|
Name |
Accession |
Description |
Interval |
E-value |
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
255-1035 |
0e+00 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 729.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 255 SIEELLNEIASESSYEGQIVqeALHTYPAVEAQYGALSRPLSQELINALyTSRNIEKTYKHQADAINHLWNGFHVIVSTS 334
Cdd:COG1205 3 RLEELLERLRASPRYGDQIV--HVRTIPAREARYAPWPDWLPPELRAAL-KKRGIERLYSHQAEAIEAARAGKNVVIATP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 335 TSSGKSLIYQIPILQSLLEDNQSTAFFVFPTKSLAQDQKKSLIDILSYMPTlkNIRVDTFDGDTPLESRESIIRSANIIF 414
Cdd:COG1205 80 TASGKSLAYLLPVLEALLEDPGATALYLYPTKALARDQLRRLRELAEALGL--GVRVATYDGDTPPEERRWIREHPDIVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 415 TNPDMLHQTILPNANRWYYFFKNLKLFVLDEAHVYNGIFGVHVAFVLRRMRRIAEYFGnSQYRFVSCSATIEDPLQHMKK 494
Cdd:COG1205 158 TNPDMLHYGLLPHHTRWARFFRNLRYVVIDEAHTYRGVFGSHVANVLRRLRRICRHYG-SDPQFILASATIGNPAEHAER 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 495 IFGVDnIKLINYTSSPSGSKKFVMWNPPYVDpkhpDDGKKSAISEASKLLIKFAEKRVRTIVFCRVRKTCESLMRLVRQE 574
Cdd:COG1205 237 LTGRP-VTVVDEDGSPRGERTFVLWNPPLVD----DGIRRSALAEAARLLADLVREGLRTLVFTRSRRGAELLARYARRA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 575 LktkQKGDLLSKIQSYRAGYTVQERRKIESEMFNGKLYGIIATNALELGIDIGSLDAVITIGFPYSLSNLRQQFGRAGRR 654
Cdd:COG1205 312 L---REPDLADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 655 NKSSLAVYIVETFPVDQFYLKHPILIHTQPNAELTLDLTNEVLLASHLQCAAYELPInIRSDEKFFGNQIQDICEanlEM 734
Cdd:COG1205 389 GQDSLVVLVAGDDPLDQYYVRHPEELFERPPEAAVIDPDNPYVLAPHLLCAAAELPL-TEGDLELFGPEARELLD---AL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 735 VEESY---RPHPKYL---PFPASQVRIRSVSEDMFTLVDVTNDKnvILELLEPFRVALTAYEGAVYVYQGKTFIIRLLNI 808
Cdd:COG1205 465 VEEGLlrrRGDGWYWtgdDRPARDVSLRGAGGENVVIVDATTGR--VIGTVDLPRALRELHPGAIYLHQGETYRVEELDL 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 809 NKRIITAHQVDVEWSTLQRDFTDVDPVRSLMKKTmHGSTNIYFGAVKATLHVFGYFKVN-KQKDILDVVDITDHPVEIDS 887
Cdd:COG1205 543 EERKAYVRPVDVDYYTRALSETDIRILEVLEERE-LGGVTVHFGEVEVTEQVTGYKKRRlYTGEVLGEVPLDLPPRTLRT 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 888 RGFWIDVPWHIIEVLSLKKINGAASIHAAQHALLSLMPIFISNSGNDIrteckAGekeYKEAKSERRRPSRLIFYDNC-G 966
Cdd:COG1205 622 KAVWLTIPPDLLEAAGLDPEDFPGALHAAEHALIGLLPLFALCDRWDI-----GG---VSTPLHPDTGAPTIFIYDGYpG 693
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63054629 967 dssGAGLCNKAYEHTDELITMAIERIESCDCKvrEGCPGCITSSKfeggvCSG--EVLDKVGALILLKMLL 1035
Cdd:COG1205 694 ---GVGLAERGYERFEELLEATRDLIASCPCE--DGCPSCVQSPK-----CGNgnEPLDKAAALRLLEALL 754
|
|
| DECH_helic |
TIGR03817 |
helicase/secretion neighborhood putative DEAH-box helicase; A conserved gene neighborhood ... |
302-1035 |
2.85e-161 |
|
helicase/secretion neighborhood putative DEAH-box helicase; A conserved gene neighborhood widely spread in the Actinobacteria contains this uncharacterized DEAH-box family helicase encoded convergently towards an operon of genes for protein homologous to type II secretion and pilus formation proteins. The context suggests that this helicase may play a role in conjugal transfer of DNA.
Pssm-ID: 274800 [Multi-domain] Cd Length: 742 Bit Score: 494.64 E-value: 2.85e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 302 ALYTSRNIEKTYKHQADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSLLEDNQSTAFFVFPTKSLAQDQKKSLIDIls 381
Cdd:TIGR03817 27 AALEAAGIHRPWQHQARAAELAHAGRHVVVATGTASGKSLAYQLPVLSALADDPRATALYLAPTKALAADQLRAVREL-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 382 ympTLKNIRVDTFDGDTPLESRESIIRSANIIFTNPDMLHQTILPNANRWYYFFKNLKLFVLDEAHVYNGIFGVHVAFVL 461
Cdd:TIGR03817 105 ---TLRGVRPATYDGDTPTEERRWAREHARYVLTNPDMLHRGILPSHARWARFLRRLRYVVIDECHSYRGVFGSHVALVL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 462 RRMRRIAEYFGnSQYRFVSCSATIEDPLQHMKKIFGVDnIKLINYTSSPSGSKKFVMWNPPYVDPKHPDDGK--KSAISE 539
Cdd:TIGR03817 182 RRLRRLCARYG-ASPVFVLASATTADPAAAASRLIGAP-VVAVTEDGSPRGARTVALWEPPLTELTGENGAPvrRSASAE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 540 ASKLLIKFAEKRVRTIVFCRVRKTCESLMRLVRQELkTKQKGDLLSKIQSYRAGYTVQERRKIESEMFNGKLYGIIATNA 619
Cdd:TIGR03817 260 AADLLADLVAEGARTLTFVRSRRGAELVAAIARRLL-GEVDPDLAERVAAYRAGYLPEDRRELERALRDGELLGVATTNA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 620 LELGIDIGSLDAVITIGFPYSLSNLRQQFGRAGRRNKSSLAVYIVETFPVDQFYLKHPILIHTQPNAELTLDLTNEVLLA 699
Cdd:TIGR03817 339 LELGVDISGLDAVVIAGFPGTRASLWQQAGRAGRRGQGALVVLVARDDPLDTYLVHHPEALFDRPVEATVFDPDNPYVLG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 700 SHLQCAAYELPINiRSDEKFFGNQIQDICEAnleMVEESY---RP---HPKYLPFPASQVRIRSVSEDMFTLVDVTNDKn 773
Cdd:TIGR03817 419 PHLCCAAAELPLT-EADLELFGPAAAEVLDQ---LVEQGLlrrRPagwFWTRRERAHDAVDIRGGGGAPVAIVEAETGR- 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 774 vILELLEPFRVALTAYEGAVYVYQGKTFIIRLLNINKRIITAHQVDVEWSTLQRDFTDVDPVRSLmKKTMHGSTNIYFGA 853
Cdd:TIGR03817 494 -LLGTVDAGAAHSTVHPGAVYLHQGESYVVDELDLEDGVALVHAEDPDYTTFARETTDISVVEER-RRRAWGDVRVALGE 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 854 VKATLHVFGYF-KVNKQKDILDVVDITDHPVEIDSRGFWIDVPWHIIEVLSLKKINGAASIHAAQHALLSLMPIFISNSG 932
Cdd:TIGR03817 572 VEVTSQVVGYLrRRLITGEVLDEVPLDLPPRTLRTRAVWYTVTPELLDDAGIDAADVPGALHAAEHAAIGLLPLVATCDR 651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 933 NDIRTECKAgekeykeAKSERRRPSrlIF-YDncGDSSGAGLCNKAYEHTDELITMAIERIESCDCKvrEGCPGCITSSK 1011
Cdd:TIGR03817 652 WDIGGVSTA-------VHPDTGLPT--VFvYD--GHPGGAGFAERGFAKAREWLAATRDAIASCECE--SGCPSCVQSPK 718
|
730 740
....*....|....*....|....
gi 63054629 1012 FEGGvcsGEVLDKVGALILLKMLL 1035
Cdd:TIGR03817 719 CGNG---NDPLDKAGAARLLAAVL 739
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
313-495 |
2.10e-94 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 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: 350681 [Multi-domain] Cd Length: 182 Bit Score: 297.57 E-value: 2.10e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 313 YKHQADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSLLEDNQSTAFFVFPTKSLAQDQKKSLIDILSYMptLKNIRVD 392
Cdd:cd17923 2 YSHQAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGSRALYLYPTKALAQDQLRSLRELLEQL--GLGIRVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 393 TFDGDTPLESRESIIRS-ANIIFTNPDMLHQTILPNANRWYYFFKNLKLFVLDEAHVYNGIFGVHVAFVLRRMRRIAEyF 471
Cdd:cd17923 80 TYDGDTPREERRAIIRNpPRILLTNPDMLHYALLPHHDRWARFLRNLRYVVLDEAHTYRGVFGSHVALLLRRLRRLCR-R 158
|
170 180
....*....|....*....|....
gi 63054629 472 GNSQYRFVSCSATIEDPLQHMKKI 495
Cdd:cd17923 159 YGADPQFILTSATIGNPAEHARTL 182
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
516-664 |
1.33e-71 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases 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: 350184 [Multi-domain] Cd Length: 146 Bit Score: 234.07 E-value: 1.33e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 516 FVMWNPPYVDPKHPDDGkkSAISEASKLLIKFAEKRVRTIVFCRVRKTCESLMRLVRQELKTKQKgdLLSKIQSYRAGYT 595
Cdd:cd18797 2 FVLWNPPLLDRKDGERG--SARREAARLFADLVRAGVKTIVFCRSRKLAELLLRYLKARLVEEGP--LASKVASYRAGYL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054629 596 VQERRKIESEMFNGKLYGIIATNALELGIDIGSLDAVITIGFPYSLSNLRQQFGRAGRRNKSSLAVYIV 664
Cdd:cd18797 78 AEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVILVA 146
|
|
| CDT1 |
smart01075 |
DNA replication factor CDT1 like; CDT1 is a component of the replication licensing system and ... |
51-222 |
2.07e-34 |
|
DNA replication factor CDT1 like; CDT1 is a component of the replication licensing system and promotes the loading of the mini-chromosome maintenance complex onto chromatin. Geminin is an inhibitor of CDT1 and prevents inappropriate re-initiation of replication on an already fired origin. This region of CDT1 binds to Geminin.
Pssm-ID: 215014 Cd Length: 164 Bit Score: 129.44 E-value: 2.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 51 IPSIFDNLFNLFKVINTTYTFLYLRNSlTITFPLLNSSVKQSLKKELTIGDLSQLREICPQIIELNYKslaslaleinKN 130
Cdd:smart01075 1 LPEKYEVLAEMFKGLDTIVAMLLNRNE-TPTFAKLKPGVQNLTRKRFSEDHLAQIKHIYPEAIEFKQE----------KN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 131 VYTdlnpelyTGSTVSQsSEYVLVIELLETQERSSKRRRREgpTMKANIQRQKLDFNNLKKAIELRNQKFLQGIKEYIKK 210
Cdd:smart01075 70 VKT-------FGSGTKV-STYQLTIEPNLEDEDRSKVRPSL--NASRLLERRKVFRRKLVKIVKEHHQEFLASLNPNIPK 139
|
170
....*....|..
gi 63054629 211 CQLTELDPTQQL 222
Cdd:smart01075 140 DKLTRWHPRFNL 151
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
313-490 |
1.78e-31 |
|
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: 121.20 E-value: 1.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 313 YKHQADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSL-LEDNQSTAFFVFPTKSLAQDQKKSLIDILSYMptlkNIRV 391
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALdKLDNGPQALVLAPTRELAEQIYEELKKLGKGL----GLKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 392 DTFDGDTPLESRESIIRSANIIFTNPDMLHqTILPNANRwyyfFKNLKLFVLDEAHVYNGI-FGVHVAFVLRRMRriaey 470
Cdd:pfam00270 77 ASLLGGDSRKEQLEKLKGPDILVGTPGRLL-DLLQERKL----LKNLKLLVLDEAHRLLDMgFGPDLEEILRRLP----- 146
|
170 180
....*....|....*....|
gi 63054629 471 fgnSQYRFVSCSATIEDPLQ 490
Cdd:pfam00270 147 ---KKRQILLLSATLPRNLE 163
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
326-484 |
1.22e-24 |
|
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: 100.94 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 326 GFHVIVSTSTSSGKSLIYQIPILQsLLEDNQSTAFFVFPTKSLAQDQKKSLIDILSymptlKNIRVDTFDGDTPLESRES 405
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALL-LLLKKGKKVLVLVPTKALALQTAERLRELFG-----PGIRVAVLVGGSSAEEREK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 406 -IIRSANIIFTNPDMLHQTILPNanrWYYFFKNLKLFVLDEAHVYNGIFgvhvaFVLRRMRRIAEYFGNSQYRFVSCSAT 484
Cdd:cd00046 75 nKLGDADIIIATPDMLLNLLLRE---DRLFLKDLKLIIVDEAHALLIDS-----RGALILDLAVRKAGLKNAQVILLSAT 146
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
307-504 |
2.01e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 102.18 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 307 RNIEKTYKHQADAINHLWNGF-HVIVSTSTSSGKSLIYQIPILQSLLEDNQSTAFFVFPTKSLAQDQKKSLIDILSYMPt 385
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLG- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 386 lkNIRVDTFDGDTPLESRESIIRS-ANIIFTNPDMLHQtilpNANRWYYFFKNLKLFVLDEAHVY-NGIFGVHVAFVLRR 463
Cdd:smart00487 83 --LKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLD----LLENDKLSLSNVDLVILDEAHRLlDGGFGDQLEKLLKL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 63054629 464 MRRIAeyfgnsqyRFVSCSATIEDPLQHMKKIFGVDNIKLI 504
Cdd:smart00487 157 LPKNV--------QLLLLSATPPEEIENLLELFLNDPVFID 189
|
|
| MZB |
pfam09369 |
MrfA Zn-binding domain; This is the C-terminal MrfA Zn+2-binding domain (MZB, also referred to ... |
916-1007 |
1.04e-22 |
|
MrfA Zn-binding domain; This is the C-terminal MrfA Zn+2-binding domain (MZB, also referred to as DUF1998) which contains a conserved four-cysteine signature motif. These four Cys reside in a short coil between two alpha-helices and form a metal ion-binding site. This domain is frequently found at the C-terminal of ndNTPases, however, it is also found encoded in a standalone gene, downstream of putative helicase domain-encoding genes associated with bacterial anti-phage defense system DISARM. MrfA (Mitomycin repair factor A, also known as YprA in Bacillus subtilis) is a DNA helicase that supports repair of mitomycin C-induced DNA damage. MrfA homologs are widely distributed in bacteria and are also present in archaea, fungi and plants. The MrfA-homolog in yeast, Hrq1, also reduces mitomycin C sensitivity. Hrq1 has high similarity to human RecQ4 and was therefore assigned to the RecQ-like helicase family. MrfA homologs appear to be missing in Enterobacteria, however, certain pathogenic Escherichia coli and Salmonella strains harbour Z5898-like helicases with this domain.
Pssm-ID: 462776 [Multi-domain] Cd Length: 78 Bit Score: 92.64 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 916 AQHALLSLMPIFISNSGNDIRTECKAGEKeykeakserrRPSRLIFYDNCGDssGAGLCNKAYEHTDELITMAIERIESC 995
Cdd:pfam09369 1 LEHALISALPLFLGCDRSDIGGESYPPDT----------GRPRILIYDAYPG--GAGLAEKAFELLGELLEAALERLESC 68
|
90
....*....|..
gi 63054629 996 DCKvrEGCPGCI 1007
Cdd:pfam09369 69 DCE--AGCPSCL 78
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
295-702 |
1.57e-20 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 96.50 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 295 LSQELINALYTSRNIEKTYKHQADAI-NHLWNGFHVIVSTSTSSGKSLIYQIPILQSLLedNQSTAFFVFPTKSLAQDQK 373
Cdd:COG1204 6 LPLEKVIEFLKERGIEELYPPQAEALeAGLLEGKNLVVSAPTASGKTLIAELAILKALL--NGGKALYIVPLRALASEKY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 374 KSLIDILSymptLKNIRVDTFDGDtpLESRESIIRSANIIFTNPDMLHQTILPNANrwyyFFKNLKLFVLDEAH-VYNGI 452
Cdd:COG1204 84 REFKRDFE----ELGIKVGVSTGD--YDSDDEWLGRYDILVATPEKLDSLLRNGPS----WLRDVDLVVVDEAHlIDDES 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 453 FGVHVAFVLRRMRRIaeyfgNSQYRFVSCSATIEDPlQHMKKIFGVDNIKlINYtsSPSGSKKFVMwnppYVDPKHPDDG 532
Cdd:COG1204 154 RGPTLEVLLARLRRL-----NPEAQIVALSATIGNA-EEIAEWLDAELVK-SDW--RPVPLNEGVL----YDGVLRFDDG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 533 KKSAISEASKLLIKFAEKRVRTIVFCRVRKTCESLMRLVRQELK-------TKQKGDLLSKIQSYR-------------- 591
Cdd:COG1204 221 SRRSKDPTLALALDLLEEGGQVLVFVSSRRDAESLAKKLADELKrrltpeeREELEELAEELLEVSeethtnekladcle 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 592 -------AGYTVQERRKIESEMFNGKLYGIIATNALELGID-------IGSldavITIGFPYSLSNL--RQQFGRAGRRN 655
Cdd:COG1204 301 kgvafhhAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNlparrviIRD----TKRGGMVPIPVLefKQMAGRAGRPG 376
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 63054629 656 KSS--LAVYIVETFPVDQFYLKHPILihtQPNAELTLDLTNEVLLASHL 702
Cdd:COG1204 377 YDPygEAILVAKSSDEADELFERYIL---GEPEPIRSKLANESALRTHL 422
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
316-654 |
2.09e-19 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 94.18 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 316 QADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSLLE-------DNQSTAFFVFPTKSLAQDQKKSLI-------DILS 381
Cdd:PRK13767 37 QRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELFRlgregelEDKVYCLYVSPLRALNNDIHRNLEeplteirEIAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 382 YM-PTLKNIRVDTFDGDTPLESRESIIR-SANIIFTNPDMLhqTILPNANRWYYFFKNLKLFVLDEAH-VYNGIFGVHVA 458
Cdd:PRK13767 117 ERgEELPEIRVAIRTGDTSSYEKQKMLKkPPHILITTPESL--AILLNSPKFREKLRTVKWVIVDEIHsLAENKRGVHLS 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 459 FVLRRMRRIAEyfgnSQYRFVSCSATIEdPLQHMKKIFG-------------VD-------NIKLINytsspsgskkfvm 518
Cdd:PRK13767 195 LSLERLEELAG----GEFVRIGLSATIE-PLEEVAKFLVgyeddgeprdceiVDarfvkpfDIKVIS------------- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 519 wnpPYVDPKHPDDGKksaISEA-SKLLIKFAEKRVRTIVFCRVRKTCESLMRLVRQELKTKQKGDL-------LSKiqsy 590
Cdd:PRK13767 257 ---PVDDLIHTPAEE---ISEAlYETLHELIKEHRTTLIFTNTRSGAERVLYNLRKRFPEEYDEDNigahhssLSR---- 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054629 591 ragytvQERRKIESEMFNGKLYGIIATNALELGIDIGSLDAVITIGFPYSLSNLRQQFGRAGRR 654
Cdd:PRK13767 327 ------EVRLEVEEKLKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAGHR 384
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
315-654 |
4.63e-19 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 93.24 E-value: 4.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 315 HQADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSLLEDNQSTAF-------FVFPTKSLAQDQKKSLIDILSYM---- 383
Cdd:COG1201 28 PQREAWPAIAAGESTLLIAPTGSGKTLAAFLPALDELARRPRPGELpdglrvlYISPLKALANDIERNLRAPLEEIgeaa 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 384 -PTLKNIRVDTFDGDTPLESRESIIRS-ANIIFTNPDMLHqtILPNANRWYYFFKNLKLFVLDEAH-VYNGIFGVHVAFV 460
Cdd:COG1201 108 gLPLPEIRVGVRTGDTPASERQRQRRRpPHILITTPESLA--LLLTSPDARELLRGVRTVIVDEIHaLAGSKRGVHLALS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 461 LRRMRRIAEyfgnSQYRFVSCSATIEDPLQHMKKIFGVDNI---KLINytssPSGSKKFVmwnppyVDPKHPDDGKKSAI 537
Cdd:COG1201 186 LERLRALAP----RPLQRIGLSATVGPLEEVARFLVGYEDPrpvTIVD----AGAGKKPD------LEVLVPVEDLIERF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 538 SEASKLLIKFAEK---RVR----TIVFCRVRKTCEslmRLVrQELKtKQKGDL----------LSKiqsyragytvQERR 600
Cdd:COG1201 252 PWAGHLWPHLYPRvldLIEahrtTLVFTNTRSQAE---RLF-QRLN-ELNPEDalpiaahhgsLSR----------EQRL 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 63054629 601 KIESEMFNGKLYGIIATNALELGIDIGSLDAVITIGFPYSLSNLRQQFGRAGRR 654
Cdd:COG1201 317 EVEEALKAGELRAVVATSSLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAGHR 370
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
524-665 |
3.00e-17 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases 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: 350183 [Multi-domain] Cd Length: 150 Bit Score: 79.62 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 524 VDPKHPDDGKKSAISEASKLLIKFAEKRvRTIVFCRVRKTCESLMRLVRQ-------ELKTKQKGDLLSKiqsyragytv 596
Cdd:cd18796 12 VAPEIFPWAGESGADAYAEVIFLLERHK-STLVFTNTRSQAERLAQRLRElcpdrvpPDFIALHHGSLSR---------- 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 597 QERRKIESEMFNGKLYGIIATNALELGIDIGSLDAVITIGFPYSLSNLRQQFGRAGRRNKS-SLAVYIVE 665
Cdd:cd18796 81 ELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPGAaSKGRLVPT 150
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
313-488 |
4.42e-16 |
|
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: 77.30 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 313 YKHQADAINHLWN-GFHVIVSTSTSSGKSLIYQIPILQSLLEDNQsTAFFVFPTKSLAQDQKKSLIDILSYMPtlknIRV 391
Cdd:cd17921 3 NPIQREALRALYLsGDSVLVSAPTSSGKTLIAELAILRALATSGG-KAVYIAPTRALVNQKEADLRERFGPLG----KNV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 392 DTFDGDTPLESREsiIRSANIIFTNPDMLHQTILPNANRWyyfFKNLKLFVLDEAH-VYNGIFGVHVAFVLRRMRRIaey 470
Cdd:cd17921 78 GLLTGDPSVNKLL--LAEADILVATPEKLDLLLRNGGERL---IQDVRLVVVDEAHlIGDGERGVVLELLLSRLLRI--- 149
|
170
....*....|....*...
gi 63054629 471 fgNSQYRFVSCSATIEDP 488
Cdd:cd17921 150 --NKNARFVGLSATLPNA 165
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
326-488 |
6.62e-15 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from 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: 350680 [Multi-domain] Cd Length: 166 Bit Score: 73.39 E-value: 6.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 326 GFHVIVSTSTSSGKSLIYQIPILQSLLEDNQST--AFFVFPTKSLAQDQKKSLIDILSYMptLKNIRVDTFDGDTPLESR 403
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGvqVLYISPLKALINDQERRLEEPLDEI--DLEIPVAVRHGDTSQSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 404 ESIIRSA-NIIFTNPDMLHqTILPNANRWYYfFKNLKLFVLDEAH-VYNGIFGVHVAFVLRRMRRIAEyfgnSQYRFVSC 481
Cdd:cd17922 79 AKQLKNPpGILITTPESLE-LLLVNKKLREL-FAGLRYVVVDEIHaLLGSKRGVQLELLLERLRKLTG----RPLRRIGL 152
|
....*..
gi 63054629 482 SATIEDP 488
Cdd:cd17922 153 SATLGNL 159
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
335-652 |
2.09e-14 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 78.43 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 335 TSSGKSL---IYQIPILQSLLEDNQSTA--------FFVFPTKSLAQDQKKSL-IDILSYMPTLK-------NIRVDTFD 395
Cdd:PRK09751 5 TGSGKTLaafLYALDRLFREGGEDTREAhkrktsriLYISPIKALGTDVQRNLqIPLKGIADERRrrgetevNLRVGIRT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 396 GDTPLESRESIIRSA-NIIFTNPDMLHQTILPNANRwyyFFKNLKLFVLDEAHVYNGI-FGVHVAFVLRRMRRIAEyfgn 473
Cdd:PRK09751 85 GDTPAQERSKLTRNPpDILITTPESLYLMLTSRARE---TLRGVETVIIDEVHAVAGSkRGAHLALSLERLDALLH---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 474 SQYRFVSCSATIEdPLQHMKKIFGVDN-IKLINYTSSPSGSKKFV-----MWNPPYVDPKHPDD---GKKSAI---SEAS 541
Cdd:PRK09751 158 TSAQRIGLSATVR-SASDVAAFLGGDRpVTVVNPPAMRHPQIRIVvpvanMDDVSSVASGTGEDshaGREGSIwpyIETG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 542 kLLIKFAEKRvRTIVFCRVRKTCESLM---------RLVRQE---------------LKTKQKGDLLSKIQSYRAGYTVQ 597
Cdd:PRK09751 237 -ILDEVLRHR-STIVFTNSRGLAEKLTarlnelyaaRLQRSPsiavdaahfestsgaTSNRVQSSDVFIARSHHGSVSKE 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 63054629 598 ERRKIESEMFNGKLYGIIATNALELGIDIGSLDAVITIGFPYSLSNLRQQFGRAG 652
Cdd:PRK09751 315 QRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
553-655 |
4.06e-13 |
|
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: 66.47 E-value: 4.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 553 RTIVFCRVRKTCESlmrlvrQELKTKQKgdllSKIQSYRAGYTVQERRKIESEMFNGKLYGIIATNALELGIDIGSLDAV 632
Cdd:pfam00271 17 KVLIFSQTKKTLEA------ELLLEKEG----IKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLV 86
|
90 100
....*....|....*....|...
gi 63054629 633 ITIGFPYSLSNLRQQFGRAGRRN 655
Cdd:pfam00271 87 INYDLPWNPASYIQRIGRAGRAG 109
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
586-655 |
6.27e-13 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 64.93 E-value: 6.27e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 586 KIQSYRAGYTVQERRKIESEMFNGKLYGIIATNALELGIDIGSLDAVITIGFPYSLSNLRQQFGRAGRRN 655
Cdd:smart00490 13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
316-448 |
9.29e-13 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 68.33 E-value: 9.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 316 QADAINHLWNGFHVIVSTSTSSGKSLIYQIPilqSLLEDnqSTAFFVFPTKSLAQDQKKSLidilsympTLKNIRVDTFD 395
Cdd:cd17920 17 QLEAINAVLAGRDVLVVMPTGGGKSLCYQLP---ALLLD--GVTLVVSPLISLMQDQVDRL--------QQLGIRAAALN 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 63054629 396 GDTPLESRESIIR-----SANIIFTNPDML-HQTILPNANRWyYFFKNLKLFVLDEAHV 448
Cdd:cd17920 84 STLSPEEKREVLLrikngQYKLLYVTPERLlSPDFLELLQRL-PERKRLALIVVDEAHC 141
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
313-653 |
1.80e-12 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 71.45 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 313 YKHQADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSLLEDNQStaFFVFPTKSLAQDQKKSLIDILSYmptlkNIRVD 392
Cdd:PRK01172 24 YDHQRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETFLAGLKS--IYIVPLRSLAMEKYEELSRLRSL-----GMRVK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 393 TFDGDtpLESRESIIRSANIIFTNPD----MLHQTilPnanrwyYFFKNLKLFVLDEAHVYNGIF-GVHVAFVLRRMRRI 467
Cdd:PRK01172 97 ISIGD--YDDPPDFIKRYDVVILTSEkadsLIHHD--P------YIINDVGLIVADEIHIIGDEDrGPTLETVLSSARYV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 468 aeyfgNSQYRFVSCSATIEDPLQHMKKIfgvdNIKLINYTSSPSGSKKFVMwnppYVDPKHPDDGKKSAISEASkLLIKF 547
Cdd:PRK01172 167 -----NPDARILALSATVSNANELAQWL----NASLIKSNFRPVPLKLGIL----YRKRLILDGYERSQVDINS-LIKET 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 548 AEKRVRTIVFCRVRKTCESLMRLVRQEL-----------KTKQKGDLLSK-----IQSYRAGYTVQERRKIESEMFNGKL 611
Cdd:PRK01172 233 VNDGGQVLVFVSSRKNAEDYAEMLIQHFpefndfkvsseNNNVYDDSLNEmlphgVAFHHAGLSNEQRRFIEEMFRNRYI 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 63054629 612 YGIIATNALELGIDIGSLDAVITIGFPYS------LSNL--RQQFGRAGR 653
Cdd:PRK01172 313 KVIVATPTLAAGVNLPARLVIVRDITRYGnggiryLSNMeiKQMIGRAGR 362
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
316-661 |
9.69e-12 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 68.63 E-value: 9.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 316 QADAINHLWNGFHVIVSTSTSSGKSLIYQIPilqSLLEDNqsTAFFVFPTKSLAQDQKKSLidilsympTLKNIRVDTFD 395
Cdd:COG0514 22 QEEIIEAVLAGRDALVVMPTGGGKSLCYQLP---ALLLPG--LTLVVSPLIALMKDQVDAL--------RAAGIRAAFLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 396 GDTPLESRESIIRSAN-----IIFTNPDMLhqtilpNANRWYYFFKNLK--LFVLDEAH-V----------Yngifgvhv 457
Cdd:COG0514 89 SSLSAEERREVLRALRagelkLLYVAPERL------LNPRFLELLRRLKisLFAIDEAHcIsqwghdfrpdY-------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 458 afvlRRMRRIAEYFGNsqyrfVSCSAT-----------------IEDPLQHmkkIFGVD--NIKLinytsspsgskkfvm 518
Cdd:COG0514 155 ----RRLGELRERLPN-----VPVLALtatatprvradiaeqlgLEDPRVF---VGSFDrpNLRL--------------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 519 wnppYVDPKHPDDGKKsaiseaskLLIKFAEKRVR--TIVFCRVRKTCESLM-RLVRQELKTKqkgdllskiqSYRAGYT 595
Cdd:COG0514 208 ----EVVPKPPDDKLA--------QLLDFLKEHPGgsGIVYCLSRKKVEELAeWLREAGIRAA----------AYHAGLD 265
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054629 596 VQERRKIEsEMF-NGKLYGIIATNALELGIDIGSLDAVITIGFPYSLSNLRQQFGRAGRRNKSSLAV 661
Cdd:COG0514 266 AEEREANQ-DRFlRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEAL 331
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
298-653 |
1.17e-11 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 69.08 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 298 ELINALYTSRNIEKTYKHQADAI-NHLWNGFHVIVSTSTSSGKSLIYQIPILQSLLEDNQSTAFFVfPTKSLAQDQKKSL 376
Cdd:PRK00254 10 ERIKRVLKERGIEELYPPQAEALkSGVLEGKNLVLAIPTASGKTLVAEIVMVNKLLREGGKAVYLV-PLKALAEEKYREF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 377 IDILSYmptlkNIRVDTFDGDtpLESRESIIRSANIIFTNPDMLhQTILPNANRWyyfFKNLKLFVLDEAHVYNGI-FGV 455
Cdd:PRK00254 89 KDWEKL-----GLRVAMTTGD--YDSTDEWLGKYDIIIATAEKF-DSLLRHGSSW---IKDVKLVVADEIHLIGSYdRGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 456 HVAFVLRRMrriaeyFGNSQyrFVSCSATIEDPLQHMKKIfgvdNIKLINYTSSPSGSKK------FVMWnppyvdpkhp 529
Cdd:PRK00254 158 TLEMILTHM------LGRAQ--ILGLSATVGNAEELAEWL----NAELVVSDWRPVKLRKgvfyqgFLFW---------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 530 DDGKKSAISEASKLLIKFAEKRVR-TIVFCRVRKTCE----SLMRLVR--------QELKT------------KQKGDLL 584
Cdd:PRK00254 216 EDGKIERFPNSWESLVYDAVKKGKgALVFVNTRRSAEkealELAKKIKrfltkpelRALKEladsleenptneKLKKALR 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054629 585 SKIQSYRAGYTVQERRKIESEMFNGKLYGIIATNALELGIDIGSLDAVITIGFPYS--------LSNLRQQFGRAGR 653
Cdd:PRK00254 296 GGVAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYSnfgwedipVLEIQQMMGRAGR 372
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
316-485 |
5.85e-11 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 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: 350781 [Multi-domain] Cd Length: 206 Bit Score: 63.14 E-value: 5.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 316 QADAINHLWNG-FHVIVSTSTSSGKSLIYQIPILQSLLEDNQST-----AFFVFPTKSLAQDQKKSLIDILSYMptlkNI 389
Cdd:cd18023 6 QSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLKERNPLPwgnrkVVYIAPIKALCSEKYDDWKEKFGPL----GL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 390 RVDTFDGDTPLESRESIiRSANIIFTNP---DMLHQTILPNANrwyyFFKNLKLFVLDEAHVYNGIFGVHVAFVLRRMRR 466
Cdd:cd18023 82 SCAELTGDTEMDDTFEI-QDADIILTTPekwDSMTRRWRDNGN----LVQLVALVLIDEVHIIKENRGATLEVVVSRMKT 156
|
170 180
....*....|....*....|....
gi 63054629 467 IAEYFGNSQY-----RFVSCSATI 485
Cdd:cd18023 157 LSSSSELRGStvrpmRFVAVSATI 180
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
553-653 |
1.65e-10 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They 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: 350181 [Multi-domain] Cd Length: 134 Bit Score: 59.91 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 553 RTIVFCRVRKTCESL-MRLVRQELKTKqkgdllskiqSYRAGYTVQERRKIESEMFNGKLYGIIATNALELGIDIGSLDA 631
Cdd:cd18794 32 SGIIYCLSRKECEQVaARLQSKGISAA----------AYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRF 101
|
90 100
....*....|....*....|..
gi 63054629 632 VITIGFPYSLSNLRQQFGRAGR 653
Cdd:cd18794 102 VIHYSLPKSMESYYQESGRAGR 123
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
295-446 |
2.46e-08 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350804 [Multi-domain] Cd Length: 201 Bit Score: 55.14 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 295 LSQELINALYtSRNIEKTYKHQADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSL-LEDNQSTAFFVFPTKSLAQDQK 373
Cdd:cd18046 6 LKESLLRGIY-AYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIdTSLKATQALVLAPTRELAQQIQ 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054629 374 KSLIDILSYMptlkNIRVDTFDGDTPLESRESIIRSA-NIIFTNPDMLHQTIlpnaNRWYYFFKNLKLFVLDEA 446
Cdd:cd18046 85 KVVMALGDYM----GIKCHACIGGTSVRDDAQKLQAGpHIVVGTPGRVFDMI----NRRYLRTDYIKMFVLDEA 150
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
294-446 |
2.60e-08 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350697 [Multi-domain] Cd Length: 199 Bit Score: 55.02 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 294 PLSQELINALYtSRNIEKTYKHQADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSL-LEDNQSTAFFVFPTKSLAQDQ 372
Cdd:cd17939 3 GLSEDLLRGIY-AYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIdTTVRETQALVLAPTRELAQQI 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054629 373 KKSLIDILSYMptlkNIRVDTFDGDTPL-ESRESIIRSANIIFTNP----DMLhqtilpnaNRWYYFFKNLKLFVLDEA 446
Cdd:cd17939 82 QKVVKALGDYM----GVKVHACIGGTSVrEDRRKLQYGPHIVVGTPgrvfDML--------QRRSLRTDKIKMFVLDEA 148
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
313-792 |
1.04e-07 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 55.80 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 313 YKHQADAINHLWNGFH------VIVSTsTSSGKSLIyQIPILQSLLEDnQSTAFFVfPTKSLAQDQKKSLIDILsymptl 386
Cdd:COG1061 82 RPYQQEALEALLAALErgggrgLVVAP-TGTGKTVL-ALALAAELLRG-KRVLVLV-PRRELLEQWAEELRRFL------ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 387 knirvdtfdgDTPLESRESIIRSANIIFTNpdmlHQTILPNANRWYyFFKNLKLFVLDEAHvyngifgvHVAfvLRRMRR 466
Cdd:COG1061 152 ----------GDPLAGGGKKDSDAPITVAT----YQSLARRAHLDE-LGDRFGLVIIDEAH--------HAG--APSYRR 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 467 IAEYFgNSQYRfVSCSATIE-------DPLQHMKKIFGVDNIKLIN--YTSSPSGSKKFVMWNPPYVDPKHPDDGKKSAI 537
Cdd:COG1061 207 ILEAF-PAAYR-LGLTATPFrsdgreiLLFLFDGIVYEYSLKEAIEdgYLAPPEYYGIRVDLTDERAEYDALSERLREAL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 538 SEAS--------KLLIKFAEKRvRTIVFCRVRKTCESLMRLVRQELKtkqkgdllsKIQSYRAGYTVQERRKIESEMFNG 609
Cdd:COG1061 285 AADAerkdkilrELLREHPDDR-KTLVFCSSVDHAEALAELLNEAGI---------RAAVVTGDTPKKEREEILEAFRDG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 610 KLYGIIATNALELGIDIGSLDAVITIGFPYSLSNLRQQFGRA--GRRNKSSLAVYIVETFPVDQFY-----LKHPILIHT 682
Cdd:COG1061 355 ELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGlrPAPGKEDALVYDFVGNDVPVLEelakdLRDLAGYRV 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 683 QPNAELTLDLTNEVLLASHLQCAAYELPINIRSDEKFFGNQIQDICEANLEMVEESYRPHPKYLPFPASQVRIRSVSEDM 762
Cdd:COG1061 435 EFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKEL 514
|
490 500 510
....*....|....*....|....*....|
gi 63054629 763 FTLVDVTNDKNVILELLEPFRVALTAYEGA 792
Cdd:COG1061 515 LLLLALAKLLKLLLLLLLLLLLELLELLAA 544
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
316-488 |
1.32e-07 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type 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: 350786 [Multi-domain] Cd Length: 177 Bit Score: 52.72 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 316 QADAINH-LWNGFHVIVSTSTSSGKSLIYQIPILQSLLEDNqsTAFFVFPTKSLAQDQKKSLIDIlsYMPTLK-NIRVDT 393
Cdd:cd18028 6 QAEAVRAgLLKGENLLISIPTASGKTLIAEMAMVNTLLEGG--KALYLVPLRALASEKYEEFKKL--EEIGLKvGISTGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 394 FDgdtpleSRESIIRSANIIFTNPDMLhQTILPNANRWyyfFKNLKLFVLDEAHVYNGIF-GVHVAFVLRRMRRIaeyFG 472
Cdd:cd18028 82 YD------EDDEWLGDYDIIVATYEKF-DSLLRHSPSW---LRDVGVVVVDEIHLISDEErGPTLESIVARLRRL---NP 148
|
170
....*....|....*.
gi 63054629 473 NSQyrFVSCSATIEDP 488
Cdd:cd18028 149 NTQ--IIGLSATIGNP 162
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
295-446 |
7.99e-07 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350722 [Multi-domain] Cd Length: 211 Bit Score: 51.04 E-value: 7.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 295 LSQELINALyTSRNIEKTYKHQADAINHLWNGFH-VIVSTSTSSGKSLIYQIPILQSLLEDNQST------AFFVFPTKS 367
Cdd:cd17964 1 LDPSLLKAL-TRMGFETMTPVQQKTLKPILSTGDdVLARAKTGTGKTLAFLLPAIQSLLNTKPAGrrsgvsALIISPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 368 LAQDQKKSLIDILSYmptLKNIRVDTFDGDTPL-ESRESIIRSA-NIIFTNP----DMLhqtilpNANRWYYFFKNLKLF 441
Cdd:cd17964 80 LALQIAAEAKKLLQG---LRKLRVQSAVGGTSRrAELNRLRRGRpDILVATPgrliDHL------ENPGVAKAFTDLDYL 150
|
....*
gi 63054629 442 VLDEA 446
Cdd:cd17964 151 VLDEA 155
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
294-447 |
8.92e-07 |
|
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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: 350773 [Multi-domain] Cd Length: 209 Bit Score: 50.83 E-value: 8.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 294 PLSQELINALYTSRNIEKTYKHQADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSllednQSTAFFVFPTKSLAQDQK 373
Cdd:cd18015 1 PWSGKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCS-----DGFTLVVSPLISLMEDQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 374 KSL--IDILSYMPT-------LKNIRVDTFDGDTPLEsresiirsanIIFTNPDMLHQT-ILPNANRWYYFFKNLKLFVL 443
Cdd:cd18015 76 MALkkLGISATMLNassskehVKWVHAALTDKNSELK----------LLYVTPEKIAKSkRFMSKLEKAYNAGRLARIAI 145
|
....
gi 63054629 444 DEAH 447
Cdd:cd18015 146 DEVH 149
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
316-446 |
1.03e-06 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 50.52 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 316 QADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSLLEDNQSTAFFVF-----PTKSLAQDQKKSLIDILSYMptlkNIR 390
Cdd:cd00268 17 QAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGPQalvlaPTRELAMQIAEVARKLGKGT----GLK 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63054629 391 VDTFDGDTPLESRESIIRS-ANIIFTNP----DMLHQTILpnanrwyyFFKNLKLFVLDEA 446
Cdd:cd00268 93 VAAIYGGAPIKKQIEALKKgPDIVVGTPgrllDLIERGKL--------DLSNVKYLVLDEA 145
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
549-664 |
1.46e-06 |
|
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: 46.93 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 549 EKRVRTIVFCRVRKTCESLMRlvrqelktkqkgdllskiqsyragytvqerrkiesemfngKLYGIIATNALELGIDIGS 628
Cdd:cd18785 1 VMVVKIIVFTNSIEHAEEIAS----------------------------------------SLEILVATNVLGEGIDVPS 40
|
90 100 110
....*....|....*....|....*....|....*.
gi 63054629 629 LDAVITIGFPYSLSNLRQQFGRAGRRNKSSLAVYIV 664
Cdd:cd18785 41 LDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILF 76
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
295-671 |
1.96e-06 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 51.37 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 295 LSQELINALYtSRNIEKTYKHQADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSLLED-NQSTAFFVFPTKSLAQDQK 373
Cdd:PTZ00424 35 LNEDLLRGIY-SYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDlNACQALILAPTRELAQQIQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 374 KSLIDILSYMptlkNIRVDTFDGDTPL-ESRESIIRSANIIFTNPDMLHQTIlpnaNRWYYFFKNLKLFVLDEA-HVYNG 451
Cdd:PTZ00424 114 KVVLALGDYL----KVRCHACVGGTVVrDDINKLKAGVHMVVGTPGRVYDMI----DKRHLRVDDLKLFILDEAdEMLSR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 452 IFGVHVAFVLRRMrriaeyfgNSQYRFVSCSATIEDPLQHMKKIFGVDNIKLINYTSSPS--GSKKFvmwnppYVDPKHP 529
Cdd:PTZ00424 186 GFKGQIYDVFKKL--------PPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTleGIRQF------YVAVEKE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 530 DDGKKSAISEASKLLIkfaekrVRTIVFCRVRKTCESLmrlvrqelkTKQKGDLLSKIQSYRAGYTVQERRKIESEMFNG 609
Cdd:PTZ00424 252 EWKFDTLCDLYETLTI------TQAIIYCNTRRKVDYL---------TKKMHERDFTVSCMHGDMDQKDRDLIMREFRSG 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054629 610 KLYGIIATNALELGIDIGSLDAVITIGFPYSLSNLRQQFGRAGRRNKSSLAVYIVETFPVDQ 671
Cdd:PTZ00424 317 STRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQ 378
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
316-496 |
3.54e-06 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350718 [Multi-domain] Cd Length: 202 Bit Score: 48.73 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 316 QADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSLL------EDNQSTAFFVFPTKSLAQDQKKSLIDILSYMptLKNI 389
Cdd:cd17960 17 QAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLkrkanlKKGQVGALIISPTRELATQIYEVLQSFLEHH--LPKL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 390 RVDTF-DGDTPLESRESIIRS-ANIIFTNPDMLHQtILPNANRWYYfFKNLKLFVLDEAHVYNGI-FGVHVAFVLRRMRR 466
Cdd:cd17960 95 KCQLLiGGTNVEEDVKKFKRNgPNILVGTPGRLEE-LLSRKADKVK-VKSLEVLVLDEADRLLDLgFEADLNRILSKLPK 172
|
170 180 190
....*....|....*....|....*....|
gi 63054629 467 iaeyfgnsQYRFVSCSATIEDPLQHMKKIF 496
Cdd:cd17960 173 --------QRRTGLFSATQTDAVEELIKAG 194
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
316-446 |
4.52e-06 |
|
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350701 [Multi-domain] Cd Length: 192 Bit Score: 48.41 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 316 QADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSL-LEDNQSTAFFVFPTKSLAQdQKKSLIDILSymPTLKNIRVDTF 394
Cdd:cd17943 17 QLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLdLERRHPQVLILAPTREIAV-QIHDVFKKIG--KKLEGLKCEVF 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 63054629 395 DGDTPLESRESIIRSANIIFTNPDMLHQTILPNANRwyyfFKNLKLFVLDEA 446
Cdd:cd17943 94 IGGTPVKEDKKKLKGCHIAVGTPGRIKQLIELGALN----VSHVRLFVLDEA 141
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
316-496 |
4.82e-06 |
|
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350719 [Multi-domain] Cd Length: 206 Bit Score: 48.73 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 316 QADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSLLEDNQS-------TAFFVFPTKSLAQDQKKSLIDILSYMPtlKN 388
Cdd:cd17961 21 QSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAEsgeeqgtRALILVPTRELAQQVSKVLEQLTAYCR--KD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 389 IRVDTFDGDtplesrESIIRSANIIFTNPDMLHQT---ILPNANRWYYFFK-NLKLFVLDEAHVyngifgvhvafVL--- 461
Cdd:cd17961 99 VRVVNLSAS------SSDSVQRALLAEKPDIVVSTparLLSHLESGSLLLLsTLKYLVIDEADL-----------VLsyg 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 63054629 462 --RRMRRIAEYFGNSqYRFVSCSATIEDPLQHMKKIF 496
Cdd:cd17961 162 yeEDLKSLLSYLPKN-YQTFLMSATLSEDVEALKKLV 197
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
329-670 |
5.85e-06 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 49.76 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 329 VIVSTSTSSGKSLIYQIPILQSLLEDNQSTAFFVFPTKSLAQDQKKSLIDILSyMPTLKNIRVDTFDGDTPLESRESIIR 408
Cdd:TIGR01587 2 LVIEAPTGYGKTEAALLWALHSIKSQKADRVIIALPTRATINAMYRRAKELFG-SELVGLHHSSSFSRIKEMGDSEEFEH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 409 SANIIFTNPDMLHQTILPNANR---WYYFFKNLK------------LFVLDEAHVYNGIFGVHVAFVLrrmrRIAEYFGN 473
Cdd:TIGR01587 81 LFPLYIHSNDKLFLDPITVCTIdqvLKSVFGEFGhyeftlasiansLLIFDEVHFYDEYTLALILAVL----EVLKDNDV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 474 SqyrFVSCSATIEDPL-QHMKKIFGVDNIKLINYTSSPSGSkkfvmwNPPYVDPKHPDDGKKSAISEasklLIKFAEKRV 552
Cdd:TIGR01587 157 P---ILLMSATLPKFLkEYAEKIGYVEFNEPLDLKEERRFE------NHRFILIESDKVGEISSLER----LLEFIKKGG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 553 RTIVFCRVRKTCESLMRLVRqELKTKQKGDLlskiqsYRAGYTVQERRKIE----SEMF-NGKLYGIIATNALELGIDIg 627
Cdd:TIGR01587 224 SIAIIVNTVDRAQEFYQQLK-EKAPEEEIIL------YHSRFTEKDRAKKEaellREMKkSNEKFVIVATQVIEASLDI- 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 63054629 628 SLDAVITIGFPysLSNLRQQFG---RAGRRNKSSLAVYIVETFPVD 670
Cdd:TIGR01587 296 SADVMITELAP--IDSLIQRLGrlhRYGRKIGENFEVYIITIAPEG 339
|
|
| Cas3_I-D |
cd09710 |
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; ... |
315-489 |
6.39e-06 |
|
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; 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; Diverged DNA helicase Cas3'; signature gene for Type I and subtype I-D
Pssm-ID: 187841 [Multi-domain] Cd Length: 353 Bit Score: 49.48 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 315 HQADAINHLWNG--FHVIVSTSTSSGKSLIYQIPILQSllednQSTAFFVFPTKSLAQDQK---KSLIDILSYMPTLKNI 389
Cdd:cd09710 1 HQVATFEALQSKdaDIIFNTAPTGAGKTLAWLTPLLHG-----ENKAIALYPTNALIEDQTeaiKEFVDDANPRHQVKSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 390 RV---DTFDGDTPLESRE-----SIIRSA------NIIFTNPDMLHQtilpnANRWYY---------FFKNLKLFVLDEA 446
Cdd:cd09710 76 SAsdiTLWPNDKNVGSSKgeklyNLLRNDigtstpIILLTNPDIFVY-----LTRFAYidrgdiaagFYTKFSTVIFDEF 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 63054629 447 HVYNGIFGVHVAFVLRRMrRIAEYFGNSQYrFVSCSATIEDPL 489
Cdd:cd09710 151 HLYDAKQLVGLLFYLAYM-QLIRFFECRRK-FVFLSATPDPAL 191
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
302-398 |
6.45e-06 |
|
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.
Pssm-ID: 350784 [Multi-domain] Cd Length: 202 Bit Score: 47.98 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 302 ALYTSRNIEKTYKHQADAINH--LWNGFHVIVSTSTSSGKSLIYQIPILQSLLEdNQSTAFFVFPTKSLAQDQKKSLIDI 379
Cdd:cd18026 7 EAYAKKGIKKLYDWQKECLSLpgLLEGRNLVYSLPTSGGKTLVAEILMLKRLLE-RRKKALFVLPYVSIVQEKVDALSPL 85
|
90
....*....|....*....
gi 63054629 380 LSYmptlKNIRVDTFDGDT 398
Cdd:cd18026 86 FEE----LGFRVEGYAGNK 100
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
329-677 |
2.08e-05 |
|
CRISPR/Cas system-associated protein Cas3; 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; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 47.81 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 329 VIVSTSTSSGKSLIYQIPILQSLLEDNQSTAFFVFPTKSLAQDQKKSLIDILSYMPTLKNIRvdTFDGDTPLESRESIIR 408
Cdd:cd09639 2 LVIEAPTGYGKTEAALLWALHSLKSQKADRVIIALPTRATINAMYRRAKEAFGETGLYHSSI--LSSRIKEMGDSEEFEH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 409 SANIIFTNPDMLHQTILPNANR---WYYFFKNLK------------LFVLDEAHVYNGIFGVHVAFVLrrmrRIAEYFGN 473
Cdd:cd09639 80 LFPLYIHSNDTLFLDPITVCTIdqvLKSVFGEFGhyeftlasiansLLIFDEVHFYDEYTLALILAVL----EVLKDNDV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 474 SqyrFVSCSATIEDPLqhMKKIFGVDN-IKLINYTSSPSGSKKFVmwnppyvdpkHPDDGKKSAISEASkLLIKFAEKRV 552
Cdd:cd09639 156 P---ILLMSATLPKFL--KEYAEKIGYvEENEPLDLKPNERAPFI----------KIESDKVGEISSLE-RLLEFIKKGG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 553 RTIVFCRVRKTCESLMRLVRqELKTKQKGDLlskiqsYRAGYTVQERRKIE----SEMFNGKLYGIIATNALELGIDIgS 628
Cdd:cd09639 220 SVAIIVNTVDRAQEFYQQLK-EKGPEEEIML------IHSRFTEKDRAKKEaellLEFKKSEKFVIVATQVIEASLDI-S 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 63054629 629 LDAVITIGFPysLSNLRQQFGRAGRRN-KSSLAVYIVETFPVDQFYLKHP 677
Cdd:cd09639 292 VDVMITELAP--IDSLIQRLGRLHRYGeKNGEEVYIITDAPDGKGQKPYP 339
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
295-675 |
2.28e-05 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 48.22 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 295 LSQELINALyTSRNIEKTYKHQADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSLLEDNQST--AFFVFPTKSLAQdQ 372
Cdd:COG0513 9 LSPPLLKAL-AELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRApqALILAPTRELAL-Q 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 373 -KKSLIDILSYMptlkNIRVDTFDGDTPLES-RESIIRSANIIFTNP----DMLHQTILpnanrwyyFFKNLKLFVLDEA 446
Cdd:COG0513 87 vAEELRKLAKYL----GLRVATVYGGVSIGRqIRALKRGVDIVVATPgrllDLIERGAL--------DLSGVETLVLDEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 447 HvyngifgvhvafvlrRM---------RRIAEY---------FgnsqyrfvscSATIEDPLQHMKKIFgVDNIKLINYTS 508
Cdd:COG0513 155 D---------------RMldmgfiediERILKLlpkerqtllF----------SATMPPEIRKLAKRY-LKNPVRIEVAP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 509 SPSGSKK----FVMwnppyVDPKHpddgKKSAISEasklLIKfAEKRVRTIVFCRVRKTCEslmRLVRQeLKtkqkgdll 584
Cdd:COG0513 209 ENATAETieqrYYL-----VDKRD----KLELLRR----LLR-DEDPERAIVFCNTKRGAD---RLAEK-LQ-------- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 585 skiqsyRAGYTV---------QERRKIESEMFNGKLYGIIATN-ALElGIDIGSLDAVITigfpYSLSNLRQQF----GR 650
Cdd:COG0513 263 ------KRGISAaalhgdlsqGQRERALDAFRNGKIRVLVATDvAAR-GIDIDDVSHVIN----YDLPEDPEDYvhriGR 331
|
410 420
....*....|....*....|....*
gi 63054629 651 AGRRNKSSLAVYIVEtfPVDQFYLK 675
Cdd:COG0513 332 TGRAGAEGTAISLVT--PDERRLLR 354
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
329-484 |
2.48e-05 |
|
DEAH-box helicase domain of FANCM; 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. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM 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: 350791 [Multi-domain] Cd Length: 182 Bit Score: 46.16 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 329 VIVSTSTSSGKSLIYQIPILQSLLEDNQSTAFFVFPTKSLAQDQKKSLIDILSyMPTLKNIrvdTFDGDTPLESRESIIR 408
Cdd:cd18033 19 TLVALPTGLGKTFIAAVVMLNYYRWFPKGKIVFMAPTKPLVSQQIEACYKITG-IPSSQTA---ELTGSVPPTKRAELWA 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054629 409 SANIIFTNPdmlhQTILPNANRWYYFFKNLKLFVLDEAHVYNGIFGvhVAFVLRRMRRIaeyfgNSQYRFVSCSAT 484
Cdd:cd18033 95 SKRVFFLTP----QTLENDLKEGDCDPKSIVCLVIDEAHRATGNYA--YCQVVRELMRY-----NSHFRILALTAT 159
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
329-447 |
3.87e-05 |
|
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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: 350772 [Multi-domain] Cd Length: 205 Bit Score: 45.93 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 329 VIVSTSTSSGKSLIYQIPILQSlledNQSTAFFVfPTKSLAQDQKKSLIdilsympTLKnIRVDTFDGDTPLESRESII- 407
Cdd:cd18014 32 VFVCMPTGAGKSLCYQLPALLA----KGITIVIS-PLIALIQDQVDHLK-------TLK-IRVDSLNSKLSAQERKRIIa 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 63054629 408 ------RSANIIFTNPDMLH----QTILPNANRwyyfFKNLKLFVLDEAH 447
Cdd:cd18014 99 dlesekPQTKFLYITPEMAAtssfQPLLSSLVS----RNLLSYLVVDEAH 144
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
540-653 |
5.09e-05 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 47.58 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 540 ASKL---LIKFAEKRV---RTIVFCRVRKTCESLMRLVRQELKTK-QKG-------------------DLLS-KIQSYRA 592
Cdd:COG1202 377 AKKLgakLVEYEERPVpleRHLTFADGREKIRIINKLVKREFDTKsSKGyrgqtiiftnsrrrcheiaRALGyKAAPYHA 456
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63054629 593 GYTVQERRKIESEMFNGKLYGIIATNALELGIDigsldavitigFPYS-------------LSNlrQQF----GRAGR 653
Cdd:COG1202 457 GLDYGERKKVERRFADQELAAVVTTAALAAGVD-----------FPASqvifdslamgiewLSV--QEFhqmlGRAGR 521
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
316-497 |
5.17e-05 |
|
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350713 [Multi-domain] Cd Length: 204 Bit Score: 45.29 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 316 QADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSLLEDNQST-AFFVFPTKSLAqdqkkslIDILSYMPTLK---NIRV 391
Cdd:cd17955 26 QKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIfALVLTPTRELA-------YQIAEQFRALGaplGLRC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 392 DTFDGDTPLESRESIIRS-ANIIFTNPDMLHQTILpNANRWYYFFKNLKLFVLDEA-HVYNGIFGVHVAFVLRRM--RRI 467
Cdd:cd17955 99 CVIVGGMDMVKQALELSKrPHIVVATPGRLADHLR-SSDDTTKVLSRVKFLVLDEAdRLLTGSFEDDLATILSALppKRQ 177
|
170 180 190
....*....|....*....|....*....|
gi 63054629 468 AEYFgnsqyrfvscSATIEDPLQHMKKIFG 497
Cdd:cd17955 178 TLLF----------SATLTDALKALKELFG 197
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
527-654 |
1.90e-04 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases 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: 350182 [Multi-domain] Cd Length: 154 Bit Score: 42.93 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 527 KHPDDGKKSAISEASKLLIKFAEKRVR----TIVFCRVRKTCESLMRLvrqelktkqkgdlLSKIQSYRAGYTVQERRKI 602
Cdd:cd18795 15 LGIKLRVDVMNKFDSDIIVLLKIETVSegkpVLVFCSSRKECEKTAKD-------------LAGIAFHHAGLTREDRELV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63054629 603 EsEMF-NGKLYGIIATNALELGID-------IGSLDAVITIGF-PYSLSNLRQQFGRAGRR 654
Cdd:cd18795 82 E-ELFrEGLIKVLVATSTLAAGVNlpartviIKGTQRYDGKGYrELSPLEYLQMIGRAGRP 141
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
316-446 |
2.40e-04 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350699 [Multi-domain] Cd Length: 198 Bit Score: 43.43 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 316 QADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSLL-----EDNQSTAFFVFPTKSLAQdqkkSLIDILSYMPTLKNIR 390
Cdd:cd17941 17 QRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYrerwtPEDGLGALIISPTRELAM----QIFEVLRKVGKYHSFS 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 63054629 391 VDTFDGDTPLESRESIIRSANIIFTNPDMLHQTILPNAnrwYYFFKNLKLFVLDEA 446
Cdd:cd17941 93 AGLIIGGKDVKEEKERINRMNILVCTPGRLLQHMDETP---GFDTSNLQMLVLDEA 145
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
316-370 |
2.47e-04 |
|
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350712 [Multi-domain] Cd Length: 203 Bit Score: 43.46 E-value: 2.47e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 63054629 316 QADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSLLEDNQstAFFVF---PTKSLAQ 370
Cdd:cd17954 27 QEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQ--RFFALvlaPTRELAQ 82
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
308-446 |
2.65e-04 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 43.51 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 308 NIEKTYKHQADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSLLED--------NQSTAFFVFPTKSLAQDQKKSLIDI 379
Cdd:cd17948 9 GITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYkllaegpfNAPRGLVITPSRELAEQIGSVAQSL 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 380 LSYMPtlknIRVDTFDGDtplESRESIIrsaNIIFTNPDMLHQT---ILPNANRWYYFFKNLKLFVLDEA 446
Cdd:cd17948 89 TEGLG----LKVKVITGG---RTKRQIR---NPHFEEVDILVATpgaLSKLLTSRIYSLEQLRHLVLDEA 148
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
316-488 |
3.25e-04 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350696 [Multi-domain] Cd Length: 204 Bit Score: 43.08 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 316 QADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSLLednqstAFFVFPTKSLAQdQKKSLIDILSYMPTLKNIRVDTFD 395
Cdd:cd17938 26 QAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV------ALILEPSRELAE-QTYNCIENFKKYLDNPKLRVALLI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 396 GDTPLESRESIIRS-ANIIFTNPDMLHQTIlpnaNRWYYFFKNLKLFVLDEAH--VYNGifgvHVAFVLRRMRRIAEYfG 472
Cdd:cd17938 99 GGVKAREQLKRLESgVDIVVGTPGRLEDLI----KTGKLDLSSVRFFVLDEADrlLSQG----NLETINRIYNRIPKI-T 169
|
170
....*....|....*...
gi 63054629 473 NSQYRF--VSCSATIEDP 488
Cdd:cd17938 170 SDGKRLqvIVCSATLHSF 187
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
303-409 |
4.75e-04 |
|
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350702 [Multi-domain] Cd Length: 202 Bit Score: 42.53 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 303 LYTSRNIEKTYKHQADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSLLEDNQSTA-------FFVFPTKSLAQDQKKS 375
Cdd:cd17944 4 LLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKrgrapkvLVLAPTRELANQVTKD 83
|
90 100 110
....*....|....*....|....*....|....
gi 63054629 376 LIDIlsymptLKNIRVDTFDGDTPLESRESIIRS 409
Cdd:cd17944 84 FKDI------TRKLSVACFYGGTPYQQQIFAIRN 111
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
329-446 |
4.88e-04 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 43.00 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 329 VIVSTSTSSGKSLIYQIPILQSLLE--DNQSTAFFVFPTKSLAQdQKKSLIDILSympTLKNIRVDTFDGDT-------- 398
Cdd:cd17956 39 LCVSAPTGSGKTLAYVLPIVQALSKrvVPRLRALIVVPTKELVQ-QVYKVFESLC---KGTGLKVVSLSGQKsfkkeqkl 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 63054629 399 --PLESRESIIRsANIIFTNP----DMLHQTILPNanrwyyfFKNLKLFVLDEA 446
Cdd:cd17956 115 llVDTSGRYLSR-VDILVATPgrlvDHLNSTPGFT-------LKHLRFLVIDEA 160
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
316-446 |
5.45e-04 |
|
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350700 [Multi-domain] Cd Length: 198 Bit Score: 42.35 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 316 QADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSL-----LEDNQSTAFFVFPTKSLAQDQKKSLIDILSYmptlkniR 390
Cdd:cd17942 17 QAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLyklkfKPRNGTGVIIISPTRELALQIYGVAKELLKY-------H 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054629 391 VDTF----DGDTPLESRESIIRSANIIFTNPDML--HqtiLPNANRWYYffKNLKLFVLDEA 446
Cdd:cd17942 90 SQTFgiviGGANRKAEAEKLGKGVNILVATPGRLldH---LQNTKGFLY--KNLQCLIIDEA 146
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
295-665 |
6.58e-04 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 43.68 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 295 LSQELINALyTSRNIEKTYKHQADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSLLEDNQSTAFFVF-PTKSLAQDQK 373
Cdd:PRK11634 13 LKAPILEAL-NDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLaPTRELAVQVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 374 KSLIDILSYMPTLkNIrVDTFDGDTPLESRESIIRSANIIFTNPDMLhqtiLPNANRWYYFFKNLKLFVLDEAHvyngif 453
Cdd:PRK11634 92 EAMTDFSKHMRGV-NV-VALYGGQRYDVQLRALRQGPQIVVGTPGRL----LDHLKRGTLDLSKLSGLVLDEAD------ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 454 gvhvafvlrRMRRIAeyfgnsqyrFVSCSATI--EDPLQHMKKIFGV---DNIKLInytsspsgSKKFvMWNPPYVDPK- 527
Cdd:PRK11634 160 ---------EMLRMG---------FIEDVETImaQIPEGHQTALFSAtmpEAIRRI--------TRRF-MKEPQEVRIQs 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 528 ----HPDdgkksaISEA---------SKLLIKF--AEKRVRTIVFCRVRK-TCESLMRLVRQELKTKQ-KGDLlskIQSY 590
Cdd:PRK11634 213 svttRPD------ISQSywtvwgmrkNEALVRFleAEDFDAAIIFVRTKNaTLEVAEALERNGYNSAAlNGDM---NQAL 283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054629 591 RAgyTVQERRKiesemfNGKLYGIIATNALELGIDIGSLDAVITIGFPYSLSNLRQQFGRAGRRNKSSLAVYIVE 665
Cdd:PRK11634 284 RE--QTLERLK------DGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVE 350
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
295-446 |
7.77e-04 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor 4A-III (EIF4AIII, also known as DDX48) is part of the exon junction complex (EJC) that plays a major role in posttranscriptional regulation of mRNA. EJC consists of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. DDX48 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350803 [Multi-domain] Cd Length: 201 Bit Score: 42.07 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 295 LSQELINALYtSRNIEKTYKHQADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSL-LEDNQSTAFFVFPTKSLAQDQK 373
Cdd:cd18045 6 LREDLLRGIY-AYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLdIQVRETQALILSPTRELAVQIQ 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054629 374 KSLIDILSYMptlkNIRVDTFDGDTPLESRESIIRSA-NIIFTNPDMLHQTIlpnaNRWYYFFKNLKLFVLDEA 446
Cdd:cd18045 85 KVLLALGDYM----NVQCHACIGGTSVGDDIRKLDYGqHIVSGTPGRVFDMI----RRRSLRTRHIKMLVLDEA 150
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
326-446 |
9.72e-04 |
|
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350704 [Multi-domain] Cd Length: 235 Bit Score: 41.84 E-value: 9.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 326 GFHVIVSTSTSSGKSLIYQIPILQSLLEDNQS----------TAFFVFPTKSLAQDQKKSLIDILSYMptlkNIRVDTFD 395
Cdd:cd17946 28 GKDVIGAAETGSGKTLAFGIPILERLLSQKSSngvggkqkplRALILTPTRELAVQVKDHLKAIAKYT----NIKIASIV 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 63054629 396 GDTPLESRESII-RSANIIFTNPDMLHQTIlPNANRWYYFFKNLKLFVLDEA 446
Cdd:cd17946 104 GGLAVQKQERLLkKRPEIVVATPGRLWELI-QEGNEHLANLKSLRFLVLDEA 154
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
329-468 |
1.29e-03 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350779 [Multi-domain] Cd Length: 191 Bit Score: 41.09 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 329 VIVSTSTSSGKSLIYQIPILQSLLEDNQSTAFFVFPTKSLA----QDQKKSLIDILSymptlKNIRVDTfdGDTPLESRe 404
Cdd:cd18021 22 VFVGAPTGSGKTVCAELALLRHWRQNPKGRAVYIAPMQELVdaryKDWRAKFGPLLG-----KKVVKLT--GETSTDLK- 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054629 405 sIIRSANIIFTNP---DMLhqtilpnANRWyyffK------NLKLFVLDEAHVYNGIFGVHVAFVLRRMRRIA 468
Cdd:cd18021 94 -LLAKSDVILATPeqwDVL-------SRRW----KqrknvqSVELFIADELHLIGGENGPVYEVVVSRMRYIS 154
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
315-447 |
1.30e-03 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 41.09 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 315 HQADAINHLWNGFHVIVSTSTSSGKSLIYQIPILqsLLEDNQSTAFFVF-PTKSLAQDQKKSLIdilsymPTLKNIRVDT 393
Cdd:cd18018 16 GQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPAL--LLRRRGPGLTLVVsPLIALMKDQVDALP------RAIKAAALNS 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054629 394 fdGDTPLESRESI--IRSANI--------IFTNPD---MLHQTilpnanrwyyffKNLKLFVLDEAH 447
Cdd:cd18018 88 --SLTREERRRILekLRAGEVkilyvspeRLVNESfreLLRQT------------PPISLLVVDEAH 140
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
299-495 |
1.32e-03 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350707 [Multi-domain] Cd Length: 214 Bit Score: 41.42 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 299 LINALYTSRNIEKTYKHQADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSLLED------NQST-AFFVFPTKSLAQD 371
Cdd:cd17949 1 LVSHLKSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLeprvdrSDGTlALVLVPTRELALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 372 QKKSLIDILSYMPtlkNIRVDTFDGDtplESRES----IIRSANIIFTNP----DMLHQTilpNANRwyyfFKNLKLFVL 443
Cdd:cd17949 81 IYEVLEKLLKPFH---WIVPGYLIGG---EKRKSekarLRKGVNILIATPgrllDHLKNT---QSFD----VSNLRWLVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054629 444 DEA---------HVYNGIFGvhvafVLRRMRRIAEYFGN--SQYRFVSCSATIEDPLQHMKKI 495
Cdd:cd17949 148 DEAdrlldmgfeKDITKILE-----LLDDKRSKAGGEKSkpSRRQTVLVSATLTDGVKRLAGL 205
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
295-446 |
1.47e-03 |
|
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350708 [Multi-domain] Cd Length: 208 Bit Score: 41.18 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 295 LSQELINALytsrnIEKTYKH----QADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSL-LEDNQSTAFFVFPTKSLA 369
Cdd:cd17950 9 LKPELLRAI-----VDCGFEHpsevQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLePVDGQVSVLVICHTRELA 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054629 370 QDQKKSLIDILSYMPtlkNIRVDTFDGDTPLESRESIIRSA--NIIFTNPDmlhqTILPNANRWYYFFKNLKLFVLDEA 446
Cdd:cd17950 84 FQISNEYERFSKYMP---NVKTAVFFGGVPIKKDIEVLKNKcpHIVVGTPG----RILALVREKKLKLSHVKHFVLDEC 155
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
294-488 |
2.16e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 42.25 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 294 PLSQELINAlYTSRNIEKTYKHQADAINH-LWNGFHVIVSTSTSSGKSLIYQIPILQSLLEDnqSTAFFVFPTKSLAQDQ 372
Cdd:PRK02362 7 PLPEGVIEF-YEAEGIEELYPPQAEAVEAgLLDGKNLLAAIPTASGKTLIAELAMLKAIARG--GKALYIVPLRALASEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 373 KKSLIDILSYmptlkNIRVDTFDGDtpLESRESIIRSANIIFTNP---DMLhqtiLPNANRWyyfFKNLKLFVLDEAH-V 448
Cdd:PRK02362 84 FEEFERFEEL-----GVRVGISTGD--YDSRDEWLGDNDIIVATSekvDSL----LRNGAPW---LDDITCVVVDEVHlI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 63054629 449 YNGIFGVHVAFVLRRMRRIaeyfgNSQYRFVSCSATIEDP 488
Cdd:PRK02362 150 DSANRGPTLEVTLAKLRRL-----NPDLQVVALSATIGNA 184
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
313-342 |
2.51e-03 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 41.85 E-value: 2.51e-03
10 20 30
....*....|....*....|....*....|
gi 63054629 313 YKHQADAINHLWNGFHVIVSTSTSSGKSLI 342
Cdd:COG4581 27 DPFQEEAILALEAGRSVLVAAPTGSGKTLV 56
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
328-484 |
3.51e-03 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 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: 350688 [Multi-domain] Cd Length: 186 Bit Score: 39.58 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 328 HVIVSTSTSSGKSLIYQIPILQSLLEDNQSTAFFVFPTKSLAQDQKKSLIDILSYMPTLKNIR-------VDTFDGDTPL 400
Cdd:cd17930 3 LVILEAPTGSGKTEAALLWALKLAARGGKRRIIYALPTRATINQMYERIREILGRLDDEDKVLllhskaaLELLESDEEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 401 --------ESRESIIRS--ANIIFTNPDMLHQTILPNaNRWYYFFKNL--KLFVLDEAHVYNGIFGvhvAFVLRRMRRIA 468
Cdd:cd17930 83 dddpveavDWALLLKRSwlAPIVVTTIDQLLESLLKY-KHFERRLHGLanSVVVLDEVQAYDPEYM---ALLLKALLELL 158
|
170
....*....|....*.
gi 63054629 469 EYFGNSqyrFVSCSAT 484
Cdd:cd17930 159 GELGGP---VVLMTAT 171
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
297-653 |
4.28e-03 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 40.84 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 297 QELINALYTSRNieKTYKHQADAINHLWNGFH-----VIVSTSTSSGK---SLIYqipILQSLLEDNQSTAFFVFPTKSL 368
Cdd:COG1203 115 ERLLPKKSKPRT--PINPLQNEALELALEAAEeepglFILTAPTGGGKteaALLF---ALRLAAKHGGRRIIYALPFTSI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 369 AQDQKKSLIDILSymPTLK----NIRVDTFDGDTPLESRESIIRSAN------IIFTNPDMLHQTILPNANRWYYFFKNL 438
Cdd:COG1203 190 INQTYDRLRDLFG--EDVLlhhsLADLDLLEEEEEYESEARWLKLLKelwdapVVVTTIDQLFESLFSNRKGQERRLHNL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 439 --KLFVLDEAHVYNgifgVHVAFVLRRMRRIAEYFGNsqyRFVSCSATIedPLQHMKKIFgvDNIKLInytssPSGSKKF 516
Cdd:COG1203 268 anSVIILDEVQAYP----PYMLALLLRLLEWLKNLGG---SVILMTATL--PPLLREELL--EAYELI-----PDEPEEL 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 517 VMWNPPYVDPKHPDDGKKSAISEASKLLIKFAEKRVRTIVFCRVRKTCeslmRLVRQELKTKQKGD---LLSkiqsyrAG 593
Cdd:COG1203 332 PEYFRAFVRKRVELKEGPLSDEELAELILEALHKGKSVLVIVNTVKDA----QELYEALKEKLPDEevyLLH------SR 401
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054629 594 YTVQERRKIESE---MFNGKLYGI-IATNALELGIDIgSLDAVITigfpySLSNLRQQFGRAGR 653
Cdd:COG1203 402 FCPADRSEIEKEikeRLERGKPCIlVSTQVVEAGVDI-DFDVVIR-----DLAPLDSLIQRAGR 459
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
295-446 |
4.62e-03 |
|
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350698 [Multi-domain] Cd Length: 201 Bit Score: 39.59 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 295 LSQELINALYtsrniEKTYKH----QADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSL-LEDNQSTAFFVFPTKSLA 369
Cdd:cd17940 6 LKRELLMGIF-----EKGFEKpspiQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIdPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 370 QDQKKSLIDILSYMptlkNIRVDTFDGDTPLesRESIIR---SANIIFTNPDmlhqTILPNANRWYYFFKNLKLFVLDEA 446
Cdd:cd17940 81 LQTSQVCKELGKHM----GVKVMVTTGGTSL--RDDIMRlyqTVHVLVGTPG----RILDLAKKGVADLSHCKTLVLDEA 150
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
307-370 |
8.32e-03 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 38.72 E-value: 8.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054629 307 RNIEKT-YKH----QADAINHLWNGFHVIVSTSTSSGKSLIYQIPILQSLLEDNQSTAFF---VFPTKSLAQ 370
Cdd:cd17957 3 NNLEESgYREptpiQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKGLRaliLAPTRELAS 74
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
553-665 |
9.34e-03 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 40.10 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054629 553 RTIVFCRVRKTCESLM-RLVRQELKTK----QKGDLLSKiqsyraGYTVQERRKIESEMFNGKLYGIIATNALELGIDIG 627
Cdd:COG1111 355 RIIVFTQYRDTAEMIVeFLSEPGIKAGrfvgQASKEGDK------GLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIP 428
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 63054629 628 SLDAVItigFpYSL--SNLR--QQFGRAGRRNKSSLAVYIVE 665
Cdd:COG1111 429 EVDLVI---F-YEPvpSEIRsiQRKGRTGRKREGRVVVLIAK 466
|
|
| |
