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Conserved domains on  [gi|45553113|ref|NP_996084|]
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helicase with zinc finger, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
805-1030 7.35e-144

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: 445.39  E-value: 7.35e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  805 KLNAKQREAVNAITTALSIKLPPILLIGPFGTGKTYTLAQAIKQLLTQPEAKILICTHSNSAADLYIKEYLHPWIEEGLK 884
Cdd:cd18077    1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPETRILICTHSNSAADLYIKEYLHPYVETGNP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  885 EATPLRVYYHKRWSATVNGVVQKYCITDGVGNFLRPTVEDIMRHRIVVVTLSISMELATLGLPKGLFTHIFLDEAAQAME 964
Cdd:cd18077   81 RARPLRVYYRNRWVKTVHPVVQKYCLIDEHGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQAME 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45553113  965 CEAIMPLALANDSTRIVLAGDHMQMSPELFSAFAKERKLHISLLERLYDHYPSNFPCKILLCENYR 1030
Cdd:cd18077  161 CEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSEHPCRILLCENYR 226
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
925-1236 4.35e-49

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


:

Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 189.95  E-value: 4.35e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  925 IMRHRIVVVTL-SISmelATLGLPKGLFTHIFLDEAAQAMECEAIMPLALANdstRIVLAGDHMQMSPELFS---AFAKE 1000
Cdd:COG1112  532 LELAPVVGMTPaSVA---RLLPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVFGeeaEEVAE 605
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113 1001 RKLHISLLERLYDHYPsnfPCKILLCENYRAHEAIIRFTSELFYEQKLVA---SGKQPRHDRFYPLTFFTTRGEDVQDKN 1077
Cdd:COG1112  606 EGLDESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDGVYERRGG 682
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113 1078 STafYNNAEVYEVVERVSELRKRWPsawgklNDTSIGIMTPYSDQVFRIRSELRKRRMGGISVERVLNV---QGKQFRAV 1154
Cdd:COG1112  683 SR--TNPEEAEAVVELVRELLEDGP------DGESIGVITPYRAQVALIRELLREALGDGLEPVFVGTVdrfQGDERDVI 754
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113 1155 FLSTVRTRRTCMPQGsapgsasttsigdadadYGFLSNS-KLLNTAITRAQSLVAVVGDPvALCSIGRCRKVWERFIEIC 1233
Cdd:COG1112  755 IFSLVYSNDEDVPRN-----------------FGFLNGGpRRLNVAVSRARRKLIVVGSR-ELLDSDPSTPALKRLLEYL 816

                 ...
gi 45553113 1234 DEH 1236
Cdd:COG1112  817 ERA 819
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
329-353 1.71e-04

Zinc finger C-x8-C-x5-C-x3-H type (and similar);


:

Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 40.25  E-value: 1.71e-04
                           10        20
                   ....*....|....*....|....*
gi 45553113    329 YSLCETFSEAHICHYGAQCVEAHGQ 353
Cdd:pfam00642    3 TELCRFFLRTGYCKYGDRCKFAHGQ 27
 
Name Accession Description Interval E-value
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
805-1030 7.35e-144

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: 445.39  E-value: 7.35e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  805 KLNAKQREAVNAITTALSIKLPPILLIGPFGTGKTYTLAQAIKQLLTQPEAKILICTHSNSAADLYIKEYLHPWIEEGLK 884
Cdd:cd18077    1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPETRILICTHSNSAADLYIKEYLHPYVETGNP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  885 EATPLRVYYHKRWSATVNGVVQKYCITDGVGNFLRPTVEDIMRHRIVVVTLSISMELATLGLPKGLFTHIFLDEAAQAME 964
Cdd:cd18077   81 RARPLRVYYRNRWVKTVHPVVQKYCLIDEHGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQAME 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45553113  965 CEAIMPLALANDSTRIVLAGDHMQMSPELFSAFAKERKLHISLLERLYDHYPSNFPCKILLCENYR 1030
Cdd:cd18077  161 CEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSEHPCRILLCENYR 226
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
925-1236 4.35e-49

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 189.95  E-value: 4.35e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  925 IMRHRIVVVTL-SISmelATLGLPKGLFTHIFLDEAAQAMECEAIMPLALANdstRIVLAGDHMQMSPELFS---AFAKE 1000
Cdd:COG1112  532 LELAPVVGMTPaSVA---RLLPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVFGeeaEEVAE 605
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113 1001 RKLHISLLERLYDHYPsnfPCKILLCENYRAHEAIIRFTSELFYEQKLVA---SGKQPRHDRFYPLTFFTTRGEDVQDKN 1077
Cdd:COG1112  606 EGLDESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDGVYERRGG 682
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113 1078 STafYNNAEVYEVVERVSELRKRWPsawgklNDTSIGIMTPYSDQVFRIRSELRKRRMGGISVERVLNV---QGKQFRAV 1154
Cdd:COG1112  683 SR--TNPEEAEAVVELVRELLEDGP------DGESIGVITPYRAQVALIRELLREALGDGLEPVFVGTVdrfQGDERDVI 754
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113 1155 FLSTVRTRRTCMPQGsapgsasttsigdadadYGFLSNS-KLLNTAITRAQSLVAVVGDPvALCSIGRCRKVWERFIEIC 1233
Cdd:COG1112  755 IFSLVYSNDEDVPRN-----------------FGFLNGGpRRLNVAVSRARRKLIVVGSR-ELLDSDPSTPALKRLLEYL 816

                 ...
gi 45553113 1234 DEH 1236
Cdd:COG1112  817 ERA 819
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
1003-1213 1.84e-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: 168.88  E-value: 1.84e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113   1003 LHISLLERLYDHYPSnfpCKILLCENYRAHEAIIRFTSELFYEQKLVASGKQPRH---------DRFYPLTFF-TTRGED 1072
Cdd:pfam13087    1 LDRSLFERLQELGPS---AVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERplpddfhlpDPLGPLVFIdVDGSEE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113   1073 VQDKNSTAFYNNAEVYEVVERVSELRKRWPSAWGKlndtsIGIMTPYSDQVFRIRSELRKRRMG--GISVERVLNVQGKQ 1150
Cdd:pfam13087   78 EESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSD-----IGVITPYRAQVRLIRKLLKRKLGGklEIEVNTVDGFQGRE 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553113   1151 FRAVFLSTVRTRRtcmpqgsapgsasttsigdaDADYGFLSNSKLLNTAITRAQSLVAVVGDP 1213
Cdd:pfam13087  153 KDVIIFSCVRSNE--------------------KGGIGFLSDPRRLNVALTRAKRGLIIVGNA 195
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
1032-1233 2.16e-47

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: 168.18  E-value: 2.16e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113 1032 HEAIIRFTSELFYEQKLVAS-------GKQPRHDRFYPLTFFTTRGEDVQDKNSTAFYNNAEVYEVVERVSELRKRWpsa 1104
Cdd:cd18808    2 HPEISEFPSKLFYEGKLKAGvsvaarlNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG--- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113 1105 wgkLNDTSIGIMTPYSDQVFRIRSELRKRRMG--GISVERVLNVQGKQFRAVFLSTVRTRRTCMPqgsapgsasttsigd 1182
Cdd:cd18808   79 ---VKPSSIGVITPYRAQVALIRELLRKRGGLleDVEVGTVDNFQGREKDVIILSLVRSNESGGS--------------- 140
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 45553113 1183 adadYGFLSNSKLLNTAITRAQSLVAVVGDPVALCSigrcRKVWERFIEIC 1233
Cdd:cd18808  141 ----IGFLSDPRRLNVALTRAKRGLIIVGNPDTLSK----DPLWKKLLEYL 183
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
657-1236 2.44e-42

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: 166.53  E-value: 2.44e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113    657 AGMATSTAKYSLAGEL--FALMRLGKDISEDT--SPGRLILSncssvyiskpedpdSKADPTKRAVYEALIEdKGKNVIY 732
Cdd:TIGR00376   25 RGRAILNLQGKIRGGLlgFLLVRFGRRKAIATeiSVGDIVLV--------------SRGNPLQSDLTGVVTR-VGKRFIT 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113    733 LKLSAKcVEAMALQadtelEVDIQFQLNRMPYCEWHNAVDKITDFR---LIFPATELEPS-IPWTPKKQWADSCepkLNA 808
Cdd:TIGR00376   90 VALEES-VPQWSLK-----RVRIDLYANDVTFKRMKEALRALTENHsrlLEFLLGREAPSkASEIHDFQFFDPN---LNE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113    809 KQREAVNAittALSIKlpPILLI-GPFGTGKTYTLAQAIKQLLTQPEaKILICTHSNSAADlYIKEYL-----------H 876
Cdd:TIGR00376  161 SQKEAVLF---ALSSK--DLFLIhGPPGTGKTRTVVELIRQLVKRGL-RVLVTAPSNIAVD-NLLERLalcdqkivrlgH 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113    877 P-----------------------------------------------WIEEGLKEATPLRVYYHKRWSATVNGVVQKYC 909
Cdd:TIGR00376  234 ParllksnkqhsldylienhpkyqivadirekidelieernkktkpspQKRRGLSDIKILRKALKKREARGIESLKIASM 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113    910 I--------TDGVGNFLRPTVEDIMRHRIVVVTLSISMElATLGLPKGLFTHIFLDEAAQAMECEAIMPLALANdstRIV 981
Cdd:TIGR00376  314 AewietnksIDRLLKLLPESEERIMNEILAESDATNSMA-GSEILNGQYFDVAVIDEASQAMEPSCLIPLLKAR---KLI 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113    982 LAGDHMQMSPELFSAFAKErkLHISLLERLYDHYPSNfpCKILLCEnYRAHEAIIRFTSELFYEQKLVASGKQPRH---- 1057
Cdd:TIGR00376  390 LAGDHKQLPPTILSHDAEE--LSLTLFERLIKEYPER--SRTLNVQ-YRMNQKIMEFPSREFYNGKLTAHESVANIllrd 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113   1058 -------------DRFYPLTFFTTRG---EDVQDKNSTAFYNNAEVYEVVERVSELRKRwpsawgKLNDTSIGIMTPYSD 1121
Cdd:TIGR00376  465 lpkveateseddlETGIPLLFIDTSGcelFELKEADSTSKYNPGEAELVSEIIQALVKM------GVPANDIGVITPYDA 538
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113   1122 QVFRIRsELRKRRMGGISVERVLNVQGKQFRAVFLSTVRTRRtcmpqgsapgsasttsigdaDADYGFLSNSKLLNTAIT 1201
Cdd:TIGR00376  539 QVDLLR-QLLEHRHIDIEVSSVDGFQGREKEVIIISFVRSNR--------------------KGEVGFLKDLRRLNVALT 597
                          650       660       670
                   ....*....|....*....|....*....|....*
gi 45553113   1202 RAQSLVAVVGDPVALcsigRCRKVWERFIEICDEH 1236
Cdd:TIGR00376  598 RARRKLIVIGDSRTL----SNHKFYKRLIEWCKQH 628
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
815-995 8.60e-11

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: 64.29  E-value: 8.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113    815 NAITTALSikLPPILLI-GPFGTGKTYTLAQAIKQLLTQPEA------KILICTHSNSAAD----LYIKEYL-------- 875
Cdd:pfam13086    4 EAIRSALS--SSHFTLIqGPPGTGKTTTIVELIRQLLSYPATsaaagpRILVCAPSNAAVDnileRLLRKGQkygpkivr 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113    876 --HP-WIEEGLKEAT---PLRVYYHKRWSAT---------------------VNGVVQKYCITDGVGNFLRPTVEDIM-- 926
Cdd:pfam13086   82 igHPaAISEAVLPVSldyLVESKLNNEEDAQivkdiskeleklakalrafekEIIVEKLLKSRNKDKSKLEQERRKLRse 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113    927 ---------------------RHRIVVVTLSISMELATLGLPKglFTHIFLDEAAQAMECEAIMPLALAndSTRIVLAGD 985
Cdd:pfam13086  162 rkelrkelrrreqslereildEAQIVCSTLSGAGSRLLSSLAN--FDVVIIDEAAQALEPSTLIPLLRG--PKKVVLVGD 237
                          250
                   ....*....|
gi 45553113    986 HMQMSPELFS 995
Cdd:pfam13086  238 PKQLPPTVIS 247
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
803-959 5.96e-07

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 54.65  E-value: 5.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  803 EPKLNAKQREAVNAITTALSIKLPPILLIGPFGTGKTYTLAQAIKQLLTQPeaKILICTHSnsaadlyiKEYLHPWIEEg 882
Cdd:COG1061   78 SFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGK--RVLVLVPR--------RELLEQWAEE- 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  883 LKEATPLRVYYHKRWSATvngvvqkycitdgvgnflrptvedimrHRIVVVT---LSISMELATLGlpkGLFTHIFLDEA 959
Cdd:COG1061  147 LRRFLGDPLAGGGKKDSD---------------------------APITVATyqsLARRAHLDELG---DRFGLVIIDEA 196
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
329-353 1.71e-04

Zinc finger C-x8-C-x5-C-x3-H type (and similar);


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 40.25  E-value: 1.71e-04
                           10        20
                   ....*....|....*....|....*
gi 45553113    329 YSLCETFSEAHICHYGAQCVEAHGQ 353
Cdd:pfam00642    3 TELCRFFLRTGYCKYGDRCKFAHGQ 27
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
824-883 1.47e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 41.20  E-value: 1.47e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113     824 KLPPILLIGPFGTGKTyTLAQAIKQLLTQPEAKILICTHSNSAADLYIKEYLHPWIEEGL 883
Cdd:smart00382    1 PGEVILIVGPPGSGKT-TLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKA 59
 
Name Accession Description Interval E-value
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
805-1030 7.35e-144

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: 445.39  E-value: 7.35e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  805 KLNAKQREAVNAITTALSIKLPPILLIGPFGTGKTYTLAQAIKQLLTQPEAKILICTHSNSAADLYIKEYLHPWIEEGLK 884
Cdd:cd18077    1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPETRILICTHSNSAADLYIKEYLHPYVETGNP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  885 EATPLRVYYHKRWSATVNGVVQKYCITDGVGNFLRPTVEDIMRHRIVVVTLSISMELATLGLPKGLFTHIFLDEAAQAME 964
Cdd:cd18077   81 RARPLRVYYRNRWVKTVHPVVQKYCLIDEHGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQAME 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45553113  965 CEAIMPLALANDSTRIVLAGDHMQMSPELFSAFAKERKLHISLLERLYDHYPSNFPCKILLCENYR 1030
Cdd:cd18077  161 CEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSEHPCRILLCENYR 226
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
806-1030 5.77e-78

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: 257.93  E-value: 5.77e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  806 LNAKQREAVNAITTALSiKLPPILLIGPFGTGKTYTLAQAIKQLL-TQPEAKILICTHSNSAADLYIKEYLHpwieEGLK 884
Cdd:cd18038    2 LNDEQKLAVRNIVTGTS-RPPPYIIFGPPGTGKTVTLVEAILQVLrQPPEARILVCAPSNSAADLLAERLLN----ALVT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  885 EATPLRVYYHKRWSATVNGVVQKYCITDGVGNFLRPTVEDIMRHRIVVVTLSISMELATLGLPKGLFTHIFLDEAAQAME 964
Cdd:cd18038   77 KREILRLNAPSRDRASVPPELLPYCNSKAEGTFRLPSLEELKKYRIVVCTLMTAGRLVQAGVPNGHFTHIFIDEAGQATE 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553113  965 CEAIMPLA-LANDSTRIVLAGDHMQMSPELFSAFAKERKLHISLLERLYDHYPS------NFPCKILLCENYR 1030
Cdd:cd18038  157 PEALIPLSeLASKNTQIVLAGDPKQLGPVVRSPLARKYGLGKSLLERLMERPLYykdgeyNPSYITKLLKNYR 229
DEXXQc_HELZ2-N cd18076
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
806-1030 8.61e-70

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: 234.40  E-value: 8.61e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  806 LNAKQREAVNAITTALS--IKLPPILLIGPFGTGKTYTLAQAIKQLLTQPEAKILICTHSNSAADLYIKEYLHPWIEEGL 883
Cdd:cd18076    2 GNNKQQLAFNFIAGKPSeaRFVPPLLIYGPFGTGKTFTLAMAALEVIREPGTKVLICTHTNSAADIYIREYFHPYVDKGH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  884 KEATPLRVYYHKRWSATVNGVVQKY-CITDGVGNFLRPTVEDIMRHRIVVVTLSISMELATlglPKGLFTHIFLDEAAQA 962
Cdd:cd18076   82 PEARPLRIKATDRPNAITDPDTITYcCLTKDRQCFRLPTRDELDFHNIVITTTAMAFNLHV---LSGFFTHIFIDEAAQM 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553113  963 MECEAIMPLALANDSTRIVLAGDHMQMSPELFSAfAKERKLHISLLERLYDHYPSN-----FPCKILLCENYR 1030
Cdd:cd18076  159 LECEALIPLSYAGPKTRVVLAGDHMQMTPKLFSV-ADYNRANHTLLNRLFHYYQGEkhevaVKSRVIFSENYR 230
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
925-1236 4.35e-49

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 189.95  E-value: 4.35e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  925 IMRHRIVVVTL-SISmelATLGLPKGLFTHIFLDEAAQAMECEAIMPLALANdstRIVLAGDHMQMSPELFS---AFAKE 1000
Cdd:COG1112  532 LELAPVVGMTPaSVA---RLLPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVFGeeaEEVAE 605
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113 1001 RKLHISLLERLYDHYPsnfPCKILLCENYRAHEAIIRFTSELFYEQKLVA---SGKQPRHDRFYPLTFFTTRGEDVQDKN 1077
Cdd:COG1112  606 EGLDESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDGVYERRGG 682
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113 1078 STafYNNAEVYEVVERVSELRKRWPsawgklNDTSIGIMTPYSDQVFRIRSELRKRRMGGISVERVLNV---QGKQFRAV 1154
Cdd:COG1112  683 SR--TNPEEAEAVVELVRELLEDGP------DGESIGVITPYRAQVALIRELLREALGDGLEPVFVGTVdrfQGDERDVI 754
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113 1155 FLSTVRTRRTCMPQGsapgsasttsigdadadYGFLSNS-KLLNTAITRAQSLVAVVGDPvALCSIGRCRKVWERFIEIC 1233
Cdd:COG1112  755 IFSLVYSNDEDVPRN-----------------FGFLNGGpRRLNVAVSRARRKLIVVGSR-ELLDSDPSTPALKRLLEYL 816

                 ...
gi 45553113 1234 DEH 1236
Cdd:COG1112  817 ERA 819
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
1003-1213 1.84e-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: 168.88  E-value: 1.84e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113   1003 LHISLLERLYDHYPSnfpCKILLCENYRAHEAIIRFTSELFYEQKLVASGKQPRH---------DRFYPLTFF-TTRGED 1072
Cdd:pfam13087    1 LDRSLFERLQELGPS---AVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERplpddfhlpDPLGPLVFIdVDGSEE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113   1073 VQDKNSTAFYNNAEVYEVVERVSELRKRWPSAWGKlndtsIGIMTPYSDQVFRIRSELRKRRMG--GISVERVLNVQGKQ 1150
Cdd:pfam13087   78 EESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSD-----IGVITPYRAQVRLIRKLLKRKLGGklEIEVNTVDGFQGRE 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553113   1151 FRAVFLSTVRTRRtcmpqgsapgsasttsigdaDADYGFLSNSKLLNTAITRAQSLVAVVGDP 1213
Cdd:pfam13087  153 KDVIIFSCVRSNE--------------------KGGIGFLSDPRRLNVALTRAKRGLIIVGNA 195
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
1032-1233 2.16e-47

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: 168.18  E-value: 2.16e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113 1032 HEAIIRFTSELFYEQKLVAS-------GKQPRHDRFYPLTFFTTRGEDVQDKNSTAFYNNAEVYEVVERVSELRKRWpsa 1104
Cdd:cd18808    2 HPEISEFPSKLFYEGKLKAGvsvaarlNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG--- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113 1105 wgkLNDTSIGIMTPYSDQVFRIRSELRKRRMG--GISVERVLNVQGKQFRAVFLSTVRTRRTCMPqgsapgsasttsigd 1182
Cdd:cd18808   79 ---VKPSSIGVITPYRAQVALIRELLRKRGGLleDVEVGTVDNFQGREKDVIILSLVRSNESGGS--------------- 140
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 45553113 1183 adadYGFLSNSKLLNTAITRAQSLVAVVGDPVALCSigrcRKVWERFIEIC 1233
Cdd:cd18808  141 ----IGFLSDPRRLNVALTRAKRGLIIVGNPDTLSK----DPLWKKLLEYL 183
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
657-1236 2.44e-42

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: 166.53  E-value: 2.44e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113    657 AGMATSTAKYSLAGEL--FALMRLGKDISEDT--SPGRLILSncssvyiskpedpdSKADPTKRAVYEALIEdKGKNVIY 732
Cdd:TIGR00376   25 RGRAILNLQGKIRGGLlgFLLVRFGRRKAIATeiSVGDIVLV--------------SRGNPLQSDLTGVVTR-VGKRFIT 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113    733 LKLSAKcVEAMALQadtelEVDIQFQLNRMPYCEWHNAVDKITDFR---LIFPATELEPS-IPWTPKKQWADSCepkLNA 808
Cdd:TIGR00376   90 VALEES-VPQWSLK-----RVRIDLYANDVTFKRMKEALRALTENHsrlLEFLLGREAPSkASEIHDFQFFDPN---LNE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113    809 KQREAVNAittALSIKlpPILLI-GPFGTGKTYTLAQAIKQLLTQPEaKILICTHSNSAADlYIKEYL-----------H 876
Cdd:TIGR00376  161 SQKEAVLF---ALSSK--DLFLIhGPPGTGKTRTVVELIRQLVKRGL-RVLVTAPSNIAVD-NLLERLalcdqkivrlgH 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113    877 P-----------------------------------------------WIEEGLKEATPLRVYYHKRWSATVNGVVQKYC 909
Cdd:TIGR00376  234 ParllksnkqhsldylienhpkyqivadirekidelieernkktkpspQKRRGLSDIKILRKALKKREARGIESLKIASM 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113    910 I--------TDGVGNFLRPTVEDIMRHRIVVVTLSISMElATLGLPKGLFTHIFLDEAAQAMECEAIMPLALANdstRIV 981
Cdd:TIGR00376  314 AewietnksIDRLLKLLPESEERIMNEILAESDATNSMA-GSEILNGQYFDVAVIDEASQAMEPSCLIPLLKAR---KLI 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113    982 LAGDHMQMSPELFSAFAKErkLHISLLERLYDHYPSNfpCKILLCEnYRAHEAIIRFTSELFYEQKLVASGKQPRH---- 1057
Cdd:TIGR00376  390 LAGDHKQLPPTILSHDAEE--LSLTLFERLIKEYPER--SRTLNVQ-YRMNQKIMEFPSREFYNGKLTAHESVANIllrd 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113   1058 -------------DRFYPLTFFTTRG---EDVQDKNSTAFYNNAEVYEVVERVSELRKRwpsawgKLNDTSIGIMTPYSD 1121
Cdd:TIGR00376  465 lpkveateseddlETGIPLLFIDTSGcelFELKEADSTSKYNPGEAELVSEIIQALVKM------GVPANDIGVITPYDA 538
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113   1122 QVFRIRsELRKRRMGGISVERVLNVQGKQFRAVFLSTVRTRRtcmpqgsapgsasttsigdaDADYGFLSNSKLLNTAIT 1201
Cdd:TIGR00376  539 QVDLLR-QLLEHRHIDIEVSSVDGFQGREKEVIIISFVRSNR--------------------KGEVGFLKDLRRLNVALT 597
                          650       660       670
                   ....*....|....*....|....*....|....*
gi 45553113   1202 RAQSLVAVVGDPVALcsigRCRKVWERFIEICDEH 1236
Cdd:TIGR00376  598 RARRKLIVIGDSRTL----SNHKFYKRLIEWCKQH 628
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
805-1030 2.47e-42

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: 155.60  E-value: 2.47e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  805 KLNAKQREAVNAITTALSIKLPPILLiGPFGTGKTYTLAQAIKQLLTQ-PEAKILICTHSNSAADLyIKEYLHP--WIEE 881
Cdd:cd18078    1 DLNELQKEAVKRILGGECRPLPYILF-GPPGTGKTVTIIEAILQVVYNlPRSRILVCAPSNSAADL-VTSRLHEskVLKP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  882 GlkeaTPLRVYYHKRWSATVNGVVQKYCItdgvgnfLRPTVEDIMRHRIVVVTLSISMELATLGLPKGLFTHIFLDEAAQ 961
Cdd:cd18078   79 G----DMVRLNAVNRFESTVIDARKLYCR-------LGEDLSKASRHRIVISTCSTAGLLYQMGLPVGHFTHVFVDEAGQ 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  962 AMECEAIMPLALANDST-RIVLAGDHMQMSPELFSAFAKERKLHISLLERL-----YDHYPSNFPCKIL--------LCE 1027
Cdd:cd18078  148 ATEPESLIPLGLISSRDgQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLmnrplYLRDPNRFGESGGynpllvtkLVD 227

                 ...
gi 45553113 1028 NYR 1030
Cdd:cd18078  228 NYR 230
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
805-1030 5.36e-26

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


Pssm-ID: 350802 [Multi-domain]  Cd Length: 191  Bit Score: 107.31  E-value: 5.36e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  805 KLNAKQREAVNaittaLSIKLPPILLI-GPFGTGKTYTLAQAIKQLLtQPEAKILICTHSNSAADlYIKEYLhpwIEEGL 883
Cdd:cd18044    1 NLNDSQKEAVK-----FALSQKDVALIhGPPGTGKTTTVVEIILQAV-KRGEKVLACAPSNIAVD-NLVERL---VALKV 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  884 KeatPLRVYYHKRwsatVNGVVQKYCItdgvgnflrptvEDIMRHRIVVVTLSISMelATLGLPKGLFTHIFLDEAAQAM 963
Cdd:cd18044   71 K---VVRIGHPAR----LLESVLDHSL------------DALVAAQVVLATNTGAG--SRQLLPNELFDVVVIDEAAQAL 129
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45553113  964 ECEAIMPLALANdstRIVLAGDHMQMSPELFSAFAKERKLHISLLERLYDHYPSNfpCKILLCENYR 1030
Cdd:cd18044  130 EASCWIPLLKAR---RCILAGDHKQLPPTILSDKAARGGLGVTLFERLVNLYGES--VVRMLTVQYR 191
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
805-1030 9.32e-20

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: 89.60  E-value: 9.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  805 KLNAKQREAVNAITTALSIKLppILliGPFGTGKTYTLAQAIKQLLTQPEaKILICTHSNSAAD-LYIKeyLHPWIEEGL 883
Cdd:cd18041    1 GLNKDQRQAIKKVLNAKDYAL--IL--GMPGTGKTTTIAALVRILVALGK-SVLLTSYTHSAVDnILLK--LKKFGVNFL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  884 KEATPLRVyyHKRwsatvngvVQKYCITDGVGNFlrPTVEDI----MRHRIVVVT-LSISMELatlgLPKGLFTHIFLDE 958
Cdd:cd18041   74 RLGRLKKI--HPD--------VQEFTLEAILKSC--KSVEELeskyESVSVVATTcLGINHPI----FRRRTFDYCIVDE 137
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45553113  959 AAQAMECEAIMPLALANdstRIVLAGDHMQMSPELFSAFAKERKLHISLLERLYDHYPSNFpckILLCENYR 1030
Cdd:cd18041  138 ASQITLPICLGPLRLAK---KFVLVGDHYQLPPLVKSREARELGMDESLFKRLSEAHPDAV---VQLTIQYR 203
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
805-1030 8.88e-19

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: 87.69  E-value: 8.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  805 KLNAKQreaVNAITTALSiklPPILLI-GPFGTGKTYTLAQAIKQLLTQPEAKILICTHSNSAADlYIKEYLHpwiEEGL 883
Cdd:cd18039    1 ELNHSQ---VDAVKTALQ---RPLSLIqGPPGTGKTVTSATIVYHLVKQGNGPVLVCAPSNVAVD-QLTEKIH---QTGL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  884 K---------EATPLRVYY---HK--RWSATVNGVVQKYCITDGVGNF----------LRPTVE-DIMRHRIVVVTLSIS 938
Cdd:cd18039   71 KvvrlcaksrEAVESPVSFlalHNqvRNLDSAEKLELLKLLKLETGELssadekryrkLKRKAErELLRNADVICCTCVG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  939 MelATLGLPKGLFTHIFLDEAAQAMECEAIMPLALAndSTRIVLAGDHMQMSPELFSAFAKERKLHISLLERLYD--HYP 1016
Cdd:cd18039  151 A--GDPRLSKMKFRTVLIDEATQATEPECLIPLVHG--AKQVILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVQlgIRP 226
                        250
                 ....*....|....
gi 45553113 1017 snfpckILLCENYR 1030
Cdd:cd18039  227 ------IRLQVQYR 234
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
806-1030 4.56e-17

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: 82.26  E-value: 4.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  806 LNAKQREAVNAITtalsIKLPPILLI-GPFGTGKTYTL------------------------AQAIKQLLTQPEAKILIC 860
Cdd:cd18042    1 LNESQLEAIASAL----QNSPGITLIqGPPGTGKTKTIvgilsvllagkyrkyyekvkkklrKLQRNLNNKKKKNRILVC 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  861 THSNSAADlyikEYLHPWIEEGLKeatplrvyyhkrwsatvngvvqkycitDGVGNFLRPTV-----EDIMRH-----RI 930
Cdd:cd18042   77 APSNAAVD----EIVLRLLSEGFL---------------------------DGDGRSYKPNVvrvgrQELRASilneaDI 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  931 VVVTLSIS--MELATLGLPkglFTHIFLDEAAQAMECEAIMPLALanDSTRIVLAGDHMQMSPELFSAFAKERKLHISLL 1008
Cdd:cd18042  126 VCTTLSSSgsDLLESLPRG---FDTVIIDEAAQAVELSTLIPLRL--GCKRLILVGDPKQLPATVFSKVAQKLGYDRSLF 200
                        250       260
                 ....*....|....*....|..
gi 45553113 1009 ERLYDHypsNFPCkILLCENYR 1030
Cdd:cd18042  201 ERLQLA---GYPV-LMLTTQYR 218
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
806-1024 1.74e-12

EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that represses class II MHC (major histocompatibility complex) gene expression. NFX1 binds a conserved cis-acting element, termed the X-box, in promoters of human class II MHC genes. The Cys-rich region contains several NFX1-type zinc finger domains. Frequently, a R3H domain is present in the C-terminus, and a RING finger domain and a PAM2 motif are present in the N-terminus. The lack of R3H and PAM2 motifs in the plant proteins indicates functional differences. Plant NFX1-like proteins are proposed to modulate growth and survival by coordinating reactive oxygen species, salicylic acid, further biotic stress and abscisic acid responses. A common feature of all members may be E3 ubiquitin ligase, due to the presence of a RING finger domain, as well as DNA binding. NFX1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350694 [Multi-domain]  Cd Length: 178  Bit Score: 67.95  E-value: 1.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  806 LNAKQREA-VNAITTALSIklppilLIGPFGTGKTYTLAQAIKQLLT----QPEAKILICTHSNSAADlyikEYLhpwie 880
Cdd:cd17936    2 LDPSQLEAlKHALTSELAL------IQGPPGTGKTFLGVKLVRALLQnqdlSITGPILVVCYTNHALD----QFL----- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  881 EGLKEATPlrvyyhkrwsatvngvvqkycitdgvgnflrptvEDIMRH--RIVVVTLSISMELATLgLPKGLFTHIFLDE 958
Cdd:cd17936   67 EGLLDFGP----------------------------------TKIVRLgaRVIGMTTTGAAKYREL-LQALGPKVVIVEE 111
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45553113  959 AAQAMECEAIMplALANDSTRIVLAGDHMQMSP--ELFSAFAKERKLHISLLERLYDhypSNFPCKIL 1024
Cdd:cd17936  112 AAEVLEAHILA--ALTPSTEHLILIGDHKQLRPkvNVYELTAKKYNLDVSLFERLVK---NGLPFVTL 174
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
829-1030 7.88e-12

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


Pssm-ID: 438708 [Multi-domain]  Cd Length: 121  Bit Score: 64.18  E-value: 7.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  829 LLIGPFGTGKTYTLAQAIKQLLTQ-PEAKILICTHSNSAADlyikeylhpwieeglkeatplrvyyhkrwsatvNgvvqk 907
Cdd:cd17934    3 LIQGPPGTGKTTTIAAIVLQLLKGlRGKRVLVTAQSNVAVD---------------------------------N----- 44
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  908 ycitdgvgnflrptvedimrhrivvvtlsismelatlglpkglFTHIFLDEAAQAMECEAIMPLALAndsTRIVLAGDHM 987
Cdd:cd17934   45 -------------------------------------------VDVVIIDEASQITEPELLIALIRA---KKVVLVGDPK 78
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 45553113  988 QMSPELFS--AFAKERKLHISLLERLYDHYPsNFPcKILLCENYR 1030
Cdd:cd17934   79 QLPPVVQEdhAALLGLSFILSLLLLFRLLLP-GSP-KVMLDTQYR 121
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
815-995 8.60e-11

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: 64.29  E-value: 8.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113    815 NAITTALSikLPPILLI-GPFGTGKTYTLAQAIKQLLTQPEA------KILICTHSNSAAD----LYIKEYL-------- 875
Cdd:pfam13086    4 EAIRSALS--SSHFTLIqGPPGTGKTTTIVELIRQLLSYPATsaaagpRILVCAPSNAAVDnileRLLRKGQkygpkivr 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113    876 --HP-WIEEGLKEAT---PLRVYYHKRWSAT---------------------VNGVVQKYCITDGVGNFLRPTVEDIM-- 926
Cdd:pfam13086   82 igHPaAISEAVLPVSldyLVESKLNNEEDAQivkdiskeleklakalrafekEIIVEKLLKSRNKDKSKLEQERRKLRse 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113    927 ---------------------RHRIVVVTLSISMELATLGLPKglFTHIFLDEAAQAMECEAIMPLALAndSTRIVLAGD 985
Cdd:pfam13086  162 rkelrkelrrreqslereildEAQIVCSTLSGAGSRLLSSLAN--FDVVIIDEAAQALEPSTLIPLLRG--PKKVVLVGD 237
                          250
                   ....*....|
gi 45553113    986 HMQMSPELFS 995
Cdd:pfam13086  238 PKQLPPTVIS 247
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
805-1011 5.57e-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: 58.21  E-value: 5.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  805 KLNAKQreaVNAITTALSIKLppILLIGPFGTGKTYTLAQAIKQLL-TQPEAKILICTHSNSAA-DLYIKeylhpwIEEg 882
Cdd:cd17935    5 KFTPTQ---IEAIRSGMQPGL--TMVVGPPGTGKTDVAVQIISNLYhNFPNQRTLIVTHSNQALnQLFEK------IMA- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  883 lkeatpLRVYyhkrwsatvngvvQKYCITDGVGNflrptvedimrhRIVVVT-LSISMELATLgLPKGL-FTHIFLDEAA 960
Cdd:cd17935   73 ------LDID-------------ERHLLRLGHGA------------KIIAMTcTHAALKRGEL-VELGFkYDNILMEEAA 120
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 45553113  961 QAMECEAIMPLALANDST------RIVLAGDHMQMSPELFS-AFAKERKLHISLLERL 1011
Cdd:cd17935  121 QILEIETFIPLLLQNPEDgpnrlkRLIMIGDHHQLPPVIKNmAFQKYSNMEQSLFTRL 178
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
805-1011 1.05e-07

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: 55.61  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  805 KLNAKQREAV-NAITTalsiklPPILLIGPFGTGKTYT----------LAQAIKQLLTQPEAK--ILICTHSNSAADLyI 871
Cdd:cd18040    1 KLNPSQNHAVrTALTK------PFTLIQGPPGTGKTVTgvhiaywfakQNREIQSVSGEGDGGpcVLYCGPSNKSVDV-V 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  872 KEYLHPwiEEGLKeatPLRVY----------------------------YHKRWSATVNGVVQK----YC--ITDGVGNF 917
Cdd:cd18040   74 AELLLK--VPGLK---ILRVYseqietteypipneprhpnkksereskpNSELSSITLHHRIRQpsnpHSqqIKAFEARF 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  918 LRP----TVEDIMRHRIVVVTLSISmELATLGL---------PKGLFTH-----IFLDEAAQAMECEAIMPLALANDSTR 979
Cdd:cd18040  149 ERTqekiTEEDIKTYKILIWEARFE-ELETVDVilctcseaaSQKMRTHanvkqCIVDECGMCTEPESLIPIVSAPRAEQ 227
                        250       260       270
                 ....*....|....*....|....*....|..
gi 45553113  980 IVLAGDHMQMSPELFSAFAKERKLHISLLERL 1011
Cdd:cd18040  228 VVLIGDHKQLRPVVQNKEAQKLGLGRSLFERY 259
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
807-994 5.92e-07

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: 50.27  E-value: 5.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  807 NAKQREAVNAITTALSIklppiLLIGPFGTGKTYTLAQAIKQLLTQPEaKILICTHSNSAADlyikeylhpwieeglkea 886
Cdd:cd18043    1 DSSQEAAIISARNGKNV-----VIQGPPGTGKSQTIANIIANALARGK-RVLFVSEKKAALD------------------ 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  887 tplrvyyhkrwsatvngVVQKYCItdgvgnflrptvedIMRHRIVvvtlsismeLATLGLPKGLFTHIFLDEAAQAMECE 966
Cdd:cd18043   57 -----------------VVRFPCW--------------IMSPLSV---------SQYLPLNRNLFDLVIFDEASQIPIEE 96
                        170       180
                 ....*....|....*....|....*...
gi 45553113  967 AIMPLALANdstRIVLAGDHMQMSPELF 994
Cdd:cd18043   97 ALPALFRGK---QVVVVGDDKQLPPSIL 121
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
803-959 5.96e-07

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 54.65  E-value: 5.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  803 EPKLNAKQREAVNAITTALSIKLPPILLIGPFGTGKTYTLAQAIKQLLTQPeaKILICTHSnsaadlyiKEYLHPWIEEg 882
Cdd:COG1061   78 SFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGK--RVLVLVPR--------RELLEQWAEE- 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  883 LKEATPLRVYYHKRWSATvngvvqkycitdgvgnflrptvedimrHRIVVVT---LSISMELATLGlpkGLFTHIFLDEA 959
Cdd:COG1061  147 LRRFLGDPLAGGGKKDSD---------------------------APITVATyqsLARRAHLDELG---DRFGLVIIDEA 196
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
809-991 3.19e-06

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: 49.09  E-value: 3.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  809 KQREAVNAITTAlsiklPPILLIGPFGTGKTYTLAQAIKqLLTQPEAKILICTHSNSAADlyikeylhpwieeGLKEATP 888
Cdd:cd17933    1 EQKAAVRLVLRN-----RVSVLTGGAGTGKTTTLKALLA-ALEAEGKRVVLAAPTGKAAK-------------RLSESTG 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  889 LRVYyhkrwsaTvngvVQKYCITDGVGNFLRPTVEDIMRHRIVVVTlSISMelatLGLPkgLFTHIfldeaaqameceai 968
Cdd:cd17933   62 IEAS-------T----IHRLLGINPGGGGFYYNEENPLDADLLIVD-EASM----VDTR--LMAAL-------------- 109
                        170       180
                 ....*....|....*....|...
gi 45553113  969 mpLALANDSTRIVLAGDHMQMSP 991
Cdd:cd17933  110 --LSAIPAGARLILVGDPDQLPS 130
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
810-886 7.03e-06

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: 47.91  E-value: 7.03e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45553113  810 QREAVNAITTALSIK-LPPILLIGPFGTGKTyTLAQAIKQLLTQPEAKILICTHSNSAADLYIKEYLHPWIEEGLKEA 886
Cdd:cd00009    3 QEEAIEALREALELPpPKNLLLYGPPGTGKT-TLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFEL 79
ResIII pfam04851
Type III restriction enzyme, res subunit;
803-959 1.87e-05

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 46.90  E-value: 1.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113    803 EPKLNAKQREAVNAITTALSIKLPPILLIGPFGTGKTYTLAQAIKQLLTQ-PEAKILICTHSNsaaDLYIKeylhpWIEE 881
Cdd:pfam04851    1 KLELRPYQIEAIENLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKgPIKKVLFLVPRK---DLLEQ-----ALEE 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113    882 glkeatplrvyYHKRWSATVNGvvqkycITDGVGNFLRPTVEDImrhRIVVVT---LSISMELATLGLPKGLFTHIFLDE 958
Cdd:pfam04851   73 -----------FKKFLPNYVEI------GEIISGDKKDESVDDN---KIVVTTiqsLYKALELASLELLPDFFDVIIIDE 132

                   .
gi 45553113    959 A 959
Cdd:pfam04851  133 A 133
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
810-865 4.16e-05

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs 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: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 46.02  E-value: 4.16e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 45553113  810 QREAVNAITTALSIKLPPILLIGPFGTGKTYTLAQAIKQLL-TQPEAKILICTHSNS 865
Cdd:cd18032    5 QQEAIEALEEAREKGQRRALLVMATGTGKTYTAAFLIKRLLeANRKKRILFLAHREE 61
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
744-867 4.88e-05

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: 48.43  E-value: 4.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  744 ALQADTELEVDIQFQLNRMPYCEWHNAVDKITDFRLIFPATELEPSIPWtpkkqWADSCEPKLNAKQREAVNAITTALSI 823
Cdd:COG0507   68 ALVESGPLVLDGRRYLTRLLEAEQRLARRLRRLARPALDEADVEAALAA-----LEPRAGITLSDEQREAVALALTTRRV 142
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 45553113  824 klppILLIGPFGTGKTYTLAqAIKQLLTQPEAKILICTHSNSAA 867
Cdd:COG0507  143 ----SVLTGGAGTGKTTTLR-ALLAALEALGLRVALAAPTGKAA 181
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
827-868 6.15e-05

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: 44.40  E-value: 6.15e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 45553113  827 PILLIGPFGTGKTYTLAQAIKQLLTQ---PEAKILICTHSNSAAD 868
Cdd:cd17914    1 LSLIQGPPGTGKTRVLVKIVAALMQNkngEPGRILLVTPTNKAAA 45
UvrD-helicase pfam00580
UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural ...
806-868 8.36e-05

UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural domains. The Rep family function as dimers. REP helicases catalyze ATP dependent unwinding of double stranded DNA to single stranded DNA. Swiss:P23478, Swiss:P08394 have large insertions near to the carboxy-terminus relative to other members of the family.


Pssm-ID: 395462 [Multi-domain]  Cd Length: 267  Bit Score: 46.47  E-value: 8.36e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45553113    806 LNAKQREAVNAITTalsiklpPILLIGPFGTGKTYTLAQAIKQLLTQ----PEaKILICTHSNSAAD 868
Cdd:pfam00580    1 LNPEQRKAVTHLGG-------PLLVLAGAGSGKTRVLTERIAYLILEggidPE-EILAVTFTNKAAR 59
DEXQc_UvrD cd17932
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch ...
807-1029 1.08e-04

DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. UvrD 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: 350690 [Multi-domain]  Cd Length: 189  Bit Score: 45.20  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  807 NAKQREAVNAITTalsiklpPILLI-GPfGTGKTYTLAQAIKQLL----TQPEaKILICTHSNSAADlYIKEYLHPWIee 881
Cdd:cd17932    1 NPEQREAVTHPDG-------PLLVLaGA-GSGKTRVLTHRIAYLIleggVPPE-RILAVTFTNKAAK-EMRERLRKLL-- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113  882 GLKEATPLRVY-YHkrwsATVNGVVQKYcitdgvGNFlrptvEDIMRHrivvvTLSIsMELATLGLPK--GLFTHIFLDE 958
Cdd:cd17932   69 GEQLASGVWIGtFH----SFALRILRRY------GDF-----DDLLLY-----ALEL-LEENPDVREKlqSRFRYILVDE 127
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45553113  959 A-----AQamecEAIMpLALANDSTRIVLAGDHMQmspelfS--AFakeRKLHISLLERLYDHYPSnfPCKILLCENY 1029
Cdd:cd17932  128 YqdtnpLQ----YELL-KLLAGDGKNLFVVGDDDQ------SiyGF---RGADPENILDFEKDFPD--AKVIKLEENY 189
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
329-353 1.71e-04

Zinc finger C-x8-C-x5-C-x3-H type (and similar);


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 40.25  E-value: 1.71e-04
                           10        20
                   ....*....|....*....|....*
gi 45553113    329 YSLCETFSEAHICHYGAQCVEAHGQ 353
Cdd:pfam00642    3 TELCRFFLRTGYCKYGDRCKFAHGQ 27
UvrD COG0210
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
805-867 3.31e-04

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


Pssm-ID: 439980 [Multi-domain]  Cd Length: 721  Bit Score: 45.70  E-value: 3.31e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45553113  805 KLNAKQREAVNAIttalsikLPPILLI-GPfGTGKTYTLAQAIKQLLTQ----PEaKILICTHSNSAA 867
Cdd:COG0210    6 GLNPEQRAAVEHP-------EGPLLVLaGA-GSGKTRVLTHRIAYLIAEggvdPE-QILAVTFTNKAA 64
AAA_19 pfam13245
AAA domain;
810-868 5.36e-04

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 42.21  E-value: 5.36e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45553113    810 QREAVNAITTAlsiklPPILLIGPFGTGKTYTLAQAIKQLLT--QPEAKILICTHSNSAAD 868
Cdd:pfam13245    1 QREAVRTALPS-----KVVLLTGGPGTGKTTTIRHIVALLVAlgGVSFPILLAAPTGRAAK 56
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
806-991 7.02e-04

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: 42.94  E-value: 7.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113    806 LNAKQREAVNAITT---ALSIklppilLIGPFGTGKTYTLAqAIKQLLTQPEAKILICTHSNSAADlyikeylhpwieeG 882
Cdd:pfam13604    2 LNAEQAAAVRALLTsgdRVAV------LVGPAGTGKTTALK-ALREAWEAAGYRVIGLAPTGRAAK-------------V 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113    883 LKEATPLRvyyhkrwSATVNGVVqkYCITDGVgnflrptveDIMRHRIVVVtlsismelatlglpkglfthiflDEAAQA 962
Cdd:pfam13604   62 LGEELGIP-------ADTIAKLL--HRLGGRA---------GLDPGTLLIV-----------------------DEAGMV 100
                          170       180       190
                   ....*....|....*....|....*....|
gi 45553113    963 MECEAIMPLALANDS-TRIVLAGDHMQMSP 991
Cdd:pfam13604  101 GTRQMARLLKLAEDAgARVILVGDPRQLPS 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
824-883 1.47e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 41.20  E-value: 1.47e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553113     824 KLPPILLIGPFGTGKTyTLAQAIKQLLTQPEAKILICTHSNSAADLYIKEYLHPWIEEGL 883
Cdd:smart00382    1 PGEVILIVGPPGSGKT-TLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKA 59
AAA_22 pfam13401
AAA domain;
828-872 2.00e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 40.40  E-value: 2.00e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 45553113    828 ILLIGPFGTGKTYTLAQAIKQLLTQPEAKILI-CTHSNSAADLYIK 872
Cdd:pfam13401    8 LVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVdLPSGTSPKDLLRA 53
DEAD-like_helicase_N cd17912
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
828-867 5.60e-03

N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase superfamily is a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. The N-terminal domain contains the ATP-binding region.


Pssm-ID: 350670 [Multi-domain]  Cd Length: 81  Bit Score: 37.88  E-value: 5.60e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 45553113  828 ILLIGPFGTGKTYTLAQAIKQLLTQPEaKILICTHSNSAA 867
Cdd:cd17912    2 ILHLGPTGSGKTLVAIQKIASAMSSGK-SVLVVTPTKLLA 40
 
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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