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Conserved domains on  [gi|1676316918|ref|NP_001317376|]
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probable helicase with zinc finger domain isoform 2 [Homo sapiens]

Protein Classification

DEXXQc_HELZ and SF1_C_Upf1 domain-containing protein( domain architecture ID 13638697)

protein containing domains zf-CCCH, DEXXQc_HELZ, and SF1_C_Upf1

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 ...
641-868 8.27e-152

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: 466.19  E-value: 8.27e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  641 RLNAKQKEAVLAITTPLAIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETsRILICTHSNSAADLYIKDYLHPYVEAGN 720
Cdd:cd18077      1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPET-RILICTHSNSAADLYIKEYLHPYVETGN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  721 PQARPLRVYFRNRWVKTVHPVVHQYCLISsAHSTFQMPQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQA 800
Cdd:cd18077     80 PRARPLRVYYRNRWVKTVHPVVQKYCLID-EHGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQA 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1676316918  801 MECETIMPLALATQNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEFPCRILLCENYR 868
Cdd:cd18077    159 MECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSEHPCRILLCENYR 226
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
766-1075 9.05e-42

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


:

Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 167.23  E-value: 9.05e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  766 HRVVVVTLNTSQYLcqLDLEPGFFTHILLDEAAQAMECETIMPLALATqntRIVLAGDHMQLSPFV---YSEFARERNLH 842
Cdd:COG1112    535 APVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVfgeEAEEVAEEGLD 609
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  843 VSLLDRLYEHYPaefPCRILLCENYRSHEAIINYTSELFYEGKLMA---SGKQPAHKDFYPLTFFTARGedVQEKNSTAF 919
Cdd:COG1112    610 ESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDG--VYERRGGSR 684
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  920 YNnaevfevverveelrrkwP------VAW------GKLDDGSIGVVTPYADQVFRIRAELRKKRLSDV------NVERv 981
Cdd:COG1112    685 TN------------------PeeaeavVELvrelleDGPDGESIGVITPYRAQVALIRELLREALGDGLepvfvgTVDR- 745
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  982 lnVQGKQFRVLFLSTVRTRhtckhkqtpikkkeqlleDSTEDLDYGFLS-NYKLLNTAITRAQSLVAVVGDPiALCSIGR 1060
Cdd:COG1112    746 --FQGDERDVIIFSLVYSN------------------DEDVPRNFGFLNgGPRRLNVAVSRARRKLIVVGSR-ELLDSDP 804
                          330
                   ....*....|....*
gi 1676316918 1061 CRKFWERFIALCHEN 1075
Cdd:COG1112    805 STPALKRLLEYLERA 819
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
181-205 5.93e-06

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


:

Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 44.49  E-value: 5.93e-06
                           10        20
                   ....*....|....*....|....*
gi 1676316918  181 YTLCKRFLEQGICRYGAQCTSAHSQ 205
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 ...
641-868 8.27e-152

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: 466.19  E-value: 8.27e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  641 RLNAKQKEAVLAITTPLAIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETsRILICTHSNSAADLYIKDYLHPYVEAGN 720
Cdd:cd18077      1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPET-RILICTHSNSAADLYIKEYLHPYVETGN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  721 PQARPLRVYFRNRWVKTVHPVVHQYCLISsAHSTFQMPQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQA 800
Cdd:cd18077     80 PRARPLRVYYRNRWVKTVHPVVQKYCLID-EHGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQA 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1676316918  801 MECETIMPLALATQNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEFPCRILLCENYR 868
Cdd:cd18077    159 MECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSEHPCRILLCENYR 226
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
766-1075 9.05e-42

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 167.23  E-value: 9.05e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  766 HRVVVVTLNTSQYLcqLDLEPGFFTHILLDEAAQAMECETIMPLALATqntRIVLAGDHMQLSPFV---YSEFARERNLH 842
Cdd:COG1112    535 APVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVfgeEAEEVAEEGLD 609
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  843 VSLLDRLYEHYPaefPCRILLCENYRSHEAIINYTSELFYEGKLMA---SGKQPAHKDFYPLTFFTARGedVQEKNSTAF 919
Cdd:COG1112    610 ESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDG--VYERRGGSR 684
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  920 YNnaevfevverveelrrkwP------VAW------GKLDDGSIGVVTPYADQVFRIRAELRKKRLSDV------NVERv 981
Cdd:COG1112    685 TN------------------PeeaeavVELvrelleDGPDGESIGVITPYRAQVALIRELLREALGDGLepvfvgTVDR- 745
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  982 lnVQGKQFRVLFLSTVRTRhtckhkqtpikkkeqlleDSTEDLDYGFLS-NYKLLNTAITRAQSLVAVVGDPiALCSIGR 1060
Cdd:COG1112    746 --FQGDERDVIIFSLVYSN------------------DEDVPRNFGFLNgGPRRLNVAVSRARRKLIVVGSR-ELLDSDP 804
                          330
                   ....*....|....*
gi 1676316918 1061 CRKFWERFIALCHEN 1075
Cdd:COG1112    805 STPALKRLLEYLERA 819
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
869-1069 1.07e-35

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: 134.67  E-value: 1.07e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  869 SHEAIINYTSELFYEGKLMAS-------GKQPAHKDFYPLTFFTARGEDVQEKNSTAFYNNAEVFEVVERVEELRRKWpv 941
Cdd:cd18808      1 MHPEISEFPSKLFYEGKLKAGvsvaarlNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  942 awgkLDDGSIGVVTPYADQVFRIRAELRKKR--LSDVNVERVLNVQGKQFRVLFLSTVRTRHTCKHkqtpikkkeqlled 1019
Cdd:cd18808     79 ----VKPSSIGVITPYRAQVALIRELLRKRGglLEDVEVGTVDNFQGREKDVIILSLVRSNESGGS-------------- 140
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1676316918 1020 stedldYGFLSNYKLLNTAITRAQSLVAVVGDPIALCSIGRCRKFWERFI 1069
Cdd:cd18808    141 ------IGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
841-1052 3.87e-35

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: 133.44  E-value: 3.87e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  841 LHVSLLDRLYEHYPAefpCRILLCENYRSHEAIINYTSELFYEGKLMASGKQPAH---------KDFYPLTFF-TARGED 910
Cdd:pfam13087    1 LDRSLFERLQELGPS---AVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERplpddfhlpDPLGPLVFIdVDGSEE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  911 VQEKNSTAFYNNAEVFEVVERVEELRRKWPVAWGKlddgsIGVVTPYADQVFRIRAELRKKRLSDVNVErVLNV---QGK 987
Cdd:pfam13087   78 EESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSD-----IGVITPYRAQVRLIRKLLKRKLGGKLEIE-VNTVdgfQGR 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1676316918  988 QFRVLFLSTVRtrhtckhkqtpikkkeqlledSTEDLDYGFLSNYKLLNTAITRAQSLVAVVGDP 1052
Cdd:pfam13087  152 EKDVIIFSCVR---------------------SNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNA 195
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
646-834 1.48e-14

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: 75.46  E-value: 1.48e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  646 QKEAVLAittplAIQLPPV-LIIGPYGTGKTFTLAQAVKHILQQQETS-----RILICTHSNSAAD----LYIKDYLHPY 715
Cdd:pfam13086    2 QREAIRS-----ALSSSHFtLIQGPPGTGKTTTIVELIRQLLSYPATSaaagpRILVCAPSNAAVDnileRLLRKGQKYG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  716 VEA---GNPQARplrvyfrnrwvktvHPVVHQYCLISSAHSTFQMPQKEDILK--------------------------- 765
Cdd:pfam13086   77 PKIvriGHPAAI--------------SEAVLPVSLDYLVESKLNNEEDAQIVKdiskeleklakalrafekeiivekllk 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  766 -----------------------------------------HRVVVVTLNTS--QYLCQLDlepGFFThILLDEAAQAME 802
Cdd:pfam13086  143 srnkdkskleqerrklrserkelrkelrrreqslereildeAQIVCSTLSGAgsRLLSSLA---NFDV-VIIDEAAQALE 218
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1676316918  803 CETIMPLALATqnTRIVLAGDHMQLSPFVYSE 834
Cdd:pfam13086  219 PSTLIPLLRGP--KKVVLVGDPKQLPPTVISK 248
UvrD COG0210
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
641-704 1.98e-06

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


Pssm-ID: 439980 [Multi-domain]  Cd Length: 721  Bit Score: 53.02  E-value: 1.98e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1676316918  641 RLNAKQKEAVLAITTPLaiqlppvLII-GPyGTGKTFTLAQAVKHILQQQETS--RILICTHSNSAA 704
Cdd:COG0210      6 GLNPEQRAAVEHPEGPL-------LVLaGA-GSGKTRVLTHRIAYLIAEGGVDpeQILAVTFTNKAA 64
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
181-205 5.93e-06

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


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 44.49  E-value: 5.93e-06
                           10        20
                   ....*....|....*....|....*
gi 1676316918  181 YTLCKRFLEQGICRYGAQCTSAHSQ 205
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 ...
641-868 8.27e-152

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: 466.19  E-value: 8.27e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  641 RLNAKQKEAVLAITTPLAIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETsRILICTHSNSAADLYIKDYLHPYVEAGN 720
Cdd:cd18077      1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPET-RILICTHSNSAADLYIKEYLHPYVETGN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  721 PQARPLRVYFRNRWVKTVHPVVHQYCLISsAHSTFQMPQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQA 800
Cdd:cd18077     80 PRARPLRVYYRNRWVKTVHPVVQKYCLID-EHGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQA 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1676316918  801 MECETIMPLALATQNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEFPCRILLCENYR 868
Cdd:cd18077    159 MECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSEHPCRILLCENYR 226
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
641-868 7.11e-95

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: 306.08  E-value: 7.11e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  641 RLNAKQKEAVLAITTPlAIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETSRILICTHSNSAADLYIKDYLHPYVeagn 720
Cdd:cd18038      1 ELNDEQKLAVRNIVTG-TSRPPPYIIFGPPGTGKTVTLVEAILQVLRQPPEARILVCAPSNSAADLLAERLLNALV---- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  721 PQARPLRVYFRNRWVKTVHPVVHQYClISSAHSTFQMPQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQA 800
Cdd:cd18038     76 TKREILRLNAPSRDRASVPPELLPYC-NSKAEGTFRLPSLEELKKYRIVVCTLMTAGRLVQAGVPNGHFTHIFIDEAGQA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1676316918  801 MECETIMPLA-LATQNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYP------AEFPCRILLCENYR 868
Cdd:cd18038    155 TEPEALIPLSeLASKNTQIVLAGDPKQLGPVVRSPLARKYGLGKSLLERLMERPLyykdgeYNPSYITKLLKNYR 229
DEXXQc_HELZ2-N cd18076
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
641-868 9.71e-68

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: 228.24  E-value: 9.71e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  641 RLNAKQKEAVLAIT--TPLAIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETsRILICTHSNSAADLYIKDYLHPYVEA 718
Cdd:cd18076      1 AGNNKQQLAFNFIAgkPSEARFVPPLLIYGPFGTGKTFTLAMAALEVIREPGT-KVLICTHTNSAADIYIREYFHPYVDK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  719 GNPQARPLRVYFRNRWVKTVHPVVHQYCLISSAHSTFQMPQKEDILKHRVVVVTLNTSQylcQLDLEPGFFTHILLDEAA 798
Cdd:cd18076     80 GHPEARPLRIKATDRPNAITDPDTITYCCLTKDRQCFRLPTRDELDFHNIVITTTAMAF---NLHVLSGFFTHIFIDEAA 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1676316918  799 QAMECETIMPLALATQNTRIVLAGDHMQLSPFVYSeFARERNLHVSLLDRLYEHYPAE-----FPCRILLCENYR 868
Cdd:cd18076    157 QMLECEALIPLSYAGPKTRVVLAGDHMQMTPKLFS-VADYNRANHTLLNRLFHYYQGEkhevaVKSRVIFSENYR 230
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
766-1075 9.05e-42

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 167.23  E-value: 9.05e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  766 HRVVVVTLNTSQYLcqLDLEPGFFTHILLDEAAQAMECETIMPLALATqntRIVLAGDHMQLSPFV---YSEFARERNLH 842
Cdd:COG1112    535 APVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVfgeEAEEVAEEGLD 609
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  843 VSLLDRLYEHYPaefPCRILLCENYRSHEAIINYTSELFYEGKLMA---SGKQPAHKDFYPLTFFTARGedVQEKNSTAF 919
Cdd:COG1112    610 ESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDG--VYERRGGSR 684
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  920 YNnaevfevverveelrrkwP------VAW------GKLDDGSIGVVTPYADQVFRIRAELRKKRLSDV------NVERv 981
Cdd:COG1112    685 TN------------------PeeaeavVELvrelleDGPDGESIGVITPYRAQVALIRELLREALGDGLepvfvgTVDR- 745
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  982 lnVQGKQFRVLFLSTVRTRhtckhkqtpikkkeqlleDSTEDLDYGFLS-NYKLLNTAITRAQSLVAVVGDPiALCSIGR 1060
Cdd:COG1112    746 --FQGDERDVIIFSLVYSN------------------DEDVPRNFGFLNgGPRRLNVAVSRARRKLIVVGSR-ELLDSDP 804
                          330
                   ....*....|....*
gi 1676316918 1061 CRKFWERFIALCHEN 1075
Cdd:COG1112    805 STPALKRLLEYLERA 819
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
642-868 3.63e-40

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: 149.06  E-value: 3.63e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  642 LNAKQKEAVLAITTPLAIQLPPVlIIGPYGTGKTFTLAQAVKHILQQQETSRILICTHSNSAADLYIKDyLHPYVEAGNP 721
Cdd:cd18078      2 LNELQKEAVKRILGGECRPLPYI-LFGPPGTGKTVTIIEAILQVVYNLPRSRILVCAPSNSAADLVTSR-LHESKVLKPG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  722 QARPLRVYfrNRWVKTVHPVVHQYCLISSahstfqmpQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQAM 801
Cdd:cd18078     80 DMVRLNAV--NRFESTVIDARKLYCRLGE--------DLSKASRHRIVISTCSTAGLLYQMGLPVGHFTHVFVDEAGQAT 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  802 ECETIMPLALATQNT-RIVLAGDHMQLSPFVYSEFARERNLHVSLLDRL-----YEHYPAEFP-CRIL-------LCENY 867
Cdd:cd18078    150 EPESLIPLGLISSRDgQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLmnrplYLRDPNRFGeSGGYnpllvtkLVDNY 229

                   .
gi 1676316918  868 R 868
Cdd:cd18078    230 R 230
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
869-1069 1.07e-35

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: 134.67  E-value: 1.07e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  869 SHEAIINYTSELFYEGKLMAS-------GKQPAHKDFYPLTFFTARGEDVQEKNSTAFYNNAEVFEVVERVEELRRKWpv 941
Cdd:cd18808      1 MHPEISEFPSKLFYEGKLKAGvsvaarlNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  942 awgkLDDGSIGVVTPYADQVFRIRAELRKKR--LSDVNVERVLNVQGKQFRVLFLSTVRTRHTCKHkqtpikkkeqlled 1019
Cdd:cd18808     79 ----VKPSSIGVITPYRAQVALIRELLRKRGglLEDVEVGTVDNFQGREKDVIILSLVRSNESGGS-------------- 140
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1676316918 1020 stedldYGFLSNYKLLNTAITRAQSLVAVVGDPIALCSIGRCRKFWERFI 1069
Cdd:cd18808    141 ------IGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
841-1052 3.87e-35

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: 133.44  E-value: 3.87e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  841 LHVSLLDRLYEHYPAefpCRILLCENYRSHEAIINYTSELFYEGKLMASGKQPAH---------KDFYPLTFF-TARGED 910
Cdd:pfam13087    1 LDRSLFERLQELGPS---AVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERplpddfhlpDPLGPLVFIdVDGSEE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  911 VQEKNSTAFYNNAEVFEVVERVEELRRKWPVAWGKlddgsIGVVTPYADQVFRIRAELRKKRLSDVNVErVLNV---QGK 987
Cdd:pfam13087   78 EESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSD-----IGVITPYRAQVRLIRKLLKRKLGGKLEIE-VNTVdgfQGR 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1676316918  988 QFRVLFLSTVRtrhtckhkqtpikkkeqlledSTEDLDYGFLSNYKLLNTAITRAQSLVAVVGDP 1052
Cdd:pfam13087  152 EKDVIIFSCVR---------------------SNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNA 195
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
641-854 2.41e-25

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: 105.40  E-value: 2.41e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  641 RLNAKQKEAVLAITTPLAIqlppVLIIGPYGTGKTFTLAQAVKhILQQQETSrILICTHSNSAAD---LYIKDYLHPYVE 717
Cdd:cd18041      1 GLNKDQRQAIKKVLNAKDY----ALILGMPGTGKTTTIAALVR-ILVALGKS-VLLTSYTHSAVDnilLKLKKFGVNFLR 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  718 AGNPqarplrvyfrnrwvKTVHPVVHQYCLISSAHSTFQMPQKEDIL-KHRVVVVTL--NTSQYLCQldlepGFFTHILL 794
Cdd:cd18041     75 LGRL--------------KKIHPDVQEFTLEAILKSCKSVEELESKYeSVSVVATTClgINHPIFRR-----RTFDYCIV 135
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  795 DEAAQAMECETIMPLALATqntRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYP 854
Cdd:cd18041    136 DEASQITLPICLGPLRLAK---KFVLVGDHYQLPPLVKSREARELGMDESLFKRLSEAHP 192
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
641-868 3.84e-25

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: 104.61  E-value: 3.84e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  641 RLNAKQKEAVLaittpLAIQLPPVLII-GPYGTGKTFTLAQAVKHILQQQEtsRILICTHSNSAADLYIKDYLH---PYV 716
Cdd:cd18044      1 NLNDSQKEAVK-----FALSQKDVALIhGPPGTGKTTTVVEIILQAVKRGE--KVLACAPSNIAVDNLVERLVAlkvKVV 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  717 EAGNPqARplrvyfrnrwvktVHPVVHQYCLissahstfqmpqkEDILKHRVVVVTLNTSqylCQLDLEPG-FFTHILLD 795
Cdd:cd18044     74 RIGHP-AR-------------LLESVLDHSL-------------DALVAAQVVLATNTGA---GSRQLLPNeLFDVVVID 123
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1676316918  796 EAAQAMECETIMPLALATqntRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEfpCRILLCENYR 868
Cdd:cd18044    124 EAAQALEASCWIPLLKAR---RCILAGDHKQLPPTILSDKAARGGLGVTLFERLVNLYGES--VVRMLTVQYR 191
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
642-849 1.57e-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: 89.61  E-value: 1.57e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  642 LNAKQKEAVLAittplAIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQEtSRILICTHSNSAADlYIKDYLHpyvEAGnp 721
Cdd:cd18039      2 LNHSQVDAVKT-----ALQRPLSLIQGPPGTGKTVTSATIVYHLVKQGN-GPVLVCAPSNVAVD-QLTEKIH---QTG-- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  722 qARPLRVYFRNRW-----VK--TVHPVVHQY-----------------CLISSAHSTFQM----PQKEDILKHRVVVVTL 773
Cdd:cd18039     70 -LKVVRLCAKSREavespVSflALHNQVRNLdsaeklellkllkletgELSSADEKRYRKlkrkAERELLRNADVICCTC 148
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1676316918  774 NTSqylcqLD--LEPGFFTHILLDEAAQAMECETIMPLALATQntRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRL 849
Cdd:cd18039    149 VGA-----GDprLSKMKFRTVLIDEATQATEPECLIPLVHGAK--QVILVGDHCQLGPVVMCKKAAKAGLSQSLFERL 219
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
642-868 4.73e-19

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: 87.65  E-value: 4.73e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  642 LNAKQKEAVLAIttpLAIQLPPVLIIGPYGTGKTFTL---------------AQAVKHILQQQETS--------RILICT 698
Cdd:cd18042      1 LNESQLEAIASA---LQNSPGITLIQGPPGTGKTKTIvgilsvllagkyrkyYEKVKKKLRKLQRNlnnkkkknRILVCA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  699 HSNSAADLYIKDYLHPYVEAGNPQARPLRVyfrnrwVKTVHpvvhqyclissahstfQMPQKEDILKHRVVVVTLNTSQY 778
Cdd:cd18042     78 PSNAAVDEIVLRLLSEGFLDGDGRSYKPNV------VRVGR----------------QELRASILNEADIVCTTLSSSGS 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  779 LcQLDLEPGFFTHILLDEAAQAMECETIMPLALATQntRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEhypAEFP 858
Cdd:cd18042    136 D-LLESLPRGFDTVIIDEAAQAVELSTLIPLRLGCK--RLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQL---AGYP 209
                          250
                   ....*....|
gi 1676316918  859 CrILLCENYR 868
Cdd:cd18042    210 V-LMLTTQYR 218
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
641-849 4.27e-16

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: 77.97  E-value: 4.27e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  641 RLNAKQKEA-VLAITTPLAIqlppvlIIGPYGTGKTFTLAQAVKHILQ---QQETSRILICTHSNSAADLYIKDYLhpyv 716
Cdd:cd17936      1 TLDPSQLEAlKHALTSELAL------IQGPPGTGKTFLGVKLVRALLQnqdLSITGPILVVCYTNHALDQFLEGLL---- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  717 EAGNPQArpLRVYFRnrwvktvhpVVHqyCLISSAHSTFQMPQKediLKHRVVVVtlntsqylcqldlepgffthillDE 796
Cdd:cd17936     71 DFGPTKI--VRLGAR---------VIG--MTTTGAAKYRELLQA---LGPKVVIV-----------------------EE 111
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1676316918  797 AAQAMECETIMPLalaTQNTR-IVLAGDHMQLSPFV--YSEFARERNLHVSLLDRL 849
Cdd:cd17936    112 AAEVLEAHILAAL---TPSTEhLILIGDHKQLRPKVnvYELTAKKYNLDVSLFERL 164
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
664-868 1.78e-15

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: 74.58  E-value: 1.78e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  664 VLIIGPYGTGKTFTLAQAVKHILQQQETSRILICTHSNSAADlyikdylhpyveagnpqarplrvyfrnrwvktvhpvvh 743
Cdd:cd17934      2 SLIQGPPGTGKTTTIAAIVLQLLKGLRGKRVLVTAQSNVAVD-------------------------------------- 43
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  744 qyclissahstfqmpqkedilkhrvvvvtlntsqylcQLDlepgfftHILLDEAAQAMECETIMPLALAtqnTRIVLAGD 823
Cdd:cd17934     44 -------------------------------------NVD-------VVIIDEASQITEPELLIALIRA---KKVVLVGD 76
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1676316918  824 HMQLSPFVYSEFARE--RNLHVSLLDRLYEHYPAEFPcrILLCENYR 868
Cdd:cd17934     77 PKQLPPVVQEDHAALlgLSFILSLLLLFRLLLPGSPK--VMLDTQYR 121
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
646-834 1.48e-14

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: 75.46  E-value: 1.48e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  646 QKEAVLAittplAIQLPPV-LIIGPYGTGKTFTLAQAVKHILQQQETS-----RILICTHSNSAAD----LYIKDYLHPY 715
Cdd:pfam13086    2 QREAIRS-----ALSSSHFtLIQGPPGTGKTTTIVELIRQLLSYPATSaaagpRILVCAPSNAAVDnileRLLRKGQKYG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  716 VEA---GNPQARplrvyfrnrwvktvHPVVHQYCLISSAHSTFQMPQKEDILK--------------------------- 765
Cdd:pfam13086   77 PKIvriGHPAAI--------------SEAVLPVSLDYLVESKLNNEEDAQIVKdiskeleklakalrafekeiivekllk 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  766 -----------------------------------------HRVVVVTLNTS--QYLCQLDlepGFFThILLDEAAQAME 802
Cdd:pfam13086  143 srnkdkskleqerrklrserkelrkelrrreqslereildeAQIVCSTLSGAgsRLLSSLA---NFDV-VIIDEAAQALE 218
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1676316918  803 CETIMPLALATqnTRIVLAGDHMQLSPFVYSE 834
Cdd:pfam13086  219 PSTLIPLLRGP--KKVVLVGDPKQLPPTVISK 248
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
642-851 1.92e-12

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: 69.86  E-value: 1.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  642 LNAKQKEAVL-AITTPLaiqlppVLIIGPYGTGKTFTLAQAVKHILQQQETSR-----------ILICTHSNSAADLyIK 709
Cdd:cd18040      2 LNPSQNHAVRtALTKPF------TLIQGPPGTGKTVTGVHIAYWFAKQNREIQsvsgegdggpcVLYCGPSNKSVDV-VA 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  710 DYLhpyveAGNPQARPLRVY--------------FRNRWVK--------------TVHPVVHQ----YC-LISSAHSTFQ 756
Cdd:cd18040     75 ELL-----LKVPGLKILRVYseqietteypipnePRHPNKKsereskpnselssiTLHHRIRQpsnpHSqQIKAFEARFE 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  757 MPQ----KEDILKHRVVV------------VTLNTsqylCQLDLEPGFFTH-----ILLDEAAQAMECETIMPLALATQN 815
Cdd:cd18040    150 RTQekitEEDIKTYKILIwearfeeletvdVILCT----CSEAASQKMRTHanvkqCIVDECGMCTEPESLIPIVSAPRA 225
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1676316918  816 TRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYE 851
Cdd:cd18040    226 EQVVLIGDHKQLRPVVQNKEAQKLGLGRSLFERYAE 261
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
641-849 4.24e-11

EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds precursor-mRNA introns at a defined position and is part of a pentameric intron-binding complex (IBC). It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350693 [Multi-domain]  Cd Length: 207  Bit Score: 64.37  E-value: 4.24e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  641 RLNAKQKEAVLAittplAIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETSRILICTHSNSAA-DLYIKdylhpyVEAg 719
Cdd:cd17935      5 KFTPTQIEAIRS-----GMQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPNQRTLIVTHSNQALnQLFEK------IMA- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  720 npqarpLRVYFRNrwvktvhpvvhqycLISSAHSTfqmpqkedilkhRVVVVTLnTSQYLCQLDL-EPGF-FTHILLDEA 797
Cdd:cd17935     73 ------LDIDERH--------------LLRLGHGA------------KIIAMTC-THAALKRGELvELGFkYDNILMEEA 119
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1676316918  798 AQAMECETIMPLALATQNT------RIVLAGDHMQLSPFVYS-EFARERNLHVSLLDRL 849
Cdd:cd17935    120 AQILEIETFIPLLLQNPEDgpnrlkRLIMIGDHHQLPPVIKNmAFQKYSNMEQSLFTRL 178
DEXQc_UvrD cd17932
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch ...
643-867 1.42e-08

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: 56.37  E-value: 1.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  643 NAKQKEAVLAITTPLaiqlppvLII-GPyGTGKTFTLAQAVKHILQQQET--SRILICTHSNSAADlYIKDYLHPYVeaG 719
Cdd:cd17932      1 NPEQREAVTHPDGPL-------LVLaGA-GSGKTRVLTHRIAYLILEGGVppERILAVTFTNKAAK-EMRERLRKLL--G 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  720 NPQARPLrvyfrnrWVKTVHPVvhqyCL-ISSAHSTFqmpqkEDILkHRVVVVtLNTSQYLCQLDLEPgfFTHILLDEA- 797
Cdd:cd17932     70 EQLASGV-------WIGTFHSF----ALrILRRYGDF-----DDLL-LYALEL-LEENPDVREKLQSR--FRYILVDEYq 129
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1676316918  798 ----AQamecETIMpLALATQNTRIVLAGDHMQlSpfVYSeFareRNLHVSLLDRLYEHYPAefPCRILLCENY 867
Cdd:cd17932    130 dtnpLQ----YELL-KLLAGDGKNLFVVGDDDQ-S--IYG-F---RGADPENILDFEKDFPD--AKVIKLEENY 189
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
643-832 1.17e-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: 52.20  E-value: 1.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  643 NAKQKEAVLAittplAIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQEtsRILICTHSNSAADlyikdylhpyveagnpq 722
Cdd:cd18043      1 DSSQEAAIIS-----ARNGKNVVIQGPPGTGKSQTIANIIANALARGK--RVLFVSEKKAALD----------------- 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  723 arplrvyfrnrwvktvhpVVHQYCLISSAHSTFQMpqkedilkhrvvvvtlntsqylcqLDLEPGFFTHILLDEAAQAME 802
Cdd:cd18043     57 ------------------VVRFPCWIMSPLSVSQY------------------------LPLNRNLFDLVIFDEASQIPI 94
                          170       180       190
                   ....*....|....*....|....*....|
gi 1676316918  803 CETIMPLALATQntrIVLAGDHMQLSPFVY 832
Cdd:cd18043     95 EEALPALFRGKQ---VVVVGDDKQLPPSIL 121
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
663-705 3.02e-07

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: 50.95  E-value: 3.02e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1676316918  663 PVLIIGPYGTGKTFTLAQAVKHILQQQETS--RILICTHSNSAAD 705
Cdd:cd17914      1 LSLIQGPPGTGKTRVLVKIVAALMQNKNGEpgRILLVTPTNKAAA 45
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
645-829 1.93e-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: 49.48  E-value: 1.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  645 KQKEAVLAITtplaiQLPPVLIIGPYGTGKTFTLAQAVKHIlqQQETSRILICTHSNSAADLyikdyLHpyvEAGNPQAR 724
Cdd:cd17933      1 EQKAAVRLVL-----RNRVSVLTGGAGTGKTTTLKALLAAL--EAEGKRVVLAAPTGKAAKR-----LS---ESTGIEAS 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  725 plrvyfrnrwvkTVHPVvhqycLISSAHSTFQMPQKEDILKHRVVVVtlntsqylcqldlepgffthillDEAaqAMece 804
Cdd:cd17933     66 ------------TIHRL-----LGINPGGGGFYYNEENPLDADLLIV-----------------------DEA--SM--- 100
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1676316918  805 tiMPLALATQ-------NTRIVLAGDHMQLSP 829
Cdd:cd17933    101 --VDTRLMAAllsaipaGARLILVGDPDQLPS 130
UvrD COG0210
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
641-704 1.98e-06

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


Pssm-ID: 439980 [Multi-domain]  Cd Length: 721  Bit Score: 53.02  E-value: 1.98e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1676316918  641 RLNAKQKEAVLAITTPLaiqlppvLII-GPyGTGKTFTLAQAVKHILQQQETS--RILICTHSNSAA 704
Cdd:COG0210      6 GLNPEQRAAVEHPEGPL-------LVLaGA-GSGKTRVLTHRIAYLIAEGGVDpeQILAVTFTNKAA 64
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
181-205 5.93e-06

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


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 44.49  E-value: 5.93e-06
                           10        20
                   ....*....|....*....|....*
gi 1676316918  181 YTLCKRFLEQGICRYGAQCTSAHSQ 205
Cdd:pfam00642    3 TELCRFFLRTGYCKYGDRCKFAHGQ 27
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
632-1073 7.47e-06

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: 50.75  E-value: 7.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  632 RQWDEQLDPRLNAKQKEAVLAITTPLAIqlppVLIIGPYGTGKTFTLAQAVKHILQQQEtsRILICTHSNSAAD-LYikd 710
Cdd:COG0507    115 AALEPRAGITLSDEQREAVALALTTRRV----SVLTGGAGTGKTTTLRALLAALEALGL--RVALAAPTGKAAKrLS--- 185
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  711 ylhpyvEAGNPQARplrvyfrnrwvkTVHPVVHqyclISSAHSTFQMPQKEDILKHRVVVVtlntsqylcqldlepgfft 790
Cdd:COG0507    186 ------ESTGIEAR------------TIHRLLG----LRPDSGRFRHNRDNPLTPADLLVV------------------- 224
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  791 hillDEA--------AQAMEcetimplALATQNTRIVLAGDHMQLSP----FVYSEFARERNLHVSLLDrlyehypaefp 858
Cdd:COG0507    225 ----DEAsmvdtrlmAALLE-------ALPRAGARLILVGDPDQLPSvgagAVLRDLIESGTVPVVELT----------- 282
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  859 crillcENYRSHEAI-INYTSELFYEGKlMASGKQPAHKDFYPL----------------TFFTARGEDVQ-----EKnS 916
Cdd:COG0507    283 ------EVYRQADDSrIIELAHAIREGD-APEALNARYADVVFVeaedaeeaaeaivelyADRPAGGEDIQvlaptNA-G 354
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  917 TAFYN-------NAEVFEVVERVEELRRKW----PV-------AWGkLDDGSIGVVTPYADQVFRIRAELRKKRLSDVNV 978
Cdd:COG0507    355 VDALNqairealNPAGELERELAEDGELELyvgdRVmftrndyDLG-VFNGDIGTVLSIDEDEGRLTVRFDGREIVTYDP 433
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  979 ERVLNV-----------QGKQF-RVLFLSTvrtrhtckhkqtpikkkeqlledsteDLDYGFLSNyKLLNTAITRAQSLV 1046
Cdd:COG0507    434 SELDQLelayaitvhksQGSTFdRVILVLP--------------------------SEHSPLLSR-ELLYTALTRARELL 486
                          490       500
                   ....*....|....*....|....*..
gi 1676316918 1047 AVVGDPIALCSIgrCRKFWERFIALCH 1073
Cdd:COG0507    487 TLVGDRDALARA--VRRDTARATGLAE 511
UvrD-helicase pfam00580
UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural ...
642-739 1.04e-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: 49.17  E-value: 1.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  642 LNAKQKEAVLAITTPLaiqlppvLIIGPYGTGKTFTLAQAVKHILQQQETS--RILICTHSNSAAD---LYIKDYLhpyv 716
Cdd:pfam00580    1 LNPEQRKAVTHLGGPL-------LVLAGAGSGKTRVLTERIAYLILEGGIDpeEILAVTFTNKAARemkERILKLL---- 69
                           90       100
                   ....*....|....*....|...
gi 1676316918  717 eaGNPQARPLrvyfrnrWVKTVH 739
Cdd:pfam00580   70 --GKAELSEL-------NISTFH 83
ResIII pfam04851
Type III restriction enzyme, res subunit;
642-797 4.81e-05

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 45.74  E-value: 4.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  642 LNAKQKEAVLAITTPLAIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETSRILICTHSNsaaDLY------IKDYLHPY 715
Cdd:pfam04851    4 LRPYQIEAIENLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRK---DLLeqaleeFKKFLPNY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  716 VEAGNpqarPLRVYFRNRWVKTVHPVVhqyclissahSTFQmpqkedilkhrvvvvTLNTSQYLCQLDLEPGFFTHILLD 795
Cdd:pfam04851   81 VEIGE----IISGDKKDESVDDNKIVV----------TTIQ---------------SLYKALELASLELLPDFFDVIIID 131

                   ..
gi 1676316918  796 EA 797
Cdd:pfam04851  132 EA 133
AAA_19 pfam13245
AAA domain;
646-705 7.18e-05

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 44.52  E-value: 7.18e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1676316918  646 QKEAVLAittplAIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETS-RILICTHSNSAAD 705
Cdd:pfam13245    1 QREAVRT-----ALPSKVVLLTGGPGTGKTTTIRHIVALLVALGGVSfPILLAAPTGRAAK 56
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
641-829 1.18e-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: 44.86  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  641 RLNAKQKEAVLAITT-PLAIQLppvlIIGPYGTGKTFTLAQAVKHIlqQQETSRILICTHSNSAADLYIKDYLHPyveag 719
Cdd:pfam13604    1 TLNAEQAAAVRALLTsGDRVAV----LVGPAGTGKTTALKALREAW--EAAGYRVIGLAPTGRAAKVLGEELGIP----- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  720 npqARplrvyfrnrwvkTVHPVVHQYclissahstfqmPQKEDILKHRVVVVtlntsqylcqldlepgffthillDEAAQ 799
Cdd:pfam13604   70 ---AD------------TIAKLLHRL------------GGRAGLDPGTLLIV-----------------------DEAGM 99
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1676316918  800 A----MEcetiMPLALATQ-NTRIVLAGDHMQLSP 829
Cdd:pfam13604  100 VgtrqMA----RLLKLAEDaGARVILVGDPRQLPS 130
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
637-730 1.20e-03

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 43.86  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676316918  637 QLDPRLNAKQKEAVLAITTPLAIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQetsRILICTHS----NSAADLyIKDYL 712
Cdd:COG1061     76 GTSFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGK---RVLVLVPRrellEQWAEE-LRRFL 151
                           90
                   ....*....|....*...
gi 1676316918  713 HPYVEAGNPQARPLRVYF 730
Cdd:COG1061    152 GDPLAGGGKKDSDAPITV 169
AAA_22 pfam13401
AAA domain;
664-709 4.81e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 39.25  E-value: 4.81e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1676316918  664 VLIIGPYGTGKTfTLAQAVKHILQQQETSRILI-CTHSNSAADLYIK 709
Cdd:pfam13401    8 LVLTGESGTGKT-TLLRRLLEQLPEVRDSVVFVdLPSGTSPKDLLRA 53
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
646-702 7.78e-03

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: 39.08  E-value: 7.78e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1676316918  646 QKEAVLAITTPLAIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETSRILICTHSNS 702
Cdd:cd18032      5 QQEAIEALEEAREKGQRRALLVMATGTGKTYTAAFLIKRLLEANRKKRILFLAHREE 61
 
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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