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Conserved domains on  [gi|768031449|ref|XP_011529001|]
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RNA helicase Mov10l1 isoform X5 [Homo sapiens]

Protein Classification

DEXXQc_Mov10L1 and SF1_C_Upf1 domain-containing protein( domain architecture ID 13030947)

DEXXQc_Mov10L1 and SF1_C_Upf1 domain-containing protein

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 ...
692-921 3.56e-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: 3.56e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  692 VLNENQKLAVKRILSGDCRPLPYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAADLVCLRLHESKVLQPAT 771
Cdd:cd18078     1 DLNELQKEAVKRILGGECRPLPYILFGPPGTGKTVTIIEAILQVVYNLPRSRILVCAPSNSAADLVTSRLHESKVLKPGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  772 MVRVNATCRFEEIVIDAVKPYCRDGEDIWKASRFRIIITTCSSSGLFYQIGVRVGHFTHVFVDEAGQASEPECLIPLGLM 851
Cdd:cd18078    81 MVRLNAVNRFESTVIDARKLYCRLGEDLSKASRHRIVISTCSTAGLLYQMGLPVGHFTHVFVDEAGQATEPESLIPLGLI 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  852 SDISGQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERLMSRPAYQRDENAFGACGAHNPLLVTKLVKNYR 921
Cdd:cd18078   161 SSRDGQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLMNRPLYLRDPNRFGESGGYNPLLVTKLVDNYR 230
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
922-1157 5.66e-54

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: 186.29  E-value: 5.66e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  922 SHEALLMLPSRLFYHRELEVCADptvVTSLLGWEKLPKKGFPLIFHGVRGSEAREGKSPSWFNPAEAVQVLRYCCLLahs 1001
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGVS---VAARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYL--- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449 1002 ISSQVSASDIGVITPYRKQwlwssggdtgashaehqvsfmkhvslwcshhqaelgknpqnteekVEKIRILLRNV--DLM 1079
Cdd:cd18808    75 LKSGVKPSSIGVITPYRAQ---------------------------------------------VALIRELLRKRggLLE 109
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768031449 1080 DIKVGSVEEFQGQEYLVIIISTVRSNEDRFEddryfLGFLSNSKRFNVAITRPKALLIVLGNPHVLVRDPCFGALLEY 1157
Cdd:cd18808   110 DVEVGTVDNFQGREKDVIILSLVRSNESGGS-----IGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEY 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 ...
692-921 3.56e-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: 3.56e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  692 VLNENQKLAVKRILSGDCRPLPYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAADLVCLRLHESKVLQPAT 771
Cdd:cd18078     1 DLNELQKEAVKRILGGECRPLPYILFGPPGTGKTVTIIEAILQVVYNLPRSRILVCAPSNSAADLVTSRLHESKVLKPGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  772 MVRVNATCRFEEIVIDAVKPYCRDGEDIWKASRFRIIITTCSSSGLFYQIGVRVGHFTHVFVDEAGQASEPECLIPLGLM 851
Cdd:cd18078    81 MVRLNAVNRFESTVIDARKLYCRLGEDLSKASRHRIVISTCSTAGLLYQMGLPVGHFTHVFVDEAGQATEPESLIPLGLI 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  852 SDISGQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERLMSRPAYQRDENAFGACGAHNPLLVTKLVKNYR 921
Cdd:cd18078   161 SSRDGQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLMNRPLYLRDPNRFGESGGYNPLLVTKLVDNYR 230
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
922-1157 5.66e-54

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: 186.29  E-value: 5.66e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  922 SHEALLMLPSRLFYHRELEVCADptvVTSLLGWEKLPKKGFPLIFHGVRGSEAREGKSPSWFNPAEAVQVLRYCCLLahs 1001
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGVS---VAARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYL--- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449 1002 ISSQVSASDIGVITPYRKQwlwssggdtgashaehqvsfmkhvslwcshhqaelgknpqnteekVEKIRILLRNV--DLM 1079
Cdd:cd18808    75 LKSGVKPSSIGVITPYRAQ---------------------------------------------VALIRELLRKRggLLE 109
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768031449 1080 DIKVGSVEEFQGQEYLVIIISTVRSNEDRFEddryfLGFLSNSKRFNVAITRPKALLIVLGNPHVLVRDPCFGALLEY 1157
Cdd:cd18808   110 DVEVGTVDNFQGREKDVIILSLVRSNESGGS-----IGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEY 182
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
802-1157 3.97e-51

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 194.96  E-value: 3.97e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  802 ASRFRIIITTCSSSGLFyqIGVRVGHFTHVFVDEAGQASEPECLIPLGLmsdiSGQIVLAGDPMQLGPviksrlamaygl 881
Cdd:COG1112   532 LELAPVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALAR----AKRVVLVGDPKQLPP------------ 593
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  882 nVSFLERLMSRPAYQRDENAFGACGAHNPLLVTKLVKNYRSHEALLMLPSRLFYHRELEVCADPTVvtsllgwEKLPKKG 961
Cdd:COG1112   594 -VVFGEEAEEVAEEGLDESLLDRLLARLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKA-------RRLADPD 665
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  962 FPLIFHGVRGSEAREGKspSWFNPAEAVQVLRyccLLAHSISSQVSASDIGVITPYRKQwlwssggdtgashaehqvsfm 1041
Cdd:COG1112   666 SPLVFIDVDGVYERRGG--SRTNPEEAEAVVE---LVRELLEDGPDGESIGVITPYRAQ--------------------- 719
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449 1042 khvslwcshhqaelgknpqnteekVEKIRILLRN---VDLMDIKVGSVEEFQGQEYLVIIISTVRSNEdrfEDDRYFLGF 1118
Cdd:COG1112   720 ------------------------VALIRELLREalgDGLEPVFVGTVDRFQGDERDVIIFSLVYSND---EDVPRNFGF 772
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 768031449 1119 LSNS-KRFNVAITRPKALLIVLGNPHVLVRDP---CFGALLEY 1157
Cdd:COG1112   773 LNGGpRRLNVAVSRARRKLIVVGSRELLDSDPstpALKRLLEY 815
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
685-1164 2.18e-50

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: 189.64  E-value: 2.18e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449   685 KMEFFNPVLNENQKLAVKRILSGDCRplpYILFGPPGTGKTVTIIEAVLQVhfALPDSRILVCAPSNSAAD--------- 755
Cdd:TIGR00376  150 DFQFFDPNLNESQKEAVLFALSSKDL---FLIHGPPGTGKTRTVVELIRQL--VKRGLRVLVTAPSNIAVDnllerlalc 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449   756 -LVCLRL-HESKVLQ-------PATMVRVNATCRFEEIV--IDAV----------KPYCRDG------------------ 796
Cdd:TIGR00376  225 dQKIVRLgHPARLLKsnkqhslDYLIENHPKYQIVADIRekIDELieernkktkpSPQKRRGlsdikilrkalkkrearg 304
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449   797 -EDIWKASRFRIIITTCSSSGLF---YQIGVRVGH----------------------FTHVFVDEAGQASEPECLIPLgl 850
Cdd:TIGR00376  305 iESLKIASMAEWIETNKSIDRLLkllPESEERIMNeilaesdatnsmagseilngqyFDVAVIDEASQAMEPSCLIPL-- 382
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449   851 msdISGQ-IVLAGDPMQLGPVIKSRlaMAYGLNVSFLERLMSRpayqrdenafgacgahNPLLVTKLVKNYRSHEALLML 929
Cdd:TIGR00376  383 ---LKARkLILAGDHKQLPPTILSH--DAEELSLTLFERLIKE----------------YPERSRTLNVQYRMNQKIMEF 441
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449   930 PSRLFYHRELEvcADPTVVTSLLgwEKLPKK-----------GFPLIF---HGVRGSEAREGKSPSWFNPAEAVQVLRYC 995
Cdd:TIGR00376  442 PSREFYNGKLT--AHESVANILL--RDLPKVeateseddletGIPLLFidtSGCELFELKEADSTSKYNPGEAELVSEII 517
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449   996 CLLahsISSQVSASDIGVITPYrkqwlwssggdtgashaEHQVSFMKhvslwcshhqaelgknpQNTEEKvekirillrn 1075
Cdd:TIGR00376  518 QAL---VKMGVPANDIGVITPY-----------------DAQVDLLR-----------------QLLEHR---------- 550
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  1076 vdLMDIKVGSVEEFQGQEYLVIIISTVRSNEDRfeddryFLGFLSNSKRFNVAITRPKALLIVLGNPHVLVRDPCFGALL 1155
Cdd:TIGR00376  551 --HIDIEVSSVDGFQGREKEVIIISFVRSNRKG------EVGFLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKRLI 622

                   ....*....
gi 768031449  1156 EYSITNGVY 1164
Cdd:TIGR00376  623 EWCKQHGEV 631
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
881-1142 2.99e-47

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: 167.73  E-value: 2.99e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449   881 LNVSFLERLMSrpayqrdenafgacgaHNPLLVTKLVKNYRSHEALLMLPSRLFYHRELEvCADPTVVTSLLGWEKLPKK 960
Cdd:pfam13087    1 LDRSLFERLQE----------------LGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLK-DGPSVAERPLPDDFHLPDP 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449   961 GFPLIFHGVRGSEAREGKS-PSWFNPAEAVQVLRYCCLLAHSISSQvsASDIGVITPYRKQwlwssggdtgashaehqvs 1039
Cdd:pfam13087   64 LGPLVFIDVDGSEEEESDGgTSYSNEAEAELVVQLVEKLIKSGPEE--PSDIGVITPYRAQ------------------- 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  1040 fmkhvslwcshhqaelgknpqnteekVEKIRILLRNVDLM--DIKVGSVEEFQGQEYLVIIISTVRSNEDRfeddryFLG 1117
Cdd:pfam13087  123 --------------------------VRLIRKLLKRKLGGklEIEVNTVDGFQGREKDVIIFSCVRSNEKG------GIG 170
                          250       260
                   ....*....|....*....|....*
gi 768031449  1118 FLSNSKRFNVAITRPKALLIVLGNP 1142
Cdd:pfam13087  171 FLSDPRRLNVALTRAKRGLIIVGNA 195
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
697-874 7.55e-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: 7.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449   697 QKLAVKRILSgdcRPLPYILFGPPGTGKTVTIIEAVLQVHF-----ALPDSRILVCAPSNSAADLVCLRLHESKVLQPAT 771
Cdd:pfam13086    2 QREAIRSALS---SSHFTLIQGPPGTGKTTTIVELIRQLLSypatsAAAGPRILVCAPSNAAVDNILERLLRKGQKYGPK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449   772 MVRVNAtcrfEEIVIDAVKPYCRD-------------------------------------------------------- 795
Cdd:pfam13086   79 IVRIGH----PAAISEAVLPVSLDylvesklnneedaqivkdiskeleklakalrafekeiivekllksrnkdkskleqe 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449   796 -----------GEDIWKASRF---------RIIITTCSSSG---LFYQIGVRVghfthVFVDEAGQASEPECLIPLglms 852
Cdd:pfam13086  155 rrklrserkelRKELRRREQSlereildeaQIVCSTLSGAGsrlLSSLANFDV-----VIIDEAAQALEPSTLIPL---- 225
                          250       260
                   ....*....|....*....|....
gi 768031449   853 dISG--QIVLAGDPMQLGPVIKSR 874
Cdd:pfam13086  226 -LRGpkKVVLVGDPKQLPPTVISK 248
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
676-870 4.42e-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: 4.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  676 DEIQTPKARKMEFFNPVLNENQKLAVKRILSGdcRPLpYILFGPPGTGKTvTIIEAVLQVHFALPDsRILVCAPSNSAAd 755
Cdd:COG0507   108 ADVEAALAALEPRAGITLSDEQREAVALALTT--RRV-SVLTGGAGTGKT-TTLRALLAALEALGL-RVALAAPTGKAA- 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  756 lvcLRLHESKVLQPATMvrvnatCRFEEIVIDAVKPYCRDGEDIWKAsrfRIIIttcsssglfyqigvrvghfthvfVDE 835
Cdd:COG0507   182 ---KRLSESTGIEARTI------HRLLGLRPDSGRFRHNRDNPLTPA---DLLV-----------------------VDE 226
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 768031449  836 AGqasepecLIPLGLMSDI-------SGQIVLAGDPMQLGPV 870
Cdd:COG0507   227 AS-------MVDTRLMAALlealpraGARLILVGDPDQLPSV 261
DEXDc smart00487
DEAD-like helicases superfamily;
687-836 6.43e-09

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 57.12  E-value: 6.43e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449    687 EFFNPVLNENQKLAVKRILSGDCRplpYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAADLVCLRLheSKV 766
Cdd:smart00487    3 KFGFEPLRPYQKEAIEALLSGLRD---VILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEEL--KKL 77
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768031449    767 LQPATMVRVNATCRFEEividavkpycRDGEDIWKASRFRIIITTCSS-SGLFYQIGVRVGHFTHVFVDEA 836
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 ...
692-921 3.56e-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: 3.56e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  692 VLNENQKLAVKRILSGDCRPLPYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAADLVCLRLHESKVLQPAT 771
Cdd:cd18078     1 DLNELQKEAVKRILGGECRPLPYILFGPPGTGKTVTIIEAILQVVYNLPRSRILVCAPSNSAADLVTSRLHESKVLKPGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  772 MVRVNATCRFEEIVIDAVKPYCRDGEDIWKASRFRIIITTCSSSGLFYQIGVRVGHFTHVFVDEAGQASEPECLIPLGLM 851
Cdd:cd18078    81 MVRLNAVNRFESTVIDARKLYCRLGEDLSKASRHRIVISTCSTAGLLYQMGLPVGHFTHVFVDEAGQATEPESLIPLGLI 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  852 SDISGQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERLMSRPAYQRDENAFGACGAHNPLLVTKLVKNYR 921
Cdd:cd18078   161 SSRDGQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLMNRPLYLRDPNRFGESGGYNPLLVTKLVDNYR 230
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
692-921 3.97e-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: 3.97e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  692 VLNENQKLAVKRILSGDCRPLPYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAADLVCLRLHeSKVLQPAT 771
Cdd:cd18038     1 ELNDEQKLAVRNIVTGTSRPPPYIIFGPPGTGKTVTLVEAILQVLRQPPEARILVCAPSNSAADLLAERLL-NALVTKRE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  772 MVRVNATCRFEEIVIDAVKPYCRDGED-------IWKASRFRIIITTCSSSGLFYQIGVRVGHFTHVFVDEAGQASEPEC 844
Cdd:cd18038    80 ILRLNAPSRDRASVPPELLPYCNSKAEgtfrlpsLEELKKYRIVVCTLMTAGRLVQAGVPNGHFTHIFIDEAGQATEPEA 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768031449  845 LIPLGLMSDISGQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERLMSRPAYQRDenafgacGAHNPLLVTKLVKNYR 921
Cdd:cd18038   160 LIPLSELASKNTQIVLAGDPKQLGPVVRSPLARKYGLGKSLLERLMERPLYYKD-------GEYNPSYITKLLKNYR 229
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
922-1157 5.66e-54

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: 186.29  E-value: 5.66e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  922 SHEALLMLPSRLFYHRELEVCADptvVTSLLGWEKLPKKGFPLIFHGVRGSEAREGKSPSWFNPAEAVQVLRYCCLLahs 1001
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGVS---VAARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYL--- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449 1002 ISSQVSASDIGVITPYRKQwlwssggdtgashaehqvsfmkhvslwcshhqaelgknpqnteekVEKIRILLRNV--DLM 1079
Cdd:cd18808    75 LKSGVKPSSIGVITPYRAQ---------------------------------------------VALIRELLRKRggLLE 109
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768031449 1080 DIKVGSVEEFQGQEYLVIIISTVRSNEDRFEddryfLGFLSNSKRFNVAITRPKALLIVLGNPHVLVRDPCFGALLEY 1157
Cdd:cd18808   110 DVEVGTVDNFQGREKDVIILSLVRSNESGGS-----IGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEY 182
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
802-1157 3.97e-51

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 194.96  E-value: 3.97e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  802 ASRFRIIITTCSSSGLFyqIGVRVGHFTHVFVDEAGQASEPECLIPLGLmsdiSGQIVLAGDPMQLGPviksrlamaygl 881
Cdd:COG1112   532 LELAPVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALAR----AKRVVLVGDPKQLPP------------ 593
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  882 nVSFLERLMSRPAYQRDENAFGACGAHNPLLVTKLVKNYRSHEALLMLPSRLFYHRELEVCADPTVvtsllgwEKLPKKG 961
Cdd:COG1112   594 -VVFGEEAEEVAEEGLDESLLDRLLARLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKA-------RRLADPD 665
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  962 FPLIFHGVRGSEAREGKspSWFNPAEAVQVLRyccLLAHSISSQVSASDIGVITPYRKQwlwssggdtgashaehqvsfm 1041
Cdd:COG1112   666 SPLVFIDVDGVYERRGG--SRTNPEEAEAVVE---LVRELLEDGPDGESIGVITPYRAQ--------------------- 719
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449 1042 khvslwcshhqaelgknpqnteekVEKIRILLRN---VDLMDIKVGSVEEFQGQEYLVIIISTVRSNEdrfEDDRYFLGF 1118
Cdd:COG1112   720 ------------------------VALIRELLREalgDGLEPVFVGTVDRFQGDERDVIIFSLVYSND---EDVPRNFGF 772
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 768031449 1119 LSNS-KRFNVAITRPKALLIVLGNPHVLVRDP---CFGALLEY 1157
Cdd:COG1112   773 LNGGpRRLNVAVSRARRKLIVVGSRELLDSDPstpALKRLLEY 815
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
685-1164 2.18e-50

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: 189.64  E-value: 2.18e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449   685 KMEFFNPVLNENQKLAVKRILSGDCRplpYILFGPPGTGKTVTIIEAVLQVhfALPDSRILVCAPSNSAAD--------- 755
Cdd:TIGR00376  150 DFQFFDPNLNESQKEAVLFALSSKDL---FLIHGPPGTGKTRTVVELIRQL--VKRGLRVLVTAPSNIAVDnllerlalc 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449   756 -LVCLRL-HESKVLQ-------PATMVRVNATCRFEEIV--IDAV----------KPYCRDG------------------ 796
Cdd:TIGR00376  225 dQKIVRLgHPARLLKsnkqhslDYLIENHPKYQIVADIRekIDELieernkktkpSPQKRRGlsdikilrkalkkrearg 304
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449   797 -EDIWKASRFRIIITTCSSSGLF---YQIGVRVGH----------------------FTHVFVDEAGQASEPECLIPLgl 850
Cdd:TIGR00376  305 iESLKIASMAEWIETNKSIDRLLkllPESEERIMNeilaesdatnsmagseilngqyFDVAVIDEASQAMEPSCLIPL-- 382
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449   851 msdISGQ-IVLAGDPMQLGPVIKSRlaMAYGLNVSFLERLMSRpayqrdenafgacgahNPLLVTKLVKNYRSHEALLML 929
Cdd:TIGR00376  383 ---LKARkLILAGDHKQLPPTILSH--DAEELSLTLFERLIKE----------------YPERSRTLNVQYRMNQKIMEF 441
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449   930 PSRLFYHRELEvcADPTVVTSLLgwEKLPKK-----------GFPLIF---HGVRGSEAREGKSPSWFNPAEAVQVLRYC 995
Cdd:TIGR00376  442 PSREFYNGKLT--AHESVANILL--RDLPKVeateseddletGIPLLFidtSGCELFELKEADSTSKYNPGEAELVSEII 517
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449   996 CLLahsISSQVSASDIGVITPYrkqwlwssggdtgashaEHQVSFMKhvslwcshhqaelgknpQNTEEKvekirillrn 1075
Cdd:TIGR00376  518 QAL---VKMGVPANDIGVITPY-----------------DAQVDLLR-----------------QLLEHR---------- 550
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  1076 vdLMDIKVGSVEEFQGQEYLVIIISTVRSNEDRfeddryFLGFLSNSKRFNVAITRPKALLIVLGNPHVLVRDPCFGALL 1155
Cdd:TIGR00376  551 --HIDIEVSSVDGFQGREKEVIIISFVRSNRKG------EVGFLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKRLI 622

                   ....*....
gi 768031449  1156 EYSITNGVY 1164
Cdd:TIGR00376  623 EWCKQHGEV 631
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
881-1142 2.99e-47

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: 167.73  E-value: 2.99e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449   881 LNVSFLERLMSrpayqrdenafgacgaHNPLLVTKLVKNYRSHEALLMLPSRLFYHRELEvCADPTVVTSLLGWEKLPKK 960
Cdd:pfam13087    1 LDRSLFERLQE----------------LGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLK-DGPSVAERPLPDDFHLPDP 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449   961 GFPLIFHGVRGSEAREGKS-PSWFNPAEAVQVLRYCCLLAHSISSQvsASDIGVITPYRKQwlwssggdtgashaehqvs 1039
Cdd:pfam13087   64 LGPLVFIDVDGSEEEESDGgTSYSNEAEAELVVQLVEKLIKSGPEE--PSDIGVITPYRAQ------------------- 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  1040 fmkhvslwcshhqaelgknpqnteekVEKIRILLRNVDLM--DIKVGSVEEFQGQEYLVIIISTVRSNEDRfeddryFLG 1117
Cdd:pfam13087  123 --------------------------VRLIRKLLKRKLGGklEIEVNTVDGFQGREKDVIIFSCVRSNEKG------GIG 170
                          250       260
                   ....*....|....*....|....*
gi 768031449  1118 FLSNSKRFNVAITRPKALLIVLGNP 1142
Cdd:pfam13087  171 FLSDPRRLNVALTRAKRGLIIVGNA 195
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
693-889 1.78e-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: 146.62  E-value: 1.78e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  693 LNENQKLAVKRILSgdcRPLPYILfGPPGTGKTVTIIEAVLQVHFALPdSRILVCAPSNSAADLVCLRLHES--KVlqpa 770
Cdd:cd18039     2 LNHSQVDAVKTALQ---RPLSLIQ-GPPGTGKTVTSATIVYHLVKQGN-GPVLVCAPSNVAVDQLTEKIHQTglKV---- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  771 tmVRVNATCR-----------FEEIVIDAVKPYCRDGEDIWKA----------SRFR---------------IIITTCSS 814
Cdd:cd18039    73 --VRLCAKSReavespvsflaLHNQVRNLDSAEKLELLKLLKLetgelssadeKRYRklkrkaerellrnadVICCTCVG 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768031449  815 SGlfyqiGVRVG--HFTHVFVDEAGQASEPECLIPLGLMSDisgQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERL 889
Cdd:cd18039   151 AG-----DPRLSkmKFRTVLIDEATQATEPECLIPLVHGAK---QVILVGDHCQLGPVVMCKKAAKAGLSQSLFERL 219
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
693-921 3.83e-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: 3.83e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  693 LNENQKLAVKRILSGdcRPLpYILFGPPGTGKTVTIIEAVLQVhfALPDSRILVCAPSNSAADLVCLRLheskVLQPATM 772
Cdd:cd18044     2 LNDSQKEAVKFALSQ--KDV-ALIHGPPGTGKTTTVVEIILQA--VKRGEKVLACAPSNIAVDNLVERL----VALKVKV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  773 VRVNATCRfeeiVIDAVKPYCRDgediwKASRFRIIITTCSSSGLFyqiGVRVG-HFTHVFVDEAGQASEPECLIPLGLM 851
Cdd:cd18044    73 VRIGHPAR----LLESVLDHSLD-----ALVAAQVVLATNTGAGSR---QLLPNeLFDVVVIDEAAQALEASCWIPLLKA 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  852 SdisgQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERLMSRpayqrdenafgacgaHNPLLVTKLVKNYR 921
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 ...
693-889 6.65e-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: 6.65e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  693 LNENQKLAVKRILSGDCRPLPYILF-GPPGTGKTVTIIEAVLQVhFALPDSRILVCAPSNSAADLVC---LRLHESKVLQ 768
Cdd:cd18077     2 LNAKQKEAVLAITTPLSIQLPPVLLiGPFGTGKTFTLAQAVKHI-LQQPETRILICTHSNSAADLYIkeyLHPYVETGNP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  769 PATMVRVNATCRFEEIVIDAVKPYC---RDG-------EDIWKAsrfRIIITTCSSSGLFYQIGVRVGHFTHVFVDEAGQ 838
Cdd:cd18077    81 RARPLRVYYRNRWVKTVHPVVQKYClidEHGtfrmptrEDVMRH---RVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQ 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768031449  839 ASEPECLIPLGLMSDiSGQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERL 889
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 ...
693-891 5.02e-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: 118.86  E-value: 5.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  693 LNENQKLAVKRILSGDcrplPYI--LFGPPGTGKTVTIIEAVLQVHFALPDS-----------------------RILVC 747
Cdd:cd18042     1 LNESQLEAIASALQNS----PGItlIQGPPGTGKTKTIVGILSVLLAGKYRKyyekvkkklrklqrnlnnkkkknRILVC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  748 APSNSAADLVCLRLHESKVLQPatmvrvNATCRFEEIVidavkpycRDGEDIWKASRFR---IIITTCSSSG-LFYQIGV 823
Cdd:cd18042    77 APSNAAVDEIVLRLLSEGFLDG------DGRSYKPNVV--------RVGRQELRASILNeadIVCTTLSSSGsDLLESLP 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768031449  824 RvgHFTHVFVDEAGQASEPECLIPLGLmsdISGQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERLMS 891
Cdd:cd18042   143 R--GFDTVIIDEAAQAVELSTLIPLRL---GCKRLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQL 205
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
693-921 2.46e-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: 113.48  E-value: 2.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  693 LNENQKLAVKRILSgdCRPLPYILfGPPGTGKTVTIIEAVLQvhFALPDSRILVCAPSNSAADLVCLRLHESKVlqpaTM 772
Cdd:cd18041     2 LNKDQRQAIKKVLN--AKDYALIL-GMPGTGKTTTIAALVRI--LVALGKSVLLTSYTHSAVDNILLKLKKFGV----NF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  773 VRVNATCR----FEEIVIDAVKPYCRDGEDIWKA-SRFRIIITTCSSsglFYQIGVRVGHFTHVFVDEAGQASEPECLIP 847
Cdd:cd18041    73 LRLGRLKKihpdVQEFTLEAILKSCKSVEELESKyESVSVVATTCLG---INHPIFRRRTFDYCIVDEASQITLPICLGP 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768031449  848 LgLMSDisgQIVLAGDPMQLGPVIKSRLAMAYGLNVSFLERLmsrpayqrdenafgaCGAHnPLLVTKLVKNYR 921
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, ...
715-895 1.60e-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: 1.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  715 ILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAADlvclrlheskvlqpatmvrvnatcrfeeiVIDavkpycr 794
Cdd:cd17934     3 LIQGPPGTGKTTTIAAIVLQLLKGLRGKRVLVTAQSNVAVD-----------------------------NVD------- 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  795 dgediwkasrfriiittcsssglfyqigvrvghftHVFVDEAGQASEPECLIPLGLmsdiSGQIVLAGDPMQLGPVIKSR 874
Cdd:cd17934    47 -----------------------------------VVIIDEASQITEPELLIALIR----AKKVVLVGDPKQLPPVVQED 87
                         170       180
                  ....*....|....*....|.
gi 768031449  875 LAMAYGLNVSFLERLMSRPAY 895
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 ...
692-889 1.93e-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: 1.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  692 VLNENQKLAVKRIL---SGDCRPLPYILFGPPGTGKTVTIIEAVLQVhFALPDSRILVCAPSNSAADLVC---LRLHESK 765
Cdd:cd18076     1 AGNNKQQLAFNFIAgkpSEARFVPPLLIYGPFGTGKTFTLAMAALEV-IREPGTKVLICTHTNSAADIYIreyFHPYVDK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  766 VLQPATMVRVNATCRFEEIVIDAVKPYCRDGEDIW--------KASRFRIIITTCSSSglfYQIGVRVGHFTHVFVDEAG 837
Cdd:cd18076    80 GHPEARPLRIKATDRPNAITDPDTITYCCLTKDRQcfrlptrdELDFHNIVITTTAMA---FNLHVLSGFFTHIFIDEAA 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768031449  838 QASEPECLIPLGLMSdISGQIVLAGDPMQLGPVIKSrLAMAYGLNVSFLERL 889
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 ...
697-874 7.55e-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: 7.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449   697 QKLAVKRILSgdcRPLPYILFGPPGTGKTVTIIEAVLQVHF-----ALPDSRILVCAPSNSAADLVCLRLHESKVLQPAT 771
Cdd:pfam13086    2 QREAIRSALS---SSHFTLIQGPPGTGKTTTIVELIRQLLSypatsAAAGPRILVCAPSNAAVDNILERLLRKGQKYGPK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449   772 MVRVNAtcrfEEIVIDAVKPYCRD-------------------------------------------------------- 795
Cdd:pfam13086   79 IVRIGH----PAAISEAVLPVSLDylvesklnneedaqivkdiskeleklakalrafekeiivekllksrnkdkskleqe 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449   796 -----------GEDIWKASRF---------RIIITTCSSSG---LFYQIGVRVghfthVFVDEAGQASEPECLIPLglms 852
Cdd:pfam13086  155 rrklrserkelRKELRRREQSlereildeaQIVCSTLSGAGsrlLSSLANFDV-----VIIDEAAQALEPSTLIPL---- 225
                          250       260
                   ....*....|....*....|....
gi 768031449   853 dISG--QIVLAGDPMQLGPVIKSR 874
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 ...
693-889 2.62e-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: 86.42  E-value: 2.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  693 LNENQKLAVKRILsgdCRPLpYILFGPPGTGKTVTII-----------EAVLQVHFALPDSRILVCAPSNSAADLVC--- 758
Cdd:cd18040     2 LNPSQNHAVRTAL---TKPF-TLIQGPPGTGKTVTGVhiaywfakqnrEIQSVSGEGDGGPCVLYCGPSNKSVDVVAell 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  759 LRLHESKVLQ-------------PATMVRVN-------------------------------ATCRFEEIVIDAVKPYCR 794
Cdd:cd18040    78 LKVPGLKILRvyseqietteypiPNEPRHPNkksereskpnselssitlhhrirqpsnphsqQIKAFEARFERTQEKITE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  795 DGED-----IWKASRFR-----IIITTCSSSGlfyqiGVRVGHFTHV---FVDEAGQASEPECLIPLGLMSDISgQIVLA 861
Cdd:cd18040   158 EDIKtykilIWEARFEEletvdVILCTCSEAA-----SQKMRTHANVkqcIVDECGMCTEPESLIPIVSAPRAE-QVVLI 231
                         250       260
                  ....*....|....*....|....*...
gi 768031449  862 GDPMQLGPVIKSRLAMAYGLNVSFLERL 889
Cdd:cd18040   232 GDHKQLRPVVQNKEAQKLGLGRSLFERY 259
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
693-897 1.19e-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: 1.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  693 LNENQKLAVKRILSgdcRPLPYILfGPPGTGKT---VTIIEAVLQVHFALPDSRILVCAPSNSAADLVCLRLHESkvlQP 769
Cdd:cd17936     2 LDPSQLEALKHALT---SELALIQ-GPPGTGKTflgVKLVRALLQNQDLSITGPILVVCYTNHALDQFLEGLLDF---GP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  770 ATMVRVNATcrfeeiVIdavkpycrdGEDIWKASRFRiiittcsssGLFYQIGVRVghfthVFVDEAGQASEPE---CLI 846
Cdd:cd17936    75 TKIVRLGAR------VI---------GMTTTGAAKYR---------ELLQALGPKV-----VIVEEAAEVLEAHilaALT 125
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 768031449  847 PlglmsDISgQIVLAGDPMQLGPVIKSRL--AMAYGLNVSFLERL------MSRPAYQR 897
Cdd:cd17936   126 P-----STE-HLILIGDHKQLRPKVNVYEltAKKYNLDVSLFERLvknglpFVTLNVQR 178
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
694-879 1.85e-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: 1.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  694 NENQKLAVKRILSGDCrplpYILFGPPGTGKTVTIieAVLQVHFALPDSRILVCAPSNSAADLVclrlheskvlqpatmv 773
Cdd:cd18043     1 DSSQEAAIISARNGKN----VVIQGPPGTGKSQTI--ANIIANALARGKRVLFVSEKKAALDVV---------------- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  774 rvnatcrfeeividavkpycrdgediwkasRFRIIITTCSSSGLFYQIGvrVGHFTHVFVDEAGQASePECLIPLGLMSD 853
Cdd:cd18043    59 ------------------------------RFPCWIMSPLSVSQYLPLN--RNLFDLVIFDEASQIP-IEEALPALFRGK 105
                         170       180
                  ....*....|....*....|....*.
gi 768031449  854 isgQIVLAGDPMQLGPVIksRLAMAY 879
Cdd:cd18043   106 ---QVVVVGDDKQLPPSI--LLREHY 126
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
676-870 4.42e-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: 4.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  676 DEIQTPKARKMEFFNPVLNENQKLAVKRILSGdcRPLpYILFGPPGTGKTvTIIEAVLQVHFALPDsRILVCAPSNSAAd 755
Cdd:COG0507   108 ADVEAALAALEPRAGITLSDEQREAVALALTT--RRV-SVLTGGAGTGKT-TTLRALLAALEALGL-RVALAAPTGKAA- 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  756 lvcLRLHESKVLQPATMvrvnatCRFEEIVIDAVKPYCRDGEDIWKAsrfRIIIttcsssglfyqigvrvghfthvfVDE 835
Cdd:COG0507   182 ---KRLSESTGIEARTI------HRLLGLRPDSGRFRHNRDNPLTPA---DLLV-----------------------VDE 226
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 768031449  836 AGqasepecLIPLGLMSDI-------SGQIVLAGDPMQLGPV 870
Cdd:COG0507   227 AS-------MVDTRLMAALlealpraGARLILVGDPDQLPSV 261
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
701-889 1.11e-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: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  701 VKRILSGdCRPLPYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAADLVclrlheskvlqpatmvrvnatcr 780
Cdd:cd17935    11 IEAIRSG-MQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPNQRTLIVTHSNQALNQL----------------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  781 FEEIVidavKPYCRDGEDIWKASRFRIIITTCSSSGLFYQIGVRVG-HFTHVFVDEAGQASEPECLIPLGLMSDISG--- 856
Cdd:cd17935    67 FEKIM----ALDIDERHLLRLGHGAKIIAMTCTHAALKRGELVELGfKYDNILMEEAAQILEIETFIPLLLQNPEDGpnr 142
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 768031449  857 --QIVLAGDPMQLGPVIKSRLAMAYG-LNVSFLERL 889
Cdd:cd17935   143 lkRLIMIGDHHQLPPVIKNMAFQKYSnMEQSLFTRL 178
DEXDc smart00487
DEAD-like helicases superfamily;
687-836 6.43e-09

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 57.12  E-value: 6.43e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449    687 EFFNPVLNENQKLAVKRILSGDCRplpYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAADLVCLRLheSKV 766
Cdd:smart00487    3 KFGFEPLRPYQKEAIEALLSGLRD---VILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEEL--KKL 77
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768031449    767 LQPATMVRVNATCRFEEividavkpycRDGEDIWKASRFRIIITTCSS-SGLFYQIGVRVGHFTHVFVDEA 836
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 ...
693-870 7.92e-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: 7.92e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449   693 LNENQKLAVKRILSGDCRPLpyILFGPPGTGKTvTIIEAVLQVHFALPdSRILVCAPSNSAAdlvclrlhesKVLQpatm 772
Cdd:pfam13604    2 LNAEQAAAVRALLTSGDRVA--VLVGPAGTGKT-TALKALREAWEAAG-YRVIGLAPTGRAA----------KVLG---- 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449   773 vrvnatcrfEEIVIDAVkpycrdgediwkasrfriiiTTcssSGLFYQIGVRVGHFTH--VFVDEAGQASEPECLIPLGL 850
Cdd:pfam13604   64 ---------EELGIPAD--------------------TI---AKLLHRLGGRAGLDPGtlLIVDEAGMVGTRQMARLLKL 111
                          170       180
                   ....*....|....*....|
gi 768031449   851 MSDISGQIVLAGDPMQLGPV 870
Cdd:pfam13604  112 AEDAGARVILVGDPRQLPSV 131
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
718-891 5.96e-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: 5.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  718 GPPGTGKT---VTIIEAVLQVHfALPDSRILVCAPSNSAADlvclrlheskvlqpatmvrvnatcrfeeividavkpycr 794
Cdd:cd17914     6 GPPGTGKTrvlVKIVAALMQNK-NGEPGRILLVTPTNKAAA--------------------------------------- 45
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  795 dgediwkasRFRIIittcsssglfyqigvrvghfthvFVDEAGQASEPECLIPLGLMSDiSGQIVLAGDPMQLGPVIKSR 874
Cdd:cd17914    46 ---------QLDNI-----------------------LVDEAAQILEPETSRLIDLALD-QGRVILVGDHDQLGPVWRGA 92
                         170
                  ....*....|....*..
gi 768031449  875 LAMAYGLNVSFLERLMS 891
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. ...
697-870 1.22e-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: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  697 QKLAVKRILSGdcrplPYILF-GPPGTGKTvTIIEAVLQVhFALPDSRILVCAPSNSAADlvclRLHESKVLQPATMvrv 775
Cdd:cd17933     2 QKAAVRLVLRN-----RVSVLtGGAGTGKT-TTLKALLAA-LEAEGKRVVLAAPTGKAAK----RLSESTGIEASTI--- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  776 natCRFEEIVIDAVKPYcRDGEDIwkaSRFRIIIttcsssglfyqigvrvghfthvfVDEAGqasepecLIPLGLMSDI- 854
Cdd:cd17933    68 ---HRLLGINPGGGGFY-YNEENP---LDADLLI-----------------------VDEAS-------MVDTRLMAALl 110
                         170       180
                  ....*....|....*....|.
gi 768031449  855 -----SGQIVLAGDPMQLGPV 870
Cdd:cd17933   111 saipaGARLILVGDPDQLPSV 131
AAA_19 pfam13245
AAA domain;
697-771 4.73e-04

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 41.43  E-value: 4.73e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768031449   697 QKLAVKRILSGDcrplPYILFGPPGTGKT---VTIIEAVLQVHFAlpDSRILVCAPSNSAADlvclRLHESkVLQPAT 771
Cdd:pfam13245    1 QREAVRTALPSK----VVLLTGGPGTGKTttiRHIVALLVALGGV--SFPILLAAPTGRAAK----RLSER-TGLPAS 67
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
692-734 3.55e-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: 39.44  E-value: 3.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 768031449  692 VLNENQKLAVKRILSGDcRPLPYILFGPPGTGKTvTIIEAVLQ 734
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 ...
697-755 6.64e-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: 6.64e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 768031449  697 QKLAVKRILSGDcrplPYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNSAAD 755
Cdd:cd18013     5 QKVAINFIIEHP----YCGLFLDMGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARS 59
ResIII pfam04851
Type III restriction enzyme, res subunit;
690-752 8.50e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 38.42  E-value: 8.50e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768031449   690 NPVLNENQKLAVKRIL-SGDCRPLPYILFGPPGTGKTVTIIEAVLQVHFALPDSRILVCAPSNS 752
Cdd:pfam04851    1 KLELRPYQIEAIENLLeSIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKD 64
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
651-737 9.00e-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: 9.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768031449  651 TEERRVGDKDLPVLAPFTAEMSDWVDEIQTPKARKMEFFNPVLNENQKLAVKRILS------------GDCRPLPYILFG 718
Cdd:COG0464   119 LELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEVKEELRELVAlplkrpelreeyGLPPPRGLLLYG 198
                          90       100
                  ....*....|....*....|..
gi 768031449  719 PPGTGKTvTIIEAV---LQVHF 737
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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