|
Name |
Accession |
Description |
Interval |
E-value |
| DEXXQc_HELZ2-N |
cd18076 |
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
760-990 |
9.12e-129 |
|
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB, and RXRA. It belongs to 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: 350834 [Multi-domain] Cd Length: 230 Bit Score: 403.89 E-value: 9.12e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 760 RGNHKQKLAVGLIAGRRPEGTKhIPPLLIYGPFGTGKTYTLAMAALEVVQQPHTKVLICTHTNSAADIYIREYFHDYVSS 839
Cdd:cd18076 1 AGNNKQQLAFNFIAGKPSEARF-VPPLLIYGPFGTGKTFTLAMAALEVIREPGTKVLICTHTNSAADIYIREYFHPYVDK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 840 GHPEATPLRVMYADRPPRQTDPTTLQYCCLTEDRQAFRPPTGPELVHHRLVVTTTSQARELQVPAGFFSHIFIDEAAQML 919
Cdd:cd18076 80 GHPEARPLRIKATDRPNAITDPDTITYCCLTKDRQCFRLPTRDELDFHNIVITTTAMAFNLHVLSGFFTHIFIDEAAQML 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568920187 920 ECEALIPLSYALSLTRVVLAGDHMQVTPRLFSVPRDKSARHTLLHRLFLYYQQEAHKIAQQSRIIFHENYR 990
Cdd:cd18076 160 ECEALIPLSYAGPKTRVVLAGDHMQMTPKLFSVADYNRANHTLLNRLFHYYQGEKHEVAVKSRVIFSENYR 230
|
|
| DEXXc_HELZ2-C |
cd18040 |
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
2448-2724 |
1.84e-124 |
|
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB and RXRA. It belongs to 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: 350798 [Multi-domain] Cd Length: 271 Bit Score: 393.43 E-value: 1.84e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2448 KLNQSQDRAVRSALQKQFTVIQGPPGTGKTVVGFHIVYWFHRSNQEQmptdsSPSGEEQLGGPCVLYCGPSNKSVDVLGG 2527
Cdd:cd18040 1 KLNPSQNHAVRTALTKPFTLIQGPPGTGKTVTGVHIAYWFAKQNREI-----QSVSGEGDGGPCVLYCGPSNKSVDVVAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2528 LLLRRKtEMKPLRVYGEQAEATEFPLPGVSnRSLFGKTSQEGRPNQSLRSITLHHRIRQAPNPYAAEIRKFDAQL-REGK 2606
Cdd:cd18040 76 LLLKVP-GLKILRVYSEQIETTEYPIPNEP-RHPNKKSERESKPNSELSSITLHHRIRQPSNPHSQQIKAFEARFeRTQE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2607 IFSKEDLRVYRRVLGKARKHELERHSVILCTCSCAASKSLK-ILNVRQILIDEAGMATEPETLIPLVCFsKTVEKVVLLG 2685
Cdd:cd18040 154 KITEEDIKTYKILIWEARFEELETVDVILCTCSEAASQKMRtHANVKQCIVDECGMCTEPESLIPIVSA-PRAEQVVLIG 232
|
250 260 270
....*....|....*....|....*....|....*....
gi 568920187 2686 DHKQLRPVVKSEQLQSLGMDRSLFERYHRDAIMLDTQYR 2724
Cdd:cd18040 233 DHKQLRPVVQNKEAQKLGLGRSLFERYAEKACMLDTQYR 271
|
|
| RNB |
smart00955 |
This domain is the catalytic domain of ribonuclease II; |
1567-1924 |
2.35e-70 |
|
This domain is the catalytic domain of ribonuclease II;
Pssm-ID: 214935 [Multi-domain] Cd Length: 286 Bit Score: 238.71 E-value: 2.35e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1567 REDYRHFLTFTVDPQGACNLDDALSVRDLGP-VYEVAVHIADVASLVPKDGALDVEARQQGTVFYAPNRePVLMLPASLC 1645
Cdd:smart00955 1 RVDLRDLPLFTIDPEDAKDIDDAVSVEKLDNgGYRLGVHIADVSHYVKPGSALDREARKRGTSVYLPDR-VIPMLPEELS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1646 QDALSLLPGQDRLAISLFLTMEKGGGQIKSLRFAPSIIRSDRQLSYEEAEELIKRHpgaglelpaHLDSVEACVvaacyf 1725
Cdd:smart00955 80 NGLCSLNPGEDRLALSVEMTLDADGGEILDYEFYRSVIRSKARLTYEEVDAILEKI---------VLDEEGKIE------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1726 sWMLRRQRLsaacyyeppdedsvlgfrTAHIMVQEYMIQFNSHVAEFLVSNKHTqtlTPLRWQPTPSRQQLDSVFKKYRG 1805
Cdd:smart00955 145 -DIVPRERN------------------DAHSLVEEFMILANEAVARFLAKNGIP---GLYRVHEGPDPEKLAELLKEFLA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1806 LVPLSLhlchhsntdytpnkqlhlltslwkqvQLAAGTQDYSQMVDLIAaddMHPSLAPACLDLRRALGRSVFGRSSQGk 1885
Cdd:smart00955 203 LLGLLL--------------------------LGGDGPKALAKLLEKIR---DSPEERLLELLLLRSMPHAEYSVDNSG- 252
|
330 340 350
....*....|....*....|....*....|....*....
gi 568920187 1886 qqpavHHSLQVDWYTWATSPIRRYLDVVLQRLILLALGH 1924
Cdd:smart00955 253 -----HFGLALDAYTHFTSPIRRYPDLIVHRQLKAALRG 286
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
2704-2909 |
4.98e-65 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Pssm-ID: 463780 [Multi-domain] Cd Length: 196 Bit Score: 219.73 E-value: 4.98e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2704 MDRSLFER----YHRDAIMLDTQYRMHKDICSFPSVEFYGGKLKTWSDLR-RLPSILGHTGKPSCSVIFGSVQGHEQKll 2778
Cdd:pfam13087 1 LDRSLFERlqelGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAeRPLPDDFHLPDPLGPLVFIDVDGSEEE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2779 vstEDGNENSRANPEEVTQVVRIIKQLTLDRTVDPKDIAVLTPYNAQAAAISRGLMQRGVT--GVTVTSITKSQGSEWRY 2856
Cdd:pfam13087 79 ---ESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSDIGVITPYRAQVRLIRKLLKRKLGGklEIEVNTVDGFQGREKDV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568920187 2857 VIVSTVRTCPRSDVdqrptkswlkkflGFVVDPHQVNVAITRAQEALCIIGDH 2909
Cdd:pfam13087 156 IIFSCVRSNEKGGI-------------GFLSDPRRLNVALTRAKRGLIIVGNA 195
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
2539-2928 |
2.12e-57 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 216.15 E-value: 2.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2539 LRVYGEQAEATEFPLPGVSNRSLFGKTSQEGRPNQSLRSITLHHRIRQAPNPYAAEIRKFDAQLREGKIFSKEdLRVYRR 2618
Cdd:COG1112 444 LAAALAALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPEELEKLIAELREAARLRRALRRE-LKKRRE 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2619 VLGKARKHELERHSVILCTC-SCAASKSLKILNVRQILIDEAGMATEPETLIPLVCFsktvEKVVLLGDHKQLRPVVKSE 2697
Cdd:COG1112 523 LRKLLWDALLELAPVVGMTPaSVARLLPLGEGSFDLVIIDEASQATLAEALGALARA----KRVVLVGDPKQLPPVVFGE 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2698 ---QLQSLGMDRSLFER----YHRDAIMLDTQYRMHKDICSFPSVEFYGGKLKTwsdlrrLPSILGHTGK-PSCSVIFGS 2769
Cdd:COG1112 599 eaeEVAEEGLDESLLDRllarLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVP------LPSPKARRLAdPDSPLVFID 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2770 VQGHEQKllvstedgNENSRANPEEVTQVVRIIKQLtLDRTVDPKDIAVLTPYNAQAAAISRGLMQR---GVTGVTVTSI 2846
Cdd:COG1112 673 VDGVYER--------RGGSRTNPEEAEAVVELVREL-LEDGPDGESIGVITPYRAQVALIRELLREAlgdGLEPVFVGTV 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2847 TKSQGSEWRYVIVSTVRTcPRSDVDQRptkswlkkfLGFVV-DPHQVNVAITRAQEALCIIGDHLLLRCCP---LWHRLL 2922
Cdd:COG1112 744 DRFQGDERDVIIFSLVYS-NDEDVPRN---------FGFLNgGPRRLNVAVSRARRKLIVVGSRELLDSDPstpALKRLL 813
|
....*.
gi 568920187 2923 DFCEAQ 2928
Cdd:COG1112 814 EYLERA 819
|
|
| RNB |
pfam00773 |
RNB domain; This domain is the catalytic domain of ribonuclease II. |
1567-1922 |
2.31e-57 |
|
RNB domain; This domain is the catalytic domain of ribonuclease II.
Pssm-ID: 459934 [Multi-domain] Cd Length: 314 Bit Score: 202.51 E-value: 2.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1567 REDYRHFLTFTVDPQGACNLDDALSVRDLGPV-YEVAVHIADVASLVPKDGALDVEARQQGTVFYAPNRepVL-MLPASL 1644
Cdd:pfam00773 1 RKDLRDLPFITIDPADAKDLDDAISVEKLPNGgYRLGVHIADVSHYVPPGSPLDREARKRGTSVYLPDR--VIpMLPEKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1645 CQDALSLLPGQDRLAISLFLTMEKgGGQIKSLRFAPSIIRSDRQLSYEEAEELIKRhPGAGLELPAHLDSVEacvvAACY 1724
Cdd:pfam00773 79 SNDLCSLNPGEDRLALSVEITIDA-DGEVTSYEIYPSVIRSKARLTYEEVDDLLEG-KDAEKDKPDLAEDLR----LLYE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1725 FSWMLRRQRLSA-ACYYEPP------DEDSVLGFRT-----AHIMVQEYMIQFNSHVAEFLVSNKHTqtlTPLRWQPTPS 1792
Cdd:pfam00773 153 LAKILRAKRLQRgALDLDTPenklilDEEGVIDILIqertdAHSLIEEFMLLANEAVARHLQELGIP---ALYRVHPEPD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1793 RQQLDsvfkkyrglvplslhlchhsntdytpnkqlhlltSLWKQVQLAAGTQDYSQMVDLIAADDMHPSLApacldLRRA 1872
Cdd:pfam00773 230 LEKLN----------------------------------SLIKLLQLLPDDKGLSKSLEKIKDDERLLSIL-----LLRT 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 568920187 1873 LGRSVFGrssqgkQQPAVHHSLQVDWYTWATSPIRRYLDVVLQRLILLAL 1922
Cdd:pfam00773 271 MPRAEYS------PEPLGHFGLGLDIYTHFTSPIRRYPDLIVHRQLKALL 314
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
2452-2697 |
6.56e-57 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Pssm-ID: 404072 [Multi-domain] Cd Length: 248 Bit Score: 198.72 E-value: 6.56e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2452 SQDRAVRSALQKQ-FTVIQGPPGTGKTvvgFHIVYWFHRSNqeqmptdsSPSGEEQLGGPCVLYCGPSNKSVDVLGGLLL 2530
Cdd:pfam13086 1 SQREAIRSALSSShFTLIQGPPGTGKT---TTIVELIRQLL--------SYPATSAAAGPRILVCAPSNAAVDNILERLL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2531 R--RKTEMKPLRVYGEQAeatefplPGVSNRSLFGKTSQEGRPNQSlRSITLHHRIRQAPNPYAAEIRKFDAQ-----LR 2603
Cdd:pfam13086 70 RkgQKYGPKIVRIGHPAA-------ISEAVLPVSLDYLVESKLNNE-EDAQIVKDISKELEKLAKALRAFEKEiivekLL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2604 EGKIFSKEDLRVYRRVLGKARK---------------HELERHSVILCTCSCAASKSLKIL-NVRQILIDEAGMATEPET 2667
Cdd:pfam13086 142 KSRNKDKSKLEQERRKLRSERKelrkelrrreqslerEILDEAQIVCSTLSGAGSRLLSSLaNFDVVIIDEAAQALEPST 221
|
250 260 270
....*....|....*....|....*....|
gi 568920187 2668 LIPLVCFSKtveKVVLLGDHKQLRPVVKSE 2697
Cdd:pfam13086 222 LIPLLRGPK---KVVLVGDPKQLPPTVISK 248
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
2449-2936 |
5.01e-51 |
|
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273041 [Multi-domain] Cd Length: 636 Bit Score: 193.49 E-value: 5.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2449 LNQSQDRAVRSAL-QKQFTVIQGPPGTGKTVVGFHIVywfhrsNQEQMPtdsspsgeeqlgGPCVLYCGPSNKSVDVLGG 2527
Cdd:TIGR00376 158 LNESQKEAVLFALsSKDLFLIHGPPGTGKTRTVVELI------RQLVKR------------GLRVLVTAPSNIAVDNLLE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2528 LLLrrKTEMKPLRVyGEQA----EATEFPLPGVSNRSLFGKTSQEGRpnQSLRSITLHHRIRQAPNPyaaEIRKF--DAQ 2601
Cdd:TIGR00376 220 RLA--LCDQKIVRL-GHPArllkSNKQHSLDYLIENHPKYQIVADIR--EKIDELIEERNKKTKPSP---QKRRGlsDIK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2602 L-------REGKIFSKEDLRVYRRV--LGKARKHEL------------ERHSVILCTCSCAASKSLKILNVRQILIDEAG 2660
Cdd:TIGR00376 292 IlrkalkkREARGIESLKIASMAEWieTNKSIDRLLkllpeseerimnEILAESDATNSMAGSEILNGQYFDVAVIDEAS 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2661 MATEPETLIPLVcfskTVEKVVLLGDHKQLRPVVKSEQLQSLgmDRSLFER----YHRDAIMLDTQYRMHKDICSFPSVE 2736
Cdd:TIGR00376 372 QAMEPSCLIPLL----KARKLILAGDHKQLPPTILSHDAEEL--SLTLFERlikeYPERSRTLNVQYRMNQKIMEFPSRE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2737 FYGGKLKTWSD-----LRRLPS--------ILGhTGKPscsVIFGSVQGHEqklLVSTEDGNENSRANPEEVTQVVRIIK 2803
Cdd:TIGR00376 446 FYNGKLTAHESvanilLRDLPKveatesedDLE-TGIP---LLFIDTSGCE---LFELKEADSTSKYNPGEAELVSEIIQ 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2804 QLtLDRTVDPKDIAVLTPYNAQAAAISRGLMQRgVTGVTVTSITKSQGSEWRYVIVSTVRTCPRSDVdqrptkswlkkfl 2883
Cdd:TIGR00376 519 AL-VKMGVPANDIGVITPYDAQVDLLRQLLEHR-HIDIEVSSVDGFQGREKEVIIISFVRSNRKGEV------------- 583
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 568920187 2884 GFVVDPHQVNVAITRAQEALCIIGDHLLLRCCPLWHRLLDFCEAQHSLVSAEK 2936
Cdd:TIGR00376 584 GFLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKRLIEWCKQHGEVREAFK 636
|
|
| VacB |
COG0557 |
Exoribonuclease R [Transcription]; |
1396-1938 |
1.79e-50 |
|
Exoribonuclease R [Transcription];
Pssm-ID: 440323 [Multi-domain] Cd Length: 711 Bit Score: 193.01 E-value: 1.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1396 AFTGDEVLVQILGPAGDDRcvpgsLQGRVMGVLKRRRHELAFVCRMDEWDPRImIPINGSVTK-IFVA--EMKDPQQvpi 1472
Cdd:COG0557 103 ALHGDRVLVRVTKEDRRGR-----PEGRVVEILERANTRVVGRFEKEKGFGFV-VPDDKRLLQdIFIPpdDLNGAKD--- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1473 hrliqGQVqrVRhetlkpedrstrlfwVRIVLWRERFYYPLGIVLEVL-----PKAITweqgLYILdLEHGLkahtPD-- 1545
Cdd:COG0557 174 -----GDL--VV---------------VEITRYPERRGPPEGRVVEVLgspgdPGAEI----LIAI-RKHGL----PHef 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1546 PASVSKALQRYRSELNTAA-GHREDYRHFLTFTVDPQGACNLDDALSVRDLGP-VYEVAVHIADVASLVPKDGALDVEAR 1623
Cdd:COG0557 223 PEEVLAEAEALPDEVPEADlKGRRDLRDLPLVTIDGEDAKDFDDAVSAEKLDNgGWRLGVHIADVSHYVRPGSALDREAR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1624 QQGTVFYAPNRepVL-MLPASLCQDALSLLPGQDRLAISLFLTMEKgGGQIKSLRFAPSIIRSDRQLSYEEAEELIKRHP 1702
Cdd:COG0557 303 KRGTSVYLPDR--VIpMLPERLSNGLCSLNPGEDRLAMSCEMEIDA-KGEVVSYEFYRSVIRSDARLTYEEVQAILDGKD 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1703 GAGLELPAHLDSV-----EACVVaacyfswmLRRQR---------LSaacyyEPP---DEDSVLG---FRT---AHIMVQ 1759
Cdd:COG0557 380 EELREEYADLVPMleelyELAKI--------LRKARekrgaidfdLP-----ETKiilDEEGKPEdivPRErndAHKLIE 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1760 EYMIQFNSHVAEFLVSNKHTqtlTPLRWQPTPSRQQLDSvFKKYrgLVPLSLHLchhsntdytpnkqlhlltSLWKQVQl 1839
Cdd:COG0557 447 EFMLLANEAVAEFLEKLKLP---FLYRVHEEPDPEKLEA-LREF--LANLGLKL------------------KGGDEPT- 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1840 aagTQDYSQMVDLIAADDMHPSLAPACLdlrralgRSvfgrssqgkQQPAV-------HHSLQVDWYTWATSPIRRYLDV 1912
Cdd:COG0557 502 ---PKDLQKLLEQVKGRPEEELLNTLLL-------RS---------MKQAVyspenigHFGLALEAYTHFTSPIRRYPDL 562
|
570 580 590
....*....|....*....|....*....|
gi 568920187 1913 VLQRLILLALGHRGST----YSNRDIDGLC 1938
Cdd:COG0557 563 LVHRALKAYLEGKRSPglqeYLEEELEEIA 592
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
2725-2926 |
2.18e-50 |
|
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350195 [Multi-domain] Cd Length: 184 Bit Score: 177.43 E-value: 2.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2725 MHKDICSFPSVEFYGGKLKTWSDLRRLPSILgHTGKPSCSVIFGSVQGHEQkllvstEDGNENSRANPEEVTQVVRIIKQ 2804
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKAGVSVAARLNPP-PLPGPSKPLVFVDVSGGEE------REESGTSKSNEAEAELVVELVKY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2805 LtLDRTVDPKDIAVLTPYNAQAAAISRGLMQRG--VTGVTVTSITKSQGSEWRYVIVSTVRTCPRsdvdqrptkswlKKF 2882
Cdd:cd18808 74 L-LKSGVKPSSIGVITPYRAQVALIRELLRKRGglLEDVEVGTVDNFQGREKDVIILSLVRSNES------------GGS 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568920187 2883 LGFVVDPHQVNVAITRAQEALCIIGDHLLLRCCPLWHRLLDFCE 2926
Cdd:cd18808 141 IGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
961-1161 |
2.31e-35 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Pssm-ID: 463780 [Multi-domain] Cd Length: 196 Bit Score: 134.60 E-value: 2.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 961 TLLHRLFLYYQQeahkiaqqSRIIFHENYRSTAAIINFVSHHFYlakGNPIQASGKVPRHPQH---------YPLMFCHV 1031
Cdd:pfam13087 4 SLFERLQELGPS--------AVVMLDTQYRMHPEIMEFPSKLFY---GGKLKDGPSVAERPLPddfhlpdplGPLVFIDV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1032 AGSPEQDM-SMTSWLNSAEVTQVVEKVREIYNTWPHCWgpreqRHICAVS-HGAQVSALRQELRRRNLG--EVSVGSFEI 1107
Cdd:pfam13087 73 DGSEEEESdGGTSYSNEAEAELVVQLVEKLIKSGPEEP-----SDIGVITpYRAQVRLIRKLLKRKLGGklEIEVNTVDG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568920187 1108 LPGREFRVVVLSSVH-NRNSLLSpgaptseFFTEPRVLNTVMTRAQSQLVAVGDA 1161
Cdd:pfam13087 148 FQGREKDVIIFSCVRsNEKGGIG-------FLSDPRRLNVALTRAKRGLIIVGNA 195
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
886-1184 |
4.11e-34 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 143.73 E-value: 4.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 886 HHRLVVTTTSQ-ARELQVPAGFFSHIFIDEAAQMLECEALIPLSYAlslTRVVLAGDHMQVTPRLFSVPRDKSARHTLLH 964
Cdd:COG1112 534 LAPVVGMTPASvARLLPLGEGSFDLVIIDEASQATLAEALGALARA---KRVVLVGDPKQLPPVVFGEEAEEVAEEGLDE 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 965 RLFlyyqQEAHKIAQQSRIIFHENYRSTAAIINFVSHHFYlakGNPIQASGKVPRHPQ---HYPLMFCHVAGSPEQDmsM 1041
Cdd:COG1112 611 SLL----DRLLARLPERGVMLREHYRMHPEIIAFSNRLFY---DGKLVPLPSPKARRLadpDSPLVFIDVDGVYERR--G 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1042 TSWLNSAEVTQVVEKVREIYNTWPhcwgprEQRHICAVS-HGAQVSALRQELRRRNLGE---VSVGSFEILPGREFRVVV 1117
Cdd:COG1112 682 GSRTNPEEAEAVVELVRELLEDGP------DGESIGVITpYRAQVALIRELLREALGDGlepVFVGTVDRFQGDERDVII 755
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568920187 1118 LSSVHNRNSLLSPGAptsEFFTE-PRVLNTVMTRAQSQLVAVGDAVALCSSGAcRNLWRSFIRECIEH 1184
Cdd:COG1112 756 FSLVYSNDEDVPRNF---GFLNGgPRRLNVAVSRARRKLIVVGSRELLDSDPS-TPALKRLLEYLERA 819
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
994-1182 |
1.66e-32 |
|
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350195 [Multi-domain] Cd Length: 184 Bit Score: 126.19 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 994 AIINFVSHHFY----LAKGNPIQASGKVPRHPQHYPLMFCHVAGSPEQDMSMTSWLNSAEVTQVVEKVREIYNTWphcwg 1069
Cdd:cd18808 4 EISEFPSKLFYegklKAGVSVAARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1070 pREQRHICAVSH-GAQVSALRQELRRRN--LGEVSVGSFEILPGREFRVVVLSSVHNRNSLLSPGaptseFFTEPRVLNT 1146
Cdd:cd18808 79 -VKPSSIGVITPyRAQVALIRELLRKRGglLEDVEVGTVDNFQGREKDVIILSLVRSNESGGSIG-----FLSDPRRLNV 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 568920187 1147 VMTRAQSQLVAVGDAVALCSSGacrnLWRSFIRECI 1182
Cdd:cd18808 153 ALTRAKRGLIIVGNPDTLSKDP----LWKKLLEYLE 184
|
|
| 3_prime_RNase |
TIGR00358 |
VacB and RNase II family 3'-5' exoribonucleases; This model is defined to identify a pair of ... |
1369-1938 |
8.09e-29 |
|
VacB and RNase II family 3'-5' exoribonucleases; This model is defined to identify a pair of paralogous 3-prime exoribonucleases in E. coli, plus the set of proteins apparently orthologous to one or the other in other eubacteria. VacB was characterized originally as required for the expression of virulence genes, but is now recognized as the exoribonuclease RNase R (Rnr). Its paralog in E. coli and H. influenzae is designated exoribonuclease II (Rnb). Both are involved in the degradation of mRNA, and consequently have strong pleiotropic effects that may be difficult to disentangle. Both these proteins share domain-level similarity (RNB, S1) with a considerable number of other proteins, and full-length similarity scoring below the trusted cutoff to proteins associated with various phenotypes but uncertain biochemistry; it may be that these latter proteins are also 3-prime exoribonucleases. [Transcription, Degradation of RNA]
Pssm-ID: 273033 [Multi-domain] Cd Length: 654 Bit Score: 125.60 E-value: 8.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1369 FERALATPLDDMASSPIQVRGRLNcgmaftGDEVLVQILGPagDDRcvpGSLQGRVMGVLKRRRHELAfvcrmdewdpri 1448
Cdd:TIGR00358 30 FLRPDDDDKKDYFIPPPQMKKVMH------GDLVEACPLSQ--PQR---GRFEAEVERILEPALTRFV------------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1449 mipinGSVTkifvaEMKDPQQ-VPIHRLIqGQVQRVRHETLKPEDRSTRLFWVRIVLWRERFYYPLGIVLEVL----PKA 1523
Cdd:TIGR00358 87 -----GKFL-----GENDFGFvVPDDPRI-YLDIIVPKASVKNELAEGDKVVVELTEYPLRRNLFYGEITQILgnndDPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1524 ITWEQGLyildLEHGLKAHTPDPASVSKALQRYRSELNTAAGhREDYRHFLTFTVDPQGACNLDDALSVRDLGPV-YEVA 1602
Cdd:TIGR00358 156 IPWWVTL----ARHEIPFEFPDGVEQQAAKLQFDVDEQAKKY-REDLTDLAFVTIDGADAKDLDDAVYVKKLPDGgWKLY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1603 VHIADVASLVPKDGALDVEARQQGTVFYAPNREpVLMLPASLCQDALSLLPGQDRLAISLFLTMEkGGGQIKSLRFAPSI 1682
Cdd:TIGR00358 231 VAIADVSYYVAENSPLDKEAKHRGFSVYLPGFV-IPMLPEELSNGLCSLNPNEDRLVLVCEMTIS-AQGRITDNEFYPAT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1683 IRSDRQLSYEEAEELIKRHPGAGLELPAHLDSVEacvvAACYFSWMLRRQRLS-AACYYEPPDEDSVLG----------- 1750
Cdd:TIGR00358 309 IESKARLTYDKVNDWLENDDELQPEYETLVEQLK----ALHQLSQALGEWRHKrGLIDFEHPETKFIVDeegrvidivae 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1751 -FRTAHIMVQEYMIQFNSHVAEFLVSNKHTqtlTPLRWQPTPSRQQLDSvfkkyrglvpLSLHLCHHSNTdyTPNKQLHL 1829
Cdd:TIGR00358 385 vRRIAEKIIEEAMIVANICAARFLHNHKVP---GIYRVHPGPSKKKLQS----------LLEFLAELGLT--LPGGNAEN 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1830 LTSLWKQVQLAA--GTQDYSQMVDLiaaddmhpslapacldLRRALGRSVFgrssqgKQQPAVHHSLQVDWYTWATSPIR 1907
Cdd:TIGR00358 450 VTTLDGACWLREvkDRPEYEILVTR----------------LLRSLSQAEY------SPEPLGHFGLGLEHYAHFTSPIR 507
|
570 580 590
....*....|....*....|....*....|....*
gi 568920187 1908 RYLDVVLQRLI--LLALGH--RGSTYSNRDIDGLC 1938
Cdd:TIGR00358 508 RYPDLTNHRLIkaVLAKEQtdTERYQPQDELLQIA 542
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
722-1160 |
1.92e-23 |
|
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273041 [Multi-domain] Cd Length: 636 Bit Score: 108.36 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 722 MTFRFWHQAVDALLEEHLVVPDLpACTLPHPWPTPP--SFRG-----NHKQKLAVGLIAGRRPEgtkhippLLIYGPFGT 794
Cdd:TIGR00376 113 VTFKRMKEALRALTENHSRLLEF-LLGREAPSKASEihDFQFfdpnlNESQKEAVLFALSSKDL-------FLIHGPPGT 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 795 GKTYTLamaaLEVVQQP---HTKVLICTHTNSAADiYIREYF-----------H-------------DYVSSGHPEATPL 847
Cdd:TIGR00376 185 GKTRTV----VELIRQLvkrGLRVLVTAPSNIAVD-NLLERLalcdqkivrlgHparllksnkqhslDYLIENHPKYQIV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 848 RVMYAD------RPPRQTDPT--------TLQYCCLTEDRQAFRpPTGPELVHHRLVVTTTSQA---------------- 897
Cdd:TIGR00376 260 ADIREKidelieERNKKTKPSpqkrrglsDIKILRKALKKREAR-GIESLKIASMAEWIETNKSidrllkllpeseerim 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 898 ----RELQVPAG----------FFSHIFIDEAAQMLECEALIPLSYAlslTRVVLAGDHMQVTPRLFSVPRDKSARhTLL 963
Cdd:TIGR00376 339 neilAESDATNSmagseilngqYFDVAVIDEASQAMEPSCLIPLLKA---RKLILAGDHKQLPPTILSHDAEELSL-TLF 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 964 HRLflyyqqeAHKIAQQSRIIfHENYRSTAAIINFVSHHFYLAKgnpIQASGKVPRH-----------------PQHYPL 1026
Cdd:TIGR00376 415 ERL-------IKEYPERSRTL-NVQYRMNQKIMEFPSREFYNGK---LTAHESVANIllrdlpkveateseddlETGIPL 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1027 MFCHVAG---SPEQDMSMTSWLNSAEVTQVVEKVREI--YNTwphcwgPREQrhICAVS-HGAQVSALRQELRRRNLgEV 1100
Cdd:TIGR00376 484 LFIDTSGcelFELKEADSTSKYNPGEAELVSEIIQALvkMGV------PAND--IGVITpYDAQVDLLRQLLEHRHI-DI 554
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568920187 1101 SVGSFEILPGREFRVVVLSSVH-NRNSLLSpgaptseFFTEPRVLNTVMTRAQSQLVAVGD 1160
Cdd:TIGR00376 555 EVSSVDGFQGREKEVIIISFVRsNRKGEVG-------FLKDLRRLNVALTRARRKLIVIGD 608
|
|
| PRK05054 |
PRK05054 |
exoribonuclease II; Provisional |
1559-1918 |
8.22e-11 |
|
exoribonuclease II; Provisional
Pssm-ID: 179920 [Multi-domain] Cd Length: 644 Bit Score: 67.59 E-value: 8.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1559 ELNTAAGHREDYRHFLTFTVDPQGACNLDDALSVRDLGPV-YEVAVHIADVASLVPKDGALDVEARQQGTVFYAPNREpV 1637
Cdd:PRK05054 182 EMLDEGLEREDLTALDFVTIDSASTEDMDDALYVEKLPDGgLQLTVAIADPTAYIAEGSKLDKAARQRAFTNYLPGFN-I 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1638 LMLPASLCQDALSLLPGQDRLAISLFLTMEKGGGQIKSLRFAPSIIRSDRQLSYEEAEELIKrhpGAGLELPAhlDSVEA 1717
Cdd:PRK05054 261 PMLPRELSDDLCSLRPNERRPALACRVTIDADGTIEDDIRFFAAWIESKAKLAYDNVSDWLE---NGGDWQPE--SEAIA 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1718 CVVAACYFSWMLRRQ--RLSAACYYEPPDEDSVLG------------FRTAHIMVQEYMIQFNSHVAEFLVSNKHTqtlt 1783
Cdd:PRK05054 336 EQIRLLHQFCLARSEwrKQHALVFKDRPDYRFELGekgevldivaepRRIANRIVEESMIAANICAARVLRDKLGF---- 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1784 plrwqptpsrqqldSVFKKYRGLVPLSL----HLCHHSNTDYTPNKqlhlLTSLwkqvqlaagtQDYSQMVDLIaadDMH 1859
Cdd:PRK05054 412 --------------GIYNVHSGFDPANAeqavALLKEHGLHFDAEE----LLTL----------EGFCKLRREL---DAQ 460
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568920187 1860 PSlapACLD--LRRALGRSVFgrssqgKQQPAVHHSLQVDWY-TWaTSPIRRYLDVVLQRLI 1918
Cdd:PRK05054 461 PT---GYLDsrIRRFQSFAEI------STEPGPHFGLGLEAYaTW-TSPIRKYGDMINHRLL 512
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
765-951 |
5.88e-10 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Pssm-ID: 404072 [Multi-domain] Cd Length: 248 Bit Score: 62.36 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 765 QKLAVGLIAGRRPEGtkhipplLIYGPFGTGKTYTLamaaLEVVQQ----------PHTKVLICTHTNSAAD-IYIReyf 833
Cdd:pfam13086 2 QREAIRSALSSSHFT-------LIQGPPGTGKTTTI----VELIRQllsypatsaaAGPRILVCAPSNAAVDnILER--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 834 hdYVSSG-HPEATPLRVMYADRPPRQTDPTTLQYCC----------------------LTEDRQAFRPPTGPELVH---- 886
Cdd:pfam13086 68 --LLRKGqKYGPKIVRIGHPAAISEAVLPVSLDYLVesklnneedaqivkdiskelekLAKALRAFEKEIIVEKLLksrn 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 887 --------------------------------------HRLVVTT-TSQARELQVPAGFFSHIFIDEAAQMLECEALIPL 927
Cdd:pfam13086 146 kdkskleqerrklrserkelrkelrrreqslereildeAQIVCSTlSGAGSRLLSSLANFDVVIIDEAAQALEPSTLIPL 225
|
250 260
....*....|....*....|....
gi 568920187 928 SYALSltRVVLAGDHMQVTPRLFS 951
Cdd:pfam13086 226 LRGPK--KVVLVGDPKQLPPTVIS 247
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
2443-2913 |
5.08e-06 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 51.90 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2443 PAGHHKLNQSQDRAVRSALQK-QFTVIQGPPGTGKT-VVGfHIVYWFhrsnqeqmptdsspsgeEQLGGPCVLyCGPSNK 2520
Cdd:COG0507 119 PRAGITLSDEQREAVALALTTrRVSVLTGGAGTGKTtTLR-ALLAAL-----------------EALGLRVAL-AAPTGK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2521 SVDVLgglllrrktemkplrvygeqAEATefplpgvsnrslfGKTSQegrpnqslrsiTLHHRIRQAPNpyaaeirkfda 2600
Cdd:COG0507 180 AAKRL--------------------SEST-------------GIEAR-----------TIHRLLGLRPD----------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2601 qlregkifskedlrvyRRVLGKARKHELERHSVilctcscaaskslkilnvrqILIDEAGMATEP--ETLIPLVCFSKTv 2678
Cdd:COG0507 205 ----------------SGRFRHNRDNPLTPADL--------------------LVVDEASMVDTRlmAALLEALPRAGA- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2679 eKVVLLGDHKQLRPVVKSEQLqslgmdRSLFERYHRDAIMLDTQYRMHKDicsfpsvefyGGKLKTWSDLRRlpsilght 2758
Cdd:COG0507 248 -RLILVGDPDQLPSVGAGAVL------RDLIESGTVPVVELTEVYRQADD----------SRIIELAHAIRE-------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2759 gkpscsvifgsvqGHEQKLLvsTEDGNENSRANPEEVTQVVRIIKQLTLDRTVDPKDIAVLTPYNAQAAAISRGL----- 2833
Cdd:COG0507 303 -------------GDAPEAL--NARYADVVFVEAEDAEEAAEAIVELYADRPAGGEDIQVLAPTNAGVDALNQAIrealn 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2834 -----------------------MQR----------GVTGvTVTSIT--------------------------------- 2847
Cdd:COG0507 368 pagelerelaedgelelyvgdrvMFTrndydlgvfnGDIG-TVLSIDedegrltvrfdgreivtydpseldqlelayait 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568920187 2848 --KSQGSEWRYVIVstvrtcprsDVDQRPTKswlkkflgfVVDPHQVNVAITRAQEALCIIGDHLLLR 2913
Cdd:COG0507 447 vhKSQGSTFDRVIL---------VLPSEHSP---------LLSRELLYTALTRARELLTLVGDRDALA 496
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DEXXQc_HELZ2-N |
cd18076 |
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
760-990 |
9.12e-129 |
|
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB, and RXRA. It belongs to 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: 350834 [Multi-domain] Cd Length: 230 Bit Score: 403.89 E-value: 9.12e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 760 RGNHKQKLAVGLIAGRRPEGTKhIPPLLIYGPFGTGKTYTLAMAALEVVQQPHTKVLICTHTNSAADIYIREYFHDYVSS 839
Cdd:cd18076 1 AGNNKQQLAFNFIAGKPSEARF-VPPLLIYGPFGTGKTFTLAMAALEVIREPGTKVLICTHTNSAADIYIREYFHPYVDK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 840 GHPEATPLRVMYADRPPRQTDPTTLQYCCLTEDRQAFRPPTGPELVHHRLVVTTTSQARELQVPAGFFSHIFIDEAAQML 919
Cdd:cd18076 80 GHPEARPLRIKATDRPNAITDPDTITYCCLTKDRQCFRLPTRDELDFHNIVITTTAMAFNLHVLSGFFTHIFIDEAAQML 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568920187 920 ECEALIPLSYALSLTRVVLAGDHMQVTPRLFSVPRDKSARHTLLHRLFLYYQQEAHKIAQQSRIIFHENYR 990
Cdd:cd18076 160 ECEALIPLSYAGPKTRVVLAGDHMQMTPKLFSVADYNRANHTLLNRLFHYYQGEKHEVAVKSRVIFSENYR 230
|
|
| DEXXc_HELZ2-C |
cd18040 |
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
2448-2724 |
1.84e-124 |
|
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB and RXRA. It belongs to 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: 350798 [Multi-domain] Cd Length: 271 Bit Score: 393.43 E-value: 1.84e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2448 KLNQSQDRAVRSALQKQFTVIQGPPGTGKTVVGFHIVYWFHRSNQEQmptdsSPSGEEQLGGPCVLYCGPSNKSVDVLGG 2527
Cdd:cd18040 1 KLNPSQNHAVRTALTKPFTLIQGPPGTGKTVTGVHIAYWFAKQNREI-----QSVSGEGDGGPCVLYCGPSNKSVDVVAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2528 LLLRRKtEMKPLRVYGEQAEATEFPLPGVSnRSLFGKTSQEGRPNQSLRSITLHHRIRQAPNPYAAEIRKFDAQL-REGK 2606
Cdd:cd18040 76 LLLKVP-GLKILRVYSEQIETTEYPIPNEP-RHPNKKSERESKPNSELSSITLHHRIRQPSNPHSQQIKAFEARFeRTQE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2607 IFSKEDLRVYRRVLGKARKHELERHSVILCTCSCAASKSLK-ILNVRQILIDEAGMATEPETLIPLVCFsKTVEKVVLLG 2685
Cdd:cd18040 154 KITEEDIKTYKILIWEARFEELETVDVILCTCSEAASQKMRtHANVKQCIVDECGMCTEPESLIPIVSA-PRAEQVVLIG 232
|
250 260 270
....*....|....*....|....*....|....*....
gi 568920187 2686 DHKQLRPVVKSEQLQSLGMDRSLFERYHRDAIMLDTQYR 2724
Cdd:cd18040 233 DHKQLRPVVQNKEAQKLGLGRSLFERYAEKACMLDTQYR 271
|
|
| DEXXQc_HELZ |
cd18077 |
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ... |
760-990 |
5.08e-74 |
|
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. HELZ is a member of the family I class of RNA helicases 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: 350835 [Multi-domain] Cd Length: 226 Bit Score: 246.63 E-value: 5.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 760 RGNHKQKLAVGLIAGrrpEGTKHIPPLLIYGPFGTGKTYTLAMAALEVVQQPHTKVLICTHTNSAADIYIREYFHDYVSS 839
Cdd:cd18077 1 RLNAKQKEAVLAITT---PLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPETRILICTHSNSAADLYIKEYLHPYVET 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 840 GHPEATPLRVMYADRPPRQTDPTTLQYcCLTEDRQAFRPPTGPELVHHRLVVTTTSQAREL---QVPAGFFSHIFIDEAA 916
Cdd:cd18077 78 GNPRARPLRVYYRNRWVKTVHPVVQKY-CLIDEHGTFRMPTREDVMRHRVVVVTLSTSQYLcqlDLEPGFFTHILLDEAA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568920187 917 QMLECEALIPLSYALSLTRVVLAGDHMQVTPRLFSV-PRDKSARHTLLHRLFLYYQQEahkiaQQSRIIFHENYR 990
Cdd:cd18077 157 QAMECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEfARERNLHISLLERLYEHYPSE-----HPCRILLCENYR 226
|
|
| RNB |
smart00955 |
This domain is the catalytic domain of ribonuclease II; |
1567-1924 |
2.35e-70 |
|
This domain is the catalytic domain of ribonuclease II;
Pssm-ID: 214935 [Multi-domain] Cd Length: 286 Bit Score: 238.71 E-value: 2.35e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1567 REDYRHFLTFTVDPQGACNLDDALSVRDLGP-VYEVAVHIADVASLVPKDGALDVEARQQGTVFYAPNRePVLMLPASLC 1645
Cdd:smart00955 1 RVDLRDLPLFTIDPEDAKDIDDAVSVEKLDNgGYRLGVHIADVSHYVKPGSALDREARKRGTSVYLPDR-VIPMLPEELS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1646 QDALSLLPGQDRLAISLFLTMEKGGGQIKSLRFAPSIIRSDRQLSYEEAEELIKRHpgaglelpaHLDSVEACVvaacyf 1725
Cdd:smart00955 80 NGLCSLNPGEDRLALSVEMTLDADGGEILDYEFYRSVIRSKARLTYEEVDAILEKI---------VLDEEGKIE------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1726 sWMLRRQRLsaacyyeppdedsvlgfrTAHIMVQEYMIQFNSHVAEFLVSNKHTqtlTPLRWQPTPSRQQLDSVFKKYRG 1805
Cdd:smart00955 145 -DIVPRERN------------------DAHSLVEEFMILANEAVARFLAKNGIP---GLYRVHEGPDPEKLAELLKEFLA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1806 LVPLSLhlchhsntdytpnkqlhlltslwkqvQLAAGTQDYSQMVDLIAaddMHPSLAPACLDLRRALGRSVFGRSSQGk 1885
Cdd:smart00955 203 LLGLLL--------------------------LGGDGPKALAKLLEKIR---DSPEERLLELLLLRSMPHAEYSVDNSG- 252
|
330 340 350
....*....|....*....|....*....|....*....
gi 568920187 1886 qqpavHHSLQVDWYTWATSPIRRYLDVVLQRLILLALGH 1924
Cdd:smart00955 253 -----HFGLALDAYTHFTSPIRRYPDLIVHRQLKAALRG 286
|
|
| DEXXQc_Helz-like |
cd18038 |
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ... |
760-990 |
1.62e-68 |
|
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and similar proteins. Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. All are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350796 [Multi-domain] Cd Length: 229 Bit Score: 230.97 E-value: 1.62e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 760 RGNHKQKLAVGLIAGrrpeGTKHIPPLLIYGPFGTGKTYTLAMAALEVV-QQPHTKVLICTHTNSAADIYIREYFHdyvs 838
Cdd:cd18038 1 ELNDEQKLAVRNIVT----GTSRPPPYIIFGPPGTGKTVTLVEAILQVLrQPPEARILVCAPSNSAADLLAERLLN---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 839 SGHPEATPLRVMYADRPPRQTDPTTLQYCCLTEDRqAFRPPTGPELVHHRLVVTTTSQA---RELQVPAGFFSHIFIDEA 915
Cdd:cd18038 73 ALVTKREILRLNAPSRDRASVPPELLPYCNSKAEG-TFRLPSLEELKKYRIVVCTLMTAgrlVQAGVPNGHFTHIFIDEA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568920187 916 AQMLECEALIPLSY-ALSLTRVVLAGDHMQVTPRLFSVPRDK-SARHTLLHRLFLYYQ-QEAHKIAQQSRIIFHENYR 990
Cdd:cd18038 152 GQATEPEALIPLSElASKNTQIVLAGDPKQLGPVVRSPLARKyGLGKSLLERLMERPLyYKDGEYNPSYITKLLKNYR 229
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
2704-2909 |
4.98e-65 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Pssm-ID: 463780 [Multi-domain] Cd Length: 196 Bit Score: 219.73 E-value: 4.98e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2704 MDRSLFER----YHRDAIMLDTQYRMHKDICSFPSVEFYGGKLKTWSDLR-RLPSILGHTGKPSCSVIFGSVQGHEQKll 2778
Cdd:pfam13087 1 LDRSLFERlqelGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAeRPLPDDFHLPDPLGPLVFIDVDGSEEE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2779 vstEDGNENSRANPEEVTQVVRIIKQLTLDRTVDPKDIAVLTPYNAQAAAISRGLMQRGVT--GVTVTSITKSQGSEWRY 2856
Cdd:pfam13087 79 ---ESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSDIGVITPYRAQVRLIRKLLKRKLGGklEIEVNTVDGFQGREKDV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568920187 2857 VIVSTVRTCPRSDVdqrptkswlkkflGFVVDPHQVNVAITRAQEALCIIGDH 2909
Cdd:pfam13087 156 IIFSCVRSNEKGGI-------------GFLSDPRRLNVALTRAKRGLIIVGNA 195
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
2539-2928 |
2.12e-57 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 216.15 E-value: 2.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2539 LRVYGEQAEATEFPLPGVSNRSLFGKTSQEGRPNQSLRSITLHHRIRQAPNPYAAEIRKFDAQLREGKIFSKEdLRVYRR 2618
Cdd:COG1112 444 LAAALAALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPEELEKLIAELREAARLRRALRRE-LKKRRE 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2619 VLGKARKHELERHSVILCTC-SCAASKSLKILNVRQILIDEAGMATEPETLIPLVCFsktvEKVVLLGDHKQLRPVVKSE 2697
Cdd:COG1112 523 LRKLLWDALLELAPVVGMTPaSVARLLPLGEGSFDLVIIDEASQATLAEALGALARA----KRVVLVGDPKQLPPVVFGE 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2698 ---QLQSLGMDRSLFER----YHRDAIMLDTQYRMHKDICSFPSVEFYGGKLKTwsdlrrLPSILGHTGK-PSCSVIFGS 2769
Cdd:COG1112 599 eaeEVAEEGLDESLLDRllarLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVP------LPSPKARRLAdPDSPLVFID 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2770 VQGHEQKllvstedgNENSRANPEEVTQVVRIIKQLtLDRTVDPKDIAVLTPYNAQAAAISRGLMQR---GVTGVTVTSI 2846
Cdd:COG1112 673 VDGVYER--------RGGSRTNPEEAEAVVELVREL-LEDGPDGESIGVITPYRAQVALIRELLREAlgdGLEPVFVGTV 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2847 TKSQGSEWRYVIVSTVRTcPRSDVDQRptkswlkkfLGFVV-DPHQVNVAITRAQEALCIIGDHLLLRCCP---LWHRLL 2922
Cdd:COG1112 744 DRFQGDERDVIIFSLVYS-NDEDVPRN---------FGFLNgGPRRLNVAVSRARRKLIVVGSRELLDSDPstpALKRLL 813
|
....*.
gi 568920187 2923 DFCEAQ 2928
Cdd:COG1112 814 EYLERA 819
|
|
| RNB |
pfam00773 |
RNB domain; This domain is the catalytic domain of ribonuclease II. |
1567-1922 |
2.31e-57 |
|
RNB domain; This domain is the catalytic domain of ribonuclease II.
Pssm-ID: 459934 [Multi-domain] Cd Length: 314 Bit Score: 202.51 E-value: 2.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1567 REDYRHFLTFTVDPQGACNLDDALSVRDLGPV-YEVAVHIADVASLVPKDGALDVEARQQGTVFYAPNRepVL-MLPASL 1644
Cdd:pfam00773 1 RKDLRDLPFITIDPADAKDLDDAISVEKLPNGgYRLGVHIADVSHYVPPGSPLDREARKRGTSVYLPDR--VIpMLPEKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1645 CQDALSLLPGQDRLAISLFLTMEKgGGQIKSLRFAPSIIRSDRQLSYEEAEELIKRhPGAGLELPAHLDSVEacvvAACY 1724
Cdd:pfam00773 79 SNDLCSLNPGEDRLALSVEITIDA-DGEVTSYEIYPSVIRSKARLTYEEVDDLLEG-KDAEKDKPDLAEDLR----LLYE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1725 FSWMLRRQRLSA-ACYYEPP------DEDSVLGFRT-----AHIMVQEYMIQFNSHVAEFLVSNKHTqtlTPLRWQPTPS 1792
Cdd:pfam00773 153 LAKILRAKRLQRgALDLDTPenklilDEEGVIDILIqertdAHSLIEEFMLLANEAVARHLQELGIP---ALYRVHPEPD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1793 RQQLDsvfkkyrglvplslhlchhsntdytpnkqlhlltSLWKQVQLAAGTQDYSQMVDLIAADDMHPSLApacldLRRA 1872
Cdd:pfam00773 230 LEKLN----------------------------------SLIKLLQLLPDDKGLSKSLEKIKDDERLLSIL-----LLRT 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 568920187 1873 LGRSVFGrssqgkQQPAVHHSLQVDWYTWATSPIRRYLDVVLQRLILLAL 1922
Cdd:pfam00773 271 MPRAEYS------PEPLGHFGLGLDIYTHFTSPIRRYPDLIVHRQLKALL 314
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
2452-2697 |
6.56e-57 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Pssm-ID: 404072 [Multi-domain] Cd Length: 248 Bit Score: 198.72 E-value: 6.56e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2452 SQDRAVRSALQKQ-FTVIQGPPGTGKTvvgFHIVYWFHRSNqeqmptdsSPSGEEQLGGPCVLYCGPSNKSVDVLGGLLL 2530
Cdd:pfam13086 1 SQREAIRSALSSShFTLIQGPPGTGKT---TTIVELIRQLL--------SYPATSAAAGPRILVCAPSNAAVDNILERLL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2531 R--RKTEMKPLRVYGEQAeatefplPGVSNRSLFGKTSQEGRPNQSlRSITLHHRIRQAPNPYAAEIRKFDAQ-----LR 2603
Cdd:pfam13086 70 RkgQKYGPKIVRIGHPAA-------ISEAVLPVSLDYLVESKLNNE-EDAQIVKDISKELEKLAKALRAFEKEiivekLL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2604 EGKIFSKEDLRVYRRVLGKARK---------------HELERHSVILCTCSCAASKSLKIL-NVRQILIDEAGMATEPET 2667
Cdd:pfam13086 142 KSRNKDKSKLEQERRKLRSERKelrkelrrreqslerEILDEAQIVCSTLSGAGSRLLSSLaNFDVVIIDEAAQALEPST 221
|
250 260 270
....*....|....*....|....*....|
gi 568920187 2668 LIPLVCFSKtveKVVLLGDHKQLRPVVKSE 2697
Cdd:pfam13086 222 LIPLLRGPK---KVVLVGDPKQLPPTVISK 248
|
|
| DEXXQc_UPF1 |
cd18039 |
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ... |
2448-2724 |
3.32e-56 |
|
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of Nonsense Transcripts, or ATP-Dependent Helicase RENT1) is an RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. It is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. It is recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) located downstream from the termination codon through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Diseases associated with UPF1 include juvenile amyotrophic lateral sclerosis and epidermolysis bullosa, junctional, non-Herlitz type. UPF1 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: 350797 [Multi-domain] Cd Length: 234 Bit Score: 195.93 E-value: 3.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2448 KLNQSQDRAVRSALQKQFTVIQGPPGTGKTVVGFHIVYWFHRSNQEQmptdsspsgeeqlggpcVLYCGPSNKSVDVLGG 2527
Cdd:cd18039 1 ELNHSQVDAVKTALQRPLSLIQGPPGTGKTVTSATIVYHLVKQGNGP-----------------VLVCAPSNVAVDQLTE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2528 LLlrRKTEMKPLRVYGEQAEATEfplpgvsnrslfgktsqegrpnQSLRSITLHHRIRQAPNPYAAEIRKFdaQLREGKI 2607
Cdd:cd18039 64 KI--HQTGLKVVRLCAKSREAVE----------------------SPVSFLALHNQVRNLDSAEKLELLKL--LKLETGE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2608 FSKEDLRVYRRVLGKARKHELERHSVILCTCSCAASKSLKILNVRQILIDEAGMATEPETLIPLVcfsKTVEKVVLLGDH 2687
Cdd:cd18039 118 LSSADEKRYRKLKRKAERELLRNADVICCTCVGAGDPRLSKMKFRTVLIDEATQATEPECLIPLV---HGAKQVILVGDH 194
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568920187 2688 KQLRPVVKSEQLQSLGMDRSLFERY----HRdAIMLDTQYR 2724
Cdd:cd18039 195 CQLGPVVMCKKAAKAGLSQSLFERLvqlgIR-PIRLQVQYR 234
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
2449-2936 |
5.01e-51 |
|
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273041 [Multi-domain] Cd Length: 636 Bit Score: 193.49 E-value: 5.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2449 LNQSQDRAVRSAL-QKQFTVIQGPPGTGKTVVGFHIVywfhrsNQEQMPtdsspsgeeqlgGPCVLYCGPSNKSVDVLGG 2527
Cdd:TIGR00376 158 LNESQKEAVLFALsSKDLFLIHGPPGTGKTRTVVELI------RQLVKR------------GLRVLVTAPSNIAVDNLLE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2528 LLLrrKTEMKPLRVyGEQA----EATEFPLPGVSNRSLFGKTSQEGRpnQSLRSITLHHRIRQAPNPyaaEIRKF--DAQ 2601
Cdd:TIGR00376 220 RLA--LCDQKIVRL-GHPArllkSNKQHSLDYLIENHPKYQIVADIR--EKIDELIEERNKKTKPSP---QKRRGlsDIK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2602 L-------REGKIFSKEDLRVYRRV--LGKARKHEL------------ERHSVILCTCSCAASKSLKILNVRQILIDEAG 2660
Cdd:TIGR00376 292 IlrkalkkREARGIESLKIASMAEWieTNKSIDRLLkllpeseerimnEILAESDATNSMAGSEILNGQYFDVAVIDEAS 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2661 MATEPETLIPLVcfskTVEKVVLLGDHKQLRPVVKSEQLQSLgmDRSLFER----YHRDAIMLDTQYRMHKDICSFPSVE 2736
Cdd:TIGR00376 372 QAMEPSCLIPLL----KARKLILAGDHKQLPPTILSHDAEEL--SLTLFERlikeYPERSRTLNVQYRMNQKIMEFPSRE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2737 FYGGKLKTWSD-----LRRLPS--------ILGhTGKPscsVIFGSVQGHEqklLVSTEDGNENSRANPEEVTQVVRIIK 2803
Cdd:TIGR00376 446 FYNGKLTAHESvanilLRDLPKveatesedDLE-TGIP---LLFIDTSGCE---LFELKEADSTSKYNPGEAELVSEIIQ 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2804 QLtLDRTVDPKDIAVLTPYNAQAAAISRGLMQRgVTGVTVTSITKSQGSEWRYVIVSTVRTCPRSDVdqrptkswlkkfl 2883
Cdd:TIGR00376 519 AL-VKMGVPANDIGVITPYDAQVDLLRQLLEHR-HIDIEVSSVDGFQGREKEVIIISFVRSNRKGEV------------- 583
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 568920187 2884 GFVVDPHQVNVAITRAQEALCIIGDHLLLRCCPLWHRLLDFCEAQHSLVSAEK 2936
Cdd:TIGR00376 584 GFLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKRLIEWCKQHGEVREAFK 636
|
|
| VacB |
COG0557 |
Exoribonuclease R [Transcription]; |
1396-1938 |
1.79e-50 |
|
Exoribonuclease R [Transcription];
Pssm-ID: 440323 [Multi-domain] Cd Length: 711 Bit Score: 193.01 E-value: 1.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1396 AFTGDEVLVQILGPAGDDRcvpgsLQGRVMGVLKRRRHELAFVCRMDEWDPRImIPINGSVTK-IFVA--EMKDPQQvpi 1472
Cdd:COG0557 103 ALHGDRVLVRVTKEDRRGR-----PEGRVVEILERANTRVVGRFEKEKGFGFV-VPDDKRLLQdIFIPpdDLNGAKD--- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1473 hrliqGQVqrVRhetlkpedrstrlfwVRIVLWRERFYYPLGIVLEVL-----PKAITweqgLYILdLEHGLkahtPD-- 1545
Cdd:COG0557 174 -----GDL--VV---------------VEITRYPERRGPPEGRVVEVLgspgdPGAEI----LIAI-RKHGL----PHef 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1546 PASVSKALQRYRSELNTAA-GHREDYRHFLTFTVDPQGACNLDDALSVRDLGP-VYEVAVHIADVASLVPKDGALDVEAR 1623
Cdd:COG0557 223 PEEVLAEAEALPDEVPEADlKGRRDLRDLPLVTIDGEDAKDFDDAVSAEKLDNgGWRLGVHIADVSHYVRPGSALDREAR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1624 QQGTVFYAPNRepVL-MLPASLCQDALSLLPGQDRLAISLFLTMEKgGGQIKSLRFAPSIIRSDRQLSYEEAEELIKRHP 1702
Cdd:COG0557 303 KRGTSVYLPDR--VIpMLPERLSNGLCSLNPGEDRLAMSCEMEIDA-KGEVVSYEFYRSVIRSDARLTYEEVQAILDGKD 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1703 GAGLELPAHLDSV-----EACVVaacyfswmLRRQR---------LSaacyyEPP---DEDSVLG---FRT---AHIMVQ 1759
Cdd:COG0557 380 EELREEYADLVPMleelyELAKI--------LRKARekrgaidfdLP-----ETKiilDEEGKPEdivPRErndAHKLIE 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1760 EYMIQFNSHVAEFLVSNKHTqtlTPLRWQPTPSRQQLDSvFKKYrgLVPLSLHLchhsntdytpnkqlhlltSLWKQVQl 1839
Cdd:COG0557 447 EFMLLANEAVAEFLEKLKLP---FLYRVHEEPDPEKLEA-LREF--LANLGLKL------------------KGGDEPT- 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1840 aagTQDYSQMVDLIAADDMHPSLAPACLdlrralgRSvfgrssqgkQQPAV-------HHSLQVDWYTWATSPIRRYLDV 1912
Cdd:COG0557 502 ---PKDLQKLLEQVKGRPEEELLNTLLL-------RS---------MKQAVyspenigHFGLALEAYTHFTSPIRRYPDL 562
|
570 580 590
....*....|....*....|....*....|
gi 568920187 1913 VLQRLILLALGHRGST----YSNRDIDGLC 1938
Cdd:COG0557 563 LVHRALKAYLEGKRSPglqeYLEEELEEIA 592
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
2725-2926 |
2.18e-50 |
|
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350195 [Multi-domain] Cd Length: 184 Bit Score: 177.43 E-value: 2.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2725 MHKDICSFPSVEFYGGKLKTWSDLRRLPSILgHTGKPSCSVIFGSVQGHEQkllvstEDGNENSRANPEEVTQVVRIIKQ 2804
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKAGVSVAARLNPP-PLPGPSKPLVFVDVSGGEE------REESGTSKSNEAEAELVVELVKY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2805 LtLDRTVDPKDIAVLTPYNAQAAAISRGLMQRG--VTGVTVTSITKSQGSEWRYVIVSTVRTCPRsdvdqrptkswlKKF 2882
Cdd:cd18808 74 L-LKSGVKPSSIGVITPYRAQVALIRELLRKRGglLEDVEVGTVDNFQGREKDVIILSLVRSNES------------GGS 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568920187 2883 LGFVVDPHQVNVAITRAQEALCIIGDHLLLRCCPLWHRLLDFCE 2926
Cdd:cd18808 141 IGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
961-1161 |
2.31e-35 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Pssm-ID: 463780 [Multi-domain] Cd Length: 196 Bit Score: 134.60 E-value: 2.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 961 TLLHRLFLYYQQeahkiaqqSRIIFHENYRSTAAIINFVSHHFYlakGNPIQASGKVPRHPQH---------YPLMFCHV 1031
Cdd:pfam13087 4 SLFERLQELGPS--------AVVMLDTQYRMHPEIMEFPSKLFY---GGKLKDGPSVAERPLPddfhlpdplGPLVFIDV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1032 AGSPEQDM-SMTSWLNSAEVTQVVEKVREIYNTWPHCWgpreqRHICAVS-HGAQVSALRQELRRRNLG--EVSVGSFEI 1107
Cdd:pfam13087 73 DGSEEEESdGGTSYSNEAEAELVVQLVEKLIKSGPEEP-----SDIGVITpYRAQVRLIRKLLKRKLGGklEIEVNTVDG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568920187 1108 LPGREFRVVVLSSVH-NRNSLLSpgaptseFFTEPRVLNTVMTRAQSQLVAVGDA 1161
Cdd:pfam13087 148 FQGREKDVIIFSCVRsNEKGGIG-------FLSDPRRLNVALTRAKRGLIIVGNA 195
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
886-1184 |
4.11e-34 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 143.73 E-value: 4.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 886 HHRLVVTTTSQ-ARELQVPAGFFSHIFIDEAAQMLECEALIPLSYAlslTRVVLAGDHMQVTPRLFSVPRDKSARHTLLH 964
Cdd:COG1112 534 LAPVVGMTPASvARLLPLGEGSFDLVIIDEASQATLAEALGALARA---KRVVLVGDPKQLPPVVFGEEAEEVAEEGLDE 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 965 RLFlyyqQEAHKIAQQSRIIFHENYRSTAAIINFVSHHFYlakGNPIQASGKVPRHPQ---HYPLMFCHVAGSPEQDmsM 1041
Cdd:COG1112 611 SLL----DRLLARLPERGVMLREHYRMHPEIIAFSNRLFY---DGKLVPLPSPKARRLadpDSPLVFIDVDGVYERR--G 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1042 TSWLNSAEVTQVVEKVREIYNTWPhcwgprEQRHICAVS-HGAQVSALRQELRRRNLGE---VSVGSFEILPGREFRVVV 1117
Cdd:COG1112 682 GSRTNPEEAEAVVELVRELLEDGP------DGESIGVITpYRAQVALIRELLREALGDGlepVFVGTVDRFQGDERDVII 755
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568920187 1118 LSSVHNRNSLLSPGAptsEFFTE-PRVLNTVMTRAQSQLVAVGDAVALCSSGAcRNLWRSFIRECIEH 1184
Cdd:COG1112 756 FSLVYSNDEDVPRNF---GFLNGgPRRLNVAVSRARRKLIVVGSRELLDSDPS-TPALKRLLEYLERA 819
|
|
| DEXXQc_SETX |
cd18042 |
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ... |
2449-2724 |
1.14e-33 |
|
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in transcription, neurogenesis, and antiviral response. SEXT is an R-loop-associated protein that is thought to function as an RNA/DNA helicase. R-loops consist of RNA/DNA hybrids, formed during transcription when nascent RNA hybridizes to the DNA template strand, displacing the non-template DNA strand. Mutations in SETX are linked to two neurodegenerative disorders: ataxia with oculomotor apraxia type 2 (AOA2) and amyotrophic lateral sclerosis type 4 (ALS4). S. cerevisiae homolog splicing endonuclease 1 (Sen1) is an exclusively nuclear protein, important for nucleolar organization. S. cerevisiae Sen1 and its ortholog, the Schizosaccharomyces pombe Sen1, share conserved domains and belong to the family I class of helicases. Both proteins translocate 5' to 3' and unwind both DNA and RNA duplexes and also RNA/DNA hybrids in vitro. SETX 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: 438712 [Multi-domain] Cd Length: 218 Bit Score: 130.80 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2449 LNQSQDRAVRSALQKQ--FTVIQGPPGTGKT--VVGfhIVYWFHRSNQEQMPTDSSPSGEEQLG-------GPCVLYCGP 2517
Cdd:cd18042 1 LNESQLEAIASALQNSpgITLIQGPPGTGKTktIVG--ILSVLLAGKYRKYYEKVKKKLRKLQRnlnnkkkKNRILVCAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2518 SNKSVDvlgGLLLRRKTEmkplrvygeqaeatefplpgvsnrslfgktsqegrpnqslrsitlhhrirqapNPYAAEIRK 2597
Cdd:cd18042 79 SNAAVD---EIVLRLLSE-----------------------------------------------------GFLDGDGRS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2598 FDAQLregkifskedLRVYRRvlgKARKHELERHSVILCTCSCAASKSLKILNVR--QILIDEAGMATEPETLIPLvcfS 2675
Cdd:cd18042 103 YKPNV----------VRVGRQ---ELRASILNEADIVCTTLSSSGSDLLESLPRGfdTVIIDEAAQAVELSTLIPL---R 166
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 568920187 2676 KTVEKVVLLGDHKQLRPVVKSEQLQSLGMDRSLFERYHR---DAIMLDTQYR 2724
Cdd:cd18042 167 LGCKRLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQLagyPVLMLTTQYR 218
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
994-1182 |
1.66e-32 |
|
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350195 [Multi-domain] Cd Length: 184 Bit Score: 126.19 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 994 AIINFVSHHFY----LAKGNPIQASGKVPRHPQHYPLMFCHVAGSPEQDMSMTSWLNSAEVTQVVEKVREIYNTWphcwg 1069
Cdd:cd18808 4 EISEFPSKLFYegklKAGVSVAARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1070 pREQRHICAVSH-GAQVSALRQELRRRN--LGEVSVGSFEILPGREFRVVVLSSVHNRNSLLSPGaptseFFTEPRVLNT 1146
Cdd:cd18808 79 -VKPSSIGVITPyRAQVALIRELLRKRGglLEDVEVGTVDNFQGREKDVIILSLVRSNESGGSIG-----FLSDPRRLNV 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 568920187 1147 VMTRAQSQLVAVGDAVALCSSGacrnLWRSFIRECI 1182
Cdd:cd18808 153 ALTRAKRGLIIVGNPDTLSKDP----LWKKLLEYLE 184
|
|
| DEXXQc_Helz-like |
cd18038 |
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ... |
2449-2725 |
4.70e-30 |
|
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and similar proteins. Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. All are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350796 [Multi-domain] Cd Length: 229 Bit Score: 120.42 E-value: 4.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2449 LNQSQDRAVRSALQKQFT----VIQGPPGTGKTVVGFHIVYWFHRsnqeqmptdsspsgeeQLGGPCVLYCGPSNKSVDV 2524
Cdd:cd18038 2 LNDEQKLAVRNIVTGTSRpppyIIFGPPGTGKTVTLVEAILQVLR----------------QPPEARILVCAPSNSAADL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2525 LGGLLLRR-KTEMKPLRVYGEQAEATEFPlpgvsnrslfgktsqegrpnqslrsitlhhrirqapnpyaAEIRKFDAQLR 2603
Cdd:cd18038 66 LAERLLNAlVTKREILRLNAPSRDRASVP----------------------------------------PELLPYCNSKA 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2604 EGKIFSKEdlrvyrrvlgkarKHELERHSVILCTCSCAASksLKILNVRQ-----ILIDEAGMATEPETLIPLVCFSKTV 2678
Cdd:cd18038 106 EGTFRLPS-------------LEELKKYRIVVCTLMTAGR--LVQAGVPNghfthIFIDEAGQATEPEALIPLSELASKN 170
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 568920187 2679 EKVVLLGDHKQLRPVVKSEQLQSLGMDRSLFERyhrdaIMLDTQYRM 2725
Cdd:cd18038 171 TQIVLAGDPKQLGPVVRSPLARKYGLGKSLLER-----LMERPLYYK 212
|
|
| 3_prime_RNase |
TIGR00358 |
VacB and RNase II family 3'-5' exoribonucleases; This model is defined to identify a pair of ... |
1369-1938 |
8.09e-29 |
|
VacB and RNase II family 3'-5' exoribonucleases; This model is defined to identify a pair of paralogous 3-prime exoribonucleases in E. coli, plus the set of proteins apparently orthologous to one or the other in other eubacteria. VacB was characterized originally as required for the expression of virulence genes, but is now recognized as the exoribonuclease RNase R (Rnr). Its paralog in E. coli and H. influenzae is designated exoribonuclease II (Rnb). Both are involved in the degradation of mRNA, and consequently have strong pleiotropic effects that may be difficult to disentangle. Both these proteins share domain-level similarity (RNB, S1) with a considerable number of other proteins, and full-length similarity scoring below the trusted cutoff to proteins associated with various phenotypes but uncertain biochemistry; it may be that these latter proteins are also 3-prime exoribonucleases. [Transcription, Degradation of RNA]
Pssm-ID: 273033 [Multi-domain] Cd Length: 654 Bit Score: 125.60 E-value: 8.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1369 FERALATPLDDMASSPIQVRGRLNcgmaftGDEVLVQILGPagDDRcvpGSLQGRVMGVLKRRRHELAfvcrmdewdpri 1448
Cdd:TIGR00358 30 FLRPDDDDKKDYFIPPPQMKKVMH------GDLVEACPLSQ--PQR---GRFEAEVERILEPALTRFV------------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1449 mipinGSVTkifvaEMKDPQQ-VPIHRLIqGQVQRVRHETLKPEDRSTRLFWVRIVLWRERFYYPLGIVLEVL----PKA 1523
Cdd:TIGR00358 87 -----GKFL-----GENDFGFvVPDDPRI-YLDIIVPKASVKNELAEGDKVVVELTEYPLRRNLFYGEITQILgnndDPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1524 ITWEQGLyildLEHGLKAHTPDPASVSKALQRYRSELNTAAGhREDYRHFLTFTVDPQGACNLDDALSVRDLGPV-YEVA 1602
Cdd:TIGR00358 156 IPWWVTL----ARHEIPFEFPDGVEQQAAKLQFDVDEQAKKY-REDLTDLAFVTIDGADAKDLDDAVYVKKLPDGgWKLY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1603 VHIADVASLVPKDGALDVEARQQGTVFYAPNREpVLMLPASLCQDALSLLPGQDRLAISLFLTMEkGGGQIKSLRFAPSI 1682
Cdd:TIGR00358 231 VAIADVSYYVAENSPLDKEAKHRGFSVYLPGFV-IPMLPEELSNGLCSLNPNEDRLVLVCEMTIS-AQGRITDNEFYPAT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1683 IRSDRQLSYEEAEELIKRHPGAGLELPAHLDSVEacvvAACYFSWMLRRQRLS-AACYYEPPDEDSVLG----------- 1750
Cdd:TIGR00358 309 IESKARLTYDKVNDWLENDDELQPEYETLVEQLK----ALHQLSQALGEWRHKrGLIDFEHPETKFIVDeegrvidivae 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1751 -FRTAHIMVQEYMIQFNSHVAEFLVSNKHTqtlTPLRWQPTPSRQQLDSvfkkyrglvpLSLHLCHHSNTdyTPNKQLHL 1829
Cdd:TIGR00358 385 vRRIAEKIIEEAMIVANICAARFLHNHKVP---GIYRVHPGPSKKKLQS----------LLEFLAELGLT--LPGGNAEN 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1830 LTSLWKQVQLAA--GTQDYSQMVDLiaaddmhpslapacldLRRALGRSVFgrssqgKQQPAVHHSLQVDWYTWATSPIR 1907
Cdd:TIGR00358 450 VTTLDGACWLREvkDRPEYEILVTR----------------LLRSLSQAEY------SPEPLGHFGLGLEHYAHFTSPIR 507
|
570 580 590
....*....|....*....|....*....|....*
gi 568920187 1908 RYLDVVLQRLI--LLALGH--RGSTYSNRDIDGLC 1938
Cdd:TIGR00358 508 RYPDLTNHRLIkaVLAKEQtdTERYQPQDELLQIA 542
|
|
| DEXXQc_SMUBP2 |
cd18044 |
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ... |
2448-2724 |
3.94e-25 |
|
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, or IGHMBP2) is a 5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction. It is a DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence (5'-GGGCT-3') related to the immunoglobulin mu chain switch region. The IGHMBP2 gene is responsible for Charcot-Marie-Tooth disease (CMT) type 2S and spinal muscular atrophy with respiratory distress type 1 (SMARD1). It is also thought to play a role in frontotemporal dementia (FTD) with amyotrophic lateral sclerosis (ALS) and major depressive disorder (MDD). SMUBP2 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: 350802 [Multi-domain] Cd Length: 191 Bit Score: 105.00 E-value: 3.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2448 KLNQSQDRAVRSAL-QKQFTVIQGPPGTGKTVVGFHIVYwfhrsnQEQMPtdsspsgeeqlgGPCVLYCGPSNKSVDVLG 2526
Cdd:cd18044 1 NLNDSQKEAVKFALsQKDVALIHGPPGTGKTTTVVEIIL------QAVKR------------GEKVLACAPSNIAVDNLV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2527 GLLLRRKteMKPLRVygeqaeatefplpgvsnrslfgktsqeGRPNqslrsitlhhrirqapnpyaaeirkfdaqlregk 2606
Cdd:cd18044 63 ERLVALK--VKVVRI---------------------------GHPA---------------------------------- 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2607 ifskedlrvyrRVLGKARKHELERHS---VILCTCSCAASKSLK-ILNVRQILIDEAGMATEPETLIPLVCFSKtvekVV 2682
Cdd:cd18044 80 -----------RLLESVLDHSLDALVaaqVVLATNTGAGSRQLLpNELFDVVVIDEAAQALEASCWIPLLKARR----CI 144
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 568920187 2683 LLGDHKQLRPVVKSEQLQSLGMDRSLFERY---HRDAI--MLDTQYR 2724
Cdd:cd18044 145 LAGDHKQLPPTILSDKAARGGLGVTLFERLvnlYGESVvrMLTVQYR 191
|
|
| DEXXQc_Mov10L1 |
cd18078 |
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ... |
762-990 |
4.47e-25 |
|
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. Mov10L1 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: 350836 [Multi-domain] Cd Length: 230 Bit Score: 106.30 E-value: 4.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 762 NHKQKLAVgliagRRPEGTKHIP-PLLIYGPFGTGKTYTLAMAALEVVQQ-PHTKVLICTHTNSAADIyIREYFHDyvsS 839
Cdd:cd18078 3 NELQKEAV-----KRILGGECRPlPYILFGPPGTGKTVTIIEAILQVVYNlPRSRILVCAPSNSAADL-VTSRLHE---S 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 840 GHPEATPL-RVMYADRPPRQTDPTTLQYCCLTEDRQAfrpptgpeLVHHRLVVTTTSQARELQ---VPAGFFSHIFIDEA 915
Cdd:cd18078 74 KVLKPGDMvRLNAVNRFESTVIDARKLYCRLGEDLSK--------ASRHRIVISTCSTAGLLYqmgLPVGHFTHVFVDEA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 916 AQMLECEALIPLSYALSLT-RVVLAGDHMQVTPRLFSvpRDKSA---RHTLLHRLFLY--YQQEAHKIAQQS----RIIF 985
Cdd:cd18078 146 GQATEPESLIPLGLISSRDgQIILAGDPMQLGPVIKS--RLASAyglGVSFLERLMNRplYLRDPNRFGESGgynpLLVT 223
|
....*..
gi 568920187 986 H--ENYR 990
Cdd:cd18078 224 KlvDNYR 230
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
722-1160 |
1.92e-23 |
|
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273041 [Multi-domain] Cd Length: 636 Bit Score: 108.36 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 722 MTFRFWHQAVDALLEEHLVVPDLpACTLPHPWPTPP--SFRG-----NHKQKLAVGLIAGRRPEgtkhippLLIYGPFGT 794
Cdd:TIGR00376 113 VTFKRMKEALRALTENHSRLLEF-LLGREAPSKASEihDFQFfdpnlNESQKEAVLFALSSKDL-------FLIHGPPGT 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 795 GKTYTLamaaLEVVQQP---HTKVLICTHTNSAADiYIREYF-----------H-------------DYVSSGHPEATPL 847
Cdd:TIGR00376 185 GKTRTV----VELIRQLvkrGLRVLVTAPSNIAVD-NLLERLalcdqkivrlgHparllksnkqhslDYLIENHPKYQIV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 848 RVMYAD------RPPRQTDPT--------TLQYCCLTEDRQAFRpPTGPELVHHRLVVTTTSQA---------------- 897
Cdd:TIGR00376 260 ADIREKidelieERNKKTKPSpqkrrglsDIKILRKALKKREAR-GIESLKIASMAEWIETNKSidrllkllpeseerim 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 898 ----RELQVPAG----------FFSHIFIDEAAQMLECEALIPLSYAlslTRVVLAGDHMQVTPRLFSVPRDKSARhTLL 963
Cdd:TIGR00376 339 neilAESDATNSmagseilngqYFDVAVIDEASQAMEPSCLIPLLKA---RKLILAGDHKQLPPTILSHDAEELSL-TLF 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 964 HRLflyyqqeAHKIAQQSRIIfHENYRSTAAIINFVSHHFYLAKgnpIQASGKVPRH-----------------PQHYPL 1026
Cdd:TIGR00376 415 ERL-------IKEYPERSRTL-NVQYRMNQKIMEFPSREFYNGK---LTAHESVANIllrdlpkveateseddlETGIPL 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1027 MFCHVAG---SPEQDMSMTSWLNSAEVTQVVEKVREI--YNTwphcwgPREQrhICAVS-HGAQVSALRQELRRRNLgEV 1100
Cdd:TIGR00376 484 LFIDTSGcelFELKEADSTSKYNPGEAELVSEIIQALvkMGV------PAND--IGVITpYDAQVDLLRQLLEHRHI-DI 554
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568920187 1101 SVGSFEILPGREFRVVVLSSVH-NRNSLLSpgaptseFFTEPRVLNTVMTRAQSQLVAVGD 1160
Cdd:TIGR00376 555 EVSSVDGFQGREKEVIIISFVRsNRKGEVG-------FLKDLRRLNVALTRARRKLIVIGD 608
|
|
| DEXXQc_DNA2 |
cd18041 |
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ... |
2448-2724 |
2.01e-20 |
|
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5-3 helicase, and endonuclease activities, and is involved in DNA replication and DNA repair in the nucleus and mitochondrion. It is involved in Okazaki fragment processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. It is also involved in 5-end resection of DNA during double-strand break (DSB) repair; it is recruited by BLM and mediates the cleavage of 5-ssDNA, while the 3-ssDNA cleavage is prevented by the presence of RPA. DNA2 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: 350799 [Multi-domain] Cd Length: 203 Bit Score: 91.91 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2448 KLNQSQDRAVRSALQ-KQFTVIQGPPGTGKTVVGFHIVYWFHRSNQeqmptdsspsgeeqlggpCVLYCGPSNKSVDVLG 2526
Cdd:cd18041 1 GLNKDQRQAIKKVLNaKDYALILGMPGTGKTTTIAALVRILVALGK------------------SVLLTSYTHSAVDNIL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2527 GLLLRRKTEMkpLRVYgeqaeatefplpgvsnrslfgktsqegrpnqslRSITLHHRIRQapnPYAAEIRKfdaqlregK 2606
Cdd:cd18041 63 LKLKKFGVNF--LRLG---------------------------------RLKKIHPDVQE---FTLEAILK--------S 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2607 IFSKEDLrvyrrvlgkarKHELERHSVILCTCSCAASKslkILNVRQI---LIDEAGMATEPETLIPLVCfsktVEKVVL 2683
Cdd:cd18041 97 CKSVEEL-----------ESKYESVSVVATTCLGINHP---IFRRRTFdycIVDEASQITLPICLGPLRL----AKKFVL 158
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 568920187 2684 LGDHKQLRPVVKSEQLQSLGMDRSLFERY---HRDAI-MLDTQYR 2724
Cdd:cd18041 159 VGDHYQLPPLVKSREARELGMDESLFKRLseaHPDAVvQLTIQYR 203
|
|
| DEXXQc_Mov10L1 |
cd18078 |
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ... |
2448-2718 |
2.53e-20 |
|
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. Mov10L1 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: 350836 [Multi-domain] Cd Length: 230 Bit Score: 92.43 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2448 KLNQSQDRAVRSALQKQFT----VIQGPPGTGKTVVG----FHIVYWFHRSNqeqmptdsspsgeeqlggpcVLYCGPSN 2519
Cdd:cd18078 1 DLNELQKEAVKRILGGECRplpyILFGPPGTGKTVTIieaiLQVVYNLPRSR--------------------ILVCAPSN 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2520 KSVDvlggLLLRRKTEMKPLRvygeqaeatefplpgvsnrslfgktsqegrPNQSLRSITLHHRIRQAPNPyaaeirkfd 2599
Cdd:cd18078 61 SAAD----LVTSRLHESKVLK------------------------------PGDMVRLNAVNRFESTVIDA--------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2600 aqlregkifskedlrVYRRVLGKARKHELERHSVILCTCSCAASK---SLKILNVRQILIDEAGMATEPETLIPLVCFSK 2676
Cdd:cd18078 98 ---------------RKLYCRLGEDLSKASRHRIVISTCSTAGLLyqmGLPVGHFTHVFVDEAGQATEPESLIPLGLISS 162
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 568920187 2677 TVEKVVLLGDHKQLRPVVKSEQLQSLGMDRSLFER------YHRDAIM 2718
Cdd:cd18078 163 RDGQIILAGDPMQLGPVIKSRLASAYGLGVSFLERlmnrplYLRDPNR 210
|
|
| DEXXQc_Upf1-like |
cd17934 |
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ... |
2650-2724 |
1.30e-18 |
|
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), coronavirus Nsp13, and similar proteins. They belong to 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: 438708 [Multi-domain] Cd Length: 121 Bit Score: 83.82 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2650 NVRQILIDEAGMATEPETLIPLVCfsktVEKVVLLGDHKQLRPVVKSEQLQSLG-------MDRSLFERYHRDAIMLDTQ 2722
Cdd:cd17934 44 NVDVVIIDEASQITEPELLIALIR----AKKVVLVGDPKQLPPVVQEDHAALLGlsfilslLLLFRLLLPGSPKVMLDTQ 119
|
..
gi 568920187 2723 YR 2724
Cdd:cd17934 120 YR 121
|
|
| DEXXQc_SMUBP2 |
cd18044 |
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ... |
762-967 |
9.76e-16 |
|
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, or IGHMBP2) is a 5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction. It is a DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence (5'-GGGCT-3') related to the immunoglobulin mu chain switch region. The IGHMBP2 gene is responsible for Charcot-Marie-Tooth disease (CMT) type 2S and spinal muscular atrophy with respiratory distress type 1 (SMARD1). It is also thought to play a role in frontotemporal dementia (FTD) with amyotrophic lateral sclerosis (ALS) and major depressive disorder (MDD). SMUBP2 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: 350802 [Multi-domain] Cd Length: 191 Bit Score: 78.04 E-value: 9.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 762 NHKQKLAVGLIAGRRPEGtkhipplLIYGPFGTGKTYTLAMAALEVVQQpHTKVLICTHTNSAADIYIREYFHDYVSS-- 839
Cdd:cd18044 3 NDSQKEAVKFALSQKDVA-------LIHGPPGTGKTTTVVEIILQAVKR-GEKVLACAPSNIAVDNLVERLVALKVKVvr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 840 -GHPEatplRVMYAdrpprqtdpttLQYCCLTEdrqafrpptgpeLVHHRLVVTTTSQARELQV-PAGFFSHIFIDEAAQ 917
Cdd:cd18044 75 iGHPA----RLLES-----------VLDHSLDA------------LVAAQVVLATNTGAGSRQLlPNELFDVVVIDEAAQ 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568920187 918 MLECEALIPLsyaLSLTRVVLAGDHMQVTPRLFSvprDKSARHTLLHRLF 967
Cdd:cd18044 128 ALEASCWIPL---LKARRCILAGDHKQLPPTILS---DKAARGGLGVTLF 171
|
|
| EEXXEc_NFX1 |
cd17936 |
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ... |
2449-2711 |
1.41e-15 |
|
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that represses class II MHC (major histocompatibility complex) gene expression. NFX1 binds a conserved cis-acting element, termed the X-box, in promoters of human class II MHC genes. The Cys-rich region contains several NFX1-type zinc finger domains. Frequently, a R3H domain is present in the C-terminus, and a RING finger domain and a PAM2 motif are present in the N-terminus. The lack of R3H and PAM2 motifs in the plant proteins indicates functional differences. Plant NFX1-like proteins are proposed to modulate growth and survival by coordinating reactive oxygen species, salicylic acid, further biotic stress and abscisic acid responses. A common feature of all members may be E3 ubiquitin ligase, due to the presence of a RING finger domain, as well as DNA binding. NFX1 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: 350694 [Multi-domain] Cd Length: 178 Bit Score: 77.20 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2449 LNQSQDRAVRSALQKQFTVIQGPPGTGKTVVGFHIVYWFHRsNQEQMPTdsspsgeeqlgGP--CVLYcgpSNKSVD-VL 2525
Cdd:cd17936 2 LDPSQLEALKHALTSELALIQGPPGTGKTFLGVKLVRALLQ-NQDLSIT-----------GPilVVCY---TNHALDqFL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2526 GGLLlrrktemkplrvygeqaeatefplpgvsnrslfgktsqegrpnqslrsitlhhrirqapnpyaaeirkfdaqlreg 2605
Cdd:cd17936 67 EGLL---------------------------------------------------------------------------- 70
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2606 KIFSKEDLRVYRRVLGkarkhelerhsvilCTCSCAASKS--LKILNVRQILIDEAGMATEPETLiplVCFSKTVEKVVL 2683
Cdd:cd17936 71 DFGPTKIVRLGARVIG--------------MTTTGAAKYRelLQALGPKVVIVEEAAEVLEAHIL---AALTPSTEHLIL 133
|
250 260 270
....*....|....*....|....*....|
gi 568920187 2684 LGDHKQLRPVVKSEQLQSLG--MDRSLFER 2711
Cdd:cd17936 134 IGDHKQLRPKVNVYELTAKKynLDVSLFER 163
|
|
| EEXXQc_AQR |
cd17935 |
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ... |
2446-2731 |
4.26e-14 |
|
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds precursor-mRNA introns at a defined position and is part of a pentameric intron-binding complex (IBC). It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350693 [Multi-domain] Cd Length: 207 Bit Score: 73.62 E-value: 4.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2446 HHKLNQSQDRAVRSALQKQFTVIQGPPGTGKTVVGFHIVywfhrsnqeqmptdsspsgeeqlggpCVLYcgpsnksvdvl 2525
Cdd:cd17935 3 TVKFTPTQIEAIRSGMQPGLTMVVGPPGTGKTDVAVQII--------------------------SNLY----------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2526 gglllrrktemkplrvygeqaeatefplpgvsnrslfgktsqEGRPNQslRSITLHHRiRQAPNPYAAEIRKFDaqlreg 2605
Cdd:cd17935 46 ------------------------------------------HNFPNQ--RTLIVTHS-NQALNQLFEKIMALD------ 74
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2606 kIFSKEDLRvyrrvLGKARKhelerhsVILCTCSCAASK--SLKILNVR--QILIDEAGMATEPETLIPLV-----CFSK 2676
Cdd:cd17935 75 -IDERHLLR-----LGHGAK-------IIAMTCTHAALKrgELVELGFKydNILMEEAAQILEIETFIPLLlqnpeDGPN 141
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 568920187 2677 TVEKVVLLGDHKQLRPVVKSEQLQSLG-MDRSLFERYHR---DAIMLDTQYRMHKDICS 2731
Cdd:cd17935 142 RLKRLIMIGDHHQLPPVIKNMAFQKYSnMEQSLFTRLVRlgvPTVDLDAQGRARASISS 200
|
|
| DEXXQc_UPF1 |
cd18039 |
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ... |
787-951 |
1.35e-12 |
|
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of Nonsense Transcripts, or ATP-Dependent Helicase RENT1) is an RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. It is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. It is recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) located downstream from the termination codon through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Diseases associated with UPF1 include juvenile amyotrophic lateral sclerosis and epidermolysis bullosa, junctional, non-Herlitz type. UPF1 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: 350797 [Multi-domain] Cd Length: 234 Bit Score: 69.97 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 787 LIYGPFGTGKTYTLAMAALEVVQQPHTKVLICTHTNSAADiYIREYFHdyvssghpeATPLRV--MYADRppRQTDPTTL 864
Cdd:cd18039 20 LIQGPPGTGKTVTSATIVYHLVKQGNGPVLVCAPSNVAVD-QLTEKIH---------QTGLKVvrLCAKS--REAVESPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 865 QYCCL------------TEDRQAFRPPTGpEL--------------VHHRL-----VVTTTSqarelqVPAG-------F 906
Cdd:cd18039 88 SFLALhnqvrnldsaekLELLKLLKLETG-ELssadekryrklkrkAERELlrnadVICCTC------VGAGdprlskmK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568920187 907 FSHIFIDEAAQMLECEALIPLsyALSLTRVVLAGDHMQVTPRLFS 951
Cdd:cd18039 161 FRTVLIDEATQATEPECLIPL--VHGAKQVILVGDHCQLGPVVMC 203
|
|
| DEXXQc_Upf1-like |
cd17934 |
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ... |
786-990 |
5.97e-11 |
|
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), coronavirus Nsp13, and similar proteins. They belong to 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: 438708 [Multi-domain] Cd Length: 121 Bit Score: 62.25 E-value: 5.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 786 LLIYGPFGTGKTYTLAMAALEVVQQPHTK-VLICTHTNSAADiyireyfhdyvssghpeatplrvmyadrpprqtdpttl 864
Cdd:cd17934 2 SLIQGPPGTGKTTTIAAIVLQLLKGLRGKrVLVTAQSNVAVD-------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 865 qyccltedrqafrpptgpelvhhrlVVTTtsqarelqvpagffshIFIDEAAQMLECEALIPLSYAlslTRVVLAGDHMQ 944
Cdd:cd17934 44 -------------------------NVDV----------------VIIDEASQITEPELLIALIRA---KKVVLVGDPKQ 79
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568920187 945 VTPRLFSVPRDKSARHTLLHRLFLyyqqEAHKIAQQSRIIFHENYR 990
Cdd:cd17934 80 LPPVVQEDHAALLGLSFILSLLLL----FRLLLPGSPKVMLDTQYR 121
|
|
| PRK05054 |
PRK05054 |
exoribonuclease II; Provisional |
1559-1918 |
8.22e-11 |
|
exoribonuclease II; Provisional
Pssm-ID: 179920 [Multi-domain] Cd Length: 644 Bit Score: 67.59 E-value: 8.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1559 ELNTAAGHREDYRHFLTFTVDPQGACNLDDALSVRDLGPV-YEVAVHIADVASLVPKDGALDVEARQQGTVFYAPNREpV 1637
Cdd:PRK05054 182 EMLDEGLEREDLTALDFVTIDSASTEDMDDALYVEKLPDGgLQLTVAIADPTAYIAEGSKLDKAARQRAFTNYLPGFN-I 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1638 LMLPASLCQDALSLLPGQDRLAISLFLTMEKGGGQIKSLRFAPSIIRSDRQLSYEEAEELIKrhpGAGLELPAhlDSVEA 1717
Cdd:PRK05054 261 PMLPRELSDDLCSLRPNERRPALACRVTIDADGTIEDDIRFFAAWIESKAKLAYDNVSDWLE---NGGDWQPE--SEAIA 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1718 CVVAACYFSWMLRRQ--RLSAACYYEPPDEDSVLG------------FRTAHIMVQEYMIQFNSHVAEFLVSNKHTqtlt 1783
Cdd:PRK05054 336 EQIRLLHQFCLARSEwrKQHALVFKDRPDYRFELGekgevldivaepRRIANRIVEESMIAANICAARVLRDKLGF---- 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1784 plrwqptpsrqqldSVFKKYRGLVPLSL----HLCHHSNTDYTPNKqlhlLTSLwkqvqlaagtQDYSQMVDLIaadDMH 1859
Cdd:PRK05054 412 --------------GIYNVHSGFDPANAeqavALLKEHGLHFDAEE----LLTL----------EGFCKLRREL---DAQ 460
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568920187 1860 PSlapACLD--LRRALGRSVFgrssqgKQQPAVHHSLQVDWY-TWaTSPIRRYLDVVLQRLI 1918
Cdd:PRK05054 461 PT---GYLDsrIRRFQSFAEI------STEPGPHFGLGLEAYaTW-TSPIRKYGDMINHRLL 512
|
|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
2618-2723 |
4.11e-10 |
|
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. 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. SF1 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: 438706 [Multi-domain] Cd Length: 121 Bit Score: 59.81 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2618 RVLGKARKHELERHSVILCTCSCAASKSLkilnvRQILIDEAGMATEPETLIPlVCFSKTVEKVVLLGDHKQLRPVVKSE 2697
Cdd:cd17914 19 IVAALMQNKNGEPGRILLVTPTNKAAAQL-----DNILVDEAAQILEPETSRL-IDLALDQGRVILVGDHDQLGPVWRGA 92
|
90 100
....*....|....*....|....*....
gi 568920187 2698 QLQSLGMDRSLFER--YHRDA-IMLDTQY 2723
Cdd:cd17914 93 VLAKICNEQSLFTRlvRLGVSlIRLQVQY 121
|
|
| DEXXQc_DNA2 |
cd18041 |
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ... |
762-947 |
4.91e-10 |
|
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5-3 helicase, and endonuclease activities, and is involved in DNA replication and DNA repair in the nucleus and mitochondrion. It is involved in Okazaki fragment processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. It is also involved in 5-end resection of DNA during double-strand break (DSB) repair; it is recruited by BLM and mediates the cleavage of 5-ssDNA, while the 3-ssDNA cleavage is prevented by the presence of RPA. DNA2 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: 350799 [Multi-domain] Cd Length: 203 Bit Score: 61.87 E-value: 4.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 762 NHKQKLAVGLIAGrrpegTKHIppLLIYGPFGTGKTYTLAmAALEVVQQPHTKVLICTHTNSAAD---IYIREYFHDYVS 838
Cdd:cd18041 3 NKDQRQAIKKVLN-----AKDY--ALILGMPGTGKTTTIA-ALVRILVALGKSVLLTSYTHSAVDnilLKLKKFGVNFLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 839 SG-----HPEATPLRVMyadrpprqtdpTTLQYCCLTEDRQAFrpptgpelVHHRLVVTTTSqarelqvpAGFFSHIF-- 911
Cdd:cd18041 75 LGrlkkiHPDVQEFTLE-----------AILKSCKSVEELESK--------YESVSVVATTC--------LGINHPIFrr 127
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568920187 912 -------IDEAAQMLECEALIPLSYAlslTRVVLAGDHMQVTP 947
Cdd:cd18041 128 rtfdyciVDEASQITLPICLGPLRLA---KKFVLVGDHYQLPP 167
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
765-951 |
5.88e-10 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Pssm-ID: 404072 [Multi-domain] Cd Length: 248 Bit Score: 62.36 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 765 QKLAVGLIAGRRPEGtkhipplLIYGPFGTGKTYTLamaaLEVVQQ----------PHTKVLICTHTNSAAD-IYIReyf 833
Cdd:pfam13086 2 QREAIRSALSSSHFT-------LIQGPPGTGKTTTI----VELIRQllsypatsaaAGPRILVCAPSNAAVDnILER--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 834 hdYVSSG-HPEATPLRVMYADRPPRQTDPTTLQYCC----------------------LTEDRQAFRPPTGPELVH---- 886
Cdd:pfam13086 68 --LLRKGqKYGPKIVRIGHPAAISEAVLPVSLDYLVesklnneedaqivkdiskelekLAKALRAFEKEIIVEKLLksrn 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 887 --------------------------------------HRLVVTT-TSQARELQVPAGFFSHIFIDEAAQMLECEALIPL 927
Cdd:pfam13086 146 kdkskleqerrklrserkelrkelrrreqslereildeAQIVCSTlSGAGSRLLSSLANFDVVIIDEAAQALEPSTLIPL 225
|
250 260
....*....|....*....|....
gi 568920187 928 SYALSltRVVLAGDHMQVTPRLFS 951
Cdd:pfam13086 226 LRGPK--KVVLVGDPKQLPPTVIS 247
|
|
| DEXXQc_SETX |
cd18042 |
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ... |
787-967 |
8.00e-09 |
|
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in transcription, neurogenesis, and antiviral response. SEXT is an R-loop-associated protein that is thought to function as an RNA/DNA helicase. R-loops consist of RNA/DNA hybrids, formed during transcription when nascent RNA hybridizes to the DNA template strand, displacing the non-template DNA strand. Mutations in SETX are linked to two neurodegenerative disorders: ataxia with oculomotor apraxia type 2 (AOA2) and amyotrophic lateral sclerosis type 4 (ALS4). S. cerevisiae homolog splicing endonuclease 1 (Sen1) is an exclusively nuclear protein, important for nucleolar organization. S. cerevisiae Sen1 and its ortholog, the Schizosaccharomyces pombe Sen1, share conserved domains and belong to the family I class of helicases. Both proteins translocate 5' to 3' and unwind both DNA and RNA duplexes and also RNA/DNA hybrids in vitro. SETX 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: 438712 [Multi-domain] Cd Length: 218 Bit Score: 58.38 E-value: 8.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 787 LIYGPFGTGKTYTLaMAALEVV-------------------------QQPHTKVLICTHTNSAADiyireyfhdyvssgh 841
Cdd:cd18042 21 LIQGPPGTGKTKTI-VGILSVLlagkyrkyyekvkkklrklqrnlnnKKKKNRILVCAPSNAAVD--------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 842 pEATpLRVMYAdrPPRQTDPTTLQYCCLTEDRQAFRPptgpELVHHRLVVTTT---SQARELQVPAGFFSHIFIDEAAQM 918
Cdd:cd18042 85 -EIV-LRLLSE--GFLDGDGRSYKPNVVRVGRQELRA----SILNEADIVCTTlssSGSDLLESLPRGFDTVIIDEAAQA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568920187 919 LECEALIPLsyALSLTRVVLAGDHMQVTPRLFSvprdKSARHTLLHR-LF 967
Cdd:cd18042 157 VELSTLIPL--RLGCKRLILVGDPKQLPATVFS----KVAQKLGYDRsLF 200
|
|
| DEXXQc_HELZ |
cd18077 |
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ... |
2625-2711 |
2.15e-08 |
|
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. HELZ is a member of the family I class of RNA helicases 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: 350835 [Multi-domain] Cd Length: 226 Bit Score: 57.50 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2625 KHELERHSVI---LCTCSCAASKSLKILNVRQILIDEAGMATEPETLIPLVCFSKTVeKVVLLGDHKQLRPVVKSEQLQS 2701
Cdd:cd18077 118 REDVMRHRVVvvtLSTSQYLCQLDLEPGFFTHILLDEAAQAMECEAIMPLALATKST-RIVLAGDHMQLSPEVYSEFARE 196
|
90
....*....|
gi 568920187 2702 LGMDRSLFER 2711
Cdd:cd18077 197 RNLHISLLER 206
|
|
| SF1_C |
cd18786 |
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ... |
2815-2907 |
8.12e-08 |
|
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Similar to SF2 helicases, they do not form toroidal, predominantly hexameric structures like SF3-6. SF1 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: 350173 [Multi-domain] Cd Length: 89 Bit Score: 52.05 E-value: 8.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2815 DIAVLTPYNAQAAAISRGLMQRGVTG-----VTVTSITKSQGSEWRYVIVStvrtCPRSDVDqrptkswlkkflgfvvDP 2889
Cdd:cd18786 12 KGVVLTPYHRDRAYLNQYLQGLSLDEfdlqlVGAITIDSSQGLTFDVVTLY----LPTANSL----------------TP 71
|
90
....*....|....*...
gi 568920187 2890 HQVNVAITRAQEALCIIG 2907
Cdd:cd18786 72 RRLYVALTRARKRLVIYD 89
|
|
| PRK11642 |
PRK11642 |
ribonuclease R; |
1567-1928 |
1.78e-07 |
|
ribonuclease R;
Pssm-ID: 236944 [Multi-domain] Cd Length: 813 Bit Score: 57.06 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1567 REDYRHFLTFTVDPQGACNLDDALSV-RDLGPVYEVAVHIADVASLVPKDGALDVEARQQGTVFYAPNrEPVLMLPASLC 1645
Cdd:PRK11642 260 RVDLRDLPLVTIDGEDARDFDDAVYCeKKRGGGWRLWVAIADVSYYVRPPTPLDREARNRGTSVYFPS-QVVPMLPEVLS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1646 QDALSLLPGQDRLAISLFLTMEkGGGQIKSLRFAPSIIRSDRQLSY------------------------EEAEELIKRH 1701
Cdd:PRK11642 339 NGLCSLNPQVDRLCMVCEMTIS-SKGRLTGYKFYEAVMSSHARLTYtkvwhilqgdqdlreqyaplvkhlEELHNLYKVL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1702 PGAGLELPA-HLDSVEACVVaacyFSWMLRRQRLsaacyyEPPDEDSvlgfrtAHIMVQEYMIQFNSHVAEFLVSNKHTQ 1780
Cdd:PRK11642 418 DKAREERGGiSFESEEAKFI----FNAERRIERI------EQTQRND------AHKLIEECMILANISAARFVEKAKEPA 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 1781 TltpLRWQPTPSRQQ---LDSVFKKyrglvpLSLhlchhsntdytpnkqlhlltslwkqvQLAAGTQ----DYSQMVDLI 1853
Cdd:PRK11642 482 L---FRIHDKPSTEAitsFRSVLAE------LGL--------------------------ELPGGNKpeprDYAELLESV 526
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568920187 1854 AADDMHPSLAPACLdlrRALGRSVFGRSSQGkqqpavHHSLQVDWYTWATSPIRRYLDVVLQRLI--LLA--LGHRGST 1928
Cdd:PRK11642 527 ADRPDAEMLQTMLL---RSMKQAIYDPENRG------HFGLALQSYAHFTSPIRRYPDLSLHRAIkyLLAkeQGHKGNT 596
|
|
| EEXXQc_AQR |
cd17935 |
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ... |
757-947 |
4.24e-07 |
|
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds precursor-mRNA introns at a defined position and is part of a pentameric intron-binding complex (IBC). It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350693 [Multi-domain] Cd Length: 207 Bit Score: 53.20 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 757 PSFRGNHKQKLAVglIAGRRPEGTkhipplLIYGPFGTGKTyTLAMAALEVVQQ--PHTKVLICTHTNSAadiyIREYFH 834
Cdd:cd17935 2 NTVKFTPTQIEAI--RSGMQPGLT------MVVGPPGTGKT-DVAVQIISNLYHnfPNQRTLIVTHSNQA----LNQLFE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 835 dyvssghpeatplRVMYADrpprqtdpttlqycclTEDRQAFRPPTGPELVhhrlVVTTTSQARELQ--VPAGF-FSHIF 911
Cdd:cd17935 69 -------------KIMALD----------------IDERHLLRLGHGAKII----AMTCTHAALKRGelVELGFkYDNIL 115
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568920187 912 IDEAAQMLECEALIPLSYALS------LTRVVLAGDHMQVTP 947
Cdd:cd17935 116 MEEAAQILEIETFIPLLLQNPedgpnrLKRLIMIGDHHQLPP 157
|
|
| DEXXQc_SF1 |
cd18043 |
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ... |
2450-2477 |
8.13e-07 |
|
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are nucleic acid motor proteins that couple ATP hydrolysis to translocation along with the concomitant unwinding of DNA or RNA. This is central to many aspects of cellular DNA and RNA metabolism and accordingly, they are implicated in a wide range of nucleic acid processing events including DNA replication, recombination, and repair as well as many aspects of RNA metabolism. Superfamily 1 helicases are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350801 [Multi-domain] Cd Length: 127 Bit Score: 50.27 E-value: 8.13e-07
10 20
....*....|....*....|....*...
gi 568920187 2450 NQSQDRAVRSALQKQFTVIQGPPGTGKT 2477
Cdd:cd18043 1 DSSQEAAIISARNGKNVVIQGPPGTGKS 28
|
|
| SF1_C_UvrD |
cd18807 |
C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase ... |
2793-2907 |
1.06e-06 |
|
C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. This family also includes ATP-dependent helicase/nuclease AddA and helicase/nuclease RecBCD subunit RecB, among others. UvrD family helicases are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350194 [Multi-domain] Cd Length: 150 Bit Score: 50.69 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2793 EEVTQVVRIIKQLTLDRTVDPKDIAVLTPYNAQAAAISRGLMqrgvtgVTVTSITKSQGSEWRYVIVstvrtcPRSDVDQ 2872
Cdd:cd18807 44 DEAKAIADEIKRLIESGPVQYSDIAILVRTNRQARVIEEALR------VTLMTIHASKGLEFPVVFI------VGLGEGF 111
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 568920187 2873 RPTKSWLKKFLgfvVDPHQVN-------VAITRAQEALCIIG 2907
Cdd:cd18807 112 IPSDASYHAAK---EDEERLEeerrllyVALTRAKKELYLVG 150
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
2443-2913 |
5.08e-06 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 51.90 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2443 PAGHHKLNQSQDRAVRSALQK-QFTVIQGPPGTGKT-VVGfHIVYWFhrsnqeqmptdsspsgeEQLGGPCVLyCGPSNK 2520
Cdd:COG0507 119 PRAGITLSDEQREAVALALTTrRVSVLTGGAGTGKTtTLR-ALLAAL-----------------EALGLRVAL-AAPTGK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2521 SVDVLgglllrrktemkplrvygeqAEATefplpgvsnrslfGKTSQegrpnqslrsiTLHHRIRQAPNpyaaeirkfda 2600
Cdd:COG0507 180 AAKRL--------------------SEST-------------GIEAR-----------TIHRLLGLRPD----------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2601 qlregkifskedlrvyRRVLGKARKHELERHSVilctcscaaskslkilnvrqILIDEAGMATEP--ETLIPLVCFSKTv 2678
Cdd:COG0507 205 ----------------SGRFRHNRDNPLTPADL--------------------LVVDEASMVDTRlmAALLEALPRAGA- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2679 eKVVLLGDHKQLRPVVKSEQLqslgmdRSLFERYHRDAIMLDTQYRMHKDicsfpsvefyGGKLKTWSDLRRlpsilght 2758
Cdd:COG0507 248 -RLILVGDPDQLPSVGAGAVL------RDLIESGTVPVVELTEVYRQADD----------SRIIELAHAIRE-------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2759 gkpscsvifgsvqGHEQKLLvsTEDGNENSRANPEEVTQVVRIIKQLTLDRTVDPKDIAVLTPYNAQAAAISRGL----- 2833
Cdd:COG0507 303 -------------GDAPEAL--NARYADVVFVEAEDAEEAAEAIVELYADRPAGGEDIQVLAPTNAGVDALNQAIrealn 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2834 -----------------------MQR----------GVTGvTVTSIT--------------------------------- 2847
Cdd:COG0507 368 pagelerelaedgelelyvgdrvMFTrndydlgvfnGDIG-TVLSIDedegrltvrfdgreivtydpseldqlelayait 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568920187 2848 --KSQGSEWRYVIVstvrtcprsDVDQRPTKswlkkflgfVVDPHQVNVAITRAQEALCIIGDHLLLR 2913
Cdd:COG0507 447 vhKSQGSTFDRVIL---------VLPSEHSP---------LLSRELLYTALTRARELLTLVGDRDALA 496
|
|
| DEXXc_HELZ2-C |
cd18040 |
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
883-982 |
9.63e-06 |
|
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB and RXRA. It belongs to 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: 350798 [Multi-domain] Cd Length: 271 Bit Score: 49.83 E-value: 9.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 883 ELVHHRLVVTTTSQA--RELQVPAGFfSHIFIDEAAQMLECEALIPLSYALSLTRVVLAGDHMQVTPrlfsVPRDKSARH 960
Cdd:cd18040 174 ELETVDVILCTCSEAasQKMRTHANV-KQCIVDECGMCTEPESLIPIVSAPRAEQVVLIGDHKQLRP----VVQNKEAQK 248
|
90 100
....*....|....*....|...
gi 568920187 961 TLLHR-LFLYYQQEAHKIAQQSR 982
Cdd:cd18040 249 LGLGRsLFERYAEKACMLDTQYR 271
|
|
| CoV_Nsp13-helicase |
cd21718 |
helicase domain of coronavirus non-structural protein 13; This model represents the helicase ... |
2654-2908 |
1.47e-05 |
|
helicase domain of coronavirus non-structural protein 13; This model represents the helicase domain of non-structural protein 13 (Nsp13) from alpha-, beta-, gamma-, and deltacoronavirus, including pathogenic human viruses such as Severe acute respiratory syndrome coronavirus (SARS-CoV), SARS-CoV2 (also called 2019 novel CoV or 2019-nCoV), and Middle East respiratory syndrome-related (MERS) CoV. Helicases catalyze NTP-dependent unwinding of nucleic acid duplexes into single strands and are classified based on the arrangement of conserved motifs into six superfamilies. CoV Nsp13 is a member of the helicase superfamily 1 (SF1); SF1 and SF2 helicases do not form toroidal structures, while SF3-6 helicases do. Nsp13 is a component of the viral RNA synthesis replication and transcription complex (RTC). It is a multidomain protein containing a Cys/His rich zinc-binding domain (CH/ZBD), a stalk domain, a 1B domain involved in nucleic acid substrate binding, and a SF1 helicase core.
Pssm-ID: 409652 [Multi-domain] Cd Length: 341 Bit Score: 49.84 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2654 ILIDEAGMATEPEtlIPLVCFSKTVEKVVLLGDHKQL---RPVVKSEQLQSLGMDRSLFERYHRDA-IMLDTQYRMHKDI 2729
Cdd:cd21718 121 VVVDEVSMCTNYD--LSVVNARLKYKHIVYVGDPAQLpapRTLLTEGSLEPKDYNVVTRLMVGSGPdVFLSKCYRCPKEI 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2730 CSFPSVEFYGGKLKTWSDLRRlpsilghtgkpSCSVIFG-SVQGHEqkllvstedgneNSRANPEEVTQVVRIIkqltLD 2808
Cdd:cd21718 199 VDTVSKLVYDNKLKAIKPKSR-----------QCFKTFGkGDVRHD------------NGSAINRPQLEFVKRF----LD 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2809 RTVDPKDIAVLTPYNAQAAAISRGLmqrgvtGVTVTSITKSQGSEWRYVIVstvrtCPRSDVDQrptkswlkkflgfVVD 2888
Cdd:cd21718 252 RNPRWRKAVFISPYNAMNNRASRLL------GLSTQTVDSSQGSEYDYVIF-----CQTTDTAH-------------ALN 307
|
250 260
....*....|....*....|.
gi 568920187 2889 PHQVNVAITRAQEA-LCIIGD 2908
Cdd:cd21718 308 INRFNVAITRAKHGiLVIMRD 328
|
|
| EEXXEc_NFX1 |
cd17936 |
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ... |
787-949 |
1.49e-05 |
|
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that represses class II MHC (major histocompatibility complex) gene expression. NFX1 binds a conserved cis-acting element, termed the X-box, in promoters of human class II MHC genes. The Cys-rich region contains several NFX1-type zinc finger domains. Frequently, a R3H domain is present in the C-terminus, and a RING finger domain and a PAM2 motif are present in the N-terminus. The lack of R3H and PAM2 motifs in the plant proteins indicates functional differences. Plant NFX1-like proteins are proposed to modulate growth and survival by coordinating reactive oxygen species, salicylic acid, further biotic stress and abscisic acid responses. A common feature of all members may be E3 ubiquitin ligase, due to the presence of a RING finger domain, as well as DNA binding. NFX1 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: 350694 [Multi-domain] Cd Length: 178 Bit Score: 47.92 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 787 LIYGPFGTGKTYT---LAMAALEVVQQPHTK-VLICTHTNSAADiyireYFhdyvSSGHPEATPLRVMyadRpprqtdpt 862
Cdd:cd17936 20 LIQGPPGTGKTFLgvkLVRALLQNQDLSITGpILVVCYTNHALD-----QF----LEGLLDFGPTKIV---R-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 863 tlqyccltedrqafrpptgpelVHHRLV-VTTTSQARELQVPAGF-FSHIFIDEAAQMLECE---ALIPlsyalSLTRVV 937
Cdd:cd17936 80 ----------------------LGARVIgMTTTGAAKYRELLQALgPKVVIVEEAAEVLEAHilaALTP-----STEHLI 132
|
170
....*....|..
gi 568920187 938 LAGDHMQVTPRL 949
Cdd:cd17936 133 LIGDHKQLRPKV 144
|
|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
2466-2529 |
2.50e-05 |
|
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. 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. SF1 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: 438706 [Multi-domain] Cd Length: 121 Bit Score: 45.94 E-value: 2.50e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568920187 2466 TVIQGPPGTGKTVVGFHIVYWFHRsnqeqmptdsspsgeEQLGGPC-VLYCGPSNKSVDVLGGLL 2529
Cdd:cd17914 2 SLIQGPPGTGKTRVLVKIVAALMQ---------------NKNGEPGrILLVTPTNKAAAQLDNIL 51
|
|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
785-832 |
6.63e-05 |
|
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. 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. SF1 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: 438706 [Multi-domain] Cd Length: 121 Bit Score: 44.78 E-value: 6.63e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 568920187 785 PLLIYGPFGTGKTYTLAMAALEVVQQPHT---KVLICTHTNSAAD----IYIREY 832
Cdd:cd17914 1 LSLIQGPPGTGKTRVLVKIVAALMQNKNGepgRILLVTPTNKAAAqldnILVDEA 55
|
|
| DEXXQc_HELZ2-N |
cd18076 |
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
2625-2692 |
2.22e-04 |
|
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB, and RXRA. It belongs to 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: 350834 [Multi-domain] Cd Length: 230 Bit Score: 45.27 E-value: 2.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2625 KHELERHSVILCTCSCAasKSLKILN--VRQILIDEAGMATEPETLIPLvCFSKTVEKVVLLGDHKQLRP 2692
Cdd:cd18076 121 RDELDFHNIVITTTAMA--FNLHVLSgfFTHIFIDEAAQMLECEALIPL-SYAGPKTRVVLAGDHMQMTP 187
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
2453-2477 |
3.08e-04 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD 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: 350691 [Multi-domain] Cd Length: 155 Bit Score: 43.70 E-value: 3.08e-04
10 20
....*....|....*....|....*
gi 568920187 2453 QDRAVRSALQKQFTVIQGPPGTGKT 2477
Cdd:cd17933 2 QKAAVRLVLRNRVSVLTGGAGTGKT 26
|
|
| betaCoV_Nsp13-helicase |
cd21722 |
helicase domain of betacoronavirus non-structural protein 13; This model represents the ... |
2717-2911 |
3.10e-04 |
|
helicase domain of betacoronavirus non-structural protein 13; This model represents the helicase domain of non-structural protein 13 (Nsp13) from betacoronavirus, including pathogenic human viruses such as Severe acute respiratory syndrome coronavirus (SARS-CoV), SARS-CoV2 (also called 2019 novel CoV or 2019-nCoV), and Middle East respiratory syndrome-related (MERS) CoV. Helicases catalyze NTP-dependent unwinding of nucleic acid duplexes into single strands and are classified based on the arrangement of conserved motifs into six superfamilies. CoV Nsp13 is a member of the helicase superfamily 1 (SF1); SF1 and SF2 helicases do not form toroidal structures, while SF3-6 helicases do. Nsp13 is a component of the viral RNA synthesis replication and transcription complex (RTC). It is a multidomain protein containing a Cys/His rich zinc-binding domain (CH/ZBD), a stalk domain, a 1B domain involved in nucleic acid substrate binding, and a SF1 helicase core.
Pssm-ID: 409655 [Multi-domain] Cd Length: 340 Bit Score: 45.95 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2717 IMLDTQYRMHKDICSFPSVEFYGGKLKTwsdlrrlpsilghtGKPSCSVIFgsvqgheqKLLVSTEDGNENSRA-NPEEV 2795
Cdd:cd21722 186 IFLGTCYRCPKEIVDTVSALVYDNKLKA--------------KKDNSGQCF--------KVYYKGSVTHDSSSAiNRPQI 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2796 TQVVRIIKQltldrtvDPK--DIAVLTPYNAQAAAISRGLmqrGVTGVTVTSitkSQGSEWRYVIVS-TVRTCPRSDVDq 2872
Cdd:cd21722 244 YLVKKFLKA-------NPAwsKAVFISPYNSQNAVARRVL---GLQTQTVDS---SQGSEYDYVIYCqTAETAHSVNVN- 309
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568920187 2873 rptkswlkkflgfvvdphQVNVAITRAQEA-LCIIGDHLL 2911
Cdd:cd21722 310 ------------------RFNVAITRAKKGiLCVMSSMQL 331
|
|
| HelD |
COG3973 |
DNA helicase IV [Replication, recombination and repair]; |
2453-2482 |
5.97e-04 |
|
DNA helicase IV [Replication, recombination and repair];
Pssm-ID: 443173 [Multi-domain] Cd Length: 699 Bit Score: 45.63 E-value: 5.97e-04
10 20 30
....*....|....*....|....*....|
gi 568920187 2453 QDRAVRSALQKqFTVIQGPPGTGKTVVGFH 2482
Cdd:COG3973 196 QDRIIRADLRG-VLVVQGGAGSGKTAVALH 224
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
786-852 |
7.29e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 41.94 E-value: 7.29e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568920187 786 LLIYGPFGTGKTYTLAMAALEVVQQPHTKVLI-CTHTNSAADIYiREYFHDYVSSGHPEATPLRVMYA 852
Cdd:pfam13401 8 LVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVdLPSGTSPKDLL-RALLRALGLPLSGRLSKEELLAA 74
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
764-955 |
9.26e-04 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD 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: 350691 [Multi-domain] Cd Length: 155 Bit Score: 42.16 E-value: 9.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 764 KQKLAVGLIAGRRPegtkhippLLIYGPFGTGKTYTLAmAALEVVQQPHTKVLICTHTNSAADIyIREyfhdyvSSGHPE 843
Cdd:cd17933 1 EQKAAVRLVLRNRV--------SVLTGGAGTGKTTTLK-ALLAALEAEGKRVVLAAPTGKAAKR-LSE------STGIEA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 844 ATPLRVMYADrpPRQTDPTTLQYCCLTEDrqafrpptgpelvhhrLVVtttsqarelqvpagffshifIDEAAqMLEcea 923
Cdd:cd17933 65 STIHRLLGIN--PGGGGFYYNEENPLDAD----------------LLI--------------------VDEAS-MVD--- 102
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568920187 924 lIPLSYAL-----SLTRVVLAGDHMQ---VTPRlfSVPRD 955
Cdd:cd17933 103 -TRLMAALlsaipAGARLILVGDPDQlpsVGAG--NVLRD 139
|
|
| RecB |
COG1074 |
3#-5# helicase subunit RecB of the DNA repair enzyme RecBCD (exonuclease V) [Replication, ... |
2777-2838 |
4.11e-03 |
|
3#-5# helicase subunit RecB of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440692 [Multi-domain] Cd Length: 866 Bit Score: 42.64 E-value: 4.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 2777 LLVSTEDGNENSrANPEEVTQVVRIIKQLT--------LDRTVDPKDIAVLTPYNAQAAAISRGLMQRGV 2838
Cdd:COG1074 405 WPLEPDDVSEED-AREREARAVAARIRRLLaegttvegGGRPVRPGDIAVLVRTRSEAAAIARALKAAGI 473
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
786-915 |
6.08e-03 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 39.69 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920187 786 LLIYGPFGTGKTYTLAMAALEVVQQPHTKVLICTHTNS-AADIY--IREYFhdyvssghPEATPLRVMYADRPPRqtdpt 862
Cdd:cd00046 4 VLITAPTGSGKTLAALLAALLLLLKKGKKVLVLVPTKAlALQTAerLRELF--------GPGIRVAVLVGGSSAE----- 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 568920187 863 tlqyccltEDRQAFRPptgpelvHHRLVVTTTSQARELQVPAGF-----FSHIFIDEA 915
Cdd:cd00046 71 --------EREKNKLG-------DADIIIATPDMLLNLLLREDRlflkdLKLIIVDEA 113
|
|
| UvrD |
COG0210 |
Superfamily I DNA or RNA helicase [Replication, recombination and repair]; |
2793-2838 |
8.64e-03 |
|
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
Pssm-ID: 439980 [Multi-domain] Cd Length: 721 Bit Score: 41.84 E-value: 8.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 568920187 2793 EEVTQVVRIIKQLtLDRTVDPKDIAVLTPYNAQAAAISRGLMQRGV 2838
Cdd:COG0210 327 EEARFVADEIREL-HEEGVPLSDIAVLYRTNAQSRALEEALRRAGI 371
|
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| |
