELDFIFARARYAKALKATFPLFNDEGKIDLRQARHPLL------ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 320 VGKKVVPLNLSLDHNRRLLVISGPNAGGKSVTLKTVALAQFMLQCGLLVPMDSHSVCTVFDDFFIDIGDEQNIENDLSTY 399
Cdd:PRK00409 312 DGEKVVPKDISLGFDKTVLVITGPNTGGKTVTLKTLGLAALMAKSGLPIPANEPSEIPVFKEIFADIGDEQSIEQSLSTF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 400 SSHLMSMKHFTQFADKKSIIFIDEFGTGTEPMFGGAIAEGILLALNSTGAYGVITTHYGNLKQVAAKNQGLVNGAMRYDV 479
Cdd:PRK00409 392 SGHMTNIVRILEKADKNSLVLFDELGAGTDPDEGAALAISILEYLRKRGAKIIATTHYKELKALMYNREGVENASVEFDE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 480 EKLEPLYQLDIGKPGSSFALEIASKIGIAKDIIDYAKEHIGEERVKYDKILTKLENQMAQQESLLLENKRKERILDQRMK 559
Cdd:PRK00409 472 ETLRPTYRLLIGIPGKSNAFEIAKRLGLPENIIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKE 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 560 EYAEMKESLEQNKKKYIQEAKTEAKALLDDVNRKIENTISEIRRTQADKDKAKELRQEVEQLKAKVKPEKKTPAPEKTIK 639
Cdd:PRK00409 552 ELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQK 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 640 VISGEIAVGDHVRLKDSGAIAEVMALKKN-EAEISIGDLKSNVKLNRLEKISlGEMKKEKKSLARRVGFDTNAKMmdfsp 718
Cdd:PRK00409 632 EKQEELKVGDEVKYLSLGQKGEVLSIPDDkEAIVQAGIMKMKVPLSDLEKIQ-KPKKKKKKKPKTVKPKPRTVSL----- 705
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495902521 719 NLDIRGKRAEEIISLVQNFVDDGFMLGLKDLRIVHGKGDGILREITRNLLRSMNSVSKLEDEHADRGGAGVTLVTLK 795
Cdd:PRK00409 706 ELDLRGMRYEEALERLDKYLDDALLAGYGEVLIIHGKGTGKLRKGVQEFLKKHPSVKSFRDAPPNEGGFGVTIVELK 782
|
|
| mutS2 |
TIGR01069 |
MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch ... |
5-795 |
1.80e-141 |
|
MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch repair protein. It is likely a DNA mismatch binding protein of unknown cellular function. [DNA metabolism, Other]
Pssm-ID: 130141 [Multi-domain] Cd Length: 771 Bit Score: 435.79 E-value: 1.80e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 5 QNVEEKISFTKIRELIKEECSGPLGIQFVDKMSFSKDLSLVSRLLEQTDEFKKIIGSGELFPSSNYTDAnpyLDKARIEG 84
Cdd:TIGR01069 3 EKDLIKLEFDKVKENLLKQTFTPLGKEDAIGLKPPKSVEESKEIIIKLTALGSIENNVRFFGFEDIREL---LKRAELGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 85 SFLDQEEFHEIRLSLFTLSRcIEFFKDHEEAYPSLFALLGLVALDNTVLRAIERILDEKGKIRNNASQELSLIRSQILYE 164
Cdd:TIGR01069 80 IVKGLEYILVIQNALKTVKH-LKVLSEHVLDLEILFHLRLNLITLPPLENDIIACIDDDGKVKDGASEELDAIRESLKAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 165 ENRLRKVLDRIFREAKSKGMTpDDASITVRGGRMVIPVLAENKRKIKGFIHDESATGQTVYLEPAEVLDINNELKDLEYM 244
Cdd:TIGR01069 159 EEEVVKRLHKIIRSKELAKYL-SDTIVTIRNGRYVLPLKSGFKGKIKGIVHDTSSSGETFYIEPQAIVKLNNKLAQLKNE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 245 ERREIQRILTKLTDTMRPFIPEMRKAYHFLGMVDFIRAKAKFAIKTNSHKPILKKERQLQWSDARHPLLefalkqVGKKV 324
Cdd:TIGR01069 238 EECEIEKILRTLSEKVQEYLLELKFLFKEFDFLDSLQARARYAKAVKGEFPMPSFTGKIILENARHPLL------KEPKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 325 VPLNLSLDHNRRLLVISGPNAGGKSVTLKTVALAQFMLQCGLLVPMDSHSVCTVFDDFFIDIGDEQNIENDLSTYSSHLM 404
Cdd:TIGR01069 312 VPFTLNLKFEKRVLAITGPNTGGKTVTLKTLGLLALMFQSGIPIPANEHSEIPYFEEIFADIGDEQSIEQNLSTFSGHMK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 405 SMKHFTQFADKKSIIFIDEFGTGTEPMFGGAIAEGILLALNSTGAYGVITTHYGNLKQVAAKNQGLVNGAMRYDVEKLEP 484
Cdd:TIGR01069 392 NISAILSKTTENSLVLFDELGAGTDPDEGSALAISILEYLLKQNAQVLITTHYKELKALMYNNEGVENASVLFDEETLSP 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 485 LYQLDIGKPGSSFALEIASKIGIAKDIIDYAKEHIGEERVKYDKILTKLENQMAQQESLL--LENKRKEriLDQRMKEYA 562
Cdd:TIGR01069 472 TYKLLKGIPGESYAFEIAQRYGIPHFIIEQAKTFYGEFKEEINVLIEKLSALEKELEQKNehLEKLLKE--QEKLKKELE 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 563 EMKESLEQNKKKYIQEAKTEAKALLDDVNRKIENTISEIRRTQADKDKAKELRQEVEQLKakvkpEKKTPAPEKTIKVIS 642
Cdd:TIGR01069 550 QEMEELKERERNKKLELEKEAQEALKALKKEVESIIRELKEKKIHKAKEIKSIEDLVKLK-----ETKQKIPQKPTNFQA 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 643 GEIavGDHVRLKDSGAIAEVMALKK-NEAEISIGDLKSNVKLNRLEKISLGEMKKEKKslarrVGFDTNAKMMDFSPNLD 721
Cdd:TIGR01069 625 DKI--GDKVRIRYFGQKGKIVQILGgNKWNVTVGGMRMKVHGSELEKINKAPPPKKFK-----VPKTTKPEPKEASLTLD 697
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495902521 722 IRGKRAEEIISLVQNFVDDGFMLGLKDLRIVHGKGDGILREITRNLLRSMNSVSKLEDEHADRGGAGVTLVTLK 795
Cdd:TIGR01069 698 LRGQRSEEALDRLEKFLNDALLAGYEVVLIIHGKGSGKLRKGVQELLKNHPKVKSFRDAPPNDGGSGVTIVYLE 771
|
|
| ABC_MutS2 |
cd03280 |
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ... |
304-507 |
4.35e-85 |
|
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213247 [Multi-domain] Cd Length: 200 Bit Score: 268.73 E-value: 4.35e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 304 QWSDARHPLLefalKQVGKKVVPLNLSLDHNRRLLVISGPNAGGKSVTLKTVALAQFMLQCGLLVPMDSHSVCTVFDDFF 383
Cdd:cd03280 1 RLREARHPLL----PLQGEKVVPLDIQLGENKRVLVITGPNAGGKTVTLKTLGLLTLMAQSGLPIPAAEGSSLPVFENIF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 384 IDIGDEQNIENDLSTYSSHLMSMKHFTQFADKKSIIFIDEFGTGTEPMFGGAIAEGILLALNSTGAYGVITTHYGNLKQV 463
Cdd:cd03280 77 ADIGDEQSIEQSLSTFSSHMKNIARILQHADPDSLVLLDELGSGTDPVEGAALAIAILEELLERGALVIATTHYGELKAY 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495902521 464 AAKNQGLVNGAMRYDVEKLEPLYQLDIGKPGSSFALEIASKIGI 507
Cdd:cd03280 157 AYKREGVENASMEFDPETLKPTYRLLIGVPGRSNALEIARRLGL 200
|
|
| MUTSac |
smart00534 |
ATPase domain of DNA mismatch repair MUTS family; |
337-518 |
3.13e-49 |
|
ATPase domain of DNA mismatch repair MUTS family;
Pssm-ID: 197777 [Multi-domain] Cd Length: 185 Bit Score: 171.59 E-value: 3.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 337 LLVISGPNAGGKSVTLKTVALAQFMLQCGLLVPMDSHSVcTVFDDFFIDIGDEQNIENDLSTYSSHLMSMKHFTQFADKK 416
Cdd:smart00534 1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAEL-PVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 417 SIIFIDEFGTGTEPMFGGAIAEGILLAL-NSTGAYGVITTHYGNLKQVAAKNQGLVNGAMRYDVEKLE--PLYQLDIGKP 493
Cdd:smart00534 80 SLVLLDELGRGTSTYDGLAIAAAILEYLlEKIGARTLFATHYHELTKLADNHPGVRNLHMSALEETENitFLYKLKPGVA 159
|
170 180
....*....|....*....|....*
gi 495902521 494 GSSFALEIASKIGIAKDIIDYAKEH 518
Cdd:smart00534 160 GKSYGIEVAKLAGLPKEVIERAKRI 184
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
306-507 |
5.03e-45 |
|
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213210 [Multi-domain] Cd Length: 202 Bit Score: 160.49 E-value: 5.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 306 SDARHPLLEFALKqvGKKVVPLNLSLdHNRRLLVISGPNAGGKSVTLKTVALAQFMLQCGLLVPMDSHSVcTVFDDFFID 385
Cdd:cd03243 3 KGGRHPVLLALTK--GETFVPNDINL-GSGRLLLITGPNMGGKSTYLRSIGLAVLLAQIGCFVPAESASI-PLVDRIFTR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 386 IGDEQNIENDLSTYSSHLMSMKHFTQFADKKSIIFIDEFGTGTEPMFGGAIAEGILLALNSTGAYGVITTHYGNLKQVAA 465
Cdd:cd03243 79 IGAEDSISDGRSTFMAELLELKEILSLATPRSLVLIDELGRGTSTAEGLAIAYAVLEHLLEKGCRTLFATHFHELADLPE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495902521 466 KNQGLVNGAMRYDV--EKLEPLYQLDIGKPGSSFALEIASKIGI 507
Cdd:cd03243 159 QVPGVKNLHMEELIttGGLTFTYKLIDGICDPSYALQIAELAGL 202
|
|
| mutS1 |
TIGR01070 |
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair] |
229-551 |
3.95e-32 |
|
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273427 [Multi-domain] Cd Length: 840 Bit Score: 134.13 E-value: 3.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 229 AEVLDINNELKDLEYmerreiqRILTKLTDTMRPFIPEMRKAYHFLGMVDFIRAKAKFAIKTNSHKPILKKERQLQWSDA 308
Cdd:TIGR01070 496 DKVLEAEGKILALEK-------ELFEELRELLKKYLEALQEAARALAELDVLANLAEVAETLHYTRPRFGDDPQLRIREG 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 309 RHPLLEFALKQvgkKVVPLNLSLDHNRRLLVISGPNAGGKSVTLKTVALAQFMLQCGLLVPMDShSVCTVFDDFFIDIGD 388
Cdd:TIGR01070 569 RHPVVEQVLRT---PFVPNDLEMAHNRRMLLITGPNMGGKSTYMRQTALIALLAQIGSFVPAES-AELPLFDRIFTRIGA 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 389 EQNIENDLSTYSSHLMSMKHFTQFADKKSIIFIDEFGTGTEPMFGGAIAEGILLAL-NSTGAYGVITTHYGNLKQVAAKN 467
Cdd:TIGR01070 645 SDDLASGRSTFMVEMTEAANILHNATENSLVLFDEIGRGTSTYDGLALAWAIAEYLhEHIRAKTLFATHYFELTALEESL 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 468 QGLVN---GAMRYDvEKLEPLYQLDIGKPGSSFALEIASKIGIAKDIIDYAKEHigeervkydkiLTKLENQMAQQESLL 544
Cdd:TIGR01070 725 PGLKNvhvAALEHN-GTIVFLHQVLPGPASKSYGLAVAALAGLPKEVIARARQI-----------LTQLEARSTESEAPQ 792
|
....*..
gi 495902521 545 LENKRKE 551
Cdd:TIGR01070 793 RKAQTSA 799
|
|
| ABC_MSH3_euk |
cd03287 |
ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA ... |
307-515 |
4.55e-27 |
|
ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213254 [Multi-domain] Cd Length: 222 Bit Score: 109.88 E-value: 4.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 307 DARHPLLEFALkqvGKKVVPLNLSLD-HNRRLLVISGPNAGGKSVTLKTVALAQFMLQCGLLVPMDSHSVcTVFDDFFID 385
Cdd:cd03287 5 EGRHPMIESLL---DKSFVPNDIHLSaEGGYCQIITGPNMGGKSSYIRQVALITIMAQIGSFVPASSATL-SIFDSVLTR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 386 IGDEQNIENDLSTYSSHLMSMKHFTQFADKKSIIFIDEFGTGTEPMFGGAIAEGILLALNS-TGAYGVITTHYGNLKQVA 464
Cdd:cd03287 81 MGASDSIQHGMSTFMVELSETSHILSNCTSRSLVILDELGRGTSTHDGIAIAYATLHYLLEeKKCLVLFVTHYPSLGEIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495902521 465 AKNQGLV-NGAMRYDVEKLEP----------LYQLDIGKPGSSFALEIASKIGIAKDIIDYA 515
Cdd:cd03287 161 RRFEGSIrNYHMSYLESQKDFetsdsqsitfLYKLVRGLASRSFGLNVARLAGLPKSIISRA 222
|
|
| ABC_MSH4_euk |
cd03282 |
ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA ... |
306-472 |
7.36e-26 |
|
ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213249 [Multi-domain] Cd Length: 204 Bit Score: 105.93 E-value: 7.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 306 SDARHPLLEfalkQVGKKVVPLNLSLDHNR-RLLVISGPNAGGKSVTLKTVALAQFMLQCGLLVPMdSHSVCTVFDDFFI 384
Cdd:cd03282 3 RDSRHPILD----RDKKNFIPNDIYLTRGSsRFHIITGPNMSGKSTYLKQIALLAIMAQIGCFVPA-EYATLPIFNRLLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 385 DIGDEQNIENDLSTYSSHLMSMKHFTQFADKKSIIFIDEFGTGTEPMFGGAIAEGILLALNSTGAYGVITTHYGNLKQVA 464
Cdd:cd03282 78 RLSNDDSMERNLSTFASEMSETAYILDYADGDSLVLIDELGRGTSSADGFAISLAILECLIKKESTVFFATHFRDIAAIL 157
|
....*...
gi 495902521 465 AKNQGLVN 472
Cdd:cd03282 158 GNKSCVVH 165
|
|
| MutS_V |
pfam00488 |
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
338-518 |
3.37e-24 |
|
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam01624, pfam05188, pfam05192 and pfam05190. The mutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair; other members of the family included the eukaryotic MSH 1,2,3, 4,5 and 6 proteins. These have various roles in DNA repair and recombination. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein. The aligned region corresponds with domain V of Thermus aquaticus MutS as characterized in, which contains a Walker A motif, and is structurally similar to the ATPase domain of ABC transporters.
Pssm-ID: 425714 [Multi-domain] Cd Length: 188 Bit Score: 100.35 E-value: 3.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 338 LVISGPNAGGKSVTLKTVALAQFMLQCGLLVPMDSHSVcTVFDDFFIDIGDEQNIENDLSTYSSHLMSMKHFTQFADKKS 417
Cdd:pfam00488 1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEI-GIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 418 IIFIDEFGTGTEPMFGGAIAEGILLAL-NSTGAYGVITTHYGNLKQVAAKNQGLVNGAMryDVEKLEP----LYQLDIGK 492
Cdd:pfam00488 80 LVILDELGRGTSTYDGLAIAWAVAEHLaEKIKARTLFATHYHELTKLAEKLPAVKNLHM--AAVEDDDdivfLYKVQPGA 157
|
170 180
....*....|....*....|....*.
gi 495902521 493 PGSSFALEIASKIGIAKDIIDYAKEH 518
Cdd:pfam00488 158 ADKSYGIHVAELAGLPESVVERAREI 183
|
|
| ABC_MutS1 |
cd03284 |
ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ... |
309-517 |
1.09e-23 |
|
ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213251 [Multi-domain] Cd Length: 216 Bit Score: 100.03 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 309 RHPLLEFALKQvgKKVVPLNLSLDHNRRLLVISGPNAGGKSVTLKTVALAQFMLQCGLLVPMDSHSVCtVFDDFFIDIGD 388
Cdd:cd03284 6 RHPVVEQVLDN--EPFVPNDTELDPERQILLITGPNMAGKSTYLRQVALIALLAQIGSFVPASKAEIG-VVDRIFTRIGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 389 EQNIENDLSTYSSHLMSMKHFTQFADKKSIIFIDEFGTGTEPMFGGAIAEGILLAL-NSTGAYGVITTHYGNLKQVAAKN 467
Cdd:cd03284 83 SDDLAGGRSTFMVEMVETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAIVEYLhEKIGAKTLFATHYHELTELEGKL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495902521 468 QGLVNGAMRYDVEKLEP--LYQLDIGKPGSSFALEIASKIGIAKDIIDYAKE 517
Cdd:cd03284 163 PRVKNFHVAVKEKGGGVvfLHKIVEGAADKSYGIEVARLAGLPEEVIERARE 214
|
|
| ABC_MSH6_euk |
cd03286 |
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ... |
309-515 |
5.15e-23 |
|
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213253 [Multi-domain] Cd Length: 218 Bit Score: 97.88 E-value: 5.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 309 RHPlleFALKQVGKKVVPLNLSLDHNR-RLLVISGPNAGGKSVTLKTVALAQFMLQCGLLVPMDSHSVcTVFDDFFIDIG 387
Cdd:cd03286 6 RHP---CLNASTASSFVPNDVDLGATSpRILVLTGPNMGGKSTLLRTVCLAVIMAQMGMDVPAKSMRL-SLVDRIFTRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 388 DEQNIENDLSTYSSHLMSMKHFTQFADKKSIIFIDEFGTGTEPMFGGAIAEGILLAL-NSTGAYGVITTHYGNLKQVAAK 466
Cdd:cd03286 82 ARDDIMKGESTFMVELSETANILRHATPDSLVILDELGRGTSTHDGYAIAHAVLEYLvKKVKCLTLFSTHYHSLCDEFHE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495902521 467 NQGLVNGAMRYDVEKLEP--------LYQLDIGKPGSSFALEIASKIGIAKDIIDYA 515
Cdd:cd03286 162 HGGVRLGHMACAVKNESDptirditfLYKLVAGICPKSYGLYVALMAGIPDGVVERA 218
|
|
| ABC_MSH2_euk |
cd03285 |
ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA ... |
308-517 |
1.66e-22 |
|
ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213252 [Multi-domain] Cd Length: 222 Bit Score: 96.68 E-value: 1.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 308 ARHPLLEFalkQVGKKVVPLNLSLDHNR-RLLVISGPNAGGKSVTLKTVALAQFMLQCGLLVPMDSHSVcTVFDDFFIDI 386
Cdd:cd03285 5 ARHPCVEA---QDDVAFIPNDVTLTRGKsRFLIITGPNMGGKSTYIRQIGVIVLMAQIGCFVPCDSADI-PIVDCILARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 387 GDEQNIENDLSTYSSHLMSMKHFTQFADKKSIIFIDEFGTGTEPM--FG--GAIAEGIllaLNSTGAYGVITTHYGNLKQ 462
Cdd:cd03285 81 GASDSQLKGVSTFMAEMLETAAILKSATENSLIIIDELGRGTSTYdgFGlaWAIAEYI---ATQIKCFCLFATHFHELTA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495902521 463 VAAKNQGLVN---GAMRYDVE-KLEPLYQLDIGKPGSSFALEIASKIGIAKDIIDYAKE 517
Cdd:cd03285 158 LADEVPNVKNlhvTALTDDASrTLTMLYKVEKGACDQSFGIHVAELANFPKEVIEMAKQ 216
|
|
| ABC_MSH5_euk |
cd03281 |
ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA ... |
306-507 |
2.06e-22 |
|
ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213248 [Multi-domain] Cd Length: 213 Bit Score: 96.22 E-value: 2.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 306 SDARHPLLEfalkQVGKKVVPLNLSLDH-NRRLLVISGPNAGGKSVTLKTVALAQFMLQCGLLVPMDSHSVcTVFDDFFI 384
Cdd:cd03281 3 QGGRHPLLE----LFVDSFVPNDTEIGGgGPSIMVITGPNSSGKSVYLKQVALIVFLAHIGSFVPADSATI-GLVDKIFT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 385 DIGDEQNIENDLSTYSSHLMSMKHFTQFADKKSIIFIDEFGTGTEP-----MFGGAIAEgiLLALNSTGAYGVITTH--- 456
Cdd:cd03281 78 RMSSRESVSSGQSAFMIDLYQVSKALRLATRRSLVLIDEFGKGTDTedgagLLIATIEH--LLKRGPECPRVIVSTHfhe 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495902521 457 -------YGNLKQVAAKNQGLVNGAMRYDVEKLEPLYQLDIGKPGSSFALEIASKIGI 507
Cdd:cd03281 156 lfnrsllPERLKIKFLTMEVLLNPTSTSPNEDITYLYRLVPGLADTSFAIHCAKLAGI 213
|
|
| Smr |
pfam01713 |
Smr domain; This family includes the Smr (Small MutS Related) proteins, and the C-terminal ... |
721-795 |
1.68e-19 |
|
Smr domain; This family includes the Smr (Small MutS Related) proteins, and the C-terminal region of the MutS2 protein. It has been suggested that this domain interacts with the MutS1 protein in the case of Smr proteins and with the N-terminal MutS related region of MutS2. This domain exhibits nicking endonuclease activity that might have a role in mismatch repair or genetic recombination. It shows no significant double strand cleavage or exonuclease activity. The full-length Swiss:Q86UW6 also has the polynucleotide kinase activity.
Pssm-ID: 460303 [Multi-domain] Cd Length: 76 Bit Score: 83.28 E-value: 1.68e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495902521 721 DIRGKRAEEIISLVQNFVDDGFMLGLKDLRIVHGKGD-GILREITRNLLRSMNSVSKLEDEHADRGGAGVTLVTLK 795
Cdd:pfam01713 1 DLHGMTVEEAREALDKFLDDALLAGLRCVLIIHGKGThGVLRKAVREWLKQHPLVLAFRSAPPGEGGDGATYVLLK 76
|
|
| MUTSd |
smart00533 |
DNA-binding domain of DNA mismatch repair MUTS family; |
122-314 |
2.21e-16 |
|
DNA-binding domain of DNA mismatch repair MUTS family;
Pssm-ID: 214710 [Multi-domain] Cd Length: 308 Bit Score: 80.81 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 122 LLGLVALDNTVLRAIERILDEKGK-IRNNASQELSLIRSQILYEENRLRKVLDRIFREAKSKgmTPDDASITVRGgrMVI 200
Cdd:smart00533 117 LLELLELLLELLNDDDPLEVNDGGlIKDGFDPELDELREKLEELEEELEELLKKEREELGID--SLKLGYNKVHG--YYI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 201 PVLAENKRKIKGFIHDESATGQTVYLEPAEVLDINNELKDLEYMERREIQRILTKLTDTMRPFIPEMRKAYHFLGMVDFI 280
Cdd:smart00533 193 EVTKSEAKKVPKDFIRRSSLKNTERFTTPELKELENELLEAKEEIERLEKEILRELLEKVLEYLEELRALAEALAELDVL 272
|
170 180 190
....*....|....*....|....*....|....
gi 495902521 281 RAKAKFAIKTNSHKPILKKERQLQWSDARHPLLE 314
Cdd:smart00533 273 LSLATLAAEGNYVRPEFVDSGELEIKNGRHPVLE 306
|
|
| PRK05399 |
PRK05399 |
DNA mismatch repair protein MutS; Provisional |
229-540 |
2.02e-15 |
|
DNA mismatch repair protein MutS; Provisional
Pssm-ID: 235444 [Multi-domain] Cd Length: 854 Bit Score: 80.52 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 229 AEVLDINNELKDLEYmerreiqRILTKLTDTMRPFIPEMRKAYHFLGMVDFIRAKAKFAIKTNSHKPILKKERQLQWSDA 308
Cdd:PRK05399 510 DKILSAEEKALALEY-------ELFEELREEVAEHIERLQKLAKALAELDVLASLAEVAEENNYVRPEFTDDPGIDIEEG 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 309 RHPLLEFALkqVGKKVVPLNLSLDHNRRLLVISGPNAGGKSVTLKTVALAQFMLQCGLLVPMDSHSVCtVFDDFFIDIG- 387
Cdd:PRK05399 583 RHPVVEQVL--GGEPFVPNDCDLDEERRLLLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAESARIG-IVDRIFTRIGa 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 388 -DeqnienDLST-YSSHLMSM-------KHftqfADKKSIIFIDEFGTGTEpMFGG-----AIAEGIllaLNSTGAYGVI 453
Cdd:PRK05399 660 sD------DLASgRSTFMVEMtetanilNN----ATERSLVLLDEIGRGTS-TYDGlsiawAVAEYL---HDKIGAKTLF 725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 454 TTHYGNLKQVAAKNQGLVNgamrYDVEKLEP------LYQLdigKPGS---SFALEIASKIGIAKDIIDYAKEhigeerv 524
Cdd:PRK05399 726 ATHYHELTELEEKLPGVKN----VHVAVKEHggdivfLHKV---VPGAadkSYGIHVAKLAGLPASVIKRARE------- 791
|
330
....*....|....*.
gi 495902521 525 kydkILTKLENQMAQQ 540
Cdd:PRK05399 792 ----ILAQLESASEKA 803
|
|
| ABC_MutS-like |
cd03283 |
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ... |
309-507 |
2.07e-15 |
|
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213250 [Multi-domain] Cd Length: 199 Bit Score: 75.41 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 309 RHPLLEfalkqvGKKVVPLNLSLDhNRRLLVISGPNAGGKSVTLKTVALAQFMLQCGLLVPMDSHSvcTVFDDFFIDIGD 388
Cdd:cd03283 6 GHPLIG------REKRVANDIDME-KKNGILITGSNMSGKSTFLRTIGVNVILAQAGAPVCASSFE--LPPVKIFTSIRV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 389 EQNIENDLSTYSSHLMSMKHFTQFADKKSIIF--IDEFGTGTEPMFGGAIAEGILLALNSTGAYGVITTHYGNLKQVAAK 466
Cdd:cd03283 77 SDDLRDGISYFYAELRRLKEIVEKAKKGEPVLflLDEIFKGTNSRERQAASAAVLKFLKNKNTIGIISTHDLELADLLDL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495902521 467 NQGLVNGAMRYDVE--KLEPLYQLDIGKPGSSFALEIASKIGI 507
Cdd:cd03283 157 DSAVRNYHFREDIDdnKLIFDYKLKPGVSPTRNALRLMKKIGI 199
|
|
| MutS |
COG0249 |
DNA mismatch repair ATPase MutS [Replication, recombination and repair]; |
234-536 |
9.19e-14 |
|
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
Pssm-ID: 440019 [Multi-domain] Cd Length: 861 Bit Score: 75.10 E-value: 9.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 234 INNELKDLEYM-----ER---REiQRILTKLTDTMRPFIPEMRKAYHFLGMVDFIRAKAKFAIKTNSHKPILKKERQLQW 305
Cdd:COG0249 507 ITPELKELEDKilsaeERalaLE-YELFEELREEVAAHIERLQALARALAELDVLASLAEVAVENNYVRPELDDSPGIEI 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 306 SDARHPLLEFALKqvGKKVVPLNLSLDHNRRLLVISGPNAGGKSVTLKTVALAQFMLQCGLLVPMDSHSVCtVFDDFFID 385
Cdd:COG0249 586 EGGRHPVVEQALP--GEPFVPNDCDLDPDRRILLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAESARIG-IVDRIFTR 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 386 IG--DeqnienDL----STysshlmsmkhftqF-------------ADKKSIIFIDEFGTGTEPMFGGAIAEGILLAL-N 445
Cdd:COG0249 663 VGasD------DLargqST-------------FmvemtetanilnnATERSLVLLDEIGRGTSTYDGLSIAWAVAEYLhD 723
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 446 STGAYGVITTHYGNLKQVAAKNQGLVN---GAMRYDvEKLEPLYQLdigKPGS---SFALEIASKIGIAKDIIDYAKEhi 519
Cdd:COG0249 724 KIRARTLFATHYHELTELAEKLPGVKNyhvAVKEWG-GDIVFLHKV---VPGPadrSYGIHVAKLAGLPASVIERARE-- 797
|
330
....*....|....*..
gi 495902521 520 geervkydkILTKLENQ 536
Cdd:COG0249 798 ---------ILAELEKG 805
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
333-467 |
2.40e-09 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 56.98 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 333 HNRRLLVISGPNAGGKSVTLKTVALAQFMLQCGLLVPMDSHSVCTV-FDDFFIDIGDEQniendLSTYSSHLMSMKHFTQ 411
Cdd:cd03227 19 GEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGCIVaAVSAELIFTRLQ-----LSGGEKELSALALILA 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 495902521 412 FADKK--SIIFIDEFGTGTEPMFGGAIAEGILLALNStGAYGVITTHYGNLKQVAAKN 467
Cdd:cd03227 94 LASLKprPLYILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHLPELAELADKL 150
|
|
| MSSS |
pfam20297 |
MutS2 and Smr-associated SH3 domain; This is a SH3-like domain associated with the MutS-like ... |
647-686 |
3.39e-06 |
|
MutS2 and Smr-associated SH3 domain; This is a SH3-like domain associated with the MutS-like ABC ATPase and Smr domains. It has been predicted to play a role in lesion recognition or alternatively in mediating contacts with RNA primers or misincorporated ribonucleotides during DNA repair or interacting with the ribosome at the intersection between DNA repair and ribosome rescue.
Pssm-ID: 466447 [Multi-domain] Cd Length: 42 Bit Score: 44.33 E-value: 3.39e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 495902521 647 VGDHVRLKDSGAIAEVMAL--KKNEAEISIGDLKSNVKLNRL 686
Cdd:pfam20297 1 VGDEVRVKSLGQKGEVLEVpgKKGEVEVQVGIMKMTVKLSDL 42
|
|
| SMR |
smart00463 |
Small MutS-related domain; |
720-795 |
5.09e-05 |
|
Small MutS-related domain;
Pssm-ID: 214676 [Multi-domain] Cd Length: 80 Bit Score: 42.29 E-value: 5.09e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495902521 720 LDIRGKRAEEIISLVQNFVDDGFMLGL-KDLRIVHGKGDGILREI--TRNLLRSMNSVSKLEDEHadRGGAGVTLVTLK 795
Cdd:smart00463 4 LDLHGLTVEEALTALDKFLNNARLKGLeQKLVIITGKGKHSLGGKsgVKPALKEHLRVESFRFAE--EGNSGVLVVKLK 80
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
516-622 |
2.30e-04 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 43.82 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 516 KEHIGEERVKYDKILTKLENQM---------AQQESLLLENKRKErilDQRMKEyaEMKESLEQNKKKYIQEAKTEAKAL 586
Cdd:pfam02841 185 KEAVEEAILQTDQALTAKEKAIeaerakaeaAEAEQELLREKQKE---EEQMME--AQERSYQEHVKQLIEKMEAEREQL 259
|
90 100 110
....*....|....*....|....*....|....*...
gi 495902521 587 LDDVNRKIENT--ISEIRRTQADKDKAKELRQEVEQLK 622
Cdd:pfam02841 260 LAEQERMLEHKlqEQEELLKEGFKTEAESLQKEIQDLK 297
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
519-711 |
2.86e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 519 IGEERVKYDKILTKLENQMAQQEsllLENKRKERILDQRMKEYAEMKESLEQNKKKYIQEAKTEAKALLDDVNRKIENTi 598
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEE---AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAA- 1664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 599 SEIRRTQADKDKAKELRQEVEQLKAKVKPEKKTPAPEKTI----KVISGEIAVGDHVRLKDSGAIAEVMALKKNEAEisi 674
Cdd:PTZ00121 1665 EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAeelkKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE--- 1741
|
170 180 190
....*....|....*....|....*....|....*....
gi 495902521 675 gDLK--SNVKLNRLEKISLGEMKKEKKSLARRVGFDTNA 711
Cdd:PTZ00121 1742 -DKKkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
504-624 |
3.31e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 504 KIGIAKDIIDYAKEHIGEERVKYDKILTKLENQMAQQESLLlenKRKERILDQRMKEYAEMKESLEQnKKKYIQEAKTEA 583
Cdd:PRK12704 58 ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENL---DRKLELLEKREEELEKKEKELEQ-KQQELEKKEEEL 133
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 495902521 584 KALLDDVNRKIENtISEIRRTQADKDKAKELRQEVEQLKAK 624
Cdd:PRK12704 134 EELIEEQLQELER-ISGLTAEEAKEILLEKVEEEARHEAAV 173
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
516-626 |
3.32e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 43.33 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 516 KEHIGEERVKYDKILTKLENQMAQQEslllenkRKERILDQRMKEYAEMKESLEQNKKKYIQEAKTEAKALLDDVNRKIE 595
Cdd:cd16269 179 KEAEAEAILQADQALTEKEKEIEAER-------AKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERE 251
|
90 100 110
....*....|....*....|....*....|....*..
gi 495902521 596 NTISEIRRTQADKDKAKE------LRQEVEQLKAKVK 626
Cdd:cd16269 252 NLLKEQERALESKLKEQEalleegFKEQAELLQEEIR 288
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
492-636 |
3.74e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 43.85 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 492 KPGSSFAlEIASKIGIAKDIIDYAKEhigEERVKYDKILTK-LENQMAQQESlllenKRKERILdQRMKEyaEMKESLEQ 570
Cdd:NF033838 301 KPEKKVA-EAEKKVEEAKKKAKDQKE---EDRRNYPTNTYKtLELEIAESDV-----KVKEAEL-ELVKE--EAKEPRNE 368
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 571 NKKKYIQeAKTEAK----ALLDDVNRKIENTISEIRRTQADKDKAKELRQEVEQLKAKVKPEKKTPAPEK 636
Cdd:NF033838 369 EKIKQAK-AKVESKkaeaTRLEKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEK 437
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
561-626 |
3.91e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 3.91e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 561 YAEMKESLEQNKKKYIQEAKTEAKALLDDVNRKIENTISEIRRTQADKDKAKE----LRQEVEQLKAKVK 626
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAeidkLQAEIAEAEAEIE 82
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
530-625 |
4.31e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.53 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 530 LTKLENQMAQQESLLL----------------------ENKRKERIL-------DQRMKEYAEMKESLEQ--NKKKYIQE 578
Cdd:PRK11637 112 IAKLEQQQAAQERLLAaqldaafrqgehtglqlilsgeESQRGERILayfgylnQARQETIAELKQTREElaAQKAELEE 191
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 495902521 579 AKTEAKALLDD---VNRKIENTISEIRRT--------QADKDKAKELRQEVEQLKAKV 625
Cdd:PRK11637 192 KQSQQKTLLYEqqaQQQKLEQARNERKKTltglesslQKDQQQLSELRANESRLRDSI 249
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
547-626 |
4.37e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.88 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 547 NKRKERILDQrMKEYAEMKESLEQNKKKY---IQEAKTEAKALLDDVNRKIENTISEIR---RTQAD--KDKAK-ELRQE 617
Cdd:cd06503 29 DEREEKIAES-LEEAEKAKEEAEELLAEYeekLAEARAEAQEIIEEARKEAEKIKEEILaeaKEEAEriLEQAKaEIEQE 107
|
....*....
gi 495902521 618 VEQLKAKVK 626
Cdd:cd06503 108 KEKALAELR 116
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
513-635 |
8.37e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 513 DYAKEHIGEERVKYDKILTKLENQMAQQESLLLENKRKERILD--QRMKEYAEMKESlEQNKKKYIQEAKTEAKALLDDV 590
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaaEEKAEAAEKKKE-EAKKKADAAKKKAEEKKKADEA 1396
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 495902521 591 NRKIENT---ISEIRRTQADKDKAKELRQEVEQLK----AKVKPEKKTPAPE 635
Cdd:PTZ00121 1397 KKKAEEDkkkADELKKAAAAKKKADEAKKKAEEKKkadeAKKKAEEAKKADE 1448
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
534-724 |
1.55e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.72 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 534 ENQMAQQESLllENKRKERILDQRMKEYAEMKESLEQNKKKYIQEAKTEAKAlldDVNRKIEntiSEIRRTQADKDKAKE 613
Cdd:PRK09510 94 QKQAAEQERL--KQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAA---AAKAKAE---AEAKRAAAAAKKAAA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 614 LRQEVEQLKAKVKPE---KKTPAPEKTIKVISGEIAVGDhvrlKDSGAIAEVMALKKNEAEISIGDLKSNVklnrlEKIS 690
Cdd:PRK09510 166 EAKKKAEAEAAKKAAaeaKKKAEAEAAAKAAAEAKKKAE----AEAKKKAAAEAKKKAAAEAKAAAAKAAA-----EAKA 236
|
170 180 190
....*....|....*....|....*....|....
gi 495902521 691 LGEMKKEKKSLARRVGFDTNAKMMDFSPNLDIRG 724
Cdd:PRK09510 237 AAEKAAAAKAAEKAAAAKAAAEVDDLFGGLDSGK 270
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
527-635 |
1.63e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 527 DKILTKLENQMAQQESLLLENKRKERILDQRMKEYAEMKESLEQnKKKYIQEAKTEAKALLDDVNRKIENTISEIRRTQA 606
Cdd:COG3883 125 SKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA-AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
90 100
....*....|....*....|....*....
gi 495902521 607 DKDKAKELRQEVEQLKAKVKPEKKTPAPE 635
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| SmrA |
COG2840 |
DNA-nicking endonuclease, Smr domain [Replication, recombination and repair]; |
720-795 |
2.00e-03 |
|
DNA-nicking endonuclease, Smr domain [Replication, recombination and repair];
Pssm-ID: 442088 [Multi-domain] Cd Length: 177 Bit Score: 39.90 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 720 LDIRGKRAEEIISLVQNFVDDGFMLGLKDLRIVHGKG------DGILREITRNLLRSMNSVSKLEDEHADRGGAGVTLVT 793
Cdd:COG2840 92 LDLHGLTVEEAREALAAFLAEAQRRGLRCVLIIHGKGlgspggRPVLKSQVPRWLRQHPEVLAFHSAPPRHGGSGALYVL 171
|
..
gi 495902521 794 LK 795
Cdd:COG2840 172 LR 173
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
521-636 |
2.00e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 521 EERVKYDKILTKLENQMAQQESLLLENKRKERILDQRMKEYAEMKESLE--QNKKKYIQEAKTEAKALLDDVNRKIEnti 598
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaaEEKAEAAEKKKEEAKKKADAAKKKAE--- 1388
|
90 100 110
....*....|....*....|....*....|....*...
gi 495902521 599 sEIRRTQADKDKAKELRQEVEQLKAKVKPEKKTPAPEK 636
Cdd:PTZ00121 1389 -EKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKK 1425
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
493-630 |
2.00e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 493 PGSSFAleiASKIGIAKDIIDYAKEHIGEERVKYDKILTKLENQMAQQESLLLENKRKERILDQRMKEYAEMKESLEQNK 572
Cdd:COG3883 9 PTPAFA---DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495902521 573 KKYIQEAKTEAK---------ALL-----DDVNRKIE--NTISE-----IRRTQADKDKAKELRQEVEQLKAKVKPEKK 630
Cdd:COG3883 86 EELGERARALYRsggsvsyldVLLgsesfSDFLDRLSalSKIADadadlLEELKADKAELEAKKAELEAKLAELEALKA 164
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
530-639 |
2.46e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 530 LTKLENQMAQQESLLLENKRKERILDQRMKEYAEMKESLEQNKKKYIQEAKtEAKALLDDVNRKIENTISEIRRTQAdkd 609
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQ-ELREKRDELNEKVKELKEERDELNE--- 85
|
90 100 110
....*....|....*....|....*....|
gi 495902521 610 KAKELRQEVEQLKAKVKPEKKTPAPEKTIK 639
Cdd:COG1340 86 KLNELREELDELRKELAELNKAGGSIDKLR 115
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
532-635 |
3.97e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 40.71 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 532 KLENQMAQQESLLLENKRKE----RILDQRMKEYAE-MKESLEQNKKKYIQEAKTEAKALLDDVNRKIENTISEIRRTQA 606
Cdd:pfam15709 337 RLRAERAEMRRLEVERKRREqeeqRRLQQEQLERAEkMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQA 416
|
90 100 110
....*....|....*....|....*....|...
gi 495902521 607 DKDKAK----ELRQEVEQLKAKVKPEKKTPAPE 635
Cdd:pfam15709 417 AQERARqqqeEFRRKLQELQRKKQQEEAERAEA 449
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
509-696 |
4.01e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 509 KDIIDYAKEHIGEERVKYDKILTKLENQMAQQESLLLENKRKERILDQRMKEYAEMKESLEQNKKKYIQEAKTE-AKALL 587
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEeLKKKE 1711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 588 DDVNRKIENTISE-----------IRRTQADKDKAKELRQEvEQLKAKVKPEKKTPAPEKTIKVISGEIAVGDHVRLKDS 656
Cdd:PTZ00121 1712 AEEKKKAEELKKAeeenkikaeeaKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE 1790
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495902521 657 GAIAEV----MALKKNEAEISIGDLKSNVKLNRLEKISLGEMKK 696
Cdd:PTZ00121 1791 KRRMEVdkkiKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKE 1834
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
521-636 |
6.83e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 521 EERVKYDKILTKLENQMAQQESLLLENKRKERILDQRMKEYAEMKESLE---QNKKKYIQEAKTEAKALLDDVNRKIENT 597
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKkkaEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
90 100 110
....*....|....*....|....*....|....*....
gi 495902521 598 ISEIRRTQADKDKAKELRQEVEQLKAKVKPEKKTPAPEK 636
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKK 1405
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
521-699 |
7.57e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 521 EERVKYDKILTKLEN-QMAQQESLLLENKRKERILDQRMKEYAEMKESL---EQNKKKYIQEAKTEAKALLDDVNRKIEN 596
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEaKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAkkaAEAKKKADEAKKAEEAKKADEAKKAEEA 1533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495902521 597 TISEIRRTQADKDKAKELR--QEVEQLKAKVKPEKKTPAPE-KTIKVISGEIAvgdhvRLKDSGAIAEVMALKKNEAEIS 673
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKkaEELKKAEEKKKAEEAKKAEEdKNMALRKAEEA-----KKAEEARIEEVMKLYEEEKKMK 1608
|
170 180
....*....|....*....|....*.
gi 495902521 674 IGDLKSNVKlnrlEKISLGEMKKEKK 699
Cdd:PTZ00121 1609 AEEAKKAEE----AKIKAEELKKAEE 1630
|
|
| |
