NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|530413304|ref|XP_005257945|]
View 

probable helicase with zinc finger domain isoform X2 [Homo sapiens]

Protein Classification

zinc finger CCCH domain-containing protein; DEAD/DEAH box helicase family protein( domain architecture ID 13638697)

zinc finger CCCH domain-containing protein similar to Homo sapiens proline-rich protein 3 (PRR3); DEAD/DEAH box containing ATP-dependent helicase family protein may catalyze the unwinding of DNA or RNA

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 668-894 1.92e-153

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: 471.20  E-value: 1.92e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  668 RLNAKQKEAVLAITTPLAIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETRILICTHSNSAADLYIKDYLHPYVEAGNP 747
Cdd:cd18077     1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPETRILICTHSNSAADLYIKEYLHPYVETGNP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  748 QARPLRVYFRNRWVKTVHPVVHQYCLISsAHSTFQMPQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQAM 827
Cdd:cd18077    81 RARPLRVYYRNRWVKTVHPVVQKYCLID-EHGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQAM 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530413304  828 ECETIMPLALATQNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEFPCRILLCENYR 894
Cdd:cd18077   160 ECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSEHPCRILLCENYR 226
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
792-1101 9.23e-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: 9.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  792 HRVVVVTLNTSQYLcqLDLEPGFFTHILLDEAAQAMECETIMPLALATqntRIVLAGDHMQLSPFV---YSEFARERNLH 868
Cdd:COG1112   535 APVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVfgeEAEEVAEEGLD 609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  869 VSLLDRLYEHYPaefPCRILLCENYRSHEAIINYTSELFYEGKLMA---SGKQPAHKDFYPLTFFTARGedVQEKNSTAF 945
Cdd:COG1112   610 ESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDG--VYERRGGSR 684

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  946 YNnaevfevverveelrrkwP------VAW------GKLDDGSIGVVTPYADQVFRIRAELRKKRLSDV------NVERv 1007
Cdd:COG1112   685 TN------------------PeeaeavVELvrelleDGPDGESIGVITPYRAQVALIRELLREALGDGLepvfvgTVDR- 745

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304 1008 lnVQGKQFRVLFLSTVRTRhtckhkqtpikkkeqlleDSTEDLDYGFLS-NYKLLNTAITRAQSLVAVVGDPiALCSIGR 1086
Cdd:COG1112   746 --FQGDERDVIIFSLVYSN------------------DEDVPRNFGFLNgGPRRLNVAVSRARRKLIVVGSR-ELLDSDP 804

                         330
                  ....*....|....*
gi 530413304 1087 CRKFWERFIALCHEN 1101
Cdd:COG1112   805 STPALKRLLEYLERA 819
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
181-205 6.50e-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: 6.50e-06
                           10        20
                   ....*....|....*....|....*
gi 530413304   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 ...
 668-894 1.92e-153

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: 471.20  E-value: 1.92e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  668 RLNAKQKEAVLAITTPLAIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETRILICTHSNSAADLYIKDYLHPYVEAGNP 747
Cdd:cd18077     1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPETRILICTHSNSAADLYIKEYLHPYVETGNP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  748 QARPLRVYFRNRWVKTVHPVVHQYCLISsAHSTFQMPQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQAM 827
Cdd:cd18077    81 RARPLRVYYRNRWVKTVHPVVQKYCLID-EHGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQAM 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530413304  828 ECETIMPLALATQNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEFPCRILLCENYR 894
Cdd:cd18077   160 ECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSEHPCRILLCENYR 226
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
792-1101 9.23e-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: 9.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  792 HRVVVVTLNTSQYLcqLDLEPGFFTHILLDEAAQAMECETIMPLALATqntRIVLAGDHMQLSPFV---YSEFARERNLH 868
Cdd:COG1112   535 APVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVfgeEAEEVAEEGLD 609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  869 VSLLDRLYEHYPaefPCRILLCENYRSHEAIINYTSELFYEGKLMA---SGKQPAHKDFYPLTFFTARGedVQEKNSTAF 945
Cdd:COG1112   610 ESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDG--VYERRGGSR 684

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  946 YNnaevfevverveelrrkwP------VAW------GKLDDGSIGVVTPYADQVFRIRAELRKKRLSDV------NVERv 1007
Cdd:COG1112   685 TN------------------PeeaeavVELvrelleDGPDGESIGVITPYRAQVALIRELLREALGDGLepvfvgTVDR- 745

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304 1008 lnVQGKQFRVLFLSTVRTRhtckhkqtpikkkeqlleDSTEDLDYGFLS-NYKLLNTAITRAQSLVAVVGDPiALCSIGR 1086
Cdd:COG1112   746 --FQGDERDVIIFSLVYSN------------------DEDVPRNFGFLNgGPRRLNVAVSRARRKLIVVGSR-ELLDSDP 804

                         330
                  ....*....|....*
gi 530413304 1087 CRKFWERFIALCHEN 1101
Cdd:COG1112   805 STPALKRLLEYLERA 819
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
 895-1095 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 530413304  895 SHEAIINYTSELFYEGKLMAS-------GKQPAHKDFYPLTFFTARGEDVQEKNSTAFYNNAEVFEVVERVEELRRKWpv 967
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGvsvaarlNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  968 awgkLDDGSIGVVTPYADQVFRIRAELRKKR--LSDVNVERVLNVQGKQFRVLFLSTVRTRHTCKHkqtpikkkeqlled 1045
Cdd:cd18808    79 ----VKPSSIGVITPYRAQVALIRELLRKRGglLEDVEVGTVDNFQGREKDVIILSLVRSNESGGS-------------- 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 530413304 1046 stedldYGFLSNYKLLNTAITRAQSLVAVVGDPIALCSIGRCRKFWERFI 1095
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 ...
 867-1078 3.96e-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: 3.96e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304   867 LHVSLLDRLYEHYPAefpCRILLCENYRSHEAIINYTSELFYEGKLMASGKQPAH---------KDFYPLTFF-TARGED 936
Cdd:pfam13087    1 LDRSLFERLQELGPS---AVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERplpddfhlpDPLGPLVFIdVDGSEE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304   937 VQEKNSTAFYNNAEVFEVVERVEELRRKWPVAWGKlddgsIGVVTPYADQVFRIRAELRKKRLSDVNVErVLNV---QGK 1013
Cdd:pfam13087   78 EESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSD-----IGVITPYRAQVRLIRKLLKRKLGGKLEIE-VNTVdgfQGR 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530413304  1014 QFRVLFLSTVRtrhtckhkqtpikkkeqlledSTEDLDYGFLSNYKLLNTAITRAQSLVAVVGDP 1078
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 ...
 673-860 3.03e-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: 74.69  E-value: 3.03e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304   673 QKEAVLAittplAIQLPPV-LIIGPYGTGKTFTLAQAVKHILQQQET------RILICTHSNSAAD----LYIKDYLHPY 741
Cdd:pfam13086    2 QREAIRS-----ALSSSHFtLIQGPPGTGKTTTIVELIRQLLSYPATsaaagpRILVCAPSNAAVDnileRLLRKGQKYG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304   742 VEA---GNPQARplrvyfrnrwvktvHPVVHQYCLISSAHSTFQMPQKEDILK--------------------------- 791
Cdd:pfam13086   77 PKIvriGHPAAI--------------SEAVLPVSLDYLVESKLNNEEDAQIVKdiskeleklakalrafekeiivekllk 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304   792 -----------------------------------------HRVVVVTLNTS--QYLCQLDlepGFFThILLDEAAQAME 828
Cdd:pfam13086  143 srnkdkskleqerrklrserkelrkelrrreqslereildeAQIVCSTLSGAgsRLLSSLA---NFDV-VIIDEAAQALE 218

                          250       260       270
                   ....*....|....*....|....*....|..
gi 530413304   829 CETIMPLALATqnTRIVLAGDHMQLSPFVYSE 860
Cdd:pfam13086  219 PSTLIPLLRGP--KKVVLVGDPKQLPPTVISK 248
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 659-1099 6.70e-07

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: 54.21  E-value: 6.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  659 RQWDEQLDPRLNAKQKEAVLAITTPLAIqlppVLIIGPYGTGKTFTLAqAVKHILQQQETRILICTHSNSAAD-LYikdy 737
Cdd:COG0507   115 AALEPRAGITLSDEQREAVALALTTRRV----SVLTGGAGTGKTTTLR-ALLAALEALGLRVALAAPTGKAAKrLS---- 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  738 lhpyvEAGNPQARplrvyfrnrwvkTVHPVVHqyclISSAHSTFQMPQKEDILKHRVVVVtlntsqylcqldlepgffth 817
Cdd:COG0507   186 -----ESTGIEAR------------TIHRLLG----LRPDSGRFRHNRDNPLTPADLLVV-------------------- 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  818 illDEA--------AQAMEcetimplALATQNTRIVLAGDHMQLSP----FVYSEFARERNLHVSLLDrlyehypaefpc 885
Cdd:COG0507   225 ---DEAsmvdtrlmAALLE-------ALPRAGARLILVGDPDQLPSvgagAVLRDLIESGTVPVVELT------------ 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  886 rillcENYRSHEAI-INYTSELFYEGKlMASGKQPAHKDFYPL----------------TFFTARGEDVQ-----EKnST 943
Cdd:COG0507   283 -----EVYRQADDSrIIELAHAIREGD-APEALNARYADVVFVeaedaeeaaeaivelyADRPAGGEDIQvlaptNA-GV 355

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  944 AFYN-------NAEVFEVVERVEELRRKW----PV-------AWGkLDDGSIGVVTPYADQVFRIRAELRKKRLSDVNVE 1005
Cdd:COG0507   356 DALNqairealNPAGELERELAEDGELELyvgdRVmftrndyDLG-VFNGDIGTVLSIDEDEGRLTVRFDGREIVTYDPS 434

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304 1006 RVLNV-----------QGKQF-RVLFLSTvrtrhtckhkqtpikkkeqlledsteDLDYGFLSNyKLLNTAITRAQSLVA 1073
Cdd:COG0507   435 ELDQLelayaitvhksQGSTFdRVILVLP--------------------------SEHSPLLSR-ELLYTALTRARELLT 487

                         490       500
                  ....*....|....*....|....*.
gi 530413304 1074 VVGDPIALCSIgrCRKFWERFIALCH 1099
Cdd:COG0507   488 LVGDRDALARA--VRRDTARATGLAE 511
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
181-205 6.50e-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: 6.50e-06
                           10        20
                   ....*....|....*....|....*
gi 530413304   181 YTLCKRFLEQGICRYGAQCTSAHSQ 205
Cdd:pfam00642    3 TELCRFFLRTGYCKYGDRCKFAHGQ 27
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 690-768 1.99e-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: 40.82  E-value: 1.99e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530413304    690 PVLIIGPYGTGKTfTLAQAVKHILQQQETRILICTHSNSAADLYIKDYLHPYVEAGNPQARPLRVYFRNRWVKTVHPVV 768
Cdd:smart00382    4 VILIVGPPGSGKT-TLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDV 81
 
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 ...
 668-894 1.92e-153

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: 471.20  E-value: 1.92e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  668 RLNAKQKEAVLAITTPLAIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETRILICTHSNSAADLYIKDYLHPYVEAGNP 747
Cdd:cd18077     1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPETRILICTHSNSAADLYIKEYLHPYVETGNP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  748 QARPLRVYFRNRWVKTVHPVVHQYCLISsAHSTFQMPQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQAM 827
Cdd:cd18077    81 RARPLRVYYRNRWVKTVHPVVQKYCLID-EHGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQAM 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530413304  828 ECETIMPLALATQNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEFPCRILLCENYR 894
Cdd:cd18077   160 ECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSEHPCRILLCENYR 226
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
 668-894 6.24e-94

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: 303.39  E-value: 6.24e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  668 RLNAKQKEAVLAITTPlAIQLPPVLIIGPYGTGKTFTLAQAVKHIL-QQQETRILICTHSNSAADLYIKDYLHPYVeagn 746
Cdd:cd18038     1 ELNDEQKLAVRNIVTG-TSRPPPYIIFGPPGTGKTVTLVEAILQVLrQPPEARILVCAPSNSAADLLAERLLNALV---- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  747 PQARPLRVYFRNRWVKTVHPVVHQYClISSAHSTFQMPQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQA 826
Cdd:cd18038    76 TKREILRLNAPSRDRASVPPELLPYC-NSKAEGTFRLPSLEELKKYRIVVCTLMTAGRLVQAGVPNGHFTHIFIDEAGQA 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530413304  827 MECETIMPLA-LATQNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYP------AEFPCRILLCENYR 894
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 ...
 668-894 2.39e-69

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: 233.24  E-value: 2.39e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  668 RLNAKQKEAVLAIT--TPLAIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETRILICTHSNSAADLYIKDYLHPYVEAG 745
Cdd:cd18076     1 AGNNKQQLAFNFIAgkPSEARFVPPLLIYGPFGTGKTFTLAMAALEVIREPGTKVLICTHTNSAADIYIREYFHPYVDKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  746 NPQARPLRVYFRNRWVKTVHPVVHQYCLISSAHSTFQMPQKEDILKHRVVVVTLNTSQylcQLDLEPGFFTHILLDEAAQ 825
Cdd:cd18076    81 HPEARPLRIKATDRPNAITDPDTITYCCLTKDRQCFRLPTRDELDFHNIVITTTAMAF---NLHVLSGFFTHIFIDEAAQ 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530413304  826 AMECETIMPLALATQNTRIVLAGDHMQLSPFVYSeFARERNLHVSLLDRLYEHYPAE-----FPCRILLCENYR 894
Cdd:cd18076   158 MLECEALIPLSYAGPKTRVVLAGDHMQMTPKLFS-VADYNRANHTLLNRLFHYYQGEkhevaVKSRVIFSENYR 230
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
792-1101 9.23e-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: 9.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  792 HRVVVVTLNTSQYLcqLDLEPGFFTHILLDEAAQAMECETIMPLALATqntRIVLAGDHMQLSPFV---YSEFARERNLH 868
Cdd:COG1112   535 APVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVfgeEAEEVAEEGLD 609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  869 VSLLDRLYEHYPaefPCRILLCENYRSHEAIINYTSELFYEGKLMA---SGKQPAHKDFYPLTFFTARGedVQEKNSTAF 945
Cdd:COG1112   610 ESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDG--VYERRGGSR 684

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  946 YNnaevfevverveelrrkwP------VAW------GKLDDGSIGVVTPYADQVFRIRAELRKKRLSDV------NVERv 1007
Cdd:COG1112   685 TN------------------PeeaeavVELvrelleDGPDGESIGVITPYRAQVALIRELLREALGDGLepvfvgTVDR- 745

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304 1008 lnVQGKQFRVLFLSTVRTRhtckhkqtpikkkeqlleDSTEDLDYGFLS-NYKLLNTAITRAQSLVAVVGDPiALCSIGR 1086
Cdd:COG1112   746 --FQGDERDVIIFSLVYSN------------------DEDVPRNFGFLNgGPRRLNVAVSRARRKLIVVGSR-ELLDSDP 804

                         330
                  ....*....|....*
gi 530413304 1087 CRKFWERFIALCHEN 1101
Cdd:COG1112   805 STPALKRLLEYLERA 819
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
 669-894 2.51e-39

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: 146.74  E-value: 2.51e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  669 LNAKQKEAVLAITTPLAIQLPPVlIIGPYGTGKTFTLAQAvkhILQQQ----ETRILICTHSNSAADLYIKDyLHPYVEA 744
Cdd:cd18078     2 LNELQKEAVKRILGGECRPLPYI-LFGPPGTGKTVTIIEA---ILQVVynlpRSRILVCAPSNSAADLVTSR-LHESKVL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  745 GNPQARPLRVYfrNRWVKTVHPVVHQYCLISSahstfqmpQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAA 824
Cdd:cd18078    77 KPGDMVRLNAV--NRFESTVIDARKLYCRLGE--------DLSKASRHRIVISTCSTAGLLYQMGLPVGHFTHVFVDEAG 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  825 QAMECETIMPLALATQNT-RIVLAGDHMQLSPFVYSEFARERNLHVSLLDRL-----YEHYPAEFP-CRIL-------LC 890
Cdd:cd18078   147 QATEPESLIPLGLISSRDgQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLmnrplYLRDPNRFGeSGGYnpllvtkLV 226


                  ....
gi 530413304  891 ENYR 894
Cdd:cd18078   227 DNYR 230
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
 895-1095 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 530413304  895 SHEAIINYTSELFYEGKLMAS-------GKQPAHKDFYPLTFFTARGEDVQEKNSTAFYNNAEVFEVVERVEELRRKWpv 967
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGvsvaarlNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  968 awgkLDDGSIGVVTPYADQVFRIRAELRKKR--LSDVNVERVLNVQGKQFRVLFLSTVRTRHTCKHkqtpikkkeqlled 1045
Cdd:cd18808    79 ----VKPSSIGVITPYRAQVALIRELLRKRGglLEDVEVGTVDNFQGREKDVIILSLVRSNESGGS-------------- 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 530413304 1046 stedldYGFLSNYKLLNTAITRAQSLVAVVGDPIALCSIGRCRKFWERFI 1095
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 ...
 867-1078 3.96e-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: 3.96e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304   867 LHVSLLDRLYEHYPAefpCRILLCENYRSHEAIINYTSELFYEGKLMASGKQPAH---------KDFYPLTFF-TARGED 936
Cdd:pfam13087    1 LDRSLFERLQELGPS---AVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERplpddfhlpDPLGPLVFIdVDGSEE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304   937 VQEKNSTAFYNNAEVFEVVERVEELRRKWPVAWGKlddgsIGVVTPYADQVFRIRAELRKKRLSDVNVErVLNV---QGK 1013
Cdd:pfam13087   78 EESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSD-----IGVITPYRAQVRLIRKLLKRKLGGKLEIE-VNTVdgfQGR 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530413304  1014 QFRVLFLSTVRtrhtckhkqtpikkkeqlledSTEDLDYGFLSNYKLLNTAITRAQSLVAVVGDP 1078
Cdd:pfam13087  152 EKDVIIFSCVR---------------------SNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNA 195
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
 668-880 2.00e-26

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: 108.86  E-value: 2.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  668 RLNAKQKEAVLAITTPLAIqlppVLIIGPYGTGKTFTLAQAVKhILQQQETRILICTHSNSAAD---LYIKDYLHPYVEA 744
Cdd:cd18041     1 GLNKDQRQAIKKVLNAKDY----ALILGMPGTGKTTTIAALVR-ILVALGKSVLLTSYTHSAVDnilLKLKKFGVNFLRL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  745 GNPqarplrvyfrnrwvKTVHPVVHQYCLISSAHSTFQMPQKEDIL-KHRVVVVTL--NTSQYLCQldlepGFFTHILLD 821
Cdd:cd18041    76 GRL--------------KKIHPDVQEFTLEAILKSCKSVEELESKYeSVSVVATTClgINHPIFRR-----RTFDYCIVD 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530413304  822 EAAQAMECETIMPLALATqntRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYP 880
Cdd:cd18041   137 EASQITLPICLGPLRLAK---KFVLVGDHYQLPPLVKSREARELGMDESLFKRLSEAHP 192
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
 668-894 2.04e-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: 105.38  E-value: 2.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  668 RLNAKQKEAVLaittpLAIQLPPVLII-GPYGTGKTFTLAQAvkhILQ--QQETRILICTHSNSAADLYIKDYLH---PY 741
Cdd:cd18044     1 NLNDSQKEAVK-----FALSQKDVALIhGPPGTGKTTTVVEI---ILQavKRGEKVLACAPSNIAVDNLVERLVAlkvKV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  742 VEAGNPqARplrvyfrnrwvktVHPVVHQYCLissahstfqmpqkEDILKHRVVVVTLNTSqylCQLDLEPG-FFTHILL 820
Cdd:cd18044    73 VRIGHP-AR-------------LLESVLDHSL-------------DALVAAQVVLATNTGA---GSRQLLPNeLFDVVVI 122

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530413304  821 DEAAQAMECETIMPLALATqntRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEfpCRILLCENYR 894
Cdd:cd18044   123 DEAAQALEASCWIPLLKAR---RCILAGDHKQLPPTILSDKAARGGLGVTLFERLVNLYGES--VVRMLTVQYR 191
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
 669-875 7.20e-21

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: 93.47  E-value: 7.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  669 LNAKQKEAVLAittplAIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETRILICTHSNSAADlYIKDYLHpyvEAGnpq 748
Cdd:cd18039     2 LNHSQVDAVKT-----ALQRPLSLIQGPPGTGKTVTSATIVYHLVKQGNGPVLVCAPSNVAVD-QLTEKIH---QTG--- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  749 ARPLRVYFRNRW-----VK--TVHPVVHQY-----------------CLISSAHSTFQM----PQKEDILKHRVVVVTLN 800
Cdd:cd18039    70 LKVVRLCAKSREavespVSflALHNQVRNLdsaeklellkllkletgELSSADEKRYRKlkrkAERELLRNADVICCTCV 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530413304  801 TSqylcqLD--LEPGFFTHILLDEAAQAMECETIMPLALATQntRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRL 875
Cdd:cd18039   150 GA-----GDprLSKMKFRTVLIDEATQATEPECLIPLVHGAK--QVILVGDHCQLGPVVMCKKAAKAGLSQSLFERL 219
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
 669-894 1.10e-18

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: 86.88  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  669 LNAKQKEAVLAIttpLAIQLPPVLIIGPYGTGKTFTL---------------AQAVKHILQQQET---------RILICT 724
Cdd:cd18042     1 LNESQLEAIASA---LQNSPGITLIQGPPGTGKTKTIvgilsvllagkyrkyYEKVKKKLRKLQRnlnnkkkknRILVCA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  725 HSNSAADLYIKDYLHPYVEAGNPQARPLRVyfrnrwVKTVHpvvhqyclissahstfQMPQKEDILKHRVVVVTLNTSQY 804
Cdd:cd18042    78 PSNAAVDEIVLRLLSEGFLDGDGRSYKPNV------VRVGR----------------QELRASILNEADIVCTTLSSSGS 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  805 LcQLDLEPGFFTHILLDEAAQAMECETIMPLALATQntRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEhypAEFP 884
Cdd:cd18042   136 D-LLESLPRGFDTVIIDEAAQAVELSTLIPLRLGCK--RLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQL---AGYP 209

                         250
                  ....*....|
gi 530413304  885 CrILLCENYR 894
Cdd:cd18042   210 V-LMLTTQYR 218
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
 668-875 4.64e-15

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: 75.27  E-value: 4.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  668 RLNAKQKEA-VLAITTPLAIqlppvlIIGPYGTGKTFTLAQAVKHILQ----QQETRILICTHSNSAADLYIKDYLhpyv 742
Cdd:cd17936     1 TLDPSQLEAlKHALTSELAL------IQGPPGTGKTFLGVKLVRALLQnqdlSITGPILVVCYTNHALDQFLEGLL---- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  743 EAGNPQArpLRVYFRnrwvktvhpVVHqyCLISSAHSTFQMPQKediLKHRVVVVtlntsqylcqldlepgffthillDE 822
Cdd:cd17936    71 DFGPTKI--VRLGAR---------VIG--MTTTGAAKYRELLQA---LGPKVVIV-----------------------EE 111

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530413304  823 AAQAMECETIMPLalaTQNTR-IVLAGDHMQLSPFV--YSEFARERNLHVSLLDRL 875
Cdd:cd17936   112 AAEVLEAHILAAL---TPSTEhLILIGDHKQLRPKVnvYELTAKKYNLDVSLFERL 164
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 673-860 3.03e-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: 74.69  E-value: 3.03e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304   673 QKEAVLAittplAIQLPPV-LIIGPYGTGKTFTLAQAVKHILQQQET------RILICTHSNSAAD----LYIKDYLHPY 741
Cdd:pfam13086    2 QREAIRS-----ALSSSHFtLIQGPPGTGKTTTIVELIRQLLSYPATsaaagpRILVCAPSNAAVDnileRLLRKGQKYG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304   742 VEA---GNPQARplrvyfrnrwvktvHPVVHQYCLISSAHSTFQMPQKEDILK--------------------------- 791
Cdd:pfam13086   77 PKIvriGHPAAI--------------SEAVLPVSLDYLVESKLNNEEDAQIVKdiskeleklakalrafekeiivekllk 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304   792 -----------------------------------------HRVVVVTLNTS--QYLCQLDlepGFFThILLDEAAQAME 828
Cdd:pfam13086  143 srnkdkskleqerrklrserkelrkelrrreqslereildeAQIVCSTLSGAgsRLLSSLA---NFDV-VIIDEAAQALE 218

                          250       260       270
                   ....*....|....*....|....*....|..
gi 530413304   829 CETIMPLALATqnTRIVLAGDHMQLSPFVYSE 860
Cdd:pfam13086  219 PSTLIPLLRGP--KKVVLVGDPKQLPPTVISK 248
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
 691-894 8.91e-14

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: 69.57  E-value: 8.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  691 VLIIGPYGTGKTFTLAQAVKHILQQQET-RILICTHSNSAADlyikdylhpyveagnpqarplrvyfrnrwvktvhpvvh 769
Cdd:cd17934     2 SLIQGPPGTGKTTTIAAIVLQLLKGLRGkRVLVTAQSNVAVD-------------------------------------- 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  770 qyclissahstfqmpqkedilkhrvvvvtlntsqylcQLDlepgfftHILLDEAAQAMECETIMPLALATqntRIVLAGD 849
Cdd:cd17934    44 -------------------------------------NVD-------VVIIDEASQITEPELLIALIRAK---KVVLVGD 76

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 530413304  850 HMQLSPFVYSEFARE--RNLHVSLLDRLYEHYPAEFPcrILLCENYR 894
Cdd:cd17934    77 PKQLPPVVQEDHAALlgLSFILSLLLLFRLLLPGSPK--VMLDTQYR 121
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
 669-877 2.37e-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: 69.48  E-value: 2.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  669 LNAKQKEAVL-AITTPLaiqlppVLIIGPYGTGKTFTLAQAVKHILQQQETR------------ILICTHSNSAADLyIK 735
Cdd:cd18040     2 LNPSQNHAVRtALTKPF------TLIQGPPGTGKTVTGVHIAYWFAKQNREIqsvsgegdggpcVLYCGPSNKSVDV-VA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  736 DYLhpyveAGNPQARPLRVY--------------FRNRWVK--------------TVHPVVHQ----YC-LISSAHSTFQ 782
Cdd:cd18040    75 ELL-----LKVPGLKILRVYseqietteypipnePRHPNKKsereskpnselssiTLHHRIRQpsnpHSqQIKAFEARFE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  783 MPQ----KEDILKHRVVV------------VTLNTsqylCQLDLEPGFFTH-----ILLDEAAQAMECETIMPLALATQN 841
Cdd:cd18040   150 RTQekitEEDIKTYKILIwearfeeletvdVILCT----CSEAASQKMRTHanvkqCIVDECGMCTEPESLIPIVSAPRA 225

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 530413304  842 TRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYE 877
Cdd:cd18040   226 EQVVLIGDHKQLRPVVQNKEAQKLGLGRSLFERYAE 261
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
 668-875 3.68e-10

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: 61.67  E-value: 3.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  668 RLNAKQKEAVLAittplAIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQ-ETRILICTHSNSAA-DLYIKdylhpyVEAg 745
Cdd:cd17935     5 KFTPTQIEAIRS-----GMQPGLTMVVGPPGTGKTDVAVQIISNLYHNFpNQRTLIVTHSNQALnQLFEK------IMA- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  746 npqarpLRVYFRNrwvktvhpvvhqycLISSAHSTfqmpqkedilkhRVVVVTLnTSQYLCQLDL-EPGF-FTHILLDEA 823
Cdd:cd17935    73 ------LDIDERH--------------LLRLGHGA------------KIIAMTC-THAALKRGELvELGFkYDNILMEEA 119

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530413304  824 AQAMECETIMPLALATQNT------RIVLAGDHMQLSPFVYS-EFARERNLHVSLLDRL 875
Cdd:cd17935   120 AQILEIETFIPLLLQNPEDgpnrlkRLIMIGDHHQLPPVIKNmAFQKYSNMEQSLFTRL 178
DEXQc_UvrD cd17932
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch ...
 670-893 3.60e-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: 55.21  E-value: 3.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  670 NAKQKEAVLAITTPLaiqlppvLII-GPyGTGKTFTLAQAVKHILQQQET---RILICTHSNSAADlYIKDYLHPYVeaG 745
Cdd:cd17932     1 NPEQREAVTHPDGPL-------LVLaGA-GSGKTRVLTHRIAYLILEGGVppeRILAVTFTNKAAK-EMRERLRKLL--G 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  746 NPQARPLrvyfrnrWVKTVHPVvhqyCL-ISSAHSTFqmpqkEDILkHRVVVVtLNTSQYLCQLDLEPgfFTHILLDEA- 823
Cdd:cd17932    70 EQLASGV-------WIGTFHSF----ALrILRRYGDF-----DDLL-LYALEL-LEENPDVREKLQSR--FRYILVDEYq 129

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530413304  824 ----AQamecETIMpLALATQNTRIVLAGDHMQlSpfVYSeFareRNLHVSLLDRLYEHYPAefPCRILLCENY 893
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 ...
 670-858 8.15e-08

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: 52.58  E-value: 8.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  670 NAKQKEAVLAittplAIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQEtRILICTHSNSAADlyikdylhpyveagnpqa 749
Cdd:cd18043     1 DSSQEAAIIS-----ARNGKNVVIQGPPGTGKSQTIANIIANALARGK-RVLFVSEKKAALD------------------ 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  750 rplrvyfrnrwvktvhpVVHQYCLISSAHSTFQMpqkedilkhrvvvvtlntsqylcqLDLEPGFFTHILLDEAAQAMEC 829
Cdd:cd18043    57 -----------------VVRFPCWIMSPLSVSQY------------------------LPLNRNLFDLVIFDEASQIPIE 95

                         170       180
                  ....*....|....*....|....*....
gi 530413304  830 ETIMPLALATQntrIVLAGDHMQLSPFVY 858
Cdd:cd18043    96 EALPALFRGKQ---VVVVGDDKQLPPSIL 121
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
 672-855 3.37e-07

DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 51.79  E-value: 3.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  672 KQKEAVLAITtplaiQLPPVLIIGPYGTGKTFTLAQAVKhILQQQETRILICTHSNSAADLyikdyLHpyvEAGNPQARp 751
Cdd:cd17933     1 EQKAAVRLVL-----RNRVSVLTGGAGTGKTTTLKALLA-ALEAEGKRVVLAAPTGKAAKR-----LS---ESTGIEAS- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  752 lrvyfrnrwvkTVHPVvhqycLISSAHSTFQMPQKEDILKHRVVVVtlntsqylcqldlepgffthillDEAaqAMecet 831
Cdd:cd17933    66 -----------TIHRL-----LGINPGGGGFYYNEENPLDADLLIV-----------------------DEA--SM---- 100

                         170       180       190
                  ....*....|....*....|....*....|.
gi 530413304  832 iMPLALATQ-------NTRIVLAGDHMQLSP 855
Cdd:cd17933   101 -VDTRLMAAllsaipaGARLILVGDPDQLPS 130
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
 690-731 6.33e-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: 50.18  E-value: 6.33e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 530413304  690 PVLIIGPYGTGKTFTLAQAVKHILQQ---QETRILICTHSNSAAD 731
Cdd:cd17914     1 LSLIQGPPGTGKTRVLVKIVAALMQNkngEPGRILLVTPTNKAAA 45
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 659-1099 6.70e-07

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: 54.21  E-value: 6.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  659 RQWDEQLDPRLNAKQKEAVLAITTPLAIqlppVLIIGPYGTGKTFTLAqAVKHILQQQETRILICTHSNSAAD-LYikdy 737
Cdd:COG0507   115 AALEPRAGITLSDEQREAVALALTTRRV----SVLTGGAGTGKTTTLR-ALLAALEALGLRVALAAPTGKAAKrLS---- 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  738 lhpyvEAGNPQARplrvyfrnrwvkTVHPVVHqyclISSAHSTFQMPQKEDILKHRVVVVtlntsqylcqldlepgffth 817
Cdd:COG0507   186 -----ESTGIEAR------------TIHRLLG----LRPDSGRFRHNRDNPLTPADLLVV-------------------- 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  818 illDEA--------AQAMEcetimplALATQNTRIVLAGDHMQLSP----FVYSEFARERNLHVSLLDrlyehypaefpc 885
Cdd:COG0507   225 ---DEAsmvdtrlmAALLE-------ALPRAGARLILVGDPDQLPSvgagAVLRDLIESGTVPVVELT------------ 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  886 rillcENYRSHEAI-INYTSELFYEGKlMASGKQPAHKDFYPL----------------TFFTARGEDVQ-----EKnST 943
Cdd:COG0507   283 -----EVYRQADDSrIIELAHAIREGD-APEALNARYADVVFVeaedaeeaaeaivelyADRPAGGEDIQvlaptNA-GV 355

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  944 AFYN-------NAEVFEVVERVEELRRKW----PV-------AWGkLDDGSIGVVTPYADQVFRIRAELRKKRLSDVNVE 1005
Cdd:COG0507   356 DALNqairealNPAGELERELAEDGELELyvgdRVmftrndyDLG-VFNGDIGTVLSIDEDEGRLTVRFDGREIVTYDPS 434

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304 1006 RVLNV-----------QGKQF-RVLFLSTvrtrhtckhkqtpikkkeqlledsteDLDYGFLSNyKLLNTAITRAQSLVA 1073
Cdd:COG0507   435 ELDQLelayaitvhksQGSTFdRVILVLP--------------------------SEHSPLLSR-ELLYTALTRARELLT 487

                         490       500
                  ....*....|....*....|....*.
gi 530413304 1074 VVGDPIALCSIgrCRKFWERFIALCH 1099
Cdd:COG0507   488 LVGDRDALARA--VRRDTARATGLAE 511
UvrD COG0210
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
668-730 5.20e-06

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


Pssm-ID: 439980 [Multi-domain]  Cd Length: 721  Bit Score: 51.47  E-value: 5.20e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530413304  668 RLNAKQKEAVLAITTPLaiqlppvLII-GPyGTGKTFTLAQAVKHILQQQET---RILICTHSNSAA 730
Cdd:COG0210     6 GLNPEQRAAVEHPEGPL-------LVLaGA-GSGKTRVLTHRIAYLIAEGGVdpeQILAVTFTNKAA 64
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
181-205 6.50e-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: 6.50e-06
                           10        20
                   ....*....|....*....|....*
gi 530413304   181 YTLCKRFLEQGICRYGAQCTSAHSQ 205
Cdd:pfam00642    3 TELCRFFLRTGYCKYGDRCKFAHGQ 27
UvrD-helicase pfam00580
UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural ...
 669-765 2.49e-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: 48.01  E-value: 2.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304   669 LNAKQKEAVLAITTPLaiqlppvLIIGPYGTGKTFTLAQAVKHILQQ---QETRILICTHSNSAAD---LYIKDYLhpyv 742
Cdd:pfam00580    1 LNPEQRKAVTHLGGPL-------LVLAGAGSGKTRVLTERIAYLILEggiDPEEILAVTFTNKAARemkERILKLL---- 69

                           90       100
                   ....*....|....*....|...
gi 530413304   743 eaGNPQARPLrvyfrnrWVKTVH 765
Cdd:pfam00580   70 --GKAELSEL-------NISTFH 83
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 668-855 5.11e-05

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: 46.02  E-value: 5.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304   668 RLNAKQKEAVLAITT-PLAIQLppvlIIGPYGTGKTFTLAqAVKHILQQQETRILICTHSNSAADLYIKDYLHPyveagn 746
Cdd:pfam13604    1 TLNAEQAAAVRALLTsGDRVAV----LVGPAGTGKTTALK-ALREAWEAAGYRVIGLAPTGRAAKVLGEELGIP------ 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304   747 pqARplrvyfrnrwvkTVHPVVHQYclissahstfqmPQKEDILKHRVVVVtlntsqylcqldlepgffthillDEAAQA 826
Cdd:pfam13604   70 --AD------------TIAKLLHRL------------GGRAGLDPGTLLIV-----------------------DEAGMV 100

                          170       180       190
                   ....*....|....*....|....*....|....
gi 530413304   827 ----MEcetiMPLALATQ-NTRIVLAGDHMQLSP 855
Cdd:pfam13604  101 gtrqMA----RLLKLAEDaGARVILVGDPRQLPS 130
AAA_19 pfam13245
AAA domain;
673-731 1.92e-04

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 43.36  E-value: 1.92e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530413304   673 QKEAVLAittplAIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQET--RILICTHSNSAAD 731
Cdd:pfam13245    1 QREAVRT-----ALPSKVVLLTGGPGTGKTTTIRHIVALLVALGGVsfPILLAAPTGRAAK 56
ResIII pfam04851
Type III restriction enzyme, res subunit;
669-823 7.03e-04

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 42.27  E-value: 7.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304   669 LNAKQKEAVLAITTPLAIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQ-ETRILICTHSNsaaDLY------IKDYLHPY 741
Cdd:pfam04851    4 LRPYQIEAIENLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGpIKKVLFLVPRK---DLLeqaleeFKKFLPNY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304   742 VEAGNpqarPLRVYFRNRWVKTVHPVVhqyclissahSTFQmpqkedilkhrvvvvTLNTSQYLCQLDLEPGFFTHILLD 821
Cdd:pfam04851   81 VEIGE----IISGDKKDESVDDNKIVV----------TTIQ---------------SLYKALELASLELLPDFFDVIIID 131


                   ..
gi 530413304   822 EA 823
Cdd:pfam04851  132 EA 133
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
664-756 9.29e-04

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 44.25  E-value: 9.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304  664 QLDPRLNAKQKEAVLAITTPLAIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQetRILICTHS----NSAADLyIKDYLH 739
Cdd:COG1061    76 GTSFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGK--RVLVLVPRrellEQWAEE-LRRFLG 152

                          90
                  ....*....|....*..
gi 530413304  740 PYVEAGNPQARPLRVYF 756
Cdd:COG1061   153 DPLAGGGKKDSDAPITV 169
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 690-768 1.99e-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: 40.82  E-value: 1.99e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530413304    690 PVLIIGPYGTGKTfTLAQAVKHILQQQETRILICTHSNSAADLYIKDYLHPYVEAGNPQARPLRVYFRNRWVKTVHPVV 768
Cdd:smart00382    4 VILIVGPPGSGKT-TLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDV 81
PhoH pfam02562
PhoH-like protein; PhoH is a cytoplasmic protein and predicted ATPase that is induced by ...
 669-752 8.69e-03

PhoH-like protein; PhoH is a cytoplasmic protein and predicted ATPase that is induced by phosphate starvation.


Pssm-ID: 460592 [Multi-domain]  Cd Length: 204  Bit Score: 39.77  E-value: 8.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413304   669 LNAKQKEAVLAIttpLAIQLppVLIIGPYGTGKTF-TLAQAVKHILQQQETRILIcthsnsaadlyikdyLHPYVEAG-- 745
Cdd:pfam02562    4 KTLGQKRYVEAI---KKNDI--VFGIGPAGTGKTYlAVAMAVDALKNGKVKRIIL---------------TRPAVEAGek 63

                           90
                   ....*....|....*....
gi 530413304   746 ------------NPQARPL 752
Cdd:pfam02562   64 lgflpgdleekvDPYLRPL 82
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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