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Conserved domains on  [gi|530377937|ref|XP_005263172|]
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5'-3' DNA helicase ZGRF1 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
1686-2057 1.03e-68

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


:

Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 249.66  E-value: 1.03e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1686 ARPWKLLISSSTNVAVDRVLLGLLSLGFENFIRVGSVRKIAKPILPYSLHAGSENESEQLKELHALMKEDLTPTERVY-- 1763
Cdd:COG1112   437 LLALLLLLAAALAALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPEELEKLIAELREAARLRRALRre 516
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1764 VRKSIEQHKLGTNRtLLKQVRVVGVTCAACP-FPCMNDLKFPVVVLDECSQITEPASLLPIARfeCEKLILVGDPKQLPP 1842
Cdd:COG1112   517 LKKRRELRKLLWDA-LLELAPVVGMTPASVArLLPLGEGSFDLVIIDEASQATLAEALGALAR--AKRVVLVGDPKQLPP 593
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1843 TIQGSDAA--HENGLEQTLFDRLC-LMGHKPILLRTQYRCHPAISAIANDLFYKGALMNGVTEIERSPLLEWLPtLCFYN 1919
Cdd:COG1112   594 VVFGEEAEevAEEGLDESLLDRLLaRLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRLADPDSP-LVFID 672
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1920 VKGLEQiERDNSFHNVAEATFTLKLIQSLIASGIAGSMIGVITLYKSQMYKLCHLLSAVDFHHPDikTVQVSTVDAFQGA 1999
Cdd:COG1112   673 VDGVYE-RRGGSRTNPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVALIRELLREALGDGLE--PVFVGTVDRFQGD 749
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530377937 2000 EKEIIILSCVRT------RQVGFI-DSEKRMNVALTRGKRHLLIVGNLACL---RKNQLWGRVIQHCE 2057
Cdd:COG1112   750 ERDVIIFSLVYSndedvpRNFGFLnGGPRRLNVAVSRARRKLIVVGSRELLdsdPSTPALKRLLEYLE 817
DUF2439 pfam10382
Protein of unknown function (DUF2439); This domain can be found in proteins that have been ...
4-74 6.53e-23

Protein of unknown function (DUF2439); This domain can be found in proteins that have been implicated in telomere maintenance in Saccharomyces cerevisiae and in meiotic chromosome segregation in Schizosaccharomyces pombe. It can also be found in Mte1 (Mph1-associated telomere maintenance protein 1), human zinc finger protein ZGRF1 (C4ORF21) and fission yeast Dbl2. Mte1 is a D-loop-binding protein that interacts and stimulates the helicase and fork regression activities of Mph1 while inhibiting the ability of Mph1 to dissociate recombination intermediates. Mph1 and Mte1 interdependently colocalize at DNA damage-induced foci and dysfunctional telomeres. Mte1 is indicated to play a role in regulation of crossover recombination, response to replication stress, and telomere maintenance. The fission yeast, Dbl2 is needed for cellular resistance to the topoisomerase I poison camptothecin, forms DNA damage-induced foci, and is needed for the optimal recruitment of Fml1 to DNA damage, while the human ZGRF1 protein has been linked to DNA cross-link repair and mutations of it have been found in a variety of human tumors. ZGRF1 is a 5'-to-3'helicase that interacts with RAD51 and stimulates homologous recombination and, thus, promotes the repair of replication-blocking DNA lesions. Having said that, there is no evidence to suggest that this domain is implicated in DNA damage resistance or for nuclear focus formation.


:

Pssm-ID: 463065  Cd Length: 74  Bit Score: 94.11  E-value: 6.53e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530377937     4 QEFIVLYTHQKMKKSKVWQDGILKITHLGNKAILYDDKGACLESLFLK-CLEVKPGDDLESDRYLITVEEVK 74
Cdd:pfam10382    2 HEYRCLYTHDVRKKHKRWHDGKLKYHTFNKRVMLYDEDGNLIGSDFWTsSEDLEEGEELELDRYLVQIEELL 73
zf-GRF pfam06839
GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding ...
1347-1391 2.42e-12

GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding proteins. It seems likely that this domain is involved in nucleic acid binding. It is named GRF after three conserved residues in the centre of the alignment of the domain. This zinc finger may be related to pfam01396.


:

Pssm-ID: 462017  Cd Length: 45  Bit Score: 63.19  E-value: 2.42e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 530377937  1347 PSCHHSQPAKLVMVKKEGPNKGRLFYTCDGPKADRCKFFKWLEDV 1391
Cdd:pfam06839    1 PLCPCGQRAVLLTVRKTGPNPGRQFYKCPVGREKQCGFFQWADEV 45
 
Name Accession Description Interval E-value
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
1686-2057 1.03e-68

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 249.66  E-value: 1.03e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1686 ARPWKLLISSSTNVAVDRVLLGLLSLGFENFIRVGSVRKIAKPILPYSLHAGSENESEQLKELHALMKEDLTPTERVY-- 1763
Cdd:COG1112   437 LLALLLLLAAALAALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPEELEKLIAELREAARLRRALRre 516
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1764 VRKSIEQHKLGTNRtLLKQVRVVGVTCAACP-FPCMNDLKFPVVVLDECSQITEPASLLPIARfeCEKLILVGDPKQLPP 1842
Cdd:COG1112   517 LKKRRELRKLLWDA-LLELAPVVGMTPASVArLLPLGEGSFDLVIIDEASQATLAEALGALAR--AKRVVLVGDPKQLPP 593
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1843 TIQGSDAA--HENGLEQTLFDRLC-LMGHKPILLRTQYRCHPAISAIANDLFYKGALMNGVTEIERSPLLEWLPtLCFYN 1919
Cdd:COG1112   594 VVFGEEAEevAEEGLDESLLDRLLaRLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRLADPDSP-LVFID 672
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1920 VKGLEQiERDNSFHNVAEATFTLKLIQSLIASGIAGSMIGVITLYKSQMYKLCHLLSAVDFHHPDikTVQVSTVDAFQGA 1999
Cdd:COG1112   673 VDGVYE-RRGGSRTNPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVALIRELLREALGDGLE--PVFVGTVDRFQGD 749
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530377937 2000 EKEIIILSCVRT------RQVGFI-DSEKRMNVALTRGKRHLLIVGNLACL---RKNQLWGRVIQHCE 2057
Cdd:COG1112   750 ERDVIIFSLVYSndedvpRNFGFLnGGPRRLNVAVSRARRKLIVVGSRELLdsdPSTPALKRLLEYLE 817
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
1855-2039 1.66e-67

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: 226.28  E-value: 1.66e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937  1855 LEQTLFDRLCLMG-HKPILLRTQYRCHPAISAIANDLFYKGALMNGVTEIERSPL-LEWLPT----LCFYNVKGLEQIER 1928
Cdd:pfam13087    1 LDRSLFERLQELGpSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPdDFHLPDplgpLVFIDVDGSEEEES 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937  1929 D--NSFHNVAEATFTLKLIQSLIASGI-AGSMIGVITLYKSQMYKLCHLLSAVDFHHPDIKtvqVSTVDAFQGAEKEIII 2005
Cdd:pfam13087   81 DggTSYSNEAEAELVVQLVEKLIKSGPeEPSDIGVITPYRAQVRLIRKLLKRKLGGKLEIE---VNTVDGFQGREKDVII 157
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 530377937  2006 LSCVRTRQ---VGFIDSEKRMNVALTRGKRHLLIVGN 2039
Cdd:pfam13087  158 FSCVRSNEkggIGFLSDPRRLNVALTRAKRGLIIVGN 194
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
1879-2057 2.17e-57

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: 197.07  E-value: 2.17e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1879 CHPAISAIANDLFYKGALMNGVTEIERSPLLEWLPT---LCFYNVKGLEQIERD-NSFHNVAEATFTLKLIQSLIASGIA 1954
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGVSVAARLNPPPLPGPskpLVFVDVSGGEEREESgTSKSNEAEAELVVELVKYLLKSGVK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1955 GSMIGVITLYKSQMYKLCHLLSAvdfHHPDIKTVQVSTVDAFQGAEKEIIILSCVRTRQ----VGFIDSEKRMNVALTRG 2030
Cdd:cd18808    81 PSSIGVITPYRAQVALIRELLRK---RGGLLEDVEVGTVDNFQGREKDVIILSLVRSNEsggsIGFLSDPRRLNVALTRA 157
                         170       180
                  ....*....|....*....|....*..
gi 530377937 2031 KRHLLIVGNLACLRKNQLWGRVIQHCE 2057
Cdd:cd18808   158 KRGLIIVGNPDTLSKDPLWKKLLEYLE 184
DUF2439 pfam10382
Protein of unknown function (DUF2439); This domain can be found in proteins that have been ...
4-74 6.53e-23

Protein of unknown function (DUF2439); This domain can be found in proteins that have been implicated in telomere maintenance in Saccharomyces cerevisiae and in meiotic chromosome segregation in Schizosaccharomyces pombe. It can also be found in Mte1 (Mph1-associated telomere maintenance protein 1), human zinc finger protein ZGRF1 (C4ORF21) and fission yeast Dbl2. Mte1 is a D-loop-binding protein that interacts and stimulates the helicase and fork regression activities of Mph1 while inhibiting the ability of Mph1 to dissociate recombination intermediates. Mph1 and Mte1 interdependently colocalize at DNA damage-induced foci and dysfunctional telomeres. Mte1 is indicated to play a role in regulation of crossover recombination, response to replication stress, and telomere maintenance. The fission yeast, Dbl2 is needed for cellular resistance to the topoisomerase I poison camptothecin, forms DNA damage-induced foci, and is needed for the optimal recruitment of Fml1 to DNA damage, while the human ZGRF1 protein has been linked to DNA cross-link repair and mutations of it have been found in a variety of human tumors. ZGRF1 is a 5'-to-3'helicase that interacts with RAD51 and stimulates homologous recombination and, thus, promotes the repair of replication-blocking DNA lesions. Having said that, there is no evidence to suggest that this domain is implicated in DNA damage resistance or for nuclear focus formation.


Pssm-ID: 463065  Cd Length: 74  Bit Score: 94.11  E-value: 6.53e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530377937     4 QEFIVLYTHQKMKKSKVWQDGILKITHLGNKAILYDDKGACLESLFLK-CLEVKPGDDLESDRYLITVEEVK 74
Cdd:pfam10382    2 HEYRCLYTHDVRKKHKRWHDGKLKYHTFNKRVMLYDEDGNLIGSDFWTsSEDLEEGEELELDRYLVQIEELL 73
zf-GRF pfam06839
GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding ...
1347-1391 2.42e-12

GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding proteins. It seems likely that this domain is involved in nucleic acid binding. It is named GRF after three conserved residues in the centre of the alignment of the domain. This zinc finger may be related to pfam01396.


Pssm-ID: 462017  Cd Length: 45  Bit Score: 63.19  E-value: 2.42e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 530377937  1347 PSCHHSQPAKLVMVKKEGPNKGRLFYTCDGPKADRCKFFKWLEDV 1391
Cdd:pfam06839    1 PLCPCGQRAVLLTVRKTGPNPGRQFYKCPVGREKQCGFFQWADEV 45
 
Name Accession Description Interval E-value
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
1686-2057 1.03e-68

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 249.66  E-value: 1.03e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1686 ARPWKLLISSSTNVAVDRVLLGLLSLGFENFIRVGSVRKIAKPILPYSLHAGSENESEQLKELHALMKEDLTPTERVY-- 1763
Cdd:COG1112   437 LLALLLLLAAALAALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPEELEKLIAELREAARLRRALRre 516
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1764 VRKSIEQHKLGTNRtLLKQVRVVGVTCAACP-FPCMNDLKFPVVVLDECSQITEPASLLPIARfeCEKLILVGDPKQLPP 1842
Cdd:COG1112   517 LKKRRELRKLLWDA-LLELAPVVGMTPASVArLLPLGEGSFDLVIIDEASQATLAEALGALAR--AKRVVLVGDPKQLPP 593
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1843 TIQGSDAA--HENGLEQTLFDRLC-LMGHKPILLRTQYRCHPAISAIANDLFYKGALMNGVTEIERSPLLEWLPtLCFYN 1919
Cdd:COG1112   594 VVFGEEAEevAEEGLDESLLDRLLaRLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRLADPDSP-LVFID 672
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1920 VKGLEQiERDNSFHNVAEATFTLKLIQSLIASGIAGSMIGVITLYKSQMYKLCHLLSAVDFHHPDikTVQVSTVDAFQGA 1999
Cdd:COG1112   673 VDGVYE-RRGGSRTNPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVALIRELLREALGDGLE--PVFVGTVDRFQGD 749
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530377937 2000 EKEIIILSCVRT------RQVGFI-DSEKRMNVALTRGKRHLLIVGNLACL---RKNQLWGRVIQHCE 2057
Cdd:COG1112   750 ERDVIIFSLVYSndedvpRNFGFLnGGPRRLNVAVSRARRKLIVVGSRELLdsdPSTPALKRLLEYLE 817
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
1855-2039 1.66e-67

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: 226.28  E-value: 1.66e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937  1855 LEQTLFDRLCLMG-HKPILLRTQYRCHPAISAIANDLFYKGALMNGVTEIERSPL-LEWLPT----LCFYNVKGLEQIER 1928
Cdd:pfam13087    1 LDRSLFERLQELGpSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPdDFHLPDplgpLVFIDVDGSEEEES 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937  1929 D--NSFHNVAEATFTLKLIQSLIASGI-AGSMIGVITLYKSQMYKLCHLLSAVDFHHPDIKtvqVSTVDAFQGAEKEIII 2005
Cdd:pfam13087   81 DggTSYSNEAEAELVVQLVEKLIKSGPeEPSDIGVITPYRAQVRLIRKLLKRKLGGKLEIE---VNTVDGFQGREKDVII 157
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 530377937  2006 LSCVRTRQ---VGFIDSEKRMNVALTRGKRHLLIVGN 2039
Cdd:pfam13087  158 FSCVRSNEkggIGFLSDPRRLNVALTRAKRGLIIVGN 194
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
1879-2057 2.17e-57

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: 197.07  E-value: 2.17e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1879 CHPAISAIANDLFYKGALMNGVTEIERSPLLEWLPT---LCFYNVKGLEQIERD-NSFHNVAEATFTLKLIQSLIASGIA 1954
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGVSVAARLNPPPLPGPskpLVFVDVSGGEEREESgTSKSNEAEAELVVELVKYLLKSGVK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1955 GSMIGVITLYKSQMYKLCHLLSAvdfHHPDIKTVQVSTVDAFQGAEKEIIILSCVRTRQ----VGFIDSEKRMNVALTRG 2030
Cdd:cd18808    81 PSSIGVITPYRAQVALIRELLRK---RGGLLEDVEVGTVDNFQGREKDVIILSLVRSNEsggsIGFLSDPRRLNVALTRA 157
                         170       180
                  ....*....|....*....|....*..
gi 530377937 2031 KRHLLIVGNLACLRKNQLWGRVIQHCE 2057
Cdd:cd18808   158 KRGLIIVGNPDTLSKDPLWKKLLEYLE 184
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
1614-1878 7.11e-34

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: 130.05  E-value: 7.11e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1614 KLNKDQATALIQIaqMMASHesieevkelqthtfpITIIHGVFGAGKSYLLAVVILFFVQLfekseaptiGNarpwKLLI 1693
Cdd:cd18041     1 GLNKDQRQAIKKV--LNAKD---------------YALILGMPGTGKTTTIAALVRILVAL---------GK----SVLL 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1694 SSSTNVAVDRVLLGLLSLGFeNFIRVGSVRKIAKPILPYSLHAGSENESEqLKELHalmkedltptervyvrksieqhkl 1773
Cdd:cd18041    51 TSYTHSAVDNILLKLKKFGV-NFLRLGRLKKIHPDVQEFTLEAILKSCKS-VEELE------------------------ 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1774 gtnrTLLKQVRVVGVTCAACPFPCMNDLKFPVVVLDECSQITEPASLLPIARfeCEKLILVGDPKQLPPTIQgSDAAHEN 1853
Cdd:cd18041   105 ----SKYESVSVVATTCLGINHPIFRRRTFDYCIVDEASQITLPICLGPLRL--AKKFVLVGDHYQLPPLVK-SREAREL 177
                         250       260
                  ....*....|....*....|....*.
gi 530377937 1854 GLEQTLFDRLCLMGHKPIL-LRTQYR 1878
Cdd:cd18041   178 GMDESLFKRLSEAHPDAVVqLTIQYR 203
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
1615-1878 1.85e-28

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: 115.00  E-value: 1.85e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1615 LNKDQATALIQIAQMMashesieevkelqthtFPITIIHGVFGAGK--------SYLLAVVILFFVQLFEKSEAPTIGNA 1686
Cdd:cd18042     1 LNESQLEAIASALQNS----------------PGITLIQGPPGTGKtktivgilSVLLAGKYRKYYEKVKKKLRKLQRNL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1687 RPW----KLLISSSTNVAVDRVLLGLLSLGFENFIRVGSVRKIAkpilpyslhagseneseqlkelhalmkedltpteRV 1762
Cdd:cd18042    65 NNKkkknRILVCAPSNAAVDEIVLRLLSEGFLDGDGRSYKPNVV----------------------------------RV 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1763 yVRKSIEQHklgtnrtLLKQVRVVGVT--CAACPFPCMNDLKFPVVVLDECSQITEPASLLPIaRFECEKLILVGDPKQL 1840
Cdd:cd18042   111 -GRQELRAS-------ILNEADIVCTTlsSSGSDLLESLPRGFDTVIIDEAAQAVELSTLIPL-RLGCKRLILVGDPKQL 181
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 530377937 1841 PPTIQGSDAAhENGLEQTLFDRLCLMGHKPILLRTQYR 1878
Cdd:cd18042   182 PATVFSKVAQ-KLGYDRSLFERLQLAGYPVLMLTTQYR 218
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
1648-1878 3.34e-28

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: 115.04  E-value: 3.34e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1648 PITIIHGVFGAGKSYLLAVVILFFVQLfekseapTIGnarpwKLLISSSTNVAVDRVLLGLLSLGFeNFIRVGSVRK--I 1725
Cdd:cd18039    17 PLSLIQGPPGTGKTVTSATIVYHLVKQ-------GNG-----PVLVCAPSNVAVDQLTEKIHQTGL-KVVRLCAKSReaV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1726 AKPILPYSLH----AGSENESEQLKELHALMKEDLTPTERVYVRKSIEQhklgTNRTLLKQVRVVGVTCAACPFPCMNDL 1801
Cdd:cd18039    84 ESPVSFLALHnqvrNLDSAEKLELLKLLKLETGELSSADEKRYRKLKRK----AERELLRNADVICCTCVGAGDPRLSKM 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530377937 1802 KFPVVVLDECSQITEPASLLPIARfECEKLILVGDPKQLPPTIQGSDAAhENGLEQTLFDRLCLMGHKPILLRTQYR 1878
Cdd:cd18039   160 KFRTVLIDEATQATEPECLIPLVH-GAKQVILVGDHCQLGPVVMCKKAA-KAGLSQSLFERLVQLGIRPIRLQVQYR 234
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
1648-1878 2.60e-26

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: 108.08  E-value: 2.60e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1648 PITIIHGVFGAGKSYLLAVVILFFVQlfekseaptignaRPWKLLISSSTNVAVDRVLLGLLSLGfENFIRVGSVRKIAK 1727
Cdd:cd18044    18 DVALIHGPPGTGKTTTVVEIILQAVK-------------RGEKVLACAPSNIAVDNLVERLVALK-VKVVRIGHPARLLE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1728 PILPYSLHAgseneseqlkelhalmkedltptervyvrksieqhklgtnrtlLKQVRVVGVTC-AACPFPCMNDLKFPVV 1806
Cdd:cd18044    84 SVLDHSLDA-------------------------------------------LVAAQVVLATNtGAGSRQLLPNELFDVV 120
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530377937 1807 VLDECSQITEPASLLPIARFEceKLILVGDPKQLPPTIQgSDAAHENGLEQTLFDRLcLMGHKP---ILLRTQYR 1878
Cdd:cd18044   121 VIDEAAQALEASCWIPLLKAR--RCILAGDHKQLPPTIL-SDKAARGGLGVTLFERL-VNLYGEsvvRMLTVQYR 191
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
1649-1878 1.55e-24

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: 100.39  E-value: 1.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1649 ITIIHGVFGAGKSYLLAVVILFFVQlfekseaptigNARPWKLLISSSTNVAVDRVllgllslgfenfirvgsvrkiakp 1728
Cdd:cd17934     1 ISLIQGPPGTGKTTTIAAIVLQLLK-----------GLRGKRVLVTAQSNVAVDNV------------------------ 45
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1729 ilpyslhagseneseqlkelhalmkedltptervyvrksieqhklgtnrtllkqvrvvgvtcaacpfpcmndlkfPVVVL 1808
Cdd:cd17934    46 ---------------------------------------------------------------------------DVVII 50
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530377937 1809 DECSQITEPASLLPIARfeCEKLILVGDPKQLPPTIQGSDAAH---ENGLEQTLFDRLCLMGHKPILLRTQYR 1878
Cdd:cd17934    51 DEASQITEPELLIALIR--AKKVVLVGDPKQLPPVVQEDHAALlglSFILSLLLLFRLLLPGSPKVMLDTQYR 121
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
1648-1844 1.11e-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: 102.42  E-value: 1.11e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937  1648 PITIIHGVFGAGKSyllaVVIL-FFVQLFekSEAPTIGNARPwKLLISSSTNVAVDRVLLGLLSLGFE---NFIRVGSVR 1723
Cdd:pfam13086   14 HFTLIQGPPGTGKT----TTIVeLIRQLL--SYPATSAAAGP-RILVCAPSNAAVDNILERLLRKGQKygpKIVRIGHPA 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937  1724 KIAKPILPYSL----------------------------HAGSENESEQLKELHALMKEDLTPTERVY----------VR 1765
Cdd:pfam13086   87 AISEAVLPVSLdylvesklnneedaqivkdiskeleklaKALRAFEKEIIVEKLLKSRNKDKSKLEQErrklrserkeLR 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937  1766 KSIEQHKLGTNRTLLKQVRVVGVTCAACPFPCMNDL-KFPVVVLDECSQITEPASLLPIaRFECEKLILVGDPKQLPPTI 1844
Cdd:pfam13086  167 KELRRREQSLEREILDEAQIVCSTLSGAGSRLLSSLaNFDVVIIDEAAQALEPSTLIPL-LRGPKKVVLVGDPKQLPPTV 245
DUF2439 pfam10382
Protein of unknown function (DUF2439); This domain can be found in proteins that have been ...
4-74 6.53e-23

Protein of unknown function (DUF2439); This domain can be found in proteins that have been implicated in telomere maintenance in Saccharomyces cerevisiae and in meiotic chromosome segregation in Schizosaccharomyces pombe. It can also be found in Mte1 (Mph1-associated telomere maintenance protein 1), human zinc finger protein ZGRF1 (C4ORF21) and fission yeast Dbl2. Mte1 is a D-loop-binding protein that interacts and stimulates the helicase and fork regression activities of Mph1 while inhibiting the ability of Mph1 to dissociate recombination intermediates. Mph1 and Mte1 interdependently colocalize at DNA damage-induced foci and dysfunctional telomeres. Mte1 is indicated to play a role in regulation of crossover recombination, response to replication stress, and telomere maintenance. The fission yeast, Dbl2 is needed for cellular resistance to the topoisomerase I poison camptothecin, forms DNA damage-induced foci, and is needed for the optimal recruitment of Fml1 to DNA damage, while the human ZGRF1 protein has been linked to DNA cross-link repair and mutations of it have been found in a variety of human tumors. ZGRF1 is a 5'-to-3'helicase that interacts with RAD51 and stimulates homologous recombination and, thus, promotes the repair of replication-blocking DNA lesions. Having said that, there is no evidence to suggest that this domain is implicated in DNA damage resistance or for nuclear focus formation.


Pssm-ID: 463065  Cd Length: 74  Bit Score: 94.11  E-value: 6.53e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530377937     4 QEFIVLYTHQKMKKSKVWQDGILKITHLGNKAILYDDKGACLESLFLK-CLEVKPGDDLESDRYLITVEEVK 74
Cdd:pfam10382    2 HEYRCLYTHDVRKKHKRWHDGKLKYHTFNKRVMLYDEDGNLIGSDFWTsSEDLEEGEELELDRYLVQIEELL 73
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
1614-1878 1.17e-17

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: 85.27  E-value: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1614 KLNKDQATAliqiaqmmashesieeVKELQTHtfPITIIHGVFGAGKSYLLAVVILFFVQLFEKSEAPTIGNARPWKLLI 1693
Cdd:cd18040     1 KLNPSQNHA----------------VRTALTK--PFTLIQGPPGTGKTVTGVHIAYWFAKQNREIQSVSGEGDGGPCVLY 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1694 SSSTNVAVDRVLLGLLSLGFENFIRVGSVR----KIAKPILPYSLHAGSENESEQLKE-----LHALMKEDLTPT----- 1759
Cdd:cd18040    63 CGPSNKSVDVVAELLLKVPGLKILRVYSEQiettEYPIPNEPRHPNKKSERESKPNSElssitLHHRIRQPSNPHsqqik 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1760 --ERVYVRksiEQHKLGTNRT-------------LLKQVRVVGVTCAACPFPCMNdLKFPV--VVLDECSQITEPASLLP 1822
Cdd:cd18040   143 afEARFER---TQEKITEEDIktykiliwearfeELETVDVILCTCSEAASQKMR-THANVkqCIVDECGMCTEPESLIP 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530377937 1823 I-ARFECEKLILVGDPKQLPPTIQgSDAAHENGLEQTLFDRLclmGHKPILLRTQYR 1878
Cdd:cd18040   219 IvSAPRAEQVVLIGDHKQLRPVVQ-NKEAQKLGLGRSLFERY---AEKACMLDTQYR 271
zf-GRF pfam06839
GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding ...
1347-1391 2.42e-12

GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding proteins. It seems likely that this domain is involved in nucleic acid binding. It is named GRF after three conserved residues in the centre of the alignment of the domain. This zinc finger may be related to pfam01396.


Pssm-ID: 462017  Cd Length: 45  Bit Score: 63.19  E-value: 2.42e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 530377937  1347 PSCHHSQPAKLVMVKKEGPNKGRLFYTCDGPKADRCKFFKWLEDV 1391
Cdd:pfam06839    1 PLCPCGQRAVLLTVRKTGPNPGRQFYKCPVGREKQCGFFQWADEV 45
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
1615-1877 3.00e-12

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: 67.18  E-value: 3.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1615 LNKDQATALiqiaQMMASHEsieevkelqthtfpITIIHGVFGAGKSYLLAVVILFFVQLFEKSEAPTIgnarpwklLIS 1694
Cdd:cd17936     2 LDPSQLEAL----KHALTSE--------------LALIQGPPGTGKTFLGVKLVRALLQNQDLSITGPI--------LVV 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1695 SSTNVAVDRVLLGLLSLGFENFIRVGsvrkiakpilpyslhagseneseqlkelhalmkedltptervyvrksieqhklg 1774
Cdd:cd17936    56 CYTNHALDQFLEGLLDFGPTKIVRLG------------------------------------------------------ 81
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1775 tnrtllkqVRVVGVT--CAACPFPCMNDLKFPVVVLDECSQITEP---ASLLPiarfECEKLILVGDPKQLPPTIQG-SD 1848
Cdd:cd17936    82 --------ARVIGMTttGAAKYRELLQALGPKVVIVEEAAEVLEAhilAALTP----STEHLILIGDHKQLRPKVNVyEL 149
                         250       260
                  ....*....|....*....|....*....
gi 530377937 1849 AAHENGLEQTLFDRLCLMGHKPILLRTQY 1877
Cdd:cd17936   150 TAKKYNLDVSLFERLVKNGLPFVTLNVQR 178
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
1615-1865 7.68e-12

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: 67.26  E-value: 7.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1615 LNKDQATALIQIAQmmashesieevkelQTHTFPITIIHGVFGAGKSYLLAVVILFFVQLFEKSeaptignarpwKLLIS 1694
Cdd:cd18038     2 LNDEQKLAVRNIVT--------------GTSRPPPYIIFGPPGTGKTVTLVEAILQVLRQPPEA-----------RILVC 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1695 SSTNVAVDRVLLGLLslgfenfirvgsvRKIAKPILPYSLHAGSENESEQLKELHALMKEDLtptERVYVRKSIEQhklg 1774
Cdd:cd18038    57 APSNSAADLLAERLL-------------NALVTKREILRLNAPSRDRASVPPELLPYCNSKA---EGTFRLPSLEE---- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1775 tnrtlLKQVRVVGVTC--------AACPFPcmndlKFPVVVLDECSQITEPASLLPIAR---FECEkLILVGDPKQLPPT 1843
Cdd:cd18038   117 -----LKKYRIVVCTLmtagrlvqAGVPNG-----HFTHIFIDEAGQATEPEALIPLSElasKNTQ-IVLAGDPKQLGPV 185
                         250       260
                  ....*....|....*....|..
gi 530377937 1844 IQgSDAAHENGLEQTLFDRLCL 1865
Cdd:cd18038   186 VR-SPLARKYGLGKSLLERLME 206
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
1784-1888 8.96e-11

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: 63.60  E-value: 8.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1784 RVVGVTCAACPFP----CMNDLKFPVVVLDECSQITEPASLLPIA--RFECE-----KLILVGDPKQLPPTIQGSDAAHE 1852
Cdd:cd17935    88 KIIAMTCTHAALKrgelVELGFKYDNILMEEAAQILEIETFIPLLlqNPEDGpnrlkRLIMIGDHHQLPPVIKNMAFQKY 167
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 530377937 1853 NGLEQTLFDRLCLMGHKPILLRTQYRCHPAISAIAN 1888
Cdd:cd17935   168 SNMEQSLFTRLVRLGVPTVDLDAQGRARASISSLYN 203
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
1801-1877 5.96e-10

DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. Their helicase core is surrounded by C and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains or domains engaged in protein-protein interactions. SF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438706 [Multi-domain]  Cd Length: 121  Bit Score: 58.65  E-value: 5.96e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530377937 1801 LKFPVVVLDECSQITEPASLLPIARFE-CEKLILVGDPKQLPPTIQGSDAAhENGLEQTLFDRLCLMGHKPILLRTQY 1877
Cdd:cd17914    45 AQLDNILVDEAAQILEPETSRLIDLALdQGRVILVGDHDQLGPVWRGAVLA-KICNEQSLFTRLVRLGVSLIRLQVQY 121
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
1958-2038 1.87e-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: 1.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1958 IGVITLYKSQMYKLCHLLSAVDFHHPDIKTVQVSTVDAFQGAEKEIIILSCVRTrqvgFIDSEKRMNVALTRGKRHLLIV 2037
Cdd:cd18786    13 GVVLTPYHRDRAYLNQYLQGLSLDEFDLQLVGAITIDSSQGLTFDVVTLYLPTA----NSLTPRRLYVALTRARKRLVIY 88

                  .
gi 530377937 2038 G 2038
Cdd:cd18786    89 D 89
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
1651-1863 3.88e-09

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: 59.30  E-value: 3.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1651 IIHGVFGAGKSYLLAVVILFFVQLFEKSeaptignarpwKLLISSSTNVAVDRVLLGLLSlgfENFIRVGSVRKIAKpil 1730
Cdd:cd18078    24 ILFGPPGTGKTVTIIEAILQVVYNLPRS-----------RILVCAPSNSAADLVTSRLHE---SKVLKPGDMVRLNA--- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1731 pyslhagseneseqlkelHALMKEDLTPTERVYVRKSIEQHKLGTNRTLLKQVRVVGVtcaacpfpcMNDLKFPV----- 1805
Cdd:cd18078    87 ------------------VNRFESTVIDARKLYCRLGEDLSKASRHRIVISTCSTAGL---------LYQMGLPVghfth 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1806 VVLDECSQITEPASLLPIARFECE--KLILVGDPKQLPPTIQgSDAAHENGLEQTLFDRL 1863
Cdd:cd18078   140 VFVDEAGQATEPESLIPLGLISSRdgQIILAGDPMQLGPVIK-SRLASAYGLGVSFLERL 198
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
1802-1844 1.37e-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: 49.50  E-value: 1.37e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 530377937 1802 KFPVVVLDECSQITEPASLLPIARfeCEKLILVGDPKQLPPTI 1844
Cdd:cd18043    80 LFDLVIFDEASQIPIEEALPALFR--GKQVVVVGDDKQLPPSI 120
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
1648-1878 1.67e-06

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: 51.33  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1648 PITIIhGVFGAGKSYLLAVVIlffVQLFEKSEAptignarpwKLLISSSTNVAVDrvllgllsLGFENFIR--VGSVRKI 1725
Cdd:cd18077    23 PVLLI-GPFGTGKTFTLAQAV---KHILQQPET---------RILICTHSNSAAD--------LYIKEYLHpyVETGNPR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1726 AKPILPYsLHAGSENESEQLKELHALMKEDltPTERVYVRKSIEQHklgtnrtllkqvRVVGVTCAACPFPCMNDLK--- 1802
Cdd:cd18077    82 ARPLRVY-YRNRWVKTVHPVVQKYCLIDEH--GTFRMPTREDVMRH------------RVVVVTLSTSQYLCQLDLEpgf 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1803 FPVVVLDECSQITEPASLLPIARFECE-KLILVGDPKQLPPTIQgSDAAHENGLEQTLFDRlcLMGHKP------ILLRT 1875
Cdd:cd18077   147 FTHILLDEAAQAMECEAIMPLALATKStRIVLAGDHMQLSPEVY-SEFARERNLHISLLER--LYEHYPsehpcrILLCE 223

                  ...
gi 530377937 1876 QYR 1878
Cdd:cd18077   224 NYR 226
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
1799-1842 5.22e-05

DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 45.62  E-value: 5.22e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 530377937 1799 NDLKFPVVVLDECSQITEP--ASLLPIARFECeKLILVGDPKQLPP 1842
Cdd:cd17933    86 NPLDADLLIVDEASMVDTRlmAALLSAIPAGA-RLILVGDPDQLPS 130
alphaCoV_Nsp13-helicase cd21723
helicase domain of alphacoronavirus non-structural protein 13; This model represents the ...
1805-2037 6.85e-05

helicase domain of alphacoronavirus non-structural protein 13; This model represents the helicase domain of non-structural protein 13 (Nsp13) from alphacoronavirus, including Porcine epidemic diarrhea virus and Human coronavirus (CoV) NL63. Helicases catalyze NTP-dependent unwinding of nucleic acid duplexes into single strands and are classified based on the arrangement of conserved motifs into six superfamilies. CoV Nsp13 is a member of the helicase superfamily 1 (SF1); SF1 and SF2 helicases do not form toroidal structures, while SF3-6 helicases do. Nsp13 is a component of the viral RNA synthesis replication and transcription complex (RTC). It is a multidomain protein containing a Cys/His rich zinc-binding domain (CH/ZBD), a stalk domain, a 1B domain involved in nucleic acid substrate binding, and a SF1 helicase core.


Pssm-ID: 409656 [Multi-domain]  Cd Length: 340  Bit Score: 47.42  E-value: 6.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1805 VVVLDECSQITEPASLLPIARFECEKLILVGDPKQLP-PTIQGSDAAHENGLEQTLFDRLCLMGhKPILLRTQYRCHPAI 1883
Cdd:cd21723   120 IVVVDEVSMCTNYDLSVINQRVSYKHIVYVGDPQQLPaPRTMITRGVLEPKDYNVVTQRMCALG-PDVFLHKCYRCPAEI 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377937 1884 SAIANDLFYKGALMnGVTEIERSpllewlptlCF-YNVKGLEQIERDNSFHNVaeatfTLKLIQSLIASGIAGSMIGVIT 1962
Cdd:cd21723   199 VNTVSELVYENKFK-PVHPESKQ---------CFkIFCKGNVQVDNGSSINRR-----QLDVVKMFLAKNPKWSKAVFIS 263
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530377937 1963 LYKSQMYKLCHLLSavdfhhpdiktVQVSTVDAFQGAEKEIIILScvRTRQVGFIDSEKRMNVALTRGKRHLLIV 2037
Cdd:cd21723   264 PYNSQNYVASRVLG-----------LQIQTVDSSQGSEYDYVIYT--QTSDTAHACNVNRFNVAITRAKKGILCV 325
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
1805-1842 3.29e-04

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 45.74  E-value: 3.29e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 530377937 1805 VVVLDECSQITEP--ASLLPIARFECEKLILVGDPKQLPP 1842
Cdd:COG0507   221 LLVVDEASMVDTRlmAALLEALPRAGARLILVGDPDQLPS 260
 
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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