NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|34783731|gb|AAH36913|]
View 

AQR protein, partial [Homo sapiens]

Protein Classification

CWF11/aquarius family DEAD/DEAH box helicase( domain architecture ID 13027904)

CWF11/aquarius family DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; similar to Schizosaccharomyces pombe pre-mRNA-splicing factor cwf11 involved in mRNA splicing where it associates with cdc5 and the other cwf proteins as part of the spliceosome

EC:  3.6.4.-
Gene Ontology:  GO:0003676|GO:0004386
PubMed:  20206133

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
 110-258 1.19e-84

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: 262.75  E-value: 1.19e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 110 IFTQLEEFRASE--LLRSGldrskyllvKEAKIIAMTCTHAALKRHDLVKLGFKYDNILMEEAAQILEIETFIPLLLQNP 187
Cdd:cd17935  66 LFEKIMALDIDErhLLRLG---------HGAKIIAMTCTHAALKRGELVELGFKYDNILMEEAAQILEIETFIPLLLQNP 136

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34783731 188 QDGFSRLKRWIMIGDHHQLPPVIKNMAFQKYSNMEQSLFTRFVRVGVPTVDLDAQGRARASLCNLYNWRYK 258
Cdd:cd17935 137 EDGPNRLKRLIMIGDHHQLPPVIKNMAFQKYSNMEQSLFTRLVRLGVPTVDLDAQGRARASISSLYNWRYK 207
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
 246-429 3.85e-50

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: 171.26  E-value: 3.85e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 246 RASLCNLYNWRYKNLGNLPHVQLLP-EFSTANAGLLYDFQLINVEdfqGVGESEPNPYFYQNLGEAEYVVALFMYMCLLG 324
Cdd:cd18808   2 HPEISEFPSKLFYEGKLKAGVSVAArLNPPPLPGPSKPLVFVDVS---GGEEREESGTSKSNEAEAELVVELVKYLLKSG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 325 YPADKISILTTYNGQKHLIRDIINRRCGNNPLIgrpnKVTTVDRFQGQQNDYILLSLVRTR----AVGHLRDVRRLVVAM 400
Cdd:cd18808  79 VKPSSIGVITPYRAQVALIRELLRKRGGLLEDV----EVGTVDNFQGREKDVIILSLVRSNesggSIGFLSDPRRLNVAL 154

                       170       180
                ....*....|....*....|....*....
gi 34783731 401 SRARLGLYIFARVSLFQNCFELTPAFSQL 429
Cdd:cd18808 155 TRAKRGLIIVGNPDTLSKDPLWKKLLEYL 183
 
Name Accession Description Interval E-value
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
 110-258 1.19e-84

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: 262.75  E-value: 1.19e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 110 IFTQLEEFRASE--LLRSGldrskyllvKEAKIIAMTCTHAALKRHDLVKLGFKYDNILMEEAAQILEIETFIPLLLQNP 187
Cdd:cd17935  66 LFEKIMALDIDErhLLRLG---------HGAKIIAMTCTHAALKRGELVELGFKYDNILMEEAAQILEIETFIPLLLQNP 136

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34783731 188 QDGFSRLKRWIMIGDHHQLPPVIKNMAFQKYSNMEQSLFTRFVRVGVPTVDLDAQGRARASLCNLYNWRYK 258
Cdd:cd17935 137 EDGPNRLKRLIMIGDHHQLPPVIKNMAFQKYSNMEQSLFTRLVRLGVPTVDLDAQGRARASISSLYNWRYK 207
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
 246-429 3.85e-50

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: 171.26  E-value: 3.85e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 246 RASLCNLYNWRYKNLGNLPHVQLLP-EFSTANAGLLYDFQLINVEdfqGVGESEPNPYFYQNLGEAEYVVALFMYMCLLG 324
Cdd:cd18808   2 HPEISEFPSKLFYEGKLKAGVSVAArLNPPPLPGPSKPLVFVDVS---GGEEREESGTSKSNEAEAELVVELVKYLLKSG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 325 YPADKISILTTYNGQKHLIRDIINRRCGNNPLIgrpnKVTTVDRFQGQQNDYILLSLVRTR----AVGHLRDVRRLVVAM 400
Cdd:cd18808  79 VKPSSIGVITPYRAQVALIRELLRKRGGLLEDV----EVGTVDNFQGREKDVIILSLVRSNesggSIGFLSDPRRLNVAL 154

                       170       180
                ....*....|....*....|....*....
gi 34783731 401 SRARLGLYIFARVSLFQNCFELTPAFSQL 429
Cdd:cd18808 155 TRAKRGLIIVGNPDTLSKDPLWKKLLEYL 183
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
105-429 6.36e-37

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 146.81  E-value: 6.36e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 105 RHIKKIFTQLEEFRASELLRSGLDRSKY-----------LLVKEAKIIAMTCthAALKRHDLVKLGfKYDNILMEEAAQI 173
Cdd:COG1112 491 EHPEELEKLIAELREAARLRRALRRELKkrrelrkllwdALLELAPVVGMTP--ASVARLLPLGEG-SFDLVIIDEASQA 567

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 174 LEIETFIPLllqnpqdgfSRLKRWIMIGDHHQLPPVIK--NMAFQKYSNMEQSLFTRFVRV-GVPTVDLDAQGRARASLC 250
Cdd:COG1112 568 TLAEALGAL---------ARAKRVVLVGDPKQLPPVVFgeEAEEVAEEGLDESLLDRLLARlPERGVMLREHYRMHPEII 638

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 251 NLYNWR-YKNlgnlphvQLLPEFSTANAGLLYDFQLINVEDFQGVGESEPNPYFyqNLGEAEYVVALFMYMCLLGYPADK 329
Cdd:COG1112 639 AFSNRLfYDG-------KLVPLPSPKARRLADPDSPLVFIDVDGVYERRGGSRT--NPEEAEAVVELVRELLEDGPDGES 709

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 330 ISILTTYNGQKHLIRDIINRRCGNNpliGRPNKVTTVDRFQGQQNDYILLSLVRTRAVGHLR-------DVRRLVVAMSR 402
Cdd:COG1112 710 IGVITPYRAQVALIRELLREALGDG---LEPVFVGTVDRFQGDERDVIIFSLVYSNDEDVPRnfgflngGPRRLNVAVSR 786

                       330       340
                ....*....|....*....|....*..
gi 34783731 403 ARLGLYIFARVSLFQNcFELTPAFSQL 429
Cdd:COG1112 787 ARRKLIVVGSRELLDS-DPSTPALKRL 812
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 221-409 4.54e-29

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: 114.18  E-value: 4.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731   221 MEQSLFTRFVRVG-VPTVDLDAQGRARASLCNLYN-WRYKN-LGNLPHVQLLPEFSTANAGL-LYDFQLINVEDFQGVGE 296
Cdd:pfam13087   1 LDRSLFERLQELGpSAVVMLDTQYRMHPEIMEFPSkLFYGGkLKDGPSVAERPLPDDFHLPDpLGPLVFIDVDGSEEEES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731   297 SEPNPYFyqNLGEAEYVVALFMYMCLLGYPADK-ISILTTYNGQKHLIRDIINRRCGNNPLIgrpnKVTTVDRFQGQQND 375
Cdd:pfam13087  81 DGGTSYS--NEAEAELVVQLVEKLIKSGPEEPSdIGVITPYRAQVRLIRKLLKRKLGGKLEI----EVNTVDGFQGREKD 154

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 34783731   376 YILLSLVRTRA---VGHLRDVRRLVVAMSRARLGLYI 409
Cdd:pfam13087 155 VIIFSCVRSNEkggIGFLSDPRRLNVALTRAKRGLII 191
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
 91-418 3.58e-25

DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273041 [Multi-domain]  Cd Length: 636  Bit Score: 110.29  E-value: 3.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731    91 RSYEEDM-EIAEGCFRHIKKiFTQLEEFRASE-LLRSGLDRSKYLLVKEAKIIAM---TCTHAALKR-HDLVK------- 157
Cdd:TIGR00376 260 ADIREKIdELIEERNKKTKP-SPQKRRGLSDIkILRKALKKREARGIESLKIASMaewIETNKSIDRlLKLLPeseerim 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731   158 -------------------LGFKYDNILMEEAAQILEIETFIPLLlqnpqdgfsRLKRWIMIGDHHQLPPVIKNmafQKY 218
Cdd:TIGR00376 339 neilaesdatnsmagseilNGQYFDVAVIDEASQAMEPSCLIPLL---------KARKLILAGDHKQLPPTILS---HDA 406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731   219 SNMEQSLFTRFV-RVGVPTVDLDAQGRARASLC-----NLYNWRYK---NLGNLPHVQLLPEFSTANAGLLYD---FQLI 286
Cdd:TIGR00376 407 EELSLTLFERLIkEYPERSRTLNVQYRMNQKIMefpsrEFYNGKLTaheSVANILLRDLPKVEATESEDDLETgipLLFI 486

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731   287 NVEDFQGVGESEPNPYFYQNLGEAEYVVALFMYMCLLGYPADKISILTTYNGQKHLIRDIINRRcgnNPLIgrpnKVTTV 366
Cdd:TIGR00376 487 DTSGCELFELKEADSTSKYNPGEAELVSEIIQALVKMGVPANDIGVITPYDAQVDLLRQLLEHR---HIDI----EVSSV 559

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 34783731   367 DRFQGQQNDYILLSLVRT---RAVGHLRDVRRLVVAMSRARLGLYIFARVSLFQN 418
Cdd:TIGR00376 560 DGFQGREKEVIIISFVRSnrkGEVGFLKDLRRLNVALTRARRKLIVIGDSRTLSN 614
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 107-213 1.70e-12

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: 67.75  E-value: 1.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731   107 IKKIFTQLEEFRASeLLRSGLDrskyllvkEAKIIAMTCTHAAlkRHDLVKLgFKYDNILMEEAAQILEIETFIPLLLqn 186
Cdd:pfam13086 162 RKELRKELRRREQS-LEREILD--------EAQIVCSTLSGAG--SRLLSSL-ANFDVVIIDEAAQALEPSTLIPLLR-- 227

                          90       100
                  ....*....|....*....|....*..
gi 34783731   187 pqdgfsRLKRWIMIGDHHQLPPVIKNM 213
Cdd:pfam13086 228 ------GPKKVVLVGDPKQLPPTVISK 248
 
Name Accession Description Interval E-value
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
 110-258 1.19e-84

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: 262.75  E-value: 1.19e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 110 IFTQLEEFRASE--LLRSGldrskyllvKEAKIIAMTCTHAALKRHDLVKLGFKYDNILMEEAAQILEIETFIPLLLQNP 187
Cdd:cd17935  66 LFEKIMALDIDErhLLRLG---------HGAKIIAMTCTHAALKRGELVELGFKYDNILMEEAAQILEIETFIPLLLQNP 136

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34783731 188 QDGFSRLKRWIMIGDHHQLPPVIKNMAFQKYSNMEQSLFTRFVRVGVPTVDLDAQGRARASLCNLYNWRYK 258
Cdd:cd17935 137 EDGPNRLKRLIMIGDHHQLPPVIKNMAFQKYSNMEQSLFTRLVRLGVPTVDLDAQGRARASISSLYNWRYK 207
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
 246-429 3.85e-50

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: 171.26  E-value: 3.85e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 246 RASLCNLYNWRYKNLGNLPHVQLLP-EFSTANAGLLYDFQLINVEdfqGVGESEPNPYFYQNLGEAEYVVALFMYMCLLG 324
Cdd:cd18808   2 HPEISEFPSKLFYEGKLKAGVSVAArLNPPPLPGPSKPLVFVDVS---GGEEREESGTSKSNEAEAELVVELVKYLLKSG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 325 YPADKISILTTYNGQKHLIRDIINRRCGNNPLIgrpnKVTTVDRFQGQQNDYILLSLVRTR----AVGHLRDVRRLVVAM 400
Cdd:cd18808  79 VKPSSIGVITPYRAQVALIRELLRKRGGLLEDV----EVGTVDNFQGREKDVIILSLVRSNesggSIGFLSDPRRLNVAL 154

                       170       180
                ....*....|....*....|....*....
gi 34783731 401 SRARLGLYIFARVSLFQNCFELTPAFSQL 429
Cdd:cd18808 155 TRAKRGLIIVGNPDTLSKDPLWKKLLEYL 183
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
105-429 6.36e-37

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 146.81  E-value: 6.36e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 105 RHIKKIFTQLEEFRASELLRSGLDRSKY-----------LLVKEAKIIAMTCthAALKRHDLVKLGfKYDNILMEEAAQI 173
Cdd:COG1112 491 EHPEELEKLIAELREAARLRRALRRELKkrrelrkllwdALLELAPVVGMTP--ASVARLLPLGEG-SFDLVIIDEASQA 567

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 174 LEIETFIPLllqnpqdgfSRLKRWIMIGDHHQLPPVIK--NMAFQKYSNMEQSLFTRFVRV-GVPTVDLDAQGRARASLC 250
Cdd:COG1112 568 TLAEALGAL---------ARAKRVVLVGDPKQLPPVVFgeEAEEVAEEGLDESLLDRLLARlPERGVMLREHYRMHPEII 638

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 251 NLYNWR-YKNlgnlphvQLLPEFSTANAGLLYDFQLINVEDFQGVGESEPNPYFyqNLGEAEYVVALFMYMCLLGYPADK 329
Cdd:COG1112 639 AFSNRLfYDG-------KLVPLPSPKARRLADPDSPLVFIDVDGVYERRGGSRT--NPEEAEAVVELVRELLEDGPDGES 709

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 330 ISILTTYNGQKHLIRDIINRRCGNNpliGRPNKVTTVDRFQGQQNDYILLSLVRTRAVGHLR-------DVRRLVVAMSR 402
Cdd:COG1112 710 IGVITPYRAQVALIRELLREALGDG---LEPVFVGTVDRFQGDERDVIIFSLVYSNDEDVPRnfgflngGPRRLNVAVSR 786

                       330       340
                ....*....|....*....|....*..
gi 34783731 403 ARLGLYIFARVSLFQNcFELTPAFSQL 429
Cdd:COG1112 787 ARRKLIVVGSRELLDS-DPSTPALKRL 812
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 221-409 4.54e-29

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: 114.18  E-value: 4.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731   221 MEQSLFTRFVRVG-VPTVDLDAQGRARASLCNLYN-WRYKN-LGNLPHVQLLPEFSTANAGL-LYDFQLINVEDFQGVGE 296
Cdd:pfam13087   1 LDRSLFERLQELGpSAVVMLDTQYRMHPEIMEFPSkLFYGGkLKDGPSVAERPLPDDFHLPDpLGPLVFIDVDGSEEEES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731   297 SEPNPYFyqNLGEAEYVVALFMYMCLLGYPADK-ISILTTYNGQKHLIRDIINRRCGNNPLIgrpnKVTTVDRFQGQQND 375
Cdd:pfam13087  81 DGGTSYS--NEAEAELVVQLVEKLIKSGPEEPSdIGVITPYRAQVRLIRKLLKRKLGGKLEI----EVNTVDGFQGREKD 154

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 34783731   376 YILLSLVRTRA---VGHLRDVRRLVVAMSRARLGLYI 409
Cdd:pfam13087 155 VIIFSCVRSNEkggIGFLSDPRRLNVALTRAKRGLII 191
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
 91-418 3.58e-25

DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273041 [Multi-domain]  Cd Length: 636  Bit Score: 110.29  E-value: 3.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731    91 RSYEEDM-EIAEGCFRHIKKiFTQLEEFRASE-LLRSGLDRSKYLLVKEAKIIAM---TCTHAALKR-HDLVK------- 157
Cdd:TIGR00376 260 ADIREKIdELIEERNKKTKP-SPQKRRGLSDIkILRKALKKREARGIESLKIASMaewIETNKSIDRlLKLLPeseerim 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731   158 -------------------LGFKYDNILMEEAAQILEIETFIPLLlqnpqdgfsRLKRWIMIGDHHQLPPVIKNmafQKY 218
Cdd:TIGR00376 339 neilaesdatnsmagseilNGQYFDVAVIDEASQAMEPSCLIPLL---------KARKLILAGDHKQLPPTILS---HDA 406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731   219 SNMEQSLFTRFV-RVGVPTVDLDAQGRARASLC-----NLYNWRYK---NLGNLPHVQLLPEFSTANAGLLYD---FQLI 286
Cdd:TIGR00376 407 EELSLTLFERLIkEYPERSRTLNVQYRMNQKIMefpsrEFYNGKLTaheSVANILLRDLPKVEATESEDDLETgipLLFI 486

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731   287 NVEDFQGVGESEPNPYFYQNLGEAEYVVALFMYMCLLGYPADKISILTTYNGQKHLIRDIINRRcgnNPLIgrpnKVTTV 366
Cdd:TIGR00376 487 DTSGCELFELKEADSTSKYNPGEAELVSEIIQALVKMGVPANDIGVITPYDAQVDLLRQLLEHR---HIDI----EVSSV 559

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 34783731   367 DRFQGQQNDYILLSLVRT---RAVGHLRDVRRLVVAMSRARLGLYIFARVSLFQN 418
Cdd:TIGR00376 560 DGFQGREKEVIIISFVRSnrkGEVGFLKDLRRLNVALTRARRKLIVIGDSRTLSN 614
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
 140-243 1.59e-24

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


Pssm-ID: 438706 [Multi-domain]  Cd Length: 121  Bit Score: 98.71  E-value: 1.59e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 140 IIAMTCTHAALKRhdlvklgfkYDNILMEEAAQILEIETFIPlllqnpQDGFSRLKRWIMIGDHHQLPPVIKNMAFQKYS 219
Cdd:cd17914  34 ILLVTPTNKAAAQ---------LDNILVDEAAQILEPETSRL------IDLALDQGRVILVGDHDQLGPVWRGAVLAKIC 98

                        90       100
                ....*....|....*....|....
gi 34783731 220 NmEQSLFTRFVRVGVPTVDLDAQG 243
Cdd:cd17914  99 N-EQSLFTRLVRLGVSLIRLQVQY 121
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
 101-244 9.23e-20

DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in transcription, neurogenesis, and antiviral response. SEXT is an R-loop-associated protein that is thought to function as an RNA/DNA helicase. R-loops consist of RNA/DNA hybrids, formed during transcription when nascent RNA hybridizes to the DNA template strand, displacing the non-template DNA strand. Mutations in SETX are linked to two neurodegenerative disorders: ataxia with oculomotor apraxia type 2 (AOA2) and amyotrophic lateral sclerosis type 4 (ALS4). S. cerevisiae homolog splicing endonuclease 1 (Sen1) is an exclusively nuclear protein, important for nucleolar organization. S. cerevisiae Sen1 and its ortholog, the Schizosaccharomyces pombe Sen1, share conserved domains and belong to the family I class of helicases. Both proteins translocate 5' to 3' and unwind both DNA and RNA duplexes and also RNA/DNA hybrids in vitro. SETX is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438712 [Multi-domain]  Cd Length: 218  Bit Score: 88.04  E-value: 9.23e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 101 EGCFRHIKKIFTQLE-EFRASELLRSGLDRSKYLLVKEAKIIAmtCTHAALKRHDLVKLGFKYDNILMEEAAQILEIETF 179
Cdd:cd18042  85 EIVLRLLSEGFLDGDgRSYKPNVVRVGRQELRASILNEADIVC--TTLSSSGSDLLESLPRGFDTVIIDEAAQAVELSTL 162

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34783731 180 IPLLLqnpqdgfsRLKRWIMIGDHHQLPPVIKNMAFQKYsNMEQSLFTRFVRVGVPTVDLDAQGR 244
Cdd:cd18042 163 IPLRL--------GCKRLILVGDPKQLPATVFSKVAQKL-GYDRSLFERLQLAGYPVLMLTTQYR 218
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
 138-242 1.61e-14

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: 71.81  E-value: 1.61e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 138 AKIIAMTCTHAALKRHDLVKLGFKYdnILMEEAAQILE--IETFIPlllqnpqdgfSRLKRWIMIGDHHQLPPVIKNMAF 215
Cdd:cd17936  82 ARVIGMTTTGAAKYRELLQALGPKV--VIVEEAAEVLEahILAALT----------PSTEHLILIGDHKQLRPKVNVYEL 149

                        90       100
                ....*....|....*....|....*....
gi 34783731 216 Q--KYsNMEQSLFTRFVRVGVPTVDLDAQ 242
Cdd:cd17936 150 TakKY-NLDVSLFERLVKNGLPFVTLNVQ 177
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 107-213 1.70e-12

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: 67.75  E-value: 1.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731   107 IKKIFTQLEEFRASeLLRSGLDrskyllvkEAKIIAMTCTHAAlkRHDLVKLgFKYDNILMEEAAQILEIETFIPLLLqn 186
Cdd:pfam13086 162 RKELRKELRRREQS-LEREILD--------EAQIVCSTLSGAG--SRLLSSL-ANFDVVIIDEAAQALEPSTLIPLLR-- 227

                          90       100
                  ....*....|....*....|....*..
gi 34783731   187 pqdgfsRLKRWIMIGDHHQLPPVIKNM 213
Cdd:pfam13086 228 ------GPKKVVLVGDPKQLPPTVISK 248
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
 138-244 5.17e-12

DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), coronavirus Nsp13, and similar proteins. They belong to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438708 [Multi-domain]  Cd Length: 121  Bit Score: 63.02  E-value: 5.17e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 138 AKIIAMTCTHAALKRHDLVklgfkydniLMEEAAQILEIETFIPLLlqnpqdgfsRLKRWIMIGDHHQLPPVIKNMAFQK 217
Cdd:cd17934  30 KRVLVTAQSNVAVDNVDVV---------IIDEASQITEPELLIALI---------RAKKVVLVGDPKQLPPVVQEDHAAL 91

                        90       100       110
                ....*....|....*....|....*....|
gi 34783731 218 Y---SNMEQSLFTRFVRVGVPTVDLDAQGR 244
Cdd:cd17934  92 LglsFILSLLLLFRLLLPGSPKVMLDTQYR 121
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
 136-253 1.08e-11

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: 64.95  E-value: 1.08e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 136 KEAKIIAMTCTHAALkrhdLVKLGFK---YDNILMEEAAQILEIETFIPLLLQNPQDGfsrlkRWIMIGDHHQLPPVIKN 212
Cdd:cd18038 118 KKYRIVVCTLMTAGR----LVQAGVPnghFTHIFIDEAGQATEPEALIPLSELASKNT-----QIVLAGDPKQLGPVVRS 188

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 34783731 213 MAFQKYsNMEQSLFTRFVRVGVPTVDLDAQGRARASLCNLY 253
Cdd:cd18038 189 PLARKY-GLGKSLLERLMERPLYYKDGEYNPSYITKLLKNY 228
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
 106-244 1.18e-11

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: 64.96  E-value: 1.18e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 106 HIKKIFTQLEEFRASELLRSGLDRSKYL-------LVKEAKIIAMTCTHAALKRhdLVKlgFKYDNILMEEAAQILEIET 178
Cdd:cd18039 102 AEKLELLKLLKLETGELSSADEKRYRKLkrkaereLLRNADVICCTCVGAGDPR--LSK--MKFRTVLIDEATQATEPEC 177

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34783731 179 FIPLLLQnpqdgfsrLKRWIMIGDHHQLPPVIKNMAFQKYSnMEQSLFTRFVRVGVPTVDLDAQGR 244
Cdd:cd18039 178 LIPLVHG--------AKQVILVGDHCQLGPVVMCKKAAKAG-LSQSLFERLVQLGIRPIRLQVQYR 234
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
 107-229 4.61e-11

DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5-3 helicase, and endonuclease activities, and is involved in DNA replication and DNA repair in the nucleus and mitochondrion. It is involved in Okazaki fragment processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. It is also involved in 5-end resection of DNA during double-strand break (DSB) repair; it is recruited by BLM and mediates the cleavage of 5-ssDNA, while the 3-ssDNA cleavage is prevented by the presence of RPA. DNA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350799 [Multi-domain]  Cd Length: 203  Bit Score: 62.25  E-value: 4.61e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 107 IKKIFTQLEEFRASELLRSGLDRSKY-LLVKEAKIIAMTC---THAALKRHdlvklgfKYDNILMEEAAQILEIETFIPL 182
Cdd:cd18041  78 LKKIHPDVQEFTLEAILKSCKSVEELeSKYESVSVVATTClgiNHPIFRRR-------TFDYCIVDEASQITLPICLGPL 150

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 34783731 183 LLQnpqdgfsrlKRWIMIGDHHQLPPVIKNMAFQKySNMEQSLFTRF 229
Cdd:cd18041 151 RLA---------KKFVLVGDHYQLPPLVKSREARE-LGMDESLFKRL 187
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
 122-237 1.19e-10

DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, or IGHMBP2) is a 5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction. It is a DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence (5'-GGGCT-3') related to the immunoglobulin mu chain switch region. The IGHMBP2 gene is responsible for Charcot-Marie-Tooth disease (CMT) type 2S and spinal muscular atrophy with respiratory distress type 1 (SMARD1). It is also thought to play a role in frontotemporal dementia (FTD) with amyotrophic lateral sclerosis (ALS) and major depressive disorder (MDD). SMUBP2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350802 [Multi-domain]  Cd Length: 191  Bit Score: 61.09  E-value: 1.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 122 LLRSGLDRSKYLLVkEAKIIAMTCTHAAlkrHDLVKLGFKYDNILMEEAAQILEIETFIPLLlqnpqdgfsRLKRWIMIG 201
Cdd:cd18044  81 LLESVLDHSLDALV-AAQVVLATNTGAG---SRQLLPNELFDVVVIDEAAQALEASCWIPLL---------KARRCILAG 147

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 34783731 202 DHHQLPPVIKNMAFQKYsNMEQSLFTRFVRVGVPTV 237
Cdd:cd18044 148 DHKQLPPTILSDKAARG-GLGVTLFERLVNLYGESV 182
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
 329-409 9.02e-10

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: 55.52  E-value: 9.02e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 329 KISILTTYNGQKHLIRDIInRRCGNNPLIGRPNKVTTVDRFQGQQNDYILLSLVRTravgHLRDVRRLVVAMSRARLGLY 408
Cdd:cd18786  12 KGVVLTPYHRDRAYLNQYL-QGLSLDEFDLQLVGAITIDSSQGLTFDVVTLYLPTA----NSLTPRRLYVALTRARKRLV 86


                .
gi 34783731 409 I 409
Cdd:cd18786  87 I 87
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
 118-229 5.40e-09

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: 57.53  E-value: 5.40e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 118 RASELLRSG-LDRSKYLLVKEAK-------IIAMTCTHAALKRhdlVKLGFKYDNILMEEAAQILEIETFIPLLlqnpqd 189
Cdd:cd18040 150 RTQEKITEEdIKTYKILIWEARFeeletvdVILCTCSEAASQK---MRTHANVKQCIVDECGMCTEPESLIPIV------ 220

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 34783731 190 GFSRLKRWIMIGDHHQLPPVIKNMAFQKYSnMEQSLFTRF 229
Cdd:cd18040 221 SAPRAEQVVLIGDHKQLRPVVQNKEAQKLG-LGRSLFERY 259
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
 135-228 1.36e-05

DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. HELZ is a member of the family I class of RNA helicases of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350835 [Multi-domain]  Cd Length: 226  Bit Score: 46.71  E-value: 1.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 135 VKEAKIIAMT-CTHAALKRHDLVKLGFKYdnILMEEAAQILEIETFIPLLLQNpqdgfsRLKRWIMIGDHHQLPPVIKNm 213
Cdd:cd18077 121 VMRHRVVVVTlSTSQYLCQLDLEPGFFTH--ILLDEAAQAMECEAIMPLALAT------KSTRIVLAGDHMQLSPEVYS- 191

                        90
                ....*....|....*
gi 34783731 214 AFQKYSNMEQSLFTR 228
Cdd:cd18077 192 EFARERNLHISLLER 206
DEXXQc_HELZ2-N cd18076
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
 146-228 3.13e-04

N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB, and RXRA. It belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350834 [Multi-domain]  Cd Length: 230  Bit Score: 42.57  E-value: 3.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34783731 146 THAALKRHDLVKLGFkYDNILMEEAAQILEIETFIPLLLQNPQdgfsrlKRWIMIGDHHQLPPviKNMAFQKYSNMEQSL 225
Cdd:cd18076 132 TTTAMAFNLHVLSGF-FTHIFIDEAAQMLECEALIPLSYAGPK------TRVVLAGDHMQMTP--KLFSVADYNRANHTL 202


                ...
gi 34783731 226 FTR 228
Cdd:cd18076 203 LNR 205
UvrD_C_2 pfam13538
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety ...
 363-409 8.90e-04

UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety of helicase enzymes. This domain has a AAA-like structural fold.


Pssm-ID: 463913 [Multi-domain]  Cd Length: 52  Bit Score: 37.55  E-value: 8.90e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 34783731   363 VTTVDRFQGQQNDYILLSLVRTRAVGHLRDVRRLV-VAMSRARLGLYI 409
Cdd:pfam13538   4 ALTVHKAQGSEFPAVFLVDPDLTAHYHSMLRRRLLyTAVTRARKKLVL 51
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
 138-211 4.13e-03

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: 39.27  E-value: 4.13e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34783731 138 AKIIAMTCTHAALkrhdLVKLGFK---YDNILMEEAAQILEIETFIPLLLQNPQDGfsrlkRWIMIGDHHQLPPVIK 211
Cdd:cd18078 114 HRIVISTCSTAGL----LYQMGLPvghFTHVFVDEAGQATEPESLIPLGLISSRDG-----QIILAGDPMQLGPVIK 181
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
 161-210 4.50e-03

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: 37.56  E-value: 4.50e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 34783731 161 KYDNILMEEAAQIlEIETFIPLLLqnpqdgfsRLKRWIMIGDHHQLPPVI 210
Cdd:cd18043  80 LFDLVIFDEASQI-PIEEALPALF--------RGKQVVVVGDDKQLPPSI 120
 
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