|
Name |
Accession |
Description |
Interval |
E-value |
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
248-1022 |
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: 836.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 248 PAEMVDHLKQGLGKEGQIVHIEEIPCRAASFAELPNHLSEATREALKSIGVSRLYSHQSRAIHSSIAGRHVAIATSTSSG 327
Cdd:COG1205 4 LEELLERLRASPRYGDQIVHVRTIPAREARYAPWPDWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 328 KSLCYNIPVLESLCQNLMACALYIFPTKALAQDQLRSLLEMKNALHTDIDVNIYDGDTPREDRTWIRDNARLLITNPDML 407
Cdd:COG1205 84 KSLAYLLPVLEALLEDPGATALYLYPTKALARDQLRRLRELAEALGLGVRVATYDGDTPPEERRWIREHPDIVLTNPDML 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 408 HMSILPCHGQFQRILSNLRYIVIDEAHSYKGAFGCHTALILRRLKRICSNiYGSHPTFIFCTATSANPREHVMELAKLDn 487
Cdd:COG1205 164 HYGLLPHHTRWARFFRNLRYVVIDEAHTYRGVFGSHVANVLRRLRRICRH-YGSDPQFILASATIGNPAEHAERLTGRP- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 488 VELIENDGSPCGFKYFLLWNPPLHMTkegsskdsllTRRSSPIVEVSYLLSEMVQHGLRCIAFCKTRKLCELVLAYTREI 567
Cdd:COG1205 242 VTVVDEDGSPRGERTFVLWNPPLVDD----------GIRRSALAEAARLLADLVREGLRTLVFTRSRRGAELLARYARRA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 568 LQEtaKELVDTICVYRAGYIAEDRRKIEANLFQGKLLGVAATNALELGIDVGHIDATLHLGFPGSIASLWQQAGRSGRRA 647
Cdd:COG1205 312 LRE--PDLADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 648 KQSLAIYVAFEGPLDQYFMKFPHKLFGKPIEHCQVDSHNQKLLEQHLACAAYEHPLCVQyDADYFCSSLNSVMMALKDKG 727
Cdd:COG1205 390 QDSLVVLVAGDDPLDQYYVRHPEELFERPPEAAVIDPDNPYVLAPHLLCAAAELPLTEG-DLELFGPEARELLDALVEEG 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 728 CLINNPSGpfsssmWSYVGPeKRPSQAVSIRAIEHDKYRVIDKLNNRLLEEIEESKAFF----------QGVNYLVEELD 797
Cdd:COG1205 469 LLRRRGDG------WYWTGD-DRPARDVSLRGAGGENVVIVDATTGRVIGTVDLPRALRelhpgaiylhQGETYRVEELD 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 798 LSSRTAFCRKADLKYYTKTRDYTDINVLgGEFAHlppsmcKTNGvKTTAQANDCKVTTKWFGFYRIWKSNNKISDSIELN 877
Cdd:COG1205 542 LEERKAYVRPVDVDYYTRALSETDIRIL-EVLEE------RELG-GVTVHFGEVEVTEQVTGYKKRRLYTGEVLGEVPLD 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 878 LPPYSFNSQAVWVRIPHSVKTNVEERKLQFRGGSHAASHALLNIVPLHMTCNASDLGTECANPHETRGIPdRILLYDKHP 957
Cdd:COG1205 614 LPPRTLRTKAVWLTIPPDLLEAAGLDPEDFPGALHAAEHALIGLLPLFALCDRWDIGGVSTPLHPDTGAP-TIFIYDGYP 692
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002286793 958 GGIGIALQIKSLFGELLLAALELVSECNCTSsaGCPNCIQTLTCGEYNEVLDKEAAILILKGVIE 1022
Cdd:COG1205 693 GGVGLAERGYERFEELLEATRDLIASCPCED--GCPSCVQSPKCGNGNEPLDKAAALRLLEALLG 755
|
|
| DECH_helic |
TIGR03817 |
helicase/secretion neighborhood putative DEAH-box helicase; A conserved gene neighborhood ... |
265-1020 |
0e+00 |
|
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: 625.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 265 IVHIEEIPCRAASFAELPNHLSEATREALKSIGVSRLYSHQSRAIHSSIAGRHVAIATSTSSGKSLCYNIPVLESLCQNL 344
Cdd:TIGR03817 1 LTHVEHLPARAGRTAPWPAWAHPDVVAALEAAGIHRPWQHQARAAELAHAGRHVVVATGTASGKSLAYQLPVLSALADDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 345 MACALYIFPTKALAQDQLRSLLEMKnalHTDIDVNIYDGDTPREDRTWIRDNARLLITNPDMLHMSILPCHGQFQRILSN 424
Cdd:TIGR03817 81 RATALYLAPTKALAADQLRAVRELT---LRGVRPATYDGDTPTEERRWAREHARYVLTNPDMLHRGILPSHARWARFLRR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 425 LRYIVIDEAHSYKGAFGCHTALILRRLKRICSNiYGSHPTFIFCTATSANPREHVMELAKLDnVELIENDGSPCGFKYFL 504
Cdd:TIGR03817 158 LRYVVIDECHSYRGVFGSHVALVLRRLRRLCAR-YGASPVFVLASATTADPAAAASRLIGAP-VVAVTEDGSPRGARTVA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 505 LWNPPLhmtKEGSSKDSLLTRRSSPIvEVSYLLSEMVQHGLRCIAFCKTRKLCELVLAYTREILQETAKELVDTICVYRA 584
Cdd:TIGR03817 236 LWEPPL---TELTGENGAPVRRSASA-EAADLLADLVAEGARTLTFVRSRRGAELVAAIARRLLGEVDPDLAERVAAYRA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 585 GYIAEDRRKIEANLFQGKLLGVAATNALELGIDVGHIDATLHLGFPGSIASLWQQAGRSGRRAKQSLAIYVAFEGPLDQY 664
Cdd:TIGR03817 312 GYLPEDRRELERALRDGELLGVATTNALELGVDISGLDAVVIAGFPGTRASLWQQAGRAGRRGQGALVVLVARDDPLDTY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 665 FMKFPHKLFGKPIEHCQVDSHNQKLLEQHLACAAYEHPLcVQYDADYFCSSLNSVMMALKDKGCLINNPSGpfsssmWSY 744
Cdd:TIGR03817 392 LVHHPEALFDRPVEATVFDPDNPYVLGPHLCCAAAELPL-TEADLELFGPAAAEVLDQLVEQGLLRRRPAG------WFW 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 745 VGPEkRPSQAVSIRAIEHDKYRVIDKLNNRLLEEIEESKAFF----------QGVNYLVEELDLSSRTAFCRKADLKYYT 814
Cdd:TIGR03817 465 TRRE-RAHDAVDIRGGGGAPVAIVEAETGRLLGTVDAGAAHStvhpgavylhQGESYVVDELDLEDGVALVHAEDPDYTT 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 815 KTRDYTDINVLG-GEFAHLPPsmcktngvkTTAQANDCKVTTKWFGFYRIWKSNNKISDSIELNLPPYSFNSQAVWVRIP 893
Cdd:TIGR03817 544 FARETTDISVVEeRRRRAWGD---------VRVALGEVEVTSQVVGYLRRRLITGEVLDEVPLDLPPRTLRTRAVWYTVT 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 894 HSVKTNVEERKLQFRGGSHAASHALLNIVPLHMTCNASDLGTECANPHETRGIPDrILLYDKHPGGIGIALQIKSLFGEL 973
Cdd:TIGR03817 615 PELLDDAGIDAADVPGALHAAEHAAIGLLPLVATCDRWDIGGVSTAVHPDTGLPT-VFVYDGHPGGAGFAERGFAKAREW 693
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1002286793 974 LLAALELVSECNCTSsaGCPNCIQTLTCGEYNEVLDKEAAILILKGV 1020
Cdd:TIGR03817 694 LAATRDAIASCECES--GCPSCVQSPKCGNGNDPLDKAGAARLLAAV 738
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
301-482 |
5.23e-91 |
|
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: 287.94 E-value: 5.23e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 301 LYSHQSRAIHSSIAGRHVAIATSTSSGKSLCYNIPVLESLCQNLMACALYIFPTKALAQDQLRSLLEMKNALHTDIDVNI 380
Cdd:cd17923 1 LYSHQAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGSRALYLYPTKALAQDQLRSLRELLEQLGLGIRVAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 381 YDGDTPREDRTWIRDN-ARLLITNPDMLHMSILPCHGQFQRILSNLRYIVIDEAHSYKGAFGCHTALILRRLKRICsNIY 459
Cdd:cd17923 81 YDGDTPREERRAIIRNpPRILLTNPDMLHYALLPHHDRWARFLRNLRYVVLDEAHTYRGVFGSHVALLLRRLRRLC-RRY 159
|
170 180
....*....|....*....|...
gi 1002286793 460 GSHPTFIFCTATSANPREHVMEL 482
Cdd:cd17923 160 GADPQFILTSATIGNPAEHARTL 182
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
502-656 |
6.27e-68 |
|
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: 223.67 E-value: 6.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 502 YFLLWNPPLHMTKEGSskdslltrRSSPIVEVSYLLSEMVQHGLRCIAFCKTRKLCELVLAYTREILQETAKeLVDTICV 581
Cdd:cd18797 1 HFVLWNPPLLDRKDGE--------RGSARREAARLFADLVRAGVKTIVFCRSRKLAELLLRYLKARLVEEGP-LASKVAS 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002286793 582 YRAGYIAEDRRKIEANLFQGKLLGVAATNALELGIDVGHIDATLHLGFPGSIASLWQQAGRSGRRAKQSLAIYVA 656
Cdd:cd18797 72 YRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVILVA 146
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
302-471 |
2.63e-30 |
|
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: 117.73 E-value: 2.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 302 YSHQSRAIHSSIAGRHVAIATSTSSGKSLCYNIPVLESLCQNLMAC-ALYIFPTKALAQDQLRSLLEMKNalHTDIDVN- 379
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPqALVLAPTRELAEQIYEELKKLGK--GLGLKVAs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 380 IYDGDTPREDRTWIRdNARLLITNPDMLHmSILpchgQFQRILSNLRYIVIDEAH--SYKGaFGCHTALILRRLKricsn 457
Cdd:pfam00270 79 LLGGDSRKEQLEKLK-GPDILVGTPGRLL-DLL----QERKLLKNLKLLVLDEAHrlLDMG-FGPDLEEILRRLP----- 146
|
170
....*....|....
gi 1002286793 458 iygSHPTFIFCTAT 471
Cdd:pfam00270 147 ---KKRQILLLSAT 157
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
304-646 |
4.92e-29 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 125.21 E-value: 4.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 304 HQSRAIHSSIAGRHVAIATSTSSGKSLCYNIPVLESLCQNLMAC-------ALYIFPTKALAQDQLRSLL----EMKNAL 372
Cdd:COG1201 28 PQREAWPAIAAGESTLLIAPTGSGKTLAAFLPALDELARRPRPGelpdglrVLYISPLKALANDIERNLRapleEIGEAA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 373 HT---DIDVNIYDGDTPREDRtwirdnARL-------LITNPDMLHmsILPCHGQFQRILSNLRYIVIDEAHsykgAF-- 440
Cdd:COG1201 108 GLplpEIRVGVRTGDTPASER------QRQrrrpphiLITTPESLA--LLLTSPDARELLRGVRTVIVDEIH----ALag 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 441 ---GCHTALILRRLKRICsniyGSHPTFIFCTATSANPrEHVME-LA---KLDNVELIenDGSPcgfkyfllwNPPLHMT 513
Cdd:COG1201 176 skrGVHLALSLERLRALA----PRPLQRIGLSATVGPL-EEVARfLVgyeDPRPVTIV--DAGA---------GKKPDLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 514 KEgsSKDSLLTRRSSPIVEVS-YLLSEMV----QHGLrCIAFCKTRKLCELVLAYTREILQETAkELVdticvyRA--GY 586
Cdd:COG1201 240 VL--VPVEDLIERFPWAGHLWpHLYPRVLdlieAHRT-TLVFTNTRSQAERLFQRLNELNPEDA-LPI------AAhhGS 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002286793 587 IA-EDRRKIEANLFQGKLLGVAATNALELGIDVGHIDATLHLGFPGSIASLWQQAGRSGRR 646
Cdd:COG1201 310 LSrEQRLEVEEALKAGELRAVVATSSLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAGHR 370
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
293-503 |
2.35e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 101.80 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 293 LKSIGVSRLYSHQSRAIHSSIAGRHVAIATS-TSSGKSLCYNIPVLESLCQNLMACALYIFPTKALAQDQLRSLLEMKNA 371
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAApTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 372 LHtDIDVNIYDGDTPRED-RTWIRDNARLLITNPDMLHmSILPCHGQFqriLSNLRYIVIDEAHSYKG-AFGCHTALILR 449
Cdd:smart00487 81 LG-LKVVGLYGGDSKREQlRKLESGKTDILVTTPGRLL-DLLENDKLS---LSNVDLVILDEAHRLLDgGFGDQLEKLLK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002286793 450 RLKRicsniygsHPTFIFCTATSANPREHVMELAKLDNVELIENDGSPCGFKYF 503
Cdd:smart00487 156 LLPK--------NVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPLEPIEQF 201
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
315-477 |
4.80e-23 |
|
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: 96.88 E-value: 4.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 315 GRHVAIATSTSSGKSLCYNIPVLESLCQNLMAC--ALYIFPTKALAQDQLRSLLEMKNALHTDIDVNIYDGDTPREDRTW 392
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGvqVLYISPLKALINDQERRLEEPLDEIDLEIPVAVRHGDTSQSEKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 393 IRDNAR-LLITNPDMLHmsILPCHGQFQRILSNLRYIVIDEAHSYKGA-FGCHTALILRRLKRicsnIYGSHPTFIFCTA 470
Cdd:cd17922 81 QLKNPPgILITTPESLE--LLLVNKKLRELFAGLRYVVVDEIHALLGSkRGVQLELLLERLRK----LTGRPLRRIGLSA 154
|
....*..
gi 1002286793 471 TSANPRE 477
Cdd:cd17922 155 TLGNLEE 161
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
315-471 |
2.37e-21 |
|
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: 91.31 E-value: 2.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 315 GRHVAIATSTSSGKSLCYNIPVLESLCQNlmAC-ALYIFPTKALAQDQLRsllEMKNALHTDIDVNIYDGDT-PREDRTW 392
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKK--GKkVLVLVPTKALALQTAE---RLRELFGPGIRVAVLVGGSsAEEREKN 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002286793 393 IRDNARLLITNPDMLHMSILPCHGQFQRilsNLRYIVIDEAHSYKGAFGCHTALILRRLKRICSNiygshPTFIFCTAT 471
Cdd:cd00046 76 KLGDADIIIATPDMLLNLLLREDRLFLK---DLKLIIVDEAHALLIDSRGALILDLAVRKAGLKN-----AQVILLSAT 146
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
309-646 |
4.44e-20 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 96.49 E-value: 4.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 309 IHssiAGRHVAIATSTSSGKSLCYNIPVLESLCQNLMA-------CALYIFPTKALAQD----------QLRSLLEMKNA 371
Cdd:PRK13767 44 IH---EGKNVLISSPTGSGKTLAAFLAIIDELFRLGREgeledkvYCLYVSPLRALNNDihrnleepltEIREIAKERGE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 372 LHTDIDVNIYDGDTPREDRT-WIRDNARLLITNPDMLhmSILPCHGQFQRILSNLRYIVIDEAHSYKGA-FGCHTALILR 449
Cdd:PRK13767 121 ELPEIRVAIRTGDTSSYEKQkMLKKPPHILITTPESL--AILLNSPKFREKLRTVKWVIVDEIHSLAENkRGVHLSLSLE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 450 RLKricsNIYGSHPTFIFCTATsANPREhvmELAKLdnveLI--ENDGSP--C---------GFKYFLLwnpplhmtkeg 516
Cdd:PRK13767 199 RLE----ELAGGEFVRIGLSAT-IEPLE---EVAKF----LVgyEDDGEPrdCeivdarfvkPFDIKVI----------- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 517 SSKDSLLTRRSSPIVEVSY-LLSEMVQHGLRCIAFCKTRKLCELVLAYTREILQETAKElvDTICVYRAGYIAEDRRKIE 595
Cdd:PRK13767 256 SPVDDLIHTPAEEISEALYeTLHELIKEHRTTLIFTNTRSGAERVLYNLRKRFPEEYDE--DNIGAHHSSLSREVRLEVE 333
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1002286793 596 ANLFQGKLLGVAATNALELGIDVGHIDATLHLGFPGSIASLWQQAGRSGRR 646
Cdd:PRK13767 334 EKLKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAGHR 384
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
279-645 |
1.23e-19 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 93.81 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 279 AELPnhlSEATREALKSIGVSRLYSHQSRAIHSSI-AGRHVAIATSTSSGKSLCYNIPVLESLCQNLmaCALYIFPTKAL 357
Cdd:COG1204 4 AELP---LEKVIEFLKERGIEELYPPQAEALEAGLlEGKNLVVSAPTASGKTLIAELAILKALLNGG--KALYIVPLRAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 358 A---QDQLRSLLEMKNalhtdIDVNIYDGDTPREDRtWIRDNaRLLITNPDMLHmSILPcHGqfQRILSNLRYIVIDEAH 434
Cdd:COG1204 79 AsekYREFKRDFEELG-----IKVGVSTGDYDSDDE-WLGRY-DILVATPEKLD-SLLR-NG--PSWLRDVDLVVVDEAH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 435 S----YKGAfgchTA-LILRRLKRICSNIygshpTFIFCTATSANPRehvmELAKLDNVELIENDGSPCGFKYFLLWNPP 509
Cdd:COG1204 148 LiddeSRGP----TLeVLLARLRRLNPEA-----QIVALSATIGNAE----EIAEWLDAELVKSDWRPVPLNEGVLYDGV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 510 LHMtKEGSskdsllTRRSSPIVevsYLLSEMVQHGLRCIAFCKTRKLCELVLAYTREILQ-------------------- 569
Cdd:COG1204 215 LRF-DDGS------RRSKDPTL---ALALDLLEEGGQVLVFVSSRRDAESLAKKLADELKrrltpeereeleelaeelle 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 570 -----ETAKELVDtiCVYR------AGYIAEDRRKIEANLFQGKLLGVAATNALELGID-----VghIDATLHLGFPGSI 633
Cdd:COG1204 285 vseetHTNEKLAD--CLEKgvafhhAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNlparrV--IIRDTKRGGMVPI 360
|
410
....*....|....
gi 1002286793 634 ASL--WQQAGRSGR 645
Cdd:COG1204 361 PVLefKQMAGRAGR 374
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
301-494 |
1.73e-17 |
|
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: 81.54 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 301 LYSHQSRAIHSSI-AGRHVAIATSTSSGKSLCYNIPVLESLCQNlMACALYIFPTKALAQDQLRSLLEMknALHTDIDVN 379
Cdd:cd17921 2 LNPIQREALRALYlSGDSVLVSAPTSSGKTLIAELAILRALATS-GGKAVYIAPTRALVNQKEADLRER--FGPLGKNVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 380 IYDGDtPREDRTWIRDnARLLITNPDMLHmsILPCHGQfQRILSNLRYIVIDEAHSYK-GAFGCHTALILRRLKRICSNI 458
Cdd:cd17921 79 LLTGD-PSVNKLLLAE-ADILVATPEKLD--LLLRNGG-ERLIQDVRLVVVDEAHLIGdGERGVVLELLLSRLLRINKNA 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 1002286793 459 ygshpTFIFCTATSANPRehvmELAK-LDNVELIEND 494
Cdd:cd17921 154 -----RFVGLSATLPNAE----DLAEwLGVEDLIRFD 181
|
|
| MZB |
pfam09369 |
MrfA Zn-binding domain; This is the C-terminal MrfA Zn+2-binding domain (MZB, also referred to ... |
914-996 |
2.56e-17 |
|
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: 77.24 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 914 ASHALLNIVPLHMTCNASDLGTECANPHETRGipdRILLYDKHPGGIGIALQIKSLFGELLLAALELVSECNCtsSAGCP 993
Cdd:pfam09369 1 LEHALISALPLFLGCDRSDIGGESYPPDTGRP---RILIYDAYPGGAGLAEKAFELLGELLEAALERLESCDC--EAGCP 75
|
...
gi 1002286793 994 NCI 996
Cdd:pfam09369 76 SCL 78
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
541-656 |
5.71e-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: 78.85 E-value: 5.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 541 VQHGLRCIAFCKTRKLCELVLAYTREILQEtaKELVDTICVYRAGYIAEDRRKIEANLFQGKLLGVAATNALELGIDVGH 620
Cdd:cd18796 35 LERHKSTLVFTNTRSQAERLAQRLRELCPD--RVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGD 112
|
90 100 110
....*....|....*....|....*....|....*..
gi 1002286793 621 IDATLHLGFPGSIASLWQQAGRSGRRAKQ-SLAIYVA 656
Cdd:cd18796 113 VDLVIQIGSPKSVARLLQRLGRSGHRPGAaSKGRLVP 149
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
349-644 |
2.45e-15 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 81.51 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 349 LYIFPTKALAQDQLRSL----------LEMKNALHTDIDVNIYDGDTPREDRT-WIRDNARLLITNPDMLHMSILpchGQ 417
Cdd:PRK09751 41 LYISPIKALGTDVQRNLqiplkgiadeRRRRGETEVNLRVGIRTGDTPAQERSkLTRNPPDILITTPESLYLMLT---SR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 418 FQRILSNLRYIVIDEAHSYKGA-FGCHTALILRRL--------------------KRICSNIYGSHPTFIFCTATSANPR 476
Cdd:PRK09751 118 ARETLRGVETVIIDEVHAVAGSkRGAHLALSLERLdallhtsaqriglsatvrsaSDVAAFLGGDRPVTVVNPPAMRHPQ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 477 -EHVMELAKLDNVEliendgspcgfkyfllwnpplhMTKEGSSKDSLLTRRSS--PIVEVSyLLSEMVQHgLRCIAFCKT 553
Cdd:PRK09751 198 iRIVVPVANMDDVS----------------------SVASGTGEDSHAGREGSiwPYIETG-ILDEVLRH-RSTIVFTNS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 554 RKLCELVLAYTREI----LQETAKELVDT--------------------ICVYRAGYIA-EDRRKIEANLFQGKLLGVAA 608
Cdd:PRK09751 254 RGLAEKLTARLNELyaarLQRSPSIAVDAahfestsgatsnrvqssdvfIARSHHGSVSkEQRAITEQALKSGELRCVVA 333
|
330 340 350
....*....|....*....|....*....|....*.
gi 1002286793 609 TNALELGIDVGHIDATLHLGFPGSIASLWQQAGRSG 644
Cdd:PRK09751 334 TSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
290-645 |
6.79e-15 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 78.64 E-value: 6.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 290 REALKSI-GVSRLYSHQSRAIHSSIAGRHVAIATSTSSGKSLCYNIPVLeslcqnLMA-CALYIFPTKALAQDQLRSLLE 367
Cdd:COG0514 6 LEVLKRVfGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPAL------LLPgLTLVVSPLIALMKDQVDALRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 368 MK-NA--LHTDIDvniydgdtpREDRTWIRDNAR-----LLITNPDMLhmsilpCHGQFQRILSNLR--YIVIDEAH--- 434
Cdd:COG0514 80 AGiRAafLNSSLS---------AEERREVLRALRagelkLLYVAPERL------LNPRFLELLRRLKisLFAIDEAHcis 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 435 --------SYkgafgchtalilRRLKRICSNIygSHPTFIFCTATsANP--REHVMELAKLDNVELI------ENdgspc 498
Cdd:COG0514 145 qwghdfrpDY------------RRLGELRERL--PNVPVLALTAT-ATPrvRADIAEQLGLEDPRVFvgsfdrPN----- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 499 gfkyfllwnppLH---MTKEGSSKDSLLtrrsspiveVSYLLSEMVQHGlrcIAFCKTRKLCElvlaytreilqETAKEL 575
Cdd:COG0514 205 -----------LRlevVPKPPDDKLAQL---------LDFLKEHPGGSG---IVYCLSRKKVE-----------ELAEWL 250
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002286793 576 VD---TICVYRAGYIAEDRRKIEANLFQGKLLGVAATNALELGID---VGHIdatLHLGFPGSIASLWQQAGRSGR 645
Cdd:COG0514 251 REagiRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDkpdVRFV---IHYDLPKSIEAYYQEIGRAGR 323
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
290-488 |
2.69e-14 |
|
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: 72.57 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 290 REALKSI-GVSRLYSHQSRAIHSSIAGRHVAIATSTSSGKSLCYNIPVLeslcqNLMACALYIFPTKALAQDQLRSLLEM 368
Cdd:cd17920 1 EQILKEVfGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL-----LLDGVTLVVSPLISLMQDQVDRLQQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 369 knalhtDIDVNIYDGDTPREDRTWIRDN-----ARLLITNPDMLhmsilpCHGQFQRILSNLRY------IVIDEAH--- 434
Cdd:cd17920 76 ------GIRAAALNSTLSPEEKREVLLRikngqYKLLYVTPERL------LSPDFLELLQRLPErkrlalIVVDEAHcvs 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002286793 435 --------SYkgafgchtalilRRLKRICSNIYgsHPTFIFCTATsANP--REHVMELAKLDNV 488
Cdd:cd17920 144 qwghdfrpDY------------LRLGRLRRALP--GVPILALTAT-ATPevREDILKRLGLRNP 192
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
291-475 |
1.20e-11 |
|
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: 65.73 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 291 EALKSIGVSRLYSHQSRAIHSSIAGRH---------VAIATSTSSGKSLCYNIPVLESLCQNLMAC--ALYIFPTKALAQ 359
Cdd:cd17956 3 KNLQNNGITSAFPVQAAVIPWLLPSSKstppyrpgdLCVSAPTGSGKTLAYVLPIVQALSKRVVPRlrALIVVPTKELVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 360 dQLRSLLEMKNAlHTDIDVNIYDG--DTPREDRTWIRDNARLLITNPDML---------HmsILPCHGqFqrILSNLRYI 428
Cdd:cd17956 83 -QVYKVFESLCK-GTGLKVVSLSGqkSFKKEQKLLLVDTSGRYLSRVDILvatpgrlvdH--LNSTPG-F--TLKHLRFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002286793 429 VIDEA-----HSYKGAFGCHTALILRR--------LKRICSNIYGSHPTFIFCTAT-SANP 475
Cdd:cd17956 156 VIDEAdrllnQSFQDWLETVMKALGRPtapdlgsfGDANLLERSVRPLQKLLFSATlTRDP 216
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
566-646 |
2.24e-11 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 60.69 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 566 EILQETAKELVDTICVYRAGYIAEDRRKIEANLFQGKLLGVAATNALELGIDVGHIDATLHLGFPGSIASLWQQAGRSGR 645
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
.
gi 1002286793 646 R 646
Cdd:smart00490 81 A 81
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
301-618 |
2.78e-11 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 67.60 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 301 LYSHQSRAIHSSIAGRHVAIATSTSSGKSLCYNIPVLESLCQNLMacALYIFPTKALAQDQLRSLLEMKNaLHTDIDVNI 380
Cdd:PRK01172 23 LYDHQRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETFLAGLK--SIYIVPLRSLAMEKYEELSRLRS-LGMRVKISI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 381 YDGDTPREdrtWIRDNARLLITNP---DMLHmsilpcHGQFqrILSNLRYIVIDEAH----SYKGAfgchtalilrRLKR 453
Cdd:PRK01172 100 GDYDDPPD---FIKRYDVVILTSEkadSLIH------HDPY--IINDVGLIVADEIHiigdEDRGP----------TLET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 454 ICSNIYGSHPT--FIFCTATSANprehVMELAKLDNVELIENDGSPCGFKYFLLWnpplhmtkegssKDSLLT---RRSS 528
Cdd:PRK01172 159 VLSSARYVNPDarILALSATVSN----ANELAQWLNASLIKSNFRPVPLKLGILY------------RKRLILdgyERSQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 529 piVEVSYLLSEMVQHGLRCIAFCKTRKLCELVLAYTREILQETA-----------------KELVDTICVYRAGYIAEDR 591
Cdd:PRK01172 223 --VDINSLIKETVNDGGQVLVFVSSRKNAEDYAEMLIQHFPEFNdfkvssennnvyddslnEMLPHGVAFHHAGLSNEQR 300
|
330 340
....*....|....*....|....*..
gi 1002286793 592 RKIEANLFQGKLLGVAATNALELGIDV 618
Cdd:PRK01172 301 RFIEEMFRNRYIKVIVATPTLAAGVNL 327
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
350-655 |
3.13e-11 |
|
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: 67.03 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 350 YIFPTKALAqDQ----LRSLLEMKNALHT-DIDVNIYDGDTPREDRT-WIRDNARLL-----ITNPDMLHMSILPCHGQF 418
Cdd:COG1203 182 YALPFTSII-NQtydrLRDLFGEDVLLHHsLADLDLLEEEEEYESEArWLKLLKELWdapvvVTTIDQLFESLFSNRKGQ 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 419 QRILSNLRY--IVIDEAHSYKGAFgchTALILRRLKRIcsNIYGShpTFIFCTATsaNPREHVMELakLDNVELIENDGS 496
Cdd:COG1203 261 ERRLHNLANsvIILDEVQAYPPYM---LALLLRLLEWL--KNLGG--SVILMTAT--LPPLLREEL--LEAYELIPDEPE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 497 PCGFKYFLLWNPPLHMTKEGSSKDSLLTrrsspivevsyLLSEMVQHGLRCIAFCKTRKLCelvlaytreilQETAKELV 576
Cdd:COG1203 330 ELPEYFRAFVRKRVELKEGPLSDEELAE-----------LILEALHKGKSVLVIVNTVKDA-----------QELYEALK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 577 DT-----ICVYRAGYIAEDRRKIEANL---FQGKLLGVA-ATNALELGIDvghIDATlhLGF--PGSIASLWQQAG---R 642
Cdd:COG1203 388 EKlpdeeVYLLHSRFCPADRSEIEKEIkerLERGKPCILvSTQVVEAGVD---IDFD--VVIrdLAPLDSLIQRAGrcnR 462
|
330
....*....|...
gi 1002286793 643 SGRRAKQSLaIYV 655
Cdd:COG1203 463 HGRKEEEGN-VYV 474
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
280-673 |
4.87e-11 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 66.76 E-value: 4.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 280 ELPnhLSEATREALKSIGVSRLYSHQSRAIHSSI-AGRHVAIATSTSSGKSLCYNIPVLESLCQNlMACALYIFPTKALA 358
Cdd:PRK00254 5 ELR--VDERIKRVLKERGIEELYPPQAEALKSGVlEGKNLVLAIPTASGKTLVAEIVMVNKLLRE-GGKAVYLVPLKALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 359 QDQLRsllEMKNALHTDIDVNIYDGDTPREDRtWIrDNARLLITNPDMLHmSILPcHGqfQRILSNLRYIVIDEAH---S 435
Cdd:PRK00254 82 EEKYR---EFKDWEKLGLRVAMTTGDYDSTDE-WL-GKYDIIIATAEKFD-SLLR-HG--SSWIKDVKLVVADEIHligS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 436 Y-KGAfgchtalilrRLKRICSNIYGsHPTFIFCTATSANPRehvmELAKLDNVELIENDGSPCGFKY------FLLWNP 508
Cdd:PRK00254 153 YdRGA----------TLEMILTHMLG-RAQILGLSATVGNAE----ELAEWLNAELVVSDWRPVKLRKgvfyqgFLFWED 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 509 PlHMTKEGSSKDSLL---------------TRRSSPivEVSYLLSEMVQhglRCIAFCKTRKLCELVlaytrEILQET-- 571
Cdd:PRK00254 218 G-KIERFPNSWESLVydavkkgkgalvfvnTRRSAE--KEALELAKKIK---RFLTKPELRALKELA-----DSLEENpt 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 572 ----AKELVDTICVYRAGYIAEDRRKIEANLFQGKLLGVAATNALELGIDVGHI-----DATLHLGF-----PgsIASLW 637
Cdd:PRK00254 287 neklKKALRGGVAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFrviirDTKRYSNFgwediP--VLEIQ 364
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1002286793 638 QQAGRSGRRA--KQSLAIYVA-FEGP---LDQYFMKFPHKLF 673
Cdd:PRK00254 365 QMMGRAGRPKydEVGEAIIVAtTEEPsklMERYIFGKPEKLF 406
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
542-645 |
4.97e-11 |
|
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: 60.69 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 542 QHGLRCIAFCKTRKLCELvlaytrEILQETAKElvdTICVYRAGYIAEDRRKIEANLFQGKLLGVAATNALELGIDVGHI 621
Cdd:pfam00271 13 ERGGKVLIFSQTKKTLEA------ELLLEKEGI---KVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDV 83
|
90 100
....*....|....*....|....
gi 1002286793 622 DATLHLGFPGSIASLWQQAGRSGR 645
Cdd:pfam00271 84 DLVINYDLPWNPASYIQRIGRAGR 107
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
548-653 |
1.09e-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: 60.30 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 548 IAFCKTRKLCELVLAYTREILQETAkelvdticVYRAGYIAEDRRKIEANLFQGKLLGVAATNALELGIDVGHIDATLHL 627
Cdd:cd18794 34 IIYCLSRKECEQVAARLQSKGISAA--------AYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHY 105
|
90 100
....*....|....*....|....*.
gi 1002286793 628 GFPGSIASLWQQAGRSGRRAKQSLAI 653
Cdd:cd18794 106 SLPKSMESYYQESGRAGRDGLPSECI 131
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
324-679 |
8.24e-10 |
|
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: 61.70 E-value: 8.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 324 TSSGKSLCYNIPVLESLCQNLMACALYIFPTKALAQDQLRSLLEM-----KNALHTDIDVNIYD-GDTPREDRTW---IR 394
Cdd:TIGR01587 8 TGYGKTEAALLWALHSIKSQKADRVIIALPTRATINAMYRRAKELfgselVGLHHSSSFSRIKEmGDSEEFEHLFplyIH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 395 DNARLL-----ITNPDMLHMSILPCHGQFQRILSNLRY--IVIDEAHSYKGAFGCHTALILRRLKRICSNIygshptfIF 467
Cdd:TIGR01587 88 SNDKLFldpitVCTIDQVLKSVFGEFGHYEFTLASIANslLIFDEVHFYDEYTLALILAVLEVLKDNDVPI-------LL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 468 CTATsanprehvmeLAKLdNVELIENDGSPCGFKYFLLWNPPLHmtkegsSKDSLLTRRSSPIVEVSYL--LSEMVQHGL 545
Cdd:TIGR01587 161 MSAT----------LPKF-LKEYAEKIGYVEFNEPLDLKEERRF------ENHRFILIESDKVGEISSLerLLEFIKKGG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 546 RCIAFCKTRKLcelvlayTREILQEtAKELVDT--ICVYRAGYIAEDRRKIEA----NLFQGKLLGVA-ATNALELGIDv 618
Cdd:TIGR01587 224 SIAIIVNTVDR-------AQEFYQQ-LKEKAPEeeIILYHSRFTEKDRAKKEAellrEMKKSNEKFVIvATQVIEASLD- 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002286793 619 ghIDATLHLGFPGSIASLWQQAG---RSGRRAKQSLAIYVAFEGPLDQYFMkFPHKLFGKPIEH 679
Cdd:TIGR01587 295 --ISADVMITELAPIDSLIQRLGrlhRYGRKIGENFEVYIITIAPEGKLFP-YPYELVERTIQK 355
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
286-434 |
5.93e-09 |
|
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: 57.38 E-value: 5.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 286 SEATREALKSI-GVSRLYSHQSRAIHSSIAGRHVAIATSTSSGKSLCYNIPvleSLCQNlmACALYIFPTKALAQDQLRS 364
Cdd:cd18015 3 SGKVKDTLKNVfKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLP---ALCSD--GFTLVVSPLISLMEDQLMA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 365 LLEMknalhtDIDVNIYDGDTPREDRTWI-------RDNARLLITNPDMLH-----MSIL-PCH--GQFQRilsnlryIV 429
Cdd:cd18015 78 LKKL------GISATMLNASSSKEHVKWVhaaltdkNSELKLLYVTPEKIAkskrfMSKLeKAYnaGRLAR-------IA 144
|
....*
gi 1002286793 430 IDEAH 434
Cdd:cd18015 145 IDEVH 149
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
289-433 |
1.68e-08 |
|
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: 55.53 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 289 TREALKSIGVSRLYSHQSRAIHSSIAGRHVAIATSTSSGKSLCYNIPVLESLCQNLMAC-----ALYIFPTKALAQ---D 360
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKgrgpqALVLAPTRELAMqiaE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002286793 361 QLRSLLEmknalHTDIDVN-IYDGDTPREDRTWIRDNARLLITNP----DMLHMsilpchGQFQriLSNLRYIVIDEA 433
Cdd:cd00268 81 VARKLGK-----GTGLKVAaIYGGAPIKKQIEALKKGPDIVVGTPgrllDLIER------GKLD--LSNVKYLVLDEA 145
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
291-433 |
4.37e-08 |
|
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: 55.07 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 291 EALKSIGVSRLYSHQSRAIHSSIAGRHVAIATSTSSGKSLCYNIPVLESLCQNLMAC--------ALYIFPTKALAQdQL 362
Cdd:cd17948 3 EILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAegpfnaprGLVITPSRELAE-QI 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002286793 363 RSLLEmKNALHTDIDVN-IYDGDTPREDRTWIRDNARLLITNPDMLhmsilpCHGQFQRI--LSNLRYIVIDEA 433
Cdd:cd17948 82 GSVAQ-SLTEGLGLKVKvITGGRTKRQIRNPHFEEVDILVATPGAL------SKLLTSRIysLEQLRHLVLDEA 148
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
289-485 |
5.21e-08 |
|
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: 54.22 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 289 TREALKSIGVSRLYSHQSRAIHSSIAGRHVAIATSTSSGKSLCYNIPVLESLCQNLMAC-----ALYIFPTKALAQ---D 360
Cdd:cd17941 1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPedglgALIISPTRELAMqifE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 361 QLRSLlemknALHTDIDVNIYDGDTP-REDRTWIrDNARLLITNPDML--HMSILPCHGqfqriLSNLRYIVIDEAH--- 434
Cdd:cd17941 81 VLRKV-----GKYHSFSAGLIIGGKDvKEEKERI-NRMNILVCTPGRLlqHMDETPGFD-----TSNLQMLVLDEADril 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1002286793 435 --SYKGAfgchtalilrrLKRICSNIYGSHPTFIFctatSANPREHVMELAKL 485
Cdd:cd17941 150 dmGFKET-----------LDAIVENLPKSRQTLLF----SATQTKSVKDLARL 187
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
297-476 |
1.84e-07 |
|
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: 52.64 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 297 GVSRLYSHQSRAIHSSIAGRHVAIATSTSSGKSLCYNIPVLeSLCQNLMACALYIFPTKALAQDQLRSLlemKNAlhtdI 376
Cdd:cd18018 9 GHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPAL-LLRRRGPGLTLVVSPLIALMKDQVDAL---PRA----I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 377 DVNIYDGDTPREDRTWIRDNAR------LLITnPDMLhmsilpCHGQFQRILSNLRYI---VIDEAH-----------SY 436
Cdd:cd18018 81 KAAALNSSLTREERRRILEKLRagevkiLYVS-PERL------VNESFRELLRQTPPIsllVVDEAHcisewshnfrpDY 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1002286793 437 kgafgchtalilRRLKRICSNIYGSHPtFIFCTATsANPR 476
Cdd:cd18018 154 ------------LRLCRVLRELLGAPP-VLALTAT-ATKR 179
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
292-485 |
2.06e-07 |
|
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: 52.59 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 292 ALKSIGVSRLYSHQSRAIHSSIAGRHVAIATSTSSGKSLCYNIPVLES-LCQNLMAC------ALYIFPTKALAQ---DQ 361
Cdd:cd17961 8 AIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKiLKAKAESGeeqgtrALILVPTRELAQqvsKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 362 LRSLLEMKNAlhtDID-VNIYDGDTPREDRTWIRDNARLLITNPdmlhmSILPCHGQFQRI--LSNLRYIVIDEAH---S 435
Cdd:cd17961 88 LEQLTAYCRK---DVRvVNLSASSSDSVQRALLAEKPDIVVSTP-----ARLLSHLESGSLllLSTLKYLVIDEADlvlS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1002286793 436 YkgafGCHTAlilrrLKRICSNIYGSHPTFIfctaTSANPREHVMELAKL 485
Cdd:cd17961 160 Y----GYEED-----LKSLLSYLPKNYQTFL----MSATLSEDVEALKKL 196
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
305-434 |
3.12e-07 |
|
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: 52.09 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 305 QSRAIHSSIAGRH-VAIATSTSSGKSLCYNIPVLESlcqnlMACALYIFPTKALAQDQLRSLLEMKnalhtdIDVNIYDG 383
Cdd:cd18014 18 QEKATMAVVKGNKdVFVCMPTGAGKSLCYQLPALLA-----KGITIVISPLIALIQDQVDHLKTLK------IRVDSLNS 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002286793 384 DTPREDRTWI-------RDNARLLITNPDMLHMSilpchgQFQRILS------NLRYIVIDEAH 434
Cdd:cd18014 87 KLSAQERKRIiadleseKPQTKFLYITPEMAATS------SFQPLLSslvsrnLLSYLVVDEAH 144
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
591-645 |
3.80e-07 |
|
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: 48.47 E-value: 3.80e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1002286793 591 RRKIEANLFQGKLLGVAATNALELGIDVGHIDATLHLGFPGSIASLWQQAGRSGR 645
Cdd:cd18785 11 NSIEHAEEIASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGR 65
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
277-645 |
7.11e-07 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 53.18 E-value: 7.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 277 SFAELPNHLSEATREALKSIGVSRLYSHQSRAIHSSIAGRHVAIATSTSSGKSLCYNIP--VLESLcqnlmacALYIFPT 354
Cdd:PRK11057 2 AQAEVLNLESLAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPalVLDGL-------TLVVSPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 355 KALAQDQLRSLLEmknalhTDIDVNIYDGDTPREDR--TWIRDNA---RLLITNPDMLHMSilpchgQFQRILSNLR--Y 427
Cdd:PRK11057 75 ISLMKDQVDQLLA------NGVAAACLNSTQTREQQleVMAGCRTgqiKLLYIAPERLMMD------NFLEHLAHWNpaL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 428 IVIDEAH-----------SYKGafgchtaliLRRLKRICSNIygshpTFIFCTATSAnprehvmELAKLDNVELIEndgs 496
Cdd:PRK11057 143 LAVDEAHcisqwghdfrpEYAA---------LGQLRQRFPTL-----PFMALTATAD-------DTTRQDIVRLLG---- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 497 pcgfkyflLWNPPLHMtkegSSKDS-----LLTRRSSPIVEVSYLLSEmvQHGLRCIAFCKTRKLCElvlaytreilqET 571
Cdd:PRK11057 198 --------LNDPLIQI----SSFDRpniryTLVEKFKPLDQLMRYVQE--QRGKSGIIYCNSRAKVE-----------DT 252
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002286793 572 AKELVD---TICVYRAGYIAEDRRKIEANLFQGKLLGVAATNALELGIDVGHIDATLHLGFPGSIASLWQQAGRSGR 645
Cdd:PRK11057 253 AARLQSrgiSAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGR 329
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
285-433 |
1.85e-06 |
|
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: 49.89 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 285 LSEATREALKSIGVSRLYSHQSRAIHSSIAGRH--VAIAtSTSSGKSLCYNIPVLESLCQNLMAC------ALYIFPTKA 356
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILSTGDdvLARA-KTGTGKTLAFLLPAIQSLLNTKPAGrrsgvsALIISPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 357 LAQ---DQLRSLLEMknalHTDIDVNIYDGDTPR--EDRTWIRDNARLLITNPDMLHMSILPCHgqFQRILSNLRYIVID 431
Cdd:cd17964 80 LALqiaAEAKKLLQG----LRKLRVQSAVGGTSRraELNRLRRGRPDILVATPGRLIDHLENPG--VAKAFTDLDYLVLD 153
|
..
gi 1002286793 432 EA 433
Cdd:cd17964 154 EA 155
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
350-471 |
2.93e-06 |
|
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: 48.83 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 350 YIFPTKALAQ---DQLRSLLEMKNA------LHTDIDVNIYD-----GDTPREDRTWIRDNARLL-----ITNPDMLHMS 410
Cdd:cd17930 36 YALPTRATINqmyERIREILGRLDDedkvllLHSKAALELLEsdeepDDDPVEAVDWALLLKRSWlapivVTTIDQLLES 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002286793 411 ILPcHGQFQRILSNL--RYIVIDEAHSYKGAFgchTALILRRLKRICSNIYGshpTFIFCTAT 471
Cdd:cd17930 116 LLK-YKHFERRLHGLanSVVVLDEVQAYDPEY---MALLLKALLELLGELGG---PVVLMTAT 171
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
324-679 |
3.47e-06 |
|
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: 50.51 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 324 TSSGKSLCYNIPVLESLCQNLMACALYIFPTKALAQDQLRSLLEM---KNALHTDIDV-NIYD-GDTPREDRTW---IRD 395
Cdd:cd09639 8 TGYGKTEAALLWALHSLKSQKADRVIIALPTRATINAMYRRAKEAfgeTGLYHSSILSsRIKEmGDSEEFEHLFplyIHS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 396 NARLL-----ITNPDMLHMSILPCHGQFQRILSNLRY--IVIDEAHSYKGAFGCHTALILRRLKRICSNIygshptfIFC 468
Cdd:cd09639 88 NDTLFldpitVCTIDQVLKSVFGEFGHYEFTLASIANslLIFDEVHFYDEYTLALILAVLEVLKDNDVPI-------LLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 469 TATSAnprEHVMELAKldNVELIENDGSP--CGFKYFLLWnpplHMTKEGSSKDSLLTRrsspivevsylLSEMVQHGLR 546
Cdd:cd09639 161 SATLP---KFLKEYAE--KIGYVEENEPLdlKPNERAPFI----KIESDKVGEISSLER-----------LLEFIKKGGS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 547 CIAFCKTRKLcelvlayTREILQEtAKELVDT--ICVYRAGYIAEDRRKIEANL---FQGKLLGVA-ATNALELGIDvgh 620
Cdd:cd09639 221 VAIIVNTVDR-------AQEFYQQ-LKEKGPEeeIMLIHSRFTEKDRAKKEAELlleFKKSEKFVIvATQVIEASLD--- 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 621 IDATLHLGFPGSIASLWQQAGRSGRRA-KQSLAIYVAFEGPLDQYFMKFPHKLFGKPIEH 679
Cdd:cd09639 290 ISVDVMITELAPIDSLIQRLGRLHRYGeKNGEEVYIITDAPDGKGQKPYPYDLVERTIEL 349
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
305-433 |
5.55e-06 |
|
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: 48.09 E-value: 5.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 305 QSRAIHSSIAGRHVaIATSTS-SGKSLCYNIPVLESLCQNLMAC-ALYIFPTKALA---QDQLRSLlemknALHTDIDVN 379
Cdd:cd17939 24 QQRAIVPIIKGRDV-IAQAQSgTGKTATFSIGALQRIDTTVRETqALVLAPTRELAqqiQKVVKAL-----GDYMGVKVH 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002286793 380 IYDGDTP-REDRTWIRDNARLLITNP----DMLHMSILpchgqfqrILSNLRYIVIDEA 433
Cdd:cd17939 98 ACIGGTSvREDRRKLQYGPHIVVGTPgrvfDMLQRRSL--------RTDKIKMFVLDEA 148
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
277-433 |
1.71e-05 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 48.60 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 277 SFAELPnhLSEATREALKSIGvsrlYSH----QSRAIHSSIAGRHV-AIAtSTSSGKSLCYNIPVLESLCQNLMAC--AL 349
Cdd:COG0513 3 SFADLG--LSPPLLKALAELG----YTTptpiQAQAIPLILAGRDVlGQA-QTGTGKTAAFLLPLLQRLDPSRPRApqAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 350 YIFPTKALAQ---DQLRSLLEmknalHTDIDVN-IYDGDTPREDRTWIRDNARLLITNP----DMLHMSILpchgqfqrI 421
Cdd:COG0513 76 ILAPTRELALqvaEELRKLAK-----YLGLRVAtVYGGVSIGRQIRALKRGVDIVVATPgrllDLIERGAL--------D 142
|
170
....*....|..
gi 1002286793 422 LSNLRYIVIDEA 433
Cdd:COG0513 143 LSGVETLVLDEA 154
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
285-439 |
3.11e-05 |
|
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: 46.05 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 285 LSEATREALKSIGVSRLYSHQSRAIHSSIA--GRHVAIATSTSSGKSLCYNIPVL-ESLCQNLMacALYIFPTKALAQDQ 361
Cdd:cd18026 1 LPDAVREAYAKKGIKKLYDWQKECLSLPGLleGRNLVYSLPTSGGKTLVAEILMLkRLLERRKK--ALFVLPYVSIVQEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 362 LRSLLEMKNALHtdIDVNIYDGDTPRedRTWIRDNAR-LLITNPDMLHMsiLPCHGQFQRILSNLRYIVIDEAH----SY 436
Cdd:cd18026 79 VDALSPLFEELG--FRVEGYAGNKGR--SPPKRRKSLsVAVCTIEKANS--LVNSLIEEGRLDELGLVVVDELHmlgdGH 152
|
...
gi 1002286793 437 KGA 439
Cdd:cd18026 153 RGA 155
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
300-494 |
3.31e-05 |
|
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: 45.40 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 300 RLYSHQSRAIHSSIA-GRHVAIATSTSSGKSLCYNIPVLESLCQNLMAcaLYIFPTKALAQDQLRsllEMKNALHTDIDV 378
Cdd:cd18028 1 ELYPPQAEAVRAGLLkGENLLISIPTASGKTLIAEMAMVNTLLEGGKA--LYLVPLRALASEKYE---EFKKLEEIGLKV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 379 NIYDGDTPREDRtWIrDNARLLITNPDMLHmSILPcHGqfQRILSNLRYIVIDEAH---SYKGafGCHTALILRRLKRIC 455
Cdd:cd18028 76 GISTGDYDEDDE-WL-GDYDIIVATYEKFD-SLLR-HS--PSWLRDVGVVVVDEIHlisDEER--GPTLESIVARLRRLN 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 1002286793 456 SNiygshPTFIFCTATSANPRehvmELAKLDNVELIEND 494
Cdd:cd18028 148 PN-----TQIIGLSATIGNPD----ELAEWLNAELVESD 177
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
278-365 |
3.48e-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: 46.06 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 278 FAELPnhLSEATREALKSIGVSRLYSHQSRAIHSSIAGRHVAIATSTSSGKSLCYNIPVLESLCQNLMAC-ALYIFPTKA 356
Cdd:cd17955 1 FEDLG--LSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIfALVLTPTRE 78
|
90
....*....|..
gi 1002286793 357 LA-Q--DQLRSL 365
Cdd:cd17955 79 LAyQiaEQFRAL 90
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
305-476 |
3.90e-05 |
|
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ATP-dependent helicase or WRN) 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 Werner's syndrome.
Pssm-ID: 350775 [Multi-domain] Cd Length: 193 Bit Score: 45.54 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 305 QSRAIHSSI-AGRHVAIATSTSSGKSLCYNIPVLesLCQNLmacALYIFPTKALAQDQLRSlLEMKNalhtdIDVNIYDG 383
Cdd:cd18017 17 QWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSV--LLNSL---TLVISPLISLMEDQVLQ-LVMSN-----IPACFLGS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 384 DTPREDRTWIRDNA-RLLITNPDMLHMSIlpchGQFQRILSNLRYIVIDEA-------HSYKGAFGChtaliLRRLKRIC 455
Cdd:cd18017 86 AQSQNVLDDIKMGKiRVIYVTPEFVSKGL----ELLQQLRNGITLIAIDEAhcvsqwgHDFRSSYRH-----LGSIRNRL 156
|
170 180
....*....|....*....|.
gi 1002286793 456 SNIygshpTFIFCTATsANPR 476
Cdd:cd18017 157 PNV-----PIVALTAT-ATPS 171
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
289-433 |
4.19e-05 |
|
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: 45.81 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 289 TREALKSIGVSRLYSHQSRAIHSSIAGRHVAIATSTSSGKSLCYNIPVLESLCQ------NLMACaLYIFPTKALAQ--- 359
Cdd:cd17942 1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKlkfkprNGTGV-IIISPTRELALqiy 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002286793 360 DQLRSLLemknALHTDIDVNIYDGDTPREDRTWIRDNARLLITNPDML--HMSILPchgQFqrILSNLRYIVIDEA 433
Cdd:cd17942 80 GVAKELL----KYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLldHLQNTK---GF--LYKNLQCLIIDEA 146
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
294-434 |
1.47e-04 |
|
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) 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 in RecQ2 cause Bloom syndrome.
Pssm-ID: 350774 [Multi-domain] Cd Length: 208 Bit Score: 44.05 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 294 KSIGVSRLYSHQSRAIHSSIAGRHVAIATSTSSGKSLCYNIPVLESlcqnlMACALYIFPTKALAQDQLRSLLEMknalh 373
Cdd:cd18016 11 KKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVS-----PGVTVVISPLRSLIVDQVQKLTSL----- 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002286793 374 tDIDVNIYDGDTPREDRTWI-----RDNA--RLLITNPDMLHMSilpchGQFQRILSNL-------RYiVIDEAH 434
Cdd:cd18016 81 -DIPATYLTGDKTDAEATKIylqlsKKDPiiKLLYVTPEKISAS-----NRLISTLENLyerkllaRF-VIDEAH 148
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
285-451 |
1.55e-04 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 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: 350717 [Multi-domain] Cd Length: 205 Bit Score: 44.22 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 285 LSEATREALKSIGVSRLYSHQSRAIHSSIAGRHVAIATSTSSGKSLCYNIPVLESL---CQNLMACALYIFPTKALAQDQ 361
Cdd:cd17959 8 LSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLkahSPTVGARALILSPTRELALQT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 362 LRSLLEMknALHTDIDVN-IYDGDTPREDRTWIRDNARLLITNPD-MLHMSIlpchgQFQRILSNLRYIVIDEAHS-YKG 438
Cdd:cd17959 88 LKVTKEL--GKFTDLRTAlLVGGDSLEEQFEALASNPDIIIATPGrLLHLLV-----EMNLKLSSVEYVVFDEADRlFEM 160
|
170
....*....|...
gi 1002286793 439 AFGCHTALILRRL 451
Cdd:cd17959 161 GFAEQLHEILSRL 173
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
279-616 |
1.90e-04 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 45.33 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 279 AELPnhLSEATREALKSIGVSRLYSHQSRAIHSSIA-GRHVAIATSTSSGKSLCYNIPVLESLCQNlmACALYIFPTKAL 357
Cdd:PRK02362 4 AELP--LPEGVIEFYEAEGIEELYPPQAEAVEAGLLdGKNLLAAIPTASGKTLIAELAMLKAIARG--GKALYIVPLRAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 358 AQDQLRsllEMKNALHTDIDVNIYDGDTPREDRtWIRDNARLLITNP--DMLHMSILPChgqfqriLSNLRYIVIDEAHs 435
Cdd:PRK02362 80 ASEKFE---EFERFEELGVRVGISTGDYDSRDE-WLGDNDIIVATSEkvDSLLRNGAPW-------LDDITCVVVDEVH- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 436 ykgafgchtaLI---------------LRRLKRICSNIYGShptfifctATSANPRehvmELAKLDNVELIENDGSPCGF 500
Cdd:PRK02362 148 ----------LIdsanrgptlevtlakLRRLNPDLQVVALS--------ATIGNAD----ELADWLDAELVDSEWRPIDL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 501 KYFLLWNPPLHMTKegsSKDSLLTRRSSPIVEvsyLLSEMVQHGLRCIAFCKTRKLCE------------LVLAYTREIL 568
Cdd:PRK02362 206 REGVFYGGAIHFDD---SQREVEVPSKDDTLN---LVLDTLEEGGQCLVFVSSRRNAEgfakraasalkkTLTAAERAEL 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002286793 569 QETAKELVDT----------ICVYR------AGYIAEDRRKIEANLFQGKLLGVAATNALELGI 616
Cdd:PRK02362 280 AELAEEIREVsdtetskdlaDCVAKgaafhhAGLSREHRELVEDAFRDRLIKVISSTPTLAAGL 343
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
514-646 |
2.10e-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: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 514 KEGSSKDSLLTRRSSPIVEVSYLLSEMVQHGLRCIAFCKTRKLCELvlaytreilqeTAKELVDtICVYRAGYIAEDRRK 593
Cdd:cd18795 13 NGLGIKLRVDVMNKFDSDIIVLLKIETVSEGKPVLVFCSSRKECEK-----------TAKDLAG-IAFHHAGLTREDREL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002286793 594 IEaNLFQGKLLGV-AATNALELGID------VghIDATLHLGFPG----SIASLWQQAGRSGRR 646
Cdd:cd18795 81 VE-ELFREGLIKVlVATSTLAAGVNlpartvI--IKGTQRYDGKGyrelSPLEYLQMIGRAGRP 141
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
305-433 |
2.64e-04 |
|
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: 43.44 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 305 QSRAIHSSIAGRHVAIATSTSSGKSLCYNIPVLESLCQNLMAC-ALYIFPTKALAQDQLRSLLEMknALHTDIDVNIYDG 383
Cdd:cd17940 26 QEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIqALILVPTRELALQTSQVCKEL--GKHMGVKVMVTTG 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1002286793 384 DTP-REDRTWIRDNARLLITNPDmlhmSILPCHGQFQRILSNLRYIVIDEA 433
Cdd:cd17940 104 GTSlRDDIMRLYQTVHVLVGTPG----RILDLAKKGVADLSHCKTLVLDEA 150
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
289-432 |
2.76e-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: 43.30 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 289 TREALKSIGVSRLYSHQSRAIHSSIAGRHVAIATSTSSGKSLCYNIPVLESLCQNLMACA-------LYIFPTKALAQDQ 361
Cdd:cd17944 1 TIKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKrgrapkvLVLAPTRELANQV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002286793 362 LRSLLEMKNALhtdiDVNIYDGDTPREDRTW-IRDNARLLITNPDMLHMsilpcHGQFQRI-LSNLRYIVIDE 432
Cdd:cd17944 81 TKDFKDITRKL----SVACFYGGTPYQQQIFaIRNGIDILVGTPGRIKD-----HLQNGRLdLTKLKHVVLDE 144
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
305-474 |
1.44e-03 |
|
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: 41.19 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 305 QSRAIHSSI-AGRHVAIATSTSSGKSLCYNIPVLESLCQNLMAC-----ALYIFPTKALAQDQLRSLLEMKNALhtDIDV 378
Cdd:cd18023 6 QSEVFPDLLySDKNFVVSAPTGSGKTVLFELAILRLLKERNPLPwgnrkVVYIAPIKALCSEKYDDWKEKFGPL--GLSC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 379 NIYDGDTPREDrTWIRDNARLLITNPDMLHmSILPCHGQFQRILSNLRYIVIDEAHSYKGAFGCHTALILRRLKRICSNI 458
Cdd:cd18023 84 AELTGDTEMDD-TFEIQDADIILTTPEKWD-SMTRRWRDNGNLVQLVALVLIDEVHIIKENRGATLEVVVSRMKTLSSSS 161
|
170 180
....*....|....*....|.
gi 1002286793 459 YGSHPT-----FIFCTATSAN 474
Cdd:cd18023 162 ELRGSTvrpmrFVAVSATIPN 182
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
292-433 |
2.41e-03 |
|
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 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: 350705 [Multi-domain] Cd Length: 196 Bit Score: 40.32 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 292 ALKSIGVSRLYSHQSRAIHSSIAGRHVAIATSTSSGKSLCYNIPVLESLC----QNLMACALYIFPTKALA---QDQLRS 364
Cdd:cd17947 4 ALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLyrpkKKAATRVLVLVPTRELAmqcFSVLQQ 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002286793 365 LlemknALHTDIDVN-IYDGDTPREDRTWIRDNARLLITNP----DMLHMSIlpchgQFQriLSNLRYIVIDEA 433
Cdd:cd17947 84 L-----AQFTDITFAlAVGGLSLKAQEAALRARPDIVIATPgrliDHLRNSP-----SFD--LDSIEILVLDEA 145
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
277-433 |
2.95e-03 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 41.37 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 277 SFAELpnHLSEATREALKSIGVSRLYSHQSRAIHSSIAGRHVAIATSTSSGKSLCYNIPVLESLCQNLMACALYIF-PTK 355
Cdd:PRK11634 7 TFADL--GLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLaPTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 356 ALAQDQLRSLLEMKNALHTDIDVNIYDGDTPREDRTWIRDNARLLITNPDML--HMSilpcHGQFQriLSNLRYIVIDEA 433
Cdd:PRK11634 85 ELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLldHLK----RGTLD--LSKLSGLVLDEA 158
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
305-433 |
3.04e-03 |
|
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: 40.30 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 305 QSRAIHSSIAGRHVAI-ATSTSSGKSLCYNIPVLESLCQNLM----------ACALYIFPTKALA---QDQLRSLLEmkn 370
Cdd:cd17946 17 QALALPAAIRDGKDVIgAAETGSGKTLAFGIPILERLLSQKSsngvggkqkpLRALILTPTRELAvqvKDHLKAIAK--- 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002286793 371 alHTDIDVNIYDG--DTPREDRTwIRDNARLLITNPDMLhMSILPCHGQFQRILSNLRYIVIDEA 433
Cdd:cd17946 94 --YTNIKIASIVGglAVQKQERL-LKKRPEIVVATPGRL-WELIQEGNEHLANLKSLRFLVLDEA 154
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
305-433 |
3.51e-03 |
|
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: 39.74 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 305 QSRAIHSSIAGRHVAIATSTSSGKSLCYNIPVLESLCQNLMAC-ALYIFPTKALAQDQLRSLLemknALHTDIDVNIY-- 381
Cdd:cd18046 26 QQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATqALVLAPTRELAQQIQKVVM----ALGDYMGIKCHac 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002286793 382 -DGDTPREDRTWIRDNARLLITNP----DMLHmsilpchgqfQRILS--NLRYIVIDEA 433
Cdd:cd18046 102 iGGTSVRDDAQKLQAGPHIVVGTPgrvfDMIN----------RRYLRtdYIKMFVLDEA 150
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
289-433 |
4.76e-03 |
|
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: 39.48 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 289 TREALKSIGVSRLYSHQSRAIHSSIAGRHVAIATSTSSGKSLCYNIPVLESLCQNLMAC------ALYIFPTKALAQdQL 362
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLkkgqvgALIISPTRELAT-QI 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002286793 363 RSLLE-MKNALHTDIDVNIYDG--DTPREDRTWIRDNARLLITNP----DMLHMSilpchgQFQRILSNLRYIVIDEA 433
Cdd:cd17960 80 YEVLQsFLEHHLPKLKCQLLIGgtNVEEDVKKFKRNGPNILVGTPgrleELLSRK------ADKVKVKSLEVLVLDEA 151
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
285-433 |
5.39e-03 |
|
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 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: 350711 [Multi-domain] Cd Length: 222 Bit Score: 39.67 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 285 LSEATREALKSIGVSRLYSHQSRAIHSSIAGRHVAIATSTSSGKSLCYNIPVLESLCQNLM------ACALYIFPTKALA 358
Cdd:cd17953 19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPvkpgegPIGLIMAPTRELA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 359 QDQLRSLLEMKNALHTDIdVNIYDGDTPREDRTWIRDNARLLITNP----DMLHMSilpchgqfQRILSNLR---YIVID 431
Cdd:cd17953 99 LQIYVECKKFSKALGLRV-VCVYGGSGISEQIAELKRGAEIVVCTPgrmiDILTAN--------NGRVTNLRrvtYVVLD 169
|
..
gi 1002286793 432 EA 433
Cdd:cd17953 170 EA 171
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
301-434 |
6.72e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 38.42 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286793 301 LYSHQSRAIHSSIAG-----RHVAIATSTSSGKSLCYnipvlESLCQNLMAC-----ALYIFPTKALAqDQLRSllEMKN 370
Cdd:pfam04851 4 LRPYQIEAIENLLESikngqKRGLIVMATGSGKTLTA-----AKLIARLFKKgpikkVLFLVPRKDLL-EQALE--EFKK 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002286793 371 ALHTDIDVN-IYDGDTPREdrtwIRDNARLLITNPDMLHMSIlpcHGQFQRILSNLR-YIVIDEAH 434
Cdd:pfam04851 76 FLPNYVEIGeIISGDKKDE----SVDDNKIVVTTIQSLYKAL---ELASLELLPDFFdVIIIDEAH 134
|
|
| |
