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Conserved domains on  [gi|1811574662|ref|XP_032357229|]
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RNA helicase aquarius isoform X2 [Etheostoma spectabile]

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 ...
21-806 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: 1198.13  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662   21 INAEYVTQLANKYWAPHAK-NKLPFDPKVMEDVYEKEILKSKFAIRKIMLLEFSQYLENYLWVNYAPKvSSNAYLMSICC 99
Cdd:pfam16399    1 IQEDRIAQLARKHWLKSKKsKKVKVKPEVVKKIYWDELEKEGFSLRSLLLLEFLQYLENYLWPNYTED-ASNAHVLLIVL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  100 IVNEKFRENVPAWEVFKKEPSHFPFFFKCVMEASLADEkacLTLKEQTVLLVFLDHCFNSLEVDLIREQVQQLIALPMWM 179
Cdd:pfam16399   80 MVNEKFREHLPAWELFSDRPDDFSSFFRRVLSLSLDRS---LSTAERTALLSFLIHAFQSLENELVRKECAPLVSISIWH 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  180 CL-LPSRLQQELKKVPKLQKFWNLIKKKCDKMDAESAEQAKKERTFLSALIKKFLGVLMSIPPSGPVSMDKVHYCERFIE 258
Cdd:pfam16399  157 NLsSEGRREQELDKNPQLRKAWRAAQKRYDAADDATKARLRFERSWLYTLLLDFLDVLYDIPEDGEVDDDNVRYCERFLE 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  259 LMIDLEALLPTRRWFNTVLDDSHLVVSCHLSSLTQREkEGHLFCQLLDMLKFYTGFEINDQTGNALTEKEMTTLHYDKIL 338
Cdd:pfam16399  237 LLIDLESQLPTRRYVNTLLQDLHLLPACRLSPLYNDE-EGGLFRQLLDLLKHYTYFEIDDQTGEQLSDQEVYDAHYARLA 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  339 SLQRAAFAHFPE-LQDFALSNVAAVDTRESLMKHFGHLSPNTLHQVASYLCL-LPELPEGQDTTYEKEVLLELLVSRHER 416
Cdd:pfam16399  316 RLQRTAFKHFKEkLTILALSNYGSIDKREELEKHLSALSDEELRELCSLLGLrTVPYPESDNIVYDRKFLLEVLLSRFEK 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  417 RISQIEQLNQMPLYPTEKIIWDENIVPTEYYSGEGCLALPKLNLQFLTLHDYLLRNFNLFRLESTYEIRQDIEDVVWRMK 496
Cdd:pfam16399  396 RPSQQEAANELPLYPTEKTLWDENLVRTEYYDGSRPLALPKLNLQYLTLGDFLLRNFNLFRLESFYEIRQDIEDAVKRLK 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  497 PWQSEYGGAVFGGWARMAQMITSFSIVEVAKPNIGESWPARVRADVTVNL-NVQDHIKHEWEGLRKHDVCLLITVRPNLP 575
Cdd:pfam16399  476 PRLGEDGETRFGGWSRMALPISKPAIVEVAPPNVGESKPSRVRAEVTIDVsRLRDNIRREWESLRPHDVVFLLAVRPPDE 555
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  576 YGTRFDRRQPFVEQTGLVYVRGCEVQGMLDDKGRVIEE------GPDPKPKLrgdaRTFRVWLDPNQYQQDMTsSIQSGT 649
Cdd:pfam16399  556 TYNKLTGSQSFAEQLGLVYVRGAEVIQVLDENGRVLREpqgqtnGPEPRPRQ----RRLRVRLDANQYKADMD-RAAEGK 630
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  650 EDPYETFNIIMRRKPKENNFKAVLETIRNLMNTECVVPDWLHDIILGYGDPGSAHYSKMPNQISTLDFNDTFLSLDHLHL 729
Cdd:pfam16399  631 PDVYETFNVLVRRKPRENNFKAVLETIRDLMNSDCVVPDWLHDVFLGYGDPAAAHYKNLPNRLKTVDFRDTFLDWQHLIE 710
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  730 CFPGYTIKVTEENPDLQVFPFRITFPISNKAD----KVKKRKADDEVEDKEEDMTLIVEPYVTLNRGPYPYNQPKRNTIQ 805
Cdd:pfam16399  711 SFPGKTIEPSDDVSGSFGPPYVLEFPDSPPEPapakPSKKRRRDQEPAPQAEPETIRVSTYKPPNRGPYPVDAPKLNSVR 790

                   .
gi 1811574662  806 F 806
Cdd:pfam16399  791 F 791
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
801-1156 3.02e-127

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: 392.95  E-value: 3.02e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  801 RNTIQFTPTQIEAIRAGMQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPEQRTLIVTHSNQALNQLFEKIMALDIDERHL 880
Cdd:cd17935      1 QNTVKFTPTQIEAIRSGMQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPNQRTLIVTHSNQALNQLFEKIMALDIDERHL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  881 LRLGHGeeeletekdfsrygrvnyvlarrlellrevgrlqesldvpgdvsytcetaghfylyqvisrweeymskvkpkqg 960
Cdd:cd17935     81 LRLGHG-------------------------------------------------------------------------- 86
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  961 ktvevqavaahfpfhkyfsnapqpvfkgrsyeeemdiaegcyrhikkiftqleefrafellrsgldrskyllvkeAKIIA 1040
Cdd:cd17935     87 ---------------------------------------------------------------------------AKIIA 91
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1041 MTCTHAALKRHDLVELGFKYDNILMEEAAQILEIETFIPLLLQNPEDGYSRLKRWIMIGDHHQLPPVIKNMAFQKYSNME 1120
Cdd:cd17935     92 MTCTHAALKRGELVELGFKYDNILMEEAAQILEIETFIPLLLQNPEDGPNRLKRLIMIGDHHQLPPVIKNMAFQKYSNME 171
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1811574662 1121 QSLFTRFVRLGVPTIDLDAQGRARASLCNLYNWRYK 1156
Cdd:cd17935    172 QSLFTRLVRLGVPTVDLDAQGRARASISSLYNWRYK 207
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
1144-1327 2.35e-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: 170.49  E-value: 2.35e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1144 RASLCNLYNWRYKHLGNLPHVQ-QLPEFQVPNPGLTFDFQLINVEdfnGVGESEPNPYFYQNLAEAEYTVALYMYMRLLG 1222
Cdd:cd18808      2 HPEISEFPSKLFYEGKLKAGVSvAARLNPPPLPGPSKPLVFVDVS---GGEEREESGTSKSNEAEAELVVELVKYLLKSG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1223 YPADRISILTTYNGQKHLIRDVINQRCAGNPFFsqpnKVTTVDRFQGQQNDYIILSLVRTK----AVGHLRDVRRLVVAM 1298
Cdd:cd18808     79 VKPSSIGVITPYRAQVALIRELLRKRGGLLEDV----EVGTVDNFQGREKDVIILSLVRSNesggSIGFLSDPRRLNVAL 154
                          170       180
                   ....*....|....*....|....*....
gi 1811574662 1299 SRARLGLYIFARVALFQNCFELTPVFNQL 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 ...
21-806 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: 1198.13  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662   21 INAEYVTQLANKYWAPHAK-NKLPFDPKVMEDVYEKEILKSKFAIRKIMLLEFSQYLENYLWVNYAPKvSSNAYLMSICC 99
Cdd:pfam16399    1 IQEDRIAQLARKHWLKSKKsKKVKVKPEVVKKIYWDELEKEGFSLRSLLLLEFLQYLENYLWPNYTED-ASNAHVLLIVL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  100 IVNEKFRENVPAWEVFKKEPSHFPFFFKCVMEASLADEkacLTLKEQTVLLVFLDHCFNSLEVDLIREQVQQLIALPMWM 179
Cdd:pfam16399   80 MVNEKFREHLPAWELFSDRPDDFSSFFRRVLSLSLDRS---LSTAERTALLSFLIHAFQSLENELVRKECAPLVSISIWH 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  180 CL-LPSRLQQELKKVPKLQKFWNLIKKKCDKMDAESAEQAKKERTFLSALIKKFLGVLMSIPPSGPVSMDKVHYCERFIE 258
Cdd:pfam16399  157 NLsSEGRREQELDKNPQLRKAWRAAQKRYDAADDATKARLRFERSWLYTLLLDFLDVLYDIPEDGEVDDDNVRYCERFLE 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  259 LMIDLEALLPTRRWFNTVLDDSHLVVSCHLSSLTQREkEGHLFCQLLDMLKFYTGFEINDQTGNALTEKEMTTLHYDKIL 338
Cdd:pfam16399  237 LLIDLESQLPTRRYVNTLLQDLHLLPACRLSPLYNDE-EGGLFRQLLDLLKHYTYFEIDDQTGEQLSDQEVYDAHYARLA 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  339 SLQRAAFAHFPE-LQDFALSNVAAVDTRESLMKHFGHLSPNTLHQVASYLCL-LPELPEGQDTTYEKEVLLELLVSRHER 416
Cdd:pfam16399  316 RLQRTAFKHFKEkLTILALSNYGSIDKREELEKHLSALSDEELRELCSLLGLrTVPYPESDNIVYDRKFLLEVLLSRFEK 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  417 RISQIEQLNQMPLYPTEKIIWDENIVPTEYYSGEGCLALPKLNLQFLTLHDYLLRNFNLFRLESTYEIRQDIEDVVWRMK 496
Cdd:pfam16399  396 RPSQQEAANELPLYPTEKTLWDENLVRTEYYDGSRPLALPKLNLQYLTLGDFLLRNFNLFRLESFYEIRQDIEDAVKRLK 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  497 PWQSEYGGAVFGGWARMAQMITSFSIVEVAKPNIGESWPARVRADVTVNL-NVQDHIKHEWEGLRKHDVCLLITVRPNLP 575
Cdd:pfam16399  476 PRLGEDGETRFGGWSRMALPISKPAIVEVAPPNVGESKPSRVRAEVTIDVsRLRDNIRREWESLRPHDVVFLLAVRPPDE 555
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  576 YGTRFDRRQPFVEQTGLVYVRGCEVQGMLDDKGRVIEE------GPDPKPKLrgdaRTFRVWLDPNQYQQDMTsSIQSGT 649
Cdd:pfam16399  556 TYNKLTGSQSFAEQLGLVYVRGAEVIQVLDENGRVLREpqgqtnGPEPRPRQ----RRLRVRLDANQYKADMD-RAAEGK 630
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  650 EDPYETFNIIMRRKPKENNFKAVLETIRNLMNTECVVPDWLHDIILGYGDPGSAHYSKMPNQISTLDFNDTFLSLDHLHL 729
Cdd:pfam16399  631 PDVYETFNVLVRRKPRENNFKAVLETIRDLMNSDCVVPDWLHDVFLGYGDPAAAHYKNLPNRLKTVDFRDTFLDWQHLIE 710
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  730 CFPGYTIKVTEENPDLQVFPFRITFPISNKAD----KVKKRKADDEVEDKEEDMTLIVEPYVTLNRGPYPYNQPKRNTIQ 805
Cdd:pfam16399  711 SFPGKTIEPSDDVSGSFGPPYVLEFPDSPPEPapakPSKKRRRDQEPAPQAEPETIRVSTYKPPNRGPYPVDAPKLNSVR 790

                   .
gi 1811574662  806 F 806
Cdd:pfam16399  791 F 791
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
801-1156 3.02e-127

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: 392.95  E-value: 3.02e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  801 RNTIQFTPTQIEAIRAGMQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPEQRTLIVTHSNQALNQLFEKIMALDIDERHL 880
Cdd:cd17935      1 QNTVKFTPTQIEAIRSGMQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPNQRTLIVTHSNQALNQLFEKIMALDIDERHL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  881 LRLGHGeeeletekdfsrygrvnyvlarrlellrevgrlqesldvpgdvsytcetaghfylyqvisrweeymskvkpkqg 960
Cdd:cd17935     81 LRLGHG-------------------------------------------------------------------------- 86
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  961 ktvevqavaahfpfhkyfsnapqpvfkgrsyeeemdiaegcyrhikkiftqleefrafellrsgldrskyllvkeAKIIA 1040
Cdd:cd17935     87 ---------------------------------------------------------------------------AKIIA 91
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1041 MTCTHAALKRHDLVELGFKYDNILMEEAAQILEIETFIPLLLQNPEDGYSRLKRWIMIGDHHQLPPVIKNMAFQKYSNME 1120
Cdd:cd17935     92 MTCTHAALKRGELVELGFKYDNILMEEAAQILEIETFIPLLLQNPEDGPNRLKRLIMIGDHHQLPPVIKNMAFQKYSNME 171
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1811574662 1121 QSLFTRFVRLGVPTIDLDAQGRARASLCNLYNWRYK 1156
Cdd:cd17935    172 QSLFTRLVRLGVPTVDLDAQGRARASISSLYNWRYK 207
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
1144-1327 2.35e-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: 170.49  E-value: 2.35e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1144 RASLCNLYNWRYKHLGNLPHVQ-QLPEFQVPNPGLTFDFQLINVEdfnGVGESEPNPYFYQNLAEAEYTVALYMYMRLLG 1222
Cdd:cd18808      2 HPEISEFPSKLFYEGKLKAGVSvAARLNPPPLPGPSKPLVFVDVS---GGEEREESGTSKSNEAEAELVVELVKYLLKSG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1223 YPADRISILTTYNGQKHLIRDVINQRCAGNPFFsqpnKVTTVDRFQGQQNDYIILSLVRTK----AVGHLRDVRRLVVAM 1298
Cdd:cd18808     79 VKPSSIGVITPYRAQVALIRELLRKRGGLLEDV----EVGTVDNFQGREKDVIILSLVRSNesggSIGFLSDPRRLNVAL 154
                          170       180
                   ....*....|....*....|....*....
gi 1811574662 1299 SRARLGLYIFARVALFQNCFELTPVFNQL 1327
Cdd:cd18808    155 TRAKRGLIIVGNPDTLSKDPLWKKLLEYL 183
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
849-1316 5.27e-36

Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 148.35  E-value: 5.27e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  849 PEQRTLIVTHSNQALNQLFEKIMALDIDERHLLRLGHGEEELETEKDFSRYGRVNYVLARRLELLREVGRLQESLDVPGD 928
Cdd:COG1112    355 ALLRLLAALLLALALLLLLALEELLLLALLRLLAEGLALLLLLLLAALLRLARALLLLALLLAAAAAALAALLLLALALL 434
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  929 VSYTCETAGHFYLYQVISRWEEYMSKVKPKQGKTVEVQAVAAHFPFHKYFSNAPQPVFKGRSYEEEMDIAEGCyRHIKKI 1008
Cdd:COG1112    435 AALLALLLLLAAALAALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPEELEKLIAELREAA-RLRRAL 513
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1009 FTQLEEFRAFELLRSgldrskYLLVKEAKIIAMTCthAALKRHDLVELGfKYDNILMEEAAQILEIETFIPLllqnpedg 1088
Cdd:COG1112    514 RRELKKRRELRKLLW------DALLELAPVVGMTP--ASVARLLPLGEG-SFDLVIIDEASQATLAEALGAL-------- 576
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1089 ySRLKRWIMIGDHHQLPPVIK--NMAFQKYSNMEQSLFTRFV-RLGVPTIDLDAQGRARASLCNLYNWR-YK-HLGNLPH 1163
Cdd:COG1112    577 -ARAKRVVLVGDPKQLPPVVFgeEAEEVAEEGLDESLLDRLLaRLPERGVMLREHYRMHPEIIAFSNRLfYDgKLVPLPS 655
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1164 VQQLPeFQVPNPGLTFdfqlINVEdfnGVGESEPNPYFyqNLAEAEYTVALYMYMRLLGYPADRISILTTYNGQKHLIRD 1243
Cdd:COG1112    656 PKARR-LADPDSPLVF----IDVD---GVYERRGGSRT--NPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVALIRE 725
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1244 VINQRCAGNPffsQPNKVTTVDRFQGQQNDYIILSLVRTKAVGHLR-------DVRRLVVAMSRARLGLYIFARVALFQN 1316
Cdd:COG1112    726 LLREALGDGL---EPVFVGTVDRFQGDERDVIIFSLVYSNDEDVPRnfgflngGPRRLNVAVSRARRKLIVVGSRELLDS 802
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
794-1302 7.21e-30

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: 127.62  E-value: 7.21e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  794 YPYNQPKRNTIQFTP-------TQIEAIR-AGMQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPeqRTLIVTHSNQALNQ 865
Cdd:TIGR00376  139 REAPSKASEIHDFQFfdpnlneSQKEAVLfALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGL--RVLVTAPSNIAVDN 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  866 LFEKIMALDIderHLLRLGHGeeeletekdfsrygrvnyvlARRLELLrevgrLQESLDVpgdvsytcetaghfylyqVI 945
Cdd:TIGR00376  217 LLERLALCDQ---KIVRLGHP--------------------ARLLKSN-----KQHSLDY------------------LI 250
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  946 SRWEEYmSKVKPKQGKTVEVqavaahfpfhkyfsnapqpvfkgrsyEEEMDiaegcyRHIKKiFTQLEEFRA-FELLRSG 1024
Cdd:TIGR00376  251 ENHPKY-QIVADIREKIDEL--------------------------IEERN------KKTKP-SPQKRRGLSdIKILRKA 296
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1025 LDRSKYLLVKEAKIIAM---TCTHAALKR---------------------------HDLVELGFKYDNILMEEAAQILEI 1074
Cdd:TIGR00376  297 LKKREARGIESLKIASMaewIETNKSIDRllkllpeseerimneilaesdatnsmaGSEILNGQYFDVAVIDEASQAMEP 376
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1075 ETFIPLLlqnpedgysRLKRWIMIGDHHQLPPVIKNmafQKYSNMEQSLFTRFVRL-GVPTIDLDAQGRARASLC----- 1148
Cdd:TIGR00376  377 SCLIPLL---------KARKLILAGDHKQLPPTILS---HDAEELSLTLFERLIKEyPERSRTLNVQYRMNQKIMefpsr 444
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1149 NLYNWRYKH--------LGNLPHVQQLPEFQVPNPGLTfdFQLINVEDFNGVGESEPNPYFYQNLAEAEYTVALYMYMRL 1220
Cdd:TIGR00376  445 EFYNGKLTAhesvanilLRDLPKVEATESEDDLETGIP--LLFIDTSGCELFELKEADSTSKYNPGEAELVSEIIQALVK 522
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1221 LGYPADRISILTTYNGQKHLIRDVINQRcagnpffsQPN-KVTTVDRFQGQQNDYIILSLVRTK---AVGHLRDVRRLVV 1296
Cdd:TIGR00376  523 MGVPANDIGVITPYDAQVDLLRQLLEHR--------HIDiEVSSVDGFQGREKEVIIISFVRSNrkgEVGFLKDLRRLNV 594

                   ....*.
gi 1811574662 1297 AMSRAR 1302
Cdd:TIGR00376  595 ALTRAR 600
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
1119-1307 1.17e-27

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: 111.49  E-value: 1.17e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1119 MEQSLFTRFVRLG-VPTIDLDAQGRARASLCNLYN-WRYKhlGNL---PHVQQLPEFQVPNPGLTFD-FQLINVEDFNGV 1192
Cdd:pfam13087    1 LDRSLFERLQELGpSAVVMLDTQYRMHPEIMEFPSkLFYG--GKLkdgPSVAERPLPDDFHLPDPLGpLVFIDVDGSEEE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1193 GESEPNPYFyqNLAEAEYTVALYMYMRLLGYPADR-ISILTTYNGQKHLIRDVINQRCAGNPFFsqpnKVTTVDRFQGQQ 1271
Cdd:pfam13087   79 ESDGGTSYS--NEAEAELVVQLVEKLIKSGPEEPSdIGVITPYRAQVRLIRKLLKRKLGGKLEI----EVNTVDGFQGRE 152
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1811574662 1272 NDYIILSLVRT---KAVGHLRDVRRLVVAMSRARLGLYI 1307
Cdd:pfam13087  153 KDVIIFSCVRSnekGGIGFLSDPRRLNVALTRAKRGLII 191
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
809-1111 1.86e-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: 1.86e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  809 TQIEAIRAGM-QPGLTMVVGPPGTGKTDVAVQIISNLY-----HNFPEQRTLIVTHSNQALNQLFEKIMALDID-ERHLL 881
Cdd:pfam13086    1 SQREAIRSALsSSHFTLIQGPPGTGKTTTIVELIRQLLsypatSAAAGPRILVCAPSNAAVDNILERLLRKGQKyGPKIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  882 RLGHGEEELETEKDFSRYGRVN--YVLARRLELLREVGRLQESLdvpgdvsytcetaghfylyqvisrweEYMSKVKPKQ 959
Cdd:pfam13086   81 RIGHPAAISEAVLPVSLDYLVEskLNNEEDAQIVKDISKELEKL--------------------------AKALRAFEKE 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  960 GKTVEVQAVAAHFPfhkyfsnapqpvfkgRSYEEEmdiAEGCYRHIKKIFTQLEEFRAFeLLRSGLDrskyllvkEAKII 1039
Cdd:pfam13086  135 IIVEKLLKSRNKDK---------------SKLEQE---RRKLRSERKELRKELRRREQS-LEREILD--------EAQIV 187
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1811574662 1040 AMTCTHAAlkRHDLVELgFKYDNILMEEAAQILEIETFIPLLLqnpedgysRLKRWIMIGDHHQLPPVIKNM 1111
Cdd:pfam13086  188 CSTLSGAG--SRLLSSL-ANFDVVIIDEAAQALEPSTLIPLLR--------GPKKVVLVGDPKQLPPTVISK 248
DEXDc smart00487
DEAD-like helicases superfamily;
799-919 6.33e-07

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 51.72  E-value: 6.33e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662   799 PKRNTIQFTPTQIEAIRAGMQ-PGLTMVVGPPGTGKTDVAVQIISNLYHNFPEQRTLIVTHSNQALNQLFEKIMAL--DI 875
Cdd:smart00487    2 EKFGFEPLRPYQKEAIEALLSgLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLgpSL 81
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1811574662   876 DERHLLRLGhGEEELETEKDFSR---------YGRVNYVLARRLELLREVGRL 919
Cdd:smart00487   82 GLKVVGLYG-GDSKREQLRKLESgktdilvttPGRLLDLLENDKLSLSNVDLV 133
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
810-870 3.40e-06

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 51.56  E-value: 3.40e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1811574662  810 QIEAIRA-------GMQPGLtmVVGPPGTGKTDVAVQIISNLYHNfpeQRTLIVTHSNQALNQLFEKI 870
Cdd:COG1061     85 QQEALEAllaalerGGGRGL--VVAPTGTGKTVLALALAAELLRG---KRVLVLVPRRELLEQWAEEL 147
 
Name Accession Description Interval E-value
Aquarius_N pfam16399
Intron-binding protein aquarius N-terminus; This family represents the N-terminus of ...
21-806 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: 1198.13  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662   21 INAEYVTQLANKYWAPHAK-NKLPFDPKVMEDVYEKEILKSKFAIRKIMLLEFSQYLENYLWVNYAPKvSSNAYLMSICC 99
Cdd:pfam16399    1 IQEDRIAQLARKHWLKSKKsKKVKVKPEVVKKIYWDELEKEGFSLRSLLLLEFLQYLENYLWPNYTED-ASNAHVLLIVL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  100 IVNEKFRENVPAWEVFKKEPSHFPFFFKCVMEASLADEkacLTLKEQTVLLVFLDHCFNSLEVDLIREQVQQLIALPMWM 179
Cdd:pfam16399   80 MVNEKFREHLPAWELFSDRPDDFSSFFRRVLSLSLDRS---LSTAERTALLSFLIHAFQSLENELVRKECAPLVSISIWH 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  180 CL-LPSRLQQELKKVPKLQKFWNLIKKKCDKMDAESAEQAKKERTFLSALIKKFLGVLMSIPPSGPVSMDKVHYCERFIE 258
Cdd:pfam16399  157 NLsSEGRREQELDKNPQLRKAWRAAQKRYDAADDATKARLRFERSWLYTLLLDFLDVLYDIPEDGEVDDDNVRYCERFLE 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  259 LMIDLEALLPTRRWFNTVLDDSHLVVSCHLSSLTQREkEGHLFCQLLDMLKFYTGFEINDQTGNALTEKEMTTLHYDKIL 338
Cdd:pfam16399  237 LLIDLESQLPTRRYVNTLLQDLHLLPACRLSPLYNDE-EGGLFRQLLDLLKHYTYFEIDDQTGEQLSDQEVYDAHYARLA 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  339 SLQRAAFAHFPE-LQDFALSNVAAVDTRESLMKHFGHLSPNTLHQVASYLCL-LPELPEGQDTTYEKEVLLELLVSRHER 416
Cdd:pfam16399  316 RLQRTAFKHFKEkLTILALSNYGSIDKREELEKHLSALSDEELRELCSLLGLrTVPYPESDNIVYDRKFLLEVLLSRFEK 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  417 RISQIEQLNQMPLYPTEKIIWDENIVPTEYYSGEGCLALPKLNLQFLTLHDYLLRNFNLFRLESTYEIRQDIEDVVWRMK 496
Cdd:pfam16399  396 RPSQQEAANELPLYPTEKTLWDENLVRTEYYDGSRPLALPKLNLQYLTLGDFLLRNFNLFRLESFYEIRQDIEDAVKRLK 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  497 PWQSEYGGAVFGGWARMAQMITSFSIVEVAKPNIGESWPARVRADVTVNL-NVQDHIKHEWEGLRKHDVCLLITVRPNLP 575
Cdd:pfam16399  476 PRLGEDGETRFGGWSRMALPISKPAIVEVAPPNVGESKPSRVRAEVTIDVsRLRDNIRREWESLRPHDVVFLLAVRPPDE 555
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  576 YGTRFDRRQPFVEQTGLVYVRGCEVQGMLDDKGRVIEE------GPDPKPKLrgdaRTFRVWLDPNQYQQDMTsSIQSGT 649
Cdd:pfam16399  556 TYNKLTGSQSFAEQLGLVYVRGAEVIQVLDENGRVLREpqgqtnGPEPRPRQ----RRLRVRLDANQYKADMD-RAAEGK 630
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  650 EDPYETFNIIMRRKPKENNFKAVLETIRNLMNTECVVPDWLHDIILGYGDPGSAHYSKMPNQISTLDFNDTFLSLDHLHL 729
Cdd:pfam16399  631 PDVYETFNVLVRRKPRENNFKAVLETIRDLMNSDCVVPDWLHDVFLGYGDPAAAHYKNLPNRLKTVDFRDTFLDWQHLIE 710
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  730 CFPGYTIKVTEENPDLQVFPFRITFPISNKAD----KVKKRKADDEVEDKEEDMTLIVEPYVTLNRGPYPYNQPKRNTIQ 805
Cdd:pfam16399  711 SFPGKTIEPSDDVSGSFGPPYVLEFPDSPPEPapakPSKKRRRDQEPAPQAEPETIRVSTYKPPNRGPYPVDAPKLNSVR 790

                   .
gi 1811574662  806 F 806
Cdd:pfam16399  791 F 791
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
801-1156 3.02e-127

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: 392.95  E-value: 3.02e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  801 RNTIQFTPTQIEAIRAGMQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPEQRTLIVTHSNQALNQLFEKIMALDIDERHL 880
Cdd:cd17935      1 QNTVKFTPTQIEAIRSGMQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPNQRTLIVTHSNQALNQLFEKIMALDIDERHL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  881 LRLGHGeeeletekdfsrygrvnyvlarrlellrevgrlqesldvpgdvsytcetaghfylyqvisrweeymskvkpkqg 960
Cdd:cd17935     81 LRLGHG-------------------------------------------------------------------------- 86
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  961 ktvevqavaahfpfhkyfsnapqpvfkgrsyeeemdiaegcyrhikkiftqleefrafellrsgldrskyllvkeAKIIA 1040
Cdd:cd17935     87 ---------------------------------------------------------------------------AKIIA 91
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1041 MTCTHAALKRHDLVELGFKYDNILMEEAAQILEIETFIPLLLQNPEDGYSRLKRWIMIGDHHQLPPVIKNMAFQKYSNME 1120
Cdd:cd17935     92 MTCTHAALKRGELVELGFKYDNILMEEAAQILEIETFIPLLLQNPEDGPNRLKRLIMIGDHHQLPPVIKNMAFQKYSNME 171
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1811574662 1121 QSLFTRFVRLGVPTIDLDAQGRARASLCNLYNWRYK 1156
Cdd:cd17935    172 QSLFTRLVRLGVPTVDLDAQGRARASISSLYNWRYK 207
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
1144-1327 2.35e-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: 170.49  E-value: 2.35e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1144 RASLCNLYNWRYKHLGNLPHVQ-QLPEFQVPNPGLTFDFQLINVEdfnGVGESEPNPYFYQNLAEAEYTVALYMYMRLLG 1222
Cdd:cd18808      2 HPEISEFPSKLFYEGKLKAGVSvAARLNPPPLPGPSKPLVFVDVS---GGEEREESGTSKSNEAEAELVVELVKYLLKSG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1223 YPADRISILTTYNGQKHLIRDVINQRCAGNPFFsqpnKVTTVDRFQGQQNDYIILSLVRTK----AVGHLRDVRRLVVAM 1298
Cdd:cd18808     79 VKPSSIGVITPYRAQVALIRELLRKRGGLLEDV----EVGTVDNFQGREKDVIILSLVRSNesggSIGFLSDPRRLNVAL 154
                          170       180
                   ....*....|....*....|....*....
gi 1811574662 1299 SRARLGLYIFARVALFQNCFELTPVFNQL 1327
Cdd:cd18808    155 TRAKRGLIIVGNPDTLSKDPLWKKLLEYL 183
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
849-1316 5.27e-36

Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 148.35  E-value: 5.27e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  849 PEQRTLIVTHSNQALNQLFEKIMALDIDERHLLRLGHGEEELETEKDFSRYGRVNYVLARRLELLREVGRLQESLDVPGD 928
Cdd:COG1112    355 ALLRLLAALLLALALLLLLALEELLLLALLRLLAEGLALLLLLLLAALLRLARALLLLALLLAAAAAALAALLLLALALL 434
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  929 VSYTCETAGHFYLYQVISRWEEYMSKVKPKQGKTVEVQAVAAHFPFHKYFSNAPQPVFKGRSYEEEMDIAEGCyRHIKKI 1008
Cdd:COG1112    435 AALLALLLLLAAALAALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPEELEKLIAELREAA-RLRRAL 513
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1009 FTQLEEFRAFELLRSgldrskYLLVKEAKIIAMTCthAALKRHDLVELGfKYDNILMEEAAQILEIETFIPLllqnpedg 1088
Cdd:COG1112    514 RRELKKRRELRKLLW------DALLELAPVVGMTP--ASVARLLPLGEG-SFDLVIIDEASQATLAEALGAL-------- 576
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1089 ySRLKRWIMIGDHHQLPPVIK--NMAFQKYSNMEQSLFTRFV-RLGVPTIDLDAQGRARASLCNLYNWR-YK-HLGNLPH 1163
Cdd:COG1112    577 -ARAKRVVLVGDPKQLPPVVFgeEAEEVAEEGLDESLLDRLLaRLPERGVMLREHYRMHPEIIAFSNRLfYDgKLVPLPS 655
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1164 VQQLPeFQVPNPGLTFdfqlINVEdfnGVGESEPNPYFyqNLAEAEYTVALYMYMRLLGYPADRISILTTYNGQKHLIRD 1243
Cdd:COG1112    656 PKARR-LADPDSPLVF----IDVD---GVYERRGGSRT--NPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVALIRE 725
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1244 VINQRCAGNPffsQPNKVTTVDRFQGQQNDYIILSLVRTKAVGHLR-------DVRRLVVAMSRARLGLYIFARVALFQN 1316
Cdd:COG1112    726 LLREALGDGL---EPVFVGTVDRFQGDERDVIIFSLVYSNDEDVPRnfgflngGPRRLNVAVSRARRKLIVVGSRELLDS 802
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
794-1302 7.21e-30

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: 127.62  E-value: 7.21e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  794 YPYNQPKRNTIQFTP-------TQIEAIR-AGMQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPeqRTLIVTHSNQALNQ 865
Cdd:TIGR00376  139 REAPSKASEIHDFQFfdpnlneSQKEAVLfALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGL--RVLVTAPSNIAVDN 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  866 LFEKIMALDIderHLLRLGHGeeeletekdfsrygrvnyvlARRLELLrevgrLQESLDVpgdvsytcetaghfylyqVI 945
Cdd:TIGR00376  217 LLERLALCDQ---KIVRLGHP--------------------ARLLKSN-----KQHSLDY------------------LI 250
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  946 SRWEEYmSKVKPKQGKTVEVqavaahfpfhkyfsnapqpvfkgrsyEEEMDiaegcyRHIKKiFTQLEEFRA-FELLRSG 1024
Cdd:TIGR00376  251 ENHPKY-QIVADIREKIDEL--------------------------IEERN------KKTKP-SPQKRRGLSdIKILRKA 296
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1025 LDRSKYLLVKEAKIIAM---TCTHAALKR---------------------------HDLVELGFKYDNILMEEAAQILEI 1074
Cdd:TIGR00376  297 LKKREARGIESLKIASMaewIETNKSIDRllkllpeseerimneilaesdatnsmaGSEILNGQYFDVAVIDEASQAMEP 376
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1075 ETFIPLLlqnpedgysRLKRWIMIGDHHQLPPVIKNmafQKYSNMEQSLFTRFVRL-GVPTIDLDAQGRARASLC----- 1148
Cdd:TIGR00376  377 SCLIPLL---------KARKLILAGDHKQLPPTILS---HDAEELSLTLFERLIKEyPERSRTLNVQYRMNQKIMefpsr 444
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1149 NLYNWRYKH--------LGNLPHVQQLPEFQVPNPGLTfdFQLINVEDFNGVGESEPNPYFYQNLAEAEYTVALYMYMRL 1220
Cdd:TIGR00376  445 EFYNGKLTAhesvanilLRDLPKVEATESEDDLETGIP--LLFIDTSGCELFELKEADSTSKYNPGEAELVSEIIQALVK 522
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1221 LGYPADRISILTTYNGQKHLIRDVINQRcagnpffsQPN-KVTTVDRFQGQQNDYIILSLVRTK---AVGHLRDVRRLVV 1296
Cdd:TIGR00376  523 MGVPANDIGVITPYDAQVDLLRQLLEHR--------HIDiEVSSVDGFQGREKEVIIISFVRSNrkgEVGFLKDLRRLNV 594

                   ....*.
gi 1811574662 1297 AMSRAR 1302
Cdd:TIGR00376  595 ALTRAR 600
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
1119-1307 1.17e-27

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: 111.49  E-value: 1.17e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1119 MEQSLFTRFVRLG-VPTIDLDAQGRARASLCNLYN-WRYKhlGNL---PHVQQLPEFQVPNPGLTFD-FQLINVEDFNGV 1192
Cdd:pfam13087    1 LDRSLFERLQELGpSAVVMLDTQYRMHPEIMEFPSkLFYG--GKLkdgPSVAERPLPDDFHLPDPLGpLVFIDVDGSEEE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1193 GESEPNPYFyqNLAEAEYTVALYMYMRLLGYPADR-ISILTTYNGQKHLIRDVINQRCAGNPFFsqpnKVTTVDRFQGQQ 1271
Cdd:pfam13087   79 ESDGGTSYS--NEAEAELVVQLVEKLIKSGPEEPSdIGVITPYRAQVRLIRKLLKRKLGGKLEI----EVNTVDGFQGRE 152
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1811574662 1272 NDYIILSLVRT---KAVGHLRDVRRLVVAMSRARLGLYI 1307
Cdd:pfam13087  153 KDVIIFSCVRSnekGGIGFLSDPRRLNVALTRAKRGLII 191
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
809-1111 1.86e-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: 1.86e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  809 TQIEAIRAGM-QPGLTMVVGPPGTGKTDVAVQIISNLY-----HNFPEQRTLIVTHSNQALNQLFEKIMALDID-ERHLL 881
Cdd:pfam13086    1 SQREAIRSALsSSHFTLIQGPPGTGKTTTIVELIRQLLsypatSAAAGPRILVCAPSNAAVDNILERLLRKGQKyGPKIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  882 RLGHGEEELETEKDFSRYGRVN--YVLARRLELLREVGRLQESLdvpgdvsytcetaghfylyqvisrweEYMSKVKPKQ 959
Cdd:pfam13086   81 RIGHPAAISEAVLPVSLDYLVEskLNNEEDAQIVKDISKELEKL--------------------------AKALRAFEKE 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  960 GKTVEVQAVAAHFPfhkyfsnapqpvfkgRSYEEEmdiAEGCYRHIKKIFTQLEEFRAFeLLRSGLDrskyllvkEAKII 1039
Cdd:pfam13086  135 IIVEKLLKSRNKDK---------------SKLEQE---RRKLRSERKELRKELRRREQS-LEREILD--------EAQIV 187
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1811574662 1040 AMTCTHAAlkRHDLVELgFKYDNILMEEAAQILEIETFIPLLLqnpedgysRLKRWIMIGDHHQLPPVIKNM 1111
Cdd:pfam13086  188 CSTLSGAG--SRLLSSL-ANFDVVIIDEAAQALEPSTLIPLLR--------GPKKVVLVGDPKQLPPTVISK 248
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
1038-1141 4.35e-23

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: 96.02  E-value: 4.35e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1038 IIAMTCTHAALKRhdlvelgfkYDNILMEEAAQILEIETFIPlllqnpEDGYSRLKRWIMIGDHHQLPPVIKNMAFQKYS 1117
Cdd:cd17914     34 ILLVTPTNKAAAQ---------LDNILVDEAAQILEPETSRL------IDLALDQGRVILVGDHDQLGPVWRGAVLAKIC 98
                           90       100
                   ....*....|....*....|....
gi 1811574662 1118 NmEQSLFTRFVRLGVPTIDLDAQG 1141
Cdd:cd17914     99 N-EQSLFTRLVRLGVSLIRLQVQY 121
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
808-1142 1.08e-22

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: 98.47  E-value: 1.08e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  808 PTQIEAIRAGMQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPEQrTLIVTHSNQALNQLFEKImaldiDERHLlrlghge 887
Cdd:cd18039      4 HSQVDAVKTALQRPLSLIQGPPGTGKTVTSATIVYHLVKQGNGP-VLVCAPSNVAVDQLTEKI-----HQTGL------- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  888 eeletekdfsrygRVNYVLARRlellREvgrlqeslDVPGDVSYTCEtagHFYLYQVISrweeyMSKVKPKQGKTVEVqa 967
Cdd:cd18039     71 -------------KVVRLCAKS----RE--------AVESPVSFLAL---HNQVRNLDS-----AEKLELLKLLKLET-- 115
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  968 vaahfpfhkyfsnapqpvfkgrsyeEEMDIAEgcYRHIKKIFTQLEEfrafELLRsgldrskyllvkEAKIIAMTCTHAA 1047
Cdd:cd18039    116 -------------------------GELSSAD--EKRYRKLKRKAER----ELLR------------NADVICCTCVGAG 152
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1048 LKRhdLVelGFKYDNILMEEAAQILEIETFIPLLLQnpedgysrLKRWIMIGDHHQLPPVIKNMAFQKYSnMEQSLFTRF 1127
Cdd:cd18039    153 DPR--LS--KMKFRTVLIDEATQATEPECLIPLVHG--------AKQVILVGDHCQLGPVVMCKKAAKAG-LSQSLFERL 219
                          330
                   ....*....|....*
gi 1811574662 1128 VRLGVPTIDLDAQGR 1142
Cdd:cd18039    220 VQLGIRPIRLQVQYR 234
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
1015-1142 7.50e-20

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: 89.97  E-value: 7.50e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1015 FRAFELLRSGLDRSKYLLVKEAKIIAmtCTHAALKRHDLVELGFKYDNILMEEAAQILEIETFIPLLLqnpedgysRLKR 1094
Cdd:cd18042    102 SYKPNVVRVGRQELRASILNEADIVC--TTLSSSGSDLLESLPRGFDTVIIDEAAQAVELSTLIPLRL--------GCKR 171
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1811574662 1095 WIMIGDHHQLPPVIKNMAFQKYsNMEQSLFTRFVRLGVPTIDLDAQGR 1142
Cdd:cd18042    172 LILVGDPKQLPATVFSKVAQKL-GYDRSLFERLQLAGYPVLMLTTQYR 218
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
810-1154 3.03e-17

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: 82.67  E-value: 3.03e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  810 QIEAIRA----GMQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPEQRTLIVTHSNQALNQLfekimaldiderhLLRLgh 885
Cdd:cd18038      6 QKLAVRNivtgTSRPPPYIIFGPPGTGKTVTLVEAILQVLRQPPEARILVCAPSNSAADLL-------------AERL-- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  886 geeeletekdfsrygrVNYVLARRlELLRevgrlqesldvpgdvsytcetaghfyLYQVISRWEEYMSKVKPkqgktvev 965
Cdd:cd18038     71 ----------------LNALVTKR-EILR--------------------------LNAPSRDRASVPPELLP-------- 99
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  966 qavaahfpfhkYFSNapqpvfkgrsyeeemdIAEGCYRHIkkiftQLEEfrafellrsgldrskyllVKEAKIIAMTCTH 1045
Cdd:cd18038    100 -----------YCNS----------------KAEGTFRLP-----SLEE------------------LKKYRIVVCTLMT 129
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1046 AALkrhdLVELGFK---YDNILMEEAAQILEIETFIPLLLQNPEDGysrlkRWIMIGDHHQLPPVIKNMAFQKYsNMEQS 1122
Cdd:cd18038    130 AGR----LVQAGVPnghFTHIFIDEAGQATEPEALIPLSELASKNT-----QIVLAGDPKQLGPVVRSPLARKY-GLGKS 199
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1811574662 1123 LFTRFVRLGVPTIDLDAQGRARASLCNlyNWR 1154
Cdd:cd18038    200 LLERLMERPLYYKDGEYNPSYITKLLK--NYR 229
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
808-1140 1.73e-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: 76.04  E-value: 1.73e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  808 PTQIEAIRAGMQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPEQRT---LIVTHSNQALNQLFEKImaLDIDERHLLRLG 884
Cdd:cd17936      4 PSQLEALKHALTSELALIQGPPGTGKTFLGVKLVRALLQNQDLSITgpiLVVCYTNHALDQFLEGL--LDFGPTKIVRLG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  885 hgeeeletekdfsrygrvnyvlarrlellrevgrlqesldvpgdvsytcetaghfylyqvisrweeymskvkpkqgktve 964
Cdd:cd17936        --------------------------------------------------------------------------------
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  965 vqavaahfpfhkyfsnapqpvfkgrsyeeemdiaegcyrhikkiftqleefrafellrsgldrskyllvkeAKIIAMTCT 1044
Cdd:cd17936     82 -----------------------------------------------------------------------ARVIGMTTT 90
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1045 HAALKRHDLVELGFKYdnILMEEAAQILE--IETFIPlllqnpedgySRLKRWIMIGDHHQLPPVIKNMAFQ--KYsNME 1120
Cdd:cd17936     91 GAAKYRELLQALGPKV--VIVEEAAEVLEahILAALT----------PSTEHLILIGDHKQLRPKVNVYELTakKY-NLD 157
                          330       340
                   ....*....|....*....|
gi 1811574662 1121 QSLFTRFVRLGVPTIDLDAQ 1140
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 ...
808-1127 9.62e-13

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: 70.25  E-value: 9.62e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  808 PTQIEAIRAGMQPGLTMVVGPPGTGKTDVAVQIIsnlYHnFPEQrtlivthsNQALNQLFEKIMALDiderHLLRLGHGE 887
Cdd:cd18040      4 PSQNHAVRTALTKPFTLIQGPPGTGKTVTGVHIA---YW-FAKQ--------NREIQSVSGEGDGGP----CVLYCGPSN 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  888 EELETekdfsrygrVNYVLARRLEL--LREVGRLQESLDVPgdvsytcetaghfylyqvISRWEEYMSKVKPKQGK-TVE 964
Cdd:cd18040     68 KSVDV---------VAELLLKVPGLkiLRVYSEQIETTEYP------------------IPNEPRHPNKKSERESKpNSE 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  965 VQAVAAHFPFHKyfsnAPQPvfkgrsYEEEMdiaegcyrhikKIFTQLEEFRAFELLRSGLDRSKYLLVKEAK------- 1037
Cdd:cd18040    121 LSSITLHHRIRQ----PSNP------HSQQI-----------KAFEARFERTQEKITEEDIKTYKILIWEARFeeletvd 179
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1038 IIAMTCTHAALKRhdlVELGFKYDNILMEEAAQILEIETFIPLLlqnpedGYSRLKRWIMIGDHHQLPPVIKNMAFQKYS 1117
Cdd:cd18040    180 VILCTCSEAASQK---MRTHANVKQCIVDECGMCTEPESLIPIV------SAPRAEQVVLIGDHKQLRPVVQNKEAQKLG 250
                          330
                   ....*....|
gi 1811574662 1118 nMEQSLFTRF 1127
Cdd:cd18040    251 -LGRSLFERY 259
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
1036-1142 1.30e-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: 1.30e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1036 AKIIAMTCTHAALKRHDLVelgfkydniLMEEAAQILEIETFIPLLlqnpedgysRLKRWIMIGDHHQLPPVIKNMAFQK 1115
Cdd:cd17934     30 KRVLVTAQSNVAVDNVDVV---------IIDEASQITEPELLIALI---------RAKKVVLVGDPKQLPPVVQEDHAAL 91
                           90       100       110
                   ....*....|....*....|....*....|
gi 1811574662 1116 Y---SNMEQSLFTRFVRLGVPTIDLDAQGR 1142
Cdd:cd17934     92 LglsFILSLLLLFRLLLPGSPKVMLDTQYR 121
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
1227-1307 5.26e-11

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: 60.14  E-value: 5.26e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1227 RISILTTYNGQKHLIRDVInQRCAGNPFFSQPNKVTTVDRFQGQQNDYIILSLVRTkavgHLRDVRRLVVAMSRARLGLY 1306
Cdd:cd18786     12 KGVVLTPYHRDRAYLNQYL-QGLSLDEFDLQLVGAITIDSSQGLTFDVVTLYLPTA----NSLTPRRLYVALTRARKRLV 86

                   .
gi 1811574662 1307 I 1307
Cdd:cd18786     87 I 87
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
808-1135 3.09e-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: 3.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  808 PTQIEAIR-AGMQPGLTMVVGPPGTGKTDVAVQIISNLYHnfPEQRTLIVTHSNQALNQLFEKIMALDIDerhLLRLGHG 886
Cdd:cd18044      4 DSQKEAVKfALSQKDVALIHGPPGTGKTTTVVEIILQAVK--RGEKVLACAPSNIAVDNLVERLVALKVK---VVRIGHP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  887 eeeletekdfsrygrvnyvlARRLELLrevgrLQESLDVpgdvsytcetaghfylyqvisrweeymskvkpkqgktvevq 966
Cdd:cd18044     79 --------------------ARLLESV-----LDHSLDA----------------------------------------- 92
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  967 avaahfpfhkyfsnapqpvfkgrsyeeemdiaegcyrhikkiftqleefrafellrsgldrskyllVKEAKIIAMTCTHA 1046
Cdd:cd18044     93 ------------------------------------------------------------------LVAAQVVLATNTGA 106
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1047 AlkrHDLVELGFKYDNILMEEAAQILEIETFIPLLlqnpedgysRLKRWIMIGDHHQLPPVIKNMAFQKYsNMEQSLFTR 1126
Cdd:cd18044    107 G---SRQLLPNELFDVVVIDEAAQALEASCWIPLL---------KARRCILAGDHKQLPPTILSDKAARG-GLGVTLFER 173

                   ....*....
gi 1811574662 1127 FVRLGVPTI 1135
Cdd:cd18044    174 LVNLYGESV 182
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
1005-1127 5.32e-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: 60.71  E-value: 5.32e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1005 IKKIFTQLEEFRAFELLRSGLDRSKY-LLVKEAKIIAMTC---THAALKRHdlvelgfKYDNILMEEAAQILEIETFIPL 1080
Cdd:cd18041     78 LKKIHPDVQEFTLEAILKSCKSVEELeSKYESVSVVATTClgiNHPIFRRR-------TFDYCIVDEASQITLPICLGPL 150
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1811574662 1081 LLQnpedgysrlKRWIMIGDHHQLPPVIKNMAFQKySNMEQSLFTRF 1127
Cdd:cd18041    151 RLA---------KKFVLVGDHYQLPPLVKSREARE-LGMDESLFKRL 187
DEXDc smart00487
DEAD-like helicases superfamily;
799-919 6.33e-07

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 51.72  E-value: 6.33e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662   799 PKRNTIQFTPTQIEAIRAGMQ-PGLTMVVGPPGTGKTDVAVQIISNLYHNFPEQRTLIVTHSNQALNQLFEKIMAL--DI 875
Cdd:smart00487    2 EKFGFEPLRPYQKEAIEALLSgLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLgpSL 81
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1811574662   876 DERHLLRLGhGEEELETEKDFSR---------YGRVNYVLARRLELLREVGRL 919
Cdd:smart00487   82 GLKVVGLYG-GDSKREQLRKLESgktdilvttPGRLLDLLENDKLSLSNVDLV 133
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
808-899 7.33e-07

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: 50.00  E-value: 7.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  808 PTQIEAIRAGMQ-----PGltMVVGPPGTGKTDVAVQIISNLYhnfpEQRTLIVTHSNQALNQLFEKIMALDIDeRHLLR 882
Cdd:cd17926      3 PYQEEALEAWLAhknnrRG--ILVLPTGSGKTLTALALIAYLK----ELRTLIVVPTDALLDQWKERFEDFLGD-SSIGL 75
                           90
                   ....*....|....*....
gi 1811574662  883 LGHGEEELETEK--DFSRY 899
Cdd:cd17926     76 IGGGKKKDFDDAnvVVATY 94
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
810-870 3.40e-06

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 51.56  E-value: 3.40e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1811574662  810 QIEAIRA-------GMQPGLtmVVGPPGTGKTDVAVQIISNLYHNfpeQRTLIVTHSNQALNQLFEKI 870
Cdd:COG1061     85 QQEALEAllaalerGGGRGL--VVAPTGTGKTVLALALAAELLRG---KRVLVLVPRRELLEQWAEEL 147
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
808-887 4.19e-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: 47.58  E-value: 4.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  808 PTQIEAIRAGMQPGLTMVVGPPGTGKTDVAVQIISNLYHNfpEQRTLIVTHSNQALNQLFEKIMALDIDE-RHLLRLGHG 886
Cdd:cd18043      2 SSQEAAIISARNGKNVVIQGPPGTGKSQTIANIIANALAR--GKRVLFVSEKKAALDVVRFPCWIMSPLSvSQYLPLNRN 79

                   .
gi 1811574662  887 E 887
Cdd:cd18043     80 L 80
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
822-866 8.78e-06

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: 46.46  E-value: 8.78e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1811574662  822 LTMVVGPPGTGKTDVAVQIISNLYHNFPEQRTLIVTHSNQALNQL 866
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 3.85e-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: 46.71  E-value: 3.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1033 VKEAKIIAMT-CTHAALKRHDLVELGFKYdnILMEEAAQILEIETFIPLLLQNPEdgysrlKRWIMIGDHHQLPPVIKNm 1111
Cdd:cd18077    121 VMRHRVVVVTlSTSQYLCQLDLEPGFFTH--ILLDEAAQAMECEAIMPLALATKS------TRIVLAGDHMQLSPEVYS- 191
                           90
                   ....*....|....*
gi 1811574662 1112 AFQKYSNMEQSLFTR 1126
Cdd:cd18077    192 EFARERNLHISLLER 206
DEXXQc_HELZ2-N cd18076
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
1026-1126 1.99e-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: 44.50  E-value: 1.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662 1026 DRSKYLLVKEAKI----IAMTCThaALKRHDLVELGFkYDNILMEEAAQILEIETFIPLLLQNPEdgysrlKRWIMIGDH 1101
Cdd:cd18076    112 DRQCFRLPTRDELdfhnIVITTT--AMAFNLHVLSGF-FTHIFIDEAAQMLECEALIPLSYAGPK------TRVVLAGDH 182
                           90       100
                   ....*....|....*....|....*
gi 1811574662 1102 HQLPPviKNMAFQKYSNMEQSLFTR 1126
Cdd:cd18076    183 MQMTP--KLFSVADYNRANHTLLNR 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 2.01e-04

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: 40.25  E-value: 2.01e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1811574662 1261 VTTVDRFQGQQNDYIILSLVRTKAVGHLRDVRRLV-VAMSRARLGLYI 1307
Cdd:pfam13538    4 ALTVHKAQGSEFPAVFLVDPDLTAHYHSMLRRRLLyTAVTRARKKLVL 51
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
827-940 2.13e-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: 44.28  E-value: 2.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  827 GPPGTGKTDVAVQIISNLYHNFPEQRTLIVTHSNQALNQLFEKIMaldidERHLLRLGhgeeeletekDFSRYGRVNYVL 906
Cdd:cd18078     27 GPPGTGKTVTIIEAILQVVYNLPRSRILVCAPSNSAADLVTSRLH-----ESKVLKPG----------DMVRLNAVNRFE 91
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1811574662  907 ARRLELLREVGRLQESLDVPGD---VSYTCETAGHFY 940
Cdd:cd18078     92 STVIDARKLYCRLGEDLSKASRhriVISTCSTAGLLY 128
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
810-868 3.67e-04

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: 42.55  E-value: 3.67e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1811574662  810 QIEAIRA---GMQPGLT--MVVGPPGTGKTDVAVQIISNLYHNFPEQRTLIVTHSN----QALNQLFE 868
Cdd:cd18032      5 QQEAIEAleeAREKGQRraLLVMATGTGKTYTAAFLIKRLLEANRKKRILFLAHREelleQAERSFKE 72
DEXQc_UvrD cd17932
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch ...
807-870 8.87e-04

DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. UvrD 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: 350690 [Multi-domain]  Cd Length: 189  Bit Score: 42.12  E-value: 8.87e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1811574662  807 TPTQIEAIRAGMQPGLtmVVGPPGTGKTDVAVQIISNL--YHNFPEQRTLIVTHSNQALNQLFEKI 870
Cdd:cd17932      1 NPEQREAVTHPDGPLL--VLAGAGSGKTRVLTHRIAYLilEGGVPPERILAVTFTNKAAKEMRERL 64
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
807-921 7.92e-03

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 38.76  E-value: 7.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811574662  807 TPTQIEAIRAGMQPGLTMVVGPPGTGKTDVAVQ-IISNLYHNFPEQRTLIVTH----SNQALNQlFEKIMALDIDERHLL 881
Cdd:pfam00270    1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLpALEALDKLDNGPQALVLAPtrelAEQIYEE-LKKLGKGLGLKVASL 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1811574662  882 RLGHgeeelETEKDFSRYGRVNYVLA---RRLELLREVGRLQE 921
Cdd:pfam00270   80 LGGD-----SRKEQLEKLKGPDILVGtpgRLLDLLQERKLLKN 117
 
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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