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Conserved domains on  [gi|163644327|ref|NP_033832|]
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RNA helicase aquarius isoform a [Mus musculus]

Protein Classification

RNA helicase aquarius( domain architecture ID 13872322)

RNA helicase 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); belongs to the DEAD/DEAH box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding

Graphical summary

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List of domain hits

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
 
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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 163644327  806 QIEAIRA---GMQPGLT--MVVGPPGTGKTDVAVQIISNIYHNFPEQRTLIVTHSNQALNQLFEKIMAL 869
Cdd:cd18032     5 QQEAIEAleeAREKGQRraLLVMATGTGKTYTAAFLIKRLLEANRKKRILFLAHREELLEQAERSFKEV 73
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
820-858 9.88e-03

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
                  ....*....|....*....|....*....|....*....
gi 163644327  820 MVVGPPGTGKTDVAVQIISNIYHNfPEQRTLIVTHSNQA 858
Cdd:cd18077    25 LLIGPFGTGKTFTLAQAVKHILQQ-PETRILICTHSNSA 62
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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