NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767932266|ref|XP_011530393|]
View 

protein ZGRF1 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
1669-2040 1.02e-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: 1.02e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1669 ARPWKLLISSSTNVAVDRVLLGLLSLGFENFIRVGSVRKIAKPILPYSLHAGSENESEQLKELHALMKEDLTPTERVY-- 1746
Cdd:COG1112   437 LLALLLLLAAALAALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPEELEKLIAELREAARLRRALRre 516

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1747 VRKSIEQHKLGTNRtLLKQVRVVGVTCAACP-FPCMNDLKFPVVVLDECSQITEPASLLPIARfeCEKLILVGDPKQLPP 1825
Cdd:COG1112   517 LKKRRELRKLLWDA-LLELAPVVGMTPASVArLLPLGEGSFDLVIIDEASQATLAEALGALAR--AKRVVLVGDPKQLPP 593

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1826 TIQGSDAA--HENGLEQTLFDRLC-LMGHKPILLRTQYRCHPAISAIANDLFYKGALMNGVTEIERSPLLEWLPtLCFYN 1902
Cdd:COG1112   594 VVFGEEAEevAEEGLDESLLDRLLaRLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRLADPDSP-LVFID 672

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1903 VKGLEQiERDNSFHNVAEATFTLKLIQSLIASGIAGSMIGVITLYKSQMYKLCHLLSAVDFHHPDikTVQVSTVDAFQGA 1982
Cdd:COG1112   673 VDGVYE-RRGGSRTNPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVALIRELLREALGDGLE--PVFVGTVDRFQGD 749

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767932266 1983 EKEIIILSCVRT------RQVGFI-DSEKRMNVALTRGKRHLLIVGNLACL---RKNQLWGRVIQHCE 2040
Cdd:COG1112   750 ERDVIIFSLVYSndedvpRNFGFLnGGPRRLNVAVSRARRKLIVVGSRELLdsdPSTPALKRLLEYLE 817
DUF2439 pfam10382
Protein of unknown function (DUF2439); This domain can be found in proteins that have been ...
 4-74 5.93e-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: 5.93e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767932266     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 ...
 1330-1374 2.40e-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: 2.40e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 767932266  1330 PSCHHSQPAKLVMVKKEGPNKGRLFYTCDGPKADRCKFFKWLEDV 1374
Cdd:pfam06839    1 PLCPCGQRAVLLTVRKTGPNPGRQFYKCPVGREKQCGFFQWADEV 45
 
Name Accession Description Interval E-value
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
1669-2040 1.02e-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: 1.02e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1669 ARPWKLLISSSTNVAVDRVLLGLLSLGFENFIRVGSVRKIAKPILPYSLHAGSENESEQLKELHALMKEDLTPTERVY-- 1746
Cdd:COG1112   437 LLALLLLLAAALAALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPEELEKLIAELREAARLRRALRre 516

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1747 VRKSIEQHKLGTNRtLLKQVRVVGVTCAACP-FPCMNDLKFPVVVLDECSQITEPASLLPIARfeCEKLILVGDPKQLPP 1825
Cdd:COG1112   517 LKKRRELRKLLWDA-LLELAPVVGMTPASVArLLPLGEGSFDLVIIDEASQATLAEALGALAR--AKRVVLVGDPKQLPP 593

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1826 TIQGSDAA--HENGLEQTLFDRLC-LMGHKPILLRTQYRCHPAISAIANDLFYKGALMNGVTEIERSPLLEWLPtLCFYN 1902
Cdd:COG1112   594 VVFGEEAEevAEEGLDESLLDRLLaRLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRLADPDSP-LVFID 672

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1903 VKGLEQiERDNSFHNVAEATFTLKLIQSLIASGIAGSMIGVITLYKSQMYKLCHLLSAVDFHHPDikTVQVSTVDAFQGA 1982
Cdd:COG1112   673 VDGVYE-RRGGSRTNPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVALIRELLREALGDGLE--PVFVGTVDRFQGD 749

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767932266 1983 EKEIIILSCVRT------RQVGFI-DSEKRMNVALTRGKRHLLIVGNLACL---RKNQLWGRVIQHCE 2040
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 ...
 1838-2022 1.54e-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: 226.66  E-value: 1.54e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266  1838 LEQTLFDRLCLMG-HKPILLRTQYRCHPAISAIANDLFYKGALMNGVTEIERSPL-LEWLPT----LCFYNVKGLEQIER 1911
Cdd:pfam13087    1 LDRSLFERLQELGpSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPdDFHLPDplgpLVFIDVDGSEEEES 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266  1912 D--NSFHNVAEATFTLKLIQSLIASGI-AGSMIGVITLYKSQMYKLCHLLSAVDFHHPDIKtvqVSTVDAFQGAEKEIII 1988
Cdd:pfam13087   81 DggTSYSNEAEAELVVQLVEKLIKSGPeEPSDIGVITPYRAQVRLIRKLLKRKLGGKLEIE---VNTVDGFQGREKDVII 157

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 767932266  1989 LSCVRTRQ---VGFIDSEKRMNVALTRGKRHLLIVGN 2022
Cdd:pfam13087  158 FSCVRSNEkggIGFLSDPRRLNVALTRAKRGLIIVGN 194
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
 1862-2040 2.03e-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: 2.03e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1862 CHPAISAIANDLFYKGALMNGVTEIERSPLLEWLPT---LCFYNVKGLEQIERD-NSFHNVAEATFTLKLIQSLIASGIA 1937
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGVSVAARLNPPPLPGPskpLVFVDVSGGEEREESgTSKSNEAEAELVVELVKYLLKSGVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1938 GSMIGVITLYKSQMYKLCHLLSAvdfHHPDIKTVQVSTVDAFQGAEKEIIILSCVRTRQ----VGFIDSEKRMNVALTRG 2013
Cdd:cd18808    81 PSSIGVITPYRAQVALIRELLRK---RGGLLEDVEVGTVDNFQGREKDVIILSLVRSNEsggsIGFLSDPRRLNVALTRA 157

                         170       180
                  ....*....|....*....|....*..
gi 767932266 2014 KRHLLIVGNLACLRKNQLWGRVIQHCE 2040
Cdd:cd18808   158 KRGLIIVGNPDTLSKDPLWKKLLEYLE 184
DUF2439 pfam10382
Protein of unknown function (DUF2439); This domain can be found in proteins that have been ...
 4-74 5.93e-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: 5.93e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767932266     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 ...
 1330-1374 2.40e-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: 2.40e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 767932266  1330 PSCHHSQPAKLVMVKKEGPNKGRLFYTCDGPKADRCKFFKWLEDV 1374
Cdd:pfam06839    1 PLCPCGQRAVLLTVRKTGPNPGRQFYKCPVGREKQCGFFQWADEV 45
 
Name Accession Description Interval E-value
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
1669-2040 1.02e-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: 1.02e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1669 ARPWKLLISSSTNVAVDRVLLGLLSLGFENFIRVGSVRKIAKPILPYSLHAGSENESEQLKELHALMKEDLTPTERVY-- 1746
Cdd:COG1112   437 LLALLLLLAAALAALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPEELEKLIAELREAARLRRALRre 516

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1747 VRKSIEQHKLGTNRtLLKQVRVVGVTCAACP-FPCMNDLKFPVVVLDECSQITEPASLLPIARfeCEKLILVGDPKQLPP 1825
Cdd:COG1112   517 LKKRRELRKLLWDA-LLELAPVVGMTPASVArLLPLGEGSFDLVIIDEASQATLAEALGALAR--AKRVVLVGDPKQLPP 593

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1826 TIQGSDAA--HENGLEQTLFDRLC-LMGHKPILLRTQYRCHPAISAIANDLFYKGALMNGVTEIERSPLLEWLPtLCFYN 1902
Cdd:COG1112   594 VVFGEEAEevAEEGLDESLLDRLLaRLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRLADPDSP-LVFID 672

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1903 VKGLEQiERDNSFHNVAEATFTLKLIQSLIASGIAGSMIGVITLYKSQMYKLCHLLSAVDFHHPDikTVQVSTVDAFQGA 1982
Cdd:COG1112   673 VDGVYE-RRGGSRTNPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVALIRELLREALGDGLE--PVFVGTVDRFQGD 749

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767932266 1983 EKEIIILSCVRT------RQVGFI-DSEKRMNVALTRGKRHLLIVGNLACL---RKNQLWGRVIQHCE 2040
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 ...
 1838-2022 1.54e-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: 226.66  E-value: 1.54e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266  1838 LEQTLFDRLCLMG-HKPILLRTQYRCHPAISAIANDLFYKGALMNGVTEIERSPL-LEWLPT----LCFYNVKGLEQIER 1911
Cdd:pfam13087    1 LDRSLFERLQELGpSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPdDFHLPDplgpLVFIDVDGSEEEES 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266  1912 D--NSFHNVAEATFTLKLIQSLIASGI-AGSMIGVITLYKSQMYKLCHLLSAVDFHHPDIKtvqVSTVDAFQGAEKEIII 1988
Cdd:pfam13087   81 DggTSYSNEAEAELVVQLVEKLIKSGPeEPSDIGVITPYRAQVRLIRKLLKRKLGGKLEIE---VNTVDGFQGREKDVII 157

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 767932266  1989 LSCVRTRQ---VGFIDSEKRMNVALTRGKRHLLIVGN 2022
Cdd:pfam13087  158 FSCVRSNEkggIGFLSDPRRLNVALTRAKRGLIIVGN 194
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
 1862-2040 2.03e-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: 2.03e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1862 CHPAISAIANDLFYKGALMNGVTEIERSPLLEWLPT---LCFYNVKGLEQIERD-NSFHNVAEATFTLKLIQSLIASGIA 1937
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGVSVAARLNPPPLPGPskpLVFVDVSGGEEREESgTSKSNEAEAELVVELVKYLLKSGVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1938 GSMIGVITLYKSQMYKLCHLLSAvdfHHPDIKTVQVSTVDAFQGAEKEIIILSCVRTRQ----VGFIDSEKRMNVALTRG 2013
Cdd:cd18808    81 PSSIGVITPYRAQVALIRELLRK---RGGLLEDVEVGTVDNFQGREKDVIILSLVRSNEsggsIGFLSDPRRLNVALTRA 157

                         170       180
                  ....*....|....*....|....*..
gi 767932266 2014 KRHLLIVGNLACLRKNQLWGRVIQHCE 2040
Cdd:cd18808   158 KRGLIIVGNPDTLSKDPLWKKLLEYLE 184
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
 1597-1861 6.78e-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: 130.43  E-value: 6.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1597 KLNKDQATALIQIaqMMASHesieevkelqthtfpITIIHGVFGAGKSYLLAVVILFFVQLfekseaptiGNarpwKLLI 1676
Cdd:cd18041     1 GLNKDQRQAIKKV--LNAKD---------------YALILGMPGTGKTTTIAALVRILVAL---------GK----SVLL 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1677 SSSTNVAVDRVLLGLLSLGFeNFIRVGSVRKIAKPILPYSLHAGSENESEqLKELHalmkedltptervyvrksieqhkl 1756
Cdd:cd18041    51 TSYTHSAVDNILLKLKKFGV-NFLRLGRLKKIHPDVQEFTLEAILKSCKS-VEELE------------------------ 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1757 gtnrTLLKQVRVVGVTCAACPFPCMNDLKFPVVVLDECSQITEPASLLPIARfeCEKLILVGDPKQLPPTIQgSDAAHEN 1836
Cdd:cd18041   105 ----SKYESVSVVATTCLGINHPIFRRRTFDYCIVDEASQITLPICLGPLRL--AKKFVLVGDHYQLPPLVK-SREAREL 177

                         250       260
                  ....*....|....*....|....*.
gi 767932266 1837 GLEQTLFDRLCLMGHKPIL-LRTQYR 1861
Cdd:cd18041   178 GMDESLFKRLSEAHPDAVVqLTIQYR 203
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
 1598-1861 1.72e-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: 115.39  E-value: 1.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1598 LNKDQATALIQIAQMMashesieevkelqthtFPITIIHGVFGAGK--------SYLLAVVILFFVQLFEKSEAPTIGNA 1669
Cdd:cd18042     1 LNESQLEAIASALQNS----------------PGITLIQGPPGTGKtktivgilSVLLAGKYRKYYEKVKKKLRKLQRNL 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1670 RPW----KLLISSSTNVAVDRVLLGLLSLGFENFIRVGSVRKIAkpilpyslhagseneseqlkelhalmkedltpteRV 1745
Cdd:cd18042    65 NNKkkknRILVCAPSNAAVDEIVLRLLSEGFLDGDGRSYKPNVV----------------------------------RV 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1746 yVRKSIEQHklgtnrtLLKQVRVVGVT--CAACPFPCMNDLKFPVVVLDECSQITEPASLLPIaRFECEKLILVGDPKQL 1823
Cdd:cd18042   111 -GRQELRAS-------ILNEADIVCTTlsSSGSDLLESLPRGFDTVIIDEAAQAVELSTLIPL-RLGCKRLILVGDPKQL 181

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767932266 1824 PPTIQGSDAAhENGLEQTLFDRLCLMGHKPILLRTQYR 1861
Cdd:cd18042   182 PATVFSKVAQ-KLGYDRSLFERLQLAGYPVLMLTTQYR 218
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
 1631-1861 2.95e-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: 2.95e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1631 PITIIHGVFGAGKSYLLAVVILFFVQLfekseapTIGnarpwKLLISSSTNVAVDRVLLGLLSLGFeNFIRVGSVRK--I 1708
Cdd:cd18039    17 PLSLIQGPPGTGKTVTSATIVYHLVKQ-------GNG-----PVLVCAPSNVAVDQLTEKIHQTGL-KVVRLCAKSReaV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1709 AKPILPYSLH----AGSENESEQLKELHALMKEDLTPTERVYVRKSIEQhklgTNRTLLKQVRVVGVTCAACPFPCMNDL 1784
Cdd:cd18039    84 ESPVSFLALHnqvrNLDSAEKLELLKLLKLETGELSSADEKRYRKLKRK----AERELLRNADVICCTCVGAGDPRLSKM 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767932266 1785 KFPVVVLDECSQITEPASLLPIARfECEKLILVGDPKQLPPTIQGSDAAhENGLEQTLFDRLCLMGHKPILLRTQYR 1861
Cdd:cd18039   160 KFRTVLIDEATQATEPECLIPLVH-GAKQVILVGDHCQLGPVVMCKKAA-KAGLSQSLFERLVQLGIRPIRLQVQYR 234
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
 1631-1861 2.58e-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: 2.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1631 PITIIHGVFGAGKSYLLAVVILFFVQlfekseaptignaRPWKLLISSSTNVAVDRVLLGLLSLGfENFIRVGSVRKIAK 1710
Cdd:cd18044    18 DVALIHGPPGTGKTTTVVEIILQAVK-------------RGEKVLACAPSNIAVDNLVERLVALK-VKVVRIGHPARLLE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1711 PILPYSLHAgseneseqlkelhalmkedltptervyvrksieqhklgtnrtlLKQVRVVGVTC-AACPFPCMNDLKFPVV 1789
Cdd:cd18044    84 SVLDHSLDA-------------------------------------------LVAAQVVLATNtGAGSRQLLPNELFDVV 120

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767932266 1790 VLDECSQITEPASLLPIARFEceKLILVGDPKQLPPTIQgSDAAHENGLEQTLFDRLcLMGHKP---ILLRTQYR 1861
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, ...
 1632-1861 1.53e-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: 1.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1632 ITIIHGVFGAGKSYLLAVVILFFVQlfekseaptigNARPWKLLISSSTNVAVDRVllgllslgfenfirvgsvrkiakp 1711
Cdd:cd17934     1 ISLIQGPPGTGKTTTIAAIVLQLLK-----------GLRGKRVLVTAQSNVAVDNV------------------------ 45

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1712 ilpyslhagseneseqlkelhalmkedltptervyvrksieqhklgtnrtllkqvrvvgvtcaacpfpcmndlkfPVVVL 1791
Cdd:cd17934    46 ---------------------------------------------------------------------------DVVII 50

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767932266 1792 DECSQITEPASLLPIARfeCEKLILVGDPKQLPPTIQGSDAAH---ENGLEQTLFDRLCLMGHKPILLRTQYR 1861
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 ...
 1631-1827 1.01e-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: 1.01e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266  1631 PITIIHGVFGAGKSyllaVVIL-FFVQLFekSEAPTIGNARPwKLLISSSTNVAVDRVLLGLLSLGFE---NFIRVGSVR 1706
Cdd:pfam13086   14 HFTLIQGPPGTGKT----TTIVeLIRQLL--SYPATSAAAGP-RILVCAPSNAAVDNILERLLRKGQKygpKIVRIGHPA 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266  1707 KIAKPILPYSL----------------------------HAGSENESEQLKELHALMKEDLTPTERVY----------VR 1748
Cdd:pfam13086   87 AISEAVLPVSLdylvesklnneedaqivkdiskeleklaKALRAFEKEIIVEKLLKSRNKDKSKLEQErrklrserkeLR 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266  1749 KSIEQHKLGTNRTLLKQVRVVGVTCAACPFPCMNDL-KFPVVVLDECSQITEPASLLPIaRFECEKLILVGDPKQLPPTI 1827
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 5.93e-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: 5.93e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767932266     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 ...
 1597-1861 1.01e-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: 85.65  E-value: 1.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1597 KLNKDQATAliqiaqmmashesieeVKELQTHtfPITIIHGVFGAGKSYLLAVVILFFVQLFEKSEAPTIGNARPWKLLI 1676
Cdd:cd18040     1 KLNPSQNHA----------------VRTALTK--PFTLIQGPPGTGKTVTGVHIAYWFAKQNREIQSVSGEGDGGPCVLY 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1677 SSSTNVAVDRVLLGLLSLGFENFIRVGSVR----KIAKPILPYSLHAGSENESEQLKE-----LHALMKEDLTPT----- 1742
Cdd:cd18040    63 CGPSNKSVDVVAELLLKVPGLKILRVYSEQiettEYPIPNEPRHPNKKSERESKPNSElssitLHHRIRQPSNPHsqqik 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1743 --ERVYVRksiEQHKLGTNRT-------------LLKQVRVVGVTCAACPFPCMNdLKFPV--VVLDECSQITEPASLLP 1805
Cdd:cd18040   143 afEARFER---TQEKITEEDIktykiliwearfeELETVDVILCTCSEAASQKMR-THANVkqCIVDECGMCTEPESLIP 218

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767932266 1806 I-ARFECEKLILVGDPKQLPPTIQgSDAAHENGLEQTLFDRLclmGHKPILLRTQYR 1861
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 ...
 1330-1374 2.40e-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: 2.40e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 767932266  1330 PSCHHSQPAKLVMVKKEGPNKGRLFYTCDGPKADRCKFFKWLEDV 1374
Cdd:pfam06839    1 PLCPCGQRAVLLTVRKTGPNPGRQFYKCPVGREKQCGFFQWADEV 45
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
 1598-1860 2.98e-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: 2.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1598 LNKDQATALiqiaQMMASHEsieevkelqthtfpITIIHGVFGAGKSYLLAVVILFFVQLFEKSEAPTIgnarpwklLIS 1677
Cdd:cd17936     2 LDPSQLEAL----KHALTSE--------------LALIQGPPGTGKTFLGVKLVRALLQNQDLSITGPI--------LVV 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1678 SSTNVAVDRVLLGLLSLGFENFIRVGsvrkiakpilpyslhagseneseqlkelhalmkedltptervyvrksieqhklg 1757
Cdd:cd17936    56 CYTNHALDQFLEGLLDFGPTKIVRLG------------------------------------------------------ 81

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1758 tnrtllkqVRVVGVT--CAACPFPCMNDLKFPVVVLDECSQITEP---ASLLPiarfECEKLILVGDPKQLPPTIQG-SD 1831
Cdd:cd17936    82 --------ARVIGMTttGAAKYRELLQALGPKVVIVEEAAEVLEAhilAALTP----STEHLILIGDHKQLRPKVNVyEL 149

                         250       260
                  ....*....|....*....|....*....
gi 767932266 1832 AAHENGLEQTLFDRLCLMGHKPILLRTQY 1860
Cdd:cd17936   150 TAKKYNLDVSLFERLVKNGLPFVTLNVQR 178
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
 1598-1848 7.61e-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: 7.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1598 LNKDQATALIQIAQmmashesieevkelQTHTFPITIIHGVFGAGKSYLLAVVILFFVQLFEKSeaptignarpwKLLIS 1677
Cdd:cd18038     2 LNDEQKLAVRNIVT--------------GTSRPPPYIIFGPPGTGKTVTLVEAILQVLRQPPEA-----------RILVC 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1678 SSTNVAVDRVLLGLLslgfenfirvgsvRKIAKPILPYSLHAGSENESEQLKELHALMKEDLtptERVYVRKSIEQhklg 1757
Cdd:cd18038    57 APSNSAADLLAERLL-------------NALVTKREILRLNAPSRDRASVPPELLPYCNSKA---EGTFRLPSLEE---- 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1758 tnrtlLKQVRVVGVTC--------AACPFPcmndlKFPVVVLDECSQITEPASLLPIAR---FECEkLILVGDPKQLPPT 1826
Cdd:cd18038   117 -----LKKYRIVVCTLmtagrlvqAGVPNG-----HFTHIFIDEAGQATEPEALIPLSElasKNTQ-IVLAGDPKQLGPV 185

                         250       260
                  ....*....|....*....|..
gi 767932266 1827 IQgSDAAHENGLEQTLFDRLCL 1848
Cdd:cd18038   186 VR-SPLARKYGLGKSLLERLME 206
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
 1767-1871 8.79e-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: 8.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1767 RVVGVTCAACPFP----CMNDLKFPVVVLDECSQITEPASLLPIA--RFECE-----KLILVGDPKQLPPTIQGSDAAHE 1835
Cdd:cd17935    88 KIIAMTCTHAALKrgelVELGFKYDNILMEEAAQILEIETFIPLLlqNPEDGpnrlkRLIMIGDHHQLPPVIKNMAFQKY 167

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767932266 1836 NGLEQTLFDRLCLMGHKPILLRTQYRCHPAISAIAN 1871
Cdd:cd17935   168 SNMEQSLFTRLVRLGVPTVDLDAQGRARASISSLYN 203
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
 1784-1860 5.91e-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: 5.91e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767932266 1784 LKFPVVVLDECSQITEPASLLPIARFE-CEKLILVGDPKQLPPTIQGSDAAhENGLEQTLFDRLCLMGHKPILLRTQY 1860
Cdd:cd17914    45 AQLDNILVDEAAQILEPETSRLIDLALdQGRVILVGDHDQLGPVWRGAVLA-KICNEQSLFTRLVRLGVSLIRLQVQY 121
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
 1941-2021 1.86e-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: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1941 IGVITLYKSQMYKLCHLLSAVDFHHPDIKTVQVSTVDAFQGAEKEIIILSCVRTrqvgFIDSEKRMNVALTRGKRHLLIV 2020
Cdd:cd18786    13 GVVLTPYHRDRAYLNQYLQGLSLDEFDLQLVGAITIDSSQGLTFDVVTLYLPTA----NSLTPRRLYVALTRARKRLVIY 88


                  .
gi 767932266 2021 G 2021
Cdd:cd18786    89 D 89
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
 1634-1846 3.85e-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: 3.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1634 IIHGVFGAGKSYLLAVVILFFVQLFEKSeaptignarpwKLLISSSTNVAVDRVLLGLLSlgfENFIRVGSVRKIAKpil 1713
Cdd:cd18078    24 ILFGPPGTGKTVTIIEAILQVVYNLPRS-----------RILVCAPSNSAADLVTSRLHE---SKVLKPGDMVRLNA--- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1714 pyslhagseneseqlkelHALMKEDLTPTERVYVRKSIEQHKLGTNRTLLKQVRVVGVtcaacpfpcMNDLKFPV----- 1788
Cdd:cd18078    87 ------------------VNRFESTVIDARKLYCRLGEDLSKASRHRIVISTCSTAGL---------LYQMGLPVghfth 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1789 VVLDECSQITEPASLLPIARFECE--KLILVGDPKQLPPTIQgSDAAHENGLEQTLFDRL 1846
Cdd:cd18078   140 VFVDEAGQATEPESLIPLGLISSRdgQIILAGDPMQLGPVIK-SRLASAYGLGVSFLERL 198
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
 1785-1827 1.36e-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: 1.36e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 767932266 1785 KFPVVVLDECSQITEPASLLPIARfeCEKLILVGDPKQLPPTI 1827
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 ...
 1631-1861 1.72e-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: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1631 PITIIhGVFGAGKSYLLAVVIlffVQLFEKSEAptignarpwKLLISSSTNVAVDrvllgllsLGFENFIR--VGSVRKI 1708
Cdd:cd18077    23 PVLLI-GPFGTGKTFTLAQAV---KHILQQPET---------RILICTHSNSAAD--------LYIKEYLHpyVETGNPR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1709 AKPILPYsLHAGSENESEQLKELHALMKEDltPTERVYVRKSIEQHklgtnrtllkqvRVVGVTCAACPFPCMNDLK--- 1785
Cdd:cd18077    82 ARPLRVY-YRNRWVKTVHPVVQKYCLIDEH--GTFRMPTREDVMRH------------RVVVVTLSTSQYLCQLDLEpgf 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1786 FPVVVLDECSQITEPASLLPIARFECE-KLILVGDPKQLPPTIQgSDAAHENGLEQTLFDRlcLMGHKP------ILLRT 1858
Cdd:cd18077   147 FTHILLDEAAQAMECEAIMPLALATKStRIVLAGDHMQLSPEVY-SEFARERNLHISLLER--LYEHYPsehpcrILLCE 223


                  ...
gi 767932266 1859 QYR 1861
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. ...
 1782-1825 5.17e-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: 5.17e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 767932266 1782 NDLKFPVVVLDECSQITEP--ASLLPIARFECeKLILVGDPKQLPP 1825
Cdd:cd17933    86 NPLDADLLIVDEASMVDTRlmAALLSAIPAGA-RLILVGDPDQLPS 130
alphaCoV_Nsp13-helicase cd21723
helicase domain of alphacoronavirus non-structural protein 13; This model represents the ...
 1788-2020 7.21e-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: 7.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1788 VVVLDECSQITEPASLLPIARFECEKLILVGDPKQLP-PTIQGSDAAHENGLEQTLFDRLCLMGhKPILLRTQYRCHPAI 1866
Cdd:cd21723   120 IVVVDEVSMCTNYDLSVINQRVSYKHIVYVGDPQQLPaPRTMITRGVLEPKDYNVVTQRMCALG-PDVFLHKCYRCPAEI 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932266 1867 SAIANDLFYKGALMnGVTEIERSpllewlptlCF-YNVKGLEQIERDNSFHNVaeatfTLKLIQSLIASGIAGSMIGVIT 1945
Cdd:cd21723   199 VNTVSELVYENKFK-PVHPESKQ---------CFkIFCKGNVQVDNGSSINRR-----QLDVVKMFLAKNPKWSKAVFIS 263

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767932266 1946 LYKSQMYKLCHLLSavdfhhpdiktVQVSTVDAFQGAEKEIIILScvRTRQVGFIDSEKRMNVALTRGKRHLLIV 2020
Cdd:cd21723   264 PYNSQNYVASRVLG-----------LQIQTVDSSQGSEYDYVIYT--QTSDTAHACNVNRFNVAITRAKKGILCV 325
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 1788-1825 3.26e-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: 3.26e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 767932266 1788 VVVLDECSQITEP--ASLLPIARFECEKLILVGDPKQLPP 1825
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH