|
Name |
Accession |
Description |
Interval |
E-value |
| COG4889 |
COG4889 |
Predicted helicase [General function prediction only]; |
1-1647 |
0e+00 |
|
Predicted helicase [General function prediction only];
Pssm-ID: 443917 [Multi-domain] Cd Length: 1571 Bit Score: 2187.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 1 MSTFSDVLDQLRKNQP----QGKYgiaFEKLMVNYFRNDPTLSEEYEDVGRFVDW--KYYDGQSDTGIDLVARRREDGRW 74
Cdd:COG4889 2 MTTLDDLLDQLRNAARsereKGTY---FERLMRAYLRNDPTYADLYSDVWLWSDWpeLYGRSKKDTGIDLVARDRDTGEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 75 VAIQCKFYEPTAYLQKSHLDSFFEKSGrsfdtehgKDSFAQRIIISTTDRWSKNAEEMLDNQLIPTNRIGTASIAESPID 154
Cdd:COG4889 79 WAIQCKFYDPDYTIQKADIDSFFTASG--------KKYFSRRLIVSTTDWWSNNAEAALAQQQIPVNRIGLSDLEESPID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 155 WDITFPGSDIAInlTRKEVYQPRPHQDEAIAKAIAGFEAHDRGKLIMACGTGKTFTALRLAERFAelnGNKARVLFLVPS 234
Cdd:COG4889 151 WSQFQWEPPEEV--VLKAKKTLRPHQQEAIEAVLAGFKTHDRGKLIMACGTGKTFTSLRIAEELA---GKGGRVLFLVPS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 235 ISLLSQTLKEWTAQSQThlPLKPYAVCSDQKVSKK----AEDIASYDLDVPVSTNGADIKLRTEQGKRRQGLNVIFSTYQ 310
Cdd:COG4889 226 ISLLSQTLREWTAESEV--PLRSFAVCSDSKVGKRrkkdDEDTSAHDLAYPATTDAEKLAAAAQKRHDADRMTVVFSTYQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 311 SIEAIHEAQELGMDDFDLVICDEAHRTTGVTLAGEDASNFVKIHDENYIKASKRLYMTATPRLFDDNVKGKAEEHSAELA 390
Cdd:COG4889 304 SIDVVADAQKLGLPEFDLIICDEAHRTTGATLAGEDESAFVRVHDNDYIKAKKRLYMTATPRIYGDDAKKKAKEASAVLA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 391 SMDDEDIYGPEFYRLGFGEAVDKGLLTDYKVLVMTVEEDIAADV---LAAYPTNEINLTTASAMIGAWNGLAKRSGAEQD 467
Cdd:COG4889 384 SMDDEALFGPEFHRLGFGEAVERGLLTDYKVIVLAVDESHVSRRlqqLLADNGNELKLDDAAKIVGCWNGLAKRGGEEDG 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 468 TKSGfeagaQPMRRTVAFAKDIKASKTIQETFPTLIRQYQEQLKDHAATNDVSLlnidlQVAVEHVDGTMNALERGNKIS 547
Cdd:COG4889 464 TDDP-----APMKRAVAFCQTIKESKRIAEHFVSVVNIYLMFQDDEAEEDAPSL-----RCEAEHVDGTMNALERNEKLD 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 548 WLESSIPEDETRILTNARCLSEGVDVPALDSVIFFHPRNSMVDVVQSVGRVMRKAEGKDYGYIILPVAIPPGVSPSQALN 627
Cdd:COG4889 534 WLKAETPENTCRILSNARCLSEGVDVPALDAVLFLTPRKSQVDVVQSVGRVMRKAPGKKYGYIILPVVIPAGVEPEEALD 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 628 DNTRFRVVWQILNALRAHDDRFNAKVNSIALNEKVELPIDIESVKKTKRDEEQTNEDKakeakakldasdatpasqsess 707
Cdd:COG4889 614 DNETYKVVWQVLNALRSHDDRFDAMINKIELNGPDPDKIEVIGITDDIERDPSKTTGE---------------------- 671
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 708 GEQELTPEQMTLFSLEAWQEAMYVKLVDKVGTRTYWEDWADDVATIAEAQIARIKALINAADDTIRKEFEVFIEGLRGNL 787
Cdd:COG4889 672 QKKADPEQQELEFELGEIERAIYAKIVKKVGNRRYWEDWAKDVAKIAQRHITRIKAILENPDQPAREAFDRFLKGLRDNL 751
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 788 NDSITEDEAISMLSQHLITAPVFNALFTEHDFAAHNPVARVMQRMVDALSDAKLESETKSLTDFYESVRVRASEVSSASG 867
Cdd:COG4889 752 NDSITEDEAIEMLAQHLITKPVFDALFAGYSFAAHNPVSQAMQRMLDVLDEHGLEKETETLEKFYESVRMRAEGIDNAEG 831
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 868 KQQVIKDLYERFFRKAFKKQSEALGIVYTPVEIVDFILRSADQISRWHFGKGLTDEGVHILDPFTGTGTFMVRLLQSGLI 947
Cdd:COG4889 832 RQKIIVELYDKFFKTAFPKTTERLGIVYTPVEVVDFILHSVDDVLRKEFGQSLADEGVHILDPFTGTGTFIVRLLQSGLI 911
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 948 EPEDLARKYACELHATEIMLLAYYVAAVNIETTYNALQAEraqrdgepepGYVPFDGIALADTFQIHEEGDIPDLKVFKE 1027
Cdd:COG4889 912 PPEDLPRKYANELHANEIVLLAYYIAAINIEATYHELMGG----------DYVPFEGIVLTDTFQMYEDEDDLDDEVFPD 981
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 1028 NNAAIQRQIDAPINVIIGNPPYSAKQTSANDDNANLKYPTLDSRIESTFAANSTATNKNSLYDSYLRAFRWSIDRLGTHG 1107
Cdd:COG4889 982 NSERRKRQKKLPIRVIVGNPPYSVGQKSANDNNANLKYPTLDARIRSTYAARSTATNKNSLYDSYIRAIRWASDRIGDRG 1061
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 1108 VLAFVSNGGWIDSNTADGVRLSLEDELSDIYVYNLRGNQRTAGEQSRKEGGKVFGSGSRNTVAVIIAVKReiPDDV---C 1184
Cdd:COG4889 1062 VIAFVTNAGWIDGNAADGMRKCLAEEFSSIYVFNLRGNQRTSGELSRKEGGKIFGSGSRAPIAITILVKN--PDHSgpgR 1139
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 1185 IHYRDIGDYLSADEKLAIVDRST-LDNVEWQNIEPNIYGEWLNQRDEDFETWPAIGEKKDKKTPVVFHNYSRGLSTARDV 1263
Cdd:COG4889 1140 IHYHDIGDYLSREEKLAKIAEFGsIAGITWQRIIPNEHGDWLNQRDDDFDSFIPLGDKKKKSPPSLFENYSRGVKTNRDA 1219
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 1264 WCYGSTPSAVTSQMQTLITTYDAARDEFRDWIQSARITKPRETDVnaflakrpeyadlSKISWNRSLKQQLAGNKIISFN 1343
Cdd:COG4889 1220 WVYNFSKEKLAENMQRMIEFYNSELDRYQAAVKQIDVDDFIDNDP-------------TKISWSRSLKQDLERGKKLEFD 1286
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 1344 ASRIMKSLYRPFHVQFAYFHQPVNDMVYQLPKLFPTPHHDNMTILLAGPYPNIAGHCFSTKVLPDLNVLTA-SQNFPRWT 1422
Cdd:COG4889 1287 PDAIVTSLYRPFTKQWLYFDRRLNDMVYQMPKIFPTPTHENLVICVTGPGSGKGFSALITDVLPDLHLLIGgGQCFPLYL 1366
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 1423 WEPVETPEGELDFGMGASEGSEPGT-EGEILDGYRRVDNVTDEILGIYREALGSNVTKDDIFYFVYGQLHDPGYREKYAA 1501
Cdd:COG4889 1367 YEKVESDGGLLSAEDGSADRDDAITdEVLDAFAAAYGDYFISKGDIFYYTYYYLDLLLYSEEYRYYAAKELPKKPLRRFA 1446
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 1502 DLKKMLPHIETPTLRARFDQLTAAGRELMDLHVNYEDVEPWPVTVDVkasadendretwRVQKMKWAKKKDpstgknVND 1581
Cdd:COG4889 1447 PAFDAAARAPAELAILRFAAETLALEELIDLDLAEVPGEIGDNEEEV------------RVKKMKKGKETK------KKD 1508
|
1610 1620 1630 1640 1650 1660
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092649119 1582 VTTLVYNKSVTVRDIPaeaDEYMLGSRSALAWIIDRYQVKKDKASGIVNDPNDWADEVGNPRYIVD 1647
Cdd:COG4889 1509 KKDIIYNTIITITKIP---LDAYGYVVNAKEALDWPYERYEVKVDGISGIANDAIDDVNDPNDDPL 1571
|
|
| Type_ISP_C |
pfam18135 |
Type ISP C-terminal specificity domain; This is the C-terminal domain of Type ISP ... |
1249-1648 |
8.39e-101 |
|
Type ISP C-terminal specificity domain; This is the C-terminal domain of Type ISP restriction-modification enzyme LLaBIII present in Lactococcus lactis subsp. cremoris. Type ISP restriction-modification (RM) enzymes provide a potent defence against infection by foreign and bacteriophage DNA. This domain interacts extensively with DNA and is known as the target recognition domain (TRD). TRD works by recognising 6/7 base pairs of asymmetric sequence.
Pssm-ID: 465663 Cd Length: 342 Bit Score: 327.29 E-value: 8.39e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 1249 VFHNYSRGLSTARDVWCYGSTPSAVTSQMQTLITTYDAARDefrdwiqsaritkpretdvnaflAKRPEYADLSKISWNR 1328
Cdd:pfam18135 2 LFPWYSPGVKTNRDAWVYNFSKEELEKRWKRLIDEYNEERR-----------------------RLLFLTRDSTKIKWSR 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 1329 SLKQQLAGNKIISFNASRIMKSLYRPFHVQFAYFHQPVNDMVYqlPKLFPTPHHDNMTILLAGPYPNIAGHCFSTKVLPD 1408
Cdd:pfam18135 59 ALKGDLERGKKLSFDEPKIVRILYRPFDKQWLYYDPRLIDRPR--PELFPHLDDDNLVIVVSGQGSGKGFSALVTDLIPD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 1409 LNVL--TASQNFPRWTWEpvetpegeldfgmgasegsepgTEGEILDGYRRVDNVTDEILGIYREA-LGSNVTKDDIFYF 1485
Cdd:pfam18135 137 LHLFsgGGGQVFPLYRYP----------------------ETTPNLAPGERRDNITDELLAKFREAyGGATVTKEDIFYY 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 1486 VYGQLHDPGYREKYAADLKKMLPHIETPTLRARFDQLTAAGRELMDLHVNYEDVEPWPVTVDVKASADENdretwRVQKM 1565
Cdd:pfam18135 195 IYAVLHSPEYRERYAEDLKKDFPRIPLTADFELFWELVELGRELADLHLNYERVAPLPPGITTYPPDGDY-----RVEKM 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 1566 KWAKKKdpstgknvnDVTTLVYNKSVTVRDIPAEADEYMLGSRSALAWIIDRYQVKKDKASGIVNDPNDWADeVGNPRYI 1645
Cdd:pfam18135 270 KYDKKK---------DKGTIIINGEGTFTGVPPEAWEYVVGGKSALEWLKDRYGVKLDKDSGILNDPNDWAK-LDETEEI 339
|
...
gi 1092649119 1646 VDL 1648
Cdd:pfam18135 340 LDL 342
|
|
| LlaBIII_nuclease-like |
cd22333 |
nuclease domain of type ISB restriction-modification enzyme LlaBIII and similar nuclease ... |
4-160 |
6.28e-53 |
|
nuclease domain of type ISB restriction-modification enzyme LlaBIII and similar nuclease domains; This N-terminal nuclease domain belongs to a superfamily of PDDEXK nucleases including very short patch repair (Vsr) endonucleases, archaeal Holliday junction resolvases, MutH methyl-directed DNA mismatch-repair endonucleases, and catalytic domains of many restriction endonucleases, such as EcoRI, BamHI, and FokI.
Pssm-ID: 411737 Cd Length: 149 Bit Score: 182.35 E-value: 6.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 4 FSDVLDQLRK--NQPQGKyGIAFEKLMVNYFRNDPTLSEEYEDVGRFVDWKYYDGQSDTGIDLVARRReDGRWVAIQCKF 81
Cdd:cd22333 1 FDDLLDQLRKlsKSERDK-GTRFERLMKAYLLTDPTYADQFSEVWLWNEWPGRAGGKDTGIDLVAKTR-DGELWAIQCKF 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092649119 82 YEPTAYLQKSHLDSFFEKSGRSFdtehgkdsFAQRIIISTTDRWSKNAEEMLDNQLIPTNRIGTASIAESPIDWDITFP 160
Cdd:cd22333 79 YDPDHTISKADIDSFLSASGKKP--------FTHRLIVSTTDKWSSNAEEALENQSKPVTRIGLSDLENSPIDWSKFDK 149
|
|
| Mrr_cat_2 |
pfam13156 |
Restriction endonuclease; Prokaryotic family found in type II restriction enzymes containing ... |
33-165 |
5.90e-49 |
|
Restriction endonuclease; Prokaryotic family found in type II restriction enzymes containing the hallmark (D/E)-(D/E)XK active site. Presence of catalytic residues implicates this region in the enzymatic cleavage of DNA
Pssm-ID: 433001 Cd Length: 127 Bit Score: 170.15 E-value: 5.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 33 RNDPTLSEEYEDVGRFVDWKYYDGQS--DTGIDLVARRREDGRWVAIQCKFYEPTAYLQKSHLDSFFEKSGrsfdtehgK 110
Cdd:pfam13156 1 KTDPLYADEFDDVWLWKEWPTRKGLGghDTGIDLVARTRDTGEYWAIQCKFYDPDHKIQKPDIDSFFSASG--------K 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1092649119 111 DSFAQRIIISTTDRWSKNAEEMLDNQLIPTNRIGTASIAESPIDWDITFPGSDIA 165
Cdd:pfam13156 73 SPFTDRLIISTTDKWSKNAEEALANQTIPVSRIGLADLAESPIDWSKLSPGAEGE 127
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
174-760 |
7.42e-48 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 181.38 E-value: 7.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 174 YQPRPHQDEAIAKAIAGFE-AHDRGKLIMACGTGKTFTALRLAERFaelnGNKARVLFLVPSISLLSQTlkewtaqsqth 252
Cdd:COG1061 79 FELRPYQQEALEALLAALErGGGRGLVVAPTGTGKTVLALALAAEL----LRGKRVLVLVPRRELLEQW----------- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 253 lplkpyavcsdqkvskkAEDIASYDLDVPVStngadiklrteQGKRRQGLNVIFSTYQSIEAIHEAQELGmDDFDLVICD 332
Cdd:COG1061 144 -----------------AEELRRFLGDPLAG-----------GGKKDSDAPITVATYQSLARRAHLDELG-DRFGLVIID 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 333 EAHRTTgvtlagedASNFVKIHDenYIKASKRLYMTATPrlfddnvkgkaeehsaelASMDDEDIYGPEF----YRLGFG 408
Cdd:COG1061 195 EAHHAG--------APSYRRILE--AFPAAYRLGLTATP------------------FRSDGREILLFLFdgivYEYSLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 409 EAVDKGLLTDYKVLVMTVEEDiaaDVLAAYPTNEINLTTASAMIGAWNGLAKRSGAEQDTKSgfeagaqpmRRTVAFAKD 488
Cdd:COG1061 247 EAIEDGYLAPPEYYGIRVDLT---DERAEYDALSERLREALAADAERKDKILRELLREHPDD---------RKTLVFCSS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 489 IKASKTIQETFPtlirqyqeqlkdhaatndvsllniDLQVAVEHVDGTMNALERGNKISWLEssipEDETRILTNARCLS 568
Cdd:COG1061 315 VDHAEALAELLN------------------------EAGIRAAVVTGDTPKKEREEILEAFR----DGELRILVTVDVLN 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 569 EGVDVPALDSVIFFHPRNSMVDVVQSVGRVMRKAEGKDYGYIILpvAIPPGVSPSQALNDNTRFRVVWQI-LNALRAHDD 647
Cdd:COG1061 367 EGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKEDALVYD--FVGNDVPVLEELAKDLRDLAGYRVeFLDEEESEE 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 648 RFNAKVNSIALNEKVELPIDIESVKKTKRDEEQTNEDKAKEAKAKLDASDATPASQSESSGEQELTPEQMTLFSLEAWQE 727
Cdd:COG1061 445 LALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLL 524
|
570 580 590
....*....|....*....|....*....|...
gi 1092649119 728 AMYVKLVDKVGTRTYWEDWADDVATIAEAQIAR 760
Cdd:COG1061 525 KLLLLLLLLLLLELLELLAALLRLEELAALLLK 557
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
174-371 |
2.41e-31 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 121.24 E-value: 2.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 174 YQPRPHQDEAIAKAIAGFEAHD-RGKLIMACGTGKTFTALRLAERFAElNGNKARVLFLVPSISLLSQTLKEWtaqsqth 252
Cdd:pfam04851 2 LELRPYQIEAIENLLESIKNGQkRGLIVMATGSGKTLTAAKLIARLFK-KGPIKKVLFLVPRKDLLEQALEEF------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 253 lplKPYAVCSDQKVSKKAEDiasydldvpvstngadiKLRTEQGKRRqglnVIFSTYQSI--EAIHEAQELGMDDFDLVI 330
Cdd:pfam04851 74 ---KKFLPNYVEIGEIISGD-----------------KKDESVDDNK----IVVTTIQSLykALELASLELLPDFFDVII 129
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1092649119 331 CDEAHRTTgvtlagedASNFVKIhdENYIKASKRLYMTATP 371
Cdd:pfam04851 130 IDEAHRSG--------ASSYRNI--LEYFKPAFLLGLTATP 160
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
176-371 |
1.28e-28 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 112.78 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 176 PRPHQDEAIaKAIAGFEAHDRGKLIMACGTGKTFTALRLAERFAELngnkaRVLFLVPSISLLSQTlkewtaqsqthlpl 255
Cdd:cd17926 1 LRPYQEEAL-EAWLAHKNNRRGILVLPTGSGKTLTALALIAYLKEL-----RTLIVVPTDALLDQW-------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 256 kpyavcsdqkvskkAEDIASYDLDVPVSTNGADIKlrteqgKRRQGLNVIFSTYQSIEAIHEAQELGMDDFDLVICDEAH 335
Cdd:cd17926 61 --------------KERFEDFLGDSSIGLIGGGKK------KDFDDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAH 120
|
170 180 190
....*....|....*....|....*....|....*.
gi 1092649119 336 RTTgvtlagedASNFVKIHDEnyIKASKRLYMTATP 371
Cdd:cd17926 121 HLP--------AKTFSEILKE--LNAKYRLGLTATP 146
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
176-376 |
8.50e-26 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350790 [Multi-domain] Cd Length: 163 Bit Score: 105.34 E-value: 8.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 176 PRPHQDEAIAKAIAGFEA-HDRGKLIMACGTGKTFTALRLAERFAELNGNKaRVLFLVPSISLLSQTLKEwtaqSQTHLP 254
Cdd:cd18032 1 PRYYQQEAIEALEEAREKgQRRALLVMATGTGKTYTAAFLIKRLLEANRKK-RILFLAHREELLEQAERS----FKEVLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 255 lkpyavcsdqkvskkaeDIASYDLDVpvstngadiklrteQGKRRQGLNVIFSTYQSIEAIHEAQELGMDDFDLVICDEA 334
Cdd:cd18032 76 -----------------DGSFGNLKG--------------GKKKPDDARVVFATVQTLNKRKRLEKFPPDYFDLIIIDEA 124
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1092649119 335 HRTTgvtlagedASNFVKIHDenYIKASKRLYMTATPRLFDD 376
Cdd:cd18032 125 HHAI--------ASSYRKILE--YFEPAFLLGLTATPERTDG 156
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
168-377 |
3.88e-21 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 93.33 E-value: 3.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 168 LTRKEVYQPRPHQDEAIAKAIAGFEahdRGKLIMACGTGKTFTALRLAERFAeLNGNKARVLFLVPSISLLSQTLKEWta 247
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPTRELAEQWAEEL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 248 qsqthlplkpyavcsdqkvskkaEDIASYDLDVPVSTNGADIKLRTEQGKRRQGLNVIFSTYQSIEAIHEAQELGMDDFD 327
Cdd:smart00487 75 -----------------------KKLGPSLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVD 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1092649119 328 LVICDEAHRTTGVTlAGEDASNFVKIHdenyIKASKRLYMTATPRLFDDN 377
Cdd:smart00487 132 LVILDEAHRLLDGG-FGDQLEKLLKLL----PKNVQLLLLSATPPEEIEN 176
|
|
| HsdR |
COG4096 |
Type I site-specific restriction endonuclease, part of a restriction-modification system ... |
176-611 |
1.41e-18 |
|
Type I site-specific restriction endonuclease, part of a restriction-modification system [Defense mechanisms];
Pssm-ID: 443272 [Multi-domain] Cd Length: 806 Bit Score: 92.21 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 176 PRPHQDEAIAKAIAGFEAHDRGKLI-MACGTGKTFTALRLAERFaeLNGNKA-RVLFLVPSISLLSQTLKEWtaqsQTHL 253
Cdd:COG4096 159 LRYYQIEAIRRVEEAIAKGQRRALLvMATGTGKTRTAIALIYRL--LKAGRAkRILFLADRNALVDQAKNAF----KPFL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 254 PlkpyavcSDQKVSKkaedIASYDLDVPVSTngadiklrteqgkrrqglNVIFSTYQSI-------EAIHEAQELGMDDF 326
Cdd:COG4096 233 P-------DLDAFTK----LYNKSKDIDKSA------------------RVYFSTYQTMmnridgeEEEPGYRQFPPDFF 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 327 DLVICDEAHRttGVtlagedASNFVKIHDenYIKASKrLYMTATPRLFDDNvkgkaeeHSAELasmddediygpeF---- 402
Cdd:COG4096 284 DLIIIDECHR--GI------YSKWRAILD--YFDALQ-IGLTATPKDTIDR-------NTYEY------------Fngnp 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 403 -YRLGFGEAVDKGLLTDYKVLVMT-----------------------VEEDIAADVLaAYPTNEIN--LTTAS---AMIG 453
Cdd:COG4096 334 vYTYSLEQAVADGFLVPYKVIRIDtkfdregirydagedlsdeegeeIELEELEEDR-EYEAKDFNrkVVNEDttrKVLE 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 454 AWnglakrsgaeqdTKSGFEAGAQPMRRTVAFAKDIKASKTIQETFptliRQYQEQLKDHAA---TNDVsllnidlqvav 530
Cdd:COG4096 413 EL------------MEYLDKPGGDRLGKTIIFAKNDDHADRIVQAL----RELYPELGGDFVkkiTGDD----------- 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 531 ehvdgtmnalERGNkiSWLES-SIPEDETRILTNARCLSEGVDVPALDSVIFFHPRNSMVDVVQSVGRVMRKAE----GK 605
Cdd:COG4096 466 ----------DYGK--SLIDNfKNPEKYPRIAVTVDMLDTGIDVPEVVNLVFMRPVKSRIKFEQMIGRGTRLCPdlfpGK 533
|
....*.
gi 1092649119 606 DYGYII 611
Cdd:COG4096 534 THFTIF 539
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
174-397 |
4.51e-13 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 69.77 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 174 YQPRPHQDEAIAKAIagfeahdRGKLIMAC---GTGKTFTALRLAERFAE--LNGNKARVLFLVPSISLLSQTLKEWtaq 248
Cdd:cd17927 1 FKPRNYQLELAQPAL-------KGKNTIIClptGSGKTFVAVLICEHHLKkfPAGRKGKVVFLANKVPLVEQQKEVF--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 249 sQTHLPLKPYAVcsdQKVSkkaediasydldvpvstngADIKLRTEQGKRRQGLNVIFSTYQSIE-AIHEAQELGMDDFD 327
Cdd:cd17927 71 -RKHFERPGYKV---TGLS-------------------GDTSENVSVEQIVESSDVIIVTPQILVnDLKSGTIVSLSDFS 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092649119 328 LVICDEAHRTTGVTLAGEDASNFVKIHDENYIKASKRLYMTATPRLFDDNVKGKAEEHSAEL-ASMDDEDI 397
Cdd:cd17927 128 LLVFDECHNTTKNHPYNEIMFRYLDQKLGSSGPLPQILGLTASPGVGGAKNTEEALEHICKLcANLDISVI 198
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
560-614 |
1.01e-11 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The 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: 350172 [Multi-domain] Cd Length: 77 Bit Score: 61.95 E-value: 1.01e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1092649119 560 ILTNARCLSEGVDVPALDSVIFFHPRNSMVDVVQSVGRVMRKaeGKDYGYIILPV 614
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRG--GKDEGEVILFV 77
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
174-339 |
1.20e-11 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 65.75 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 174 YQPRPHQDEAiakaiagFEAHDRGKLI--MACGTGKTFTALRLAERFAELNG----NKARVLFLVPSISLLSQtlkewta 247
Cdd:cd18034 1 FTPRSYQLEL-------FEAALKRNTIvvLPTGSGKTLIAVMLIKEMGELNRkeknPKKRAVFLVPTVPLVAQ------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 248 QS---QTHLPLKPYAVCSDQKVSKKA-----EDIASYdlDVPVSTngADIKlrteqgkrrqgLNVIFSTYqsieaiheaq 319
Cdd:cd18034 67 QAeaiRSHTDLKVGEYSGEMGVDKWTkerwkEELEKY--DVLVMT--AQIL-----------LDALRHGF---------- 121
|
170 180
....*....|....*....|
gi 1092649119 320 eLGMDDFDLVICDEAHRTTG 339
Cdd:cd18034 122 -LSLSDINLLIFDECHHATG 140
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
199-370 |
2.75e-11 |
|
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: 63.19 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 199 LIMACGTGKTFTALRLAERFAELNGnkARVLFLVPSISLLSQTLKEwtaqsqthlpLKPYavcsdqkvskkaediasYDL 278
Cdd:cd00046 6 ITAPTGSGKTLAALLAALLLLLKKG--KKVLVLVPTKALALQTAER----------LREL-----------------FGP 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 279 DVPVSTNGADIKLRTEQGKRRQGLNVIFSTYQSIE-AIHEAQELGMDDFDLVICDEAHRttgvTLAGEDASNFVKIHDEN 357
Cdd:cd00046 57 GIRVAVLVGGSSAEEREKNKLGDADIIIATPDMLLnLLLREDRLFLKDLKLIIVDEAHA----LLIDSRGALILDLAVRK 132
|
170
....*....|....
gi 1092649119 358 YI-KASKRLYMTAT 370
Cdd:cd00046 133 AGlKNAQVILLSAT 146
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
479-611 |
1.34e-10 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. 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: 350186 [Multi-domain] Cd Length: 116 Bit Score: 60.27 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 479 MRRTVAFAKDIKASKTIQETFPTLIRQYQEQLKDHA--ATNDvsllnidlqvavehvdgtmNALERGNKIswlessipED 556
Cdd:cd18799 6 EIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSdrERGD-------------------EALILLFFG--------EL 58
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1092649119 557 ETRILTNARCLSEGVDVPALDSVIFFHPRNSMVDVVQSVGRVMRKAEGKDYGYII 611
Cdd:cd18799 59 KPPILVTVDLLTTGVDIPEVDNVVFLRPTESRTLFLQMLGRGLRLHEGKDFFTIL 113
|
|
| HsdM |
COG0286 |
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms]; |
871-1127 |
1.56e-10 |
|
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
Pssm-ID: 440055 [Multi-domain] Cd Length: 243 Bit Score: 63.28 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 871 VIKDLYERFFRKAFKKQSEALGIVYTPVEIVDFILRSADQisrwhfgkgltDEGVHILDPFTGTGTFMV----RLLQSGL 946
Cdd:COG0286 2 VLGDAYEYLLRKFAEESGKKAGEFYTPREVVRLMVELLDP-----------KPGETVYDPACGSGGFLVeaaeYLKEHGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 947 IEPEDLArkyaceLHATEIMLLAYYVAAVNIettynALQaeraqrdGEPEPgyvpfdGIALADTFqiheEGDIPDLKVFk 1026
Cdd:COG0286 71 DERKKLS------LYGQEINPTTYRLAKMNL-----LLH-------GIGDP------NIELGDTL----SNDGDELEKF- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 1027 ennaaiqrqidapiNVIIGNPPYSAKqtSANDDNANLKYPTLDSRIESTfaanstaTNKNSLYdsYLRAFRWsidrLGTH 1106
Cdd:COG0286 122 --------------DVVLANPPFGGK--WKKEELKDDLLGRFGYGLPPK-------SNADLLF--LQHILSL----LKPG 172
|
250 260
....*....|....*....|.
gi 1092649119 1107 GVLAFVSNGGWIDSNTADGVR 1127
Cdd:COG0286 173 GRAAVVLPDGVLFRGAEKEIR 193
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
176-424 |
5.13e-10 |
|
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350769 [Multi-domain] Cd Length: 207 Bit Score: 61.15 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 176 PRPHQDEAIAKAIAgfeaHDRGKLIMA--CGTGKTFTALRLAeRFAELNGNKARVLFLVPSiSLLSQtlkeWTAQSQTHL 253
Cdd:cd18011 1 PLPHQIDAVLRALR----KPPVRLLLAdeVGLGKTIEAGLII-KELLLRGDAKRVLILCPA-SLVEQ----WQDELQDKF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 254 PLKPYAVcSDQKVSKKAEDIASYDLDVPVSTNGADikLRTEQGKRRQGLNVIfstyqsieaiheaqelgmdDFDLVICDE 333
Cdd:cd18011 71 GLPFLIL-DRETAAQLRRLIGNPFEEFPIVIVSLD--LLKRSEERRGLLLSE-------------------EWDLVVVDE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 334 AHRttgvtLAGEDASNFVKIHD--ENYIKASKR-LYMTATPrlfddnVKGKAEEHSAELASMDdediygPEFYRLGFGEA 410
Cdd:cd18011 129 AHK-----LRNSGGGKETKRYKlgRLLAKRARHvLLLTATP------HNGKEEDFRALLSLLD------PGRFAVLGRFL 191
|
250
....*....|....
gi 1092649119 411 VDKGLLTDYKVLVM 424
Cdd:cd18011 192 RLDGLREVLAKVLL 205
|
|
| uvsW |
PHA02558 |
UvsW helicase; Provisional |
175-606 |
2.07e-09 |
|
UvsW helicase; Provisional
Pssm-ID: 222875 [Multi-domain] Cd Length: 501 Bit Score: 61.95 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 175 QPRPHQDEAIAKAIAgfeaHDRGKLIMACGTGKTFTALRLAERFaeLNGNKARVLFLVPSISLLSQTLKewtaqsqthlp 254
Cdd:PHA02558 114 EPHWYQYDAVYEGLK----NNRRLLNLPTSAGKSLIQYLLSRYY--LENYEGKVLIIVPTTSLVTQMID----------- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 255 lkpyavcsdqkvskkaeDIASYDLDVpvstNGADIKLRTeqGKRRQG-LNVIFSTYQSIeaIHEAQELgMDDFDLVICDE 333
Cdd:PHA02558 177 -----------------DFVDYRLFP----REAMHKIYS--GTAKDTdAPIVVSTWQSA--VKQPKEW-FDQFGMVIVDE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 334 AHRTTGVTLagedaSNFVKihdeNYIKASKRLYMTATPRlfddnvKGKAeehsaelASMDDEDIYGPEFYRLGFGEAVDK 413
Cdd:PHA02558 231 CHLFTGKSL-----TSIIT----KLDNCKFKFGLTGSLR------DGKA-------NILQYVGLFGDIFKPVTTSQLMEE 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 414 GLLTDYKVLVMTV---EEDIAADVLAAYpTNEINLTTASAMIGAW-----NGLAKRSGaeqdtksgfeagaqpmrRTVAF 485
Cdd:PHA02558 289 GQVTDLKINSIFLrypDEDRVKLKGEDY-QEEIKYITSHTKRNKWianlaLKLAKKGE-----------------NTFVM 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 486 AKDIKASKTIQETfptLIRQYQEqlkdhaatndvsllnidlqvaVEHVDGTMNALERgNKISwlesSIPEDETRILTNAR 565
Cdd:PHA02558 351 FKYVEHGKPLYEM---LKKVYDK---------------------VYYVSGEVDTEDR-NEMK----KIAEGGKGIIIVAS 401
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1092649119 566 --CLSEGVDVPALDSVIFFHPRNSMVDVVQSVGRVMRKAEGKD 606
Cdd:PHA02558 402 ygVFSTGISIKNLHHVIFAHPSKSKIIVLQSIGRVLRKHGSKS 444
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
175-375 |
3.49e-08 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 58.31 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 175 QPRPHQDEAIAKAIAGFEAHDRGKLIMACGTGKTFTAL-RLAERFAElnGNKARVLFLVPSiSLLSQtlkeWTAQSQTHL 253
Cdd:COG0553 241 TLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALaLLLELKER--GLARPVLIVAPT-SLVGN----WQRELAKFA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 254 P-LKPYAVCSDQKVSKKAEDIASYDLdvpvstngadiklrteqgkrrqglnVIfSTY----QSIEAIHEAqelgmdDFDL 328
Cdd:COG0553 314 PgLRVLVLDGTRERAKGANPFEDADL-------------------------VI-TSYgllrRDIELLAAV------DWDL 361
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1092649119 329 VICDEAHR----TTGVTLAGEDasnfvkihdenyIKASKRLYMTATP---RLFD 375
Cdd:COG0553 362 VILDEAQHiknpATKRAKAVRA------------LKARHRLALTGTPvenRLEE 403
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
177-336 |
7.26e-08 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 53.79 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 177 RPHQDEAIAKAIAGfeaHDrgklIMAC---GTGKTFTALRLAERFAELNGNKARVLFLVPSISLLSQTLKEWTaqsqthl 253
Cdd:pfam00270 1 TPIQAEAIPAILEG---RD----VLVQaptGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELK------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 254 plkpyavcsdqkvskkaEDIASYDLDVPVSTNGADIKlrtEQGKRRQGLNVIFSTYQSIeAIHEAQELGMDDFDLVICDE 333
Cdd:pfam00270 67 -----------------KLGKGLGLKVASLLGGDSRK---EQLEKLKGPDILVGTPGRL-LDLLQERKLLKNLKLLVLDE 125
|
...
gi 1092649119 334 AHR 336
Cdd:pfam00270 126 AHR 128
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
177-419 |
1.61e-07 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 56.50 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 177 RPHQDEAIA---KAIAgfeahdRGK----LIMACGTGKTFTAL----RL--AERFaelngnkARVLFLVPSISLLSQTLK 243
Cdd:PRK11448 415 RYYQEDAIQaveKAIV------EGQreilLAMATGTGKTRTAIalmyRLlkAKRF-------RRILFLVDRSALGEQAED 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 244 EwtaqsqthlpLKPYAVCSDQKVS-----KKAEDIASYDldvpvSTNgadIKLRTEQG--KRrqglnvifsTYQSIEaih 316
Cdd:PRK11448 482 A----------FKDTKIEGDQTFAsiydiKGLEDKFPED-----ETK---VHVATVQGmvKR---------ILYSDD--- 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 317 EAQELGMDDFDLVICDEAHRttGVTLAGEDASNFVKIHDEN-YIKASKRL--Y-------MTATPRLfddnvkgkaeeHS 386
Cdd:PRK11448 532 PMDKPPVDQYDCIIVDEAHR--GYTLDKEMSEGELQFRDQLdYVSKYRRVldYfdavkigLTATPAL-----------HT 598
|
250 260 270
....*....|....*....|....*....|...
gi 1092649119 387 AElasmddedIYGPEFYRLGFGEAVDKGLLTDY 419
Cdd:PRK11448 599 TE--------IFGEPVYTYSYREAVIDGYLIDH 623
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
204-371 |
2.88e-07 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 55.51 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 204 GTGKTFTALRL-AERFAELNGnkaRVLFLVPSISLLSQ---TLKEwtaqsqtHLPLKPyavcsdqkvskkaEDIASYDLD 279
Cdd:COG1111 27 GLGKTAVALLViAERLHKKGG---KVLFLAPTKPLVEQhaeFFKE-------ALNIPE-------------DEIVVFTGE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 280 VPVstngADIKLRTEQGKrrqglnVIFSTYQSIEAIHEAQELGMDDFDLVICDEAHRTTgvtlaGEDASNFVKIHDENYI 359
Cdd:COG1111 84 VSP----EKRKELWEKAR------IIVATPQVIENDLIAGRIDLDDVSLLIFDEAHRAV-----GNYAYVYIAERYHEDA 148
|
170
....*....|..
gi 1092649119 360 KASKRLYMTATP 371
Cdd:COG1111 149 KDPLILGMTASP 160
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
526-601 |
3.21e-07 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 49.52 E-value: 3.21e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092649119 526 LQVAVEHVDGTMNALERgnkiSWLESSIPEDETRILTNARCLSEGVDVPALDSVIFFHPRNSMVDVVQSVGRVMRK 601
Cdd:smart00490 10 LGIKVARLHGGLSQEER----EEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRA 81
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
518-600 |
3.52e-07 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 50.29 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 518 DVSLLNIDLQVAVEHVDGTMNALERgnkiSWLESSIPEDETRILTNARCLSEGVDVPALDSVIFFHPRNSMVDVVQSVGR 597
Cdd:pfam00271 29 EAELLLEKEGIKVARLHGDLSQEER----EEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGR 104
|
...
gi 1092649119 598 VMR 600
Cdd:pfam00271 105 AGR 107
|
|
| DEXHc_RE_I_HsdR |
cd18030 |
DEXH-box helicase domain of type I restriction enzyme HdsR subunit; The HdsR motor subunit of ... |
176-343 |
3.72e-07 |
|
DEXH-box helicase domain of type I restriction enzyme HdsR subunit; The HdsR motor subunit of type I restriction-modification enzymes contains the DNA cleavage and ATP-dependent DNA translocation activities of the heteromeric complex. It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350788 [Multi-domain] Cd Length: 208 Bit Score: 52.61 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 176 PRPHQDEAIAKA---IAGFEAHD---RGKLIM-ACGTGKTFTALRLAERFAELNGNkARVLFLVPSISLLSQTLKEWTAq 248
Cdd:cd18030 22 ARYYQYYAVEAAlerIKTATNKDgdkKGGYIWhTQGSGKSLTMFKAAKLLIEDPKN-PKVVFVVDRKDLDYQTSSTFSR- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 249 sqthlplkpyavCSDQKVsKKAEDIAS-YDLdvpvstngadikLRTEQGKrrqglnVIFSTYQSIEAI---HEAQELGMD 324
Cdd:cd18030 100 ------------FAAEDV-VRANSTKElKEL------------LKNLSGG------IIVTTIQKFNNAvkeESKPVLIYR 148
|
170
....*....|....*....
gi 1092649119 325 DFDLVICDEAHRTTGVTLA 343
Cdd:cd18030 149 KNIVVIVDEAHRSQFGELA 167
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
176-397 |
2.04e-06 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 50.17 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 176 PRPHQDEAIAKAIagfeahdRGKLIMAC---GTGKTFTALRLAERFAE---LNGNKARVLFLVPSISLLSQTLKEWTaqs 249
Cdd:cd18036 3 LRNYQLELVLPAL-------RGKNTIICaptGSGKTRVAVYICRHHLEkrrSAGEKGRVVVLVNKVPLVEQQLEKFF--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 250 qthlplkpyavcsdqKVSKKAEDIASYDLDVPVSTNGADIKLRTeqgkrrqglNVIFSTYQ----SIEAIHEAQELGMDD 325
Cdd:cd18036 73 ---------------KYFRKGYKVTGLSGDSSHKVSFGQIVKAS---------DVIICTPQilinNLLSGREEERVYLSD 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092649119 326 FDLVICDEAHRTtgvtlAGEDASNFVKIHDENYIKASKR-----LYMTATPRLFDDNVKGKAEEHSAEL-ASMDDEDI 397
Cdd:cd18036 129 FSLLIFDECHHT-----QKEHPYNKIMRMYLDKKLSSQGplpqiLGLTASPGVGGARSFEEALEHILKLcANLDASVI 201
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
175-371 |
5.08e-06 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 48.66 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 175 QPRPHQDEAIAKAIAGfeahdRGKLIMACGTGKTFTALRLAErfAELNGNKARVLFLVPSISLLSQtlKEWTAQSQTHLP 254
Cdd:cd18035 2 ERRLYQVLIAAVALNG-----NTLIVLPTGLGKTIIAILVAA--DRLTKKGGKVLILAPSRPLVEQ--HAENLKRVLNIP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 255 LKPYAVCSDQKVSKKAEdiasydldvpvstngadiklRTEQGKrrqglnVIFSTYQSIEAIHEAQELGMDDFDLVICDEA 334
Cdd:cd18035 73 DKITSLTGEVKPEERAE--------------------RWDASK------IIVATPQVIENDLLAGRITLDDVSLLIFDEA 126
|
170 180 190
....*....|....*....|....*....|....*..
gi 1092649119 335 HRTTGVTLAGEDASNFVKIHDENYIkaskrLYMTATP 371
Cdd:cd18035 127 HHAVGNYAYVYIAHRYKREANNPLI-----LGLTASP 158
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
178-335 |
1.21e-05 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong 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: 350679 [Multi-domain] Cd Length: 181 Bit Score: 47.64 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 178 PHQDEAIAkaiagfEAHDRGKLIMAC---GTGKTFTALRLAerFAELNGNKARVLFLVPSISLLSQTLKEWTaqsqthlp 254
Cdd:cd17921 4 PIQREALR------ALYLSGDSVLVSaptSSGKTLIAELAI--LRALATSGGKAVYIAPTRALVNQKEADLR-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 255 lkpyavcsdqkvskkaEDIASYDLDVPVSTNGADIKLRTEQGKRrqglnVIFSTYQSIEAI-HEAQELGMDDFDLVICDE 333
Cdd:cd17921 68 ----------------ERFGPLGKNVGLLTGDPSVNKLLLAEAD-----ILVATPEKLDLLlRNGGERLIQDVRLVVVDE 126
|
..
gi 1092649119 334 AH 335
Cdd:cd17921 127 AH 128
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
176-371 |
1.43e-05 |
|
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350677 [Multi-domain] Cd Length: 182 Bit Score: 47.56 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 176 PRPHQDEAIAKAIAGFEAHDRGKLIMACGTGKTFTALRLAERFAELNGNKARVLFLVPSiSLLSQtlkeWTAQSQTHLPl 255
Cdd:cd17919 1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPL-SVLEN----WEREFEKWTP- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 256 kpyavcsdqkvskkaediasyDLDVPVST-NGADIKLRTEQGKRRQGlNVIFSTYQSIEAihEAQELGMDDFDLVICDEA 334
Cdd:cd17919 75 ---------------------DLRVVVYHgSQRERAQIRAKEKLDKF-DVVLTTYETLRR--DKASLRKFRWDLVVVDEA 130
|
170 180 190
....*....|....*....|....*....|....*..
gi 1092649119 335 HRttgvtLAGEDASNFVKIHDenyIKASKRLYMTATP 371
Cdd:cd17919 131 HR-----LKNPKSQLSKALKA---LRAKRRLLLTGTP 159
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
168-371 |
1.45e-03 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 43.32 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 168 LTRKEVYQPRPHQdEAIAKaiagfEAHDRGKLI-MACGTGKTFTA-LRLAERFAELNGnkaRVLFLVPSISLLSQ---TL 242
Cdd:PRK13766 8 LIKPNTIEARLYQ-QLLAA-----TALKKNTLVvLPTGLGKTAIAlLVIAERLHKKGG---KVLILAPTKPLVEQhaeFF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 243 KEwtaqsqtHLPLKPyavcsdqkvskkaEDIASYDLDVPvstnGADIKLRTEQGKrrqglnVIFSTYQSIEAIHEAQELG 322
Cdd:PRK13766 79 RK-------FLNIPE-------------EKIVVFTGEVS----PEKRAELWEKAK------VIVATPQVIENDLIAGRIS 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1092649119 323 MDDFDLVICDEAHRTTgvtlaGEDASNFVKihdENYIKASKR---LYMTATP 371
Cdd:PRK13766 129 LEDVSLLIFDEAHRAV-----GNYAYVYIA---ERYHEDAKNplvLGLTASP 172
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
569-607 |
2.99e-03 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. 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: 350188 [Multi-domain] Cd Length: 143 Bit Score: 39.65 E-value: 2.99e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1092649119 569 EGVDVPALDSVIFFHPRNSMVDVVQSVGRVMRKAEGKDY 607
Cdd:cd18801 102 EGLDIGEVDLIICYDASPSPIRMIQRMGRTGRKRQGRVV 140
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
174-240 |
6.31e-03 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 41.06 E-value: 6.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092649119 174 YQPRPHQDE---AIAKAIAgfeahDRGKLIM--ACGTGKTFT----ALRLAERfaelngNKARVLFLVPSISLLSQ 240
Cdd:COG1199 13 FEPRPGQREmaeAVARALA-----EGRHLLIeaGTGTGKTLAylvpALLAARE------TGKKVVISTATKALQEQ 77
|
|
| N6_Mtase |
pfam02384 |
N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against ... |
874-1082 |
9.09e-03 |
|
N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The R-M system is a complex containing three polypeptides: M (this family), S (pfam01420), and R. This family consists of N-6 adenine-specific DNA methylase EC:2.1.1.72 from Type I and Type IC restriction systems. These methylases have the same sequence specificity as their corresponding restriction enzymes.
Pssm-ID: 426749 [Multi-domain] Cd Length: 310 Bit Score: 40.00 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 874 DLYERFFRK-AFKKQSEAlGIVYTPVEIVDFILRSADqisrwhfgkglTDEGVHILDPFTGTGTFmvrLLQsgliepedl 952
Cdd:pfam02384 7 DAYEYLLRKfAPNAGKSG-GEFFTPREVSKLIVELLD-----------PKPGESIYDPACGSGGF---LIQ--------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092649119 953 ARKYACElHATEIMLLAYYVAAVNiETTYNALQAERAQRDGEpepgyVPFDGIALADTFQIHEEGDIPdlkvfkennaai 1032
Cdd:pfam02384 63 AEKFVKE-HDGDTNDLSIYGQEKN-PTTYRLARMNMILHGIE-----YDDFHIRHGDTLTSPKFEDDK------------ 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1092649119 1033 qrqidaPINVIIGNPPYSAKqtsaNDDNANLKyPTLDSRIESTFAANSTA 1082
Cdd:pfam02384 124 ------KFDVVVANPPFSDK----WDANDTLE-NDPRFRPAYGVAPKSNA 162
|
|
| |
