|
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: 1227.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 18 INAEFVTQLACKYWAPHIK-KKSPFDIKVIEDIYEKEIVKSRFAIRKIMLLEFSQYLENYLWMNYSpEVSSKAYLMSICC 96
Cdd:pfam16399 1 IQEDRIAQLARKHWLKSKKsKKVKVKPEVVKKIYWDELEKEGFSLRSLLLLEFLQYLENYLWPNYT-EDASNAHVLLIVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 97 MVNEKFRENVPAWEIFKKKPDHFPFFFKHILKAALAETdgeFSLHEQTVLLLFLDHCFNSLEVDLIRSQVQQLISLPMWM 176
Cdd:pfam16399 80 MVNEKFREHLPAWELFSDRPDDFSSFFRRVLSLSLDRS---LSTAERTALLSFLIHAFQSLENELVRKECAPLVSISIWH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 177 GLQL-ARLELELKKTPKLRKFWNLIKKNDEKMDPEAREQAYQERRFLSQLIQKFISVLKSVPLSEPVTMDKVHYCERFIE 255
Cdd:pfam16399 157 NLSSeGRREQELDKNPQLRKAWRAAQKRYDAADDATKARLRFERSWLYTLLLDFLDVLYDIPEDGEVDDDNVRYCERFLE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 256 LMIDLEALLPTRRWFNTILDDSHLLVHCYLSNLVRREEdGHLFSQLLDMLKFYTGFEINDQTGNALTENEMTTIHYDRIT 335
Cdd:pfam16399 237 LLIDLESQLPTRRYVNTLLQDLHLLPACRLSPLYNDEE-GGLFRQLLDLLKHYTYFEIDDQTGEQLSDQEVYDAHYARLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 336 SLQRAAFAHFPE-LYDFALSNVAEVDTRESLVKFFGPLSSNTLHQVASYLCLLPTL-PKNEDTTFDKEFLLELLVSRHER 413
Cdd:pfam16399 316 RLQRTAFKHFKEkLTILALSNYGSIDKREELEKHLSALSDEELRELCSLLGLRTVPyPESDNIVYDRKFLLEVLLSRFEK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 414 RISQIQQLNQMPLYPTEKIIWDENIVPTEYYSGEGCLALPKLNLQFLTLHDYLLRNFNLFRLESTYEIRQDIEDSVSRMK 493
Cdd:pfam16399 396 RPSQQEAANELPLYPTEKTLWDENLVRTEYYDGSRPLALPKLNLQYLTLGDFLLRNFNLFRLESFYEIRQDIEDAVKRLK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 494 PWQSEYGGVVFGGWARMAQPIVAFTVVEVAKPNIGENWPTRVRADVTINL-NVRDHIKDEWEGLRKHDVCFLITVRPTKP 572
Cdd:pfam16399 476 PRLGEDGETRFGGWSRMALPISKPAIVEVAPPNVGESKPSRVRAEVTIDVsRLRDNIRREWESLRPHDVVFLLAVRPPDE 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 573 YGTKFDRRRPFIEQVGLVYVRGCEIQGMLDDKGRVIED------GPEPRPNlrgeSRTFRVFLDPNQYQQDMTNtIQNGA 646
Cdd:pfam16399 556 TYNKLTGSQSFAEQLGLVYVRGAEVIQVLDENGRVLREpqgqtnGPEPRPR----QRRLRVRLDANQYKADMDR-AAEGK 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 647 EDVYETFNIIMRRKPKENNFKAVLETIRNLMNTDCVVPDWLHDIILGYGDPSSAHYSKMPNQIATLDFNDTFLSIEHLKA 726
Cdd:pfam16399 631 PDVYETFNVLVRRKPRENNFKAVLETIRDLMNSDCVVPDWLHDVFLGYGDPAAAHYKNLPNRLKTVDFRDTFLDWQHLIE 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 727 SFPGHNVKVTVEDPALQIPPFRITFPVR-----SGKGKKRKDADVEDEDTEEAKTLIVEPHVIPNRGPYPYNQPKRNTIQ 801
Cdd:pfam16399 711 SFPGKTIEPSDDVSGSFGPPYVLEFPDSppepaPAKPSKKRRRDQEPAPQAEPETIRVSTYKPPNRGPYPVDAPKLNSVR 790
|
.
gi 38788372 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 ... |
797-1152 |
5.60e-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: 387.17 E-value: 5.60e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 797 RNTIQFTHTQIEAIRAGMQPGLTMVVGPPGTGKTDVAVQIISNIYHNFPEQRTLIVTHSNQALNQLFEKIMALDIDERHL 876
Cdd:cd17935 1 QNTVKFTPTQIEAIRSGMQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPNQRTLIVTHSNQALNQLFEKIMALDIDERHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 877 LRLGHGeeeletekdfsrygrvnyvlarrielleevkrlqkslgvpgdasytcetagyfflyqvmsrweeyiskvknkgs 956
Cdd:cd17935 81 LRLGHG-------------------------------------------------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 957 tlpdvtevstffpfheyfanapqpifkgrsyeedmeiaegcfrhikkiftqleefrasellrsgldrskyllvkeAKIIA 1036
Cdd:cd17935 87 ---------------------------------------------------------------------------AKIIA 91
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1037 MTCTHAALKRHDLVKLGFKYDNILMEEAAQILEIETFIPLLLQNPQDGFSRLKRWIMIGDHHQLPPVIKNMAFQKYSNME 1116
Cdd:cd17935 92 MTCTHAALKRGELVELGFKYDNILMEEAAQILEIETFIPLLLQNPEDGPNRLKRLIMIGDHHQLPPVIKNMAFQKYSNME 171
|
330 340 350
....*....|....*....|....*....|....*.
gi 38788372 1117 QSLFTRFVRVGVPTVDLDAQGRARASLCNLYNWRYK 1152
Cdd:cd17935 172 QSLFTRLVRLGVPTVDLDAQGRARASISSLYNWRYK 207
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
1140-1323 |
3.73e-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: 3.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1140 RASLCNLYNWRYKNLGNLPHVQLLP-EFSTANAGLLYDFQLINVEdfqGVGESEPNPYFYQNLGEAEYVVALFMYMCLLG 1218
Cdd:cd18808 2 HPEISEFPSKLFYEGKLKAGVSVAArLNPPPLPGPSKPLVFVDVS---GGEEREESGTSKSNEAEAELVVELVKYLLKSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1219 YPADKISILTTYNGQKHLIRDIINRRCGNNPLIgrpnKVTTVDRFQGQQNDYILLSLVRTR----AVGHLRDVRRLVVAM 1294
Cdd:cd18808 79 VKPSSIGVITPYRAQVALIRELLRKRGGLLEDV----EVGTVDNFQGREKDVIILSLVRSNesggSIGFLSDPRRLNVAL 154
|
170 180
....*....|....*....|....*....
gi 38788372 1295 SRARLGLYIFARVSLFQNCFELTPAFSQL 1323
Cdd:cd18808 155 TRAKRGLIIVGNPDTLSKDPLWKKLLEYL 183
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
845-1323 |
4.41e-35 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 145.27 E-value: 4.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 845 PEQRTLIVTHSNQALNQLFEKIMALDIDERHLLRLGHGEEELETEKDFSRYGRVNYVLARRIELLEEVKRLQKSLGVPGD 924
Cdd:COG1112 355 ALLRLLAALLLALALLLLLALEELLLLALLRLLAEGLALLLLLLLAALLRLARALLLLALLLAAAAAALAALLLLALALL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 925 ASYTCETAGYFFLYQVMSRWEEYISKVKNKGSTLPDVTEVSTFFPFHEYFANAPQPIFKGRSYEEDMEIAEGCfRHIKKI 1004
Cdd:COG1112 435 AALLALLLLLAAALAALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPEELEKLIAELREAA-RLRRAL 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1005 FTQLEEFRASELLRSgldrskYLLVKEAKIIAMTCthAALKRHDLVKLGfKYDNILMEEAAQILEIETFIPLllqnpqdg 1084
Cdd:COG1112 514 RRELKKRRELRKLLW------DALLELAPVVGMTP--ASVARLLPLGEG-SFDLVIIDEASQATLAEALGAL-------- 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1085 fSRLKRWIMIGDHHQLPPVIK--NMAFQKYSNMEQSLFTRFVRV-GVPTVDLDAQGRARASLCNLYNWR-YKNlgnlphv 1160
Cdd:COG1112 577 -ARAKRVVLVGDPKQLPPVVFgeEAEEVAEEGLDESLLDRLLARlPERGVMLREHYRMHPEIIAFSNRLfYDG------- 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1161 QLLPEFSTANAGLLYDFQLINVEDFQGVGESEPNPYFyqNLGEAEYVVALFMYMCLLGYPADKISILTTYNGQKHLIRDI 1240
Cdd:COG1112 649 KLVPLPSPKARRLADPDSPLVFIDVDGVYERRGGSRT--NPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVALIREL 726
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1241 INRRCGNNpliGRPNKVTTVDRFQGQQNDYILLSLVRTRAVGHLR-------DVRRLVVAMSRARLGLYIFARVSLFQNc 1313
Cdd:COG1112 727 LREALGDG---LEPVFVGTVDRFQGDERDVIIFSLVYSNDEDVPRnfgflngGPRRLNVAVSRARRKLIVVGSRELLDS- 802
|
490
....*....|
gi 38788372 1314 FELTPAFSQL 1323
Cdd:COG1112 803 DPSTPALKRL 812
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
790-1312 |
1.34e-28 |
|
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: 123.39 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 790 YPYNQPKRNTIQFT-------HTQIEAIR-AGMQPGLTMVVGPPGTGKTDVAVQIISNIYHNFPeqRTLIVTHSNQALNQ 861
Cdd:TIGR00376 139 REAPSKASEIHDFQffdpnlnESQKEAVLfALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGL--RVLVTAPSNIAVDN 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 862 LFEKIMALDIderHLLRLGHGEEELETEKDFSrygrVNYVLARRIElleevkrlqkslgvpgdasytcetagyfflYQVM 941
Cdd:TIGR00376 217 LLERLALCDQ---KIVRLGHPARLLKSNKQHS----LDYLIENHPK------------------------------YQIV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 942 SRWEEYISKVKNKgstlpdvtevstffpFHEYFANAPQpIFKGRSYEEDMEIA--EGCFRHIKKIFTQ-----LEEFRAS 1014
Cdd:TIGR00376 260 ADIREKIDELIEE---------------RNKKTKPSPQ-KRRGLSDIKILRKAlkKREARGIESLKIAsmaewIETNKSI 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1015 ELLRSGLDRSKYLLVKEakIIAMTCTHAALKRHDLVKlGFKYDNILMEEAAQILEIETFIPLLlqnpqdgfsRLKRWIMI 1094
Cdd:TIGR00376 324 DRLLKLLPESEERIMNE--ILAESDATNSMAGSEILN-GQYFDVAVIDEASQAMEPSCLIPLL---------KARKLILA 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1095 GDHHQLPPVIKNmafQKYSNMEQSLFTRFV-RVGVPTVDLDAQGRARASLC-----NLYNWRYK---NLGNLPHVQLLPE 1165
Cdd:TIGR00376 392 GDHKQLPPTILS---HDAEELSLTLFERLIkEYPERSRTLNVQYRMNQKIMefpsrEFYNGKLTaheSVANILLRDLPKV 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1166 FSTANAGLLYD---FQLINVEDFQGVGESEPNPYFYQNLGEAEYVVALFMYMCLLGYPADKISILTTYNGQKHLIRDIIN 1242
Cdd:TIGR00376 469 EATESEDDLETgipLLFIDTSGCELFELKEADSTSKYNPGEAELVSEIIQALVKMGVPANDIGVITPYDAQVDLLRQLLE 548
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38788372 1243 RRcgnNPLIgrpnKVTTVDRFQGQQNDYILLSLVRT---RAVGHLRDVRRLVVAMSRARLGLYIFARVSLFQN 1312
Cdd:TIGR00376 549 HR---HIDI----EVSSVDGFQGREKEVIIISFVRSnrkGEVGFLKDLRRLNVALTRARRKLIVIGDSRTLSN 614
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1115-1303 |
3.18e-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: 3.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1115 MEQSLFTRFVRVG-VPTVDLDAQGRARASLCNLYN-WRYKN-LGNLPHVQLLPEFSTANAGL-LYDFQLINVEDFQGVGE 1190
Cdd:pfam13087 1 LDRSLFERLQELGpSAVVMLDTQYRMHPEIMEFPSkLFYGGkLKDGPSVAERPLPDDFHLPDpLGPLVFIDVDGSEEEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1191 SEPNPYFyqNLGEAEYVVALFMYMCLLGYPADK-ISILTTYNGQKHLIRDIINRRCGNNPLIgrpnKVTTVDRFQGQQND 1269
Cdd:pfam13087 81 DGGTSYS--NEAEAELVVQLVEKLIKSGPEEPSdIGVITPYRAQVRLIRKLLKRKLGGKLEI----EVNTVDGFQGREKD 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 38788372 1270 YILLSLVRTRA---VGHLRDVRRLVVAMSRARLGLYI 1303
Cdd:pfam13087 155 VIIFSCVRSNEkggIGFLSDPRRLNVALTRAKRGLII 191
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
805-1107 |
2.15e-24 |
|
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: 103.96 E-value: 2.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 805 TQIEAIRAGM-QPGLTMVVGPPGTGKTDVAVQIISNIY-----HNFPEQRTLIVTHSNQALNQLFEKIMALDID-ERHLL 877
Cdd:pfam13086 1 SQREAIRSALsSSHFTLIQGPPGTGKTTTIVELIRQLLsypatSAAAGPRILVCAPSNAAVDNILERLLRKGQKyGPKIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 878 RLGHGEEELETEKDFSRYGRVNYVLARRiELLEEVKRLQKSlgvpgdasytcetagyfflyqvmsrweeyISKVKNKGST 957
Cdd:pfam13086 81 RIGHPAAISEAVLPVSLDYLVESKLNNE-EDAQIVKDISKE-----------------------------LEKLAKALRA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 958 LPDVTEVSTFFPFHEYFANapqpifKGRSYEEDMEIAEGCFRhikKIFTQLEEFRASELLRsgldrskyllvkEAKIIAM 1037
Cdd:pfam13086 131 FEKEIIVEKLLKSRNKDKS------KLEQERRKLRSERKELR---KELRRREQSLEREILD------------EAQIVCS 189
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1038 TCTHAAlkRHDLVKLgFKYDNILMEEAAQILEIETFIPLLLqnpqdgfsRLKRWIMIGDHHQLPPVIKNM 1107
Cdd:pfam13086 190 TLSGAG--SRLLSSL-ANFDVVIIDEAAQALEPSTLIPLLR--------GPKKVVLVGDPKQLPPTVISK 248
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
795-915 |
4.97e-05 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 45.95 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 795 PKRNTIQFTHTQIEAIRAGMQ-PGLTMVVGPPGTGKTDVAVQIISNIYHNFPEQRTLIVTHSNQALNQLFEKIMAL--DI 871
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSgLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLgpSL 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 38788372 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: 1227.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 18 INAEFVTQLACKYWAPHIK-KKSPFDIKVIEDIYEKEIVKSRFAIRKIMLLEFSQYLENYLWMNYSpEVSSKAYLMSICC 96
Cdd:pfam16399 1 IQEDRIAQLARKHWLKSKKsKKVKVKPEVVKKIYWDELEKEGFSLRSLLLLEFLQYLENYLWPNYT-EDASNAHVLLIVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 97 MVNEKFRENVPAWEIFKKKPDHFPFFFKHILKAALAETdgeFSLHEQTVLLLFLDHCFNSLEVDLIRSQVQQLISLPMWM 176
Cdd:pfam16399 80 MVNEKFREHLPAWELFSDRPDDFSSFFRRVLSLSLDRS---LSTAERTALLSFLIHAFQSLENELVRKECAPLVSISIWH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 177 GLQL-ARLELELKKTPKLRKFWNLIKKNDEKMDPEAREQAYQERRFLSQLIQKFISVLKSVPLSEPVTMDKVHYCERFIE 255
Cdd:pfam16399 157 NLSSeGRREQELDKNPQLRKAWRAAQKRYDAADDATKARLRFERSWLYTLLLDFLDVLYDIPEDGEVDDDNVRYCERFLE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 256 LMIDLEALLPTRRWFNTILDDSHLLVHCYLSNLVRREEdGHLFSQLLDMLKFYTGFEINDQTGNALTENEMTTIHYDRIT 335
Cdd:pfam16399 237 LLIDLESQLPTRRYVNTLLQDLHLLPACRLSPLYNDEE-GGLFRQLLDLLKHYTYFEIDDQTGEQLSDQEVYDAHYARLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 336 SLQRAAFAHFPE-LYDFALSNVAEVDTRESLVKFFGPLSSNTLHQVASYLCLLPTL-PKNEDTTFDKEFLLELLVSRHER 413
Cdd:pfam16399 316 RLQRTAFKHFKEkLTILALSNYGSIDKREELEKHLSALSDEELRELCSLLGLRTVPyPESDNIVYDRKFLLEVLLSRFEK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 414 RISQIQQLNQMPLYPTEKIIWDENIVPTEYYSGEGCLALPKLNLQFLTLHDYLLRNFNLFRLESTYEIRQDIEDSVSRMK 493
Cdd:pfam16399 396 RPSQQEAANELPLYPTEKTLWDENLVRTEYYDGSRPLALPKLNLQYLTLGDFLLRNFNLFRLESFYEIRQDIEDAVKRLK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 494 PWQSEYGGVVFGGWARMAQPIVAFTVVEVAKPNIGENWPTRVRADVTINL-NVRDHIKDEWEGLRKHDVCFLITVRPTKP 572
Cdd:pfam16399 476 PRLGEDGETRFGGWSRMALPISKPAIVEVAPPNVGESKPSRVRAEVTIDVsRLRDNIRREWESLRPHDVVFLLAVRPPDE 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 573 YGTKFDRRRPFIEQVGLVYVRGCEIQGMLDDKGRVIED------GPEPRPNlrgeSRTFRVFLDPNQYQQDMTNtIQNGA 646
Cdd:pfam16399 556 TYNKLTGSQSFAEQLGLVYVRGAEVIQVLDENGRVLREpqgqtnGPEPRPR----QRRLRVRLDANQYKADMDR-AAEGK 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 647 EDVYETFNIIMRRKPKENNFKAVLETIRNLMNTDCVVPDWLHDIILGYGDPSSAHYSKMPNQIATLDFNDTFLSIEHLKA 726
Cdd:pfam16399 631 PDVYETFNVLVRRKPRENNFKAVLETIRDLMNSDCVVPDWLHDVFLGYGDPAAAHYKNLPNRLKTVDFRDTFLDWQHLIE 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 727 SFPGHNVKVTVEDPALQIPPFRITFPVR-----SGKGKKRKDADVEDEDTEEAKTLIVEPHVIPNRGPYPYNQPKRNTIQ 801
Cdd:pfam16399 711 SFPGKTIEPSDDVSGSFGPPYVLEFPDSppepaPAKPSKKRRRDQEPAPQAEPETIRVSTYKPPNRGPYPVDAPKLNSVR 790
|
.
gi 38788372 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 ... |
797-1152 |
5.60e-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: 387.17 E-value: 5.60e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 797 RNTIQFTHTQIEAIRAGMQPGLTMVVGPPGTGKTDVAVQIISNIYHNFPEQRTLIVTHSNQALNQLFEKIMALDIDERHL 876
Cdd:cd17935 1 QNTVKFTPTQIEAIRSGMQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPNQRTLIVTHSNQALNQLFEKIMALDIDERHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 877 LRLGHGeeeletekdfsrygrvnyvlarrielleevkrlqkslgvpgdasytcetagyfflyqvmsrweeyiskvknkgs 956
Cdd:cd17935 81 LRLGHG-------------------------------------------------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 957 tlpdvtevstffpfheyfanapqpifkgrsyeedmeiaegcfrhikkiftqleefrasellrsgldrskyllvkeAKIIA 1036
Cdd:cd17935 87 ---------------------------------------------------------------------------AKIIA 91
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1037 MTCTHAALKRHDLVKLGFKYDNILMEEAAQILEIETFIPLLLQNPQDGFSRLKRWIMIGDHHQLPPVIKNMAFQKYSNME 1116
Cdd:cd17935 92 MTCTHAALKRGELVELGFKYDNILMEEAAQILEIETFIPLLLQNPEDGPNRLKRLIMIGDHHQLPPVIKNMAFQKYSNME 171
|
330 340 350
....*....|....*....|....*....|....*.
gi 38788372 1117 QSLFTRFVRVGVPTVDLDAQGRARASLCNLYNWRYK 1152
Cdd:cd17935 172 QSLFTRLVRLGVPTVDLDAQGRARASISSLYNWRYK 207
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
1140-1323 |
3.73e-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: 3.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1140 RASLCNLYNWRYKNLGNLPHVQLLP-EFSTANAGLLYDFQLINVEdfqGVGESEPNPYFYQNLGEAEYVVALFMYMCLLG 1218
Cdd:cd18808 2 HPEISEFPSKLFYEGKLKAGVSVAArLNPPPLPGPSKPLVFVDVS---GGEEREESGTSKSNEAEAELVVELVKYLLKSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1219 YPADKISILTTYNGQKHLIRDIINRRCGNNPLIgrpnKVTTVDRFQGQQNDYILLSLVRTR----AVGHLRDVRRLVVAM 1294
Cdd:cd18808 79 VKPSSIGVITPYRAQVALIRELLRKRGGLLEDV----EVGTVDNFQGREKDVIILSLVRSNesggSIGFLSDPRRLNVAL 154
|
170 180
....*....|....*....|....*....
gi 38788372 1295 SRARLGLYIFARVSLFQNCFELTPAFSQL 1323
Cdd:cd18808 155 TRAKRGLIIVGNPDTLSKDPLWKKLLEYL 183
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
845-1323 |
4.41e-35 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 145.27 E-value: 4.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 845 PEQRTLIVTHSNQALNQLFEKIMALDIDERHLLRLGHGEEELETEKDFSRYGRVNYVLARRIELLEEVKRLQKSLGVPGD 924
Cdd:COG1112 355 ALLRLLAALLLALALLLLLALEELLLLALLRLLAEGLALLLLLLLAALLRLARALLLLALLLAAAAAALAALLLLALALL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 925 ASYTCETAGYFFLYQVMSRWEEYISKVKNKGSTLPDVTEVSTFFPFHEYFANAPQPIFKGRSYEEDMEIAEGCfRHIKKI 1004
Cdd:COG1112 435 AALLALLLLLAAALAALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPEELEKLIAELREAA-RLRRAL 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1005 FTQLEEFRASELLRSgldrskYLLVKEAKIIAMTCthAALKRHDLVKLGfKYDNILMEEAAQILEIETFIPLllqnpqdg 1084
Cdd:COG1112 514 RRELKKRRELRKLLW------DALLELAPVVGMTP--ASVARLLPLGEG-SFDLVIIDEASQATLAEALGAL-------- 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1085 fSRLKRWIMIGDHHQLPPVIK--NMAFQKYSNMEQSLFTRFVRV-GVPTVDLDAQGRARASLCNLYNWR-YKNlgnlphv 1160
Cdd:COG1112 577 -ARAKRVVLVGDPKQLPPVVFgeEAEEVAEEGLDESLLDRLLARlPERGVMLREHYRMHPEIIAFSNRLfYDG------- 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1161 QLLPEFSTANAGLLYDFQLINVEDFQGVGESEPNPYFyqNLGEAEYVVALFMYMCLLGYPADKISILTTYNGQKHLIRDI 1240
Cdd:COG1112 649 KLVPLPSPKARRLADPDSPLVFIDVDGVYERRGGSRT--NPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVALIREL 726
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1241 INRRCGNNpliGRPNKVTTVDRFQGQQNDYILLSLVRTRAVGHLR-------DVRRLVVAMSRARLGLYIFARVSLFQNc 1313
Cdd:COG1112 727 LREALGDG---LEPVFVGTVDRFQGDERDVIIFSLVYSNDEDVPRnfgflngGPRRLNVAVSRARRKLIVVGSRELLDS- 802
|
490
....*....|
gi 38788372 1314 FELTPAFSQL 1323
Cdd:COG1112 803 DPSTPALKRL 812
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
790-1312 |
1.34e-28 |
|
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: 123.39 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 790 YPYNQPKRNTIQFT-------HTQIEAIR-AGMQPGLTMVVGPPGTGKTDVAVQIISNIYHNFPeqRTLIVTHSNQALNQ 861
Cdd:TIGR00376 139 REAPSKASEIHDFQffdpnlnESQKEAVLfALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGL--RVLVTAPSNIAVDN 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 862 LFEKIMALDIderHLLRLGHGEEELETEKDFSrygrVNYVLARRIElleevkrlqkslgvpgdasytcetagyfflYQVM 941
Cdd:TIGR00376 217 LLERLALCDQ---KIVRLGHPARLLKSNKQHS----LDYLIENHPK------------------------------YQIV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 942 SRWEEYISKVKNKgstlpdvtevstffpFHEYFANAPQpIFKGRSYEEDMEIA--EGCFRHIKKIFTQ-----LEEFRAS 1014
Cdd:TIGR00376 260 ADIREKIDELIEE---------------RNKKTKPSPQ-KRRGLSDIKILRKAlkKREARGIESLKIAsmaewIETNKSI 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1015 ELLRSGLDRSKYLLVKEakIIAMTCTHAALKRHDLVKlGFKYDNILMEEAAQILEIETFIPLLlqnpqdgfsRLKRWIMI 1094
Cdd:TIGR00376 324 DRLLKLLPESEERIMNE--ILAESDATNSMAGSEILN-GQYFDVAVIDEASQAMEPSCLIPLL---------KARKLILA 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1095 GDHHQLPPVIKNmafQKYSNMEQSLFTRFV-RVGVPTVDLDAQGRARASLC-----NLYNWRYK---NLGNLPHVQLLPE 1165
Cdd:TIGR00376 392 GDHKQLPPTILS---HDAEELSLTLFERLIkEYPERSRTLNVQYRMNQKIMefpsrEFYNGKLTaheSVANILLRDLPKV 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1166 FSTANAGLLYD---FQLINVEDFQGVGESEPNPYFYQNLGEAEYVVALFMYMCLLGYPADKISILTTYNGQKHLIRDIIN 1242
Cdd:TIGR00376 469 EATESEDDLETgipLLFIDTSGCELFELKEADSTSKYNPGEAELVSEIIQALVKMGVPANDIGVITPYDAQVDLLRQLLE 548
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38788372 1243 RRcgnNPLIgrpnKVTTVDRFQGQQNDYILLSLVRT---RAVGHLRDVRRLVVAMSRARLGLYIFARVSLFQN 1312
Cdd:TIGR00376 549 HR---HIDI----EVSSVDGFQGREKEVIIISFVRSnrkGEVGFLKDLRRLNVALTRARRKLIVIGDSRTLSN 614
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1115-1303 |
3.18e-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: 3.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1115 MEQSLFTRFVRVG-VPTVDLDAQGRARASLCNLYN-WRYKN-LGNLPHVQLLPEFSTANAGL-LYDFQLINVEDFQGVGE 1190
Cdd:pfam13087 1 LDRSLFERLQELGpSAVVMLDTQYRMHPEIMEFPSkLFYGGkLKDGPSVAERPLPDDFHLPDpLGPLVFIDVDGSEEEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1191 SEPNPYFyqNLGEAEYVVALFMYMCLLGYPADK-ISILTTYNGQKHLIRDIINRRCGNNPLIgrpnKVTTVDRFQGQQND 1269
Cdd:pfam13087 81 DGGTSYS--NEAEAELVVQLVEKLIKSGPEEPSdIGVITPYRAQVRLIRKLLKRKLGGKLEI----EVNTVDGFQGREKD 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 38788372 1270 YILLSLVRTRA---VGHLRDVRRLVVAMSRARLGLYI 1303
Cdd:pfam13087 155 VIIFSCVRSNEkggIGFLSDPRRLNVALTRAKRGLII 191
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
805-1107 |
2.15e-24 |
|
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: 103.96 E-value: 2.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 805 TQIEAIRAGM-QPGLTMVVGPPGTGKTDVAVQIISNIY-----HNFPEQRTLIVTHSNQALNQLFEKIMALDID-ERHLL 877
Cdd:pfam13086 1 SQREAIRSALsSSHFTLIQGPPGTGKTTTIVELIRQLLsypatSAAAGPRILVCAPSNAAVDNILERLLRKGQKyGPKIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 878 RLGHGEEELETEKDFSRYGRVNYVLARRiELLEEVKRLQKSlgvpgdasytcetagyfflyqvmsrweeyISKVKNKGST 957
Cdd:pfam13086 81 RIGHPAAISEAVLPVSLDYLVESKLNNE-EDAQIVKDISKE-----------------------------LEKLAKALRA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 958 LPDVTEVSTFFPFHEYFANapqpifKGRSYEEDMEIAEGCFRhikKIFTQLEEFRASELLRsgldrskyllvkEAKIIAM 1037
Cdd:pfam13086 131 FEKEIIVEKLLKSRNKDKS------KLEQERRKLRSERKELR---KELRRREQSLEREILD------------EAQIVCS 189
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1038 TCTHAAlkRHDLVKLgFKYDNILMEEAAQILEIETFIPLLLqnpqdgfsRLKRWIMIGDHHQLPPVIKNM 1107
Cdd:pfam13086 190 TLSGAG--SRLLSSL-ANFDVVIIDEAAQALEPSTLIPLLR--------GPKKVVLVGDPKQLPPTVISK 248
|
|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
1034-1137 |
4.45e-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: 4.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1034 IIAMTCTHAALKRhdlvklgfkYDNILMEEAAQILEIETFIPlllqnpQDGFSRLKRWIMIGDHHQLPPVIKNMAFQKYS 1113
Cdd:cd17914 34 ILLVTPTNKAAAQ---------LDNILVDEAAQILEPETSRL------IDLALDQGRVILVGDHDQLGPVWRGAVLAKIC 98
|
90 100
....*....|....*....|....
gi 38788372 1114 NmEQSLFTRFVRVGVPTVDLDAQG 1137
Cdd:cd17914 99 N-EQSLFTRLVRLGVSLIRLQVQY 121
|
|
| DEXXQc_UPF1 |
cd18039 |
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ... |
804-1138 |
6.91e-20 |
|
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: 90.38 E-value: 6.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 804 HTQIEAIRAGMQPGLTMVVGPPGTGKTDVAVQIISNIYHNFPEQrTLIVTHSNQALNQLFEKImaldiDERHLlrlghge 883
Cdd:cd18039 4 HSQVDAVKTALQRPLSLIQGPPGTGKTVTSATIVYHLVKQGNGP-VLVCAPSNVAVDQLTEKI-----HQTGL------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 884 eeletekdfsrygRVNYVLARRIElleevkrlqkslGVPGDASYTCetagyffLYQVMSRWEEYISKVKNKGSTLpDVTE 963
Cdd:cd18039 71 -------------KVVRLCAKSRE------------AVESPVSFLA-------LHNQVRNLDSAEKLELLKLLKL-ETGE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 964 VStffpfheyfanapqpifkgrSYEEdmeiaegcfRHIKKIFTQLEefraSELLRsgldrskyllvkEAKIIAMTCTHAA 1043
Cdd:cd18039 118 LS--------------------SADE---------KRYRKLKRKAE----RELLR------------NADVICCTCVGAG 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1044 LKRhdLVKlgFKYDNILMEEAAQILEIETFIPLLLQnpqdgfsrLKRWIMIGDHHQLPPVIKNMAFQKYSnMEQSLFTRF 1123
Cdd:cd18039 153 DPR--LSK--MKFRTVLIDEATQATEPECLIPLVHG--------AKQVILVGDHCQLGPVVMCKKAAKAG-LSQSLFERL 219
|
330
....*....|....*
gi 38788372 1124 VRVGVPTVDLDAQGR 1138
Cdd:cd18039 220 VQLGIRPIRLQVQYR 234
|
|
| DEXXQc_SETX |
cd18042 |
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ... |
995-1138 |
1.60e-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: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 995 EGCFRHIKKIFTQLE-EFRASELLRSGLDRSKYLLVKEAKIIAmtCTHAALKRHDLVKLGFKYDNILMEEAAQILEIETF 1073
Cdd:cd18042 85 EIVLRLLSEGFLDGDgRSYKPNVVRVGRQELRASILNEADIVC--TTLSSSGSDLLESLPRGFDTVIIDEAAQAVELSTL 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38788372 1074 IPLLLqnpqdgfsRLKRWIMIGDHHQLPPVIKNMAFQKYsNMEQSLFTRFVRVGVPTVDLDAQGR 1138
Cdd:cd18042 163 IPLRL--------GCKRLILVGDPKQLPATVFSKVAQKL-GYDRSLFERLQLAGYPVLMLTTQYR 218
|
|
| DEXXQc_Helz-like |
cd18038 |
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ... |
806-1150 |
4.81e-16 |
|
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: 79.20 E-value: 4.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 806 QIEAIRA----GMQPGLTMVVGPPGTGKTDVAVQIISNIYHNFPEQRTLIVTHSNQALNQLfekimaldiderhLLRLgh 881
Cdd:cd18038 6 QKLAVRNivtgTSRPPPYIIFGPPGTGKTVTLVEAILQVLRQPPEARILVCAPSNSAADLL-------------AERL-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 882 geeeletekdfsrygrVNYVLARRielleEVKRLQkslgvpgdaSYTCETAGYfflyqvmsrweeyiskvknkgstlpdv 961
Cdd:cd18038 71 ----------------LNALVTKR-----EILRLN---------APSRDRASV--------------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 962 tevstffpfheyfanaPQPIFKGRSYeedmeIAEGCFRHIkkiftQLEEfrasellrsgldrskyllVKEAKIIAMTCTH 1041
Cdd:cd18038 94 ----------------PPELLPYCNS-----KAEGTFRLP-----SLEE------------------LKKYRIVVCTLMT 129
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1042 AALkrhdLVKLGFK---YDNILMEEAAQILEIETFIPLLLQNPQDGfsrlkRWIMIGDHHQLPPVIKNMAFQKYsNMEQS 1118
Cdd:cd18038 130 AGR----LVQAGVPnghFTHIFIDEAGQATEPEALIPLSELASKNT-----QIVLAGDPKQLGPVVRSPLARKY-GLGKS 199
|
330 340 350
....*....|....*....|....*....|..
gi 38788372 1119 LFTRFVRVGVPTVDLDAQGRARASLCNlyNWR 1150
Cdd:cd18038 200 LLERLMERPLYYKDGEYNPSYITKLLK--NYR 229
|
|
| EEXXEc_NFX1 |
cd17936 |
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ... |
804-1136 |
2.29e-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: 75.66 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 804 HTQIEAIRAGMQPGLTMVVGPPGTGKTDVAVQIISNIYHNFPEQRT---LIVTHSNQALNQLFEKImaLDIDERHLLRLG 880
Cdd:cd17936 4 PSQLEALKHALTSELALIQGPPGTGKTFLGVKLVRALLQNQDLSITgpiLVVCYTNHALDQFLEGL--LDFGPTKIVRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 881 hgeeeletekdfsrygrvnyvlarrielleevkrlqkslgvpgdasytcetagyfflyqvmsrweeyiskvknkgstlpd 960
Cdd:cd17936 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 961 vtevstffpfheyfanapqpifkgrsyeedmeiaegcfrhikkiftqleefrasellrsgldrskyllvkeAKIIAMTCT 1040
Cdd:cd17936 82 -----------------------------------------------------------------------ARVIGMTTT 90
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1041 HAALKRHDLVKLGFKYdnILMEEAAQILE--IETFIPlllqnpqdgfSRLKRWIMIGDHHQLPPVIKNMAFQ--KYsNME 1116
Cdd:cd17936 91 GAAKYRELLQALGPKV--VIVEEAAEVLEahILAALT----------PSTEHLILIGDHKQLRPKVNVYELTakKY-NLD 157
|
330 340
....*....|....*....|
gi 38788372 1117 QSLFTRFVRVGVPTVDLDAQ 1136
Cdd:cd17936 158 VSLFERLVKNGLPFVTLNVQ 177
|
|
| DEXXc_HELZ2-C |
cd18040 |
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
806-1123 |
3.90e-12 |
|
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: 68.32 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 806 QIEAIRAGMQPGLTMVVGPPGTGKTDVAVQIIsniYHnFPEQrtlivthsNQALNQLFEKIMALDiderHLLRLGHGEEE 885
Cdd:cd18040 6 QNHAVRTALTKPFTLIQGPPGTGKTVTGVHIA---YW-FAKQ--------NREIQSVSGEGDGGP----CVLYCGPSNKS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 886 LEtekdfsrygrvnyVLArriELLEEVKRLqKSLGVPGDASYTCEtagyFFLYQVMSRWEEYISKVKNKGSTLPDVTevs 965
Cdd:cd18040 70 VD-------------VVA---ELLLKVPGL-KILRVYSEQIETTE----YPIPNEPRHPNKKSERESKPNSELSSIT--- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 966 tffpFHEYFANAPQPifkgrsyeedmeiaegcfrHIKKIFTQLEEF-RASELLRSG-LDRSKYLLVKEAK-------IIA 1036
Cdd:cd18040 126 ----LHHRIRQPSNP-------------------HSQQIKAFEARFeRTQEKITEEdIKTYKILIWEARFeeletvdVIL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1037 MTCTHAALKRhdlVKLGFKYDNILMEEAAQILEIETFIPLLlqnpqdGFSRLKRWIMIGDHHQLPPVIKNMAFQKYSnME 1116
Cdd:cd18040 183 CTCSEAASQK---MRTHANVKQCIVDECGMCTEPESLIPIV------SAPRAEQVVLIGDHKQLRPVVQNKEAQKLG-LG 252
|
....*..
gi 38788372 1117 QSLFTRF 1123
Cdd:cd18040 253 RSLFERY 259
|
|
| DEXXQc_Upf1-like |
cd17934 |
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ... |
1032-1138 |
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 38788372 1032 AKIIAMTCTHAALKRHDLVklgfkydniLMEEAAQILEIETFIPLLlqnpqdgfsRLKRWIMIGDHHQLPPVIKNMAFQK 1111
Cdd:cd17934 30 KRVLVTAQSNVAVDNVDVV---------IIDEASQITEPELLIALI---------RAKKVVLVGDPKQLPPVVQEDHAAL 91
|
90 100 110
....*....|....*....|....*....|
gi 38788372 1112 Y---SNMEQSLFTRFVRVGVPTVDLDAQGR 1138
Cdd:cd17934 92 LglsFILSLLLLFRLLLPGSPKVMLDTQYR 121
|
|
| DEXXQc_DNA2 |
cd18041 |
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ... |
1001-1123 |
1.28e-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: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1001 IKKIFTQLEEFRASELLRSGLDRSKY-LLVKEAKIIAMTC---THAALKRHdlvklgfKYDNILMEEAAQILEIETFIPL 1076
Cdd:cd18041 78 LKKIHPDVQEFTLEAILKSCKSVEELeSKYESVSVVATTClgiNHPIFRRR-------TFDYCIVDEASQITLPICLGPL 150
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 38788372 1077 LLQnpqdgfsrlKRWIMIGDHHQLPPVIKNMAFQKySNMEQSLFTRF 1123
Cdd:cd18041 151 RLA---------KKFVLVGDHYQLPPLVKSREARE-LGMDESLFKRL 187
|
|
| DEXXQc_SMUBP2 |
cd18044 |
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ... |
1016-1131 |
3.43e-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: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1016 LLRSGLDRSKYLLVkEAKIIAMTCTHAAlkrHDLVKLGFKYDNILMEEAAQILEIETFIPLLlqnpqdgfsRLKRWIMIG 1095
Cdd:cd18044 81 LLESVLDHSLDALV-AAQVVLATNTGAG---SRQLLPNELFDVVVIDEAAQALEASCWIPLL---------KARRCILAG 147
|
90 100 110
....*....|....*....|....*....|....*.
gi 38788372 1096 DHHQLPPVIKNMAFQKYsNMEQSLFTRFVRVGVPTV 1131
Cdd:cd18044 148 DHKQLPPTILSDKAARG-GLGVTLFERLVNLYGESV 182
|
|
| SF1_C |
cd18786 |
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ... |
1223-1303 |
1.60e-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: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1223 KISILTTYNGQKHLIRDIInRRCGNNPLIGRPNKVTTVDRFQGQQNDYILLSLVRTravgHLRDVRRLVVAMSRARLGLY 1302
Cdd:cd18786 12 KGVVLTPYHRDRAYLNQYL-QGLSLDEFDLQLVGAITIDSSQGLTFDVVTLYLPTA----NSLTPRRLYVALTRARKRLV 86
|
.
gi 38788372 1303 I 1303
Cdd:cd18786 87 I 87
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
806-895 |
3.53e-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: 48.07 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 806 QIEAIRAGMQ-----PGltMVVGPPGTGKTDVAVQIISNIYhnfpEQRTLIVTHSNQALNQLFEKIMALDIDeRHLLRLG 880
Cdd:cd17926 5 QEEALEAWLAhknnrRG--ILVLPTGSGKTLTALALIAYLK----ELRTLIVVPTDALLDQWKERFEDFLGD-SSIGLIG 77
|
90
....*....|....*..
gi 38788372 881 HGEEELETEK--DFSRY 895
Cdd:cd17926 78 GGKKKDFDDAnvVVATY 94
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
709-866 |
7.55e-06 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 50.41 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 709 IATLDFNDTFLSIEHLKASFPGHNVKVTVEDPALQIPPFRITFPVRSGKGKKRKDADVEDEDTEEAKTLIVEPHVIPNRG 788
Cdd:COG1061 1 VLLRGIAERGADKLRSSLLLLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 789 PYPYnqpkrntiqfthtQIEAIRA-------GMQPGLtmVVGPPGTGKTDVAVQIISNIYHNfpeQRTLIVTHSNQALNQ 861
Cdd:COG1061 81 LRPY-------------QQEALEAllaalerGGGRGL--VVAPTGTGKTVLALALAAELLRG---KRVLVLVPRRELLEQ 142
|
....*
gi 38788372 862 LFEKI 866
Cdd:COG1061 143 WAEEL 147
|
|
| DEXXQc_SF1 |
cd18043 |
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ... |
805-883 |
9.06e-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: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 805 TQIEAIRAGMQPGLTMVVGPPGTGKTDVAVQIISNIYHNfpEQRTLIVTHSNQALNQLFEKIMALDIDE-RHLLRLGHGE 883
Cdd:cd18043 3 SQEAAIISARNGKNVVIQGPPGTGKSQTIANIIANALAR--GKRVLFVSEKKAALDVVRFPCWIMSPLSvSQYLPLNRNL 80
|
|
| DEXXQc_Upf1-like |
cd17934 |
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ... |
818-862 |
1.21e-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: 1.21e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 38788372 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 ... |
1029-1122 |
2.46e-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: 47.09 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1029 VKEAKIIAMT-CTHAALKRHDLVKLGFKYdnILMEEAAQILEIETFIPLLLQNpqdgfsRLKRWIMIGDHHQLPPVIKNm 1107
Cdd:cd18077 121 VMRHRVVVVTlSTSQYLCQLDLEPGFFTH--ILLDEAAQAMECEAIMPLALAT------KSTRIVLAGDHMQLSPEVYS- 191
|
90
....*....|....*
gi 38788372 1108 AFQKYSNMEQSLFTR 1122
Cdd:cd18077 192 EFARERNLHISLLER 206
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
795-915 |
4.97e-05 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 45.95 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 795 PKRNTIQFTHTQIEAIRAGMQ-PGLTMVVGPPGTGKTDVAVQIISNIYHNFPEQRTLIVTHSNQALNQLFEKIMAL--DI 871
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSgLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLgpSL 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 38788372 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 |
3.01e-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: 3.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 38788372 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 ... |
1040-1122 |
5.41e-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: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38788372 1040 THAALKRHDLVKLGFkYDNILMEEAAQILEIETFIPLLLQNPQdgfsrlKRWIMIGDHHQLPPviKNMAFQKYSNMEQSL 1119
Cdd:cd18076 132 TTTAMAFNLHVLSGF-FTHIFIDEAAQMLECEALIPLSYAGPK------TRVVLAGDHMQMTP--KLFSVADYNRANHTL 202
|
...
gi 38788372 1120 FTR 1122
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 ... |
1257-1303 |
1.46e-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: 1.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 38788372 1257 VTTVDRFQGQQNDYILLSLVRTRAVGHLRDVRRLV-VAMSRARLGLYI 1303
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 |
1.69e-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: 40.62 E-value: 1.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38788372 806 QIEAIRA---GMQPGLT--MVVGPPGTGKTDVAVQIISNIYHNFPEQRTLIVTHSNQALNQLFEKIMAL 869
Cdd:cd18032 5 QQEAIEAleeAREKGQRraLLVMATGTGKTYTAAFLIKRLLEANRKKRILFLAHREELLEQAERSFKEV 73
|
|
| |
