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Conserved domains on  [gi|568976424|ref|XP_006534567|]
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probable helicase with zinc finger domain isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
 641-868 3.19e-151

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: 465.04  E-value: 3.19e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  641 RLNAKQKEAVLAITTPLSIQLPPVLIIGPYGTGKTFTLAQAAKHILQQQETsRILICTHSNSAADLYIKDYLHPYVEAGN 720
Cdd:cd18077     1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPET-RILICTHSNSAADLYIKEYLHPYVETGN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  721 PQARPLRVYFRNRWVKTVHPVVHQYCLISStQSTFQMPQKEDILKHRVVVVTLSTSQYLCQLDLEPGFFTHVLLDEAAQA 800
Cdd:cd18077    80 PRARPLRVYYRNRWVKTVHPVVQKYCLIDE-HGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQA 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568976424  801 MECETIMPLALATKNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEFPCRILLCENYR 868
Cdd:cd18077   159 MECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSEHPCRILLCENYR 226
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
766-1075 1.62e-42

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


:

Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 169.54  E-value: 1.62e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  766 HRVVVVTLSTSQYLcqLDLEPGFFTHVLLDEAAQAMECETIMPLALATkntRIVLAGDHMQLSPFV---YSEFARERNLH 842
Cdd:COG1112   535 APVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVfgeEAEEVAEEGLD 609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  843 VSLLDRLYEHYPaefPCRILLCENYRSHEAIINYTSELFYEGKLMA---SGKQPAHKDFYPLTFFTARGedVQEKNSTAF 919
Cdd:COG1112   610 ESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDG--VYERRGGSR 684

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  920 YNnaevfevverveelrrkwP------VAW------GKLDDGSIGVVTPYADQVFRIRAELRKKRLSDV------NVERv 981
Cdd:COG1112   685 TN------------------PeeaeavVELvrelleDGPDGESIGVITPYRAQVALIRELLREALGDGLepvfvgTVDR- 745

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  982 lnVQGKQFRVLFLSTVRTRhtckhkqtpikkkeqlleDSTEDLDYGFLS-NYKLLNTAITRAQSLVAVVGDPvALCSIGR 1060
Cdd:COG1112   746 --FQGDERDVIIFSLVYSN------------------DEDVPRNFGFLNgGPRRLNVAVSRARRKLIVVGSR-ELLDSDP 804

                         330
                  ....*....|....*
gi 568976424 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 5.60e-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: 5.60e-06
                           10        20
                   ....*....|....*....|....*
gi 568976424   181 YTLCKRFLEQGICRYGAQCTSAHSQ 205
Cdd:pfam00642    3 TELCRFFLRTGYCKYGDRCKFAHGQ 27
Amelogenin super family cl33250
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 1338-1414 9.80e-05

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


The actual alignment was detected with superfamily member smart00818:

Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 44.78  E-value: 9.80e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568976424   1338 LNPRHINNLPLPAPHAQYAIPSRHfHPLPQLPRPPFPASQPHTLLNQQQNNLPEQPNQMAPQPNQVAPQPNQMTPQP 1414
Cdd:smart00818   42 VSQQHPPTHTLQPHHHIPVLPAQQ-PVVPQQPLMPVPGQHSMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQPMQPQ 117
Tymo_45kd_70kd super family cl25879
Tymovirus 45/70Kd protein; Tymoviruses are single stranded RNA viruses. This family includes a ...
 1225-1414 3.41e-03

Tymovirus 45/70Kd protein; Tymoviruses are single stranded RNA viruses. This family includes a protein of unknown function that has been named based on its molecular weight. Tymoviruses such as the ononis yellow mosaic tymovirus encode only three proteins. Of these two are overlapping this protein overlaps a larger ORF that is thought to be the polymerase.


The actual alignment was detected with superfamily member pfam03251:

Pssm-ID: 281269 [Multi-domain]  Cd Length: 468  Bit Score: 42.09  E-value: 3.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  1225 PRIITHQAAMAYNMNLLHTHGRGSP----IP------YGLGHHPPVSLGQPQSQHAEKDQQEQNRNGKTDTNNPGPeiNK 1294
Cdd:pfam03251  256 PRPITPGPSNTHDLRPLSVLPRTSPrrglLPnprrhrTSTGHIPPTTTSRPTGPPSRLQRPVHLYQSSPHTPNFRP--SS 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  1295 IRTPEKKPTEPKQVDLE--SNPQN-RSPESRPGvvySNTKFPRKDHlnprhINNLPLPAPHAQYAIPSRHFHPLPQLPRP 1371
Cdd:pfam03251  334 IRKDALLQTGPRLGHLErlGQPANlRTSERSPP---TKRRLPRSSE-----PNRLPKPLPEATLAPSYRHRRPYPLLPNP 405

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 568976424  1372 P--FPASQPHTLLNQQQNNLPEQ--PNQMAPQPNQVAPQPnqmTPQP 1414
Cdd:pfam03251  406 PaaLPSIAYTSSRGKIHHSLPKGalPKEGAPPPPRRLPSP---APRP 449
 
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 3.19e-151

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: 465.04  E-value: 3.19e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  641 RLNAKQKEAVLAITTPLSIQLPPVLIIGPYGTGKTFTLAQAAKHILQQQETsRILICTHSNSAADLYIKDYLHPYVEAGN 720
Cdd:cd18077     1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPET-RILICTHSNSAADLYIKEYLHPYVETGN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  721 PQARPLRVYFRNRWVKTVHPVVHQYCLISStQSTFQMPQKEDILKHRVVVVTLSTSQYLCQLDLEPGFFTHVLLDEAAQA 800
Cdd:cd18077    80 PRARPLRVYYRNRWVKTVHPVVQKYCLIDE-HGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQA 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568976424  801 MECETIMPLALATKNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEFPCRILLCENYR 868
Cdd:cd18077   159 MECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSEHPCRILLCENYR 226
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
766-1075 1.62e-42

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 169.54  E-value: 1.62e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  766 HRVVVVTLSTSQYLcqLDLEPGFFTHVLLDEAAQAMECETIMPLALATkntRIVLAGDHMQLSPFV---YSEFARERNLH 842
Cdd:COG1112   535 APVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVfgeEAEEVAEEGLD 609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  843 VSLLDRLYEHYPaefPCRILLCENYRSHEAIINYTSELFYEGKLMA---SGKQPAHKDFYPLTFFTARGedVQEKNSTAF 919
Cdd:COG1112   610 ESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDG--VYERRGGSR 684

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  920 YNnaevfevverveelrrkwP------VAW------GKLDDGSIGVVTPYADQVFRIRAELRKKRLSDV------NVERv 981
Cdd:COG1112   685 TN------------------PeeaeavVELvrelleDGPDGESIGVITPYRAQVALIRELLREALGDGLepvfvgTVDR- 745

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  982 lnVQGKQFRVLFLSTVRTRhtckhkqtpikkkeqlleDSTEDLDYGFLS-NYKLLNTAITRAQSLVAVVGDPvALCSIGR 1060
Cdd:COG1112   746 --FQGDERDVIIFSLVYSN------------------DEDVPRNFGFLNgGPRRLNVAVSRARRKLIVVGSR-ELLDSDP 804

                         330
                  ....*....|....*
gi 568976424 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 5.67e-36

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: 135.44  E-value: 5.67e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  869 SHEAIINYTSELFYEGKLMAS-------GKQPAHKDFYPLTFFTARGEDVQEKNSTAFYNNAEVFEVVERVEELRRKWpv 941
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGvsvaarlNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  942 awgkLDDGSIGVVTPYADQVFRIRAELRKKR--LSDVNVERVLNVQGKQFRVLFLSTVRTRHTCKHkqtpikkkeqlled 1019
Cdd:cd18808    79 ----VKPSSIGVITPYRAQVALIRELLRKRGglLEDVEVGTVDNFQGREKDVIILSLVRSNESGGS-------------- 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 568976424 1020 stedldYGFLSNYKLLNTAITRAQSLVAVVGDPVALCSIGRCRKFWERFI 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 4.48e-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: 4.48e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424   841 LHVSLLDRLYEHYPAefpCRILLCENYRSHEAIINYTSELFYEGKLMASGKQPAH---------KDFYPLTFF-TARGED 910
Cdd:pfam13087    1 LDRSLFERLQELGPS---AVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERplpddfhlpDPLGPLVFIdVDGSEE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424   911 VQEKNSTAFYNNAEVFEVVERVEELRRKWPVAWGKlddgsIGVVTPYADQVFRIRAELRKKRLSDVNVErVLNV---QGK 987
Cdd:pfam13087   78 EESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSD-----IGVITPYRAQVRLIRKLLKRKLGGKLEIE-VNTVdgfQGR 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568976424   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 ...
 652-834 1.27e-16

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: 81.62  E-value: 1.27e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424   652 AITTPLSiQLPPVLIIGPYGTGKTFTLAQAAKHILQQQETS-----RILICTHSNSAAD----LYIKDYLHPYVEA---G 719
Cdd:pfam13086    5 AIRSALS-SSHFTLIQGPPGTGKTTTIVELIRQLLSYPATSaaagpRILVCAPSNAAVDnileRLLRKGQKYGPKIvriG 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424   720 NPQARplrvyfrnrwvktvHPVVHQYCLISSTQSTFQMPQKEDILK---------------------------------- 765
Cdd:pfam13086   84 HPAAI--------------SEAVLPVSLDYLVESKLNNEEDAQIVKdiskeleklakalrafekeiivekllksrnkdks 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424   766 ----------------------------------HRVVVVTLSTS--QYLCQLDlepGFFThVLLDEAAQAMECETIMPL 809
Cdd:pfam13086  150 kleqerrklrserkelrkelrrreqslereildeAQIVCSTLSGAgsRLLSSLA---NFDV-VIIDEAAQALEPSTLIPL 225

                          250       260
                   ....*....|....*....|....*
gi 568976424   810 ALATKntRIVLAGDHMQLSPFVYSE 834
Cdd:pfam13086  226 LRGPK--KVVLVGDPKQLPPTVISK 248
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 632-1073 1.28e-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: 53.44  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  632 RQWDEQLDPRLNAKQKEAVLAITTPLSIqlppVLIIGPYGTGKTFTLAQAAKHILQQQEtsRILICTHSNSAAD-LYikd 710
Cdd:COG0507   115 AALEPRAGITLSDEQREAVALALTTRRV----SVLTGGAGTGKTTTLRALLAALEALGL--RVALAAPTGKAAKrLS--- 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  711 ylhpyvEAGNPQARplrvyfrnrwvkTVHPVVHqyclISSTQSTFQMPQKEDILKHRVVVVtlstsqylcqldlepgfft 790
Cdd:COG0507   186 ------ESTGIEAR------------TIHRLLG----LRPDSGRFRHNRDNPLTPADLLVV------------------- 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  791 hvllDEA--------AQAMEcetimplALATKNTRIVLAGDHMQLSP----FVYSEFARERNLHVSLLDrlyehypaefp 858
Cdd:COG0507   225 ----DEAsmvdtrlmAALLE-------ALPRAGARLILVGDPDQLPSvgagAVLRDLIESGTVPVVELT----------- 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  859 crillcENYRSHEAI-INYTSELFYEGKlMASGKQPAHKDFYPL----------------TFFTARGEDVQ-----EKnS 916
Cdd:COG0507   283 ------EVYRQADDSrIIELAHAIREGD-APEALNARYADVVFVeaedaeeaaeaivelyADRPAGGEDIQvlaptNA-G 354

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  917 TAFYN-------NAEVFEVVERVEELRRKW----PV-------AWGkLDDGSIGVVTPYADQVFRIRAELRKKRLSDVNV 978
Cdd:COG0507   355 VDALNqairealNPAGELERELAEDGELELyvgdRVmftrndyDLG-VFNGDIGTVLSIDEDEGRLTVRFDGREIVTYDP 433

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  979 ERVLNV-----------QGKQF-RVLFLSTvrtrhtckhkqtpikkkeqlledsteDLDYGFLSNyKLLNTAITRAQSLV 1046
Cdd:COG0507   434 SELDQLelayaitvhksQGSTFdRVILVLP--------------------------SEHSPLLSR-ELLYTALTRARELL 486

                         490       500
                  ....*....|....*....|....*..
gi 568976424 1047 AVVGDPVALCSIgrCRKFWERFIALCH 1073
Cdd:COG0507   487 TLVGDRDALARA--VRRDTARATGLAE 511
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
181-205 5.60e-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: 5.60e-06
                           10        20
                   ....*....|....*....|....*
gi 568976424   181 YTLCKRFLEQGICRYGAQCTSAHSQ 205
Cdd:pfam00642    3 TELCRFFLRTGYCKYGDRCKFAHGQ 27
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 1338-1414 9.80e-05

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 44.78  E-value: 9.80e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568976424   1338 LNPRHINNLPLPAPHAQYAIPSRHfHPLPQLPRPPFPASQPHTLLNQQQNNLPEQPNQMAPQPNQVAPQPNQMTPQP 1414
Cdd:smart00818   42 VSQQHPPTHTLQPHHHIPVLPAQQ-PVVPQQPLMPVPGQHSMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQPMQPQ 117
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 1305-1414 2.74e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 46.23  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424 1305 PKQVDLESNPQnrSPESRPGVVYSNTKFPRKDHLNPRHINNLPLPaPHAQYAIPSRHFHPLPQLPRPPFPASQPHTLLNQ 1384
Cdd:PRK10263  731 PMKALLDDGPH--EPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVA-PQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQP 807

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568976424 1385 QQnnlPEQPNQMAPQPNQ-VAPQPNQMTPQP 1414
Cdd:PRK10263  808 QQ---PVAPQPQYQQPQQpVAPQPQYQQPQQ 835
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1273-1413 1.44e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.60  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  1273 DQQEQNRNGKTDTNNPGPEiNKIRTPEKKPTEPKQVDLESNPQNRSPESRPGVVYSNTKFPRKDHLNPRHINNLPLPAP- 1351
Cdd:pfam03154  122 DGRSVNDEGSSDPKDIDQD-NRSTSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPt 200

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568976424  1352 HAQYAIPSRHFHPLPQLPRPPFPASQPHTLLNQ------QQNNLPEQPNQMAPQPnqvaPQPNQMTPQ 1413
Cdd:pfam03154  201 PSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQtptlhpQRLPSPHPPLQPMTQP----PPPSQVSPQ 264
Tymo_45kd_70kd pfam03251
Tymovirus 45/70Kd protein; Tymoviruses are single stranded RNA viruses. This family includes a ...
 1225-1414 3.41e-03

Tymovirus 45/70Kd protein; Tymoviruses are single stranded RNA viruses. This family includes a protein of unknown function that has been named based on its molecular weight. Tymoviruses such as the ononis yellow mosaic tymovirus encode only three proteins. Of these two are overlapping this protein overlaps a larger ORF that is thought to be the polymerase.


Pssm-ID: 281269 [Multi-domain]  Cd Length: 468  Bit Score: 42.09  E-value: 3.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  1225 PRIITHQAAMAYNMNLLHTHGRGSP----IP------YGLGHHPPVSLGQPQSQHAEKDQQEQNRNGKTDTNNPGPeiNK 1294
Cdd:pfam03251  256 PRPITPGPSNTHDLRPLSVLPRTSPrrglLPnprrhrTSTGHIPPTTTSRPTGPPSRLQRPVHLYQSSPHTPNFRP--SS 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  1295 IRTPEKKPTEPKQVDLE--SNPQN-RSPESRPGvvySNTKFPRKDHlnprhINNLPLPAPHAQYAIPSRHFHPLPQLPRP 1371
Cdd:pfam03251  334 IRKDALLQTGPRLGHLErlGQPANlRTSERSPP---TKRRLPRSSE-----PNRLPKPLPEATLAPSYRHRRPYPLLPNP 405

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 568976424  1372 P--FPASQPHTLLNQQQNNLPEQ--PNQMAPQPNQVAPQPnqmTPQP 1414
Cdd:pfam03251  406 PaaLPSIAYTSSRGKIHHSLPKGalPKEGAPPPPRRLPSP---APRP 449
 
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 3.19e-151

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: 465.04  E-value: 3.19e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  641 RLNAKQKEAVLAITTPLSIQLPPVLIIGPYGTGKTFTLAQAAKHILQQQETsRILICTHSNSAADLYIKDYLHPYVEAGN 720
Cdd:cd18077     1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPET-RILICTHSNSAADLYIKEYLHPYVETGN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  721 PQARPLRVYFRNRWVKTVHPVVHQYCLISStQSTFQMPQKEDILKHRVVVVTLSTSQYLCQLDLEPGFFTHVLLDEAAQA 800
Cdd:cd18077    80 PRARPLRVYYRNRWVKTVHPVVQKYCLIDE-HGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQA 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568976424  801 MECETIMPLALATKNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEFPCRILLCENYR 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 6.79e-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: 6.79e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  641 RLNAKQKEAVLAITTPLSiQLPPVLIIGPYGTGKTFTLAQAAKHILQQQETSRILICTHSNSAADLYIKDYLHPYVeagn 720
Cdd:cd18038     1 ELNDEQKLAVRNIVTGTS-RPPPYIIFGPPGTGKTVTLVEAILQVLRQPPEARILVCAPSNSAADLLAERLLNALV---- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  721 PQARPLRVYFRNRWVKTVHPVVHQYCLISStQSTFQMPQKEDILKHRVVVVTLSTSQYLCQLDLEPGFFTHVLLDEAAQA 800
Cdd:cd18038    76 TKREILRLNAPSRDRASVPPELLPYCNSKA-EGTFRLPSLEELKKYRIVVCTLMTAGRLVQAGVPNGHFTHIFIDEAGQA 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568976424  801 MECETIMPLA-LATKNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYP------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 7.03e-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: 231.70  E-value: 7.03e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  641 RLNAKQKEAVLAIT--TPLSIQLPPVLIIGPYGTGKTFTLAQAAKHILQQQETsRILICTHSNSAADLYIKDYLHPYVEA 718
Cdd:cd18076     1 AGNNKQQLAFNFIAgkPSEARFVPPLLIYGPFGTGKTFTLAMAALEVIREPGT-KVLICTHTNSAADIYIREYFHPYVDK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  719 GNPQARPLRVYFRNRWVKTVHPVVHQYCLISSTQSTFQMPQKEDILKHRVVVVTLSTSQylcQLDLEPGFFTHVLLDEAA 798
Cdd:cd18076    80 GHPEARPLRIKATDRPNAITDPDTITYCCLTKDRQCFRLPTRDELDFHNIVITTTAMAF---NLHVLSGFFTHIFIDEAA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568976424  799 QAMECETIMPLALATKNTRIVLAGDHMQLSPFVYSeFARERNLHVSLLDRLYEHYPAE-----FPCRILLCENYR 868
Cdd:cd18076   157 QMLECEALIPLSYAGPKTRVVLAGDHMQMTPKLFS-VADYNRANHTLLNRLFHYYQGEkhevaVKSRVIFSENYR 230
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
766-1075 1.62e-42

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 169.54  E-value: 1.62e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  766 HRVVVVTLSTSQYLcqLDLEPGFFTHVLLDEAAQAMECETIMPLALATkntRIVLAGDHMQLSPFV---YSEFARERNLH 842
Cdd:COG1112   535 APVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVfgeEAEEVAEEGLD 609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  843 VSLLDRLYEHYPaefPCRILLCENYRSHEAIINYTSELFYEGKLMA---SGKQPAHKDFYPLTFFTARGedVQEKNSTAF 919
Cdd:COG1112   610 ESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDG--VYERRGGSR 684

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  920 YNnaevfevverveelrrkwP------VAW------GKLDDGSIGVVTPYADQVFRIRAELRKKRLSDV------NVERv 981
Cdd:COG1112   685 TN------------------PeeaeavVELvrelleDGPDGESIGVITPYRAQVALIRELLREALGDGLepvfvgTVDR- 745

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  982 lnVQGKQFRVLFLSTVRTRhtckhkqtpikkkeqlleDSTEDLDYGFLS-NYKLLNTAITRAQSLVAVVGDPvALCSIGR 1060
Cdd:COG1112   746 --FQGDERDVIIFSLVYSN------------------DEDVPRNFGFLNgGPRRLNVAVSRARRKLIVVGSR-ELLDSDP 804

                         330
                  ....*....|....*
gi 568976424 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 7.15e-41

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: 151.37  E-value: 7.15e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  642 LNAKQKEAVLAITTPLSIQLPPVlIIGPYGTGKTFTLAQAakhILQQQET---SRILICTHSNSAADLYIKDyLHPYVEA 718
Cdd:cd18078     2 LNELQKEAVKRILGGECRPLPYI-LFGPPGTGKTVTIIEA---ILQVVYNlprSRILVCAPSNSAADLVTSR-LHESKVL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  719 GNPQARPLRVYfrNRWVKTVHPVVHQYCLISStqstfqmpQKEDILKHRVVVVTLSTSQYLCQLDLEPGFFTHVLLDEAA 798
Cdd:cd18078    77 KPGDMVRLNAV--NRFESTVIDARKLYCRLGE--------DLSKASRHRIVISTCSTAGLLYQMGLPVGHFTHVFVDEAG 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  799 QAMECETIMPLALATKNT-RIVLAGDHMQLSPFVYSEFARERNLHVSLLDRL-----YEHYPAEFP-CRIL-------LC 864
Cdd:cd18078   147 QATEPESLIPLGLISSRDgQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLmnrplYLRDPNRFGeSGGYnpllvtkLV 226


                  ....
gi 568976424  865 ENYR 868
Cdd:cd18078   227 DNYR 230
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
 869-1069 5.67e-36

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: 135.44  E-value: 5.67e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  869 SHEAIINYTSELFYEGKLMAS-------GKQPAHKDFYPLTFFTARGEDVQEKNSTAFYNNAEVFEVVERVEELRRKWpv 941
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGvsvaarlNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  942 awgkLDDGSIGVVTPYADQVFRIRAELRKKR--LSDVNVERVLNVQGKQFRVLFLSTVRTRHTCKHkqtpikkkeqlled 1019
Cdd:cd18808    79 ----VKPSSIGVITPYRAQVALIRELLRKRGglLEDVEVGTVDNFQGREKDVIILSLVRSNESGGS-------------- 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 568976424 1020 stedldYGFLSNYKLLNTAITRAQSLVAVVGDPVALCSIGRCRKFWERFI 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 4.48e-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: 4.48e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424   841 LHVSLLDRLYEHYPAefpCRILLCENYRSHEAIINYTSELFYEGKLMASGKQPAH---------KDFYPLTFF-TARGED 910
Cdd:pfam13087    1 LDRSLFERLQELGPS---AVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERplpddfhlpDPLGPLVFIdVDGSEE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424   911 VQEKNSTAFYNNAEVFEVVERVEELRRKWPVAWGKlddgsIGVVTPYADQVFRIRAELRKKRLSDVNVErVLNV---QGK 987
Cdd:pfam13087   78 EESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSD-----IGVITPYRAQVRLIRKLLKRKLGGKLEIE-VNTVdgfQGR 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568976424   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 3.46e-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: 108.09  E-value: 3.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  641 RLNAKQKEAVLAITTPLSIqlppVLIIGPYGTGKTFTLAQAAKhILQQQETSrILICTHSNSAAD---LYIKDYLHPYVE 717
Cdd:cd18041     1 GLNKDQRQAIKKVLNAKDY----ALILGMPGTGKTTTIAALVR-ILVALGKS-VLLTSYTHSAVDnilLKLKKFGVNFLR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  718 AGNPqarplrvyfrnrwvKTVHPVVHQYCLISSTQSTFQMPQKEDIL-KHRVVVVT-LSTSQYLcqldLEPGFFTHVLLD 795
Cdd:cd18041    75 LGRL--------------KKIHPDVQEFTLEAILKSCKSVEELESKYeSVSVVATTcLGINHPI----FRRRTFDYCIVD 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568976424  796 EAAQAMECETIMPLALATKntrIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYP 854
Cdd:cd18041   137 EASQITLPICLGPLRLAKK---FVLVGDHYQLPPLVKSREARELGMDESLFKRLSEAHP 192
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
 641-868 3.43e-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: 3.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  641 RLNAKQKEAVLaittpLSIQLPPVLII-GPYGTGKTFTLAQAakhILQQ-QETSRILICTHSNSAADLYIKDYLH---PY 715
Cdd:cd18044     1 NLNDSQKEAVK-----FALSQKDVALIhGPPGTGKTTTVVEI---ILQAvKRGEKVLACAPSNIAVDNLVERLVAlkvKV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  716 VEAGNPqARplrvyfrnrwvktVHPVVHQYCLisstqstfqmpqkEDILKHRVVVVTLSTSqylCQLDLEPG-FFTHVLL 794
Cdd:cd18044    73 VRIGHP-AR-------------LLESVLDHSL-------------DALVAAQVVLATNTGA---GSRQLLPNeLFDVVVI 122

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568976424  795 DEAAQAMECETIMPLalaTKNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEfpCRILLCENYR 868
Cdd:cd18044   123 DEAAQALEASCWIPL---LKARRCILAGDHKQLPPTILSDKAARGGLGVTLFERLVNLYGES--VVRMLTVQYR 191
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
 642-849 1.25e-20

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: 93.08  E-value: 1.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  642 LNAKQKEAV-LAITTPLSiqlppvLIIGPYGTGKTFTLAQAAKHILQQQEtSRILICTHSNSAADlYIKDYLHpyvEAGn 720
Cdd:cd18039     2 LNHSQVDAVkTALQRPLS------LIQGPPGTGKTVTSATIVYHLVKQGN-GPVLVCAPSNVAVD-QLTEKIH---QTG- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  721 pqARPLRVYFRNRW-----VK--TVHPVVHQY-----------------CLISSTQSTFQM----PQKEDILKHRVVVVT 772
Cdd:cd18039    70 --LKVVRLCAKSREavespVSflALHNQVRNLdsaeklellkllkletgELSSADEKRYRKlkrkAERELLRNADVICCT 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568976424  773 LSTSqylcqLD--LEPGFFTHVLLDEAAQAMECETIMPLALATKntRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRL 849
Cdd:cd18039   148 CVGA-----GDprLSKMKFRTVLIDEATQATEPECLIPLVHGAK--QVILVGDHCQLGPVVMCKKAAKAGLSQSLFERL 219
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
 642-868 3.63e-20

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: 91.12  E-value: 3.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  642 LNAKQKEAVLAIttpLSIQLPPVLIIGPYGTGKTFTL---------------AQAAKHILQQQETS--------RILICT 698
Cdd:cd18042     1 LNESQLEAIASA---LQNSPGITLIQGPPGTGKTKTIvgilsvllagkyrkyYEKVKKKLRKLQRNlnnkkkknRILVCA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  699 HSNSAADLYIKDYLHPYVEAGNPQARPLRVyfrnrwVKTVHpvvhqyclisstqstfQMPQKEDILKHRVVVVTLSTSQY 778
Cdd:cd18042    78 PSNAAVDEIVLRLLSEGFLDGDGRSYKPNV------VRVGR----------------QELRASILNEADIVCTTLSSSGS 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  779 LcQLDLEPGFFTHVLLDEAAQAMECETIMPLALATKntRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEhypAEFP 858
Cdd:cd18042   136 D-LLESLPRGFDTVIIDEAAQAVELSTLIPLRLGCK--RLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQL---AGYP 209

                         250
                  ....*....|
gi 568976424  859 CrILLCENYR 868
Cdd:cd18042   210 V-LMLTTQYR 218
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 652-834 1.27e-16

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: 81.62  E-value: 1.27e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424   652 AITTPLSiQLPPVLIIGPYGTGKTFTLAQAAKHILQQQETS-----RILICTHSNSAAD----LYIKDYLHPYVEA---G 719
Cdd:pfam13086    5 AIRSALS-SSHFTLIQGPPGTGKTTTIVELIRQLLSYPATSaaagpRILVCAPSNAAVDnileRLLRKGQKYGPKIvriG 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424   720 NPQARplrvyfrnrwvktvHPVVHQYCLISSTQSTFQMPQKEDILK---------------------------------- 765
Cdd:pfam13086   84 HPAAI--------------SEAVLPVSLDYLVESKLNNEEDAQIVKdiskeleklakalrafekeiivekllksrnkdks 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424   766 ----------------------------------HRVVVVTLSTS--QYLCQLDlepGFFThVLLDEAAQAMECETIMPL 809
Cdd:pfam13086  150 kleqerrklrserkelrkelrrreqslereildeAQIVCSTLSGAgsRLLSSLA---NFDV-VIIDEAAQALEPSTLIPL 225

                          250       260
                   ....*....|....*....|....*
gi 568976424   810 ALATKntRIVLAGDHMQLSPFVYSE 834
Cdd:pfam13086  226 LRGPK--KVVLVGDPKQLPPTVISK 248
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
 641-849 4.49e-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: 4.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  641 RLNAKQKEA-VLAITTPLSIqlppvlIIGPYGTGKTFTLAQAAKHILQ---QQETSRILICTHSNSAADLYIKDYLhpyv 716
Cdd:cd17936     1 TLDPSQLEAlKHALTSELAL------IQGPPGTGKTFLGVKLVRALLQnqdLSITGPILVVCYTNHALDQFLEGLL---- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  717 eagnpqarplrvyfrnrwvktvhpvvhQYClisstqstfqmpqKEDILKH--RVVVVTLSTSQYLCQL--DLEPgffTHV 792
Cdd:cd17936    71 ---------------------------DFG-------------PTKIVRLgaRVIGMTTTGAAKYRELlqALGP---KVV 107

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  793 LLDEAAQAMECETIMPLalaTKNTR-IVLAGDHMQLSPFV--YSEFARERNLHVSLLDRL 849
Cdd:cd17936   108 IVEEAAEVLEAHILAAL---TPSTEhLILIGDHKQLRPKVnvYELTAKKYNLDVSLFERL 164
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
 664-868 3.48e-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: 73.81  E-value: 3.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  664 VLIIGPYGTGKTFTLAQAAKHILQQQETSRILICTHSNSAADlyikdylhpyveagnpqarplrvyfrnrwvktvhpvvh 743
Cdd:cd17934     2 SLIQGPPGTGKTTTIAAIVLQLLKGLRGKRVLVTAQSNVAVD-------------------------------------- 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  744 qyclisstqstfqmpqkedilkhrvvvvtlstsqylcQLDlepgfftHVLLDEAAQAMECETIMPLALATKntrIVLAGD 823
Cdd:cd17934    44 -------------------------------------NVD-------VVIIDEASQITEPELLIALIRAKK---VVLVGD 76

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568976424  824 HMQLSPFVYSEFARE--RNLHVSLLDRLYEHYPAEFPcrILLCENYR 868
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 ...
 642-851 1.30e-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: 70.25  E-value: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  642 LNAKQKEAVL-AITTPLSiqlppvLIIGPYGTGKTFTLAQAAKHILQQQETSR-----------ILICTHSNSAADLyIK 709
Cdd:cd18040     2 LNPSQNHAVRtALTKPFT------LIQGPPGTGKTVTGVHIAYWFAKQNREIQsvsgegdggpcVLYCGPSNKSVDV-VA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  710 DYLhpyveAGNPQARPLRVY--------------FRNRWVK--------------TVHPVVHQ----YC-LISSTQSTFQ 756
Cdd:cd18040    75 ELL-----LKVPGLKILRVYseqietteypipnePRHPNKKsereskpnselssiTLHHRIRQpsnpHSqQIKAFEARFE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  757 MPQ----KEDILKHRVVV------------VTLSTsqylCQLDLEPGFFTH-----VLLDEAAQAMECETIMPLALATKN 815
Cdd:cd18040   150 RTQekitEEDIKTYKILIwearfeeletvdVILCT----CSEAASQKMRTHanvkqCIVDECGMCTEPESLIPIVSAPRA 225

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 568976424  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 2.16e-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: 62.44  E-value: 2.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  641 RLNAKQKEAVLAITTP-LSiqlppvLIIGPYGTGKTFTLAQAAKHILQQQETSRILICTHSNSAA-DLYIKDYlhpyvEA 718
Cdd:cd17935     5 KFTPTQIEAIRSGMQPgLT------MVVGPPGTGKTDVAVQIISNLYHNFPNQRTLIVTHSNQALnQLFEKIM-----AL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  719 GNPQARPLRvyfrnrwvktvhpvvhqyclisstqstfqmpqkediLKH--RVVVVTlSTSQYLCQLDL-EPGF-FTHVLL 794
Cdd:cd17935    74 DIDERHLLR------------------------------------LGHgaKIIAMT-CTHAALKRGELvELGFkYDNILM 116

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568976424  795 DEAAQAMECETIMPLALATKNT------RIVLAGDHMQLSPFVYS-EFARERNLHVSLLDRL 849
Cdd:cd17935   117 EEAAQILEIETFIPLLLQNPEDgpnrlkRLIMIGDHHQLPPVIKNmAFQKYSNMEQSLFTRL 178
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
 643-832 2.78e-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: 51.43  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  643 NAKQKEAVLAIttplsIQLPPVLIIGPYGTGKTFTLAQAAKHILQQQEtsRILICTHSNSAADlyikdylhpyveagnpq 722
Cdd:cd18043     1 DSSQEAAIISA-----RNGKNVVIQGPPGTGKSQTIANIIANALARGK--RVLFVSEKKAALD----------------- 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  723 arplrvyfrnrwvktvhpVVHQYCLISSTQSTFQMpqkedilkhrvvvvtlstsqylcqLDLEPGFFTHVLLDEAAQAME 802
Cdd:cd18043    57 ------------------VVRFPCWIMSPLSVSQY------------------------LPLNRNLFDLVIFDEASQIPI 94

                         170       180       190
                  ....*....|....*....|....*....|
gi 568976424  803 CETImPLALATKntRIVLAGDHMQLSPFVY 832
Cdd:cd18043    95 EEAL-PALFRGK--QVVVVGDDKQLPPSIL 121
DEXQc_UvrD cd17932
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch ...
 643-867 5.40e-07

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: 51.75  E-value: 5.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  643 NAKQKEAVLAITTPLsiqlppvLII-GPyGTGKTFTLAQAAKHILQQQET--SRILICTHSNSAADlYIKDYLHPYVeaG 719
Cdd:cd17932     1 NPEQREAVTHPDGPL-------LVLaGA-GSGKTRVLTHRIAYLILEGGVppERILAVTFTNKAAK-EMRERLRKLL--G 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  720 NPQARPLrvyfrnrWVKTVHPVvhqyCL-ISSTQSTFqmpqkEDILkHRVVVVtLSTSQYLCQLDLEPgfFTHVLLDEA- 797
Cdd:cd17932    70 EQLASGV-------WIGTFHSF----ALrILRRYGDF-----DDLL-LYALEL-LEENPDVREKLQSR--FRYILVDEYq 129

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568976424  798 ----AQamecETIMpLALATKNTRIVLAGDHMQlSpfVYSeFareRNLHVSLLDRLYEHYPAefPCRILLCENY 867
Cdd:cd17932   130 dtnpLQ----YELL-KLLAGDGKNLFVVGDDDQ-S--IYG-F---RGADPENILDFEKDFPD--AKVIKLEENY 189
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 632-1073 1.28e-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: 53.44  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  632 RQWDEQLDPRLNAKQKEAVLAITTPLSIqlppVLIIGPYGTGKTFTLAQAAKHILQQQEtsRILICTHSNSAAD-LYikd 710
Cdd:COG0507   115 AALEPRAGITLSDEQREAVALALTTRRV----SVLTGGAGTGKTTTLRALLAALEALGL--RVALAAPTGKAAKrLS--- 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  711 ylhpyvEAGNPQARplrvyfrnrwvkTVHPVVHqyclISSTQSTFQMPQKEDILKHRVVVVtlstsqylcqldlepgfft 790
Cdd:COG0507   186 ------ESTGIEAR------------TIHRLLG----LRPDSGRFRHNRDNPLTPADLLVV------------------- 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  791 hvllDEA--------AQAMEcetimplALATKNTRIVLAGDHMQLSP----FVYSEFARERNLHVSLLDrlyehypaefp 858
Cdd:COG0507   225 ----DEAsmvdtrlmAALLE-------ALPRAGARLILVGDPDQLPSvgagAVLRDLIESGTVPVVELT----------- 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  859 crillcENYRSHEAI-INYTSELFYEGKlMASGKQPAHKDFYPL----------------TFFTARGEDVQ-----EKnS 916
Cdd:COG0507   283 ------EVYRQADDSrIIELAHAIREGD-APEALNARYADVVFVeaedaeeaaeaivelyADRPAGGEDIQvlaptNA-G 354

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  917 TAFYN-------NAEVFEVVERVEELRRKW----PV-------AWGkLDDGSIGVVTPYADQVFRIRAELRKKRLSDVNV 978
Cdd:COG0507   355 VDALNqairealNPAGELERELAEDGELELyvgdRVmftrndyDLG-VFNGDIGTVLSIDEDEGRLTVRFDGREIVTYDP 433

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  979 ERVLNV-----------QGKQF-RVLFLSTvrtrhtckhkqtpikkkeqlledsteDLDYGFLSNyKLLNTAITRAQSLV 1046
Cdd:COG0507   434 SELDQLelayaitvhksQGSTFdRVILVLP--------------------------SEHSPLLSR-ELLYTALTRARELL 486

                         490       500
                  ....*....|....*....|....*..
gi 568976424 1047 AVVGDPVALCSIgrCRKFWERFIALCH 1073
Cdd:COG0507   487 TLVGDRDALARA--VRRDTARATGLAE 511
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
 663-705 2.42e-06

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: 48.25  E-value: 2.42e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568976424  663 PVLIIGPYGTGKTFTLAQAAKHILQQQETS--RILICTHSNSAAD 705
Cdd:cd17914     1 LSLIQGPPGTGKTRVLVKIVAALMQNKNGEpgRILLVTPTNKAAA 45
UvrD COG0210
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
641-704 4.27e-06

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


Pssm-ID: 439980 [Multi-domain]  Cd Length: 721  Bit Score: 51.86  E-value: 4.27e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568976424  641 RLNAKQKEAVLAITTPLsiqlppvLII-GPyGTGKTFTLAQAAKHILQQQETS--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 5.60e-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: 5.60e-06
                           10        20
                   ....*....|....*....|....*
gi 568976424   181 YTLCKRFLEQGICRYGAQCTSAHSQ 205
Cdd:pfam00642    3 TELCRFFLRTGYCKYGDRCKFAHGQ 27
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 1.62e-05

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: 46.78  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  645 KQKEAVLAITT-PLSIqlppvlIIGPYGTGKTFTLAQAAKHIlqQQETSRILICTHSNSAADLyikdyLHpyvEAGNPQA 723
Cdd:cd17933     1 EQKAAVRLVLRnRVSV------LTGGAGTGKTTTLKALLAAL--EAEGKRVVLAAPTGKAAKR-----LS---ESTGIEA 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  724 RplrvyfrnrwvkTvhpvVHQYCLISSTQSTFQmPQKEDILKHRVVVVtlstsqylcqldlepgffthvllDEAaqAMec 803
Cdd:cd17933    65 S------------T----IHRLLGINPGGGGFY-YNEENPLDADLLIV-----------------------DEA--SM-- 100

                         170       180       190
                  ....*....|....*....|....*....|...
gi 568976424  804 etiMPLALATK-------NTRIVLAGDHMQLSP 829
Cdd:cd17933   101 ---VDTRLMAAllsaipaGARLILVGDPDQLPS 130
UvrD-helicase pfam00580
UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural ...
 642-739 2.53e-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: 2.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424   642 LNAKQKEAVLAITTPLsiqlppvLIIGPYGTGKTFTLAQAAKHILQQQETS--RILICTHSNSAAD---LYIKDYLhpyv 716
Cdd:pfam00580    1 LNPEQRKAVTHLGGPL-------LVLAGAGSGKTRVLTERIAYLILEGGIDpeEILAVTFTNKAARemkERILKLL---- 69

                           90       100
                   ....*....|....*....|...
gi 568976424   717 eaGNPQARPLrvyfrnrWVKTVH 739
Cdd:pfam00580   70 --GKAELSEL-------NISTFH 83
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 1338-1414 9.80e-05

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 44.78  E-value: 9.80e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568976424   1338 LNPRHINNLPLPAPHAQYAIPSRHfHPLPQLPRPPFPASQPHTLLNQQQNNLPEQPNQMAPQPNQVAPQPNQMTPQP 1414
Cdd:smart00818   42 VSQQHPPTHTLQPHHHIPVLPAQQ-PVVPQQPLMPVPGQHSMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQPMQPQ 117
ResIII pfam04851
Type III restriction enzyme, res subunit;
642-771 1.03e-04

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 44.59  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424   642 LNAKQKEAVLAITTPLSIQLPPVLIIGPYGTGKTFTLAQAAKHILQQQETSRILICTHSNsaaDLY------IKDYLHPY 715
Cdd:pfam04851    4 LRPYQIEAIENLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRK---DLLeqaleeFKKFLPNY 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568976424   716 VEAGNpqarPLRVYFRNRWVKTVHPVVhqyCLISSTQSTFQMPQKEDILKHRVVVV 771
Cdd:pfam04851   81 VEIGE----IISGDKKDESVDDNKIVV---TTIQSLYKALELASLELLPDFFDVII 129
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 641-829 1.42e-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: 1.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424   641 RLNAKQKEAVLAITT-PLSIQLppvlIIGPYGTGKTFTLAQAAKHIlqQQETSRILICTHSNSAADLYIKDYLHPyveag 719
Cdd:pfam13604    1 TLNAEQAAAVRALLTsGDRVAV----LVGPAGTGKTTALKALREAW--EAAGYRVIGLAPTGRAAKVLGEELGIP----- 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424   720 npqARplrvyfrnrwvkTVHPVVHQYclisstqstfqmPQKEDILKHRVVVVtlstsqylcqldlepgffthvllDEAAQ 799
Cdd:pfam13604   70 ---AD------------TIAKLLHRL------------GGRAGLDPGTLLIV-----------------------DEAGM 99

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 568976424   800 A----MEcetiMPLALATK-NTRIVLAGDHMQLSP 829
Cdd:pfam13604  100 VgtrqMA----RLLKLAEDaGARVILVGDPRQLPS 130
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 1305-1414 2.74e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 46.23  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424 1305 PKQVDLESNPQnrSPESRPGVVYSNTKFPRKDHLNPRHINNLPLPaPHAQYAIPSRHFHPLPQLPRPPFPASQPHTLLNQ 1384
Cdd:PRK10263  731 PMKALLDDGPH--EPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVA-PQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQP 807

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568976424 1385 QQnnlPEQPNQMAPQPNQ-VAPQPNQMTPQP 1414
Cdd:PRK10263  808 QQ---PVAPQPQYQQPQQpVAPQPQYQQPQQ 835
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
637-730 6.37e-04

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 44.63  E-value: 6.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  637 QLDPRLNAKQKEAVLAITTPLSIQLPPVLIIGPYGTGKTFTLAQAAKHILQQQetsRILICTHS----NSAADLyIKDYL 712
Cdd:COG1061    76 GTSFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGK---RVLVLVPRrellEQWAEE-LRRFL 151

                          90
                  ....*....|....*...
gi 568976424  713 HPYVEAGNPQARPLRVYF 730
Cdd:COG1061   152 GDPLAGGGKKDSDAPITV 169
AAA_19 pfam13245
AAA domain;
646-705 9.96e-04

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 41.43  E-value: 9.96e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568976424   646 QKEAVLAITTPlsiqlPPVLIIGPYGTGKTFTLAQAAKHILQQQETS-RILICTHSNSAAD 705
Cdd:pfam13245    1 QREAVRTALPS-----KVVLLTGGPGTGKTTTIRHIVALLVALGGVSfPILLAAPTGRAAK 56
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1273-1413 1.44e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.60  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  1273 DQQEQNRNGKTDTNNPGPEiNKIRTPEKKPTEPKQVDLESNPQNRSPESRPGVVYSNTKFPRKDHLNPRHINNLPLPAP- 1351
Cdd:pfam03154  122 DGRSVNDEGSSDPKDIDQD-NRSTSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPt 200

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568976424  1352 HAQYAIPSRHFHPLPQLPRPPFPASQPHTLLNQ------QQNNLPEQPNQMAPQPnqvaPQPNQMTPQ 1413
Cdd:pfam03154  201 PSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQtptlhpQRLPSPHPPLQPMTQP----PPPSQVSPQ 264
Tymo_45kd_70kd pfam03251
Tymovirus 45/70Kd protein; Tymoviruses are single stranded RNA viruses. This family includes a ...
 1225-1414 3.41e-03

Tymovirus 45/70Kd protein; Tymoviruses are single stranded RNA viruses. This family includes a protein of unknown function that has been named based on its molecular weight. Tymoviruses such as the ononis yellow mosaic tymovirus encode only three proteins. Of these two are overlapping this protein overlaps a larger ORF that is thought to be the polymerase.


Pssm-ID: 281269 [Multi-domain]  Cd Length: 468  Bit Score: 42.09  E-value: 3.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  1225 PRIITHQAAMAYNMNLLHTHGRGSP----IP------YGLGHHPPVSLGQPQSQHAEKDQQEQNRNGKTDTNNPGPeiNK 1294
Cdd:pfam03251  256 PRPITPGPSNTHDLRPLSVLPRTSPrrglLPnprrhrTSTGHIPPTTTSRPTGPPSRLQRPVHLYQSSPHTPNFRP--SS 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  1295 IRTPEKKPTEPKQVDLE--SNPQN-RSPESRPGvvySNTKFPRKDHlnprhINNLPLPAPHAQYAIPSRHFHPLPQLPRP 1371
Cdd:pfam03251  334 IRKDALLQTGPRLGHLErlGQPANlRTSERSPP---TKRRLPRSSE-----PNRLPKPLPEATLAPSYRHRRPYPLLPNP 405

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 568976424  1372 P--FPASQPHTLLNQQQNNLPEQ--PNQMAPQPNQVAPQPnqmTPQP 1414
Cdd:pfam03251  406 PaaLPSIAYTSSRGKIHHSLPKGalPKEGAPPPPRRLPSP---APRP 449
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1244-1416 4.21e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 4.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  1244 HGRGSPIPYglghhpPVSLGQPQSQHAEKDQQEQNRNGKTDTNNP-GPEINKIRTPEKKPTEPKqvdlesnPQNRSPESR 1322
Cdd:pfam03154  272 HGQMPPMPH------SLQTGPSHMQHPVPPQPFPLTPQSSQSQVPpGPSPAAPGQSQQRIHTPP-------SQSQLQSQQ 338

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424  1323 PgvvysntkfPRKDHLNPRhinnlPLPAPHAQyaipsrhfhPLPQLPRPPFPASQPHTLLN--------QQQNNLP---- 1390
Cdd:pfam03154  339 P---------PREQPLPPA-----PLSMPHIK---------PPPTTPIPQLPNPQSHKHPPhlsgpspfQMNSNLPpppa 395

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 568976424  1391 ---------EQPNQMAPQPNQVAPQPNQMTPQPNQ 1416
Cdd:pfam03154  396 lkplsslstHHPPSAHPPPLQLMPQSQQLPPPPAQ 430
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 1288-1414 9.30e-03

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 40.72  E-value: 9.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568976424 1288 PGPEINKIRTPEKKPTEPK---QVDLESNPQNRSP---ESRPGVVYSNTKFPRKDHLNPRHINNLPLP--APHAQYAIPS 1359
Cdd:PTZ00441  297 PTPEDDNPRPTDDEFAVPNfneGLDVPDNPQDPVPppnEGKDGNPNEENLFPPGDDEVPDESNVPPNPpnVPGGSNSEFS 376

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568976424 1360 RHFHPLPQLPRPPFPASQPHTLLNQQQNNLPEQP-NQMAPQPNQV-AP---------QPNQMTPQP 1414
Cdd:PTZ00441  377 SDVENPPNPPNPDIPEQEPNIPEDSNKEVPEDVPmEPEDDRDNNFnEPkkpenkgdgQNEPVIPKP 442
 
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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