|
Name |
Accession |
Description |
Interval |
E-value |
| Aquarius_N |
pfam16399 |
Intron-binding protein aquarius N-terminus; This family represents the N-terminus of ... |
18-802 |
0e+00 |
|
Intron-binding protein aquarius N-terminus; This family represents the N-terminus of intron-binding protein aquarius, a splicing factor which links excision of introns from pre-mRNA with snoRP assembly.
Pssm-ID: 435319 Cd Length: 791 Bit Score: 1221.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 18 INAEFVTQLACKYWAPHIK-KKSPFDIKVIEEIYEKEIVKSRFAIRKIMLLEFSQYLENYLWMNYSpEVSSKAYLMSICC 96
Cdd:pfam16399 1 IQEDRIAQLARKHWLKSKKsKKVKVKPEVVKKIYWDELEKEGFSLRSLLLLEFLQYLENYLWPNYT-EDASNAHVLLIVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 97 MVNEKFRENVPAWETFKKKPDHFPFFFKCILKAALAETdgeFSLHEQTLLLLFLDHCFNSLEVDLIRSQVQQLISLPMWM 176
Cdd:pfam16399 80 MVNEKFREHLPAWELFSDRPDDFSSFFRRVLSLSLDRS---LSTAERTALLSFLIHAFQSLENELVRKECAPLVSISIWH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 177 GL-QPARLELELKKTPKLRKFWNLIKKNDEKMDPEAREQAYQERRFLSRLIQKFISVLKSIPLSEPVTMDKVHYCERFIE 255
Cdd:pfam16399 157 NLsSEGRREQELDKNPQLRKAWRAAQKRYDAADDATKARLRFERSWLYTLLLDFLDVLYDIPEDGEVDDDNVRYCERFLE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 256 LMIDLEALLPTRRWFNTILDDSHLLVHCYLSSLVHREEdGHLFSQLLDMLKFYTGFEINDQTGNALTENEMTTIHYDRIT 335
Cdd:pfam16399 237 LLIDLESQLPTRRYVNTLLQDLHLLPACRLSPLYNDEE-GGLFRQLLDLLKHYTYFEIDDQTGEQLSDQEVYDAHYARLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 336 SLQRAAFAHFPE-LYDFALSNVAEVDARDSLVKFFGPLSSNTLHQVASYLCLLPTL-PKNEDTTFDKEFLLELLVSRHER 413
Cdd:pfam16399 316 RLQRTAFKHFKEkLTILALSNYGSIDKREELEKHLSALSDEELRELCSLLGLRTVPyPESDNIVYDRKFLLEVLLSRFEK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 414 RISQIQQLNQMPLYPTEKIIWDENIVPTEYYSGEGCLALPKLNLQFLTLHDYLLRNFNLFRLESTYEIRQDIEDSVSRMK 493
Cdd:pfam16399 396 RPSQQEAANELPLYPTEKTLWDENLVRTEYYDGSRPLALPKLNLQYLTLGDFLLRNFNLFRLESFYEIRQDIEDAVKRLK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 494 PWQSEYGGVVFGGWARMAQPIVAFTVVEVAKPNIGENWPTRVRADVTINL-NVRDHIKDEWEGLRKHDVCFLITVRPTKP 572
Cdd:pfam16399 476 PRLGEDGETRFGGWSRMALPISKPAIVEVAPPNVGESKPSRVRAEVTIDVsRLRDNIRREWESLRPHDVVFLLAVRPPDE 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 573 YGTKFDRRRPFIEQVGLVYVRGCEIQGMLDDKGRVIED------GPEPRPNlrgeSRTFRVFLDPNQYQQDMTNtIQNGA 646
Cdd:pfam16399 556 TYNKLTGSQSFAEQLGLVYVRGAEVIQVLDENGRVLREpqgqtnGPEPRPR----QRRLRVRLDANQYKADMDR-AAEGK 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 647 EDVYDTFNVIMRRKPKENNFKAVLETIRNLMNTDCVVPDWLHDIILGYGDPSSAHYSKMPNQIATLDFNDTFLSIEHLKA 726
Cdd:pfam16399 631 PDVYETFNVLVRRKPRENNFKAVLETIRDLMNSDCVVPDWLHDVFLGYGDPAAAHYKNLPNRLKTVDFRDTFLDWQHLIE 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 727 SFPGHNVKVTVSDPALQIPPFRITFPVR-----SGKGKKRKDADGEEDDTEEAKTLIVEPHVIPNRGPYPYNQPKRNTIQ 801
Cdd:pfam16399 711 SFPGKTIEPSDDVSGSFGPPYVLEFPDSppepaPAKPSKKRRRDQEPAPQAEPETIRVSTYKPPNRGPYPVDAPKLNSVR 790
|
.
gi 163644327 802 F 802
Cdd:pfam16399 791 F 791
|
|
| EEXXQc_AQR |
cd17935 |
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ... |
797-1156 |
8.41e-125 |
|
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: 386.78 E-value: 8.41e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 797 RNTIQFTHTQIEAIRAGMQPGLTMVVGPPGTGKTDVAVQIISNIYHNFPEQRTLIVTHSNQALNQLFEKIMALDIDERHL 876
Cdd:cd17935 1 QNTVKFTPTQIEAIRSGMQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPNQRTLIVTHSNQALNQLFEKIMALDIDERHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 877 LRLGHGeeeletekdfsrygrvnyvlarrielleevkrlqkslgvpgdasytcetagyfflyqvmsrweeymsrvknsgt 956
Cdd:cd17935 81 LRLGHG-------------------------------------------------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 957 acpdaapdaaqvatffpfheyfanapqpifkgrsyeedmeiaegcfrhikkiftqleefrasellrsgldrskyllvkeA 1036
Cdd:cd17935 87 -------------------------------------------------------------------------------A 87
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1037 KIIAMTCTHAALKRHDLVKLGFKYDNILMEEAAQILEIETFIPLLLQNPQDGFSRLKRWIMIGDHHQLPPVIKNMAFQKY 1116
Cdd:cd17935 88 KIIAMTCTHAALKRGELVELGFKYDNILMEEAAQILEIETFIPLLLQNPEDGPNRLKRLIMIGDHHQLPPVIKNMAFQKY 167
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 163644327 1117 SNMEQSLFTRFVRVGVPTVDLDAQGRARASLCNLYNWRYK 1156
Cdd:cd17935 168 SNMEQSLFTRLVRLGVPTVDLDAQGRARASISSLYNWRYK 207
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
1144-1327 |
3.32e-48 |
|
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: 170.11 E-value: 3.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1144 RASLCNLYNWRYKNLGNLPHVQLLP-EFSTANAGLLYDFQLINVEdfqGVGESEPNPYFYQNLGEAEYVVALFMYMCLLG 1222
Cdd:cd18808 2 HPEISEFPSKLFYEGKLKAGVSVAArLNPPPLPGPSKPLVFVDVS---GGEEREESGTSKSNEAEAELVVELVKYLLKSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1223 YPADKISILTTYNGQKHLIRDIINRRCGNNPLIgrpnKVTTVDRFQGQQNDYILLSLVRTR----AVGHLRDVRRLVVAM 1298
Cdd:cd18808 79 VKPSSIGVITPYRAQVALIRELLRKRGGLLEDV----EVGTVDNFQGREKDVIILSLVRSNesggSIGFLSDPRRLNVAL 154
|
170 180
....*....|....*....|....*....
gi 163644327 1299 SRARLGLYIFARVSLFQNCFELTPAFSQL 1327
Cdd:cd18808 155 TRAKRGLIIVGNPDTLSKDPLWKKLLEYL 183
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
1003-1327 |
1.12e-34 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 144.12 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1003 RHIKKIFTQLEEFRASELLRSGLDRSKY-----------LLVKEAKIIAMTCthAALKRHDLVKLGfKYDNILMEEAAQI 1071
Cdd:COG1112 491 EHPEELEKLIAELREAARLRRALRRELKkrrelrkllwdALLELAPVVGMTP--ASVARLLPLGEG-SFDLVIIDEASQA 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1072 LEIETFIPLllqnpqdgfSRLKRWIMIGDHHQLPPVIK--NMAFQKYSNMEQSLFTRFVRV-GVPTVDLDAQGRARASLC 1148
Cdd:COG1112 568 TLAEALGAL---------ARAKRVVLVGDPKQLPPVVFgeEAEEVAEEGLDESLLDRLLARlPERGVMLREHYRMHPEII 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1149 NLYNWR-YKNlgnlphvQLLPEFSTANAGLLYDFQLINVEDFQGVGESEPNPYFyqNLGEAEYVVALFMYMCLLGYPADK 1227
Cdd:COG1112 639 AFSNRLfYDG-------KLVPLPSPKARRLADPDSPLVFIDVDGVYERRGGSRT--NPEEAEAVVELVRELLEDGPDGES 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1228 ISILTTYNGQKHLIRDIINRRCGNNpliGRPNKVTTVDRFQGQQNDYILLSLVRTRAVGHLR-------DVRRLVVAMSR 1300
Cdd:COG1112 710 IGVITPYRAQVALIRELLREALGDG---LEPVFVGTVDRFQGDERDVIIFSLVYSNDEDVPRnfgflngGPRRLNVAVSR 786
|
330 340
....*....|....*....|....*..
gi 163644327 1301 ARLGLYIFARVSLFQNcFELTPAFSQL 1327
Cdd:COG1112 787 ARRKLIVVGSRELLDS-DPSTPALKRL 812
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1119-1307 |
2.85e-28 |
|
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: 113.41 E-value: 2.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1119 MEQSLFTRFVRVG-VPTVDLDAQGRARASLCNLYN-WRYKN-LGNLPHVQLLPEFSTANAGL-LYDFQLINVEDFQGVGE 1194
Cdd:pfam13087 1 LDRSLFERLQELGpSAVVMLDTQYRMHPEIMEFPSkLFYGGkLKDGPSVAERPLPDDFHLPDpLGPLVFIDVDGSEEEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1195 SEPNPYFyqNLGEAEYVVALFMYMCLLGYPADK-ISILTTYNGQKHLIRDIINRRCGNNPLIgrpnKVTTVDRFQGQQND 1273
Cdd:pfam13087 81 DGGTSYS--NEAEAELVVQLVEKLIKSGPEEPSdIGVITPYRAQVRLIRKLLKRKLGGKLEI----EVNTVDGFQGREKD 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 163644327 1274 YILLSLVRTRA---VGHLRDVRRLVVAMSRARLGLYI 1307
Cdd:pfam13087 155 VIIFSCVRSNEkggIGFLSDPRRLNVALTRAKRGLII 191
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
790-1316 |
1.72e-27 |
|
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: 119.92 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 790 YPYNQPKRNTIQFT-------HTQIEAIR-AGMQPGLTMVVGPPGTGKTDVAVQIISNIYHNFPeqRTLIVTHSNQALNQ 861
Cdd:TIGR00376 139 REAPSKASEIHDFQffdpnlnESQKEAVLfALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGL--RVLVTAPSNIAVDN 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 862 LFEKIMALDIderHLLRLGHGEEELETEKDFSrygrVNYVLARRIELlEEVKRLQKSLGvpgdasytcetagyfflyQVM 941
Cdd:TIGR00376 217 LLERLALCDQ---KIVRLGHPARLLKSNKQHS----LDYLIENHPKY-QIVADIREKID------------------ELI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 942 SRWEEYMSrvknsgtacpdaapdaaqvatffpfheyfaNAPQpIFKGRSYEEDMEIA--EGCFRHIKKIFTQ-----LEE 1014
Cdd:TIGR00376 271 EERNKKTK------------------------------PSPQ-KRRGLSDIKILRKAlkKREARGIESLKIAsmaewIET 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1015 FRASELLRSGLDRSKYLLVKEakIIAMTCTHAALKRHDLVKlGFKYDNILMEEAAQILEIETFIPLLlqnpqdgfsRLKR 1094
Cdd:TIGR00376 320 NKSIDRLLKLLPESEERIMNE--ILAESDATNSMAGSEILN-GQYFDVAVIDEASQAMEPSCLIPLL---------KARK 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1095 WIMIGDHHQLPPVIKNmafQKYSNMEQSLFTRFV-RVGVPTVDLDAQGRARASLC-----NLYNWRYK---NLGNLPHVQ 1165
Cdd:TIGR00376 388 LILAGDHKQLPPTILS---HDAEELSLTLFERLIkEYPERSRTLNVQYRMNQKIMefpsrEFYNGKLTaheSVANILLRD 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1166 LLPEFSTANAGLLYD---FQLINVEDFQGVGESEPNPYFYQNLGEAEYVVALFMYMCLLGYPADKISILTTYNGQKHLIR 1242
Cdd:TIGR00376 465 LPKVEATESEDDLETgipLLFIDTSGCELFELKEADSTSKYNPGEAELVSEIIQALVKMGVPANDIGVITPYDAQVDLLR 544
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 163644327 1243 DIINRRcgnNPLIgrpnKVTTVDRFQGQQNDYILLSLVRT---RAVGHLRDVRRLVVAMSRARLGLYIFARVSLFQN 1316
Cdd:TIGR00376 545 QLLEHR---HIDI----EVSSVDGFQGREKEVIIISFVRSnrkGEVGFLKDLRRLNVALTRARRKLIVIGDSRTLSN 614
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
805-1111 |
4.20e-23 |
|
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: 100.11 E-value: 4.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 805 TQIEAIRAGM-QPGLTMVVGPPGTGKTDVAVQIISNIY-----HNFPEQRTLIVTHSNQALNQLFEKIMALDID-ERHLL 877
Cdd:pfam13086 1 SQREAIRSALsSSHFTLIQGPPGTGKTTTIVELIRQLLsypatSAAAGPRILVCAPSNAAVDNILERLLRKGQKyGPKIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 878 RLGHGEEELETEKDFSRYGRVNYVLARRiELLEEVKRLQKSLgvpgdasytcetagyfflyqvmsrwEEYMSRVKNSgta 957
Cdd:pfam13086 81 RIGHPAAISEAVLPVSLDYLVESKLNNE-EDAQIVKDISKEL-------------------------EKLAKALRAF--- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 958 cpdaaPDAAQVATFFPFHEYFANapqpifKGRSYEEDMEIAEGCFRhikKIFTQLEEFRASELLRsgldrskyllvkEAK 1037
Cdd:pfam13086 132 -----EKEIIVEKLLKSRNKDKS------KLEQERRKLRSERKELR---KELRRREQSLEREILD------------EAQ 185
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 163644327 1038 IIAMTCTHAAlkRHDLVKLgFKYDNILMEEAAQILEIETFIPLLLqnpqdgfsRLKRWIMIGDHHQLPPVIKNM 1111
Cdd:pfam13086 186 IVCSTLSGAG--SRLLSSL-ANFDVVIIDEAAQALEPSTLIPLLR--------GPKKVVLVGDPKQLPPTVISK 248
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
806-866 |
1.18e-05 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 50.02 E-value: 1.18e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163644327 806 QIEAIRA-------GMQPGLtmVVGPPGTGKTDVAVQIISNIYHNfpeQRTLIVTHSNQALNQLFEKI 866
Cdd:COG1061 85 QQEALEAllaalerGGGRGL--VVAPTGTGKTVLALALAAELLRG---KRVLVLVPRRELLEQWAEEL 147
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
795-915 |
4.00e-05 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 46.33 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 795 PKRNTIQFTHTQIEAIRAGMQ-PGLTMVVGPPGTGKTDVAVQIISNIYHNFPEQRTLIVTHSNQALNQLFEKIMAL--DI 871
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSgLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLgpSL 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 163644327 872 DERHLLRLGhGEEELETEKDFSR---------YGRVNYVLARRIELLEEVKRL 915
Cdd:smart00487 82 GLKVVGLYG-GDSKREQLRKLESgktdilvttPGRLLDLLENDKLSLSNVDLV 133
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Aquarius_N |
pfam16399 |
Intron-binding protein aquarius N-terminus; This family represents the N-terminus of ... |
18-802 |
0e+00 |
|
Intron-binding protein aquarius N-terminus; This family represents the N-terminus of intron-binding protein aquarius, a splicing factor which links excision of introns from pre-mRNA with snoRP assembly.
Pssm-ID: 435319 Cd Length: 791 Bit Score: 1221.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 18 INAEFVTQLACKYWAPHIK-KKSPFDIKVIEEIYEKEIVKSRFAIRKIMLLEFSQYLENYLWMNYSpEVSSKAYLMSICC 96
Cdd:pfam16399 1 IQEDRIAQLARKHWLKSKKsKKVKVKPEVVKKIYWDELEKEGFSLRSLLLLEFLQYLENYLWPNYT-EDASNAHVLLIVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 97 MVNEKFRENVPAWETFKKKPDHFPFFFKCILKAALAETdgeFSLHEQTLLLLFLDHCFNSLEVDLIRSQVQQLISLPMWM 176
Cdd:pfam16399 80 MVNEKFREHLPAWELFSDRPDDFSSFFRRVLSLSLDRS---LSTAERTALLSFLIHAFQSLENELVRKECAPLVSISIWH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 177 GL-QPARLELELKKTPKLRKFWNLIKKNDEKMDPEAREQAYQERRFLSRLIQKFISVLKSIPLSEPVTMDKVHYCERFIE 255
Cdd:pfam16399 157 NLsSEGRREQELDKNPQLRKAWRAAQKRYDAADDATKARLRFERSWLYTLLLDFLDVLYDIPEDGEVDDDNVRYCERFLE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 256 LMIDLEALLPTRRWFNTILDDSHLLVHCYLSSLVHREEdGHLFSQLLDMLKFYTGFEINDQTGNALTENEMTTIHYDRIT 335
Cdd:pfam16399 237 LLIDLESQLPTRRYVNTLLQDLHLLPACRLSPLYNDEE-GGLFRQLLDLLKHYTYFEIDDQTGEQLSDQEVYDAHYARLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 336 SLQRAAFAHFPE-LYDFALSNVAEVDARDSLVKFFGPLSSNTLHQVASYLCLLPTL-PKNEDTTFDKEFLLELLVSRHER 413
Cdd:pfam16399 316 RLQRTAFKHFKEkLTILALSNYGSIDKREELEKHLSALSDEELRELCSLLGLRTVPyPESDNIVYDRKFLLEVLLSRFEK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 414 RISQIQQLNQMPLYPTEKIIWDENIVPTEYYSGEGCLALPKLNLQFLTLHDYLLRNFNLFRLESTYEIRQDIEDSVSRMK 493
Cdd:pfam16399 396 RPSQQEAANELPLYPTEKTLWDENLVRTEYYDGSRPLALPKLNLQYLTLGDFLLRNFNLFRLESFYEIRQDIEDAVKRLK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 494 PWQSEYGGVVFGGWARMAQPIVAFTVVEVAKPNIGENWPTRVRADVTINL-NVRDHIKDEWEGLRKHDVCFLITVRPTKP 572
Cdd:pfam16399 476 PRLGEDGETRFGGWSRMALPISKPAIVEVAPPNVGESKPSRVRAEVTIDVsRLRDNIRREWESLRPHDVVFLLAVRPPDE 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 573 YGTKFDRRRPFIEQVGLVYVRGCEIQGMLDDKGRVIED------GPEPRPNlrgeSRTFRVFLDPNQYQQDMTNtIQNGA 646
Cdd:pfam16399 556 TYNKLTGSQSFAEQLGLVYVRGAEVIQVLDENGRVLREpqgqtnGPEPRPR----QRRLRVRLDANQYKADMDR-AAEGK 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 647 EDVYDTFNVIMRRKPKENNFKAVLETIRNLMNTDCVVPDWLHDIILGYGDPSSAHYSKMPNQIATLDFNDTFLSIEHLKA 726
Cdd:pfam16399 631 PDVYETFNVLVRRKPRENNFKAVLETIRDLMNSDCVVPDWLHDVFLGYGDPAAAHYKNLPNRLKTVDFRDTFLDWQHLIE 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 727 SFPGHNVKVTVSDPALQIPPFRITFPVR-----SGKGKKRKDADGEEDDTEEAKTLIVEPHVIPNRGPYPYNQPKRNTIQ 801
Cdd:pfam16399 711 SFPGKTIEPSDDVSGSFGPPYVLEFPDSppepaPAKPSKKRRRDQEPAPQAEPETIRVSTYKPPNRGPYPVDAPKLNSVR 790
|
.
gi 163644327 802 F 802
Cdd:pfam16399 791 F 791
|
|
| EEXXQc_AQR |
cd17935 |
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ... |
797-1156 |
8.41e-125 |
|
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: 386.78 E-value: 8.41e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 797 RNTIQFTHTQIEAIRAGMQPGLTMVVGPPGTGKTDVAVQIISNIYHNFPEQRTLIVTHSNQALNQLFEKIMALDIDERHL 876
Cdd:cd17935 1 QNTVKFTPTQIEAIRSGMQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPNQRTLIVTHSNQALNQLFEKIMALDIDERHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 877 LRLGHGeeeletekdfsrygrvnyvlarrielleevkrlqkslgvpgdasytcetagyfflyqvmsrweeymsrvknsgt 956
Cdd:cd17935 81 LRLGHG-------------------------------------------------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 957 acpdaapdaaqvatffpfheyfanapqpifkgrsyeedmeiaegcfrhikkiftqleefrasellrsgldrskyllvkeA 1036
Cdd:cd17935 87 -------------------------------------------------------------------------------A 87
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1037 KIIAMTCTHAALKRHDLVKLGFKYDNILMEEAAQILEIETFIPLLLQNPQDGFSRLKRWIMIGDHHQLPPVIKNMAFQKY 1116
Cdd:cd17935 88 KIIAMTCTHAALKRGELVELGFKYDNILMEEAAQILEIETFIPLLLQNPEDGPNRLKRLIMIGDHHQLPPVIKNMAFQKY 167
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 163644327 1117 SNMEQSLFTRFVRVGVPTVDLDAQGRARASLCNLYNWRYK 1156
Cdd:cd17935 168 SNMEQSLFTRLVRLGVPTVDLDAQGRARASISSLYNWRYK 207
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
1144-1327 |
3.32e-48 |
|
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: 170.11 E-value: 3.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1144 RASLCNLYNWRYKNLGNLPHVQLLP-EFSTANAGLLYDFQLINVEdfqGVGESEPNPYFYQNLGEAEYVVALFMYMCLLG 1222
Cdd:cd18808 2 HPEISEFPSKLFYEGKLKAGVSVAArLNPPPLPGPSKPLVFVDVS---GGEEREESGTSKSNEAEAELVVELVKYLLKSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1223 YPADKISILTTYNGQKHLIRDIINRRCGNNPLIgrpnKVTTVDRFQGQQNDYILLSLVRTR----AVGHLRDVRRLVVAM 1298
Cdd:cd18808 79 VKPSSIGVITPYRAQVALIRELLRKRGGLLEDV----EVGTVDNFQGREKDVIILSLVRSNesggSIGFLSDPRRLNVAL 154
|
170 180
....*....|....*....|....*....
gi 163644327 1299 SRARLGLYIFARVSLFQNCFELTPAFSQL 1327
Cdd:cd18808 155 TRAKRGLIIVGNPDTLSKDPLWKKLLEYL 183
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
1003-1327 |
1.12e-34 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 144.12 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1003 RHIKKIFTQLEEFRASELLRSGLDRSKY-----------LLVKEAKIIAMTCthAALKRHDLVKLGfKYDNILMEEAAQI 1071
Cdd:COG1112 491 EHPEELEKLIAELREAARLRRALRRELKkrrelrkllwdALLELAPVVGMTP--ASVARLLPLGEG-SFDLVIIDEASQA 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1072 LEIETFIPLllqnpqdgfSRLKRWIMIGDHHQLPPVIK--NMAFQKYSNMEQSLFTRFVRV-GVPTVDLDAQGRARASLC 1148
Cdd:COG1112 568 TLAEALGAL---------ARAKRVVLVGDPKQLPPVVFgeEAEEVAEEGLDESLLDRLLARlPERGVMLREHYRMHPEII 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1149 NLYNWR-YKNlgnlphvQLLPEFSTANAGLLYDFQLINVEDFQGVGESEPNPYFyqNLGEAEYVVALFMYMCLLGYPADK 1227
Cdd:COG1112 639 AFSNRLfYDG-------KLVPLPSPKARRLADPDSPLVFIDVDGVYERRGGSRT--NPEEAEAVVELVRELLEDGPDGES 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1228 ISILTTYNGQKHLIRDIINRRCGNNpliGRPNKVTTVDRFQGQQNDYILLSLVRTRAVGHLR-------DVRRLVVAMSR 1300
Cdd:COG1112 710 IGVITPYRAQVALIRELLREALGDG---LEPVFVGTVDRFQGDERDVIIFSLVYSNDEDVPRnfgflngGPRRLNVAVSR 786
|
330 340
....*....|....*....|....*..
gi 163644327 1301 ARLGLYIFARVSLFQNcFELTPAFSQL 1327
Cdd:COG1112 787 ARRKLIVVGSRELLDS-DPSTPALKRL 812
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1119-1307 |
2.85e-28 |
|
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: 113.41 E-value: 2.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1119 MEQSLFTRFVRVG-VPTVDLDAQGRARASLCNLYN-WRYKN-LGNLPHVQLLPEFSTANAGL-LYDFQLINVEDFQGVGE 1194
Cdd:pfam13087 1 LDRSLFERLQELGpSAVVMLDTQYRMHPEIMEFPSkLFYGGkLKDGPSVAERPLPDDFHLPDpLGPLVFIDVDGSEEEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1195 SEPNPYFyqNLGEAEYVVALFMYMCLLGYPADK-ISILTTYNGQKHLIRDIINRRCGNNPLIgrpnKVTTVDRFQGQQND 1273
Cdd:pfam13087 81 DGGTSYS--NEAEAELVVQLVEKLIKSGPEEPSdIGVITPYRAQVRLIRKLLKRKLGGKLEI----EVNTVDGFQGREKD 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 163644327 1274 YILLSLVRTRA---VGHLRDVRRLVVAMSRARLGLYI 1307
Cdd:pfam13087 155 VIIFSCVRSNEkggIGFLSDPRRLNVALTRAKRGLII 191
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
790-1316 |
1.72e-27 |
|
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: 119.92 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 790 YPYNQPKRNTIQFT-------HTQIEAIR-AGMQPGLTMVVGPPGTGKTDVAVQIISNIYHNFPeqRTLIVTHSNQALNQ 861
Cdd:TIGR00376 139 REAPSKASEIHDFQffdpnlnESQKEAVLfALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGL--RVLVTAPSNIAVDN 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 862 LFEKIMALDIderHLLRLGHGEEELETEKDFSrygrVNYVLARRIELlEEVKRLQKSLGvpgdasytcetagyfflyQVM 941
Cdd:TIGR00376 217 LLERLALCDQ---KIVRLGHPARLLKSNKQHS----LDYLIENHPKY-QIVADIREKID------------------ELI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 942 SRWEEYMSrvknsgtacpdaapdaaqvatffpfheyfaNAPQpIFKGRSYEEDMEIA--EGCFRHIKKIFTQ-----LEE 1014
Cdd:TIGR00376 271 EERNKKTK------------------------------PSPQ-KRRGLSDIKILRKAlkKREARGIESLKIAsmaewIET 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1015 FRASELLRSGLDRSKYLLVKEakIIAMTCTHAALKRHDLVKlGFKYDNILMEEAAQILEIETFIPLLlqnpqdgfsRLKR 1094
Cdd:TIGR00376 320 NKSIDRLLKLLPESEERIMNE--ILAESDATNSMAGSEILN-GQYFDVAVIDEASQAMEPSCLIPLL---------KARK 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1095 WIMIGDHHQLPPVIKNmafQKYSNMEQSLFTRFV-RVGVPTVDLDAQGRARASLC-----NLYNWRYK---NLGNLPHVQ 1165
Cdd:TIGR00376 388 LILAGDHKQLPPTILS---HDAEELSLTLFERLIkEYPERSRTLNVQYRMNQKIMefpsrEFYNGKLTaheSVANILLRD 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1166 LLPEFSTANAGLLYD---FQLINVEDFQGVGESEPNPYFYQNLGEAEYVVALFMYMCLLGYPADKISILTTYNGQKHLIR 1242
Cdd:TIGR00376 465 LPKVEATESEDDLETgipLLFIDTSGCELFELKEADSTSKYNPGEAELVSEIIQALVKMGVPANDIGVITPYDAQVDLLR 544
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 163644327 1243 DIINRRcgnNPLIgrpnKVTTVDRFQGQQNDYILLSLVRT---RAVGHLRDVRRLVVAMSRARLGLYIFARVSLFQN 1316
Cdd:TIGR00376 545 QLLEHR---HIDI----EVSSVDGFQGREKEVIIISFVRSnrkGEVGFLKDLRRLNVALTRARRKLIVIGDSRTLSN 614
|
|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
1038-1141 |
4.43e-24 |
|
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: 98.71 E-value: 4.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1038 IIAMTCTHAALKRhdlvklgfkYDNILMEEAAQILEIETFIPlllqnpQDGFSRLKRWIMIGDHHQLPPVIKNMAFQKYS 1117
Cdd:cd17914 34 ILLVTPTNKAAAQ---------LDNILVDEAAQILEPETSRL------IDLALDQGRVILVGDHDQLGPVWRGAVLAKIC 98
|
90 100
....*....|....*....|....
gi 163644327 1118 NmEQSLFTRFVRVGVPTVDLDAQG 1141
Cdd:cd17914 99 N-EQSLFTRLVRLGVSLIRLQVQY 121
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
805-1111 |
4.20e-23 |
|
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: 100.11 E-value: 4.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 805 TQIEAIRAGM-QPGLTMVVGPPGTGKTDVAVQIISNIY-----HNFPEQRTLIVTHSNQALNQLFEKIMALDID-ERHLL 877
Cdd:pfam13086 1 SQREAIRSALsSSHFTLIQGPPGTGKTTTIVELIRQLLsypatSAAAGPRILVCAPSNAAVDNILERLLRKGQKyGPKIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 878 RLGHGEEELETEKDFSRYGRVNYVLARRiELLEEVKRLQKSLgvpgdasytcetagyfflyqvmsrwEEYMSRVKNSgta 957
Cdd:pfam13086 81 RIGHPAAISEAVLPVSLDYLVESKLNNE-EDAQIVKDISKEL-------------------------EKLAKALRAF--- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 958 cpdaaPDAAQVATFFPFHEYFANapqpifKGRSYEEDMEIAEGCFRhikKIFTQLEEFRASELLRsgldrskyllvkEAK 1037
Cdd:pfam13086 132 -----EKEIIVEKLLKSRNKDKS------KLEQERRKLRSERKELR---KELRRREQSLEREILD------------EAQ 185
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 163644327 1038 IIAMTCTHAAlkRHDLVKLgFKYDNILMEEAAQILEIETFIPLLLqnpqdgfsRLKRWIMIGDHHQLPPVIKNM 1111
Cdd:pfam13086 186 IVCSTLSGAG--SRLLSSL-ANFDVVIIDEAAQALEPSTLIPLLR--------GPKKVVLVGDPKQLPPTVISK 248
|
|
| DEXXQc_SETX |
cd18042 |
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ... |
999-1142 |
1.55e-19 |
|
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: 88.81 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 999 EGCFRHIKKIFTQLE-EFRASELLRSGLDRSKYLLVKEAKIIAmtCTHAALKRHDLVKLGFKYDNILMEEAAQILEIETF 1077
Cdd:cd18042 85 EIVLRLLSEGFLDGDgRSYKPNVVRVGRQELRASILNEADIVC--TTLSSSGSDLLESLPRGFDTVIIDEAAQAVELSTL 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 163644327 1078 IPLLLqnpqdgfsRLKRWIMIGDHHQLPPVIKNMAFQKYsNMEQSLFTRFVRVGVPTVDLDAQGR 1142
Cdd:cd18042 163 IPLRL--------GCKRLILVGDPKQLPATVFSKVAQKL-GYDRSLFERLQLAGYPVLMLTTQYR 218
|
|
| DEXXQc_UPF1 |
cd18039 |
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ... |
804-1142 |
1.46e-18 |
|
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: 86.53 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 804 HTQIEAIRAGMQPGLTMVVGPPGTGKTDVAVQIISNIYHNFPEQrTLIVTHSNQALNQLFEKImaldiDERHLlrlghge 883
Cdd:cd18039 4 HSQVDAVKTALQRPLSLIQGPPGTGKTVTSATIVYHLVKQGNGP-VLVCAPSNVAVDQLTEKI-----HQTGL------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 884 eeletekdfsrygRVNYVLARRIElleevkrlqkslGVPGDASYTCetagyfFLYQVmsrwEEYMsrvknsgtacpdaap 963
Cdd:cd18039 71 -------------KVVRLCAKSRE------------AVESPVSFLA------LHNQV----RNLD--------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 964 daaqvatffpFHEYFANAPQPIFKGRSYEEDMEiaegcfRHIKKIFTQLEefraSELLRsgldrskyllvkEAKIIAMTC 1043
Cdd:cd18039 101 ----------SAEKLELLKLLKLETGELSSADE------KRYRKLKRKAE----RELLR------------NADVICCTC 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1044 THAALKRhdLVKlgFKYDNILMEEAAQILEIETFIPLLLQnpqdgfsrLKRWIMIGDHHQLPPVIKNMAFQKYSnMEQSL 1123
Cdd:cd18039 149 VGAGDPR--LSK--MKFRTVLIDEATQATEPECLIPLVHG--------AKQVILVGDHCQLGPVVMCKKAAKAG-LSQSL 215
|
330
....*....|....*....
gi 163644327 1124 FTRFVRVGVPTVDLDAQGR 1142
Cdd:cd18039 216 FERLVQLGIRPIRLQVQYR 234
|
|
| DEXXQc_Helz-like |
cd18038 |
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ... |
806-1154 |
1.15e-15 |
|
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: 78.04 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 806 QIEAIRA----GMQPGLTMVVGPPGTGKTDVAVQIISNIYHNFPEQRTLIVTHSNQALNQLfekimaldiderhllrlgh 881
Cdd:cd18038 6 QKLAVRNivtgTSRPPPYIIFGPPGTGKTVTLVEAILQVLRQPPEARILVCAPSNSAADLL------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 882 geeeletekdfsrygrvnyvlarrielleeVKRLQKSLGVPGDasytcetagyffLYQVMSRWEEYMSrvknsgtacpda 961
Cdd:cd18038 67 ------------------------------AERLLNALVTKRE------------ILRLNAPSRDRAS------------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 962 apdaaqvatffpfheyfanAPQPIFKGRSYeedmeIAEGCFRHIkkiftQLEEfrasellrsgldrskyllVKEAKIIAM 1041
Cdd:cd18038 93 -------------------VPPELLPYCNS-----KAEGTFRLP-----SLEE------------------LKKYRIVVC 125
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1042 TCTHAALkrhdLVKLGFK---YDNILMEEAAQILEIETFIPLLLQNPQDGfsrlkRWIMIGDHHQLPPVIKNMAFQKYsN 1118
Cdd:cd18038 126 TLMTAGR----LVQAGVPnghFTHIFIDEAGQATEPEALIPLSELASKNT-----QIVLAGDPKQLGPVVRSPLARKY-G 195
|
330 340 350
....*....|....*....|....*....|....*.
gi 163644327 1119 MEQSLFTRFVRVGVPTVDLDAQGRARASLCNlyNWR 1154
Cdd:cd18038 196 LGKSLLERLMERPLYYKDGEYNPSYITKLLK--NYR 229
|
|
| EEXXEc_NFX1 |
cd17936 |
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ... |
804-1140 |
6.26e-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: 74.50 E-value: 6.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 804 HTQIEAIRAGMQPGLTMVVGPPGTGKTDVAVQIISNIYHNFPEQRT---LIVTHSNQALNQLFEKImaLDIDERHLLRLG 880
Cdd:cd17936 4 PSQLEALKHALTSELALIQGPPGTGKTFLGVKLVRALLQNQDLSITgpiLVVCYTNHALDQFLEGL--LDFGPTKIVRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 881 hgeeeletekdfsrygrvnyvlarrielleevkrlqkslgvpgdasytcetagyfflyqvmsrweeymsrvknsgtacpd 960
Cdd:cd17936 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 961 aapdaaqvatffpfheyfanapqpifkgrsyeedmeiaegcfrhikkiftqleefrasellrsgldrskyllvkeAKIIA 1040
Cdd:cd17936 82 ---------------------------------------------------------------------------ARVIG 86
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1041 MTCTHAALKRHDLVKLGFKYdnILMEEAAQILE--IETFIPlllqnpqdgfSRLKRWIMIGDHHQLPPVIKNMAFQ--KY 1116
Cdd:cd17936 87 MTTTGAAKYRELLQALGPKV--VIVEEAAEVLEahILAALT----------PSTEHLILIGDHKQLRPKVNVYELTakKY 154
|
330 340
....*....|....*....|....
gi 163644327 1117 sNMEQSLFTRFVRVGVPTVDLDAQ 1140
Cdd:cd17936 155 -NLDVSLFERLVKNGLPFVTLNVQ 177
|
|
| DEXXQc_Upf1-like |
cd17934 |
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ... |
1036-1142 |
1.39e-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: 63.02 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1036 AKIIAMTCTHAALKRHDLVklgfkydniLMEEAAQILEIETFIPLLlqnpqdgfsRLKRWIMIGDHHQLPPVIKNMAFQK 1115
Cdd:cd17934 30 KRVLVTAQSNVAVDNVDVV---------IIDEASQITEPELLIALI---------RAKKVVLVGDPKQLPPVVQEDHAAL 91
|
90 100 110
....*....|....*....|....*....|
gi 163644327 1116 Y---SNMEQSLFTRFVRVGVPTVDLDAQGR 1142
Cdd:cd17934 92 LglsFILSLLLLFRLLLPGSPKVMLDTQYR 121
|
|
| DEXXQc_DNA2 |
cd18041 |
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ... |
1005-1127 |
1.23e-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: 62.64 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1005 IKKIFTQLEEFRASELLRSGLDRSKY-LLVKEAKIIAMTC---THAALKRHdlvklgfKYDNILMEEAAQILEIETFIPL 1080
Cdd:cd18041 78 LKKIHPDVQEFTLEAILKSCKSVEELeSKYESVSVVATTClgiNHPIFRRR-------TFDYCIVDEASQITLPICLGPL 150
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 163644327 1081 LLQnpqdgfsrlKRWIMIGDHHQLPPVIKNMAFQKySNMEQSLFTRF 1127
Cdd:cd18041 151 RLA---------KKFVLVGDHYQLPPLVKSREARE-LGMDESLFKRL 187
|
|
| DEXXc_HELZ2-C |
cd18040 |
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
806-1127 |
2.82e-10 |
|
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: 62.93 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 806 QIEAIRAGMQPGLTMVVGPPGTGKTDVAVQIIsniYHnFPEQrtlivthsNQALNQLFEKIMALDiderHLLRLGHGEEE 885
Cdd:cd18040 6 QNHAVRTALTKPFTLIQGPPGTGKTVTGVHIA---YW-FAKQ--------NREIQSVSGEGDGGP----CVLYCGPSNKS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 886 LEtekdfsrygrvnyVLArriELLEEVKRLqKSLGVpgdasytcetagyfflYQVMSRWEEY-MSRVKNSGTACPDAAPD 964
Cdd:cd18040 70 VD-------------VVA---ELLLKVPGL-KILRV----------------YSEQIETTEYpIPNEPRHPNKKSERESK 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 965 AAQVATFFPFHEYFANAPQPifkgrsyeedmeiaegcfrHIKKIFTQLEEF-RASELLRSG-LDRSKYLLVKEAK----- 1037
Cdd:cd18040 117 PNSELSSITLHHRIRQPSNP-------------------HSQQIKAFEARFeRTQEKITEEdIKTYKILIWEARFeelet 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1038 --IIAMTCTHAALKrhdlvKLGFKYD--NILMEEAAQILEIETFIPLLlqnpqdGFSRLKRWIMIGDHHQLPPVIKNMAF 1113
Cdd:cd18040 178 vdVILCTCSEAASQ-----KMRTHANvkQCIVDECGMCTEPESLIPIV------SAPRAEQVVLIGDHKQLRPVVQNKEA 246
|
330
....*....|....
gi 163644327 1114 QKYSnMEQSLFTRF 1127
Cdd:cd18040 247 QKLG-LGRSLFERY 259
|
|
| DEXXQc_SMUBP2 |
cd18044 |
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ... |
1020-1135 |
3.42e-10 |
|
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: 61.09 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1020 LLRSGLDRSKYLLVkEAKIIAMTCTHAAlkrHDLVKLGFKYDNILMEEAAQILEIETFIPLLlqnpqdgfsRLKRWIMIG 1099
Cdd:cd18044 81 LLESVLDHSLDALV-AAQVVLATNTGAG---SRQLLPNELFDVVVIDEAAQALEASCWIPLL---------KARRCILAG 147
|
90 100 110
....*....|....*....|....*....|....*.
gi 163644327 1100 DHHQLPPVIKNMAFQKYsNMEQSLFTRFVRVGVPTV 1135
Cdd:cd18044 148 DHKQLPPTILSDKAARG-GLGVTLFERLVNLYGESV 182
|
|
| SF1_C |
cd18786 |
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ... |
1227-1307 |
1.55e-09 |
|
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: 56.29 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1227 KISILTTYNGQKHLIRDIInRRCGNNPLIGRPNKVTTVDRFQGQQNDYILLSLVRTravgHLRDVRRLVVAMSRARLGLY 1306
Cdd:cd18786 12 KGVVLTPYHRDRAYLNQYL-QGLSLDEFDLQLVGAITIDSSQGLTFDVVTLYLPTA----NSLTPRRLYVALTRARKRLV 86
|
.
gi 163644327 1307 I 1307
Cdd:cd18786 87 I 87
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
806-895 |
3.17e-06 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 48.46 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 806 QIEAIRAGMQ-----PGltMVVGPPGTGKTDVAVQIISNIYhnfpEQRTLIVTHSNQALNQLFEKIMALDIDeRHLLRLG 880
Cdd:cd17926 5 QEEALEAWLAhknnrRG--ILVLPTGSGKTLTALALIAYLK----ELRTLIVVPTDALLDQWKERFEDFLGD-SSIGLIG 77
|
90
....*....|....*..
gi 163644327 881 HGEEELETEK--DFSRY 895
Cdd:cd17926 78 GGKKKDFDDAnvVVATY 94
|
|
| DEXXQc_SF1 |
cd18043 |
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ... |
805-883 |
8.69e-06 |
|
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: 46.42 E-value: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 805 TQIEAIRAGMQPGLTMVVGPPGTGKTDVAVQIISNIYHNfpEQRTLIVTHSNQALNQLFEKIMALDIDE-RHLLRLGHGE 883
Cdd:cd18043 3 SQEAAIISARNGKNVVIQGPPGTGKSQTIANIIANALAR--GKRVLFVSEKKAALDVVRFPCWIMSPLSvSQYLPLNRNL 80
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
806-866 |
1.18e-05 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 50.02 E-value: 1.18e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163644327 806 QIEAIRA-------GMQPGLtmVVGPPGTGKTDVAVQIISNIYHNfpeQRTLIVTHSNQALNQLFEKI 866
Cdd:COG1061 85 QQEALEAllaalerGGGRGL--VVAPTGTGKTVLALALAAELLRG---KRVLVLVPRRELLEQWAEEL 147
|
|
| DEXXQc_Upf1-like |
cd17934 |
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ... |
818-862 |
1.20e-05 |
|
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: 46.07 E-value: 1.20e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 163644327 818 LTMVVGPPGTGKTDVAVQIISNIYHNFPEQRTLIVTHSNQALNQL 862
Cdd:cd17934 1 ISLIQGPPGTGKTTTIAAIVLQLLKGLRGKRVLVTAQSNVAVDNV 45
|
|
| DEXXQc_HELZ |
cd18077 |
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ... |
1033-1126 |
2.32e-05 |
|
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: 47.48 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1033 VKEAKIIAMT-CTHAALKRHDLVKLGFKYdnILMEEAAQILEIETFIPLLLQNpqdgfsRLKRWIMIGDHHQLPPVIKNm 1111
Cdd:cd18077 121 VMRHRVVVVTlSTSQYLCQLDLEPGFFTH--ILLDEAAQAMECEAIMPLALAT------KSTRIVLAGDHMQLSPEVYS- 191
|
90
....*....|....*
gi 163644327 1112 AFQKYSNMEQSLFTR 1126
Cdd:cd18077 192 EFARERNLHISLLER 206
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
795-915 |
4.00e-05 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 46.33 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 795 PKRNTIQFTHTQIEAIRAGMQ-PGLTMVVGPPGTGKTDVAVQIISNIYHNFPEQRTLIVTHSNQALNQLFEKIMAL--DI 871
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSgLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLgpSL 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 163644327 872 DERHLLRLGhGEEELETEKDFSR---------YGRVNYVLARRIELLEEVKRL 915
Cdd:smart00487 82 GLKVVGLYG-GDSKREQLRKLESgktdilvttPGRLLDLLENDKLSLSNVDLV 133
|
|
| DEXXQc_Mov10L1 |
cd18078 |
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ... |
823-865 |
3.00e-04 |
|
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: 43.90 E-value: 3.00e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 163644327 823 GPPGTGKTDVAVQIISNIYHNFPEQRTLIVTHSNQALNQLFEK 865
Cdd:cd18078 27 GPPGTGKTVTIIEAILQVVYNLPRSRILVCAPSNSAADLVTSR 69
|
|
| DEXXQc_HELZ2-N |
cd18076 |
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
1044-1126 |
5.30e-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: 43.34 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644327 1044 THAALKRHDLVKLGFkYDNILMEEAAQILEIETFIPLLLQNPQdgfsrlKRWIMIGDHHQLPPviKNMAFQKYSNMEQSL 1123
Cdd:cd18076 132 TTTAMAFNLHVLSGF-FTHIFIDEAAQMLECEALIPLSYAGPK------TRVVLAGDHMQMTP--KLFSVADYNRANHTL 202
|
...
gi 163644327 1124 FTR 1126
Cdd:cd18076 203 LNR 205
|
|
| UvrD_C_2 |
pfam13538 |
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety ... |
1261-1307 |
1.47e-03 |
|
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety of helicase enzymes. This domain has a AAA-like structural fold.
Pssm-ID: 463913 [Multi-domain] Cd Length: 52 Bit Score: 37.94 E-value: 1.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 163644327 1261 VTTVDRFQGQQNDYILLSLVRTRAVGHLRDVRRLV-VAMSRARLGLYI 1307
Cdd:pfam13538 4 ALTVHKAQGSEFPAVFLVDPDLTAHYHSMLRRRLLyTAVTRARKKLVL 51
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
806-869 |
1.60e-03 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350790 [Multi-domain] Cd Length: 163 Bit Score: 41.01 E-value: 1.60e-03
10 20 30 40 50 60
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gi 163644327 806 QIEAIRA---GMQPGLT--MVVGPPGTGKTDVAVQIISNIYHNFPEQRTLIVTHSNQALNQLFEKIMAL 869
Cdd:cd18032 5 QQEAIEAleeAREKGQRraLLVMATGTGKTYTAAFLIKRLLEANRKKRILFLAHREELLEQAERSFKEV 73
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| DEXXQc_HELZ |
cd18077 |
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ... |
820-858 |
9.88e-03 |
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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: 39.39 E-value: 9.88e-03
10 20 30
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gi 163644327 820 MVVGPPGTGKTDVAVQIISNIYHNfPEQRTLIVTHSNQA 858
Cdd:cd18077 25 LLIGPFGTGKTFTLAQAVKHILQQ-PETRILICTHSNSA 62
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