|
Name |
Accession |
Description |
Interval |
E-value |
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
3-784 |
0e+00 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 1013.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 3 NSKTLEKLEYHKIVQQVSHFANTEMAKSKILKMQPSIDLETIQKWQEEVEESLAILQQGKNIPIPRLVELSMAFRRLEIS 82
Cdd:COG1193 2 NEKTLEKLEFDKILELLAEYAVSELGKELARKLRPSTDLEEVERLLAETAEARRLLRLEGGLPLGGIPDIRPLLKRAEEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 83 AALNPKELGQIGRLLTTTNQVTQFFADLEAEekfYPSLKFWVDQCVSLPQVVKEIQSTVSDEGSVLNSASSQLAAIRKNQ 162
Cdd:COG1193 82 GVLSPEELLDIARTLRAARRLKRFLEELEEE---YPALKELAERLPPLPELEKEIDRAIDEDGEVKDSASPELRRIRREI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 163 SQTESQIRNQLNQLLKSKGNQ--LSDRLITIRNDRYVLPVKAEFKGQFGGTIHDQSATGQTVFMEPKVVVELNNRLAQLV 240
Cdd:COG1193 159 RSLEQRIREKLESILRSASYQkyLQDAIITIRNGRYVIPVKAEYKGKIPGIVHDQSASGQTLFIEPMAVVELNNELRELE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 241 IDERTEIERILLEISLMIAPYVEKIKHNQSMIAQLDFIQSKAEYAKSIVATKPAFSKDNQVALWQARHPLIDSDAIVAND 320
Cdd:COG1193 239 AEERREIERILRELSALVREYAEELLENLEILAELDFIFAKARYALELKAVKPELNDEGYIKLKKARHPLLDLKKVVPID 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 321 ILIGENYHILLITGPNTGGKTIILKTIGLIQLMGQSGLHVPCDSGSQLGIFQSIYADIGDEQSIEQSLSTFSSHMTNIVN 400
Cdd:COG1193 319 IELGEDFRTLVITGPNTGGKTVTLKTVGLLTLMAQSGLPIPAAEGSELPVFDNIFADIGDEQSIEQSLSTFSSHMTNIVE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 401 IVEEADYQSLVLFDELGSGTDPQEGAALAISILDYLRKVGATVLATTHYPELKVYAHERAKTINASMEFDVQTLSPTYRL 480
Cdd:COG1193 399 ILEKADENSLVLLDELGAGTDPQEGAALAIAILEELLERGARVVATTHYSELKAYAYNTEGVENASVEFDVETLSPTYRL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 481 MIGVPGRSNAIEISRRLGLRQDILEVAQKGISQDSQSLNEMVAKLERERRESELKNKEAQTFLEKAEVLWQDLRTEYDRY 560
Cdd:COG1193 479 LIGVPGRSNAFEIARRLGLPEEIIERARELLGEESIDVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEEL 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 561 LEQKQNLIERSKRQANEKVEKAQKEAEELLQEIRDLQLvqgqnqtiKEHVLIDKKKAFDQLKQ--PENLKKNKILKRV-K 637
Cdd:COG1193 559 EEEKEEILEKAREEAEEILREARKEAEELIRELREAQA--------EEEELKEARKKLEELKQelEEKLEKPKKKAKPaK 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 638 RAKKIQVGDDVEVLSYGQRGTVLEQVEKNEYIVQMGIIKMKIASDELKPISKVEPKQK------VNVQRQAGSKVKTTLD 711
Cdd:COG1193 631 PPEELKVGDRVRVLSLGQKGEVLEIPKGGEAEVQVGILKMTVKLSDLEKVEKKKPKKPkkrpagVSVSVSKASTVSPELD 710
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2290035205 712 IRGLRYEEAMIKLKQYLDQALLSNHSLVTIIHGKGTGALRQGVKDQLNNHPHVDHFEYSPPNAGGDGSTRVYF 784
Cdd:COG1193 711 LRGMRVEEALPELDKYLDDALLAGLPEVRIIHGKGTGALRKGVREYLKRHPYVKSFRLGEPGEGGDGVTVVEL 783
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
3-784 |
0e+00 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 891.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 3 NSKTLEKLEYHKIVQQVSHFANTEMAKSKILKMQPSIDLETIQKWQEEVEESLAILQQGKNIPIPRLVELSMAFRRLEIS 82
Cdd:PRK00409 2 QEKTLRVLEFNKIKEQLKTFAASELGKEKVLQLDPETDFEEVEELLEETDEAAKLLRLKGLPPFEGVKDIDDALKRAEKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 83 AALNPKELGQIGRLLTTTNQVTQFFADLEaEEKFYPSLKFWVDQCVSLPQVVKEIQSTVSDEGSVLNSASSQLAAIRKNQ 162
Cdd:PRK00409 82 GVLSGDELLEIAKTLRYFRQLKRFIEDLE-EEEELPILEEWVAKIRTLPELEQEIHNCIDEEGEVKDSASEKLRGIRRQL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 163 SQTESQIRNQLNQLLKSKGNQ--LSDRLITIRNDRYVLPVKAEFKGQFGGTIHDQSATGQTVFMEPKVVVELNNRLAQLV 240
Cdd:PRK00409 161 RRKKSRIREKLESIIRSKSLQkyLQDTIITIRNDRYVLPVKAEYKHAIKGIVHDQSSSGATLYIEPQSVVELNNEIRELR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 241 IDERTEIERILLEISLMIAPYVEKIKHNQSMIAQLDFIQSKAEYAKSIVATKPAFSKDNQVALWQARHPLIDSDAIVAND 320
Cdd:PRK00409 241 NKEEQEIERILKELSAKVAKNLDFLKFLNKIFDELDFIFARARYAKALKATFPLFNDEGKIDLRQARHPLLDGEKVVPKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 321 ILIGENYHILLITGPNTGGKTIILKTIGLIQLMGQSGLHVPCDSGSQLGIFQSIYADIGDEQSIEQSLSTFSSHMTNIVN 400
Cdd:PRK00409 321 ISLGFDKTVLVITGPNTGGKTVTLKTLGLAALMAKSGLPIPANEPSEIPVFKEIFADIGDEQSIEQSLSTFSGHMTNIVR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 401 IVEEADYQSLVLFDELGSGTDPQEGAALAISILDYLRKVGATVLATTHYPELKVYAHERAKTINASMEFDVQTLSPTYRL 480
Cdd:PRK00409 401 ILEKADKNSLVLFDELGAGTDPDEGAALAISILEYLRKRGAKIIATTHYKELKALMYNREGVENASVEFDEETLRPTYRL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 481 MIGVPGRSNAIEISRRLGLRQDILEVAQKGISQDSQSLNEMVAKLERERRESELKNKEAQTFLEKAEVLWQDLRTEYDRY 560
Cdd:PRK00409 481 LIGIPGKSNAFEIAKRLGLPENIIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 561 LEQKQNLIERSKRQANEKVEKAQKEAEELLQEIRDLQlvQGQNQTIKEHVLIDKKKafdQLKQPENLKKNKILKRVKRAK 640
Cdd:PRK00409 561 QEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQ--KGGYASVKAHELIEARK---RLNKANEKKEKKKKKQKEKQE 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 641 KIQVGDDVEVLSYGQRGTVLEQVEKNEYIVQMGIIKMKIASDELKPI--SKVEPKQKVNVQRQAGSKVKTTLDIRGLRYE 718
Cdd:PRK00409 636 ELKVGDEVKYLSLGQKGEVLSIPDDKEAIVQAGIMKMKVPLSDLEKIqkPKKKKKKKPKTVKPKPRTVSLELDLRGMRYE 715
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2290035205 719 EAMIKLKQYLDQALLSNHSLVTIIHGKGTGALRQGVKDQLNNHPHVDHFEYSPPNAGGDGSTRVYF 784
Cdd:PRK00409 716 EALERLDKYLDDALLAGYGEVLIIHGKGTGKLRKGVQEFLKKHPSVKSFRDAPPNEGGFGVTIVEL 781
|
|
| mutS2 |
TIGR01069 |
MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch ... |
5-783 |
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: 591.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 5 KTLEKLEYHKIVQQVSHFANTEMAKSKILKMQPSIDLETIQkwqEEVEESLAILQQGKNIPIPRLVELSMAFRRLEISAA 84
Cdd:TIGR01069 4 KDLIKLEFDKVKENLLKQTFTPLGKEDAIGLKPPKSVEESK---EIIIKLTALGSIENNVRFFGFEDIRELLKRAELGGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 85 LNPKElgQIGRLLTTTNQVTQFfADLEAEEKFYPSLKFWVDQCVSLPQVVKEIQSTVSDEGSVLNSASSQLAAIRKNQSQ 164
Cdd:TIGR01069 81 VKGLE--YILVIQNALKTVKHL-KVLSEHVLDLEILFHLRLNLITLPPLENDIIACIDDDGKVKDGASEELDAIRESLKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 165 TESQIRNQLNQLLKSK--GNQLSDRLITIRNDRYVLPVKAEFKGQFGGTIHDQSATGQTVFMEPKVVVELNNRLAQLVID 242
Cdd:TIGR01069 158 LEEEVVKRLHKIIRSKelAKYLSDTIVTIRNGRYVLPLKSGFKGKIKGIVHDTSSSGETFYIEPQAIVKLNNKLAQLKNE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 243 ERTEIERILLEISLMIAPYVEKIKHNQSMIAQLDFIQSKAEYAKSIVATKPAFSKDNQVALWQARHPLIDSDAIVANDIL 322
Cdd:TIGR01069 238 EECEIEKILRTLSEKVQEYLLELKFLFKEFDFLDSLQARARYAKAVKGEFPMPSFTGKIILENARHPLLKEPKVVPFTLN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 323 IGENYHILLITGPNTGGKTIILKTIGLIQLMGQSGLHVPCDSGSQLGIFQSIYADIGDEQSIEQSLSTFSSHMTNIVNIV 402
Cdd:TIGR01069 318 LKFEKRVLAITGPNTGGKTVTLKTLGLLALMFQSGIPIPANEHSEIPYFEEIFADIGDEQSIEQNLSTFSGHMKNISAIL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 403 EEADYQSLVLFDELGSGTDPQEGAALAISILDYLRKVGATVLATTHYPELKVYAHERAKTINASMEFDVQTLSPTYRLMI 482
Cdd:TIGR01069 398 SKTTENSLVLFDELGAGTDPDEGSALAISILEYLLKQNAQVLITTHYKELKALMYNNEGVENASVLFDEETLSPTYKLLK 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 483 GVPGRSNAIEISRRLGLRQDILEVAQKGISQDSQSLNEMVAKLERERRESELKNKEAQTFLEKAEVLWQDLRTEYDRYLE 562
Cdd:TIGR01069 478 GIPGESYAFEIAQRYGIPHFIIEQAKTFYGEFKEEINVLIEKLSALEKELEQKNEHLEKLLKEQEKLKKELEQEMEELKE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 563 QKQNLIERSKRQANEKVEKAQKEAEELLQEIrdlqlvqgqnQTIKEHVLIDKKKAFDQLKQPENlkKNKILKRVKRAKKI 642
Cdd:TIGR01069 558 RERNKKLELEKEAQEALKALKKEVESIIREL----------KEKKIHKAKEIKSIEDLVKLKET--KQKIPQKPTNFQAD 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 643 QVGDDVEVLSYGQRGTVLEQVEKNEYIVQMGIIKMKIASDELKPISKVEPKQKVNVQRQAGSK---VKTTLDIRGLRYEE 719
Cdd:TIGR01069 626 KIGDKVRIRYFGQKGKIVQILGGNKWNVTVGGMRMKVHGSELEKINKAPPPKKFKVPKTTKPEpkeASLTLDLRGQRSEE 705
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2290035205 720 AMIKLKQYLDQALLSNHSLVTIIHGKGTGALRQGVKDQLNNHPHVDHFEYSPPNAGGDGSTRVY 783
Cdd:TIGR01069 706 ALDRLEKFLNDALLAGYEVVLIIHGKGSGKLRKGVQELLKNHPKVKSFRDAPPNDGGSGVTIVY 769
|
|
| ABC_MutS2 |
cd03280 |
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ... |
303-499 |
1.13e-111 |
|
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: 337.68 E-value: 1.13e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 303 LWQARHPLI--DSDAIVANDILIGENYHILLITGPNTGGKTIILKTIGLIQLMGQSGLHVPCDSGSQLGIFQSIYADIGD 380
Cdd:cd03280 2 LREARHPLLplQGEKVVPLDIQLGENKRVLVITGPNAGGKTVTLKTLGLLTLMAQSGLPIPAAEGSSLPVFENIFADIGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 381 EQSIEQSLSTFSSHMTNIVNIVEEADYQSLVLFDELGSGTDPQEGAALAISILDYLRKVGATVLATTHYPELKVYAHERA 460
Cdd:cd03280 82 EQSIEQSLSTFSSHMKNIARILQHADPDSLVLLDELGSGTDPVEGAALAIAILEELLERGALVIATTHYGELKAYAYKRE 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 2290035205 461 KTINASMEFDVQTLSPTYRLMIGVPGRSNAIEISRRLGL 499
Cdd:cd03280 162 GVENASMEFDPETLKPTYRLLIGVPGRSNALEIARRLGL 200
|
|
| MUTSac |
smart00534 |
ATPase domain of DNA mismatch repair MUTS family; |
329-509 |
5.76e-69 |
|
ATPase domain of DNA mismatch repair MUTS family;
Pssm-ID: 197777 [Multi-domain] Cd Length: 185 Bit Score: 225.13 E-value: 5.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 329 ILLITGPNTGGKTIILKTIGLIQLMGQSGLHVPCDSgSQLGIFQSIYADIGDEQSIEQSLSTFSSHMTNIVNIVEEADYQ 408
Cdd:smart00534 1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAES-AELPVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 409 SLVLFDELGSGTDPQEGAALAISILDYL-RKVGATVLATTHYPELKVYAHERAKTINASMEFDVQT--LSPTYRLMIGVP 485
Cdd:smart00534 80 SLVLLDELGRGTSTYDGLAIAAAILEYLlEKIGARTLFATHYHELTKLADNHPGVRNLHMSALEETenITFLYKLKPGVA 159
|
170 180
....*....|....*....|....
gi 2290035205 486 GRSNAIEISRRLGLRQDILEVAQK 509
Cdd:smart00534 160 GKSYGIEVAKLAGLPKEVIERAKR 183
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
305-499 |
3.69e-55 |
|
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: 188.23 E-value: 3.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 305 QARHPLIDSDA----IVANDILIGENyHILLITGPNTGGKTIILKTIGLIQLMGQSGLHVPCDSGSqLGIFQSIYADIGD 380
Cdd:cd03243 4 GGRHPVLLALTkgetFVPNDINLGSG-RLLLITGPNMGGKSTYLRSIGLAVLLAQIGCFVPAESAS-IPLVDRIFTRIGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 381 EQSIEQSLSTFSSHMTNIVNIVEEADYQSLVLFDELGSGTDPQEGAALAISILDYLRKVGATVLATTHYPEL--KVYAHE 458
Cdd:cd03243 82 EDSISDGRSTFMAELLELKEILSLATPRSLVLIDELGRGTSTAEGLAIAYAVLEHLLEKGCRTLFATHFHELadLPEQVP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2290035205 459 RAKTINASMEFDVQTLSPTYRLMIGVPGRSNAIEISRRLGL 499
Cdd:cd03243 162 GVKNLHMEELITTGGLTFTYKLIDGICDPSYALQIAELAGL 202
|
|
| mutS1 |
TIGR01070 |
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair] |
36-547 |
3.01e-42 |
|
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273427 [Multi-domain] Cd Length: 840 Bit Score: 165.71 E-value: 3.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 36 QPSIDLETIQKWQEEVEESL--AILQQGKNIPIPRLVELSMAFRRLEISAAlNPKELGqigRLLTTTNQVTQFFADLEAE 113
Cdd:TIGR01070 295 RPLRDREVLEARQDTVEVLLrhFFLREGLRPLLKEVGDLERLAARVALGNA-RPRDLA---RLRTSLEQLPELRALLEEL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 114 EKfyPSLKFWVDQCVSLPQVVKEIQSTVSDEGSVLNSASsqlAAIRKNQSQTESQIRNqlnqlLKSKGNQLSDRLITIRN 193
Cdd:TIGR01070 371 EG--PTLQALAAQIDDFSELLELLEAALIENPPLVVRDG---GLIREGYDEELDELRA-----ASREGTDYLARLEARER 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 194 DRYVLP-VKAEFKGQFGGTIHDQSATGQTVFMEPKVVVELNNRlAQLVIDERTEIERILLEISLMIA------------- 259
Cdd:TIGR01070 441 ERTGIPtLKVGYNAVFGYYIEVTRGQLHLVPAHYRRRQTLKNA-ERYITPELKEKEDKVLEAEGKILalekelfeelrel 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 260 --PYVEKIKHNQSMIAQLDFIQSKAEYAKSIVATKPAFSKDNQVALWQARHPLID---SDAIVANDILIGENYHILLITG 334
Cdd:TIGR01070 520 lkKYLEALQEAARALAELDVLANLAEVAETLHYTRPRFGDDPQLRIREGRHPVVEqvlRTPFVPNDLEMAHNRRMLLITG 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 335 PNTGGKTIILKTIGLIQLMGQSGLHVPCDSgSQLGIFQSIYADIGDEQSIEQSLSTFSSHMTNIVNIVEEADYQSLVLFD 414
Cdd:TIGR01070 600 PNMGGKSTYMRQTALIALLAQIGSFVPAES-AELPLFDRIFTRIGASDDLASGRSTFMVEMTEAANILHNATENSLVLFD 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 415 ELGSGTDPQEGAALAISILDYL-RKVGATVLATTHYPELKVYAH--ERAKTINASMEFDVQTLSPTYRLMIGVPGRSNAI 491
Cdd:TIGR01070 679 EIGRGTSTYDGLALAWAIAEYLhEHIRAKTLFATHYFELTALEEslPGLKNVHVAALEHNGTIVFLHQVLPGPASKSYGL 758
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2290035205 492 EISRRLGLRQDILEVAQKGISQDSQSLNEMVAKLererRESELKNKEAQTFLEKAE 547
Cdd:TIGR01070 759 AVAALAGLPKEVIARARQILTQLEARSTESEAPQ----RKAQTSAPEQISLFDEAE 810
|
|
| ABC_MutS1 |
cd03284 |
ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ... |
307-509 |
2.70e-34 |
|
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: 130.46 E-value: 2.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 307 RHP----LIDSDAIVANDILIGENYHILLITGPNTGGKTIILKTIGLIQLMGQSGLHVPCDSgSQLGIFQSIYADIGDEQ 382
Cdd:cd03284 6 RHPvveqVLDNEPFVPNDTELDPERQILLITGPNMAGKSTYLRQVALIALLAQIGSFVPASK-AEIGVVDRIFTRIGASD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 383 SIEQSLSTFSSHMTNIVNIVEEADYQSLVLFDELGSGTDPQEGAALAISILDYL-RKVGATVLATTHYPELKVYAH--ER 459
Cdd:cd03284 85 DLAGGRSTFMVEMVETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAIVEYLhEKIGAKTLFATHYHELTELEGklPR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2290035205 460 AKTINASMEFDVQTLSPTYRLMIGVPGRSNAIEISRRLGLRQDILEVAQK 509
Cdd:cd03284 165 VKNFHVAVKEKGGGVVFLHKIVEGAADKSYGIEVARLAGLPEEVIERARE 214
|
|
| MutS_V |
pfam00488 |
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ... |
330-509 |
4.93e-34 |
|
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: 128.85 E-value: 4.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 330 LLITGPNTGGKTIILKTIGLIQLMGQSGLHVPCDSGSqLGIFQSIYADIGDEQSIEQSLSTFSSHMTNIVNIVEEADYQS 409
Cdd:pfam00488 1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAE-IGIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 410 LVLFDELGSGTDPQEGAALAISILDYL-RKVGATVLATTHYPELKVYAHERAKTINASMEF--DVQTLSPTYRLMIGVPG 486
Cdd:pfam00488 80 LVILDELGRGTSTYDGLAIAWAVAEHLaEKIKARTLFATHYHELTKLAEKLPAVKNLHMAAveDDDDIVFLYKVQPGAAD 159
|
170 180
....*....|....*....|...
gi 2290035205 487 RSNAIEISRRLGLRQDILEVAQK 509
Cdd:pfam00488 160 KSYGIHVAELAGLPESVVERARE 182
|
|
| ABC_MSH2_euk |
cd03285 |
ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA ... |
303-511 |
6.30e-33 |
|
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: 126.72 E-value: 6.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 303 LWQARHPLI---DSDAIVANDI-LIGENYHILLITGPNTGGKTIILKTIGLIQLMGQSGLHVPCDSgSQLGIFQSIYADI 378
Cdd:cd03285 2 LKEARHPCVeaqDDVAFIPNDVtLTRGKSRFLIITGPNMGGKSTYIRQIGVIVLMAQIGCFVPCDS-ADIPIVDCILARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 379 GDEQSIEQSLSTFSSHMTNIVNIVEEADYQSLVLFDELGSGTDPQEGAALAISILDYL-RKVGATVLATTHYPELKVYAH 457
Cdd:cd03285 81 GASDSQLKGVSTFMAEMLETAAILKSATENSLIIIDELGRGTSTYDGFGLAWAIAEYIaTQIKCFCLFATHFHELTALAD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2290035205 458 ERAKTIN----ASMEFDVQTLSPTYRLMIGVPGRSNAIEISRRLGLRQDILEVA-QKGI 511
Cdd:cd03285 161 EVPNVKNlhvtALTDDASRTLTMLYKVEKGACDQSFGIHVAELANFPKEVIEMAkQKAL 219
|
|
| ABC_MSH4_euk |
cd03282 |
ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA ... |
305-452 |
3.78e-32 |
|
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: 124.04 E-value: 3.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 305 QARHPLIDSDA--IVANDI-LIGENYHILLITGPNTGGKTIILKTIGLIQLMGQSGLHVPCDSGSqLGIFQSIYADIGDE 381
Cdd:cd03282 4 DSRHPILDRDKknFIPNDIyLTRGSSRFHIITGPNMSGKSTYLKQIALLAIMAQIGCFVPAEYAT-LPIFNRLLSRLSND 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2290035205 382 QSIEQSLSTFSSHMTNIVNIVEEADYQSLVLFDELGSGTDPQEGAALAISILDYLRKVGATVLATTHYPEL 452
Cdd:cd03282 83 DSMERNLSTFASEMSETAYILDYADGDSLVLIDELGRGTSSADGFAISLAILECLIKKESTVFFATHFRDI 153
|
|
| ABC_MSH5_euk |
cd03281 |
ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA ... |
305-499 |
5.18e-32 |
|
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: 123.95 E-value: 5.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 305 QARHPLID--SDAIVANDILI-GENYHILLITGPNTGGKTIILKTIGLIQLMGQSGLHVPCDSgSQLGIFQSIYADIGDE 381
Cdd:cd03281 4 GGRHPLLElfVDSFVPNDTEIgGGGPSIMVITGPNSSGKSVYLKQVALIVFLAHIGSFVPADS-ATIGLVDKIFTRMSSR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 382 QSIEQSLSTFSSHMTNIVNIVEEADYQSLVLFDELGSGTDPQEGAALAISILDYLRKVGAT---VLATTHY--------- 449
Cdd:cd03281 83 ESVSSGQSAFMIDLYQVSKALRLATRRSLVLIDEFGKGTDTEDGAGLLIATIEHLLKRGPEcprVIVSTHFhelfnrsll 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2290035205 450 PELKVYAHERAKT-INASMEFDVQTLSPTYRLMIGVPGRSNAIEISRRLGL 499
Cdd:cd03281 163 PERLKIKFLTMEVlLNPTSTSPNEDITYLYRLVPGLADTSFAIHCAKLAGI 213
|
|
| PRK05399 |
PRK05399 |
DNA mismatch repair protein MutS; Provisional |
248-452 |
6.03e-32 |
|
DNA mismatch repair protein MutS; Provisional
Pssm-ID: 235444 [Multi-domain] Cd Length: 854 Bit Score: 133.30 E-value: 6.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 248 ERIL-LEISL------MIAPYVEKIKHNQSMIAQLDFIQSKAEYAKSIVATKPAFSKDNQVALWQARHP----LIDSDAI 316
Cdd:PRK05399 517 EKALaLEYELfeelreEVAEHIERLQKLAKALAELDVLASLAEVAEENNYVRPEFTDDPGIDIEEGRHPvveqVLGGEPF 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 317 VANDILIGENYHILLITGPNTGGKTIILKTIGLIQLMGQSGLHVPCDSGsQLGIFQSIYADIG--DEQSIEQslSTFSSH 394
Cdd:PRK05399 597 VPNDCDLDEERRLLLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAESA-RIGIVDRIFTRIGasDDLASGR--STFMVE 673
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2290035205 395 MTNIVNIVEEADYQSLVLFDELGSGTDPQEGAALAISILDYL-RKVGATVLATTHYPEL 452
Cdd:PRK05399 674 MTETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAVAEYLhDKIGAKTLFATHYHEL 732
|
|
| ABC_MSH3_euk |
cd03287 |
ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA ... |
306-507 |
8.36e-32 |
|
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: 123.37 E-value: 8.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 306 ARHPLIDS---DAIVANDI-LIGENYHILLITGPNTGGKTIILKTIGLIQLMGQSGLHVPCDSgSQLGIFQSIYADIGDE 381
Cdd:cd03287 6 GRHPMIESlldKSFVPNDIhLSAEGGYCQIITGPNMGGKSSYIRQVALITIMAQIGSFVPASS-ATLSIFDSVLTRMGAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 382 QSIEQSLSTFSSHMTNIVNIVEEADYQSLVLFDELGSGTDPQEGAALAISILDYLRKV-GATVLATTHYPELKVYAHERA 460
Cdd:cd03287 85 DSIQHGMSTFMVELSETSHILSNCTSRSLVILDELGRGTSTHDGIAIAYATLHYLLEEkKCLVLFVTHYPSLGEILRRFE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2290035205 461 KTI-NASMEF----------DVQTLSPTYRLMIGVPGRSNAIEISRRLGLRQDILEVA 507
Cdd:cd03287 165 GSIrNYHMSYlesqkdfetsDSQSITFLYKLVRGLASRSFGLNVARLAGLPKSIISRA 222
|
|
| ABC_MSH6_euk |
cd03286 |
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ... |
305-507 |
8.31e-31 |
|
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: 120.61 E-value: 8.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 305 QARHPLI---DSDAIVANDILIGENY-HILLITGPNTGGKTIILKTIGLIQLMGQSGLHVPCDSgSQLGIFQSIYADIGD 380
Cdd:cd03286 4 ELRHPCLnasTASSFVPNDVDLGATSpRILVLTGPNMGGKSTLLRTVCLAVIMAQMGMDVPAKS-MRLSLVDRIFTRIGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 381 EQSIEQSLSTFSSHMTNIVNIVEEADYQSLVLFDELGSGTDPQEGAALAISILDYL-RKVGATVLATTHYPELKVYAHER 459
Cdd:cd03286 83 RDDIMKGESTFMVELSETANILRHATPDSLVILDELGRGTSTHDGYAIAHAVLEYLvKKVKCLTLFSTHYHSLCDEFHEH 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2290035205 460 AKTINASMEFDVQTLSPT--------YRLMIGVPGRSNAIEISRRLGLRQDILEVA 507
Cdd:cd03286 163 GGVRLGHMACAVKNESDPtirditflYKLVAGICPKSYGLYVALMAGIPDGVVERA 218
|
|
| MutS |
COG0249 |
DNA mismatch repair ATPase MutS [Replication, recombination and repair]; |
242-452 |
2.47e-29 |
|
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
Pssm-ID: 440019 [Multi-domain] Cd Length: 861 Bit Score: 125.17 E-value: 2.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 242 DERTEIE-RILLEISLMIAPYVEKIKHNQSMIAQLDFIQSKAEYAKSIVATKPAFSKDNQVALWQARHP----LIDSDAI 316
Cdd:COG0249 523 ERALALEyELFEELREEVAAHIERLQALARALAELDVLASLAEVAVENNYVRPELDDSPGIEIEGGRHPvveqALPGEPF 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 317 VANDILIGENYHILLITGPNTGGKTIILKTIGLIQLMGQSGLHVPCDSGsQLGIFQSIYADIG--DEqsIEQSLSTFSSH 394
Cdd:COG0249 603 VPNDCDLDPDRRILLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAESA-RIGIVDRIFTRVGasDD--LARGQSTFMVE 679
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2290035205 395 MTNIVNIVEEADYQSLVLFDELGSGTDPQEGAALAISILDYL-RKVGATVLATTHYPEL 452
Cdd:COG0249 680 MTETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAVAEYLhDKIRARTLFATHYHEL 738
|
|
| Smr |
pfam01713 |
Smr domain; This family includes the Smr (Small MutS Related) proteins, and the C-terminal ... |
711-784 |
2.07e-25 |
|
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: 99.85 E-value: 2.07e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2290035205 711 DIRGLRYEEAMIKLKQYLDQALLSNHSLVTIIHGKGT-GALRQGVKDQLNNHPHVDHFEYSPPNAGGDGSTRVYF 784
Cdd:pfam01713 1 DLHGMTVEEAREALDKFLDDALLAGLRCVLIIHGKGThGVLRKAVREWLKQHPLVLAFRSAPPGEGGDGATYVLL 75
|
|
| MUTSd |
smart00533 |
DNA-binding domain of DNA mismatch repair MUTS family; |
31-312 |
1.08e-24 |
|
DNA-binding domain of DNA mismatch repair MUTS family;
Pssm-ID: 214710 [Multi-domain] Cd Length: 308 Bit Score: 105.46 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 31 KILKMQPSIDLETIQKWQEEVEE---SLAILQQGKNiPIPRLVELSMAFRRLEISAAlNPKELGqigRLLTTTNQVTQFF 107
Cdd:smart00533 21 RRWLLQPLLDLKEINERLDAVEElveNPELRQKLRQ-LLKRIPDLERLLSRIERGRA-SPRDLL---RLYDSLEGLKEIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 108 ADLE--AEEKFYPSLKFWVDQCVSLPQVVKEI-----QSTVSDEGSVLNSASSQLAAIRKNQSQTESQIRNQLNQLLKSK 180
Cdd:smart00533 96 QLLEslDGPLLGLLLKVILEPLLELLELLLELlndddPLEVNDGGLIKDGFDPELDELREKLEELEEELEELLKKEREEL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 181 G-NQLSDRLITIRNdrYVLPVKAEFKGQFGGTIHDQSATGQTVFMEPKVVVELNNRLAQLVIDERTEIERILLEISLMIA 259
Cdd:smart00533 176 GiDSLKLGYNKVHG--YYIEVTKSEAKKVPKDFIRRSSLKNTERFTTPELKELENELLEAKEEIERLEKEILRELLEKVL 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2290035205 260 PYVEKIKHNQSMIAQLDFIQSKAEYAKSIVATKPAFSKDNQVALWQARHPLID 312
Cdd:smart00533 254 EYLEELRALAEALAELDVLLSLATLAAEGNYVRPEFVDSGELEIKNGRHPVLE 306
|
|
| ABC_MutS-like |
cd03283 |
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ... |
305-499 |
2.02e-24 |
|
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: 101.61 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 305 QARHPLIDSDAIVANDILIgENYHILLITGPNTGGKTIILKTIGLIQLMGQSGLHVPCDS--GSQLGIFQSIyaDIGDeq 382
Cdd:cd03283 4 NLGHPLIGREKRVANDIDM-EKKNGILITGSNMSGKSTFLRTIGVNVILAQAGAPVCASSfeLPPVKIFTSI--RVSD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 383 SIEQSLSTFSSHMTNIVNIVEEAD--YQSLVLFDELGSGTDPQEGAALAISILDYLRKVGATVLATTHYPEL--KVYAHE 458
Cdd:cd03283 79 DLRDGISYFYAELRRLKEIVEKAKkgEPVLFLLDEIFKGTNSRERQAASAAVLKFLKNKNTIGIISTHDLELadLLDLDS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2290035205 459 RAKTINASMEFDVQTLSPTYRLMIGVPGRSNAIEISRRLGL 499
Cdd:cd03283 159 AVRNYHFREDIDDNKLIFDYKLKPGVSPTRNALRLMKKIGI 199
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
307-453 |
1.79e-18 |
|
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: 83.18 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 307 RHPLIdsdaIVANDILIGENyHILLITGPNTGGKTIILKTIGLIQLMGQSGLHVPcdSGSQLGIFqSIYADIGDEQSIEQ 386
Cdd:cd03227 6 RFPSY----FVPNDVTFGEG-SLTIITGPNGSGKSTILDAIGLALGGAQSATRRR--SGVKAGCI-VAAVSAELIFTRLQ 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2290035205 387 sLSTFSSHMTNIVNIVEEADYQ--SLVLFDELGSGTDPQEGAALAISILDYLRKvGATVLATTHYPELK 453
Cdd:cd03227 78 -LSGGEKELSALALILALASLKprPLYILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHLPELA 144
|
|
| SMR |
smart00463 |
Small MutS-related domain; |
707-784 |
2.67e-15 |
|
Small MutS-related domain;
Pssm-ID: 214676 [Multi-domain] Cd Length: 80 Bit Score: 71.56 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 707 KTTLDIRGLRYEEAMIKLKQYLDQALLSN-HSLVTIIHGKGTGALR--QGVKDQLNNHPHVDHFEYSPPnaGGDGSTRVY 783
Cdd:smart00463 1 KWSLDLHGLTVEEALTALDKFLNNARLKGlEQKLVIITGKGKHSLGgkSGVKPALKEHLRVESFRFAEE--GNSGVLVVK 78
|
.
gi 2290035205 784 F 784
Cdd:smart00463 79 L 79
|
|
| MSSS |
pfam20297 |
MutS2 and Smr-associated SH3 domain; This is a SH3-like domain associated with the MutS-like ... |
644-684 |
1.23e-09 |
|
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: 53.96 E-value: 1.23e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2290035205 644 VGDDVEVLSYGQRGTVLE-QVEKNEYIVQMGIIKMKIASDEL 684
Cdd:pfam20297 1 VGDEVRVKSLGQKGEVLEvPGKKGEVEVQVGIMKMTVKLSDL 42
|
|
| SmrA |
COG2840 |
DNA-nicking endonuclease, Smr domain [Replication, recombination and repair]; |
709-783 |
2.43e-08 |
|
DNA-nicking endonuclease, Smr domain [Replication, recombination and repair];
Pssm-ID: 442088 [Multi-domain] Cd Length: 177 Bit Score: 54.53 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 709 TLDIRGLRYEEAMIKLKQYLDQALLSNHSLVTIIHGKGT------GALRQGVKDQLNNHPHVDHFEYSPPNAGGDGSTRV 782
Cdd:COG2840 91 RLDLHGLTVEEAREALAAFLAEAQRRGLRCVLIIHGKGLgspggrPVLKSQVPRWLRQHPEVLAFHSAPPRHGGSGALYV 170
|
.
gi 2290035205 783 Y 783
Cdd:COG2840 171 L 171
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
307-452 |
1.35e-06 |
|
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: 48.78 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 307 RHPLIDSDAIVANDILIGENyHILLITGPNTGGKTIILKTIGLIqlmgqsglhVPCDSGS----QLGIFQSIYADIGDEQ 382
Cdd:cd00267 6 SFRYGGRTALDNVSLTLKAG-EIVALVGPNGSGKSTLLRAIAGL---------LKPTSGEilidGKDIAKLPLEELRRRI 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2290035205 383 SIEQSLSTFSSHMTNIVN-IVEEADyqsLVLFDELGSGTDPQEGAALAISILDYLRKvGATVLATTHYPEL 452
Cdd:cd00267 76 GYVPQLSGGQRQRVALARaLLLNPD---LLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPEL 142
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
501-666 |
3.22e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.79 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 501 QDILEVAQKGISQDSQ---SLNEMVAKLERERRESELKNKEAQTFLEKAEVLWQDLRTEYDRYLEQKQNLiERSKRQANE 577
Cdd:TIGR04523 320 EKKLEEIQNQISQNNKiisQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL-ESQINDLES 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 578 KVEKAQKEAEELLQEIRDLQ----LVQGQNQTIKEHVlIDKKKAFDQLKQPENLKKNKI--LKRVKRAKKIQVgdDVEVL 651
Cdd:TIGR04523 399 KIQNQEKLNQQKDEQIKKLQqekeLLEKEIERLKETI-IKNNSEIKDLTNQDSVKELIIknLDNTRESLETQL--KVLSR 475
|
170
....*....|....*
gi 2290035205 652 SYGQRGTVLEQVEKN 666
Cdd:TIGR04523 476 SINKIKQNLEQKQKE 490
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
487-726 |
2.16e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 487 RSNAIEISRRLGLRQDILEVAQKgiSQDSQSLNEMVAKLERERRESELKNKEAQTflEKAEvlwqdlrtEYDRYLEQKQN 566
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKK--AEEKKKADEAKKKAEEAKKADEAKKKAEEA--KKAE--------EAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 567 lIERSKRQANE--KVEKAQKEAEELLQEIRDLQLVQGQNQTIKEHVLIDKKKAFDQLKQPENLKKNKILKRVKRAKKIQV 644
Cdd:PTZ00121 1472 -ADEAKKKAEEakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE 1550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 645 GDDVEVLSYGQRGTVLEQVEKNEYIVQMGIIKMKIAsdelkpiSKVEPKQKVNVQRQAGSKVKTTLDiRGLRYEEAMIKL 724
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA-------KKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIKA 1622
|
..
gi 2290035205 725 KQ 726
Cdd:PTZ00121 1623 EE 1624
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
520-654 |
2.93e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 520 EMVAKLERERRESELKNKEAQTFLEKAEVLWQdlRTEYDRYLEQKQNLIERSKRQANE----------KVEKAQKEAEEL 589
Cdd:PTZ00121 1665 EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK--EAEEAKKAEELKKKEAEEKKKAEElkkaeeenkiKAEEAKKEAEED 1742
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2290035205 590 LQEIRDLQLVQGQNQTIKEHVLIDKKKAFDQLKQP-----ENLKKNKILKRVKRAKKIQ-VGDDVEVLSYG 654
Cdd:PTZ00121 1743 KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKeavieEELDEEDEKRRMEVDKKIKdIFDNFANIIEG 1813
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
479-594 |
7.14e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.07 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 479 RLMIGVPGRSNAIEISRRLGLRQDiLEVAQKGISQDSQSLNEMVAKLERERRESELKNKEAQTFLEKAEVlwqDLRTEYD 558
Cdd:pfam05262 198 RDMTDLKERESQEDAKRAQQLKEE-LDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADT---SSPKEDK 273
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2290035205 559 RYLEQKQNLIERSKRQANEKVEKAQK----EAEELLQEIR 594
Cdd:pfam05262 274 QVAENQKREIEKAQIEIKKNDEEALKakdhKAFDLKQESK 313
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
505-676 |
7.62e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 505 EVAQKGISQDSQSLNEMVAKLERERRESELKNKEAQTFLEKAEvlwQDLRT--EYDRYLEQKQNLIERSKRQANE--KVE 580
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE---EDKKKaeEAKKAEEDEKKAAEALKKEAEEakKAE 1705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 581 KAQKEAEEllqEIRDLQLVQGQNQTIKEHVLIDKKKAFDQLKQPENLKKNKILKRVKRAKKIQVGDDVEVLSYGQRGTVL 660
Cdd:PTZ00121 1706 ELKKKEAE---EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
170
....*....|....*.
gi 2290035205 661 EQVEKNEYIVQMGIIK 676
Cdd:PTZ00121 1783 EELDEEDEKRRMEVDK 1798
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
487-622 |
9.88e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 487 RSNAIEISRRLGLRQDILEVAQKGISQDSQSLNEMVAKLER-ERRESELKNKEAQtfLEKAEVLWQDLRTEYDRYLEQKQ 565
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEElKKKLKELEKRLEE--LEERHELYEEAKAKKEELERLKK 379
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2290035205 566 NLIERSKRQANEKVEKAQKEAEELLQEIRDLQLVQGQNQTIKEhvliDKKKAFDQLK 622
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIK----ELKKAIEELK 432
|
|
| PRK04946 |
PRK04946 |
endonuclease SmrB; |
710-779 |
1.02e-03 |
|
endonuclease SmrB;
Pssm-ID: 235321 [Multi-domain] Cd Length: 181 Bit Score: 40.68 E-value: 1.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2290035205 710 LDIRGLRYEEAMIKLKQyLDQALLSNHSL-VTIIHGKGTGALRQGVKDQLNNHPHVDHFEYSPPNAGGDGS 779
Cdd:PRK04946 98 LDLHGLTQLQAKQELGA-LIAACRKEHVFcACVMHGHGKHILKQQTPLWLAQHPDVMAFHQAPKEWGGDAA 167
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
523-723 |
1.92e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 523 AKLERERRESELKNKEAQTFLEKAEVLWQDLRTEYDRYLEQKQNLIERSKRQANEKVEKAQKEAEELLQ-------EIRD 595
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQlkkkeaeEKKK 1648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 596 LQLVQGQNQTIKEHVLIDKKKAFDQLKQPENLKKNKILKRVK---RAKKIQVGDDVEVLSYGQRGTV--LEQVEKNEYIV 670
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAaeaLKKEAEEAKKAEELKKKEAEEKkkAEELKKAEEEN 1728
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2290035205 671 QMGIIKMKIASDELKPIS---KVEPKQKVNVQRQAGSKVKTTLDIRglRYEEAMIK 723
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKKKAeeaKKDEEEKKKIAHLKKEEEKKAEEIR--KEKEAVIE 1782
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
505-641 |
2.96e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 505 EVAQKGISQDSQSLNEMVAKLERERRESELKNKEAQTFLEKAEVLWQDLRTEYDRYLEQKQNlIERSKRQANE--KVEKA 582
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK-ADAAKKKAEEkkKADEA 1396
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2290035205 583 QKEAEELLQEIRDLQLVQGQNQTIKEHvlidKKKAFDQLKQPENLKKNKILKRVKRAKK 641
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAKKKADEA----KKKAEEKKKADEAKKKAEEAKKADEAKK 1451
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
491-643 |
3.65e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 491 IEISRRLGLRQDIlEVAQKgiSQDSQSLnEMVAKLERERRESELKNKEAQTFLEKAEvlwqdlRTEYDRYLEQKQNLIER 570
Cdd:PTZ00121 1154 VEIARKAEDARKA-EEARK--AEDAKKA-EAARKAEEVRKAEELRKAEDARKAEAAR------KAEEERKAEEARKAEDA 1223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 571 SKRQANEKVEKAQKEAEEL--LQEIRDLQLVQGQNQTIKEHVLI--------DKKKAfDQLKQPENLKKNKILKRVKRAK 640
Cdd:PTZ00121 1224 KKAEAVKKAEEAKKDAEEAkkAEEERNNEEIRKFEEARMAHFARrqaaikaeEARKA-DELKKAEEKKKADEAKKAEEKK 1302
|
...
gi 2290035205 641 KIQ 643
Cdd:PTZ00121 1303 KAD 1305
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
511-597 |
3.85e-03 |
|
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: 39.96 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 511 ISQDSQSLNEMVAKLERERRESELKNKEAQTFLEKAEVLWQDLRTEYDRYLEQKQNLIER-----------------SKR 573
Cdd:pfam02841 192 ILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEKmeaereqllaeqermleHKL 271
|
90 100
....*....|....*....|....*.
gi 2290035205 574 QANEKV--EKAQKEAEELLQEIRDLQ 597
Cdd:pfam02841 272 QEQEELlkEGFKTEAESLQKEIQDLK 297
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
487-623 |
5.88e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.43 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 487 RSNAIEISRRLGLRQDILEVAQKGI---SQDSQSLNEMVAKLERERRESELKNKEAQTFLEKAEVLWQDLRTEYDRYLEQ 563
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVeqlEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 564 KQNLIERskrqanekVEKAQKEAEELLQEIRDLQLVQGQNQTIKEhvliDKKKAFDQLKQ 623
Cdd:TIGR02168 798 LKALREA--------LDELRAELTLLNEEAANLRERLESLERRIA----ATERRLEDLEE 845
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
329-453 |
7.77e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 38.79 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 329 ILLITGPNTGGKTIILKTI-GLIQLMGQSGLHV--PCDSGSQLGIFQSIYADIGDEQSIE-----------------QSL 388
Cdd:COG2401 58 IVLIVGASGSGKSTLLRLLaGALKGTPVAGCVDvpDNQFGREASLIDAIGRKGDFKDAVEllnavglsdavlwlrrfKEL 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2290035205 389 STFSSHMTNIVNIVEEAdyQSLVLFDELGSGTDPQEGAALAISILDYLRKVGATVLATTHYPELK 453
Cdd:COG2401 138 STGQKFRFRLALLLAER--PKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVI 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
497-643 |
8.36e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 497 LGLRQDILEVAQKGISQDSQSLNEMVAKLERERRESELKNKEAQTFLEKAEVLWQDLRTEYDRYLEQKQNLiERSKRQAN 576
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL-EQDIARLE 308
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2290035205 577 EKVEKAQKEAEELLQEIRDLQLVQGQNQTIKEHVLIDKKKAFDQLKQPENLKKNKILKRVKRAKKIQ 643
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
543-623 |
9.34e-03 |
|
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: 37.03 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2290035205 543 LEKAEvlwqDLRTEYDRYLEQKQNLIERSKRQANEKVEKAQKEAEELLQEIRDL------QLVQGQNQTIKehvlIDKKK 616
Cdd:cd06503 39 LEEAE----KAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILAEakeeaeRILEQAKAEIE----QEKEK 110
|
....*..
gi 2290035205 617 AFDQLKQ 623
Cdd:cd06503 111 ALAELRK 117
|
|
| |
