|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2-803 |
0e+00 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 1037.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 2 IREETLNLLEWPRLCQHLSTFAATKLGSIAARSLPIPNERSESLHLLAQTQEAyTLETTVEGGLSFGGIRDIGSSLDRAE 81
Cdd:PRK00409 1 MQEKTLRVLEFNKIKEQLKTFAASELGKEKVLQLDPETDFEEVEELLEETDEA-AKLLRLKGLPPFEGVKDIDDALKRAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 82 IGGILDGNALLDIATTLYGARQLRRAIEKAGQntvdnaDLEFPVLERLVSELRTYPELEQEIHRCIDDRANVADRASTEL 161
Cdd:PRK00409 80 KGGVLSGDELLEIAKTLRYFRQLKRFIEDLEE------EEELPILEEWVAKIRTLPELEQEIHNCIDEEGEVKDSASEKL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 162 ESIRRQLKQTRDRIYQTLNRMMQRQG--GALQEQLITTRSDRFVLPVKAPQKDKIPGIVHDASATGATLYIEPKAIVNDN 239
Cdd:PRK00409 154 RGIRRQLRRKKSRIREKLESIIRSKSlqKYLQDTIITIRNDRYVLPVKAEYKHAIKGIVHDQSSSGATLYIEPQSVVELN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 240 NQLRTLERREKVAEEAVLRALTERVAEVKPDLERLLAIVTTLDLAAARARYGLWLEANPPRFvDTEENTTLRQLRHPLLV 319
Cdd:PRK00409 234 NEIRELRNKEEQEIERILKELSAKVAKNLDFLKFLNKIFDELDFIFARARYAKALKATFPLF-NDEGKIDLRQARHPLLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 320 WQQkheagrdVVPIDVTMSPQIRVVTITGPNTGGKTVTLKTLGLAMLMAKVGMFVPAREPVELPWFSQVLADIGDEQSIE 399
Cdd:PRK00409 313 GEK-------VVPKDISLGFDKTVLVITGPNTGGKTVTLKTLGLAALMAKSGLPIPANEPSEIPVFKEIFADIGDEQSIE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 400 QNLSTFSGHVRRISRILEAVTEddNALVLLDEVGAGTDPSEGSALAMSLLQYLCDRAGLTVATTHFGELKALKYQDDRFE 479
Cdd:PRK00409 386 QSLSTFSGHMTNIVRILEKADK--NSLVLFDELGAGTDPDEGAALAISILEYLRKRGAKIIATTHYKELKALMYNREGVE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 480 NASVEFDDASLSPTYRLLWGIPGRSNALSIARRLGLTSQVVDSAQEYVtSGISVDVNETIAQLEAQRRRQETKADEASQI 559
Cdd:PRK00409 464 NASVEFDEETLRPTYRLLIGIPGKSNAFEIAKRLGLPENIIEEAKKLI-GEDKEKLNELIASLEELERELEQKAEEAEAL 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 560 VAQAERLNQEIAEKAEQLRQREERLKLEQERAIREAIEAAKEEIAKVIRRL---QQGTPTAQDAQKATAAIDAIAERNLP 636
Cdd:PRK00409 543 LKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELrqlQKGGYASVKAHELIEARKRLNKANEK 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 637 -SRREPPKPKPGFRPKEGDRVRIPRLGQTAEVLSEADKDgELVVRFGLMKMTVPLADVESLSGEKPDLPQPKAKPAPTvt 715
Cdd:PRK00409 623 kEKKKKKQKEKQEELKVGDEVKYLSLGQKGEVLSIPDDK-EAIVQAGIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPK-- 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 716 mktapvVRTSKNTLDLRGNRIHEAEHTLENAIAEAVPVG-GALWIIHGKGTGKLREGVHEFLKRSSHIDRFELAQQKDGG 794
Cdd:PRK00409 700 ------PRTVSLELDLRGMRYEEALERLDKYLDDALLAGyGEVLIIHGKGTGKLRKGVQEFLKKHPSVKSFRDAPPNEGG 773
|
....*....
gi 516254850 795 AGVTVAYLK 803
Cdd:PRK00409 774 FGVTIVELK 782
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
3-803 |
0e+00 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 993.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 3 REETLNLLEWPRLCQHLSTFAATKLGSIAARSLPIPNERSESLHLLAQTQEAYTLETtVEGGLSFGGIRDIGSSLDRAEI 82
Cdd:COG1193 2 NEKTLEKLEFDKILELLAEYAVSELGKELARKLRPSTDLEEVERLLAETAEARRLLR-LEGGLPLGGIPDIRPLLKRAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 83 GGILDGNALLDIATTLYGARQLRRAIEkagqntvdNADLEFPVLERLVSELRTYPELEQEIHRCIDDRANVADRASTELE 162
Cdd:COG1193 81 GGVLSPEELLDIARTLRAARRLKRFLE--------ELEEEYPALKELAERLPPLPELEKEIDRAIDEDGEVKDSASPELR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 163 SIRRQLKQTRDRIYQTLNRMMQRQ--GGALQEQLITTRSDRFVLPVKAPQKDKIPGIVHDASATGATLYIEPKAIVNDNN 240
Cdd:COG1193 153 RIRREIRSLEQRIREKLESILRSAsyQKYLQDAIITIRNGRYVIPVKAEYKGKIPGIVHDQSASGQTLFIEPMAVVELNN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 241 QLRTLERREKVAEEAVLRALTERVAEVKPDLERLLAIVTTLDLAAARARYGLWLEANPPRFVDtEENTTLRQLRHPLLVW 320
Cdd:COG1193 233 ELRELEAEERREIERILRELSALVREYAEELLENLEILAELDFIFAKARYALELKAVKPELND-EGYIKLKKARHPLLDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 321 qqkheagRDVVPIDVTMSPQIRVVTITGPNTGGKTVTLKTLGLAMLMAKVGMFVPAREPVELPWFSQVLADIGDEQSIEQ 400
Cdd:COG1193 312 -------KKVVPIDIELGEDFRTLVITGPNTGGKTVTLKTVGLLTLMAQSGLPIPAAEGSELPVFDNIFADIGDEQSIEQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 401 NLSTFSGHVRRISRILEAVteDDNALVLLDEVGAGTDPSEGSALAMSLLQYLCDRAGLTVATTHFGELKALKYQDDRFEN 480
Cdd:COG1193 385 SLSTFSSHMTNIVEILEKA--DENSLVLLDELGAGTDPQEGAALAIAILEELLERGARVVATTHYSELKAYAYNTEGVEN 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 481 ASVEFDDASLSPTYRLLWGIPGRSNALSIARRLGLTSQVVDSAQEYVTSGiSVDVNETIAQLEAQRRRQETKADEASQIV 560
Cdd:COG1193 463 ASVEFDVETLSPTYRLLIGVPGRSNAFEIARRLGLPEEIIERARELLGEE-SIDVEKLIEELERERRELEEEREEAERLR 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 561 AQAERLNQEIAEKAEQLRQREERLKLEQERAIREAIEAAKEEIAKVIRRLQQGTPTAQDAQKATAAIDAIA----ERNLP 636
Cdd:COG1193 542 EELEKLREELEEKLEELEEEKEEILEKAREEAEEILREARKEAEELIRELREAQAEEEELKEARKKLEELKqeleEKLEK 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 637 SRREPPKPKPGFRPKEGDRVRIPRLGQTAEVLsEADKDGELVVRFGLMKMTVPLADVESLSGEKPDLPQpKAKPAPTVTM 716
Cdd:COG1193 622 PKKKAKPAKPPEELKVGDRVRVLSLGQKGEVL-EIPKGGEAEVQVGILKMTVKLSDLEKVEKKKPKKPK-KRPAGVSVSV 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 717 KTApvvRTSKNTLDLRGNRIHEAEHTLENAIAEAVPVG-GALWIIHGKGTGKLREGVHEFLKRSSHIDRFELAQQKDGGA 795
Cdd:COG1193 700 SKA---STVSPELDLRGMRVEEALPELDKYLDDALLAGlPEVRIIHGKGTGALRKGVREYLKRHPYVKSFRLGEPGEGGD 776
|
....*...
gi 516254850 796 GVTVAYLK 803
Cdd:COG1193 777 GVTVVELK 784
|
|
| mutS2 |
TIGR01069 |
MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch ... |
2-803 |
0e+00 |
|
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: 734.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 2 IREETLNLLEWPRLCQHLSTFAATKLGSIAARSLPIPNERSESLHLLAQTQEAYTLETTVEgglsFGGIRDIGSSLDRAE 81
Cdd:TIGR01069 1 MREKDLIKLEFDKVKENLLKQTFTPLGKEDAIGLKPPKSVEESKEIIIKLTALGSIENNVR----FFGFEDIRELLKRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 82 IGGILDG-NALLDIATTLYGARQLRRAIEKAgqntvdnadLEFPVLERLVSELRTYPELEQEIHRCIDDRANVADRASTE 160
Cdd:TIGR01069 77 LGGIVKGlEYILVIQNALKTVKHLKVLSEHV---------LDLEILFHLRLNLITLPPLENDIIACIDDDGKVKDGASEE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 161 LESIRRQLKQTRDRIYQTLNRMMQRQGGA--LQEQLITTRSDRFVLPVKAPQKDKIPGIVHDASATGATLYIEPKAIVND 238
Cdd:TIGR01069 148 LDAIRESLKALEEEVVKRLHKIIRSKELAkyLSDTIVTIRNGRYVLPLKSGFKGKIKGIVHDTSSSGETFYIEPQAIVKL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 239 NNQLRTLERREKVAEEAVLRALTERVAEVKPDLERLLAIVTTLDLAAARARYGLWLEANPPRFVDTEEnTTLRQLRHPLL 318
Cdd:TIGR01069 228 NNKLAQLKNEEECEIEKILRTLSEKVQEYLLELKFLFKEFDFLDSLQARARYAKAVKGEFPMPSFTGK-IILENARHPLL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 319 VWQQkheagrdVVPIDVTMSPQIRVVTITGPNTGGKTVTLKTLGLAMLMAKVGMFVPAREPVELPWFSQVLADIGDEQSI 398
Cdd:TIGR01069 307 KEPK-------VVPFTLNLKFEKRVLAITGPNTGGKTVTLKTLGLLALMFQSGIPIPANEHSEIPYFEEIFADIGDEQSI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 399 EQNLSTFSGHVRRISRILEAVTEddNALVLLDEVGAGTDPSEGSALAMSLLQYLCDRAGLTVATTHFGELKALKYQDDRF 478
Cdd:TIGR01069 380 EQNLSTFSGHMKNISAILSKTTE--NSLVLFDELGAGTDPDEGSALAISILEYLLKQNAQVLITTHYKELKALMYNNEGV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 479 ENASVEFDDASLSPTYRLLWGIPGRSNALSIARRLGLTSQVVDSAQEYVtSGISVDVNETIAQLEAQRRRQETKADEASQ 558
Cdd:TIGR01069 458 ENASVLFDEETLSPTYKLLKGIPGESYAFEIAQRYGIPHFIIEQAKTFY-GEFKEEINVLIEKLSALEKELEQKNEHLEK 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 559 IVAQAERLNQEIAEKAEQLRQREERLKLEQERAIREAIEAAKEEIAKVIRRLQQGTPTAQDAQKATAAIDAIAERNLPSr 638
Cdd:TIGR01069 537 LLKEQEKLKKELEQEMEELKERERNKKLELEKEAQEALKALKKEVESIIRELKEKKIHKAKEIKSIEDLVKLKETKQKI- 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 639 rePPKPKPGFRPKEGDRVRIPRLGQTAEVLsEADKDGELVVRFGLMKMTVPLADVESLSGEKPdlpqPKAKPAPTvtmKT 718
Cdd:TIGR01069 616 --PQKPTNFQADKIGDKVRIRYFGQKGKIV-QILGGNKWNVTVGGMRMKVHGSELEKINKAPP----PKKFKVPK---TT 685
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 719 APVVRTSKNTLDLRGNRIHEAEHTLENAIAEAVPVG-GALWIIHGKGTGKLREGVHEFLKRSSHIDRFELAQQKDGGAGV 797
Cdd:TIGR01069 686 KPEPKEASLTLDLRGQRSEEALDRLEKFLNDALLAGyEVVLIIHGKGSGKLRKGVQELLKNHPKVKSFRDAPPNDGGSGV 765
|
....*.
gi 516254850 798 TVAYLK 803
Cdd:TIGR01069 766 TIVYLE 771
|
|
| ABC_MutS2 |
cd03280 |
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ... |
310-515 |
5.48e-109 |
|
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: 331.13 E-value: 5.48e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 310 LRQLRHPLLVWQqkheaGRDVVPIDVTMSPQIRVVTITGPNTGGKTVTLKTLGLAMLMAKVGMFVPAREPVELPWFSQVL 389
Cdd:cd03280 2 LREARHPLLPLQ-----GEKVVPLDIQLGENKRVLVITGPNAGGKTVTLKTLGLLTLMAQSGLPIPAAEGSSLPVFENIF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 390 ADIGDEQSIEQNLSTFSGHVRRISRILEAVTEDdnALVLLDEVGAGTDPSEGSALAMSLLQYLCDRAGLTVATTHFGELK 469
Cdd:cd03280 77 ADIGDEQSIEQSLSTFSSHMKNIARILQHADPD--SLVLLDELGSGTDPVEGAALAIAILEELLERGALVIATTHYGELK 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 516254850 470 ALKYQDDRFENASVEFDDASLSPTYRLLWGIPGRSNALSIARRLGL 515
Cdd:cd03280 155 AYAYKREGVENASMEFDPETLKPTYRLLIGVPGRSNALEIARRLGL 200
|
|
| MUTSac |
smart00534 |
ATPase domain of DNA mismatch repair MUTS family; |
343-526 |
5.99e-67 |
|
ATPase domain of DNA mismatch repair MUTS family;
Pssm-ID: 197777 [Multi-domain] Cd Length: 185 Bit Score: 220.12 E-value: 5.99e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 343 VVTITGPNTGGKTVTLKTLGLAMLMAKVGMFVPAREpVELPWFSQVLADIGDEQSIEQNLSTFSGHVRRISRILEAVTEd 422
Cdd:smart00534 1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAES-AELPVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 423 dNALVLLDEVGAGTDPSEGSALAMSLLQYLCDRAG-LTVATTHFGELKALKYQDDRFENASVEFDD--ASLSPTYRLLWG 499
Cdd:smart00534 79 -NSLVLLDELGRGTSTYDGLAIAAAILEYLLEKIGaRTLFATHYHELTKLADNHPGVRNLHMSALEetENITFLYKLKPG 157
|
170 180
....*....|....*....|....*..
gi 516254850 500 IPGRSNALSIARRLGLTSQVVDSAQEY 526
Cdd:smart00534 158 VAGKSYGIEVAKLAGLPKEVIERAKRI 184
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
310-515 |
1.06e-51 |
|
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: 178.98 E-value: 1.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 310 LRQLRHPLLVWQQKheaGRDVVPIDVTMSPQiRVVTITGPNTGGKTVTLKTLGLAMLMAKVGMFVPArEPVELPWFSQVL 389
Cdd:cd03243 2 IKGGRHPVLLALTK---GETFVPNDINLGSG-RLLLITGPNMGGKSTYLRSIGLAVLLAQIGCFVPA-ESASIPLVDRIF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 390 ADIGDEQSIEQNLSTFSGHVRRISRILEAVTEDdnALVLLDEVGAGTDPSEGSALAMSLLQYLCDRAGLTVATTHFGELK 469
Cdd:cd03243 77 TRIGAEDSISDGRSTFMAELLELKEILSLATPR--SLVLIDELGRGTSTAEGLAIAYAVLEHLLEKGCRTLFATHFHELA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 516254850 470 ALKYQDDRFENASVEFDDAS--LSPTYRLLWGIPGRSNALSIARRLGL 515
Cdd:cd03243 155 DLPEQVPGVKNLHMEELITTggLTFTYKLIDGICDPSYALQIAELAGL 202
|
|
| mutS1 |
TIGR01070 |
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair] |
103-567 |
7.19e-32 |
|
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273427 [Multi-domain] Cd Length: 840 Bit Score: 133.36 E-value: 7.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 103 QLRRAIEKAGQNTVDNADLEFPVLERLVSELRTYPELEQEIHRCIDDRAN--------VADRASTELESIRRQLKQTRDR 174
Cdd:TIGR01070 352 RLRTSLEQLPELRALLEELEGPTLQALAAQIDDFSELLELLEAALIENPPlvvrdgglIREGYDEELDELRAASREGTDY 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 175 IYQTLNRMMQRQGgalqeqlITT------RSDRFVLPVKAPQKDKIPG-IVHDASATGATLYIEPKAIVNDNNQLRtLER 247
Cdd:TIGR01070 432 LARLEARERERTG-------IPTlkvgynAVFGYYIEVTRGQLHLVPAhYRRRQTLKNAERYITPELKEKEDKVLE-AEG 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 248 REKVAEEAVLRALTERVAEVKPDLERLLAIVTTLDLAAARARYGLWLEANPPRFVDtEENTTLRQLRHPLLVWQQKHEag 327
Cdd:TIGR01070 504 KILALEKELFEELRELLKKYLEALQEAARALAELDVLANLAEVAETLHYTRPRFGD-DPQLRIREGRHPVVEQVLRTP-- 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 328 rdVVPIDVTMSPQIRVVTITGPNTGGKTVTLKTLGLAMLMAKVGMFVPAREpVELPWFSQVLADIGDEQSIEQNLSTFSG 407
Cdd:TIGR01070 581 --FVPNDLEMAHNRRMLLITGPNMGGKSTYMRQTALIALLAQIGSFVPAES-AELPLFDRIFTRIGASDDLASGRSTFMV 657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 408 HVRRISRILEAVTEddNALVLLDEVGAGTDPSEGSALAMSLLQYLCDRAG-LTVATTHFGELKALKYQDDRFEN---ASV 483
Cdd:TIGR01070 658 EMTEAANILHNATE--NSLVLFDEIGRGTSTYDGLALAWAIAEYLHEHIRaKTLFATHYFELTALEESLPGLKNvhvAAL 735
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 484 EFDDaSLSPTYRLLWGIPGRSNALSIARRLGLTSQVVDSAQEYVTSGISVDVNETIAQLEAQRRRQETKAD----EASQI 559
Cdd:TIGR01070 736 EHNG-TIVFLHQVLPGPASKSYGLAVAALAGLPKEVIARARQILTQLEARSTESEAPQRKAQTSAPEQISLfdeaETHPL 814
|
....*...
gi 516254850 560 VAQAERLN 567
Cdd:TIGR01070 815 LEELAKLD 822
|
|
| ABC_MutS1 |
cd03284 |
ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ... |
314-525 |
2.55e-31 |
|
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: 121.99 E-value: 2.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 314 RHPLLvwqQKHEAGRDVVPIDVTMSPQIRVVTITGPNTGGKTVTLKTLGLAMLMAKVGMFVPAREpVELPWFSQVLADIG 393
Cdd:cd03284 6 RHPVV---EQVLDNEPFVPNDTELDPERQILLITGPNMAGKSTYLRQVALIALLAQIGSFVPASK-AEIGVVDRIFTRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 394 DEQSIEQNLSTFSGHVRRISRILEAVTEddNALVLLDEVGAGTDPSEGSALAMSLLQYLCDRAG-LTVATTHFGELKALK 472
Cdd:cd03284 82 ASDDLAGGRSTFMVEMVETANILNNATE--RSLVLLDEIGRGTSTYDGLSIAWAIVEYLHEKIGaKTLFATHYHELTELE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 516254850 473 YQDDRFEN--ASVEFDDASLSPTYRLLWGIPGRSNALSIARRLGLTSQVVDSAQE 525
Cdd:cd03284 160 GKLPRVKNfhVAVKEKGGGVVFLHKIVEGAADKSYGIEVARLAGLPEEVIERARE 214
|
|
| ABC_MSH2_euk |
cd03285 |
ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA ... |
309-525 |
4.66e-31 |
|
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: 121.33 E-value: 4.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 309 TLRQLRHPLLvwqqkhEAGRDV--VPIDVTMSPQI-RVVTITGPNTGGKTVTLKTLGLAMLMAKVGMFVPAREpVELPWF 385
Cdd:cd03285 1 VLKEARHPCV------EAQDDVafIPNDVTLTRGKsRFLIITGPNMGGKSTYIRQIGVIVLMAQIGCFVPCDS-ADIPIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 386 SQVLADIGDEQSIEQNLSTFSGHVRRISRILEAVTEddNALVLLDEVGAGTDPSEGSALAMSLLQYLCDRAG-LTVATTH 464
Cdd:cd03285 74 DCILARVGASDSQLKGVSTFMAEMLETAAILKSATE--NSLIIIDELGRGTSTYDGFGLAWAIAEYIATQIKcFCLFATH 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516254850 465 FGELKALKYQDDRFEN----ASVEFDDASLSPTYRLLWGIPGRSNALSIARRLGLTSQVVDSAQE 525
Cdd:cd03285 152 FHELTALADEVPNVKNlhvtALTDDASRTLTMLYKVEKGACDQSFGIHVAELANFPKEVIEMAKQ 216
|
|
| MutS_V |
pfam00488 |
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
346-525 |
1.17e-30 |
|
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: 119.22 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 346 ITGPNTGGKTVTLKTLGLAMLMAKVGMFVPAREpVELPWFSQVLADIGDEQSIEQNLSTFSGHVRRISRILEAVTedDNA 425
Cdd:pfam00488 3 ITGPNMGGKSTYLRQVALIVLMAQIGSFVPAES-AEIGIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNAT--DKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 426 LVLLDEVGAGTDPSEGSALAMSLLQYLCDRAG-LTVATTHFGELKALKYQDDRFEN--ASVEFDDASLSPTYRLLWGIPG 502
Cdd:pfam00488 80 LVILDELGRGTSTYDGLAIAWAVAEHLAEKIKaRTLFATHYHELTKLAEKLPAVKNlhMAAVEDDDDIVFLYKVQPGAAD 159
|
170 180
....*....|....*....|...
gi 516254850 503 RSNALSIARRLGLTSQVVDSAQE 525
Cdd:pfam00488 160 KSYGIHVAELAGLPESVVERARE 182
|
|
| ABC_MSH3_euk |
cd03287 |
ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA ... |
314-523 |
2.39e-28 |
|
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: 113.74 E-value: 2.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 314 RHPLLvwqqkhEAGRDV--VPIDVTMSPQ-IRVVTITGPNTGGKTVTLKTLGLAMLMAKVGMFVPAREpVELPWFSQVLA 390
Cdd:cd03287 7 RHPMI------ESLLDKsfVPNDIHLSAEgGYCQIITGPNMGGKSSYIRQVALITIMAQIGSFVPASS-ATLSIFDSVLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 391 DIGDEQSIEQNLSTFSGHVRRISRILEAVTEddNALVLLDEVGAGTDPSEGSALAMSLLQYLCDRAG-LTVATTHFGELK 469
Cdd:cd03287 80 RMGASDSIQHGMSTFMVELSETSHILSNCTS--RSLVILDELGRGTSTHDGIAIAYATLHYLLEEKKcLVLFVTHYPSLG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516254850 470 ALKYQ-DDRFENASVEF----------DDASLSPTYRLLWGIPGRSNALSIARRLGLTSQVVDSA 523
Cdd:cd03287 158 EILRRfEGSIRNYHMSYlesqkdfetsDSQSITFLYKLVRGLASRSFGLNVARLAGLPKSIISRA 222
|
|
| MUTSd |
smart00533 |
DNA-binding domain of DNA mismatch repair MUTS family; |
91-321 |
8.71e-28 |
|
DNA-binding domain of DNA mismatch repair MUTS family;
Pssm-ID: 214710 [Multi-domain] Cd Length: 308 Bit Score: 114.32 E-value: 8.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 91 LLDIATTLYGARQLRRAIEKAGQntVDNADLEFPVLERLVSELRTYPELEQEIHRCIDDRAN-VADRASTELESIRRQLK 169
Cdd:smart00533 81 LLRLYDSLEGLKEIRQLLESLDG--PLLGLLLKVILEPLLELLELLLELLNDDDPLEVNDGGlIKDGFDPELDELREKLE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 170 QTRDRIYQTLNRMmQRQGGALQEQLITTRSDRFVLPVKAPQKDKIPGIVHDASATGATLYIEPKAIVNDNNQLRTLERRE 249
Cdd:smart00533 159 ELEEELEELLKKE-REELGIDSLKLGYNKVHGYYIEVTKSEAKKVPKDFIRRSSLKNTERFTTPELKELENELLEAKEEI 237
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516254850 250 KVAEEAVLRALTERVAEVKPDLERLLAIVTTLDLAAARARYGLWLEANPPRFVDTEEnTTLRQLRHPLLVWQ 321
Cdd:smart00533 238 ERLEKEILRELLEKVLEYLEELRALAEALAELDVLLSLATLAAEGNYVRPEFVDSGE-LEIKNGRHPVLELQ 308
|
|
| ABC_MSH4_euk |
cd03282 |
ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA ... |
309-471 |
9.71e-28 |
|
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: 111.33 E-value: 9.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 309 TLRQLRHPLLVWQQKheagrDVVPIDVTMSP-QIRVVTITGPNTGGKTVTLKTLGLAMLMAKVGMFVPArEPVELPWFSQ 387
Cdd:cd03282 1 IIRDSRHPILDRDKK-----NFIPNDIYLTRgSSRFHIITGPNMSGKSTYLKQIALLAIMAQIGCFVPA-EYATLPIFNR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 388 VLADIGDEQSIEQNLSTFSGHVRRISRILEAVteDDNALVLLDEVGAGTDPSEGSALAMSLLQYLCDRAGLTVATTHFGE 467
Cdd:cd03282 75 LLSRLSNDDSMERNLSTFASEMSETAYILDYA--DGDSLVLIDELGRGTSSADGFAISLAILECLIKKESTVFFATHFRD 152
|
....
gi 516254850 468 LKAL 471
Cdd:cd03282 153 IAAI 156
|
|
| ABC_MSH6_euk |
cd03286 |
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ... |
310-523 |
2.30e-27 |
|
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: 110.60 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 310 LRQLRHPLLVWQQkheaGRDVVPIDVTM---SPQIRVvtITGPNTGGKTVTLKTLGLAMLMAKVGMFVPAREpVELPWFS 386
Cdd:cd03286 2 FEELRHPCLNAST----ASSFVPNDVDLgatSPRILV--LTGPNMGGKSTLLRTVCLAVIMAQMGMDVPAKS-MRLSLVD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 387 QVLADIGDEQSIEQNLSTFSGHVRRISRILEAVTEDdnALVLLDEVGAGTDPSEGSALAMSLLQYLCDRAG-LTVATTHF 465
Cdd:cd03286 75 RIFTRIGARDDIMKGESTFMVELSETANILRHATPD--SLVILDELGRGTSTHDGYAIAHAVLEYLVKKVKcLTLFSTHY 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516254850 466 GELK---------ALKYQDDRFENASvEFDDASLSPTYRLLWGIPGRSNALSIARRLGLTSQVVDSA 523
Cdd:cd03286 153 HSLCdefhehggvRLGHMACAVKNES-DPTIRDITFLYKLVAGICPKSYGLYVALMAGIPDGVVERA 218
|
|
| ABC_MSH5_euk |
cd03281 |
ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA ... |
310-515 |
1.94e-26 |
|
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: 107.77 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 310 LRQLRHPLLVwqqkhEAGRDVVPIDVTM-SPQIRVVTITGPNTGGKTVTLKTLGLAMLMAKVGMFVPAREpVELPWFSQV 388
Cdd:cd03281 2 IQGGRHPLLE-----LFVDSFVPNDTEIgGGGPSIMVITGPNSSGKSVYLKQVALIVFLAHIGSFVPADS-ATIGLVDKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 389 LADIGDEQSIEQNLSTFSGHVRRISRILEAVTedDNALVLLDEVGAGTDPSEGSALAMSLLQYLCDRAG---LTVATTHF 465
Cdd:cd03281 76 FTRMSSRESVSSGQSAFMIDLYQVSKALRLAT--RRSLVLIDEFGKGTDTEDGAGLLIATIEHLLKRGPecpRVIVSTHF 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516254850 466 GELKALKY-----------QDDRFENASVEFDDaSLSPTYRLLWGIPGRSNALSIARRLGL 515
Cdd:cd03281 154 HELFNRSLlperlkikfltMEVLLNPTSTSPNE-DITYLYRLVPGLADTSFAIHCAKLAGI 213
|
|
| ABC_MutS-like |
cd03283 |
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ... |
312-515 |
2.98e-26 |
|
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: 107.00 E-value: 2.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 312 QLRHPLLvwqqkheAGRDVVPIDVTMSPQiRVVTITGPNTGGKTVTLKTLGLAMLMAKVGMFVPAREpVELPwFSQVLAD 391
Cdd:cd03283 4 NLGHPLI-------GREKRVANDIDMEKK-NGILITGSNMSGKSTFLRTIGVNVILAQAGAPVCASS-FELP-PVKIFTS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 392 IGDEQSIEQNLSTFSGHVRRISRILEAVTEDDNALVLLDEVGAGTDPSEGSALAMSLLQYLCDRAGLTVATTHFGELKAL 471
Cdd:cd03283 74 IRVSDDLRDGISYFYAELRRLKEIVEKAKKGEPVLFLLDEIFKGTNSRERQAASAAVLKFLKNKNTIGIISTHDLELADL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 516254850 472 KYQDDRFENA--SVEFDDASLSPTYRLLWGIPGRSNALSIARRLGL 515
Cdd:cd03283 154 LDLDSAVRNYhfREDIDDNKLIFDYKLKPGVSPTRNALRLMKKIGI 199
|
|
| Smr |
pfam01713 |
Smr domain; This family includes the Smr (Small MutS Related) proteins, and the C-terminal ... |
730-803 |
1.79e-20 |
|
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: 85.98 E-value: 1.79e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516254850 730 DLRGNRIHEAEHTLENAIAEAVPVG-GALWIIHGKGT-GKLREGVHEFLKRSSHIDRFELAQQKDGGAGVTVAYLK 803
Cdd:pfam01713 1 DLHGMTVEEAREALDKFLDDALLAGlRCVLIIHGKGThGVLRKAVREWLKQHPLVLAFRSAPPGEGGDGATYVLLK 76
|
|
| PRK05399 |
PRK05399 |
DNA mismatch repair protein MutS; Provisional |
246-577 |
7.83e-16 |
|
DNA mismatch repair protein MutS; Provisional
Pssm-ID: 235444 [Multi-domain] Cd Length: 854 Bit Score: 82.07 E-value: 7.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 246 ERREKV--AEEAVL-------RALTERVAEVKPDLERLLAIVTTLDLAAA---RARYGLWleaNPPRFVDtEENTTLRQL 313
Cdd:PRK05399 507 ELEDKIlsAEEKALaleyelfEELREEVAEHIERLQKLAKALAELDVLASlaeVAEENNY---VRPEFTD-DPGIDIEEG 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 314 RHPLLvwqQKHEAGRDVVPIDVTMSPQIRVVTITGPNTGGKTVTLKTLGLAMLMAKVGMFVPAREpVELPWFSQVLADIG 393
Cdd:PRK05399 583 RHPVV---EQVLGGEPFVPNDCDLDEERRLLLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAES-ARIGIVDRIFTRIG 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 394 --DeqsieqNL----STFSGHVRRISRILEAVTEddNALVLLDEVGAGT---DpseGSALAMSLLQYLCDRAG-LTVATT 463
Cdd:PRK05399 659 asD------DLasgrSTFMVEMTETANILNNATE--RSLVLLDEIGRGTstyD---GLSIAWAVAEYLHDKIGaKTLFAT 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 464 HFGELKALKYQDDRFENASV---EFDDaSLSPTYRLLWGIPGRSNALSIARRLGLTSQVVDSAQEYVtsgisvdvnetiA 540
Cdd:PRK05399 728 HYHELTELEEKLPGVKNVHVavkEHGG-DIVFLHKVVPGAADKSYGIHVAKLAGLPASVIKRAREIL------------A 794
|
330 340 350
....*....|....*....|....*....|....*..
gi 516254850 541 QLEAQRRRQETKADEASQIVAQAERLNQEIAEKAEQL 577
Cdd:PRK05399 795 QLESASEKAKAASAEEDQLSLFAEPEESPLLEALKAL 831
|
|
| MutS |
COG0249 |
DNA mismatch repair ATPase MutS [Replication, recombination and repair]; |
242-484 |
1.42e-13 |
|
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
Pssm-ID: 440019 [Multi-domain] Cd Length: 861 Bit Score: 74.71 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 242 LRTLERR-----EKVA--EEAVLRALTERVAEVKPDLERLLAIVTTLDLAAA---RARYGLWleaNPPRFVDTEEnTTLR 311
Cdd:COG0249 511 LKELEDKilsaeERALalEYELFEELREEVAAHIERLQALARALAELDVLASlaeVAVENNY---VRPELDDSPG-IEIE 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 312 QLRHPLLVWQQKHEAgrdVVPIDVTMSPQIRVVTITGPNTGGKTVTLKTLGLAMLMAKVGMFVPAREpVELPWFSQVLAD 391
Cdd:COG0249 587 GGRHPVVEQALPGEP---FVPNDCDLDPDRRILLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAES-ARIGIVDRIFTR 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 392 IG--DeqsieqNL----STF------SghvrriSRILEAVTEddNALVLLDEVGAGTDPSEGSALAMSLLQYLCDRAG-L 458
Cdd:COG0249 663 VGasD------DLargqSTFmvemteT------ANILNNATE--RSLVLLDEIGRGTSTYDGLSIAWAVAEYLHDKIRaR 728
|
250 260
....*....|....*....|....*.
gi 516254850 459 TVATTHFGELKALKYQDDRFENASVE 484
Cdd:COG0249 729 TLFATHYHELTELAEKLPGVKNYHVA 754
|
|
| MSSS |
pfam20297 |
MutS2 and Smr-associated SH3 domain; This is a SH3-like domain associated with the MutS-like ... |
652-693 |
1.45e-13 |
|
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: 65.13 E-value: 1.45e-13
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 516254850 652 EGDRVRIPRLGQTAEVLSEADKDGELVVRFGLMKMTVPLADV 693
Cdd:pfam20297 1 VGDEVRVKSLGQKGEVLEVPGKKGEVEVQVGIMKMTVKLSDL 42
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
331-471 |
3.44e-10 |
|
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: 59.30 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 331 VPIDVTMSPQiRVVTITGPNTGGKTVTLKTLGLAMLMA----------KVGMFVPAREpVELpwfsqVLADIGDEQSiEQ 400
Cdd:cd03227 12 VPNDVTFGEG-SLTIITGPNGSGKSTILDAIGLALGGAqsatrrrsgvKAGCIVAAVS-AEL-----IFTRLQLSGG-EK 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516254850 401 NLSTfsghvrrISRILEAVTEDDNALVLLDEVGAGTDPSEGSALAMSLLQYLCDRAGLTVaTTHFGELKAL 471
Cdd:cd03227 84 ELSA-------LALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITHLPELAEL 146
|
|
| SMR |
smart00463 |
Small MutS-related domain; |
726-803 |
2.66e-09 |
|
Small MutS-related domain;
Pssm-ID: 214676 [Multi-domain] Cd Length: 80 Bit Score: 54.23 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 726 KNTLDLRGNRIHEAEHTLENAIAEA--VPVGGALWIIHGKGTGKLR--EGVHEFLKRSSHIDRFELAQQkdGGAGVTVAY 801
Cdd:smart00463 1 KWSLDLHGLTVEEALTALDKFLNNArlKGLEQKLVIITGKGKHSLGgkSGVKPALKEHLRVESFRFAEE--GNSGVLVVK 78
|
..
gi 516254850 802 LK 803
Cdd:smart00463 79 LK 80
|
|
| SmrA |
COG2840 |
DNA-nicking endonuclease, Smr domain [Replication, recombination and repair]; |
728-803 |
1.64e-05 |
|
DNA-nicking endonuclease, Smr domain [Replication, recombination and repair];
Pssm-ID: 442088 [Multi-domain] Cd Length: 177 Bit Score: 46.06 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 728 TLDLRGNRIHEAEHTLENAIAEAVPVGGALW-IIHGKGTGK------LREGVHEFLKRSSHIDRFELAQQKDGGAGVTVA 800
Cdd:COG2840 91 RLDLHGLTVEEAREALAAFLAEAQRRGLRCVlIIHGKGLGSpggrpvLKSQVPRWLRQHPEVLAFHSAPPRHGGSGALYV 170
|
...
gi 516254850 801 YLK 803
Cdd:COG2840 171 LLR 173
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
542-629 |
2.06e-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: 48.14 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 542 LEAQRRRQETKADEASQIVAQAERLNQEIAEKAEQLRQREERLKLEQE------RAIREAIEAAKEEIAKVIRRLQQGTP 615
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEeleedlSSLEQEIENVKSELKELEARIEELEE 772
|
90
....*....|....
gi 516254850 616 TAQDAQKATAAIDA 629
Cdd:TIGR02169 773 DLHKLEEALNDLEA 786
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
534-640 |
3.91e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 534 DVNETIAQLEAQRRRQETKADEASQIvaQAERLNQEIAEKAEQLRQREERLKLEQERAIREAIEAAKEEIAKVIRRLQQG 613
Cdd:PTZ00121 1086 DNRADEATEEAFGKAEEAKKTETGKA--EEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDA 1163
|
90 100 110
....*....|....*....|....*....|..
gi 516254850 614 -----TPTAQDAQKATAAIDAIAERNLPSRRE 640
Cdd:PTZ00121 1164 rkaeeARKAEDAKKAEAARKAEEVRKAEELRK 1195
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
537-621 |
4.28e-05 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 43.75 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 537 ETIAQLEAQRRRQETKADEASQIVAQAERLNQEIAEKAEqlRQREERLKLEQERAIREA----IEAAKEEIAKVIRRLQQ 612
Cdd:pfam20492 34 ETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAE--MEAEEKEQLEAELAEAQEeiarLEEEVERKEEEARRLQE 111
|
....*....
gi 516254850 613 GTPTAQDAQ 621
Cdd:pfam20492 112 ELEEAREEE 120
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
534-640 |
6.80e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 534 DVNETIAQLEAQRRRQETKADEASQIVAQAERLNQEIAEKAEQLRQREERLKLEQERAIREAIEAAKEEIAKVIRRLQQG 613
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
90 100
....*....|....*....|....*..
gi 516254850 614 TPTAQDAQKATAAIDAIAERNLPSRRE 640
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAEL 468
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
543-623 |
7.97e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 7.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 543 EAQRRRQETKADEASQIVA--QAERLNQ-EIAEKAEQLRQREERLKLEQERAIREAIEAAKEEIAKVIRRLQQGTPTAQD 619
Cdd:PTZ00121 1162 DARKAEEARKAEDAKKAEAarKAEEVRKaEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE 1241
|
....
gi 516254850 620 AQKA 623
Cdd:PTZ00121 1242 AKKA 1245
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
549-657 |
1.04e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 549 QETKADEASQivAQAERLNQEIAEKAEQLRQREERLKLEQERAIREAIEAAKEEIAKVIRRLQQGTPTAQDAQKATAAID 628
Cdd:PTZ00121 1605 KKMKAEEAKK--AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
90 100 110
....*....|....*....|....*....|....
gi 516254850 629 A-----IAERNLPSRREPPKPKPGFRPKEGDRVR 657
Cdd:PTZ00121 1683 AeedekKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
541-632 |
1.43e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.80 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 541 QLEAQRRRQETKADEASQivaQAERLNQEIAEKAEQLRQRE-ERLKLEQERaiREAIEAAKEEIAKvirrlQQGTPTAQD 619
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQ---QAEELQQKQAAEQERLKQLEkERLAAQEQK--KQAEEAAKQAALK-----QKQAEEAAA 139
|
90
....*....|...
gi 516254850 620 AQKATAAIDAIAE 632
Cdd:PRK09510 140 KAAAAAKAKAEAE 152
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
541-612 |
2.04e-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: 43.76 E-value: 2.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516254850 541 QLEAQRRRQETKADEASQIVAQAERLNQEIAEKAEQLRQREERLKlEQERAIREAIEAAKEEIAKVIRRLQQ 612
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE-EKKAELDEELAELEAELEELEAEREE 167
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
535-635 |
2.20e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 535 VNETIAQLEAQRRRQETKADEASQivaQAERLNQEIAEKAEQLRQREERLK--LEQERAIREAIEAAKEEIAKVIRRLQQ 612
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEE---RLEELEEELAELEEELEELEEELEelEEELEEAEEELEEAEAELAEAEEALLE 369
|
90 100
....*....|....*....|...
gi 516254850 613 gtpTAQDAQKATAAIDAIAERNL 635
Cdd:COG1196 370 ---AEAELAEAEEELEELAEELL 389
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
534-612 |
3.28e-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: 43.98 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 534 DVNETIAQLEAQRRRQETKADEASQivaQAERLNQEIAEKAEQLRQREERLKL---------EQERAIREAIEAAKEEIA 604
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLK---QLAALERRIAALARRIRALEQELAAleaelaeleKEIAELRAELEAQKEELA 107
|
....*...
gi 516254850 605 KVIRRLQQ 612
Cdd:COG4942 108 ELLRALYR 115
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
503-612 |
3.96e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 503 RSNALSIARRLGLTSQVVDSAQEYVTSGISVDVNETI---AQLEAQRRRQETKADEASQIVAQAERLNQEIAEKAEQLRQ 579
Cdd:COG4913 241 HEALEDAREQIELLEPIRELAERYAAARERLAELEYLraaLRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDA 320
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 516254850 580 -REERLKLEQERA---------IREAIEAAKEEIAKVIRRLQQ 612
Cdd:COG4913 321 lREELDELEAQIRgnggdrleqLEREIERLERELEERERRRAR 363
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
543-674 |
4.05e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 543 EAQRRRQETK--ADEASQivAQAERLNQEIAEKAEQLRQREERLKLEQERAIREAIEAAKEEIAKVIRRLQQgTPTAQDA 620
Cdd:PTZ00121 1487 EAKKKAEEAKkkADEAKK--AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE-LKKAEEK 1563
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 516254850 621 QKATAAIDAIAERNLPSRR-EPPKPKPGFRPKEGDRVRIPRLGQTAEVLSEADKD 674
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
543-673 |
4.60e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 543 EAQRRRQETKADEASQiVAQAERLNQEIAEKAEQLRQREERLKLEQERAiREAIEAAKEEIAKVIRRLQQGTPTAQDAQK 622
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKK-KAEEAKKADEAKKKAEEAKKKADAAKKKAEEA-KKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 516254850 623 ATAAIDAIAERNLPSRREPPKPKPGFRPKEGDRVRIPRLGQTAEVLSEADK 673
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE 1422
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
533-634 |
5.02e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 41.03 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 533 VDVNETIAQLEAQRRRQETKADEASQIVAQAERLNQEIAEKAEQLRQREERLKLEQERAIREAIEAAKEEIAKVIRRLQQ 612
Cdd:smart00935 4 VDVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQ 83
|
90 100
....*....|....*....|....*...
gi 516254850 613 GTPTAQDA------QKATAAIDAIAERN 634
Cdd:smart00935 84 DLQKRQQEelqkilDKINKAIKEVAKKK 111
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
545-644 |
5.75e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.40 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 545 QRRRQETKADEASQ-IVAQAERLNQEIAEKAEQLRQREERLKLEQERAIREAIEAAKEEIAKVIRRLQQGTPTAQDAQKA 623
Cdd:PRK05035 440 AIEQEKKKAEEAKArFEARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAV 519
|
90 100
....*....|....*....|.
gi 516254850 624 TAAIDAIAERNLPSRREPPKP 644
Cdd:PRK05035 520 IAAREARKAQARARQAEKQAA 540
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
540-610 |
6.15e-04 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 40.93 E-value: 6.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516254850 540 AQLEAQRRRQETKAdEASQIVAQA-ERLNQEIAEKAEQLRQREERLKLEQERAIREAIEAAKEEIAKVIRRL 610
Cdd:COG0711 53 ALAEYEEKLAEARA-EAAEIIAEArKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADL 123
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
543-679 |
6.57e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 543 EAQRRRQE--TKADEASQIVAQAERLNQEIAEKAEQLRQREERLKLEQERAIREAIEAAKE-EIAKVIRrlQQGTPTAQD 619
Cdd:PTZ00121 1685 EDEKKAAEalKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKaEEAKKDE--EEKKKIAHL 1762
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 620 AQKATAAIDAIAERNLPSRREPPKPKPGFRPKEGDRvRIPRLGQTAEVLSEADKDGELVV 679
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK-KIKDIFDNFANIIEGGKEGNLVI 1821
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
537-700 |
6.68e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 537 ETIAQLEAQRRRQETKADEASQIVAQAERLnqEIAEKAEQLRQREERLKLEQERAIREAIEAAKEEIAKVIRRlqqgtpt 616
Cdd:PTZ00121 1125 EDARKAEEARKAEDARKAEEARKAEDAKRV--EIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRK------- 1195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 617 AQDAQKATAAIDAIAERNLPSRREPPKPKpgfRPKEGDRVRIPRLGQTAEVLSEADKDGELVVRFGLMKMTVPLADVESL 696
Cdd:PTZ00121 1196 AEDARKAEAARKAEEERKAEEARKAEDAK---KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAI 1272
|
....
gi 516254850 697 SGEK 700
Cdd:PTZ00121 1273 KAEE 1276
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
537-640 |
6.76e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 537 ETIAQLEAQRRRQETKADEASQIVAQAERLNQEIAEKAEQLRQREERLKLEQERAIREAIEAAKeEIAKVIRRLQQgtpT 616
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA-QLEELEEAEEA---L 412
|
90 100
....*....|....*....|....
gi 516254850 617 AQDAQKATAAIDAIAERNLPSRRE 640
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEE 436
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
562-612 |
8.97e-04 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 42.94 E-value: 8.97e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 516254850 562 QAERLNQEIAEKAeqlRQREERLKLEQERAIREAIEA-AKEEIAKVIRRLQQ 612
Cdd:PLN02316 257 ELEKLAKEEAERE---RQAEEQRRREEEKAAMEADRAqAKAEVEKRREKLQN 305
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
342-464 |
9.69e-04 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 40.69 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 342 RVVTITGPNTGGKTVTLKTLGLAMLMAKVGMFVPAREPVELPWfSQVLADIGdeqSIEQnLSTfsGHVRR--ISRILeaV 419
Cdd:cd00267 26 EIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPL-EELRRRIG---YVPQ-LSG--GQRQRvaLARAL--L 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 516254850 420 TEDDnaLVLLDEVGAGTDPSEGSALAMSLLQyLCDRAGLTVATTH 464
Cdd:cd00267 97 LNPD--LLLLDEPTSGLDPASRERLLELLRE-LAEEGRTVIIVTH 138
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
536-640 |
9.75e-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: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 536 NETIAQLEAQRRRQETKADEASQIVAQAERLNQEIAEKAEQLRQREERLKLEQERAIREAIEAAKEEIAKVIRRLQQGTP 615
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV 763
|
90 100
....*....|....*....|....*
gi 516254850 616 TAQDAQKATAAIDAIAERNLPSRRE 640
Cdd:COG4913 764 ERELRENLEERIDALRARLNRAEEE 788
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
543-657 |
1.16e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 543 EAQRRRQET-KADEASQiVAQAERLNQEIAEKAEQLRQREE-RLKLEQERAIREAIEAAKEEIAKV--IRRLQQGTPTAQ 618
Cdd:PTZ00121 1435 EAKKKAEEAkKADEAKK-KAEEAKKAEEAKKKAEEAKKADEaKKKAEEAKKADEAKKKAEEAKKKAdeAKKAAEAKKKAD 1513
|
90 100 110
....*....|....*....|....*....|....*....
gi 516254850 619 DAQKATAAIDAIAERNLPSRREPPKPKPGFRPKEGDRVR 657
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
537-633 |
1.31e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 537 ETIAQLEAQRRRQETKADEASQIVAQAERLNQEIAEKAEQLRQREERL-KLEQERA-IREAIEAAKEEIAKVIRRLQQGT 614
Cdd:COG4913 668 REIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIgRLEKELEqAEEELDELQDRLEAAEDLARLEL 747
|
90
....*....|....*....
gi 516254850 615 PTAQDAQKATAAIDAIAER 633
Cdd:COG4913 748 RALLEERFAAALGDAVERE 766
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
537-635 |
1.61e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 537 ETIAQLEAQRRRQETKADEASQIVAQAERLNQEIAEKAEQLRQREERLKLEQERAIREAIEAAKE--EIAKVIRRLQQGT 614
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEElaELEEELEELEEEL 339
|
90 100
....*....|....*....|.
gi 516254850 615 PTAQDAQKATAAIDAIAERNL 635
Cdd:COG1196 340 EELEEELEEAEEELEEAEAEL 360
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
537-640 |
1.65e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 537 ETIAQLEAQRRRQETKADEASQIVAQAERLNQEIAEKAEQLRQREERL------KLEQERAIREAIEAAKEEIAKVIRRL 610
Cdd:PRK02224 502 EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELeaeaeeKREAAAEAEEEAEEAREEVAELNSKL 581
|
90 100 110
....*....|....*....|....*....|..
gi 516254850 611 QQGTPTAQDAQKATAAIDAIAE--RNLPSRRE 640
Cdd:PRK02224 582 AELKERIESLERIRTLLAAIADaeDEIERLRE 613
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
534-640 |
1.97e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 534 DVNETIAQLEAQRRRQETKADEASQivaQAERLNQEIAEKAEQLRQREErlKLEQERAIREAIEAAKEEIAKVIRRLQQg 613
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEE---ELEELEEELEEAEEELEEAEA--ELAEAEEALLEAEAELAEAEEELEELAE- 386
|
90 100
....*....|....*....|....*..
gi 516254850 614 tptaQDAQKATAAIDAIAERNLPSRRE 640
Cdd:COG1196 387 ----ELLEALRAAAELAAQLEELEEAE 409
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
534-633 |
2.04e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 534 DVNETIAQLEAQRRRQETKADEASQIVAQAERLNQEIAEKAEQLRQREERLKlEQERAIREAIEAAKEEIAKVIRRLQQg 613
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-AEEYELLAELARLEQDIARLEERRRE- 313
|
90 100
....*....|....*....|
gi 516254850 614 tpTAQDAQKATAAIDAIAER 633
Cdd:COG1196 314 --LEERLEELEEELAELEEE 331
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
534-612 |
2.91e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 534 DVNETIAQLEAQRRRQETKADEASQivAQAERLNQEIAEKAEQL-----RQREERLKLEQERAIREAIEAAKEEIAKVIR 608
Cdd:COG0542 415 ELERRLEQLEIEKEALKKEQDEASF--ERLAELRDELAELEEELealkaRWEAEKELIEEIQELKEELEQRYGKIPELEK 492
|
....
gi 516254850 609 RLQQ 612
Cdd:COG0542 493 ELAE 496
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
504-636 |
2.98e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 504 SNALSIARRLGLTSQVVDSAQEYVTS--GISVDVNETIAQLEAQRRRQETKADEASQivaQAERLNQEIAEKAEQLRQRE 581
Cdd:COG4942 129 EDFLDAVRRLQYLKYLAPARREQAEElrADLAELAALRAELEAERAELEALLAELEE---ERAALEALKAERQKLLARLE 205
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 516254850 582 ERLKLEQERAirEAIEAAKEEIAKVIRRLQQGTPTAQDAQKATAAIDAIAERNLP 636
Cdd:COG4942 206 KELAELAAEL--AELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLPWP 258
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
534-642 |
2.99e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 534 DVNETIAQLEAQRRRQETKADEASQIVAQAERLNQEIAEKAEQLRQREERLKLEQERAIREAIEAAKEEIAKVIRRLQQG 613
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
90 100
....*....|....*....|....*....
gi 516254850 614 TPTAQDAQKATAAIDAIAERNLPSRREPP 642
Cdd:COG3883 231 AAAAAAAAAAAAAASAAGAGAAGAAGAAA 259
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
513-633 |
4.14e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.21 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 513 LGLTSQVVDSAQEYVTSGIS-VDVNETIAQLEAQRRRQETKADEASQIVAQAERLNQeiAEKAEQLRQREE-RLKLEQER 590
Cdd:TIGR02794 20 LGSLYHSVKPEPGGGAEIIQaVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQ--AEEAEKQRAAEQaRQKELEQR 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 516254850 591 AIREAIEAAKEEIAKVIR--RLQQGTPTAQDAQKATAAIDAIAER 633
Cdd:TIGR02794 98 AAAEKAAKQAEQAAKQAEekQKQAEEAKAKQAAEAKAKAEAEAER 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
535-640 |
4.14e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 535 VNETIAQLEAQRRRQETKADEA----SQIVAQAERLNQEIAEKAEQLRQREERL-KLEQERAI-REAIEAAKEEIAKVIR 608
Cdd:COG1196 244 LEAELEELEAELEELEAELAELeaelEELRLELEELELELEEAQAEEYELLAELaRLEQDIARlEERRRELEERLEELEE 323
|
90 100 110
....*....|....*....|....*....|..
gi 516254850 609 RLQQGTPTAQDAQKATAAIDAIAERNLPSRRE 640
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEE 355
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
524-640 |
5.74e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 524 QEYVTSGISVDVNETIAQLEAQRRRQETKADEASQIVAQAERLNQEIAEKAEQLRQREERLK---LEQERAIREAIEAAK 600
Cdd:TIGR02169 221 REYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlgEEEQLRVKEKIGELE 300
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 516254850 601 EEIAKVIRRLQQGTPTAQDAQ----KATAAIDAIAERNLPSRRE 640
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEerlaKLEAEIDKLLAEIEELERE 344
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
511-653 |
6.77e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 511 RRLGLTSQVVDSAQEYVTSGISV--DVNETIAQLEAQRRRQETKADEASQivaQAERLNQEIAEKAEQLRQREERLKLEQ 588
Cdd:COG3883 119 DRLSALSKIADADADLLEELKADkaELEAKKAELEAKLAELEALKAELEA---AKAELEAQQAEQEALLAQLSAEEAAAE 195
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516254850 589 ERAIREAIEAAKEEIAKVIRRLQQGTPTAQDAQKATAAIDAIAERNLPSRREPPKPKPGFRPKEG 653
Cdd:COG3883 196 AQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAG 260
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
534-612 |
7.84e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 534 DVNETIAQLEAQRRRQETKADEASQIVAQAERLNQEIAEKAEQLRQREERLKLEQER--AIREAIEAAKEEIAKVIRRLQ 611
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaEAEAEIEERREELGERARALY 96
|
.
gi 516254850 612 Q 612
Cdd:COG3883 97 R 97
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
540-642 |
7.96e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.36 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 540 AQLEAQRRRQETKADEASQIVAQAERLNQEIAEKAEQlRQREERLKLEQERAIREaIEAAKEEIAKVIRRLQqgtptaQD 619
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEE-RAALEALKAERQKLLAR-LEKELAELAAELAELQ------QE 221
|
90 100
....*....|....*....|...
gi 516254850 620 AQKATAAIDAIAERNLPSRREPP 642
Cdd:COG4942 222 AEELEALIARLEAEAAAAAERTP 244
|
|
| MAT1 |
pfam06391 |
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ... |
533-646 |
9.60e-03 |
|
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.
Pssm-ID: 461894 [Multi-domain] Cd Length: 202 Bit Score: 38.38 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 533 VDVNETIAQLEAQRRrqetkaDEASQIVAQAERLNQE--------IAEKAEQLRQREERLKLEQEraIREAIEAAKEEIa 604
Cdd:pfam06391 61 IDVEETEKKIEQYEK------ENKDLILKNKMKLSQEeeeleellELEKREKEERRKEEKQEEEE--EKEKKEKAKQEL- 131
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 516254850 605 kvIRRLQQGTPTAQD----AQKATAAIDAIAERNLPSRREPPKPKP 646
Cdd:pfam06391 132 --IDELMTSNKDAEEiiaqHKKTAKKRKSERRRKLEELNRVLEQKP 175
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
542-635 |
9.86e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 39.09 E-value: 9.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516254850 542 LEAQRRRQETKADEASQI-VAQAERlNQEIAeKAEQLRQREERlKLEQERAIREAIEAAKE-EIAKVIRRLQQGTPTAQD 619
Cdd:COG2268 186 LDALGRRKIAEIIRDARIaEAEAER-ETEIA-IAQANREAEEA-ELEQEREIETARIAEAEaELAKKKAEERREAETARA 262
|
90
....*....|....*..
gi 516254850 620 AQKATAAI-DAIAERNL 635
Cdd:COG2268 263 EAEAAYEIaEANAEREV 279
|
|
| |
