NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1579876380|ref|NP_001355684|]
View 

probable helicase with zinc finger domain isoform 2 [Mus musculus]

Protein Classification

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 ...
 641-867 6.63e-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: 469.66  E-value: 6.63e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  641 RLNAKQKEAVLAITTPLSIQLPPVLIIGPYGTGKTFTLAQAAKHILQQQETRILICTHSNSAADLYIKDYLHPYVEAGNP 720
Cdd:cd18077      1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPETRILICTHSNSAADLYIKEYLHPYVETGNP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  721 QARPLRVYFRNRWVKTVHPVVHQYCLISStQSTFQMPQKEDILKHRVVVVTLSTSQYLCQLDLEPGFFTHVLLDEAAQAM 800
Cdd:cd18077     81 RARPLRVYYRNRWVKTVHPVVQKYCLIDE-HGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQAM 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1579876380  801 ECETIMPLALATKNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEFPCRILLCENYR 867
Cdd:cd18077    160 ECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSEHPCRILLCENYR 226
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
765-1074 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 1579876380  765 HRVVVVTLSTSQYLcqLDLEPGFFTHVLLDEAAQAMECETIMPLALATkntRIVLAGDHMQLSPFV---YSEFARERNLH 841
Cdd:COG1112    535 APVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVfgeEAEEVAEEGLD 609

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  842 VSLLDRLYEHYPaefPCRILLCENYRSHEAIINYTSELFYEGKLMA---SGKQPAHKDFYPLTFFTARGedVQEKNSTAF 918
Cdd:COG1112    610 ESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDG--VYERRGGSR 684

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  919 YNnaevfevverveelrrkwP------VAW------GKLDDGSIGVVTPYADQVFRIRAELRKKRLSDV------NVERv 980
Cdd:COG1112    685 TN------------------PeeaeavVELvrelleDGPDGESIGVITPYRAQVALIRELLREALGDGLepvfvgTVDR- 745

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  981 lnVQGKQFRVLFLSTVRTRhtckhkqtpikkkeqlleDSTEDLDYGFLS-NYKLLNTAITRAQSLVAVVGDPvALCSIGR 1059
Cdd:COG1112    746 --FQGDERDVIIFSLVYSN------------------DEDVPRNFGFLNgGPRRLNVAVSRARRKLIVVGSR-ELLDSDP 804

                          330
                   ....*....|....*
gi 1579876380 1060 CRKFWERFIALCHEN 1074
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 1579876380  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 ...
 1337-1413 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 1579876380  1337 LNPRHINNLPLPAPHAQYAIPSRHfHPLPQLPRPPFPASQPHTLLNQQQNNLPEQPNQMAPQPNQVAPQPNQMTPQP 1413
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 ...
 1224-1413 3.40e-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: 3.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380 1224 PRIITHQAAMAYNMNLLHTHGRGSP----IP------YGLGHHPPVSLGQPQSQHAEKDQQEQNRNGKTDTNNPGPeiNK 1293
Cdd:pfam03251  256 PRPITPGPSNTHDLRPLSVLPRTSPrrglLPnprrhrTSTGHIPPTTTSRPTGPPSRLQRPVHLYQSSPHTPNFRP--SS 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380 1294 IRTPEKKPTEPKQVDLE--SNPQN-RSPESRPGvvySNTKFPRKDHlnprhINNLPLPAPHAQYAIPSRHFHPLPQLPRP 1370
Cdd:pfam03251  334 IRKDALLQTGPRLGHLErlGQPANlRTSERSPP---TKRRLPRSSE-----PNRLPKPLPEATLAPSYRHRRPYPLLPNP 405

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1579876380 1371 P--FPASQPHTLLNQQQNNLPEQ--PNQMAPQPNQVAPQPnqmTPQP 1413
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 ...
 641-867 6.63e-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: 469.66  E-value: 6.63e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  641 RLNAKQKEAVLAITTPLSIQLPPVLIIGPYGTGKTFTLAQAAKHILQQQETRILICTHSNSAADLYIKDYLHPYVEAGNP 720
Cdd:cd18077      1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPETRILICTHSNSAADLYIKEYLHPYVETGNP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  721 QARPLRVYFRNRWVKTVHPVVHQYCLISStQSTFQMPQKEDILKHRVVVVTLSTSQYLCQLDLEPGFFTHVLLDEAAQAM 800
Cdd:cd18077     81 RARPLRVYYRNRWVKTVHPVVQKYCLIDE-HGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQAM 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1579876380  801 ECETIMPLALATKNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEFPCRILLCENYR 867
Cdd:cd18077    160 ECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSEHPCRILLCENYR 226
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
765-1074 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 1579876380  765 HRVVVVTLSTSQYLcqLDLEPGFFTHVLLDEAAQAMECETIMPLALATkntRIVLAGDHMQLSPFV---YSEFARERNLH 841
Cdd:COG1112    535 APVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVfgeEAEEVAEEGLD 609

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  842 VSLLDRLYEHYPaefPCRILLCENYRSHEAIINYTSELFYEGKLMA---SGKQPAHKDFYPLTFFTARGedVQEKNSTAF 918
Cdd:COG1112    610 ESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDG--VYERRGGSR 684

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  919 YNnaevfevverveelrrkwP------VAW------GKLDDGSIGVVTPYADQVFRIRAELRKKRLSDV------NVERv 980
Cdd:COG1112    685 TN------------------PeeaeavVELvrelleDGPDGESIGVITPYRAQVALIRELLREALGDGLepvfvgTVDR- 745

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  981 lnVQGKQFRVLFLSTVRTRhtckhkqtpikkkeqlleDSTEDLDYGFLS-NYKLLNTAITRAQSLVAVVGDPvALCSIGR 1059
Cdd:COG1112    746 --FQGDERDVIIFSLVYSN------------------DEDVPRNFGFLNgGPRRLNVAVSRARRKLIVVGSR-ELLDSDP 804

                          330
                   ....*....|....*
gi 1579876380 1060 CRKFWERFIALCHEN 1074
Cdd:COG1112    805 STPALKRLLEYLERA 819
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
 868-1068 5.72e-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: 5.72e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  868 SHEAIINYTSELFYEGKLMAS-------GKQPAHKDFYPLTFFTARGEDVQEKNSTAFYNNAEVFEVVERVEELRRKWpv 940
Cdd:cd18808      1 MHPEISEFPSKLFYEGKLKAGvsvaarlNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  941 awgkLDDGSIGVVTPYADQVFRIRAELRKKR--LSDVNVERVLNVQGKQFRVLFLSTVRTRHTCKHkqtpikkkeqlled 1018
Cdd:cd18808     79 ----VKPSSIGVITPYRAQVALIRELLRKRGglLEDVEVGTVDNFQGREKDVIILSLVRSNESGGS-------------- 140

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1579876380 1019 stedldYGFLSNYKLLNTAITRAQSLVAVVGDPVALCSIGRCRKFWERFI 1068
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 ...
 840-1051 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 1579876380  840 LHVSLLDRLYEHYPAefpCRILLCENYRSHEAIINYTSELFYEGKLMASGKQPAH---------KDFYPLTFF-TARGED 909
Cdd:pfam13087    1 LDRSLFERLQELGPS---AVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERplpddfhlpDPLGPLVFIdVDGSEE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  910 VQEKNSTAFYNNAEVFEVVERVEELRRKWPVAWGKlddgsIGVVTPYADQVFRIRAELRKKRLSDVNVErVLNV---QGK 986
Cdd:pfam13087   78 EESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSD-----IGVITPYRAQVRLIRKLLKRKLGGKLEIE-VNTVdgfQGR 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1579876380  987 QFRVLFLSTVRtrhtckhkqtpikkkeqlledSTEDLDYGFLSNYKLLNTAITRAQSLVAVVGDP 1051
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 ...
 652-833 2.57e-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: 80.85  E-value: 2.57e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  652 AITTPLSiQLPPVLIIGPYGTGKTFTLAQAAKHILQQQET------RILICTHSNSAAD----LYIKDYLHPYVEA---G 718
Cdd:pfam13086    5 AIRSALS-SSHFTLIQGPPGTGKTTTIVELIRQLLSYPATsaaagpRILVCAPSNAAVDnileRLLRKGQKYGPKIvriG 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  719 NPQARplrvyfrnrwvktvHPVVHQYCLISSTQSTFQMPQKEDILK---------------------------------- 764
Cdd:pfam13086   84 HPAAI--------------SEAVLPVSLDYLVESKLNNEEDAQIVKdiskeleklakalrafekeiivekllksrnkdks 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  765 ----------------------------------HRVVVVTLSTS--QYLCQLDlepGFFThVLLDEAAQAMECETIMPL 808
Cdd:pfam13086  150 kleqerrklrserkelrkelrrreqslereildeAQIVCSTLSGAgsRLLSSLA---NFDV-VIIDEAAQALEPSTLIPL 225

                          250       260
                   ....*....|....*....|....*
gi 1579876380  809 ALATKntRIVLAGDHMQLSPFVYSE 833
Cdd:pfam13086  226 LRGPK--KVVLVGDPKQLPPTVISK 248
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 632-1072 1.24e-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: 56.52  E-value: 1.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  632 RQWDEQLDPRLNAKQKEAVLAITTPLSIqlppVLIIGPYGTGKTFTLAqAAKHILQQQETRILICTHSNSAAD-LYikdy 710
Cdd:COG0507    115 AALEPRAGITLSDEQREAVALALTTRRV----SVLTGGAGTGKTTTLR-ALLAALEALGLRVALAAPTGKAAKrLS---- 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  711 lhpyvEAGNPQARplrvyfrnrwvkTVHPVVHqyclISSTQSTFQMPQKEDILKHRVVVVtlstsqylcqldlepgffth 790
Cdd:COG0507    186 -----ESTGIEAR------------TIHRLLG----LRPDSGRFRHNRDNPLTPADLLVV-------------------- 224

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  791 vllDEA--------AQAMEcetimplALATKNTRIVLAGDHMQLSP----FVYSEFARERNLHVSLLDrlyehypaefpc 858
Cdd:COG0507    225 ---DEAsmvdtrlmAALLE-------ALPRAGARLILVGDPDQLPSvgagAVLRDLIESGTVPVVELT------------ 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  859 rillcENYRSHEAI-INYTSELFYEGKlMASGKQPAHKDFYPL----------------TFFTARGEDVQ-----EKnST 916
Cdd:COG0507    283 -----EVYRQADDSrIIELAHAIREGD-APEALNARYADVVFVeaedaeeaaeaivelyADRPAGGEDIQvlaptNA-GV 355

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  917 AFYN-------NAEVFEVVERVEELRRKW----PV-------AWGkLDDGSIGVVTPYADQVFRIRAELRKKRLSDVNVE 978
Cdd:COG0507    356 DALNqairealNPAGELERELAEDGELELyvgdRVmftrndyDLG-VFNGDIGTVLSIDEDEGRLTVRFDGREIVTYDPS 434

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  979 RVLNV-----------QGKQF-RVLFLSTvrtrhtckhkqtpikkkeqlledsteDLDYGFLSNyKLLNTAITRAQSLVA 1046
Cdd:COG0507    435 ELDQLelayaitvhksQGSTFdRVILVLP--------------------------SEHSPLLSR-ELLYTALTRARELLT 487

                          490       500
                   ....*....|....*....|....*.
gi 1579876380 1047 VVGDPVALCSIgrCRKFWERFIALCH 1072
Cdd:COG0507    488 LVGDRDALARA--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 1579876380  181 YTLCKRFLEQGICRYGAQCTSAHSQ 205
Cdd:pfam00642    3 TELCRFFLRTGYCKYGDRCKFAHGQ 27
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 1337-1413 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 1579876380  1337 LNPRHINNLPLPAPHAQYAIPSRHfHPLPQLPRPPFPASQPHTLLNQQQNNLPEQPNQMAPQPNQVAPQPNQMTPQP 1413
Cdd:smart00818   42 VSQQHPPTHTLQPHHHIPVLPAQQ-PVVPQQPLMPVPGQHSMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQPMQPQ 117
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 1304-1413 2.73e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 46.23  E-value: 2.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380 1304 PKQVDLESNPQnrSPESRPGVVYSNTKFPRKDHLNPRHINNLPLPaPHAQYAIPSRHFHPLPQLPRPPFPASQPHTLLNQ 1383
Cdd:PRK10263   731 PMKALLDDGPH--EPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVA-PQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQP 807

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1579876380 1384 QQnnlPEQPNQMAPQPNQ-VAPQPNQMTPQP 1413
Cdd:PRK10263   808 QQ---PVAPQPQYQQPQQpVAPQPQYQQPQQ 835
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1272-1412 1.43e-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: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380 1272 DQQEQNRNGKTDTNNPGPEiNKIRTPEKKPTEPKQVDLESNPQNRSPESRPGVVYSNTKFPRKDHLNPRHINNLPLPAP- 1350
Cdd:pfam03154  122 DGRSVNDEGSSDPKDIDQD-NRSTSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPt 200

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1579876380 1351 HAQYAIPSRHFHPLPQLPRPPFPASQPHTLLNQ------QQNNLPEQPNQMAPQPnqvaPQPNQMTPQ 1412
Cdd:pfam03154  201 PSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQtptlhpQRLPSPHPPLQPMTQP----PPPSQVSPQ 264
Tymo_45kd_70kd pfam03251
Tymovirus 45/70Kd protein; Tymoviruses are single stranded RNA viruses. This family includes a ...
 1224-1413 3.40e-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: 3.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380 1224 PRIITHQAAMAYNMNLLHTHGRGSP----IP------YGLGHHPPVSLGQPQSQHAEKDQQEQNRNGKTDTNNPGPeiNK 1293
Cdd:pfam03251  256 PRPITPGPSNTHDLRPLSVLPRTSPrrglLPnprrhrTSTGHIPPTTTSRPTGPPSRLQRPVHLYQSSPHTPNFRP--SS 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380 1294 IRTPEKKPTEPKQVDLE--SNPQN-RSPESRPGvvySNTKFPRKDHlnprhINNLPLPAPHAQYAIPSRHFHPLPQLPRP 1370
Cdd:pfam03251  334 IRKDALLQTGPRLGHLErlGQPANlRTSERSPP---TKRRLPRSSE-----PNRLPKPLPEATLAPSYRHRRPYPLLPNP 405

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1579876380 1371 P--FPASQPHTLLNQQQNNLPEQ--PNQMAPQPNQVAPQPnqmTPQP 1413
Cdd:pfam03251  406 PaaLPSIAYTSSRGKIHHSLPKGalPKEGAPPPPRRLPSP---APRP 449
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 663-741 4.95e-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: 39.66  E-value: 4.95e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1579876380   663 PVLIIGPYGTGKTfTLAQAAKHILQQQETRILICTHSNSAADLYIKDYLHPYVEAGNPQARPLRVYFRNRWVKTVHPVV 741
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 ...
 641-867 6.63e-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: 469.66  E-value: 6.63e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  641 RLNAKQKEAVLAITTPLSIQLPPVLIIGPYGTGKTFTLAQAAKHILQQQETRILICTHSNSAADLYIKDYLHPYVEAGNP 720
Cdd:cd18077      1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPETRILICTHSNSAADLYIKEYLHPYVETGNP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  721 QARPLRVYFRNRWVKTVHPVVHQYCLISStQSTFQMPQKEDILKHRVVVVTLSTSQYLCQLDLEPGFFTHVLLDEAAQAM 800
Cdd:cd18077     81 RARPLRVYYRNRWVKTVHPVVQKYCLIDE-HGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQAM 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1579876380  801 ECETIMPLALATKNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEFPCRILLCENYR 867
Cdd:cd18077    160 ECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSEHPCRILLCENYR 226
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
 641-867 6.04e-93

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: 300.69  E-value: 6.04e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  641 RLNAKQKEAVLAITTPLSiQLPPVLIIGPYGTGKTFTLAQAAKHIL-QQQETRILICTHSNSAADLYIKDYLHPYVeagn 719
Cdd:cd18038      1 ELNDEQKLAVRNIVTGTS-RPPPYIIFGPPGTGKTVTLVEAILQVLrQPPEARILVCAPSNSAADLLAERLLNALV---- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  720 PQARPLRVYFRNRWVKTVHPVVHQYCLISStQSTFQMPQKEDILKHRVVVVTLSTSQYLCQLDLEPGFFTHVLLDEAAQA 799
Cdd:cd18038     76 TKREILRLNAPSRDRASVPPELLPYCNSKA-EGTFRLPSLEELKKYRIVVCTLMTAGRLVQAGVPNGHFTHIFIDEAGQA 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1579876380  800 MECETIMPLA-LATKNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYP------AEFPCRILLCENYR 867
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 ...
 641-867 1.70e-70

N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB, and RXRA. It belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350834 [Multi-domain]  Cd Length: 230  Bit Score: 236.33  E-value: 1.70e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  641 RLNAKQKEAVLAIT--TPLSIQLPPVLIIGPYGTGKTFTLAQAAKHILQQQETRILICTHSNSAADLYIKDYLHPYVEAG 718
Cdd:cd18076      1 AGNNKQQLAFNFIAgkPSEARFVPPLLIYGPFGTGKTFTLAMAALEVIREPGTKVLICTHTNSAADIYIREYFHPYVDKG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  719 NPQARPLRVYFRNRWVKTVHPVVHQYCLISSTQSTFQMPQKEDILKHRVVVVTLSTSQylcQLDLEPGFFTHVLLDEAAQ 798
Cdd:cd18076     81 HPEARPLRIKATDRPNAITDPDTITYCCLTKDRQCFRLPTRDELDFHNIVITTTAMAF---NLHVLSGFFTHIFIDEAAQ 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1579876380  799 AMECETIMPLALATKNTRIVLAGDHMQLSPFVYSeFARERNLHVSLLDRLYEHYPAE-----FPCRILLCENYR 867
Cdd:cd18076    158 MLECEALIPLSYAGPKTRVVLAGDHMQMTPKLFS-VADYNRANHTLLNRLFHYYQGEkhevaVKSRVIFSENYR 230
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
765-1074 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 1579876380  765 HRVVVVTLSTSQYLcqLDLEPGFFTHVLLDEAAQAMECETIMPLALATkntRIVLAGDHMQLSPFV---YSEFARERNLH 841
Cdd:COG1112    535 APVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVfgeEAEEVAEEGLD 609

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  842 VSLLDRLYEHYPaefPCRILLCENYRSHEAIINYTSELFYEGKLMA---SGKQPAHKDFYPLTFFTARGedVQEKNSTAF 918
Cdd:COG1112    610 ESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDG--VYERRGGSR 684

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  919 YNnaevfevverveelrrkwP------VAW------GKLDDGSIGVVTPYADQVFRIRAELRKKRLSDV------NVERv 980
Cdd:COG1112    685 TN------------------PeeaeavVELvrelleDGPDGESIGVITPYRAQVALIRELLREALGDGLepvfvgTVDR- 745

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  981 lnVQGKQFRVLFLSTVRTRhtckhkqtpikkkeqlleDSTEDLDYGFLS-NYKLLNTAITRAQSLVAVVGDPvALCSIGR 1059
Cdd:COG1112    746 --FQGDERDVIIFSLVYSN------------------DEDVPRNFGFLNgGPRRLNVAVSRARRKLIVVGSR-ELLDSDP 804

                          330
                   ....*....|....*
gi 1579876380 1060 CRKFWERFIALCHEN 1074
Cdd:COG1112    805 STPALKRLLEYLERA 819
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
 642-867 2.29e-40

DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. Mov10L1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350836 [Multi-domain]  Cd Length: 230  Bit Score: 149.83  E-value: 2.29e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  642 LNAKQKEAVLAITTPLSIQLPPVlIIGPYGTGKTFTLAQAakhILQQQ----ETRILICTHSNSAADLYIKDyLHPYVEA 717
Cdd:cd18078      2 LNELQKEAVKRILGGECRPLPYI-LFGPPGTGKTVTIIEA---ILQVVynlpRSRILVCAPSNSAADLVTSR-LHESKVL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  718 GNPQARPLRVYfrNRWVKTVHPVVHQYCLISStqstfqmpQKEDILKHRVVVVTLSTSQYLCQLDLEPGFFTHVLLDEAA 797
Cdd:cd18078     77 KPGDMVRLNAV--NRFESTVIDARKLYCRLGE--------DLSKASRHRIVISTCSTAGLLYQMGLPVGHFTHVFVDEAG 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  798 QAMECETIMPLALATKNT-RIVLAGDHMQLSPFVYSEFARERNLHVSLLDRL-----YEHYPAEFP-CRIL-------LC 863
Cdd:cd18078    147 QATEPESLIPLGLISSRDgQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLmnrplYLRDPNRFGeSGGYnpllvtkLV 226


                   ....
gi 1579876380  864 ENYR 867
Cdd:cd18078    227 DNYR 230
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
 868-1068 5.72e-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: 5.72e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  868 SHEAIINYTSELFYEGKLMAS-------GKQPAHKDFYPLTFFTARGEDVQEKNSTAFYNNAEVFEVVERVEELRRKWpv 940
Cdd:cd18808      1 MHPEISEFPSKLFYEGKLKAGvsvaarlNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  941 awgkLDDGSIGVVTPYADQVFRIRAELRKKR--LSDVNVERVLNVQGKQFRVLFLSTVRTRHTCKHkqtpikkkeqlled 1018
Cdd:cd18808     79 ----VKPSSIGVITPYRAQVALIRELLRKRGglLEDVEVGTVDNFQGREKDVIILSLVRSNESGGS-------------- 140

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1579876380 1019 stedldYGFLSNYKLLNTAITRAQSLVAVVGDPVALCSIGRCRKFWERFI 1068
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 ...
 840-1051 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 1579876380  840 LHVSLLDRLYEHYPAefpCRILLCENYRSHEAIINYTSELFYEGKLMASGKQPAH---------KDFYPLTFF-TARGED 909
Cdd:pfam13087    1 LDRSLFERLQELGPS---AVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERplpddfhlpDPLGPLVFIdVDGSEE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  910 VQEKNSTAFYNNAEVFEVVERVEELRRKWPVAWGKlddgsIGVVTPYADQVFRIRAELRKKRLSDVNVErVLNV---QGK 986
Cdd:pfam13087   78 EESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSD-----IGVITPYRAQVRLIRKLLKRKLGGKLEIE-VNTVdgfQGR 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1579876380  987 QFRVLFLSTVRtrhtckhkqtpikkkeqlledSTEDLDYGFLSNYKLLNTAITRAQSLVAVVGDP 1051
Cdd:pfam13087  152 EKDVIIFSCVR---------------------SNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNA 195
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
 641-853 2.78e-27

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: 111.17  E-value: 2.78e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  641 RLNAKQKEAVLAITTPLSIqlppVLIIGPYGTGKTFTLAQAAKhILQQQETRILICTHSNSAAD---LYIKDYLHPYVEA 717
Cdd:cd18041      1 GLNKDQRQAIKKVLNAKDY----ALILGMPGTGKTTTIAALVR-ILVALGKSVLLTSYTHSAVDnilLKLKKFGVNFLRL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  718 GNPqarplrvyfrnrwvKTVHPVVHQYCLISSTQSTFQMPQKEDIL-KHRVVVVT-LSTSQYLcqldLEPGFFTHVLLDE 795
Cdd:cd18041     76 GRL--------------KKIHPDVQEFTLEAILKSCKSVEELESKYeSVSVVATTcLGINHPI----FRRRTFDYCIVDE 137

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1579876380  796 AAQAMECETIMPLALATKntrIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYP 853
Cdd:cd18041    138 ASQITLPICLGPLRLAKK---FVLVGDHYQLPPLVKSREARELGMDESLFKRLSEAHP 192
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
 641-867 5.23e-26

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


Pssm-ID: 350802 [Multi-domain]  Cd Length: 191  Bit Score: 106.93  E-value: 5.23e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  641 RLNAKQKEAVLaittpLSIQLPPVLII-GPYGTGKTFTLAQAakhILQ--QQETRILICTHSNSAADLYIKDYLH---PY 714
Cdd:cd18044      1 NLNDSQKEAVK-----FALSQKDVALIhGPPGTGKTTTVVEI---ILQavKRGEKVLACAPSNIAVDNLVERLVAlkvKV 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  715 VEAGNPqARplrvyfrnrwvktVHPVVHQYCLisstqstfqmpqkEDILKHRVVVVTLSTSqylCQLDLEPG-FFTHVLL 793
Cdd:cd18044     73 VRIGHP-AR-------------LLESVLDHSL-------------DALVAAQVVLATNTGA---GSRQLLPNeLFDVVVI 122

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1579876380  794 DEAAQAMECETIMPLalaTKNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEfpCRILLCENYR 867
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 ...
 642-848 5.36e-22

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: 96.93  E-value: 5.36e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  642 LNAKQKEAV-LAITTPLSiqlppvLIIGPYGTGKTFTLAQAAKHILQQQETRILICTHSNSAADlYIKDYLHpyvEAGnp 720
Cdd:cd18039      2 LNHSQVDAVkTALQRPLS------LIQGPPGTGKTVTSATIVYHLVKQGNGPVLVCAPSNVAVD-QLTEKIH---QTG-- 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  721 qARPLRVYFRNRW-----VK--TVHPVVHQY-----------------CLISSTQSTFQM----PQKEDILKHRVVVVTL 772
Cdd:cd18039     70 -LKVVRLCAKSREavespVSflALHNQVRNLdsaeklellkllkletgELSSADEKRYRKlkrkAERELLRNADVICCTC 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1579876380  773 STSqylcqLD--LEPGFFTHVLLDEAAQAMECETIMPLALATKntRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRL 848
Cdd:cd18039    149 VGA-----GDprLSKMKFRTVLIDEATQATEPECLIPLVHGAK--QVILVGDHCQLGPVVMCKKAAKAGLSQSLFERL 219
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
 642-867 8.02e-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: 89.97  E-value: 8.02e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  642 LNAKQKEAVLAIttpLSIQLPPVLIIGPYGTGKTFTL---------------AQAAKHILQQQET---------RILICT 697
Cdd:cd18042      1 LNESQLEAIASA---LQNSPGITLIQGPPGTGKTKTIvgilsvllagkyrkyYEKVKKKLRKLQRnlnnkkkknRILVCA 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  698 HSNSAADLYIKDYLHPYVEAGNPQARPLRVyfrnrwVKTVHpvvhqyclisstqstfQMPQKEDILKHRVVVVTLSTSQY 777
Cdd:cd18042     78 PSNAAVDEIVLRLLSEGFLDGDGRSYKPNV------VRVGR----------------QELRASILNEADIVCTTLSSSGS 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  778 LcQLDLEPGFFTHVLLDEAAQAMECETIMPLALATKntRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEhypAEFP 857
Cdd:cd18042    136 D-LLESLPRGFDTVIIDEAAQAVELSTLIPLRLGCK--RLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQL---AGYP 209

                          250
                   ....*....|
gi 1579876380  858 CrILLCENYR 867
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 ...
 652-833 2.57e-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: 80.85  E-value: 2.57e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  652 AITTPLSiQLPPVLIIGPYGTGKTFTLAQAAKHILQQQET------RILICTHSNSAAD----LYIKDYLHPYVEA---G 718
Cdd:pfam13086    5 AIRSALS-SSHFTLIQGPPGTGKTTTIVELIRQLLSYPATsaaagpRILVCAPSNAAVDnileRLLRKGQKYGPKIvriG 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  719 NPQARplrvyfrnrwvktvHPVVHQYCLISSTQSTFQMPQKEDILK---------------------------------- 764
Cdd:pfam13086   84 HPAAI--------------SEAVLPVSLDYLVESKLNNEEDAQIVKdiskeleklakalrafekeiivekllksrnkdks 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  765 ----------------------------------HRVVVVTLSTS--QYLCQLDlepGFFThVLLDEAAQAMECETIMPL 808
Cdd:pfam13086  150 kleqerrklrserkelrkelrrreqslereildeAQIVCSTLSGAgsRLLSSLA---NFDV-VIIDEAAQALEPSTLIPL 225

                          250       260
                   ....*....|....*....|....*
gi 1579876380  809 ALATKntRIVLAGDHMQLSPFVYSE 833
Cdd:pfam13086  226 LRGPK--KVVLVGDPKQLPPTVISK 248
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
 641-848 4.99e-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: 74.89  E-value: 4.99e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  641 RLNAKQKEA-VLAITTPLSIqlppvlIIGPYGTGKTFTLAQAAKHILQ----QQETRILICTHSNSAADLYIKDYLhpyv 715
Cdd:cd17936      1 TLDPSQLEAlKHALTSELAL------IQGPPGTGKTFLGVKLVRALLQnqdlSITGPILVVCYTNHALDQFLEGLL---- 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  716 eagnpqarplrvyfrnrwvktvhpvvhQYClisstqstfqmpqKEDILKH--RVVVVTLSTSQYLCQL--DLEPgffTHV 791
Cdd:cd17936     71 ---------------------------DFG-------------PTKIVRLgaRVIGMTTTGAAKYRELlqALGP---KVV 107

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  792 LLDEAAQAMECETIMPLalaTKNTR-IVLAGDHMQLSPFV--YSEFARERNLHVSLLDRL 848
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, ...
 664-867 1.72e-13

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: 68.80  E-value: 1.72e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  664 VLIIGPYGTGKTFTLAQAAKHILQQQET-RILICTHSNSAADlyikdylhpyveagnpqarplrvyfrnrwvktvhpvvh 742
Cdd:cd17934      2 SLIQGPPGTGKTTTIAAIVLQLLKGLRGkRVLVTAQSNVAVD-------------------------------------- 43

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  743 qyclisstqstfqmpqkedilkhrvvvvtlstsqylcQLDlepgfftHVLLDEAAQAMECETIMPLALATKntrIVLAGD 822
Cdd:cd17934     44 -------------------------------------NVD-------VVIIDEASQITEPELLIALIRAKK---VVLVGD 76

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1579876380  823 HMQLSPFVYSEFARE--RNLHVSLLDRLYEHYPAEFPcrILLCENYR 867
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 ...
 642-850 1.60e-12

C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB and RXRA. It belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350798 [Multi-domain]  Cd Length: 271  Bit Score: 69.86  E-value: 1.60e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  642 LNAKQKEAVL-AITTPLSiqlppvLIIGPYGTGKTFTLAQAAKHILQQQETR------------ILICTHSNSAADLyIK 708
Cdd:cd18040      2 LNPSQNHAVRtALTKPFT------LIQGPPGTGKTVTGVHIAYWFAKQNREIqsvsgegdggpcVLYCGPSNKSVDV-VA 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  709 DYLhpyveAGNPQARPLRVY--------------FRNRWVK--------------TVHPVVHQ----YC-LISSTQSTFQ 755
Cdd:cd18040     75 ELL-----LKVPGLKILRVYseqietteypipnePRHPNKKsereskpnselssiTLHHRIRQpsnpHSqQIKAFEARFE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  756 MPQ----KEDILKHRVVV------------VTLSTsqylCQLDLEPGFFTH-----VLLDEAAQAMECETIMPLALATKN 814
Cdd:cd18040    150 RTQekitEEDIKTYKILIwearfeeletvdVILCT----CSEAASQKMRTHanvkqCIVDECGMCTEPESLIPIVSAPRA 225

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1579876380  815 TRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYE 850
Cdd:cd18040    226 EQVVLIGDHKQLRPVVQNKEAQKLGLGRSLFERYAE 261
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
 641-848 1.82e-09

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


Pssm-ID: 350693 [Multi-domain]  Cd Length: 207  Bit Score: 59.75  E-value: 1.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  641 RLNAKQKEAVLAITTP-LSiqlppvLIIGPYGTGKTFTLAQAAKHILQQ-QETRILICTHSNSAA-DLYIKDYlhpyvEA 717
Cdd:cd17935      5 KFTPTQIEAIRSGMQPgLT------MVVGPPGTGKTDVAVQIISNLYHNfPNQRTLIVTHSNQALnQLFEKIM-----AL 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  718 GNPQARPLRvyfrnrwvktvhpvvhqyclisstqstfqmpqkediLKH--RVVVVTlSTSQYLCQLDL-EPGF-FTHVLL 793
Cdd:cd17935     74 DIDERHLLR------------------------------------LGHgaKIIAMT-CTHAALKRGELvELGFkYDNILM 116

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1579876380  794 DEAAQAMECETIMPLALATKNT------RIVLAGDHMQLSPFVYS-EFARERNLHVSLLDRL 848
Cdd:cd17935    117 EEAAQILEIETFIPLLLQNPEDgpnrlkRLIMIGDHHQLPPVIKNmAFQKYSNMEQSLFTRL 178
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 632-1072 1.24e-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: 56.52  E-value: 1.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  632 RQWDEQLDPRLNAKQKEAVLAITTPLSIqlppVLIIGPYGTGKTFTLAqAAKHILQQQETRILICTHSNSAAD-LYikdy 710
Cdd:COG0507    115 AALEPRAGITLSDEQREAVALALTTRRV----SVLTGGAGTGKTTTLR-ALLAALEALGLRVALAAPTGKAAKrLS---- 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  711 lhpyvEAGNPQARplrvyfrnrwvkTVHPVVHqyclISSTQSTFQMPQKEDILKHRVVVVtlstsqylcqldlepgffth 790
Cdd:COG0507    186 -----ESTGIEAR------------TIHRLLG----LRPDSGRFRHNRDNPLTPADLLVV-------------------- 224

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  791 vllDEA--------AQAMEcetimplALATKNTRIVLAGDHMQLSP----FVYSEFARERNLHVSLLDrlyehypaefpc 858
Cdd:COG0507    225 ---DEAsmvdtrlmAALLE-------ALPRAGARLILVGDPDQLPSvgagAVLRDLIESGTVPVVELT------------ 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  859 rillcENYRSHEAI-INYTSELFYEGKlMASGKQPAHKDFYPL----------------TFFTARGEDVQ-----EKnST 916
Cdd:COG0507    283 -----EVYRQADDSrIIELAHAIREGD-APEALNARYADVVFVeaedaeeaaeaivelyADRPAGGEDIQvlaptNA-GV 355

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  917 AFYN-------NAEVFEVVERVEELRRKW----PV-------AWGkLDDGSIGVVTPYADQVFRIRAELRKKRLSDVNVE 978
Cdd:COG0507    356 DALNqairealNPAGELERELAEDGELELyvgdRVmftrndyDLG-VFNGDIGTVLSIDEDEGRLTVRFDGREIVTYDPS 434

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  979 RVLNV-----------QGKQF-RVLFLSTvrtrhtckhkqtpikkkeqlledsteDLDYGFLSNyKLLNTAITRAQSLVA 1046
Cdd:COG0507    435 ELDQLelayaitvhksQGSTFdRVILVLP--------------------------SEHSPLLSR-ELLYTALTRARELLT 487

                          490       500
                   ....*....|....*....|....*.
gi 1579876380 1047 VVGDPVALCSIgrCRKFWERFIALCH 1072
Cdd:COG0507    488 LVGDRDALARA--VRRDTARATGLAE 511
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
 643-831 2.04e-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: 51.81  E-value: 2.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  643 NAKQKEAVLAIttplsIQLPPVLIIGPYGTGKTFTLAQAAKHILQQQEtRILICTHSNSAADlyikdylhpyveagnpqa 722
Cdd:cd18043      1 DSSQEAAIISA-----RNGKNVVIQGPPGTGKSQTIANIIANALARGK-RVLFVSEKKAALD------------------ 56

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  723 rplrvyfrnrwvktvhpVVHQYCLISSTQSTFQMpqkedilkhrvvvvtlstsqylcqLDLEPGFFTHVLLDEAAQAMEC 802
Cdd:cd18043     57 -----------------VVRFPCWIMSPLSVSQY------------------------LPLNRNLFDLVIFDEASQIPIE 95

                          170       180
                   ....*....|....*....|....*....
gi 1579876380  803 ETImPLALATKntRIVLAGDHMQLSPFVY 831
Cdd:cd18043     96 EAL-PALFRGK--QVVVVGDDKQLPPSIL 121
DEXQc_UvrD cd17932
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch ...
 643-866 1.34e-06

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: 50.59  E-value: 1.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  643 NAKQKEAVLAITTPLsiqlppvLII-GPyGTGKTFTLAQAAKHILQQQET---RILICTHSNSAADlYIKDYLHPYVeaG 718
Cdd:cd17932      1 NPEQREAVTHPDGPL-------LVLaGA-GSGKTRVLTHRIAYLILEGGVppeRILAVTFTNKAAK-EMRERLRKLL--G 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  719 NPQARPLrvyfrnrWVKTVHPVvhqyCL-ISSTQSTFqmpqkEDILkHRVVVVtLSTSQYLCQLDLEPgfFTHVLLDEA- 796
Cdd:cd17932     70 EQLASGV-------WIGTFHSF----ALrILRRYGDF-----DDLL-LYALEL-LEENPDVREKLQSR--FRYILVDEYq 129

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1579876380  797 ----AQamecETIMpLALATKNTRIVLAGDHMQlSpfVYSeFareRNLHVSLLDRLYEHYPAefPCRILLCENY 866
Cdd:cd17932    130 dtnpLQ----YELL-KLLAGDGKNLFVVGDDDQ-S--IYG-F---RGADPENILDFEKDFPD--AKVIKLEENY 189
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
 645-828 2.81e-06

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


Pssm-ID: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 49.09  E-value: 2.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  645 KQKEAVLAITT-PLSIqlppvlIIGPYGTGKTFTLAQAAKhILQQQETRILICTHSNSAADLyikdyLHpyvEAGNPQAR 723
Cdd:cd17933      1 EQKAAVRLVLRnRVSV------LTGGAGTGKTTTLKALLA-ALEAEGKRVVLAAPTGKAAKR-----LS---ESTGIEAS 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  724 plrvyfrnrwvkTvhpvVHQYCLISSTQSTFQmPQKEDILKHRVVVVtlstsqylcqldlepgffthvllDEAaqAMece 803
Cdd:cd17933     66 ------------T----IHRLLGINPGGGGFY-YNEENPLDADLLIV-----------------------DEA--SM--- 100

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1579876380  804 tiMPLALATK-------NTRIVLAGDHMQLSP 828
Cdd:cd17933    101 --VDTRLMAAllsaipaGARLILVGDPDQLPS 130
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
 663-704 5.01e-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: 47.48  E-value: 5.01e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1579876380  663 PVLIIGPYGTGKTFTLAQAAKHILQQ---QETRILICTHSNSAAD 704
Cdd:cd17914      1 LSLIQGPPGTGKTRVLVKIVAALMQNkngEPGRILLVTPTNKAAA 45
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 1579876380  181 YTLCKRFLEQGICRYGAQCTSAHSQ 205
Cdd:pfam00642    3 TELCRFFLRTGYCKYGDRCKFAHGQ 27
UvrD COG0210
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
641-703 1.10e-05

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


Pssm-ID: 439980 [Multi-domain]  Cd Length: 721  Bit Score: 50.70  E-value: 1.10e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1579876380  641 RLNAKQKEAVLAITTPLsiqlppvLII-GPyGTGKTFTLAQAAKHILQQQET---RILICTHSNSAA 703
Cdd:COG0210      6 GLNPEQRAAVEHPEGPL-------LVLaGA-GSGKTRVLTHRIAYLIAEGGVdpeQILAVTFTNKAA 64
UvrD-helicase pfam00580
UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural ...
 642-738 6.15e-05

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


Pssm-ID: 395462 [Multi-domain]  Cd Length: 267  Bit Score: 46.85  E-value: 6.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  642 LNAKQKEAVLAITTPLsiqlppvLIIGPYGTGKTFTLAQAAKHILQQ---QETRILICTHSNSAAD---LYIKDYLhpyv 715
Cdd:pfam00580    1 LNPEQRKAVTHLGGPL-------LVLAGAGSGKTRVLTERIAYLILEggiDPEEILAVTFTNKAARemkERILKLL---- 69

                           90       100
                   ....*....|....*....|...
gi 1579876380  716 eaGNPQARPLrvyfrnrWVKTVH 738
Cdd:pfam00580   70 --GKAELSEL-------NISTFH 83
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 1337-1413 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 1579876380  1337 LNPRHINNLPLPAPHAQYAIPSRHfHPLPQLPRPPFPASQPHTLLNQQQNNLPEQPNQMAPQPNQVAPQPNQMTPQP 1413
Cdd:smart00818   42 VSQQHPPTHTLQPHHHIPVLPAQQ-PVVPQQPLMPVPGQHSMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQPMQPQ 117
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 641-828 9.97e-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: 45.25  E-value: 9.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  641 RLNAKQKEAVLAITT-PLSIQLppvlIIGPYGTGKTFTLAqAAKHILQQQETRILICTHSNSAADLYIKDYLHPyveagn 719
Cdd:pfam13604    1 TLNAEQAAAVRALLTsGDRVAV----LVGPAGTGKTTALK-ALREAWEAAGYRVIGLAPTGRAAKVLGEELGIP------ 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  720 pqARplrvyfrnrwvkTVHPVVHQYclisstqstfqmPQKEDILKHRVVVVtlstsqylcqldlepgffthvllDEAAQA 799
Cdd:pfam13604   70 --AD------------TIAKLLHRL------------GGRAGLDPGTLLIV-----------------------DEAGMV 100

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1579876380  800 ----MEcetiMPLALATK-NTRIVLAGDHMQLSP 828
Cdd:pfam13604  101 gtrqMA----RLLKLAEDaGARVILVGDPRQLPS 130
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 1304-1413 2.73e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 46.23  E-value: 2.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380 1304 PKQVDLESNPQnrSPESRPGVVYSNTKFPRKDHLNPRHINNLPLPaPHAQYAIPSRHFHPLPQLPRPPFPASQPHTLLNQ 1383
Cdd:PRK10263   731 PMKALLDDGPH--EPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVA-PQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQP 807

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1579876380 1384 QQnnlPEQPNQMAPQPNQ-VAPQPNQMTPQP 1413
Cdd:PRK10263   808 QQ---PVAPQPQYQQPQQpVAPQPQYQQPQQ 835
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
637-729 4.85e-04

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 45.02  E-value: 4.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  637 QLDPRLNAKQKEAVLAITTPLSIQLPPVLIIGPYGTGKTFTLAQAAKHILQQQetRILICTHS----NSAADLyIKDYLH 712
Cdd:COG1061     76 GTSFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGK--RVLVLVPRrellEQWAEE-LRRFLG 152

                           90
                   ....*....|....*..
gi 1579876380  713 PYVEAGNPQARPLRVYF 729
Cdd:COG1061    153 DPLAGGGKKDSDAPITV 169
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1272-1412 1.43e-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: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380 1272 DQQEQNRNGKTDTNNPGPEiNKIRTPEKKPTEPKQVDLESNPQNRSPESRPGVVYSNTKFPRKDHLNPRHINNLPLPAP- 1350
Cdd:pfam03154  122 DGRSVNDEGSSDPKDIDQD-NRSTSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPt 200

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1579876380 1351 HAQYAIPSRHFHPLPQLPRPPFPASQPHTLLNQ------QQNNLPEQPNQMAPQPnqvaPQPNQMTPQ 1412
Cdd:pfam03154  201 PSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQtptlhpQRLPSPHPPLQPMTQP----PPPSQVSPQ 264
ResIII pfam04851
Type III restriction enzyme, res subunit;
642-770 1.46e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 41.50  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380  642 LNAKQKEAVLAITTPLSIQLPPVLIIGPYGTGKTFTLAQAAKHILQQQ-ETRILICTHSNsaaDLY------IKDYLHPY 714
Cdd:pfam04851    4 LRPYQIEAIENLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGpIKKVLFLVPRK---DLLeqaleeFKKFLPNY 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1579876380  715 VEAGNpqarPLRVYFRNRWVKTVHPVVhqyCLISSTQSTFQMPQKEDILKHRVVVV 770
Cdd:pfam04851   81 VEIGE----IISGDKKDESVDDNKIVV---TTIQSLYKALELASLELLPDFFDVII 129
AAA_19 pfam13245
AAA domain;
646-704 2.62e-03

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 39.89  E-value: 2.62e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1579876380  646 QKEAVLAITTPlsiqlPPVLIIGPYGTGKTFTLAQAAKHILQQQET--RILICTHSNSAAD 704
Cdd:pfam13245    1 QREAVRTALPS-----KVVLLTGGPGTGKTTTIRHIVALLVALGGVsfPILLAAPTGRAAK 56
Tymo_45kd_70kd pfam03251
Tymovirus 45/70Kd protein; Tymoviruses are single stranded RNA viruses. This family includes a ...
 1224-1413 3.40e-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: 3.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380 1224 PRIITHQAAMAYNMNLLHTHGRGSP----IP------YGLGHHPPVSLGQPQSQHAEKDQQEQNRNGKTDTNNPGPeiNK 1293
Cdd:pfam03251  256 PRPITPGPSNTHDLRPLSVLPRTSPrrglLPnprrhrTSTGHIPPTTTSRPTGPPSRLQRPVHLYQSSPHTPNFRP--SS 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380 1294 IRTPEKKPTEPKQVDLE--SNPQN-RSPESRPGvvySNTKFPRKDHlnprhINNLPLPAPHAQYAIPSRHFHPLPQLPRP 1370
Cdd:pfam03251  334 IRKDALLQTGPRLGHLErlGQPANlRTSERSPP---TKRRLPRSSE-----PNRLPKPLPEATLAPSYRHRRPYPLLPNP 405

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1579876380 1371 P--FPASQPHTLLNQQQNNLPEQ--PNQMAPQPNQVAPQPnqmTPQP 1413
Cdd:pfam03251  406 PaaLPSIAYTSSRGKIHHSLPKGalPKEGAPPPPRRLPSP---APRP 449
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1243-1415 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 1579876380 1243 HGRGSPIPYglghhpPVSLGQPQSQHAEKDQQEQNRNGKTDTNNP-GPEINKIRTPEKKPTEPKqvdlesnPQNRSPESR 1321
Cdd:pfam03154  272 HGQMPPMPH------SLQTGPSHMQHPVPPQPFPLTPQSSQSQVPpGPSPAAPGQSQQRIHTPP-------SQSQLQSQQ 338

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579876380 1322 PgvvysntkfPRKDHLNPRhinnlPLPAPHAQyaipsrhfhPLPQLPRPPFPASQPHTLLN--------QQQNNLP---- 1389
Cdd:pfam03154  339 P---------PREQPLPPA-----PLSMPHIK---------PPPTTPIPQLPNPQSHKHPPhlsgpspfQMNSNLPpppa 395

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1579876380 1390 ---------EQPNQMAPQPNQVAPQPNQMTPQPNQ 1415
Cdd:pfam03154  396 lkplsslstHHPPSAHPPPLQLMPQSQQLPPPPAQ 430
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 663-741 4.95e-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: 39.66  E-value: 4.95e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1579876380   663 PVLIIGPYGTGKTfTLAQAAKHILQQQETRILICTHSNSAADLYIKDYLHPYVEAGNPQARPLRVYFRNRWVKTVHPVV 741
Cdd:smart00382    4 VILIVGPPGSGKT-TLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDV 81
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 1287-1413 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 1579876380 1287 PGPEINKIRTPEKKPTEPK---QVDLESNPQNRSP---ESRPGVVYSNTKFPRKDHLNPRHINNLPLP--APHAQYAIPS 1358
Cdd:PTZ00441   297 PTPEDDNPRPTDDEFAVPNfneGLDVPDNPQDPVPppnEGKDGNPNEENLFPPGDDEVPDESNVPPNPpnVPGGSNSEFS 376

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1579876380 1359 RHFHPLPQLPRPPFPASQPHTLLNQQQNNLPEQP-NQMAPQPNQV-AP---------QPNQMTPQP 1413
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH