|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08074 |
PRK08074 |
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated |
2-928 |
0e+00 |
|
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
Pssm-ID: 236148 [Multi-domain] Cd Length: 928 Bit Score: 1554.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 2 NKQRFVVIDVETTGNSPKKGDKIIQIAAVVIENGQITERFSKYINPNKSIPAFIEQLTGISNQMVENEQPFEAVAEEVFQ 81
Cdd:PRK08074 1 MSKRFVVVDLETTGNSPKKGDKIIQIAAVVVEDGEILERFSSFVNPERPIPPFITELTGISEEMVKQAPLFEDVAPEIVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 82 LLDGAYFVAHNIHFDLGFVKYELHKAGFQLPDCEVLDTVELSRIVFPGFEGYKLTELSEELQLRHDQPHRADSDAEVTGL 161
Cdd:PRK08074 81 LLEGAYFVAHNVHFDLNFLNEELERAGYTEIHCPKLDTVELARILLPTAESYKLRDLSEELGLEHDQPHRADSDAEVTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 162 IFLEILEKLRQLPYPTLKQLRRLSQHFISDLTHLLDMFINENRHTEIPGYTRFSSFSVREPEAIDARINEDENFSFEIES 241
Cdd:PRK08074 161 LFLQLLNKLERLPLVTLQQLRRLSDHLKSDIAELLDENILKKMMHGKPLDEEFDEYRGIALRKREVEKNLEETCRSDFDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 242 WEAGNEKALSELMPGYEKRDGQMMMMREVADAFANREHALIEAPPGIGKTIGYLIPAALFAKKSKKPVIISTYSTLLQQQ 321
Cdd:PRK08074 241 FLEKTEEKLSLAMPKYEKREGQQEMMKEVYTALRDSEHALIEAGTGTGKSLAYLLPAAYFAKKKEEPVVISTYTIQLQQQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 322 ILTKDLPIVQDLFPFPVTAAILKGQSHYLCLYKFEQVLHEEDDNYDAVLTKAQLLVWLTETNTGDVAELNLPSGGKLLWD 401
Cdd:PRK08074 321 LLEKDIPLLQKIFPFPVEAALLKGRSHYLCLRKFEQALQEEDDNYDVALTKAQLLVWLTETETGDLDELNLPSGGKLLWN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 402 RLAYDDDSYKRSRSEHVI-GFYERAKQIAMRSDLVITNHSLLLTDEASQKKRLPESGTFIIDEAHHFERAASEHLGKRAT 480
Cdd:PRK08074 401 RIASDGESDGGKQSPWFSrCFYQRAKNRAKFADLVITNHALLLTDLTSEEPLLPSYEHIIIDEAHHFEEAASRHLGEQFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 481 YIELHTKLSRIGTLKEQGLLKKMRQLFQRNSL-PVDSFFELEEWLQHVQAESDAFFSSVHSFVKRRKPKEDLNRLVFKVN 559
Cdd:PRK08074 481 YMSFQLLLSRLGTLEEDGLLSKLAKLFKKSDQaSRSSFRDLDESLKELKFEADELFQMLRSFVLKRKKQEQNGRLIYRYN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 560 KES-QDKSWSILTDGAERLCSMLTHLQQLFEAQSSLMEKHlkgMKSKTVFLADEYqRSMKGLQHYCQTLQKLFFGSDDDE 638
Cdd:PRK08074 561 TESeKGKLWDAITELANRLCYDLRDLLTLLEAQKKELQEK---MESESAFLTGEY-AHLIDLLEKMAQLLQLLFEEDPDY 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 639 AVWIEIDAKGAKNAVAIYAQPLEPGELLADQFFARKNSVVLTSATLTVEGSFQFMIERLGLSDFFPRTMRIESPFSYDER 718
Cdd:PRK08074 637 VTWIEIDAKGAINATRLYAQPVEVAERLADEFFAKKKSVILTSATLTVNGSFDYIIERLGLEDFYPRTLQIPSPFSYEEQ 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 719 MQVMIPKEMKSIQDTGQPEFIQDTARYIELMAKEKQPKILVLFTSHDMLKKVHQELKHNMSASGIQLLAQGITGGSPGKL 798
Cdd:PRK08074 717 AKLMIPTDMPPIKDVPIEEYIEEVAAYIAKIAKATKGRMLVLFTSYEMLKKTYYNLKNEEELEGYVLLAQGVSSGSRARL 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 799 MKTFKTSNQAILLGTNHFWEGVDFPGDELTTVMIVRLPFRSPDHPLHAAKCELARKKGKNPFQTVSLPEAVLTFRQGIGR 878
Cdd:PRK08074 797 TKQFQQFDKAILLGTSSFWEGIDIPGDELSCLVIVRLPFAPPDQPVMEAKSEWAKEQGENPFQELSLPQAVLRFKQGFGR 876
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 1196905317 879 LLRSAGDKGTIMILDRRIKTAGYGRLFLDALPTTSVSEMTDSELEAYVAG 928
Cdd:PRK08074 877 LIRTETDRGTVFVLDRRLTTTSYGKYFLESLPTVPVYEGTLEELLEEVEE 926
|
|
| dinG_rel |
TIGR01407 |
DnaQ family exonuclease/DinG family helicase, putative; This model represents a family of ... |
5-918 |
0e+00 |
|
DnaQ family exonuclease/DinG family helicase, putative; This model represents a family of proteins in Gram-positive bacteria. The N-terminal region of about 200 amino acids resembles the epsilon subunit of E. coli DNA polymerase III and the homologous region of the Gram-positive type DNA polymerase III alpha subunit. The epsilon subunit contains an exonuclease domain. The remainder of this protein family resembles a predicted ATP-dependent helicase, the DNA damage-inducible protein DinG of E. coli. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273602 [Multi-domain] Cd Length: 850 Bit Score: 673.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 5 RFVVIDVETTGNSPKKgDKIIQIAAVVIENGQITERFSKYINPNKSIPAFIEQLTGISNQMVENEQPFEAVAEEVFQLLD 84
Cdd:TIGR01407 1 RYAVVDLETTGTQLSF-DKIIQIGIVVVEDGEIVDTFHTDVNPNEPIPPFIQELTGISDNMLQQAPYFSQVAQEIYDLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 85 GAYFVAHNIHFDLGFVKYELHKAGFQLPDCEVLDTVELSRIVFPGFEGYKLTELSEELQLRHDQPHRADSDAEVTGLIFL 164
Cdd:TIGR01407 80 DGIFVAHNVHFDLNFLAKALKDCGYEPLPKPRIDTVELAQIFFPTEESYQLSELSEALGLTHENPHRADSDAQATAELLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 165 EILEKLRQLPYPTLKQLRRLSQHFISDLTHLLDMFINENRHTEIP-GYTRFSSFSVREPEAIdarINEDENfsfeIESWE 243
Cdd:TIGR01407 160 LLFEKMEKLPLDTLEQLLELSDQLLYESYDIIQETYRQYKIKPAPkSYEVVEQIAYRKQVAS---KKPETN----YNTLS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 244 AGNEKALSELmpGYEKRDGQMMMMREVADAFANREHALIEAPPGIGKTIGYLIPAALFAkKSKKPVIISTYSTLLQQQIL 323
Cdd:TIGR01407 233 SLFSKNIDRL--GLEYRPEQLKLAELVLDQLTHSEKSLIEAPTGTGKTLGYLLPALYYA-ITEKPVVISTNTKVLQSQLL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 324 TKDLPIVQDLFPFPVTAAILKGQSHYLCLYKFEQVLHEEDDNYDAVLTKAQLLVWLTETNTGDVAELNLPSGGKLLWDRL 403
Cdd:TIGR01407 310 EKDIPLLNEILNFKINAALIKGKSNYLSLGKFSQILKDNTDNYEFNIFKMQVLVWLTETETGDLDELNLKGGNKMFFAQV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 404 AYDDDSYKRSRsEHVIGFYERAKQIAMRSDLVITNHSLLLTDEASQKKRLPESGTFIIDEAHHFERAASEHLGKRATYIE 483
Cdd:TIGR01407 390 RHDGNLSKKDL-FYEVDFYNRAQKNAEQAQILITNHAYLITRLVDNPELFPSFRDLIIDEAHHLPDIAENQLQEELDYAD 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 484 LHTKLSRIGTLKEQGLLKKMRQLFQRNSLPVDSFFELEEWLQHVQAESDAffssvhsfvkrrkpkedlnrlvfkvnkesq 563
Cdd:TIGR01407 469 IKYQIDLIGKGENEQLLKRIQQLEKQEILEKLFDFETKDILKDLQAILDK------------------------------ 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 564 dkswsiltdgaerlcsmlthLQQLFEAQSSLMEKHLKGMKSKTVFLADEYQRsmkglqhycqtlqkLFFGSDDDEAVWIE 643
Cdd:TIGR01407 519 --------------------LNKLLQIFSELSHKTVDQLRKFDLALKDDFKN--------------IEQSLKEGHTSWIS 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 644 IDAKGAKNAVAIYAQPLEPGELLADQFFARKNSVVLTSATLTVEGSFQFMIERLGLSDFFPRTMRiESPFSYDERMQVMI 723
Cdd:TIGR01407 565 IENLQQKSTIRLYIKDYEVGDVLTKRLLPKFKSLIFTSATLKFSHSFESFPQLLGLTDVHFNTIE-PTPLNYAENQRVLI 643
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 724 PKEMKSIQDTGQPEFIQDTARYIELMAKEKQPKILVLFTSHDMLKKVHQELKHNMSASGIQLLAQGITgGSPGKLMKTFK 803
Cdd:TIGR01407 644 PTDAPAIQNKSLEEYAQEIASYIIEITAITSPKILVLFTSYEMLHMVYDMLNELPEFEGYEVLAQGIN-GSRAKIKKRFN 722
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 804 TSNQAILLGTNHFWEGVDFPGDELTTVMIVRLPFRSPDHPLHAAKCELARKKGKNPFQTVSLPEAVLTFRQGIGRLLRSA 883
Cdd:TIGR01407 723 NGEKAILLGTSSFWEGVDFPGNGLVCLVIPRLPFANPKHPLTKKYWQKLEQEGKNPFYDYVLPMAIIRLRQALGRLIRRE 802
|
890 900 910
....*....|....*....|....*....|....*
gi 1196905317 884 GDKGTIMILDRRIKTAGYGRLFLDALPTTSVSEMT 918
Cdd:TIGR01407 803 NDRGSIVILDRRLVGKRYGKRFEKSLPEYLQVKGD 837
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
245-910 |
0e+00 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 594.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 245 GNEKALSELMPGYEKRDGQMMMMREVADAFANREHALIEAPPGIGKTIGYLIPAALFAKKSKKPVIISTYSTLLQQQILT 324
Cdd:COG1199 1 ADDGLLALAFPGFEPRPGQREMAEAVARALAEGRHLLIEAGTGTGKTLAYLVPALLAARETGKKVVISTATKALQEQLVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 325 KDLPIVQDLFPFPVTAAILKGQSHYLCLYKFEQVLHEEDDNYDAVLTKAQLLVWLTETNTGDVAELNLPSGGKlLWDRLA 404
Cdd:COG1199 81 KDLPLLRKALGLPLRVALLKGRSNYLCLRRLEQALQEGDDLDDEELLLARILAWASETWTGDRDELPLPEDDE-LWRQVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 405 YDDDSYKRSRSEHV-IGFYERAKQIAMRSDLVITNHSLLLTDEASQKKRLPESGTFIIDEAHHFERAASEHLGKRATYIE 483
Cdd:COG1199 160 SDADNCLGRRCPYYgVCPYELARRLAREADVVVVNHHLLFADLALGEELLPEDDVLIIDEAHNLPDRARDMFSAELSSRS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 484 LHTKLSRIGTLKEQGLLKKMRQLFQRnslpvdsffeleewlqhVQAESDAFFSSVHSFVKRRKPkedlnrlvfkvnkesq 563
Cdd:COG1199 240 LLRLLRELRKLGLRPGLKKLLDLLER-----------------LREALDDLFLALEEEEELRLA---------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 564 dksWSILTDGAERLCSMLTHLQQLFEAQSSLMEKHLKGmksktvflADEYQRSMKGLQHYCQTLQKLFFGSDDDEAV-WI 642
Cdd:COG1199 287 ---LGELPDEPEELLEALDALRDALEALAEALEEELER--------LAELDALLERLEELLFALARFLRIAEDEGYVrWL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 643 EIDAKGaknaVAIYAQPLEPGELLADQFFARKNSVVLTSATLTVEGSFQFMIERLGLSDfFPRTMRIESPFSYDERMQVM 722
Cdd:COG1199 356 EREGGD----VRLHAAPLDPADLLRELLFSRARSVVLTSATLSVGGPFDYFARRLGLDE-DARTLSLPSPFDYENQALLY 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 723 IPKEMKSIQDtgQPEFIQDTARYIELMAKEKQPKILVLFTSHDMLKKVHQELKhnmSASGIQLLAQGitGGSPGKLMKTF 802
Cdd:COG1199 431 VPRDLPRPSD--RDGYLEAIAEAIAELLEASGGNTLVLFTSYRALEQVAELLR---ERLDIPVLVQG--DGSREALLERF 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 803 KTSNQAILLGTNHFWEGVDFPGDELTTVMIVRLPFRSPDHPLHAAKCELARKKGKNPFQTVSLPEAVLTFRQGIGRLLRS 882
Cdd:COG1199 504 REGGNSVLVGTGSFWEGVDLPGDALSLVIIVKLPFPPPDDPVLEARREALEARGGNGFMYAYLPPAVIKLKQGAGRLIRS 583
|
650 660
....*....|....*....|....*...
gi 1196905317 883 AGDKGTIMILDRRIKTAGYGRLFLDALP 910
Cdd:COG1199 584 EEDRGVVVLLDRRLLTKRYGKRFLDSLP 611
|
|
| PRK07246 |
PRK07246 |
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated |
4-909 |
5.97e-110 |
|
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
Pssm-ID: 180905 [Multi-domain] Cd Length: 820 Bit Score: 358.23 E-value: 5.97e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 4 QRFVVIDVETTGNSPKKgdKIIQIAAVVIENGQITERFSKYINPNKSIPAFIEQLTGISNQMVENEQPFEAVAEEVFQLL 83
Cdd:PRK07246 7 RKYAVVDLEATGAGPNA--SIIQVGIVIIEGGEIIDSYTTDVNPHEPLDEHIKHLTGITDQQLAQAPDFSQVARHIYDLI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 84 DGAYFVAHNIHFDLGFVKYELHKAGFQLPDCEVlDTVELSRIVFPGFEGYKLTELSEELQLRHDQPHRADSDAEVTGLIF 163
Cdd:PRK07246 85 EDCIFVAHNVKFDANLLAEALFLEGYELRTPRV-DTVELAQVFFPTLEKYSLSHLSRELNIDLADAHTAIADARATAELF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 164 LEILEKLRQLPYPTLKQLRRLSQHFISDLTHLLDMFINENRHTEIPGYTRFSSFSVREPEAIDARINEDENFSFEIeswe 243
Cdd:PRK07246 164 LKLLQKIESLPKECLERLLEYADSLLFESYLVIEEALANAKPYSSPDYIKVQGIVLKKTAASLKPRKLSQDFSINI---- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 244 agnekALSELmpgyEKRDGQMMMMREVADAFANREHALIEAPPGIGKTIGYLIPaaLFAKKSKKPVIISTYSTLLQQQIL 323
Cdd:PRK07246 240 -----ALLGL----EERPKQESFAKLVGEDFHDGPASFIEAQTGIGKTYGYLLP--LLAQSDQRQIIVSVPTKILQDQIM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 324 TKDLPIVQDLFPFPVTAaiLKGQSHYLCLYKFEQVLHEEDDNYDAVLTKAQLLVWLTETNTGDVAEL-----------NL 392
Cdd:PRK07246 309 AEEVKAIQEVFHIDCHS--LKGPQNYLKLDAFYDSLQQNDDNRLVNRYKMQLLVWLTETETGDLDEIkqkqryaayfdQL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 393 PSGGKLLWDRLAYDDDSYKRSrsehvigfYERAKQiamrSDLVITNHSLLLT----DEASQKKRLpesgtFIIDEAH--- 465
Cdd:PRK07246 387 KHDGNLSQSSLFYDYDFWKRS--------YEKAKT----ARLLITNHAYFLTrvqdDKDFARNKV-----LVFDEAQklm 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 466 -HFERAASEHLGKRATYIELHTKLSRIGTLKEQGLLKKMRqlfqrnslpvdsfFELEEWLQHVQaesdaffssvhSFVKR 544
Cdd:PRK07246 450 lQLEQLSRHQLNITSFLQTIQKALSGPLPLLQKRLLESIS-------------FELLQLSEQFY-----------QGKER 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 545 RKPKEDLNRLvfkvnkesqdkswsiltdgaerlcsmlthLQQLFEAQSSLMekhlkgmksktvfladeyqrsmkglqhyc 624
Cdd:PRK07246 506 QLIHDSLSRL-----------------------------HQYFSELEVAGF----------------------------- 527
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 625 QTLQKLFFGSDDDeaVWIEIDAKGAKNAVAIYAQPLEpgELLADQFFARKNSVVLTSATLTVeGSFQFMIERLGLSDFfp 704
Cdd:PRK07246 528 QELQAFFATAEGD--YWLESEKQSEKRVTYLNSASKA--FTHFSQLLPETCKTYFVSATLQI-SPRVSLADLLGFEEY-- 600
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 705 RTMRIESPFSYDErmQVMIPKEMKSIQDTGQPEFIQDTARYIELMAKEKQPkILVLFTSHDMLKKVHQELKHNMsasgIQ 784
Cdd:PRK07246 601 LFHKIEKDKKQDQ--LVVVDQDMPLVTETSDEVYAEEIAKRLEELKQLQQP-ILVLFNSKKHLLAVSDLLDQWQ----VS 673
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 785 LLAQGiTGGSPGKLMKTFKTSNQAILLGTNHFWEGVDF-PGDELTTVmIVRLPFRSPDHPLHAAKCELARKKGKNPFQTV 863
Cdd:PRK07246 674 HLAQE-KNGTAYNIKKRFDRGEQQILLGLGSFWEGVDFvQADRMIEV-ITRLPFDNPEDPFVKKMNQYLLQEGKNPFYDY 751
|
890 900 910 920
....*....|....*....|....*....|....*....|....*.
gi 1196905317 864 SLPEAVLTFRQGIGRLLRSAGDKGTIMILDRRIKTAGYGRLFLDAL 909
Cdd:PRK07246 752 FLPMTILRLKQAIGRTMRREDQKSAVLILDRRILTKSYGKQILASL 797
|
|
| dinG |
PRK11747 |
ATP-dependent DNA helicase DinG; Provisional |
248-910 |
2.21e-92 |
|
ATP-dependent DNA helicase DinG; Provisional
Pssm-ID: 236966 [Multi-domain] Cd Length: 697 Bit Score: 307.52 E-value: 2.21e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 248 KALSELMPGYEKRDGQMMMMREVADAFA-----NREHALIEAPPGIGKTIGYLIPAALFAKKSKKPVIISTYSTLLQQQI 322
Cdd:PRK11747 15 KALQEQLPGFIPRAGQRQMIAEVAKTLAgeylkDGRILVIEAGTGVGKTLSYLLAGIPIARAEKKKLVISTATVALQEQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 323 LTKDLPIVQDLFPFPVTAAILKGQSHYLCLYKFEQVLHEEDDN------YDAVLTKAQ-----LLVWLTETNTG------ 385
Cdd:PRK11747 95 VSKDLPLLLKISGLDFKFTLAKGRGRYVCPRKLAALASDEGTQqdlllfLDDELTPPDeeeqkLLARLAKALATgkwdgd 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 386 -DVAELNLPSGgklLWDRLAYDddsyKRS---RSEHVIG---FYERAKQIaMRSDLVITNHSLLLTDEASQKKRL---PE 455
Cdd:PRK11747 175 rDHWPEPIDDS---LWQRITTD----KHSclgRNCPYFRecpFFKARREI-DEADVVVANHDLVLADLELGGGVVlpdPE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 456 SGTFIIDEAHHFERAASEHLGKRATYielhtkLSRIGTLKEQG-LLKKMRQLFQRNSLPVDSFF-----ELEEWLQHVQA 529
Cdd:PRK11747 247 NLLYVLDEGHHLPDVARDHFAASAEL------KGTADWLEKLLkLLTKLVALIMEPPLALPERLnahceELRELLASLNQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 530 ESDAFF-----SSVHSFVKRRKPKEdlnrlvfkvnkesqdkswsiLTDGAERLCSMLTHLQQLFEAQSSLMEKHLKGMKS 604
Cdd:PRK11747 321 ILNLFLpaggeEARYRFEMGELPEE--------------------LLELAERLAKLTEKLLGLLEKLLNDLSEAMKTGKI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 605 KTVfLADEYQRSMKGLQHYCQTLQKLF--FGSDDDE-----AVWIEIDAKGAKNAVAIYAQPLEPGELLADQFFARKNSV 677
Cdd:PRK11747 381 DIV-RLERLLLELGRALGRLEALSKLWrlAAKEDQEsgapmARWITREERDGQGDYLFHASPIRVGDQLERLLWSRAPGA 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 678 VLTSATLTVEGSFQFMIERLGLSDFFP-RTMRIESPFSYDERMQVMIPKeMKSIQDTgQPEFIQDTARYI-ELMAKEKqp 755
Cdd:PRK11747 460 VLTSATLRSLNSFDRFQEQSGLPEKDGdRFLALPSPFDYPNQGKLVIPK-MRAEPDN-EEAHTAEMAEFLpELLEKHK-- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 756 KILVLFTSHDMLKKVHQELKHNMsasGIQLLAQGItgGSPGKLMKTFK-------TSnqaILLGTNHFWEGVDFPGDELT 828
Cdd:PRK11747 536 GSLVLFASRRQMQKVADLLPRDL---RLMLLVQGD--QPRQRLLEKHKkrvdegeGS---VLFGLQSFAEGLDLPGDYLT 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 829 TVMIVRLPFRSPDHPLHAAKCELARKKGKNPFQTVSLPEAVLTFRQGIGRLLRSAGDKGTIMILDRRIKTAGYGRLFLDA 908
Cdd:PRK11747 608 QVIITKIPFAVPDSPVEATLAEWLKSRGGNPFMEISVPDASFKLIQAVGRLIRSEQDRGRVTILDRRLLTKRYGKRLLDA 687
|
..
gi 1196905317 909 LP 910
Cdd:PRK11747 688 LP 689
|
|
| PolC |
COG2176 |
DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair]; ... |
4-179 |
1.33e-73 |
|
DNA polymerase III, alpha subunit (gram-positive type) [Replication, recombination and repair];
Pssm-ID: 441779 [Multi-domain] Cd Length: 181 Bit Score: 239.66 E-value: 1.33e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 4 QRFVVIDVETTGNSPKKgDKIIQIAAVVIENGQITERFSKYINPNKSIPAFIEQLTGISNQMVENEQPFEAVAEEVFQLL 83
Cdd:COG2176 8 LTYVVFDLETTGLSPKK-DEIIEIGAVKVENGEIVDRFSTLVNPGRPIPPFITELTGITDEMVADAPPFEEVLPEFLEFL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 84 DGAYFVAHNIHFDLGFVKYELHKAGFQLpDCEVLDTVELSRIVFPGFEGYKLTELSEELQLRHDQPHRADSDAEVTGLIF 163
Cdd:COG2176 87 GDAVLVAHNASFDLGFLNAALKRLGLPF-DNPVLDTLELARRLLPELKSYKLDTLAERLGIPLEDRHRALGDAEATAELF 165
|
170
....*....|....*.
gi 1196905317 164 LEILEKLRQLPYPTLK 179
Cdd:COG2176 166 LKLLEKLEEKGITTLR 181
|
|
| DnaQ |
COG0847 |
DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination ... |
5-168 |
3.97e-62 |
|
DNA polymerase III, epsilon subunit or related 3'-5' exonuclease [Replication, recombination and repair];
Pssm-ID: 440608 [Multi-domain] Cd Length: 163 Bit Score: 207.34 E-value: 3.97e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 5 RFVVIDVETTGNSPKKgDKIIQIAAVVIENGQITERFSKYINPNKSIPAFIEQLTGISNQMVENEQPFEAVAEEVFQLLD 84
Cdd:COG0847 1 RFVVLDTETTGLDPAK-DRIIEIGAVKVDDGRIVETFHTLVNPERPIPPEATAIHGITDEDVADAPPFAEVLPELLEFLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 85 GAYFVAHNIHFDLGFVKYELHKAGFQLPDCEVLDTVELSRIVFPGFEGYKLTELSEELQLRHDQPHRADSDAEVTGLIFL 164
Cdd:COG0847 80 GAVLVAHNAAFDLGFLNAELRRAGLPLPPFPVLDTLRLARRLLPGLPSYSLDALCERLGIPFDERHRALADAEATAELFL 159
|
....
gi 1196905317 165 EILE 168
Cdd:COG0847 160 ALLR 163
|
|
| Helicase_C_2 |
pfam13307 |
Helicase C-terminal domain; This domain is found at the C-terminus of DEAD-box helicases. |
747-910 |
6.35e-56 |
|
Helicase C-terminal domain; This domain is found at the C-terminus of DEAD-box helicases.
Pssm-ID: 463840 [Multi-domain] Cd Length: 168 Bit Score: 190.47 E-value: 6.35e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 747 ELMAKEKQPKILVLFTSHDMLKKVHQELKHNMSASGIQLLAQGiTGGSPGKLMKTFK-TSNQAILLGTN--HFWEGVDFP 823
Cdd:pfam13307 1 LRLLKVIPGGVLVFFPSYSYLEKVAERLKESGLEKGIEIFVQP-GEGSREKLLEEFKkKGKGAVLFGVCggSFSEGIDFP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 824 GDELTTVMIVRLPFRSPDHPLHAAKCELARKKGKNPFQTVSLPEAVLTFRQGIGRLLRSAGDKGTIMILDRRIKTAGYGR 903
Cdd:pfam13307 80 GDLLRAVIIVGLPFPNPDDPVVEAKREYLDSKGGNPFNEWYLPQAVRAVNQAIGRLIRHENDYGAIVLLDSRFLTKRYGK 159
|
....*..
gi 1196905317 904 LFLDALP 910
Cdd:pfam13307 160 LLPKWLP 166
|
|
| DEDDh |
cd06127 |
DEDDh 3'-5' exonuclease domain family; DEDDh exonucleases, part of the DnaQ-like (or DEDD) ... |
7-164 |
2.40e-54 |
|
DEDDh 3'-5' exonuclease domain family; DEDDh exonucleases, part of the DnaQ-like (or DEDD) exonuclease superfamily, catalyze the excision of nucleoside monophosphates at the DNA or RNA termini in the 3'-5' direction. These proteins contain four invariant acidic residues in three conserved sequence motifs termed ExoI, ExoII and ExoIII. DEDDh exonucleases are classified as such because of the presence of specific Hx(4)D conserved pattern at the ExoIII motif. The four conserved acidic residues are clustered around the active site and serve as ligands for the two metal ions required for catalysis. Most DEDDh exonucleases are the proofreading subunits (epsilon) or domains of bacterial DNA polymerase III, the main replicating enzyme in bacteria, which functions as the chromosomal replicase. Other members include other DNA and RNA exonucleases such as RNase T, Oligoribonuclease, and RNA exonuclease (REX), among others.
Pssm-ID: 176648 [Multi-domain] Cd Length: 159 Bit Score: 185.58 E-value: 2.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 7 VVIDVETTGNSPKKgDKIIQIAAVVIENG-QITERFSKYINPNKSIPAFIEQLTGISNQMVENEQPFEAVAEEVFQLLDG 85
Cdd:cd06127 1 VVFDTETTGLDPKK-DRIIEIGAVKVDGGiEIVERFETLVNPGRPIPPEATAIHGITDEMLADAPPFEEVLPEFLEFLGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 86 AYFVAHNIHFDLGFVKYELHKAGFQLPDCEVLDTVELSRIVFPGFEGYKLTEL-SEELQLRHDQPHRADSDAEVTGLIFL 164
Cdd:cd06127 80 RVLVAHNASFDLRFLNRELRRLGGPPLPNPWIDTLRLARRLLPGLRSHRLGLLlAERYGIPLEGAHRALADALATAELLL 159
|
|
| polC |
PRK00448 |
DNA polymerase III PolC; Validated |
4-181 |
1.08e-49 |
|
DNA polymerase III PolC; Validated
Pssm-ID: 234767 [Multi-domain] Cd Length: 1437 Bit Score: 191.59 E-value: 1.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 4 QRFVVIDVETTGNSPKKgDKIIQIAAVVIENGQITERFSKYINPNKSIPAFIEQLTGISNQMVENEQPFEAVAEEVFQLL 83
Cdd:PRK00448 419 ATYVVFDVETTGLSAVY-DEIIEIGAVKIKNGEIIDKFEFFIKPGHPLSAFTTELTGITDDMVKDAPSIEEVLPKFKEFC 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 84 DGAYFVAHNIHFDLGFVKYELHKAGFQLPDCEVLDTVELSRIVFPGFEGYKLTELSEELQLRHDQPHRADSDAEVTGLIF 163
Cdd:PRK00448 498 GDSILVAHNASFDVGFINTNYEKLGLEKIKNPVIDTLELSRFLYPELKSHRLNTLAKKFGVELEHHHRADYDAEATAYLL 577
|
170
....*....|....*...
gi 1196905317 164 LEILEKLRQLPYPTLKQL 181
Cdd:PRK00448 578 IKFLKDLKEKGITNLDEL 595
|
|
| EXOIII |
smart00479 |
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ... |
5-171 |
1.46e-48 |
|
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other exonucleases;
Pssm-ID: 214685 [Multi-domain] Cd Length: 169 Bit Score: 169.79 E-value: 1.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 5 RFVVIDVETTGNSPKKgDKIIQIAAVVIENGQITERFSKYINPNKSIPAFIEQLTGISNQMVENEQPFEAVAEEVFQLLD 84
Cdd:smart00479 1 TLVVIDCETTGLDPGK-DEIIEIAAVDVDGGEIIEVFDTYVKPDRPITDYATEIHGITPEMLDDAPTFEEVLEELLEFLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 85 GAYFVAHN-IHFDLGFVKYELHKAG-FQLPDCEVLDTVELSRIVFPGFEGYKLTELSEELQLRHDQ-PHRADSDAEVTGL 161
Cdd:smart00479 80 GRILVAGNsAHFDLRFLKLEHPRLGiKQPPKLPVIDTLKLARATNPGLPKYSLKKLAKRLLLEVIQrAHRALDDARATAK 159
|
170
....*....|
gi 1196905317 162 IFLEILEKLR 171
Cdd:smart00479 160 LFKKLLERLE 169
|
|
| RNase_T |
pfam00929 |
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ... |
7-163 |
9.73e-40 |
|
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T and the epsilon subunit of DNA polymerase III.;
Pssm-ID: 395743 [Multi-domain] Cd Length: 164 Bit Score: 144.42 E-value: 9.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 7 VVIDVETTGNSPKKgDKIIQIAAVVIENGQ--ITERFSKYINPNKS--IPAFIEQLTGISNQMVENEQPFEAVAEEVFQL 82
Cdd:pfam00929 1 VVIDLETTGLDPEK-DEIIEIAAVVIDGGEneIGETFHTYVKPTRLpkLTDECTKFTGITQAMLDNKPSFEEVLEEFLEF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 83 LD-GAYFVAHNIHFDLGFVKYELHKAGFQL--PDCEVLDTVELSRIVFPGFEGYKLTELSEELQLRHDQ-PHRADSDAEV 158
Cdd:pfam00929 80 LRkGNLLVAHNASFDVGFLRYDDKRFLKKPmpKLNPVIDTLILDKATYKELPGRSLDALAEKLGLEHIGrAHRALDDARA 159
|
....*
gi 1196905317 159 TGLIF 163
Cdd:pfam00929 160 TAKLF 164
|
|
| HELICc2 |
smart00491 |
helicase superfamily c-terminal domain; |
764-898 |
1.54e-39 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 214694 [Multi-domain] Cd Length: 142 Bit Score: 143.19 E-value: 1.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 764 HDMLKKVHQELKHNMSA-SGIQLLAQGITGGSPGKLMKTFKTSNQ---AILLGTNH--FWEGVDFPGDELTTVMIVRLPF 837
Cdd:smart00491 1 YRYLEQVVEYWKENGILeINKPVFIEGKDSGETEELLEKYSAACEargALLLAVARgkVSEGIDFPDDLGRAVIIVGIPF 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1196905317 838 RSPDHPLHAAKCE-LARKKGKNPFQTVSLPEAVLTFRQGIGRLLRSAGDKGTIMILDRRIKT 898
Cdd:smart00491 81 PNPDSPILRARLEyLDEKGGIRPFDEVYLFDAMRALAQAIGRAIRHKNDYGVVVLLDKRYAR 142
|
|
| PRK07883 |
PRK07883 |
DEDD exonuclease domain-containing protein; |
6-185 |
1.90e-37 |
|
DEDD exonuclease domain-containing protein;
Pssm-ID: 236123 [Multi-domain] Cd Length: 557 Bit Score: 148.53 E-value: 1.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 6 FVVIDVETTGNSPKkGDKIIQIAAVVIENGQITERFSKYINPNKSIPAFIEQLTGISNQMVENEQPFEAVAEEVFQLLDG 85
Cdd:PRK07883 17 FVVVDLETTGGSPA-GDAITEIGAVKVRGGEVLGEFATLVNPGRPIPPFITVLTGITTAMVAGAPPIEEVLPAFLEFARG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 86 AYFVAHNIHFDLGFVKYELHKAGFQLPDCEVLDTVELSRIVFPGFE--GYKLTELSEELQLRHDQPHRADSDAEVTGLIF 163
Cdd:PRK07883 96 AVLVAHNAPFDIGFLRAAAARCGYPWPGPPVLCTVRLARRVLPRDEapNVRLSTLARLFGATTTPTHRALDDARATVDVL 175
|
170 180
....*....|....*....|..
gi 1196905317 164 LEILEKLRQLPYPTLKQLRRLS 185
Cdd:PRK07883 176 HGLIERLGNLGVHTLEELLTYL 197
|
|
| DNA_pol_III_epsilon_like |
cd06130 |
an uncharacterized bacterial subgroup of the DEDDh 3'-5' exonuclease domain family with ... |
6-165 |
4.25e-35 |
|
an uncharacterized bacterial subgroup of the DEDDh 3'-5' exonuclease domain family with similarity to the epsilon subunit of DNA polymerase III; This subfamily is composed of uncharacterized bacterial proteins with similarity to the epsilon subunit of DNA polymerase III (Pol III), a multisubunit polymerase which is the main DNA replicating enzyme in bacteria, functioning as the chromosomal replicase. The Pol III holoenzyme is a complex of ten different subunits, three of which (alpha, epsilon, and theta) compose the catalytic core. The Pol III epsilon subunit, encoded by the dnaQ gene, is a DEDDh-type 3'-5' exonuclease which is responsible for the proofreading activity of the polymerase, increasing the fidelity of DNA synthesis. It contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. The epsilon subunit of Pol III also functions as a stabilizer of the holoenzyme complex.
Pssm-ID: 99834 [Multi-domain] Cd Length: 156 Bit Score: 130.71 E-value: 4.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 6 FVVIDVETTgNSpkKGDKIIQIAAVVIENGQITERFSKYINPNKSI-PAFIeQLTGISNQMVENEQPFEAVAEEVFQLLD 84
Cdd:cd06130 1 FVAIDFETA-NA--DRASACSIGLVKVRDGQIVDTFYTLIRPPTRFdPFNI-AIHGITPEDVADAPTFPEVWPEIKPFLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 85 GAYFVAHNIHFDLGFVKYELHKAGFQLPDCEVLDTVELSRIVFPGFEGYKLTELSEEL--QLRHdqpHRADSDAEVTGLI 162
Cdd:cd06130 77 GSLVVAHNASFDRSVLRAALEAYGLPPPPYQYLCTVRLARRVWPLLPNHKLNTVAEHLgiELNH---HDALEDARACAEI 153
|
...
gi 1196905317 163 FLE 165
Cdd:cd06130 154 LLA 156
|
|
| DNA_pol_III_epsilon_Ecoli_like |
cd06131 |
DEDDh 3'-5' exonuclease domain of the epsilon subunit of Escherichia coli DNA polymerase III ... |
7-129 |
1.32e-31 |
|
DEDDh 3'-5' exonuclease domain of the epsilon subunit of Escherichia coli DNA polymerase III and similar proteins; This subfamily is composed of the epsilon subunit of Escherichia coli DNA polymerase III (Pol III) and similar proteins. Pol III is the main DNA replicating enzyme in bacteria, functioning as the chromosomal replicase. It is a holoenzyme complex of ten different subunits, three of which (alpha, epsilon, and theta) compose the catalytic core. The Pol III epsilon subunit, encoded by the dnaQ gene, is a DEDDh-type 3'-5' exonuclease which is responsible for the proofreading activity of the polymerase, increasing the fidelity of DNA synthesis. It contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. The epsilon subunit of Pol III also functions as a stabilizer of the holoenzyme complex.
Pssm-ID: 99835 [Multi-domain] Cd Length: 167 Bit Score: 121.10 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 7 VVIDVETTGNSPKKGDKIIQIAAVVIENGQITER-FSKYINPNKSIPAFIEQLTGISNQMVENEQPFEAVAEEVFQLLDG 85
Cdd:cd06131 2 IVLDTETTGLDPREGHRIIEIGCVELINRRLTGNtFHVYINPERDIPEEAFKVHGITDEFLADKPKFAEIADEFLDFIRG 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1196905317 86 AYFVAHNIHFDLGFVKYELHKAGFQ---LPDCEVLDTVELSRIVFPG 129
Cdd:cd06131 82 AELVIHNASFDVGFLNAELSLLGLGkkiIDFCRVIDTLALARKKFPG 128
|
|
| PRK06807 |
PRK06807 |
3'-5' exonuclease; |
6-165 |
2.32e-29 |
|
3'-5' exonuclease;
Pssm-ID: 235864 [Multi-domain] Cd Length: 313 Bit Score: 119.53 E-value: 2.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 6 FVVIDVETTGNSPKKgDKIIQIAAVVIENGQITERFSKYINPNKSIPAFIEQLTGISNQMVENEQPFEAVAEEVFQLLDG 85
Cdd:PRK06807 10 YVVIDFETTGFNPYN-DKIIQVAAVKYRNHELVDQFVSYVNPERPIPDRITSLTGITNYRVSDAPTIEEVLPLFLAFLHT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 86 AYFVAHNIHFDLGFVKYELHKAGFQLPDCEVLDTVELSRIVFPGFEGYKLTELSEELQLRHDQpHRADSDAEVTGLIFLE 165
Cdd:PRK06807 89 NVIVAHNASFDMRFLKSNVNMLGLPEPKNKVIDTVFLAKKYMKHAPNHKLETLKRMLGIRLSS-HNAFDDCITCAAVYQK 167
|
|
| PRK08517 |
PRK08517 |
3'-5' exonuclease; |
1-170 |
1.63e-28 |
|
3'-5' exonuclease;
Pssm-ID: 236281 [Multi-domain] Cd Length: 257 Bit Score: 115.50 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 1 MNKQRFVVIDVETTGNSPKKGdKIIQIAAVVIENGQITERFSKYINPnKSIPAFIEQLTGISNQMVENEQPFEAVAEEVF 80
Cdd:PRK08517 65 IKDQVFCFVDIETNGSKPKKH-QIIEIGAVKVKNGEIIDRFESFVKA-KEVPEYITELTGITYEDLENAPSLKEVLEEFR 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 81 QLLDGAYFVAHNIHFDLGFVKYELHKAGFQLPDCEVLDTVELSRIVFPGfEGYKLTELSEELQLRHDQPHRADSDAEVTG 160
Cdd:PRK08517 143 LFLGDSVFVAHNVNFDYNFISRSLEEIGLGPLLNRKLCTIDLAKRTIES-PRYGLSFLKELLGIEIEVHHRAYADALAAY 221
|
170
....*....|
gi 1196905317 161 LIFLEILEKL 170
Cdd:PRK08517 222 EIFKICLLNL 231
|
|
| PRK07740 |
PRK07740 |
hypothetical protein; Provisional |
6-187 |
8.20e-28 |
|
hypothetical protein; Provisional
Pssm-ID: 236085 [Multi-domain] Cd Length: 244 Bit Score: 112.84 E-value: 8.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 6 FVVIDVETTGNSPKKGDKIIQIAAVVIENGQITER-FSKYINPNKSIPAFIEQLTGISNQMVENEQPFEAVAEEVFQLLD 84
Cdd:PRK07740 61 FVVFDLETTGFSPQQGDEILSIGAVKTKGGEVETDtFYSLVKPKRPIPEHILELTGITAEDVAFAPPLAEVLHRFYAFIG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 85 GAYFVAHNIHFDLGFVKYELHKAGFQLPDCEVLDTVELSRIVFPGFEGYKLTELSEELQLRHDQPHRADSDAEVTGLIFL 164
Cdd:PRK07740 141 AGVLVAHHAGHDKAFLRHALWRTYRQPFTHRLIDTMFLTKLLAHERDFPTLDDALAYYGIPIPRRHHALGDALMTAKLWA 220
|
170 180
....*....|....*....|....
gi 1196905317 165 EILEKLRQLPYPTLKQL-RRLSQH 187
Cdd:PRK07740 221 ILLVEAQQRGITTLHDLyAALSRC 244
|
|
| dnaq |
TIGR00573 |
exonuclease, DNA polymerase III, epsilon subunit family; All proteins in this family for which ... |
6-199 |
2.02e-27 |
|
exonuclease, DNA polymerase III, epsilon subunit family; All proteins in this family for which functions are known are components of the DNA polymerase III complex (epsilon subunit). There is, however, an outgroup that includes paralogs in some gamma-proteobacteria and the n-terminal region of DinG from some low GC gram positive bacteria. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, Degradation of DNA]
Pssm-ID: 129663 [Multi-domain] Cd Length: 217 Bit Score: 111.00 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 6 FVVIDVETTGnsPKKGDKIIQIAAVVIENGQIT-ERFSKYINPNKSIPAFIEQLTGISNQMVENEQPFEAVAEEVFQLLD 84
Cdd:TIGR00573 9 ETTGDNETTG--LYAGHDIIEIGAVEIINRRITgNKFHTYIKPDRPIDPDAIKIHGITDDMLKDKPDFKEIAEDFADYIR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 85 GAYFVAHNIHFDLGFVKYELHKAGFQLPDC-EVLDTVELSRIVFPGFEGYKLTELSEELQLRHDQPHR----ADSDAEVT 159
Cdd:TIGR00573 87 GAELVIHNASFDVGFLNYEFSKLYKVEPKTnDVIDTTDTLQYARPEFPGKRNTLDALCKRYEITNSHRalhgALADAFIL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1196905317 160 GLIFLEILEKlrQLPYPTLKQLRRLSQHFIS---DLTHLLDMF 199
Cdd:TIGR00573 167 AKLYLVMTGK--QTKYGENEGQQSRPYHAIKsivKKDMLLKLI 207
|
|
| PRK05711 |
PRK05711 |
DNA polymerase III subunit epsilon; Provisional |
1-129 |
1.53e-26 |
|
DNA polymerase III subunit epsilon; Provisional
Pssm-ID: 235574 [Multi-domain] Cd Length: 240 Bit Score: 109.18 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 1 MNKQRFVVIDVETTGNSPKKGDKIIQIAAVVIENGQITER-FSKYINPNKSIP--AFieQLTGISNQMVENEQPFEAVAE 77
Cdd:PRK05711 1 TAIMRQIVLDTETTGLNQREGHRIIEIGAVELINRRLTGRnFHVYIKPDRLVDpeAL--AVHGITDEFLADKPTFAEVAD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1196905317 78 EVFQLLDGAYFVAHNIHFDLGFVKYELHKAGFQLPD----CEVLDTVELSRIVFPG 129
Cdd:PRK05711 79 EFLDFIRGAELIIHNAPFDIGFMDYEFALLGRDIPKtntfCKVTDTLAMARRMFPG 134
|
|
| PRK06063 |
PRK06063 |
DEDDh family exonuclease; |
4-173 |
3.24e-20 |
|
DEDDh family exonuclease;
Pssm-ID: 180377 [Multi-domain] Cd Length: 313 Bit Score: 92.46 E-value: 3.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 4 QRFVVIDVETTGNSPKKgDKIIQIAAVVIE-NGQITERFSKYINPNKSI-PAFIEQLTGisnQMVENEQPFEAVAEEVFQ 81
Cdd:PRK06063 15 RGWAVVDVETSGFRPGQ-ARIISLAVLGLDaDGNVEQSVVTLLNPGVDPgPTHVHGLTA---EMLEGQPQFADIAGEVAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 82 LLDGAYFVAHNIHFDLGFVKYELHKAGFQLPDCEVLDTVELSRIVFPGFEGYKLTELSEELQLRHDQPHRADSDAEVTGL 161
Cdd:PRK06063 91 LLRGRTLVAHNVAFDYSFLAAEAERAGAELPVDQVMCTVELARRLGLGLPNLRLETLAAHWGVPQQRPHDALDDARVLAG 170
|
170
....*....|..
gi 1196905317 162 IFLEILEKLRQL 173
Cdd:PRK06063 171 ILRPSLERARER 182
|
|
| PRK06310 |
PRK06310 |
DNA polymerase III subunit epsilon; Validated |
1-184 |
5.40e-18 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 180525 [Multi-domain] Cd Length: 250 Bit Score: 84.50 E-value: 5.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 1 MNKQRFVVIDVETTGNSPKKgDKIIQIAAVVIENGQITERFSKYINPNKSIPAFIEQLTGISNQMVENEQPFEAVAEEVF 80
Cdd:PRK06310 4 LKDTEFVCLDCETTGLDVKK-DRIIEFAAIRFTFDEVIDSVEFLINPERVVSAESQRIHHISDAMLRDKPKIAEVFPQIK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 81 QLL-DGAYFVAHNIHFDLGFVKYELHKAG--FQLPDCEVLDTVELSRIvFPGFEGYKLTELSEELQLRHDQPHRADSDAE 157
Cdd:PRK06310 83 GFFkEGDYIVGHSVGFDLQVLSQESERIGetFLSKHYYIIDTLRLAKE-YGDSPNNSLEALAVHFNVPYDGNHRAMKDVE 161
|
170 180
....*....|....*....|....*..
gi 1196905317 158 VTGLIFLEILEKLRqlpypTLKQLRRL 184
Cdd:PRK06310 162 INIKVFKHLCKRFR-----TLEQLKQI 183
|
|
| PRK06195 |
PRK06195 |
DNA polymerase III subunit epsilon; Validated |
6-171 |
1.20e-16 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 235735 [Multi-domain] Cd Length: 309 Bit Score: 81.75 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 6 FVVIDVETtgnSPKKGDKIIQIAAVVIENGQITERFSKYINPN--KSIPAFIeQLTGISNQMVENEQPFEAVAEEVFQLL 83
Cdd:PRK06195 3 FVAIDFET---ANEKRNSPCSIGIVVVKDGEIVEKVHYLIKPKemRFMPINI-GIHGIRPHMVEDELEFDKIWEKIKHYF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 84 DGAYFVAHNIHFDLGFVKYELHKAGFQLPDCEVLDTVELSRIVFPGFEGYKLTELSEEL--QLRHdqpHRADSDAEVTGL 161
Cdd:PRK06195 79 NNNLVIAHNASFDISVLRKTLELYNIPMPSFEYICTMKLAKNFYSNIDNARLNTVNNFLgyEFKH---HDALADAMACSN 155
|
170
....*....|
gi 1196905317 162 IFLEILEKLR 171
Cdd:PRK06195 156 ILLNISKELN 165
|
|
| PRK09182 |
PRK09182 |
DNA polymerase III subunit epsilon; Validated |
7-186 |
4.21e-16 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 236397 [Multi-domain] Cd Length: 294 Bit Score: 80.02 E-value: 4.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 7 VVIDVETTGNSPKKgDKIIQIAAVVIEN------GQITERFSKYINPNKSIPAFIEQLTGISNQMVENEQ-PFEAVAeev 79
Cdd:PRK09182 40 VILDTETTGLDPRK-DEIIEIGMVAFEYdddgriGDVLDTFGGLQQPSRPIPPEITRLTGITDEMVAGQTiDPAAVD--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 80 fQLLDGA-YFVAHNIHFDLGFvkyelhkagfqlpdcevldtVELSRIVFP----------------GFEGYKLTELSEEL 142
Cdd:PRK09182 116 -ALIAPAdLIIAHNAGFDRPF--------------------LERFSPVFAtkpwacsvseidwsarGFEGTKLGYLAGQA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1196905317 143 QLRHDQpHRADSDAEVTglifLEILEklRQLP---YPTLKQLRRLSQ 186
Cdd:PRK09182 175 GFFHEG-HRAVDDCQAL----LELLA--RPLPetgQPPLAELLEASR 214
|
|
| ERI-1_3'hExo_like |
cd06133 |
DEDDh 3'-5' exonuclease domain of Caenorhabditis elegans ERI-1, human 3' exonuclease, and ... |
6-167 |
7.53e-14 |
|
DEDDh 3'-5' exonuclease domain of Caenorhabditis elegans ERI-1, human 3' exonuclease, and similar proteins; This subfamily is composed of Caenorhabditis elegans ERI-1, human 3' exonuclease (3'hExo), Drosophila exonuclease snipper (snp), and similar proteins from eukaryotes and bacteria. These are DEDDh-type DnaQ-like 3'-5' exonucleases containing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. ERI-1 has been implicated in the degradation of small interfering RNAs (RNAi). 3'hExo participates in the degradation of histone mRNAs. Snp is a non-essential exonuclease that efficiently degrades structured RNA and DNA substrates as long as there is a minimum of 2 nucleotides in the 3' overhang to initiate degradation. Snp is not a functional homolog of either ERI-1 or 3'hExo.
Pssm-ID: 99836 [Multi-domain] Cd Length: 176 Bit Score: 70.71 E-value: 7.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 6 FVVIDVETT--GNSPKKGDK--IIQIAAVVI--ENGQITERFSKYINP--NKSIPAFIEQLTGISNQMVENEQPFEAVAE 77
Cdd:cd06133 1 YLVIDFEATcwEGNSKPDYPneIIEIGAVLVdvKTKEIIDTFSSYVKPviNPKLSDFCTELTGITQEDVDNAPSFPEVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 78 EVFQlldgayFVAHNIHF--------DLG-FVKYELHKAGFQLPD--CEVLDTVELSRIVFPGFEGYKLTELSEELQLRH 146
Cdd:cd06133 81 EFLE------WLGKNGKYafvtwgdwDLKdLLQNQCKYKIINLPPffRQWIDLKKEFAKFYGLKKRTGLSKALEYLGLEF 154
|
170 180
....*....|....*....|..
gi 1196905317 147 D-QPHRADSDAEVTGLIFLEIL 167
Cdd:cd06133 155 EgRHHRGLDDARNIARILKRLL 176
|
|
| PRK09145 |
PRK09145 |
3'-5' exonuclease; |
6-174 |
1.79e-11 |
|
3'-5' exonuclease;
Pssm-ID: 236391 [Multi-domain] Cd Length: 202 Bit Score: 64.15 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 6 FVVIDVETTGNSPKKgDKIIQIAAVVIENGQI--TERFSKYINPNKSIPAFIEQLTGISNQMVENEQPFEAVAEEVFQLL 83
Cdd:PRK09145 31 WVALDCETTGLDPRR-AEIVSIAAVKIRGNRIltSERLELLVRPPQSLSAESIKIHRLRHQDLEDGLSEEEALRQLLAFI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 84 DGAYFVAHNIHFDLGFV-KYELHKAGFQLPDcevlDTVELSRIVF--------PGFEGYKLTELSEELQL----RHDqph 150
Cdd:PRK09145 110 GNRPLVGYYLEFDVAMLnRYVRPLLGIPLPN----PLIEVSALYYdkkerhlpDAYIDLRFDAILKHLDLpvlgRHD--- 182
|
170 180
....*....|....*....|....
gi 1196905317 151 rADSDAEVTGLIFLeileKLRQLP 174
Cdd:PRK09145 183 -ALNDAIMAALIFL----RLRKGD 201
|
|
| PRK06309 |
PRK06309 |
DNA polymerase III subunit epsilon; Validated |
5-155 |
3.32e-11 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 180524 [Multi-domain] Cd Length: 232 Bit Score: 64.06 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 5 RFVVIDVETTGNSPKKgDKIIQIAAVvieNGQITERFSKYINPNKSIPAFIEQLTGISNQMVENEQPFEAVAEEVFQLLD 84
Cdd:PRK06309 3 ALIFYDTETTGTQIDK-DRIIEIAAY---NGVTSESFQTLVNPEIPIPAEASKIHGITTDEVADAPKFPEAYQKFIEFCG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196905317 85 G-AYFVAH-NIHFDLGFVKYELHKAGFQLPDCEVLDTVELSRIVFPGFEGYKLTELSEELQLRHDQPHRADSD 155
Cdd:PRK06309 79 TdNILVAHnNDAFDFPLLRKECRRHGLEPPTLRTIDSLKWAQKYRPDLPKHNLQYLRQVYGFEENQAHRALDD 151
|
|
| PRK06722 |
PRK06722 |
exonuclease; Provisional |
2-166 |
3.27e-10 |
|
exonuclease; Provisional
Pssm-ID: 180670 [Multi-domain] Cd Length: 281 Bit Score: 61.99 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 2 NKQRFVVIDVETTGNSPKKGD--KIIQIAAVVIENG--QITERFSKYINPNKSIPAFIEQLTGISNQMVENEQPFEAVAE 77
Cdd:PRK06722 3 NATHFIVFDIERNFRPYKSEDpsEIVDIGAVKIEAStmKVIGEFSELVKPGARLTRHTTKLTGITKKDLIGVEKFPQIIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 78 EVFQLL-DGAYFVAHNIHfDLGFVKYELHKAGFQLPDCEVLDTVELSRIVFPGFEgyKLTELSEELQLRHDQ-------- 148
Cdd:PRK06722 83 KFIQFIgEDSIFVTWGKE-DYRFLSHDCTLHSVECPCMEKERRIDLQKFVFQAYE--ELFEHTPSLQSAVEQlgliwegk 159
|
170
....*....|....*...
gi 1196905317 149 PHRADSDAEVTGLIFLEI 166
Cdd:PRK06722 160 QHRALADAENTANILLKA 177
|
|
| RNaseT |
cd06134 |
DEDDh 3'-5' exonuclease domain of RNase T; RNase T is a DEDDh-type DnaQ-like 3'-5' ... |
5-170 |
3.51e-10 |
|
DEDDh 3'-5' exonuclease domain of RNase T; RNase T is a DEDDh-type DnaQ-like 3'-5' exoribonuclease E implicated in the 3' maturation of small stable RNAs and 23srRNA, and in the end turnover of tRNA. It contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. RNase T is related to the proofreading domain of DNA polymerase III. Despite its important role, RNase T is mainly found only in gammaproteobacteria. It is speculated that it might have originated from DNA polymerase III at the time the gamma division of proteobacteria diverged from other bacteria. RNase T is a homodimer with the catalytic residues of one monomer contacting a large basic patch on the other monomer to form a functional active site.
Pssm-ID: 99837 [Multi-domain] Cd Length: 189 Bit Score: 60.38 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 5 RF-----VVIDVETTGNSPKKgDKIIQIAAVVI---ENG--QITERFSKYINPNKSI---PAFIEqLTGIsnqmvENEQP 71
Cdd:cd06134 1 RFrgflpVVVDVETGGFNPQT-DALLEIAAVTLemdEQGnlYPDETFHFHILPFEGAnldPAALE-FNGI-----DPFHP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 72 F-EAVAE-----EVFQLLDG---------AYFVAHNIHFDLGFVKYELHKAGFQ---LPDCEVLDTVELSRIVfpgfegY 133
Cdd:cd06134 74 FrFAVDEkealkEIFKPIRKalkaqgctrAILVGHNAHFDLGFLNAAVARCKIKrnpFHPFSTFDTATLAGLA------Y 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1196905317 134 KLTELSEELQ-----LRHDQPHRADSDAEVTGLIFLEILEKL 170
Cdd:cd06134 148 GQTVLAKACQaagieFDNKEAHSALYDTQKTAELFCKIVNRW 189
|
|
| PRK07983 |
PRK07983 |
exodeoxyribonuclease X; Provisional |
6-168 |
1.60e-09 |
|
exodeoxyribonuclease X; Provisional
Pssm-ID: 181186 [Multi-domain] Cd Length: 219 Bit Score: 58.96 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 6 FVVIDVETTGnspKKGDkIIQIAAVVIENGQITERFSKYINPNKSIPAFIEQLTGISNQMVENEQPFEAVaeeVFQLLDG 85
Cdd:PRK07983 2 LRVIDTETCG---LQGG-IVEIASVDVIDGKIVNPMSHLVRPDRPISPQAMAIHRITEAMVADKPWIEDV---IPHYYGS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 86 AYFVAHNIHFDLGfVKYELHKagfqlpdcEVLDTVELSRIVFPGFeGYKLTELSEELQLRHDQP-----HRADSDAEVTG 160
Cdd:PRK07983 75 EWYVAHNASFDRR-VLPEMPG--------EWICTMKLARRLWPGI-KYSNMALYKSRKLNVQTPpglhhHRALYDCYITA 144
|
....*...
gi 1196905317 161 LIFLEILE 168
Cdd:PRK07983 145 ALLIDIMN 152
|
|
| Csf4_U |
cd09708 |
CRISPR/Cas system-associated DinG family helicase Csf4; CRISPR (Clustered Regularly ... |
263-895 |
1.46e-08 |
|
CRISPR/Cas system-associated DinG family helicase Csf4; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DinG family DNA helicase
Pssm-ID: 187839 [Multi-domain] Cd Length: 632 Bit Score: 58.45 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 263 QMMMMREVADAFANREHALIEAPPGIGKTIGYLIPAALFAKKSKKPVIISTYSTL-LQQQILTKDLPIVQDLFPFPVTAA 341
Cdd:cd09708 2 QALFYRNCLTSLRQKRIGMLEASTGVGKTLAMIMAALTMLKERPDQKIAIAVPTLaLMGQLWSELERLTAEGLAGPVQAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 342 ILKGQSHYLCLYKFEQVLHEED--DNYDAV---------------LTKAQLLVWLTETNTGDVAElnlPSGGKLLWDRLA 404
Cdd:cd09708 82 FFPGSQEFVSPGALQELLDQSDgpGDKDAVvrlwmgqggprkvapLFNRMRDVTLLIHDTADIRG---YVSYREQWDSLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 405 YDDDSYKR-----SRSEHVIGFYERAKQ----------------------IAMRSDLVITNHSLLLTDeasqkkRLPESG 457
Cdd:cd09708 159 RCSAMSRAptkmaSMTHDLKALATLNPQdfvtedeedkrwvtslvesreyYARKSRILACTHTMLKWG------LLPQPD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 458 TFIIDEAHHFE----RAASEHLG----KRATYIeLHTKLSRIGTLKEQGLLKKMRQLFQRNSLPVDSFFELEE---WLQH 526
Cdd:cd09708 233 ILIVDEAHLFEqnisRVYSNALSlrmlRFHLEV-SHRKTGAIGSAVVAAVSAVSHRLRQVSALGDGQTLCLDAgnkELET 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 527 VQAESDAFFS-------SVHSFVK-RRKPKEDLNRLVFKVNKE--------SQDKSWSILTDGAERLCSMLTHLQQLFEA 590
Cdd:cd09708 312 LFADLDAALEikstpnkKALSVVKdVKKARIILDNAITAIQGKqstvylqfSPDRRFPSLIVGREDLGKVMGGLWKDVTH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 591 QSSLMekhlkgmkSKTVFLADEYQrsmkglQHYCQTLQKLFFGSDDDEAVWIEIDAKGAKNAVAiyaqplepgelladqf 670
Cdd:cd09708 392 GAIIV--------SATLYLPDRFG------QMSCDYLKRVLSLPLSRLDTPSPIVAPWVRNLIP---------------- 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 671 farknSVVLTSATltvegsfqfmierlglsdffPRTMRiESPFSYDERMqvmipkemksiqDTGQPEFIQDTARYIELMA 750
Cdd:cd09708 442 -----HLHVPNAK--------------------ARFLL-SRPVGKTEQG------------DANLAGWLENVSLSTAAIL 483
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 751 KEKQPKILVLFTSHDMLKKVHQELKHNMSASGIQLLAQGITGGSPGKLMKTFKTSNQAILLGTNHFWEGVDF-----PGD 825
Cdd:cd09708 484 RKAQGGTLVLTTAFSHISAIGQLVELGIPAEIVIQSEKNRLASAEQQFLALYANGIQPVLIAAGGAWTGIDLhdpsvSPD 563
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1196905317 826 E---LTTVMIVRLPF---RSPDHplhaakceLARKKGKNPFQTVsLPEAVLTFRQGIGRLLRSAGDKGTIMILDRR 895
Cdd:cd09708 564 KdnlLTDLIITCAPFglnRSLSM--------LKRIRKTSVRPEI-INESLMMLRQGLGRLVRHPDMPINRRIHDLD 630
|
|
| SF2_C_XPD |
cd18788 |
C-terminal helicase domain of xeroderma pigmentosum group D (XPD) family DEAD-like helicases; ... |
729-895 |
2.79e-08 |
|
C-terminal helicase domain of xeroderma pigmentosum group D (XPD) family DEAD-like helicases; The xeroderma pigmentosum group D (XPD)-like family members are DEAD-box helicases belonging to superfamily (SF)2. This family includes DDX11 (also called ChlR1), a protein involved in maintaining chromosome transmission fidelity and genome stability, the TFIIH basal transcription factor complex XPD subunit, and FANCJ (also known as BRIP1), a DNA helicase required for the maintenance of chromosomal stability. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350175 [Multi-domain] Cd Length: 159 Bit Score: 54.15 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 729 SIQDTGQPEFIQDTARYIELMAKEKQPKILVLFTSHDMLKKVhqelkhnmSASGIQLLAqgITGGspgklmktfKTSnqa 808
Cdd:cd18788 20 KFQTREDEAVMDELGNLLLELCAVVPDGVLVFFPSYSYMERV--------VSRGALLLA--VCRG---------KVS--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 809 illgtnhfwEGVDFPGDELTTVMIVRLPFRSPDHPLHAAKCE----LARKKGKNPFQTVSLPeAVLTFRQGIGRLLRSAG 884
Cdd:cd18788 78 ---------EGIDFSDDLGRAVIMVGIPYPNTKDPILKLKMDdleyLRDKGLLTGEDWYTFQ-AMRAVNQAIGRAIRHKN 147
|
170
....*....|.
gi 1196905317 885 DKGTIMILDRR 895
Cdd:cd18788 148 DYGAIVLLDKR 158
|
|
| TREX1_2 |
cd06136 |
DEDDh 3'-5' exonuclease domain of three prime repair exonuclease (TREX)1, TREX2, and similar ... |
6-113 |
9.27e-08 |
|
DEDDh 3'-5' exonuclease domain of three prime repair exonuclease (TREX)1, TREX2, and similar proteins; Three prime repair exonuclease (TREX)1 and TREX2 are closely related DEDDh-type DnaQ-like 3'-5' exonucleases. They contain three conserved sequence motifs known as ExoI, II, and III, with a specific Hx(4)D conserved pattern at ExoIII. These motifs contain four conserved acidic residues that participate in coordination of divalent metal ions required for catalysis. Both proteins play a role in the metabolism and clearance of DNA. TREX1 is the major 3'-5' exonuclease activity detected in mammalian cells. Mutations in the human TREX1 gene can cause Aicardi-Goutieres syndrome (AGS), which is characterized by perturbed innate immunity and presents itself as a severe neurological disease. TREX1 degrades ssDNA generated by aberrant replication intermediates to prevent checkpoint activation and autoimmune disease. There are distinct structural differences between TREX1 and TREX2 that point to different biological roles for these proteins. The main difference is the presence of about 70 amino acids at the C-terminus of TREX1. In addition, TREX1 has a nonrepetitive proline-rich region that is not present in the TREX2 protein. Furthermore, TREX2 contains a conserved DNA binding loop positioned adjacent to the active site that has a sequence distinct from the corresponding loop in TREX1. Truncations in the C-terminus of human TREX1 cause autosomal dominant retinal vasculopathy with cerebral leukodystrophy (RVCL), a neurovascular syndrome featuring a progressive loss of visual acuity combined with a variable neurological picture.
Pssm-ID: 99839 [Multi-domain] Cd Length: 177 Bit Score: 52.72 E-value: 9.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 6 FVVIDVETTGNSPKKGDKIIQIAAVV-----IENG--------QITERFSKYINPNKSIPAFIEQLTGISNQMVENEQPF 72
Cdd:cd06136 1 FVFLDLETTGLPKHNRPEITELCLVAvhrdhLLNTsrdkpalpRVLDKLSLCFNPGRAISPGASEITGLSNDLLEHKAPF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1196905317 73 EAVAEEVFQL----LDGAY-FVAHN-IHFDLGFVKYELHKAGFQLPD 113
Cdd:cd06136 81 DSDTANLIKLflrrQPKPIcLVAHNgNRFDFPILRSELERLGTKLPD 127
|
|
| rad3 |
TIGR00604 |
DNA repair helicase (rad3); All proteins in this family for which funcitons are known are ... |
671-895 |
3.97e-07 |
|
DNA repair helicase (rad3); All proteins in this family for which funcitons are known are DNA-DNA helicases that funciton in the initiation of transcription and nucleotide excision repair as part of the TFIIH complex. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273169 [Multi-domain] Cd Length: 705 Bit Score: 53.95 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 671 FARKNSVVLTSATLTVEGSFQFMIE-RLGLSDFFPRTMRiespfsyDERMQVMI---PKEMKSIQDTGQ----PEFIQDT 742
Cdd:TIGR00604 438 FERVRSVILASGTLSPLDAFPRNLGfNPVSQDSPTHILK-------RENLLTLIvtrGSDQVPLSSTFEirndPSLVRNL 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 743 ARYIELMAKEKQPKILVLFTSHDMLKKVHQELKHNMSASGIQ----LLAQGITGGSPGKLMKTFK----TSNQAILLGT- 813
Cdd:TIGR00604 511 GELLVEFSKIIPDGIVVFFPSYSYLENIVSTWKEMGILENIEkkklIFVETKDAQETSDALERYKqavsEGRGAVLLSVa 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 814 -NHFWEGVDFPGDELTTVMIVRLPFRSPDHPLHAAkcELARKKGKNPFQTVSLPEAVLTFR---QGIGRLLRSAGDKGTI 889
Cdd:TIGR00604 591 gGKVSEGIDFCDDLGRAVIMVGIPYEYTESRILLA--RLEFLRDQYPIRENQDFYEFDAMRavnQAIGRVIRHKDDYGSI 668
|
....*.
gi 1196905317 890 MILDRR 895
Cdd:TIGR00604 669 VLLDKR 674
|
|
| REX4_like |
cd06144 |
DEDDh 3'-5' exonuclease domain of RNA exonuclease 4, XPMC2, Interferon Stimulated Gene product ... |
29-97 |
3.12e-06 |
|
DEDDh 3'-5' exonuclease domain of RNA exonuclease 4, XPMC2, Interferon Stimulated Gene product of 20 kDa, and similar proteins; This subfamily is composed of RNA exonuclease 4 (REX4 or Rex4p), XPMC2, Interferon (IFN) Stimulated Gene product of 20 kDa (ISG20), and similar proteins. REX4 is involved in pre-rRNA processing. It controls the ratio between the two forms of 5.8S rRNA in yeast. XPMC2 is a Xenopus gene which was identified through its ability to correct a mitotic defect in fission yeast. The human homolog of XPMC2 (hPMC2) may be involved in angiotensin II-induced adrenal cell cycle progression and cell proliferation. ISG20 is an IFN-induced antiviral exonuclease with a strong preference for single-stranded RNA and minor activity towards single-stranded DNA. These proteins are DEDDh-type DnaQ-like 3'-5' exonucleases containing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. REX proteins function in the processing and maturation of many RNA species, similar to the function of Escherchia coli RNase T.
Pssm-ID: 99847 Cd Length: 152 Bit Score: 47.90 E-value: 3.12e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196905317 29 AVVIENGQITerFSKYINPNKSIPAFIEQLTGISNQMVENEQPFEAVAEEVFQLLDGAYFVAHNIHFDL 97
Cdd:cd06144 23 SIVNEDGNVV--YDTYVKPQEPVTDYRTAVSGIRPEHLKDAPDFEEVQKKVAELLKGRILVGHALKNDL 89
|
|
| ISG20 |
cd06149 |
DEDDh 3'-5' exonuclease domain of Interferon Stimulated Gene product of 20 kDa, and similar ... |
7-102 |
4.33e-06 |
|
DEDDh 3'-5' exonuclease domain of Interferon Stimulated Gene product of 20 kDa, and similar proteins; Interferon (IFN) Stimulated Gene product of 20 kDa (ISG20) is an IFN-induced antiviral exonuclease with a strong preference for single-stranded RNA and minor activity towards single-stranded DNA. It was also independently identified by its response to estrogen and was called HEM45 (human estrogen regulated transcript). ISG20 is a DEDDh-type DnaQ-like 3'-5' exonuclease containing three conserved sequence motifs termed ExoI, ExoII and ExoIII with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. ISG20 may be a major effector of innate immunity against pathogens including viruses, bacteria, and parasites. It is located in promyelocytic leukemia (PML) nuclear bodies, sites for oncogenic DNA viral transcription and replication. It may carry out its function by degrading viral RNAs as part of the IFN-regulated antiviral response.
Pssm-ID: 99852 Cd Length: 157 Bit Score: 47.43 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 7 VVIDVETTGNSPKKGDKIIQIAAVVIENGQITerFSKYINPNKSIPAFIEQLTGISNQMVENEQPFEAVAEEVFQLLDGA 86
Cdd:cd06149 1 VAIDCEMVGTGPGGRESELARCSIVNYHGDVL--YDKYIRPEGPVTDYRTRWSGIRRQHLVNATPFAVAQKEILKILKGK 78
|
90
....*....|....*.
gi 1196905317 87 YFVAHNIHFDLGFVKY 102
Cdd:cd06149 79 VVVGHAIHNDFKALKY 94
|
|
| PRK07942 |
PRK07942 |
DNA polymerase III subunit epsilon; Provisional |
10-156 |
8.93e-06 |
|
DNA polymerase III subunit epsilon; Provisional
Pssm-ID: 181176 [Multi-domain] Cd Length: 232 Bit Score: 48.05 E-value: 8.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 10 DVETTGNSPKKgDKIIQIAAVVI-ENGQITERFSKYINPNKSIPAFIEQLTGISNQMV-ENEQPFEAVAEEVFQLL---- 83
Cdd:PRK07942 12 DLETTGVDPET-ARIVTAALVVVdADGEVVESREWLADPGVEIPEEASAVHGITTEYArAHGRPAAEVLAEIADALreaw 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1196905317 84 -DGAYFVAHNIHFDLGFVKYELHKAGF-QLPDCEVLDTVELSRIVFPGFEG-YKLTELSEELQLRHDQPHRADSDA 156
Cdd:PRK07942 91 aRGVPVVVFNAPYDLTVLDRELRRHGLpSLVPGPVIDPYVIDKAVDRYRKGkRTLTALCEHYGVRLDNAHEATADA 166
|
|
| UvrD_C |
pfam13361 |
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety ... |
5-82 |
1.30e-05 |
|
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety of helicase enzymes. This domain has a AAA-like structural fold.
Pssm-ID: 433145 [Multi-domain] Cd Length: 377 Bit Score: 48.56 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 5 RFVVIDVETTGNSPKKgDKIIQIAAVVI-ENGQITERFSKYINPNKSIPAFIeQLTGISNQMVEN--EQPFEAVAEEVFQ 81
Cdd:pfam13361 187 NIVVFDVETTGLDTTE-DEIIQIAAIKLnKKGVVIESFERFLRLKKPVGDSL-QVHGFSDEFLQEngETPAEALRDFLEK 264
|
.
gi 1196905317 82 L 82
Cdd:pfam13361 265 L 265
|
|
| ExoI_N |
cd06138 |
N-terminal DEDDh 3'-5' exonuclease domain of Escherichia coli exonuclease I and similar ... |
10-159 |
1.61e-05 |
|
N-terminal DEDDh 3'-5' exonuclease domain of Escherichia coli exonuclease I and similar proteins; This subfamily is composed of the N-terminal domain of Escherichia coli exonuclease I (ExoI) and similar proteins. ExoI is a monomeric enzyme that hydrolyzes single stranded DNA in the 3' to 5' direction. It plays a role in DNA recombination and repair. It primarily functions in repairing frameshift mutations. The N-terminal domain of ExoI is a DEDDh-type DnaQ-like 3'-5 exonuclease containing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. The ExoI structure is unique among DnaQ family enzymes in that there is a large distance between the two metal ions required for catalysis and the catalytic histidine is oriented away from the active site.
Pssm-ID: 99841 [Multi-domain] Cd Length: 183 Bit Score: 46.49 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 10 DVETTGNSPKKgDKIIQIAAVVI-ENGQITERFSKYINPNKS-IP---AFIeqLTGISNQMVENEQPFEA-VAEEVFQLL 83
Cdd:cd06138 4 DYETFGLNPSF-DQILQFAAIRTdENFNEIEPFNIFCRLPPDvLPspeALI--VTGITPQQLLKEGLSEYeFIAKIHRLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 84 D--GAYFVAHN-IHFDLGFVKYELHKAGFQLPDCE---------VLDTVELSRIVFPG-------FEG---YKLTELSEE 141
Cdd:cd06138 81 NtpGTCIVGYNnIRFDDEFLRFAFYRNLYDPYTWEwkngnsrwdLLDVVRAYYALRPDgivwpknDDGkpsFKLEDLAQA 160
|
170
....*....|....*...
gi 1196905317 142 LQLRHDQPHRADSDAEVT 159
Cdd:cd06138 161 NGIEHSNAHDALSDVEAT 178
|
|
| PRK05601 |
PRK05601 |
DNA polymerase III subunit epsilon; Validated |
6-107 |
1.54e-04 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 235529 [Multi-domain] Cd Length: 377 Bit Score: 45.20 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 6 FVVIDVETTGNSPKKGdKIIQIAAVVI-ENGQITERFSKYINPNKSIPAFieQLTGISNQMVENEQPFEAVAEEVFQLLD 84
Cdd:PRK05601 48 FVAVSIQTSGIHPSTS-RLITIDAVTLtADGEEVEHFHAVLNPGEDPGPF--HLHGLSAEEFAQGKRFSQILKPLDRLID 124
|
90 100
....*....|....*....|...
gi 1196905317 85 GAYFVAHNIHFDLGFVKYELHKA 107
Cdd:PRK05601 125 GRTLILHNAPRTWGFIVSEAKRA 147
|
|
| PTZ00315 |
PTZ00315 |
2'-phosphotransferase; Provisional |
6-86 |
5.96e-04 |
|
2'-phosphotransferase; Provisional
Pssm-ID: 240356 [Multi-domain] Cd Length: 582 Bit Score: 43.73 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 6 FVVIDVETTGNSPKKGD--KIIQIAAVVIE--NGQITERFSKYINP--NKSIPAFIEQLTGISNQMVENEQPFEAVAEEV 79
Cdd:PTZ00315 58 YVVLDFEATCEADRRIEdaEVIEFPMVLVDarTATPVAEFQRYVRPvkNPVLSRFCTELTGITQSMVSRADPFPVVYCEA 137
|
....*..
gi 1196905317 80 FQLLDGA 86
Cdd:PTZ00315 138 LQFLAEA 144
|
|
| DEXDc2 |
smart00488 |
DEAD-like helicases superfamily; |
257-322 |
9.00e-04 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214693 [Multi-domain] Cd Length: 289 Bit Score: 42.37 E-value: 9.00e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1196905317 257 YEKRDGQMMMMREVADAFANREHALIEAPPGIGKTIGYL--IPAALFAKKSKKPVIISTYSTLLQQQI 322
Cdd:smart00488 7 YEPYPIQYEFMEELKRVLDRGKIGILESPTGTGKTLSLLclTLTWLRSFPERIQKIKLIYLSRTVSEI 74
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
278-491 |
1.29e-03 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 40.08 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 278 EHALIEAPPGIGKTIGYLIPAA-LFAKKSKKPVIISTYSTLLQQQiltkdLPIVQDLFPFPVTAAILkgqshylclykfe 356
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALlLLLKKGKKVLVLVPTKALALQT-----AERLRELFGPGIRVAVL------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 357 qvlheeddnydavltkaqllvwltetntgdvaelnlpsggkllwdrlaYDDDSYKrsrsehvigfyERAKQIAMRSDLVI 436
Cdd:cd00046 64 ------------------------------------------------VGGSSAE-----------EREKNKLGDADIII 84
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1196905317 437 TNHSLLLTD-EASQKKRLPESGTFIIDEAHHFERAASEHLGKRATYIELHTKLSRI 491
Cdd:cd00046 85 ATPDMLLNLlLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQV 140
|
|
| PRK09146 |
PRK09146 |
DNA polymerase III subunit epsilon; Validated |
6-122 |
3.05e-03 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 236392 [Multi-domain] Cd Length: 239 Bit Score: 40.29 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 6 FVVIDVETTGNSPKKgDKIIQIAAVVIENGQITERFSKY--INPNKSIPAfiEQLT--GISNQMVENEQPFEAVAEEVFQ 81
Cdd:PRK09146 49 FVALDFETTGLDAEQ-DAIVSIGLVPFTLQRIRCRQARHwvVKPRRPLEE--ESVVihGITHSELQDAPDLERILDELLE 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1196905317 82 LLDGAYFVAHNIHFDLGFVKYELHK---AGFQLPdceVLDTVEL 122
Cdd:PRK09146 126 ALAGKVVVVHYRRIERDFLDQALRNrigEGIEFP---VIDTMEI 166
|
|
| PRK07748 |
PRK07748 |
3'-5' exonuclease KapD; |
1-82 |
3.16e-03 |
|
3'-5' exonuclease KapD;
Pssm-ID: 236087 Cd Length: 207 Bit Score: 40.06 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 1 MNKQRFVVIDVETTGNSPKKGDK-----IIQIAAVVIENGQITERFSKYINPnKSIPAFIEQ---LTGISNQMVENEQPF 72
Cdd:PRK07748 1 MDEQQFLFLDFEFTMPQHKKKPKgffpeIIEVGLVSVVGCEVEDTFSSYVKP-KTFPSLTERcksFLGITQEDVDKGISF 79
|
90
....*....|
gi 1196905317 73 EAVAEEVFQL 82
Cdd:PRK07748 80 EELVEKLAEY 89
|
|
| PRK07247 |
PRK07247 |
3'-5' exonuclease; |
24-168 |
6.01e-03 |
|
3'-5' exonuclease;
Pssm-ID: 180906 [Multi-domain] Cd Length: 195 Bit Score: 38.99 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 24 IIQIAAVVIENGQITERFSKYINPNKSIPAFIEQLTGISNQMVENEQPFEAVAEEvFQLLDGayfvahnihfDLGFVKYE 103
Cdd:PRK07247 23 IIQVSAVKYDDHKEVDSFDSYVYTDVPLQSFINGLTGITADKIADAPKVEEVLAA-FKEFVG----------ELPLIGYN 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196905317 104 LHKAGFQLPDCEVLDTVELSRI-VFP-----------GFEGYKLTELSEELQLRhDQPHRADSDAEVTGLIFLEILE 168
Cdd:PRK07247 92 AQKSDLPILAENGLDLSDQYQVdLYDeaferrssdlnGIANLKLQTVADFLGIK-GRGHNSLEDARMTARVYESFLE 167
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
237-320 |
6.33e-03 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350682 [Multi-domain] Cd Length: 189 Bit Score: 38.85 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905317 237 FEIESWEAGNEKALSELMPGYEKrdgqmMMMREVadaFANREHALIeAPPGIGKTIGYLIPAALFAKKSKKPVIISTYST 316
Cdd:cd17924 1 KEYEDFEEFFKKKTGFPPWGAQR-----TWAKRL---LRGKSFAII-APTGVGKTTFGLATSLYLASKGKRSYLIFPTKS 71
|
....
gi 1196905317 317 LLQQ 320
Cdd:cd17924 72 LVKQ 75
|
|
| PRK05359 |
PRK05359 |
oligoribonuclease; Provisional |
2-31 |
7.25e-03 |
|
oligoribonuclease; Provisional
Pssm-ID: 235429 Cd Length: 181 Bit Score: 38.60 E-value: 7.25e-03
10 20 30
....*....|....*....|....*....|
gi 1196905317 2 NKQRFVVIDVETTGNSPKKgDKIIQIAAVV 31
Cdd:PRK05359 1 NEDNLIWIDLEMTGLDPER-DRIIEIATIV 29
|
|
| |
