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Conserved domains on  [gi|530420825|ref|XP_005261980|]
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RNA helicase Mov10l1 isoform X6 [Homo sapiens]

Protein Classification

DEAD/DEAH box helicase; DEAD/DEAH box helicase family protein( domain architecture ID 13030947)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA, with similarity to RNA helicase Aquarius; DEAD/DEAH box containing ATP-dependent helicase family protein may catalyze the unwinding of DNA or RNA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
 724-953 2.68e-156

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: 465.31  E-value: 2.68e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  724 VLNENQKLAVKRILSGDCRPLPYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAADLVCLRLHESKVLQPAT 803
Cdd:cd18078     1 DLNELQKEAVKRILGGECRPLPYILFGPPGTGKTVTIIEAILQVVYNLPRSRILVCAPSNSAADLVTSRLHESKVLKPGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  804 MVRVNATCRFEEIVIDAVKPYCRDGEDIWKASRFRIIITTCSSSGLFYQIGVRVGHFTHVFVDEAGQASEPECLIPLGLM 883
Cdd:cd18078    81 MVRLNAVNRFESTVIDARKLYCRLGEDLSKASRHRIVISTCSTAGLLYQMGLPVGHFTHVFVDEAGQATEPESLIPLGLI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  884 SDISGQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERLMSRPAYQRDENAFGACGAHNPLLVTKLVKNYR 953
Cdd:cd18078   161 SSRDGQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLMNRPLYLRDPNRFGESGGYNPLLVTKLVDNYR 230
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
 954-1144 2.52e-61

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: 207.47  E-value: 2.52e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  954 SHEALLMLPSRLFYHRELEVCADptvVTSLLGWEKLPKKGFPLIFHGVRGSEAREGKSPSWFNPAEAVQVLRYCCLLahs 1033
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGVS---VAARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYL--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825 1034 ISSQVSASDIGVITPYRKQVEKIRILLRNV--DLMDIKVGSVEEFQGQEYLVIIISTVRSNEDRFEddryfLGFLSNSKR 1111
Cdd:cd18808    75 LKSGVKPSSIGVITPYRAQVALIRELLRKRggLLEDVEVGTVDNFQGREKDVIILSLVRSNESGGS-----IGFLSDPRR 149

                         170       180       190
                  ....*....|....*....|....*....|...
gi 530420825 1112 FNVAITRPKALLIVLGNPHVLVRDPCFGALLEY 1144
Cdd:cd18808   150 LNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEY 182
 
Name Accession Description Interval E-value
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
 724-953 2.68e-156

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: 465.31  E-value: 2.68e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  724 VLNENQKLAVKRILSGDCRPLPYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAADLVCLRLHESKVLQPAT 803
Cdd:cd18078     1 DLNELQKEAVKRILGGECRPLPYILFGPPGTGKTVTIIEAILQVVYNLPRSRILVCAPSNSAADLVTSRLHESKVLKPGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  804 MVRVNATCRFEEIVIDAVKPYCRDGEDIWKASRFRIIITTCSSSGLFYQIGVRVGHFTHVFVDEAGQASEPECLIPLGLM 883
Cdd:cd18078    81 MVRLNAVNRFESTVIDARKLYCRLGEDLSKASRHRIVISTCSTAGLLYQMGLPVGHFTHVFVDEAGQATEPESLIPLGLI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  884 SDISGQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERLMSRPAYQRDENAFGACGAHNPLLVTKLVKNYR 953
Cdd:cd18078   161 SSRDGQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLMNRPLYLRDPNRFGESGGYNPLLVTKLVDNYR 230
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
 954-1144 2.52e-61

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: 207.47  E-value: 2.52e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  954 SHEALLMLPSRLFYHRELEVCADptvVTSLLGWEKLPKKGFPLIFHGVRGSEAREGKSPSWFNPAEAVQVLRYCCLLahs 1033
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGVS---VAARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYL--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825 1034 ISSQVSASDIGVITPYRKQVEKIRILLRNV--DLMDIKVGSVEEFQGQEYLVIIISTVRSNEDRFEddryfLGFLSNSKR 1111
Cdd:cd18808    75 LKSGVKPSSIGVITPYRAQVALIRELLRKRggLLEDVEVGTVDNFQGREKDVIILSLVRSNESGGS-----IGFLSDPRR 149

                         170       180       190
                  ....*....|....*....|....*....|...
gi 530420825 1112 FNVAITRPKALLIVLGNPHVLVRDPCFGALLEY 1144
Cdd:cd18808   150 LNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEY 182
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
834-1144 3.33e-58

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 216.53  E-value: 3.33e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  834 ASRFRIIITTCSSSGLFyqIGVRVGHFTHVFVDEAGQASEPECLIPLGLmsdiSGQIVLAGDPMQLGPViksrlamaygl 913
Cdd:COG1112   532 LELAPVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALAR----AKRVVLVGDPKQLPPV----------- 594

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  914 nvSFLERLMSRPAYQRDENAFGACGAHNPLLVTKLVKNYRSHEALLMLPSRLFYHRELEVCADPTVvtsllgwEKLPKKG 993
Cdd:COG1112   595 --VFGEEAEEVAEEGLDESLLDRLLARLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKA-------RRLADPD 665

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  994 FPLIFHGVRGSEAREGKSpsWFNPAEAVQVLRyccLLAHSISSQVSASDIGVITPYRKQVEKIRILLRN---VDLMDIKV 1070
Cdd:COG1112   666 SPLVFIDVDGVYERRGGS--RTNPEEAEAVVE---LVRELLEDGPDGESIGVITPYRAQVALIRELLREalgDGLEPVFV 740

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530420825 1071 GSVEEFQGQEYLVIIISTVRSNEdrfEDDRYFLGFLSNS-KRFNVAITRPKALLIVLGNPHVLVRDP---CFGALLEY 1144
Cdd:COG1112   741 GTVDRFQGDERDVIIFSLVYSND---EDVPRNFGFLNGGpRRLNVAVSRARRKLIVVGSRELLDSDPstpALKRLLEY 815
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
 717-1151 2.84e-57

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: 210.44  E-value: 2.84e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825   717 KMEFFNPVLNENQKLAVKRILSGDCRplpYILFGPPGTGKTVTIIEAVLQVhfALPDSRILVCAPSNSAAD--------- 787
Cdd:TIGR00376  150 DFQFFDPNLNESQKEAVLFALSSKDL---FLIHGPPGTGKTRTVVELIRQL--VKRGLRVLVTAPSNIAVDnllerlalc 224

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825   788 -LVCLRL-HESKVLQ-------PATMVRVNATCRFEEIV--IDAV----------KPYCRDG------------------ 828
Cdd:TIGR00376  225 dQKIVRLgHPARLLKsnkqhslDYLIENHPKYQIVADIRekIDELieernkktkpSPQKRRGlsdikilrkalkkrearg 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825   829 -EDIWKASRFRIIITTCSSSGLF---YQIGVRVGH----------------------FTHVFVDEAGQASEPECLIPLgl 882
Cdd:TIGR00376  305 iESLKIASMAEWIETNKSIDRLLkllPESEERIMNeilaesdatnsmagseilngqyFDVAVIDEASQAMEPSCLIPL-- 382

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825   883 msdISGQ-IVLAGDPMQLGPVIKSRlaMAYGLNVSFLERLMSRpayqrdenafgacgahNPLLVTKLVKNYRSHEALLML 961
Cdd:TIGR00376  383 ---LKARkLILAGDHKQLPPTILSH--DAEELSLTLFERLIKE----------------YPERSRTLNVQYRMNQKIMEF 441

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825   962 PSRLFYHRELEvcADPTVVTSLLgwEKLPKK-----------GFPLIF---HGVRGSEAREGKSPSWFNPAEAVQVLRYC 1027
Cdd:TIGR00376  442 PSREFYNGKLT--AHESVANILL--RDLPKVeateseddletGIPLLFidtSGCELFELKEADSTSKYNPGEAELVSEII 517

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  1028 CLLahsISSQVSASDIGVITPYRKQVEKIRILLRNvDLMDIKVGSVEEFQGQEYLVIIISTVRSNEDRfeddryFLGFLS 1107
Cdd:TIGR00376  518 QAL---VKMGVPANDIGVITPYDAQVDLLRQLLEH-RHIDIEVSSVDGFQGREKEVIIISFVRSNRKG------EVGFLK 587

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 530420825  1108 NSKRFNVAITRPKALLIVLGNPHVLVRDPCFGALLEYSITNGVY 1151
Cdd:TIGR00376  588 DLRRLNVALTRARRKLIVIGDSRTLSNHKFYKRLIEWCKQHGEV 631
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 913-1129 1.38e-54

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: 188.53  E-value: 1.38e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825   913 LNVSFLERLMSrpayqrdenafgacgaHNPLLVTKLVKNYRSHEALLMLPSRLFYHRELEvCADPTVVTSLLGWEKLPKK 992
Cdd:pfam13087    1 LDRSLFERLQE----------------LGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLK-DGPSVAERPLPDDFHLPDP 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825   993 GFPLIFHGVRGSEAREGKS-PSWFNPAEAVQVLRYCCLLAHSISSQvsASDIGVITPYRKQVEKIRILLRNVDLM--DIK 1069
Cdd:pfam13087   64 LGPLVFIDVDGSEEEESDGgTSYSNEAEAELVVQLVEKLIKSGPEE--PSDIGVITPYRAQVRLIRKLLKRKLGGklEIE 141

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  1070 VGSVEEFQGQEYLVIIISTVRSNEDRfeddryFLGFLSNSKRFNVAITRPKALLIVLGNP 1129
Cdd:pfam13087  142 VNTVDGFQGREKDVIIFSCVRSNEKG------GIGFLSDPRRLNVALTRAKRGLIIVGNA 195
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 729-906 7.97e-24

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.


Pssm-ID: 404072 [Multi-domain]  Cd Length: 248  Bit Score: 102.04  E-value: 7.97e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825   729 QKLAVKRILSgdcRPLPYILFGPPGTGKTVTIIEAVLQVHF-----ALPDSRILVCAPSNSAADLVCLRLHESKVLQPAT 803
Cdd:pfam13086    2 QREAIRSALS---SSHFTLIQGPPGTGKTTTIVELIRQLLSypatsAAAGPRILVCAPSNAAVDNILERLLRKGQKYGPK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825   804 MVRVNAtcrfEEIVIDAVKPYCRD-------------------------------------------------------- 827
Cdd:pfam13086   79 IVRIGH----PAAISEAVLPVSLDylvesklnneedaqivkdiskeleklakalrafekeiivekllksrnkdkskleqe 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825   828 -----------GEDIWKASRF---------RIIITTCSSSG---LFYQIGVRVghfthVFVDEAGQASEPECLIPLglms 884
Cdd:pfam13086  155 rrklrserkelRKELRRREQSlereildeaQIVCSTLSGAGsrlLSSLANFDV-----VIIDEAAQALEPSTLIPL---- 225

                          250       260
                   ....*....|....*....|....
gi 530420825   885 dISG--QIVLAGDPMQLGPVIKSR 906
Cdd:pfam13086  226 -LRGpkKVVLVGDPKQLPPTVISK 248
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 708-902 4.36e-10

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: 63.84  E-value: 4.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  708 DEIQTPKARKMEFFNPVLNENQKLAVKRILSGdcRPLpYILFGPPGTGKTvTIIEAVLQVHFALPDsRILVCAPSNSAAd 787
Cdd:COG0507   108 ADVEAALAALEPRAGITLSDEQREAVALALTT--RRV-SVLTGGAGTGKT-TTLRALLAALEALGL-RVALAAPTGKAA- 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  788 lvcLRLHESKVLQPATMvrvnatCRFEEIVIDAVKPYCRDGEDIWKAsrfRIIIttcsssglfyqigvrvghfthvfVDE 867
Cdd:COG0507   182 ---KRLSESTGIEARTI------HRLLGLRPDSGRFRHNRDNPLTPA---DLLV-----------------------VDE 226

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 530420825  868 AGqasepecLIPLGLMSDI-------SGQIVLAGDPMQLGPV 902
Cdd:COG0507   227 AS-------MVDTRLMAALlealpraGARLILVGDPDQLPSV 261
DEXDc smart00487
DEAD-like helicases superfamily;
719-868 7.74e-09

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 57.12  E-value: 7.74e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825    719 EFFNPVLNENQKLAVKRILSGDCRplpYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAADLVCLRLheSKV 798
Cdd:smart00487    3 KFGFEPLRPYQKEAIEALLSGLRD---VILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEEL--KKL 77

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530420825    799 LQPATMVRVNATCRFEEividavkpycRDGEDIWKASRFRIIITTCSS-SGLFYQIGVRVGHFTHVFVDEA 868
Cdd:smart00487   78 GPSLGLKVVGLYGGDSK----------REQLRKLESGKTDILVTTPGRlLDLLENDKLSLSNVDLVILDEA 138
 
Name Accession Description Interval E-value
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
 724-953 2.68e-156

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: 465.31  E-value: 2.68e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  724 VLNENQKLAVKRILSGDCRPLPYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAADLVCLRLHESKVLQPAT 803
Cdd:cd18078     1 DLNELQKEAVKRILGGECRPLPYILFGPPGTGKTVTIIEAILQVVYNLPRSRILVCAPSNSAADLVTSRLHESKVLKPGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  804 MVRVNATCRFEEIVIDAVKPYCRDGEDIWKASRFRIIITTCSSSGLFYQIGVRVGHFTHVFVDEAGQASEPECLIPLGLM 883
Cdd:cd18078    81 MVRLNAVNRFESTVIDARKLYCRLGEDLSKASRHRIVISTCSTAGLLYQMGLPVGHFTHVFVDEAGQATEPESLIPLGLI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  884 SDISGQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERLMSRPAYQRDENAFGACGAHNPLLVTKLVKNYR 953
Cdd:cd18078   161 SSRDGQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLMNRPLYLRDPNRFGESGGYNPLLVTKLVDNYR 230
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
 724-953 3.29e-112

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: 349.23  E-value: 3.29e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  724 VLNENQKLAVKRILSGDCRPLPYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAADLVCLRLHeSKVLQPAT 803
Cdd:cd18038     1 ELNDEQKLAVRNIVTGTSRPPPYIIFGPPGTGKTVTLVEAILQVLRQPPEARILVCAPSNSAADLLAERLL-NALVTKRE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  804 MVRVNATCRFEEIVIDAVKPYCRDGED-------IWKASRFRIIITTCSSSGLFYQIGVRVGHFTHVFVDEAGQASEPEC 876
Cdd:cd18038    80 ILRLNAPSRDRASVPPELLPYCNSKAEgtfrlpsLEELKKYRIVVCTLMTAGRLVQAGVPNGHFTHIFIDEAGQATEPEA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530420825  877 LIPLGLMSDISGQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERLMSRPAYQRDenafgacGAHNPLLVTKLVKNYR 953
Cdd:cd18038   160 LIPLSELASKNTQIVLAGDPKQLGPVVRSPLARKYGLGKSLLERLMERPLYYKD-------GEYNPSYITKLLKNYR 229
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
 954-1144 2.52e-61

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: 207.47  E-value: 2.52e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  954 SHEALLMLPSRLFYHRELEVCADptvVTSLLGWEKLPKKGFPLIFHGVRGSEAREGKSPSWFNPAEAVQVLRYCCLLahs 1033
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGVS---VAARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYL--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825 1034 ISSQVSASDIGVITPYRKQVEKIRILLRNV--DLMDIKVGSVEEFQGQEYLVIIISTVRSNEDRFEddryfLGFLSNSKR 1111
Cdd:cd18808    75 LKSGVKPSSIGVITPYRAQVALIRELLRKRggLLEDVEVGTVDNFQGREKDVIILSLVRSNESGGS-----IGFLSDPRR 149

                         170       180       190
                  ....*....|....*....|....*....|...
gi 530420825 1112 FNVAITRPKALLIVLGNPHVLVRDPCFGALLEY 1144
Cdd:cd18808   150 LNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEY 182
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
834-1144 3.33e-58

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 216.53  E-value: 3.33e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  834 ASRFRIIITTCSSSGLFyqIGVRVGHFTHVFVDEAGQASEPECLIPLGLmsdiSGQIVLAGDPMQLGPViksrlamaygl 913
Cdd:COG1112   532 LELAPVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALAR----AKRVVLVGDPKQLPPV----------- 594

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  914 nvSFLERLMSRPAYQRDENAFGACGAHNPLLVTKLVKNYRSHEALLMLPSRLFYHRELEVCADPTVvtsllgwEKLPKKG 993
Cdd:COG1112   595 --VFGEEAEEVAEEGLDESLLDRLLARLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKA-------RRLADPD 665

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  994 FPLIFHGVRGSEAREGKSpsWFNPAEAVQVLRyccLLAHSISSQVSASDIGVITPYRKQVEKIRILLRN---VDLMDIKV 1070
Cdd:COG1112   666 SPLVFIDVDGVYERRGGS--RTNPEEAEAVVE---LVRELLEDGPDGESIGVITPYRAQVALIRELLREalgDGLEPVFV 740

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530420825 1071 GSVEEFQGQEYLVIIISTVRSNEdrfEDDRYFLGFLSNS-KRFNVAITRPKALLIVLGNPHVLVRDP---CFGALLEY 1144
Cdd:COG1112   741 GTVDRFQGDERDVIIFSLVYSND---EDVPRNFGFLNGGpRRLNVAVSRARRKLIVVGSRELLDSDPstpALKRLLEY 815
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
 717-1151 2.84e-57

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: 210.44  E-value: 2.84e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825   717 KMEFFNPVLNENQKLAVKRILSGDCRplpYILFGPPGTGKTVTIIEAVLQVhfALPDSRILVCAPSNSAAD--------- 787
Cdd:TIGR00376  150 DFQFFDPNLNESQKEAVLFALSSKDL---FLIHGPPGTGKTRTVVELIRQL--VKRGLRVLVTAPSNIAVDnllerlalc 224

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825   788 -LVCLRL-HESKVLQ-------PATMVRVNATCRFEEIV--IDAV----------KPYCRDG------------------ 828
Cdd:TIGR00376  225 dQKIVRLgHPARLLKsnkqhslDYLIENHPKYQIVADIRekIDELieernkktkpSPQKRRGlsdikilrkalkkrearg 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825   829 -EDIWKASRFRIIITTCSSSGLF---YQIGVRVGH----------------------FTHVFVDEAGQASEPECLIPLgl 882
Cdd:TIGR00376  305 iESLKIASMAEWIETNKSIDRLLkllPESEERIMNeilaesdatnsmagseilngqyFDVAVIDEASQAMEPSCLIPL-- 382

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825   883 msdISGQ-IVLAGDPMQLGPVIKSRlaMAYGLNVSFLERLMSRpayqrdenafgacgahNPLLVTKLVKNYRSHEALLML 961
Cdd:TIGR00376  383 ---LKARkLILAGDHKQLPPTILSH--DAEELSLTLFERLIKE----------------YPERSRTLNVQYRMNQKIMEF 441

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825   962 PSRLFYHRELEvcADPTVVTSLLgwEKLPKK-----------GFPLIF---HGVRGSEAREGKSPSWFNPAEAVQVLRYC 1027
Cdd:TIGR00376  442 PSREFYNGKLT--AHESVANILL--RDLPKVeateseddletGIPLLFidtSGCELFELKEADSTSKYNPGEAELVSEII 517

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  1028 CLLahsISSQVSASDIGVITPYRKQVEKIRILLRNvDLMDIKVGSVEEFQGQEYLVIIISTVRSNEDRfeddryFLGFLS 1107
Cdd:TIGR00376  518 QAL---VKMGVPANDIGVITPYDAQVDLLRQLLEH-RHIDIEVSSVDGFQGREKEVIIISFVRSNRKG------EVGFLK 587

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 530420825  1108 NSKRFNVAITRPKALLIVLGNPHVLVRDPCFGALLEYSITNGVY 1151
Cdd:TIGR00376  588 DLRRLNVALTRARRKLIVIGDSRTLSNHKFYKRLIEWCKQHGEV 631
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 913-1129 1.38e-54

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: 188.53  E-value: 1.38e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825   913 LNVSFLERLMSrpayqrdenafgacgaHNPLLVTKLVKNYRSHEALLMLPSRLFYHRELEvCADPTVVTSLLGWEKLPKK 992
Cdd:pfam13087    1 LDRSLFERLQE----------------LGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLK-DGPSVAERPLPDDFHLPDP 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825   993 GFPLIFHGVRGSEAREGKS-PSWFNPAEAVQVLRYCCLLAHSISSQvsASDIGVITPYRKQVEKIRILLRNVDLM--DIK 1069
Cdd:pfam13087   64 LGPLVFIDVDGSEEEESDGgTSYSNEAEAELVVQLVEKLIKSGPEE--PSDIGVITPYRAQVRLIRKLLKRKLGGklEIE 141

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  1070 VGSVEEFQGQEYLVIIISTVRSNEDRfeddryFLGFLSNSKRFNVAITRPKALLIVLGNP 1129
Cdd:pfam13087  142 VNTVDGFQGREKDVIIFSCVRSNEKG------GIGFLSDPRRLNVALTRAKRGLIIVGNA 195
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
 725-921 2.71e-39

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: 146.24  E-value: 2.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  725 LNENQKLAVKRILSgdcRPLPYILfGPPGTGKTVTIIEAVLQVHFALPdSRILVCAPSNSAADLVCLRLHES--KVlqpa 802
Cdd:cd18039     2 LNHSQVDAVKTALQ---RPLSLIQ-GPPGTGKTVTSATIVYHLVKQGN-GPVLVCAPSNVAVDQLTEKIHQTglKV---- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  803 tmVRVNATCR-----------FEEIVIDAVKPYCRDGEDIWKA----------SRFR---------------IIITTCSS 846
Cdd:cd18039    73 --VRLCAKSReavespvsflaLHNQVRNLDSAEKLELLKLLKLetgelssadeKRYRklkrkaerellrnadVICCTCVG 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530420825  847 SGlfyqiGVRVG--HFTHVFVDEAGQASEPECLIPLGLMSDisgQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERL 921
Cdd:cd18039   151 AG-----DPRLSkmKFRTVLIDEATQATEPECLIPLVHGAK---QVILVGDHCQLGPVVMCKKAAKAGLSQSLFERL 219
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
 725-953 3.71e-37

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: 138.51  E-value: 3.71e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  725 LNENQKLAVKRILSGdcRPLpYILFGPPGTGKTVTIIEAVLQVhfALPDSRILVCAPSNSAADLVCLRLheskVLQPATM 804
Cdd:cd18044     2 LNDSQKEAVKFALSQ--KDV-ALIHGPPGTGKTTTVVEIILQA--VKRGEKVLACAPSNIAVDNLVERL----VALKVKV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  805 VRVNATCRfeeiVIDAVKPYCRDgediwKASRFRIIITTCSSSGLFyqiGVRVG-HFTHVFVDEAGQASEPECLIPLGLM 883
Cdd:cd18044    73 VRIGHPAR----LLESVLDHSLD-----ALVAAQVVLATNTGAGSR---QLLPNeLFDVVVIDEAAQALEASCWIPLLKA 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  884 SdisgQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERLMSRpayqrdenafgacgaHNPLLVTKLVKNYR 953
Cdd:cd18044   141 R----RCILAGDHKQLPPTILSDKAARGGLGVTLFERLVNL---------------YGESVVRMLTVQYR 191
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
 725-921 6.02e-36

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: 136.08  E-value: 6.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  725 LNENQKLAVKRILSGDCRPLPYILF-GPPGTGKTVTIIEAVLQVhFALPDSRILVCAPSNSAADLVC---LRLHESKVLQ 800
Cdd:cd18077     2 LNAKQKEAVLAITTPLSIQLPPVLLiGPFGTGKTFTLAQAVKHI-LQQPETRILICTHSNSAADLYIkeyLHPYVETGNP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  801 PATMVRVNATCRFEEIVIDAVKPYC---RDG-------EDIWKAsrfRIIITTCSSSGLFYQIGVRVGHFTHVFVDEAGQ 870
Cdd:cd18077    81 RARPLRVYYRNRWVKTVHPVVQKYClidEHGtfrmptrEDVMRH---RVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQ 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 530420825  871 ASEPECLIPLGLMSDiSGQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERL 921
Cdd:cd18077   158 AMECEAIMPLALATK-STRIVLAGDHMQLSPEVYSEFARERNLHISLLERL 207
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
 725-923 7.65e-30

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: 118.47  E-value: 7.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  725 LNENQKLAVKRILSGDcrplPYI--LFGPPGTGKTVTIIEAVLQVHFALPDS-----------------------RILVC 779
Cdd:cd18042     1 LNESQLEAIASALQNS----PGItlIQGPPGTGKTKTIVGILSVLLAGKYRKyyekvkkklrklqrnlnnkkkknRILVC 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  780 APSNSAADLVCLRLHESKVLQPatmvrvNATCRFEEIVidavkpycRDGEDIWKASRFR---IIITTCSSSG-LFYQIGV 855
Cdd:cd18042    77 APSNAAVDEIVLRLLSEGFLDG------DGRSYKPNVV--------RVGRQELRASILNeadIVCTTLSSSGsDLLESLP 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530420825  856 RvgHFTHVFVDEAGQASEPECLIPLGLmsdISGQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERLMS 923
Cdd:cd18042   143 R--GFDTVIIDEAAQAVELSTLIPLRL---GCKRLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQL 205
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
 725-953 2.97e-28

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: 113.10  E-value: 2.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  725 LNENQKLAVKRILSgdCRPLPYILfGPPGTGKTVTIIEAVLQvhFALPDSRILVCAPSNSAADLVCLRLHESKVlqpaTM 804
Cdd:cd18041     2 LNKDQRQAIKKVLN--AKDYALIL-GMPGTGKTTTIAALVRI--LVALGKSVLLTSYTHSAVDNILLKLKKFGV----NF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  805 VRVNATCR----FEEIVIDAVKPYCRDGEDIWKA-SRFRIIITTCSSsglFYQIGVRVGHFTHVFVDEAGQASEPECLIP 879
Cdd:cd18041    73 LRLGRLKKihpdVQEFTLEAILKSCKSVEELESKyESVSVVATTCLG---INHPIFRRRTFDYCIVDEASQITLPICLGP 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530420825  880 LgLMSDisgQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERLmsrpayqrdenafgaCGAHnPLLVTKLVKNYR 953
Cdd:cd18041   150 L-RLAK---KFVLVGDHYQLPPLVKSREARELGMDESLFKRL---------------SEAH-PDAVVQLTIQYR 203
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
 747-927 1.58e-25

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: 102.70  E-value: 1.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  747 ILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAADlvclrlheskvlqpatmvrvnatcrfeeiVIDavkpycr 826
Cdd:cd17934     3 LIQGPPGTGKTTTIAAIVLQLLKGLRGKRVLVTAQSNVAVD-----------------------------NVD------- 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  827 dgediwkasrfriiittcsssglfyqigvrvghftHVFVDEAGQASEPECLIPLGLmsdiSGQIVLAGDPMQLGPVIKSR 906
Cdd:cd17934    47 -----------------------------------VVIIDEASQITEPELLIALIR----AKKVVLVGDPKQLPPVVQED 87

                         170       180
                  ....*....|....*....|.
gi 530420825  907 LAMAYGLNVSFLERLMSRPAY 927
Cdd:cd17934    88 HAALLGLSFILSLLLLFRLLL 108
DEXXQc_HELZ2-N cd18076
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
 724-921 1.91e-24

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: 103.05  E-value: 1.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  724 VLNENQKLAVKRIL---SGDCRPLPYILFGPPGTGKTVTIIEAVLQVhFALPDSRILVCAPSNSAADLVC---LRLHESK 797
Cdd:cd18076     1 AGNNKQQLAFNFIAgkpSEARFVPPLLIYGPFGTGKTFTLAMAALEV-IREPGTKVLICTHTNSAADIYIreyFHPYVDK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  798 VLQPATMVRVNATCRFEEIVIDAVKPYCRDGEDIW--------KASRFRIIITTCSSSglfYQIGVRVGHFTHVFVDEAG 869
Cdd:cd18076    80 GHPEARPLRIKATDRPNAITDPDTITYCCLTKDRQcfrlptrdELDFHNIVITTTAMA---FNLHVLSGFFTHIFIDEAA 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530420825  870 QASEPECLIPLGLMSdISGQIVLAGDPMQLGPVIKSrLAMAYGLNVSFLERL 921
Cdd:cd18076   157 QMLECEALIPLSYAG-PKTRVVLAGDHMQMTPKLFS-VADYNRANHTLLNRL 206
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 729-906 7.97e-24

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.


Pssm-ID: 404072 [Multi-domain]  Cd Length: 248  Bit Score: 102.04  E-value: 7.97e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825   729 QKLAVKRILSgdcRPLPYILFGPPGTGKTVTIIEAVLQVHF-----ALPDSRILVCAPSNSAADLVCLRLHESKVLQPAT 803
Cdd:pfam13086    2 QREAIRSALS---SSHFTLIQGPPGTGKTTTIVELIRQLLSypatsAAAGPRILVCAPSNAAVDNILERLLRKGQKYGPK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825   804 MVRVNAtcrfEEIVIDAVKPYCRD-------------------------------------------------------- 827
Cdd:pfam13086   79 IVRIGH----PAAISEAVLPVSLDylvesklnneedaqivkdiskeleklakalrafekeiivekllksrnkdkskleqe 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825   828 -----------GEDIWKASRF---------RIIITTCSSSG---LFYQIGVRVghfthVFVDEAGQASEPECLIPLglms 884
Cdd:pfam13086  155 rrklrserkelRKELRRREQSlereildeaQIVCSTLSGAGsrlLSSLANFDV-----VIIDEAAQALEPSTLIPL---- 225

                          250       260
                   ....*....|....*....|....
gi 530420825   885 dISG--QIVLAGDPMQLGPVIKSR 906
Cdd:pfam13086  226 -LRGpkKVVLVGDPKQLPPTVISK 248
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
 725-921 1.86e-18

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: 86.81  E-value: 1.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  725 LNENQKLAVKRILsgdCRPLpYILFGPPGTGKTVTII-----------EAVLQVHFALPDSRILVCAPSNSAADLVC--- 790
Cdd:cd18040     2 LNPSQNHAVRTAL---TKPF-TLIQGPPGTGKTVTGVhiaywfakqnrEIQSVSGEGDGGPCVLYCGPSNKSVDVVAell 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  791 LRLHESKVLQ-------------PATMVRVN-------------------------------ATCRFEEIVIDAVKPYCR 826
Cdd:cd18040    78 LKVPGLKILRvyseqietteypiPNEPRHPNkksereskpnselssitlhhrirqpsnphsqQIKAFEARFERTQEKITE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  827 DGED-----IWKASRFR-----IIITTCSSSGlfyqiGVRVGHFTHV---FVDEAGQASEPECLIPLGLMSDISgQIVLA 893
Cdd:cd18040   158 EDIKtykilIWEARFEEletvdVILCTCSEAA-----SQKMRTHANVkqcIVDECGMCTEPESLIPIVSAPRAE-QVVLI 231

                         250       260
                  ....*....|....*....|....*...
gi 530420825  894 GDPMQLGPVIKSRLAMAYGLNVSFLERL 921
Cdd:cd18040   232 GDHKQLRPVVQNKEAQKLGLGRSLFERY 259
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
 725-929 1.18e-13

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: 70.27  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  725 LNENQKLAVKRILSgdcRPLPYILfGPPGTGKT---VTIIEAVLQVHFALPDSRILVCAPSNSAADLVCLRLHESkvlQP 801
Cdd:cd17936     2 LDPSQLEALKHALT---SELALIQ-GPPGTGKTflgVKLVRALLQNQDLSITGPILVVCYTNHALDQFLEGLLDF---GP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  802 ATMVRVNATcrfeeiVIdavkpycrdGEDIWKASRFRiiittcsssGLFYQIGVRVghfthVFVDEAGQASEPE---CLI 878
Cdd:cd17936    75 TKIVRLGAR------VI---------GMTTTGAAKYR---------ELLQALGPKV-----VIVEEAAEVLEAHilaALT 125

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530420825  879 PlglmsDISgQIVLAGDPMQLGPVIKSRL--AMAYGLNVSFLERL------MSRPAYQR 929
Cdd:cd17936   126 P-----STE-HLILIGDHKQLRPKVNVYEltAKKYNLDVSLFERLvknglpFVTLNVQR 178
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
 726-911 2.01e-10

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: 59.52  E-value: 2.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  726 NENQKLAVKRILSGDCrplpYILFGPPGTGKTVTIieAVLQVHFALPDSRILVCAPSNSAADLVclrlheskvlqpatmv 805
Cdd:cd18043     1 DSSQEAAIISARNGKN----VVIQGPPGTGKSQTI--ANIIANALARGKRVLFVSEKKAALDVV---------------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  806 rvnatcrfeeividavkpycrdgediwkasRFRIIITTCSSSGLFYQIGvrVGHFTHVFVDEAGQASePECLIPLGLMSD 885
Cdd:cd18043    59 ------------------------------RFPCWIMSPLSVSQYLPLN--RNLFDLVIFDEASQIP-IEEALPALFRGK 105

                         170       180
                  ....*....|....*....|....*.
gi 530420825  886 isgQIVLAGDPMQLGPVIksRLAMAY 911
Cdd:cd18043   106 ---QVVVVGDDKQLPPSI--LLREHY 126
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 708-902 4.36e-10

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: 63.84  E-value: 4.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  708 DEIQTPKARKMEFFNPVLNENQKLAVKRILSGdcRPLpYILFGPPGTGKTvTIIEAVLQVHFALPDsRILVCAPSNSAAd 787
Cdd:COG0507   108 ADVEAALAALEPRAGITLSDEQREAVALALTT--RRV-SVLTGGAGTGKT-TTLRALLAALEALGL-RVALAAPTGKAA- 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  788 lvcLRLHESKVLQPATMvrvnatCRFEEIVIDAVKPYCRDGEDIWKAsrfRIIIttcsssglfyqigvrvghfthvfVDE 867
Cdd:COG0507   182 ---KRLSESTGIEARTI------HRLLGLRPDSGRFRHNRDNPLTPA---DLLV-----------------------VDE 226

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 530420825  868 AGqasepecLIPLGLMSDI-------SGQIVLAGDPMQLGPV 902
Cdd:COG0507   227 AS-------MVDTRLMAALlealpraGARLILVGDPDQLPSV 261
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
 733-921 1.09e-09

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: 59.75  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  733 VKRILSGdCRPLPYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAADLVclrlheskvlqpatmvrvnatcr 812
Cdd:cd17935    11 IEAIRSG-MQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPNQRTLIVTHSNQALNQL----------------------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  813 FEEIVidavKPYCRDGEDIWKASRFRIIITTCSSSGLFYQIGVRVG-HFTHVFVDEAGQASEPECLIPLGLMSDISG--- 888
Cdd:cd17935    67 FEKIM----ALDIDERHLLRLGHGAKIIAMTCTHAALKRGELVELGfKYDNILMEEAAQILEIETFIPLLLQNPEDGpnr 142

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 530420825  889 --QIVLAGDPMQLGPVIKSRLAMAYG-LNVSFLERL 921
Cdd:cd17935   143 lkRLIMIGDHHQLPPVIKNMAFQKYSnMEQSLFTRL 178
DEXDc smart00487
DEAD-like helicases superfamily;
719-868 7.74e-09

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 57.12  E-value: 7.74e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825    719 EFFNPVLNENQKLAVKRILSGDCRplpYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAADLVCLRLheSKV 798
Cdd:smart00487    3 KFGFEPLRPYQKEAIEALLSGLRD---VILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEEL--KKL 77

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530420825    799 LQPATMVRVNATCRFEEividavkpycRDGEDIWKASRFRIIITTCSS-SGLFYQIGVRVGHFTHVFVDEA 868
Cdd:smart00487   78 GPSLGLKVVGLYGGDSK----------REQLRKLESGKTDILVTTPGRlLDLLENDKLSLSNVDLVILDEA 138
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 725-902 7.82e-09

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. There is a Walker A and Walker B.


Pssm-ID: 433343 [Multi-domain]  Cd Length: 191  Bit Score: 56.80  E-value: 7.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825   725 LNENQKLAVKRILSGDCRPLpyILFGPPGTGKTvTIIEAVLQVHFALPdSRILVCAPSNSAAdlvclrlhesKVLQpatm 804
Cdd:pfam13604    2 LNAEQAAAVRALLTSGDRVA--VLVGPAGTGKT-TALKALREAWEAAG-YRVIGLAPTGRAA----------KVLG---- 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825   805 vrvnatcrfEEIVIDAVkpycrdgediwkasrfriiiTTcssSGLFYQIGVRVGHFTH--VFVDEAGQASEPECLIPLGL 882
Cdd:pfam13604   64 ---------EELGIPAD--------------------TI---AKLLHRLGGRAGLDPGtlLIVDEAGMVGTRQMARLLKL 111

                          170       180
                   ....*....|....*....|
gi 530420825   883 MSDISGQIVLAGDPMQLGPV 902
Cdd:pfam13604  112 AEDAGARVILVGDPRQLPSV 131
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
 750-923 5.89e-08

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: 52.49  E-value: 5.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  750 GPPGTGKT---VTIIEAVLQVHfALPDSRILVCAPSNSAADlvclrlheskvlqpatmvrvnatcrfeeividavkpycr 826
Cdd:cd17914     6 GPPGTGKTrvlVKIVAALMQNK-NGEPGRILLVTPTNKAAA--------------------------------------- 45

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  827 dgediwkasRFRIIittcsssglfyqigvrvghfthvFVDEAGQASEPECLIPLGLMSDiSGQIVLAGDPMQLGPVIKSR 906
Cdd:cd17914    46 ---------QLDNI-----------------------LVDEAAQILEPETSRLIDLALD-QGRVILVGDHDQLGPVWRGA 92

                         170
                  ....*....|....*..
gi 530420825  907 LAMAYGLNVSFLERLMS 923
Cdd:cd17914    93 VLAKICNEQSLFTRLVR 109
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
 729-902 1.20e-07

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: 52.56  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  729 QKLAVKRILSGdcrplPYILF-GPPGTGKTvTIIEAVLQVhFALPDSRILVCAPSNSAADlvclRLHESKVLQPATMvrv 807
Cdd:cd17933     2 QKAAVRLVLRN-----RVSVLtGGAGTGKT-TTLKALLAA-LEAEGKRVVLAAPTGKAAK----RLSESTGIEASTI--- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  808 natCRFEEIVIDAVKPYcRDGEDIwkaSRFRIIIttcsssglfyqigvrvghfthvfVDEAGqasepecLIPLGLMSDI- 886
Cdd:cd17933    68 ---HRLLGINPGGGGFY-YNEENP---LDADLLI-----------------------VDEAS-------MVDTRLMAALl 110

                         170       180
                  ....*....|....*....|.
gi 530420825  887 -----SGQIVLAGDPMQLGPV 902
Cdd:cd17933   111 saipaGARLILVGDPDQLPSV 131
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
 1042-1127 5.82e-05

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: 42.81  E-value: 5.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825 1042 DIGVITPYRKQVEKIRILLR-----NVDLMDIKVGSVEEFQGQEYLVIIISTVRSNEDrfeddryflgflsNSKRFNVAI 1116
Cdd:cd18786    12 KGVVLTPYHRDRAYLNQYLQglsldEFDLQLVGAITIDSSQGLTFDVVTLYLPTANSL-------------TPRRLYVAL 78

                          90
                  ....*....|.
gi 530420825 1117 TRPKALLIVLG 1127
Cdd:cd18786    79 TRARKRLVIYD 89
AAA_19 pfam13245
AAA domain;
729-803 4.68e-04

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 41.43  E-value: 4.68e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530420825   729 QKLAVKRILSGDcrplPYILFGPPGTGKT---VTIIEAVLQVHFAlpDSRILVCAPSNSAADlvclRLHESkVLQPAT 803
Cdd:pfam13245    1 QREAVRTALPSK----VVLLTGGPGTGKTttiRHIVALLVALGGV--SFPILLAAPTGRAAK----RLSER-TGLPAS 67
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 724-766 4.24e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 39.05  E-value: 4.24e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 530420825  724 VLNENQKLAVKRILSGDcRPLPYILFGPPGTGKTvTIIEAVLQ 766
Cdd:cd00009     1 VGQEEAIEALREALELP-PPKNLLLYGPPGTGKT-TLARAIAN 41
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
 729-787 6.56e-03

DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprise a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. The bacterial SNF2 present in this family 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: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 39.64  E-value: 6.56e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530420825  729 QKLAVKRILSGDcrplPYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAAD 787
Cdd:cd18013     5 QKVAINFIIEHP----YCGLFLDMGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARS 59
ResIII pfam04851
Type III restriction enzyme, res subunit;
722-784 8.40e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 38.42  E-value: 8.40e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530420825   722 NPVLNENQKLAVKRIL-SGDCRPLPYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNS 784
Cdd:pfam04851    1 KLELRPYQIEAIENLLeSIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKD 64
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 683-769 8.89e-03

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 39.89  E-value: 8.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420825  683 TEERRVGDKDLPVLAPFTAEMSDWVDEIQTPKARKMEFFNPVLNENQKLAVKRILS------------GDCRPLPYILFG 750
Cdd:COG0464   119 LELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEVKEELRELVAlplkrpelreeyGLPPPRGLLLYG 198

                          90       100
                  ....*....|....*....|..
gi 530420825  751 PPGTGKTvTIIEAV---LQVHF 769
Cdd:COG0464   199 PPGTGKT-LLARALageLGLPL 219
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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