NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|672069624|ref|XP_008766536|]
View 

probable helicase with zinc finger domain isoform X1 [Rattus norvegicus]

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 ...
658-885 3.26e-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: 3.26e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  658 RLNAKQKEAVLAITTPLCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETsRILICTHSNSAADLYIKDYLHPYVEAGN 737
Cdd:cd18077     1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPET-RILICTHSNSAADLYIKEYLHPYVETGN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  738 AQARPLRVYFRNRWVKTVHPVVHQYCLISsAHSTFQMPQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQA 817
Cdd:cd18077    80 PRARPLRVYYRNRWVKTVHPVVQKYCLID-EHGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQA 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672069624  818 MECETIMPLALATKNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEFPCRILLCENYR 885
Cdd:cd18077   159 MECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSEHPCRILLCENYR 226
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
783-1092 9.32e-42

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


:

Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 167.23  E-value: 9.32e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  783 HRVVVVTLNTSQYLcqLDLEPGFFTHILLDEAAQAMECETIMPLALATkntRIVLAGDHMQLSPFV---YSEFARERNLH 859
Cdd:COG1112   535 APVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVfgeEAEEVAEEGLD 609
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  860 VSLLDRLYEHYPaefPCRILLCENYRSHEAIINYTSELFYEGKLMA---SGKQPAHKDFYPLTFFTARGedVQEKNSTAF 936
Cdd:COG1112   610 ESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDG--VYERRGGSR 684
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  937 YNnaevfevverveelrrkwP------VAW------GKLDDGSIGVVTPYADQVFRIRAELRKKRLSDV------NVERv 998
Cdd:COG1112   685 TN------------------PeeaeavVELvrelleDGPDGESIGVITPYRAQVALIRELLREALGDGLepvfvgTVDR- 745
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  999 lnVQGKQFRVLFLSTVRTRhtckhkqtpikkkeqlleDSTEDLDYGFLS-NYKLLNTAITRAQSLVAVVGDPvALCSIGR 1077
Cdd:COG1112   746 --FQGDERDVIIFSLVYSN------------------DEDVPRNFGFLNgGPRRLNVAVSRARRKLIVVGSR-ELLDSDP 804
                         330
                  ....*....|....*
gi 672069624 1078 CRKFWERFIALCHEN 1092
Cdd:COG1112   805 STPALKRLLEYLERA 819
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
181-205 6.87e-06

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


:

Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 44.11  E-value: 6.87e-06
                           10        20
                   ....*....|....*....|....*
gi 672069624   181 YTLCKRFLEQGICRYGAQCTSAHSQ 205
Cdd:pfam00642    3 TELCRFFLRTGYCKYGDRCKFAHGQ 27
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
1336-1430 8.85e-05

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 47.77  E-value: 8.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624 1336 PESRPGVVYSNTKFPRKDNLNPRHINLPLPAPHTQYAIPSRHFHPLPQLPRPPFPISQQHTLLNQQQnnlPEQPNQMTPQ 1415
Cdd:PRK10263  743 PLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQ---PVAPQPQYQQ 819
                          90
                  ....*....|....*.
gi 672069624 1416 PNQ-VAPQPNQMAPQP 1430
Cdd:PRK10263  820 PQQpVAPQPQYQQPQQ 835
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1261-1536 5.65e-04

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.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.14  E-value: 5.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  1261 HGRGSPIPYglghhpPVNLGQPQNQHAEKDQQEQNRNGKTDTNNP-GPEINKIRTPEKKPTEPKqidlesnPQNRSPESR 1339
Cdd:pfam03154  272 HGQMPPMPH------SLQTGPSHMQHPVPPQPFPLTPQSSQSQVPpGPSPAAPGQSQQRIHTPP-------SQSQLQSQQ 338
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  1340 PgvvysntkfPRKDNLNPRhinlPLPAPHTQyaipsrhfhPLPQLPRPPFPISQQHTLLN--------QQQNNLPEQP-- 1409
Cdd:pfam03154  339 P---------PREQPLPPA----PLSMPHIK---------PPPTTPIPQLPNPQSHKHPPhlsgpspfQMNSNLPPPPal 396
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  1410 ----NQMTPQPNQVAPQPNQMAPQPNQMAPQPNQVVQQQNQAPPQAPQPAPQLSPAFQAGPTNAFFnnavahrPQSP--- 1482
Cdd:pfam03154  397 kplsSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPF-------PQHPfvp 469
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 672069624  1483 -AAEAVGPEQQVPPGLSDGHSPLRAITQPGPILASPLNNFVDESSPGLPI-EEALD 1536
Cdd:pfam03154  470 gGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIkEEALD 525
 
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 ...
658-885 3.26e-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: 3.26e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  658 RLNAKQKEAVLAITTPLCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETsRILICTHSNSAADLYIKDYLHPYVEAGN 737
Cdd:cd18077     1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPET-RILICTHSNSAADLYIKEYLHPYVETGN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  738 AQARPLRVYFRNRWVKTVHPVVHQYCLISsAHSTFQMPQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQA 817
Cdd:cd18077    80 PRARPLRVYYRNRWVKTVHPVVQKYCLID-EHGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQA 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672069624  818 MECETIMPLALATKNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEFPCRILLCENYR 885
Cdd:cd18077   159 MECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSEHPCRILLCENYR 226
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
783-1092 9.32e-42

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 167.23  E-value: 9.32e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  783 HRVVVVTLNTSQYLcqLDLEPGFFTHILLDEAAQAMECETIMPLALATkntRIVLAGDHMQLSPFV---YSEFARERNLH 859
Cdd:COG1112   535 APVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVfgeEAEEVAEEGLD 609
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  860 VSLLDRLYEHYPaefPCRILLCENYRSHEAIINYTSELFYEGKLMA---SGKQPAHKDFYPLTFFTARGedVQEKNSTAF 936
Cdd:COG1112   610 ESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDG--VYERRGGSR 684
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  937 YNnaevfevverveelrrkwP------VAW------GKLDDGSIGVVTPYADQVFRIRAELRKKRLSDV------NVERv 998
Cdd:COG1112   685 TN------------------PeeaeavVELvrelleDGPDGESIGVITPYRAQVALIRELLREALGDGLepvfvgTVDR- 745
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  999 lnVQGKQFRVLFLSTVRTRhtckhkqtpikkkeqlleDSTEDLDYGFLS-NYKLLNTAITRAQSLVAVVGDPvALCSIGR 1077
Cdd:COG1112   746 --FQGDERDVIIFSLVYSN------------------DEDVPRNFGFLNgGPRRLNVAVSRARRKLIVVGSR-ELLDSDP 804
                         330
                  ....*....|....*
gi 672069624 1078 CRKFWERFIALCHEN 1092
Cdd:COG1112   805 STPALKRLLEYLERA 819
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
886-1086 6.29e-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: 6.29e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  886 SHEAIINYTSELFYEGKLMAS-------GKQPAHKDFYPLTFFTARGEDVQEKNSTAFYNNAEVFEVVERVEELRRKWpv 958
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGvsvaarlNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  959 awgkLDDGSIGVVTPYADQVFRIRAELRKKR--LSDVNVERVLNVQGKQFRVLFLSTVRTRHTCKHkqtpikkkeqlled 1036
Cdd:cd18808    79 ----VKPSSIGVITPYRAQVALIRELLRKRGglLEDVEVGTVDNFQGREKDVIILSLVRSNESGGS-------------- 140
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 672069624 1037 stedldYGFLSNYKLLNTAITRAQSLVAVVGDPVALCSIGRCRKFWERFI 1086
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 ...
858-1069 4.88e-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: 133.06  E-value: 4.88e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624   858 LHVSLLDRLYEHYPAefpCRILLCENYRSHEAIINYTSELFYEGKLMASGKQPAH---------KDFYPLTFF-TARGED 927
Cdd:pfam13087    1 LDRSLFERLQELGPS---AVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERplpddfhlpDPLGPLVFIdVDGSEE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624   928 VQEKNSTAFYNNAEVFEVVERVEELRRKWPVAWGKlddgsIGVVTPYADQVFRIRAELRKKRLSDVNVErVLNV---QGK 1004
Cdd:pfam13087   78 EESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSD-----IGVITPYRAQVRLIRKLLKRKLGGKLEIE-VNTVdgfQGR 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672069624  1005 QFRVLFLSTVRtrhtckhkqtpikkkeqlledSTEDLDYGFLSNYKLLNTAITRAQSLVAVVGDP 1069
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 ...
663-851 3.28e-15

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: 77.38  E-value: 3.28e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624   663 QKEAVLAIttplCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETS-----RILICTHSNSAAD----LYIKDYLHPyv 733
Cdd:pfam13086    2 QREAIRSA----LSSSHFTLIQGPPGTGKTTTIVELIRQLLSYPATSaaagpRILVCAPSNAAVDnileRLLRKGQKY-- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624   734 eagnaQARPLRVYFRnrwvKTVHPVVHQYCLISSAHSTFQMPQKEDILK------------------------------- 782
Cdd:pfam13086   76 -----GPKIVRIGHP----AAISEAVLPVSLDYLVESKLNNEEDAQIVKdiskeleklakalrafekeiivekllksrnk 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624   783 -------------------------------------HRVVVVTLNTS--QYLCQLDlepGFFThILLDEAAQAMECETI 823
Cdd:pfam13086  147 dkskleqerrklrserkelrkelrrreqslereildeAQIVCSTLSGAgsRLLSSLA---NFDV-VIIDEAAQALEPSTL 222
                          250       260
                   ....*....|....*....|....*...
gi 672069624   824 MPLALATKntRIVLAGDHMQLSPFVYSE 851
Cdd:pfam13086  223 IPLLRGPK--KVVLVGDPKQLPPTVISK 248
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
649-1090 4.79e-07

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 54.60  E-value: 4.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  649 RQWDEQLDPRLNAKQKEAV--LAITTPLCIqlppvlIIGPYGTGKTFTLAQAVKHILQQQEtsRILICTHSNSAAD-LYi 725
Cdd:COG0507   115 AALEPRAGITLSDEQREAValALTTRRVSV------LTGGAGTGKTTTLRALLAALEALGL--RVALAAPTGKAAKrLS- 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  726 kdylhpyvEAGNAQARplrvyfrnrwvkTVHPVVHqyclISSAHSTFQMPQKEDILKHRVVVVtlntsqylcqldlepgf 805
Cdd:COG0507   186 --------ESTGIEAR------------TIHRLLG----LRPDSGRFRHNRDNPLTPADLLVV----------------- 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  806 fthillDEA--------AQAMEcetimplALATKNTRIVLAGDHMQLSP----FVYSEFARERNLHVSLLDrlyehypae 873
Cdd:COG0507   225 ------DEAsmvdtrlmAALLE-------ALPRAGARLILVGDPDQLPSvgagAVLRDLIESGTVPVVELT--------- 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  874 fpcrillcENYRSHEAI-INYTSELFYEGKlMASGKQPAHKDFYPL----------------TFFTARGEDVQ-----EK 931
Cdd:COG0507   283 --------EVYRQADDSrIIELAHAIREGD-APEALNARYADVVFVeaedaeeaaeaivelyADRPAGGEDIQvlaptNA 353
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  932 nSTAFYN-------NAEVFEVVERVEELRRKW----PV-------AWGkLDDGSIGVVTPYADQVFRIRAELRKKRLSDV 993
Cdd:COG0507   354 -GVDALNqairealNPAGELERELAEDGELELyvgdRVmftrndyDLG-VFNGDIGTVLSIDEDEGRLTVRFDGREIVTY 431
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  994 NVERVLNV-----------QGKQF-RVLFLSTvrtrhtckhkqtpikkkeqlledsteDLDYGFLSNyKLLNTAITRAQS 1061
Cdd:COG0507   432 DPSELDQLelayaitvhksQGSTFdRVILVLP--------------------------SEHSPLLSR-ELLYTALTRARE 484
                         490       500
                  ....*....|....*....|....*....
gi 672069624 1062 LVAVVGDPVALCSIgrCRKFWERFIALCH 1090
Cdd:COG0507   485 LLTLVGDRDALARA--VRRDTARATGLAE 511
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
181-205 6.87e-06

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


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 44.11  E-value: 6.87e-06
                           10        20
                   ....*....|....*....|....*
gi 672069624   181 YTLCKRFLEQGICRYGAQCTSAHSQ 205
Cdd:pfam00642    3 TELCRFFLRTGYCKYGDRCKFAHGQ 27
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1336-1430 8.85e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 47.77  E-value: 8.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624 1336 PESRPGVVYSNTKFPRKDNLNPRHINLPLPAPHTQYAIPSRHFHPLPQLPRPPFPISQQHTLLNQQQnnlPEQPNQMTPQ 1415
Cdd:PRK10263  743 PLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQ---PVAPQPQYQQ 819
                          90
                  ....*....|....*.
gi 672069624 1416 PNQ-VAPQPNQMAPQP 1430
Cdd:PRK10263  820 PQQpVAPQPQYQQPQQ 835
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1261-1536 5.65e-04

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: 45.14  E-value: 5.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  1261 HGRGSPIPYglghhpPVNLGQPQNQHAEKDQQEQNRNGKTDTNNP-GPEINKIRTPEKKPTEPKqidlesnPQNRSPESR 1339
Cdd:pfam03154  272 HGQMPPMPH------SLQTGPSHMQHPVPPQPFPLTPQSSQSQVPpGPSPAAPGQSQQRIHTPP-------SQSQLQSQQ 338
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  1340 PgvvysntkfPRKDNLNPRhinlPLPAPHTQyaipsrhfhPLPQLPRPPFPISQQHTLLN--------QQQNNLPEQP-- 1409
Cdd:pfam03154  339 P---------PREQPLPPA----PLSMPHIK---------PPPTTPIPQLPNPQSHKHPPhlsgpspfQMNSNLPPPPal 396
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  1410 ----NQMTPQPNQVAPQPNQMAPQPNQMAPQPNQVVQQQNQAPPQAPQPAPQLSPAFQAGPTNAFFnnavahrPQSP--- 1482
Cdd:pfam03154  397 kplsSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPF-------PQHPfvp 469
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 672069624  1483 -AAEAVGPEQQVPPGLSDGHSPLRAITQPGPILASPLNNFVDESSPGLPI-EEALD 1536
Cdd:pfam03154  470 gGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIkEEALD 525
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
1348-1433 3.62e-03

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: 40.16  E-value: 3.62e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624   1348 KFPRKDNLNPRHINLPLPAPHTqyAIPSRHFHP-LPQLPRPPFpisqqhtllnQQQNNLPEQPNQMTPQPNQVAPQPNQM 1426
Cdd:smart00818   60 VLPAQQPVVPQQPLMPVPGQHS--MTPTQHHQPnLPQPAQQPF----------QPQPLQPPQPQQPMQPQPPVHPIPPLP 127

                    ....*..
gi 672069624   1427 APQPNQM 1433
Cdd:smart00818  128 PQPPLPP 134
dnaA PRK14086
chromosomal replication initiator protein DnaA;
1314-1517 6.19e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 41.35  E-value: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624 1314 TPEKKPTEPKQIDLESNPQNRSPESRPGVVYSNTKFPRKDNLNPRHINLPLPAPhtqyAIPSRHFHPLP-QLPRPPFPIS 1392
Cdd:PRK14086   91 SAGEPAPPPPHARRTSEPELPRPGRRPYEGYGGPRADDRPPGLPRQDQLPTARP----AYPAYQQRPEPgAWPRAADDYG 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624 1393 QQHTLLNQQQNNLPEQPNQMTPQPNQVAPQPNQMAPQPNQMAPQPNQvvqqqnqappqapqpapqlsPAFQAGPTNAFFN 1472
Cdd:PRK14086  167 WQQQRLGFPPRAPYASPASYAPEQERDREPYDAGRPEYDQRRRDYDH--------------------PRPDWDRPRRDRT 226
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 672069624 1473 NavahRPQ-SPAAEAVGPEQQVPPGLSDGHSPLRAITQPGPILASP 1517
Cdd:PRK14086  227 D----RPEpPPGAGHVHRGGPGPPERDDAPVVPIRPSAPGPLAAQP 268
 
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 ...
658-885 3.26e-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: 3.26e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  658 RLNAKQKEAVLAITTPLCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETsRILICTHSNSAADLYIKDYLHPYVEAGN 737
Cdd:cd18077     1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPET-RILICTHSNSAADLYIKEYLHPYVETGN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  738 AQARPLRVYFRNRWVKTVHPVVHQYCLISsAHSTFQMPQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQA 817
Cdd:cd18077    80 PRARPLRVYYRNRWVKTVHPVVQKYCLID-EHGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQA 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672069624  818 MECETIMPLALATKNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEFPCRILLCENYR 885
Cdd:cd18077   159 MECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSEHPCRILLCENYR 226
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
658-885 1.03e-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: 305.70  E-value: 1.03e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  658 RLNAKQKEAVLAITTPLCiQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETSRILICTHSNSAADLYIKDYLHPYVEagn 737
Cdd:cd18038     1 ELNDEQKLAVRNIVTGTS-RPPPYIIFGPPGTGKTVTLVEAILQVLRQPPEARILVCAPSNSAADLLAERLLNALVT--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  738 aQARPLRVYFRNRWVKTVHPVVHQYClISSAHSTFQMPQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQA 817
Cdd:cd18038    77 -KREILRLNAPSRDRASVPPELLPYC-NSKAEGTFRLPSLEELKKYRIVVCTLMTAGRLVQAGVPNGHFTHIFIDEAGQA 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672069624  818 MECETIMPLA-LATKNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYP------AEFPCRILLCENYR 885
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 ...
658-885 3.75e-66

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: 224.00  E-value: 3.75e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  658 RLNAKQKEAVLAIT--TPLCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETsRILICTHSNSAADLYIKDYLHPYVEA 735
Cdd:cd18076     1 AGNNKQQLAFNFIAgkPSEARFVPPLLIYGPFGTGKTFTLAMAALEVIREPGT-KVLICTHTNSAADIYIREYFHPYVDK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  736 GNAQARPLRVYFRNRWVKTVHPVVHQYCLISSAHSTFQMPQKEDILKHRVVVVTLNTSQylcQLDLEPGFFTHILLDEAA 815
Cdd:cd18076    80 GHPEARPLRIKATDRPNAITDPDTITYCCLTKDRQCFRLPTRDELDFHNIVITTTAMAF---NLHVLSGFFTHIFIDEAA 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672069624  816 QAMECETIMPLALATKNTRIVLAGDHMQLSPFVYSeFARERNLHVSLLDRLYEHYPAE-----FPCRILLCENYR 885
Cdd:cd18076   157 QMLECEALIPLSYAGPKTRVVLAGDHMQMTPKLFS-VADYNRANHTLLNRLFHYYQGEkhevaVKSRVIFSENYR 230
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
659-885 7.79e-42

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


Pssm-ID: 350836 [Multi-domain]  Cd Length: 230  Bit Score: 154.06  E-value: 7.79e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  659 LNAKQKEAVLAITTPLCIQLPPVlIIGPYGTGKTFTLAQAVKHILQQQETSRILICTHSNSAADLYIKDyLHPYVEAGNA 738
Cdd:cd18078     2 LNELQKEAVKRILGGECRPLPYI-LFGPPGTGKTVTIIEAILQVVYNLPRSRILVCAPSNSAADLVTSR-LHESKVLKPG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  739 QARPLRVYfrNRWVKTVHPVVHQYCLISSahstfqmpQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQAM 818
Cdd:cd18078    80 DMVRLNAV--NRFESTVIDARKLYCRLGE--------DLSKASRHRIVISTCSTAGLLYQMGLPVGHFTHVFVDEAGQAT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  819 ECETIMPLALATKNT-RIVLAGDHMQLSPFVYSEFARERNLHVSLLDRL-----YEHYPAEFP-CRIL-------LCENY 884
Cdd:cd18078   150 EPESLIPLGLISSRDgQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLmnrplYLRDPNRFGeSGGYnpllvtkLVDNY 229

                  .
gi 672069624  885 R 885
Cdd:cd18078   230 R 230
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
783-1092 9.32e-42

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 167.23  E-value: 9.32e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  783 HRVVVVTLNTSQYLcqLDLEPGFFTHILLDEAAQAMECETIMPLALATkntRIVLAGDHMQLSPFV---YSEFARERNLH 859
Cdd:COG1112   535 APVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVfgeEAEEVAEEGLD 609
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  860 VSLLDRLYEHYPaefPCRILLCENYRSHEAIINYTSELFYEGKLMA---SGKQPAHKDFYPLTFFTARGedVQEKNSTAF 936
Cdd:COG1112   610 ESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDG--VYERRGGSR 684
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  937 YNnaevfevverveelrrkwP------VAW------GKLDDGSIGVVTPYADQVFRIRAELRKKRLSDV------NVERv 998
Cdd:COG1112   685 TN------------------PeeaeavVELvrelleDGPDGESIGVITPYRAQVALIRELLREALGDGLepvfvgTVDR- 745
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  999 lnVQGKQFRVLFLSTVRTRhtckhkqtpikkkeqlleDSTEDLDYGFLS-NYKLLNTAITRAQSLVAVVGDPvALCSIGR 1077
Cdd:COG1112   746 --FQGDERDVIIFSLVYSN------------------DEDVPRNFGFLNgGPRRLNVAVSRARRKLIVVGSR-ELLDSDP 804
                         330
                  ....*....|....*
gi 672069624 1078 CRKFWERFIALCHEN 1092
Cdd:COG1112   805 STPALKRLLEYLERA 819
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
886-1086 6.29e-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: 6.29e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  886 SHEAIINYTSELFYEGKLMAS-------GKQPAHKDFYPLTFFTARGEDVQEKNSTAFYNNAEVFEVVERVEELRRKWpv 958
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGvsvaarlNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  959 awgkLDDGSIGVVTPYADQVFRIRAELRKKR--LSDVNVERVLNVQGKQFRVLFLSTVRTRHTCKHkqtpikkkeqlled 1036
Cdd:cd18808    79 ----VKPSSIGVITPYRAQVALIRELLRKRGglLEDVEVGTVDNFQGREKDVIILSLVRSNESGGS-------------- 140
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 672069624 1037 stedldYGFLSNYKLLNTAITRAQSLVAVVGDPVALCSIGRCRKFWERFI 1086
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 ...
858-1069 4.88e-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: 133.06  E-value: 4.88e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624   858 LHVSLLDRLYEHYPAefpCRILLCENYRSHEAIINYTSELFYEGKLMASGKQPAH---------KDFYPLTFF-TARGED 927
Cdd:pfam13087    1 LDRSLFERLQELGPS---AVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERplpddfhlpDPLGPLVFIdVDGSEE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624   928 VQEKNSTAFYNNAEVFEVVERVEELRRKWPVAWGKlddgsIGVVTPYADQVFRIRAELRKKRLSDVNVErVLNV---QGK 1004
Cdd:pfam13087   78 EESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSD-----IGVITPYRAQVRLIRKLLKRKLGGKLEIE-VNTVdgfQGR 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672069624  1005 QFRVLFLSTVRtrhtckhkqtpikkkeqlledSTEDLDYGFLSNYKLLNTAITRAQSLVAVVGDP 1069
Cdd:pfam13087  152 EKDVIIFSCVR---------------------SNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNA 195
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
658-871 2.46e-25

DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5-3 helicase, and endonuclease activities, and is involved in DNA replication and DNA repair in the nucleus and mitochondrion. It is involved in Okazaki fragment processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. It is also involved in 5-end resection of DNA during double-strand break (DSB) repair; it is recruited by BLM and mediates the cleavage of 5-ssDNA, while the 3-ssDNA cleavage is prevented by the presence of RPA. DNA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350799 [Multi-domain]  Cd Length: 203  Bit Score: 105.40  E-value: 2.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  658 RLNAKQKEAVLAITTPLCIqlppVLIIGPYGTGKTFTLAQAVKhILQQQETSrILICTHSNSAAD---LYIKDYLHPYVE 734
Cdd:cd18041     1 GLNKDQRQAIKKVLNAKDY----ALILGMPGTGKTTTIAALVR-ILVALGKS-VLLTSYTHSAVDnilLKLKKFGVNFLR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  735 AGNAqarplrvyfrnrwvKTVHPVVHQYCLISSAHSTFQMPQKEDIL-KHRVVVVTL--NTSQYLCQldlepGFFTHILL 811
Cdd:cd18041    75 LGRL--------------KKIHPDVQEFTLEAILKSCKSVEELESKYeSVSVVATTClgINHPIFRR-----RTFDYCIV 135
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  812 DEAAQAMECETIMPLALATKntrIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYP 871
Cdd:cd18041   136 DEASQITLPICLGPLRLAKK---FVLVGDHYQLPPLVKSREARELGMDESLFKRLSEAHP 192
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
658-885 1.01e-23

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: 100.38  E-value: 1.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  658 RLNAKQKEAVLaittpLCIQLPPVLII-GPYGTGKTFTLAQAVKHILQQQEtsRILICTHSNSAADlYIKDYLhpyveag 736
Cdd:cd18044     1 NLNDSQKEAVK-----FALSQKDVALIhGPPGTGKTTTVVEIILQAVKRGE--KVLACAPSNIAVD-NLVERL------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  737 naQARPLRVyfrnrwVKTVHPV-----VHQYCLissahstfqmpqkEDILKHRVVVVTLNTSqylCQLDLEPG-FFTHIL 810
Cdd:cd18044    66 --VALKVKV------VRIGHPArllesVLDHSL-------------DALVAAQVVLATNTGA---GSRQLLPNeLFDVVV 121
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672069624  811 LDEAAQAMECETIMPLalaTKNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEfpCRILLCENYR 885
Cdd:cd18044   122 IDEAAQALEASCWIPL---LKARRCILAGDHKQLPPTILSDKAARGGLGVTLFERLVNLYGES--VVRMLTVQYR 191
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
659-866 1.63e-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: 92.69  E-value: 1.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  659 LNAKQKEAV-LAITTPLCiqlppvLIIGPYGTGKTFTLAQAVKHILQQQEtSRILICTHSNSAADlYIKDYLHpyveagN 737
Cdd:cd18039     2 LNHSQVDAVkTALQRPLS------LIQGPPGTGKTVTSATIVYHLVKQGN-GPVLVCAPSNVAVD-QLTEKIH------Q 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  738 AQARPLRVYFRNRW-----VK--TVHPVVHQY-----------------CLISSAHSTFQM----PQKEDILKHRVVVVT 789
Cdd:cd18039    68 TGLKVVRLCAKSREavespVSflALHNQVRNLdsaeklellkllkletgELSSADEKRYRKlkrkAERELLRNADVICCT 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672069624  790 LNTSqylcqLD--LEPGFFTHILLDEAAQAMECETIMPLALATKntRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRL 866
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 ...
659-885 3.24e-19

DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in transcription, neurogenesis, and antiviral response. SEXT is an R-loop-associated protein that is thought to function as an RNA/DNA helicase. R-loops consist of RNA/DNA hybrids, formed during transcription when nascent RNA hybridizes to the DNA template strand, displacing the non-template DNA strand. Mutations in SETX are linked to two neurodegenerative disorders: ataxia with oculomotor apraxia type 2 (AOA2) and amyotrophic lateral sclerosis type 4 (ALS4). S. cerevisiae homolog splicing endonuclease 1 (Sen1) is an exclusively nuclear protein, important for nucleolar organization. S. cerevisiae Sen1 and its ortholog, the Schizosaccharomyces pombe Sen1, share conserved domains and belong to the family I class of helicases. Both proteins translocate 5' to 3' and unwind both DNA and RNA duplexes and also RNA/DNA hybrids in vitro. SETX is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438712 [Multi-domain]  Cd Length: 218  Bit Score: 88.42  E-value: 3.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  659 LNAKQKEAVLAIttplCIQLPPV-LIIGPYGTGKTFTL---------------AQAVKHILQQQETS--------RILIC 714
Cdd:cd18042     1 LNESQLEAIASA----LQNSPGItLIQGPPGTGKTKTIvgilsvllagkyrkyYEKVKKKLRKLQRNlnnkkkknRILVC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  715 THSNSAADLYIKDYLHPYVEAGNAQARPLRVyfrnrwVKTVHpvvhqyclissahstfQMPQKEDILKHRVVVVTLNTSQ 794
Cdd:cd18042    77 APSNAAVDEIVLRLLSEGFLDGDGRSYKPNV------VRVGR----------------QELRASILNEADIVCTTLSSSG 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  795 YLcQLDLEPGFFTHILLDEAAQAMECETIMPLALATKntRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEhypAEF 874
Cdd:cd18042   135 SD-LLESLPRGFDTVIIDEAAQAVELSTLIPLRLGCK--RLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQL---AGY 208
                         250
                  ....*....|.
gi 672069624  875 PCrILLCENYR 885
Cdd:cd18042   209 PV-LMLTTQYR 218
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
681-885 1.06e-15

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


Pssm-ID: 438708 [Multi-domain]  Cd Length: 121  Bit Score: 74.96  E-value: 1.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  681 VLIIGPYGTGKTFTLAQAVKHILQQQETSRILICTHSNSAADlyikdylhpyveagNAqarplrvyfrnrwvktvhpvvh 760
Cdd:cd17934     2 SLIQGPPGTGKTTTIAAIVLQLLKGLRGKRVLVTAQSNVAVD--------------NV---------------------- 45
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  761 qyclissahstfqmpqkedilkhRVVVVtlntsqylcqldlepgffthillDEAAQAMECETIMPLALATKntrIVLAGD 840
Cdd:cd17934    46 -----------------------DVVII-----------------------DEASQITEPELLIALIRAKK---VVLVGD 76
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 672069624  841 HMQLSPFVYSEFARE--RNLHVSLLDRLYEHYPAEFPcrILLCENYR 885
Cdd:cd17934    77 PKQLPPVVQEDHAALlgLSFILSLLLLFRLLLPGSPK--VMLDTQYR 121
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
663-851 3.28e-15

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: 77.38  E-value: 3.28e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624   663 QKEAVLAIttplCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETS-----RILICTHSNSAAD----LYIKDYLHPyv 733
Cdd:pfam13086    2 QREAIRSA----LSSSHFTLIQGPPGTGKTTTIVELIRQLLSYPATSaaagpRILVCAPSNAAVDnileRLLRKGQKY-- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624   734 eagnaQARPLRVYFRnrwvKTVHPVVHQYCLISSAHSTFQMPQKEDILK------------------------------- 782
Cdd:pfam13086   76 -----GPKIVRIGHP----AAISEAVLPVSLDYLVESKLNNEEDAQIVKdiskeleklakalrafekeiivekllksrnk 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624   783 -------------------------------------HRVVVVTLNTS--QYLCQLDlepGFFThILLDEAAQAMECETI 823
Cdd:pfam13086  147 dkskleqerrklrserkelrkelrrreqslereildeAQIVCSTLSGAgsRLLSSLA---NFDV-VIIDEAAQALEPSTL 222
                          250       260
                   ....*....|....*....|....*...
gi 672069624   824 MPLALATKntRIVLAGDHMQLSPFVYSE 851
Cdd:pfam13086  223 IPLLRGPK--KVVLVGDPKQLPPTVISK 248
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
658-866 9.32e-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: 74.12  E-value: 9.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  658 RLNAKQKEA-VLAITTPLciqlppVLIIGPYGTGKTFTLAQAVKHILQ---QQETSRILICTHSNSAADLYIKDYLhpyv 733
Cdd:cd17936     1 TLDPSQLEAlKHALTSEL------ALIQGPPGTGKTFLGVKLVRALLQnqdLSITGPILVVCYTNHALDQFLEGLL---- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  734 EAGNAQArpLRVYFRnrwvktvhpVVHqyCLISSAHSTFQMPQKediLKHRVVVVtlntsqylcqldlepgffthillDE 813
Cdd:cd17936    71 DFGPTKI--VRLGAR---------VIG--MTTTGAAKYRELLQA---LGPKVVIV-----------------------EE 111
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 672069624  814 AAQAMECETIMPLalaTKNTR-IVLAGDHMQLSPFV--YSEFARERNLHVSLLDRL 866
Cdd:cd17936   112 AAEVLEAHILAAL---TPSTEhLILIGDHKQLRPKVnvYELTAKKYNLDVSLFERL 164
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
659-868 3.39e-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: 69.09  E-value: 3.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  659 LNAKQKEAVL-AITTPLciqlppVLIIGPYGTGKTFTLAQAVKHILQQQETSR-----------ILICTHSNSAADL--- 723
Cdd:cd18040     2 LNPSQNHAVRtALTKPF------TLIQGPPGTGKTVTGVHIAYWFAKQNREIQsvsgegdggpcVLYCGPSNKSVDVvae 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  724 YIKDY-----LHPYVEAGNAQARPLRVYFRNRWVK--------------TVHPVVHQ----YC-LISSAHSTFQMPQ--- 776
Cdd:cd18040    76 LLLKVpglkiLRVYSEQIETTEYPIPNEPRHPNKKsereskpnselssiTLHHRIRQpsnpHSqQIKAFEARFERTQeki 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  777 -KEDILKHRVVV------------VTLNTsqylCQLDLEPGFFTH-----ILLDEAAQAMECETIMPLALATKNTRIVLA 838
Cdd:cd18040   156 tEEDIKTYKILIwearfeeletvdVILCT----CSEAASQKMRTHanvkqCIVDECGMCTEPESLIPIVSAPRAEQVVLI 231
                         250       260       270
                  ....*....|....*....|....*....|
gi 672069624  839 GDHMQLSPFVYSEFARERNLHVSLLDRLYE 868
Cdd:cd18040   232 GDHKQLRPVVQNKEAQKLGLGRSLFERYAE 261
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
658-866 7.29e-11

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


Pssm-ID: 350693 [Multi-domain]  Cd Length: 207  Bit Score: 63.60  E-value: 7.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  658 RLNAKQKEAVLAITTPLCiqlppVLIIGPYGTGKTFTLAQAVKHILQQQETSRILICTHSNSAA-DLYIKdylhpyVEAg 736
Cdd:cd17935     5 KFTPTQIEAIRSGMQPGL-----TMVVGPPGTGKTDVAVQIISNLYHNFPNQRTLIVTHSNQALnQLFEK------IMA- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  737 naqarpLRVYFRNrwvktvhpvvhqycLISSAHSTfqmpqkedilkhRVVVVTLnTSQYLCQLDL-EPGF-FTHILLDEA 814
Cdd:cd17935    73 ------LDIDERH--------------LLRLGHGA------------KIIAMTC-THAALKRGELvELGFkYDNILMEEA 119
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 672069624  815 AQAMECETIMPLALATKNT------RIVLAGDHMQLSPFVYS-EFARERNLHVSLLDRL 866
Cdd:cd17935   120 AQILEIETFIPLLLQNPEDgpnrlkRLIMIGDHHQLPPVIKNmAFQKYSNMEQSLFTRL 178
DEXQc_UvrD cd17932
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch ...
660-884 4.22e-09

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: 58.30  E-value: 4.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  660 NAKQKEAVLAITTPLCIqlppvlIIGPyGTGKTFTLAQAVKHILQQQET--SRILICTHSNSAADlYIKDYLHPYVeaGN 737
Cdd:cd17932     1 NPEQREAVTHPDGPLLV------LAGA-GSGKTRVLTHRIAYLILEGGVppERILAVTFTNKAAK-EMRERLRKLL--GE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  738 AQARPLrvyfrnrWVKTVHPVvhqyCL-ISSAHSTFqmpqkEDILkHRVVVVtLNTSQYLCQLDLEPgfFTHILLDEA-- 814
Cdd:cd17932    71 QLASGV-------WIGTFHSF----ALrILRRYGDF-----DDLL-LYALEL-LEENPDVREKLQSR--FRYILVDEYqd 130
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672069624  815 ---AQamecETIMpLALATKNTRIVLAGDHMQlSpfVYSeFareRNLHVSLLDRLYEHYPAefPCRILLCENY 884
Cdd:cd17932   131 tnpLQ----YELL-KLLAGDGKNLFVVGDDDQ-S--IYG-F---RGADPENILDFEKDFPD--AKVIKLEENY 189
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
660-849 2.67e-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: 2.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  660 NAKQKEAVLAIttplcIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQEtsRILICTHSNSAADlyikdylhpyveagnaq 739
Cdd:cd18043     1 DSSQEAAIISA-----RNGKNVVIQGPPGTGKSQTIANIIANALARGK--RVLFVSEKKAALD----------------- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  740 arplrvyfrnrwvktvhpVVHQYCLISSAHSTFQMpqkedilkhrvvvvtlntsqylcqLDLEPGFFTHILLDEAAQAME 819
Cdd:cd18043    57 ------------------VVRFPCWIMSPLSVSQY------------------------LPLNRNLFDLVIFDEASQIPI 94
                         170       180       190
                  ....*....|....*....|....*....|
gi 672069624  820 CETImPLALATKntRIVLAGDHMQLSPFVY 849
Cdd:cd18043    95 EEAL-PALFRGK--QVVVVGDDKQLPPSIL 121
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
680-722 3.08e-07

DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. Their helicase core is surrounded by C and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains or domains engaged in protein-protein interactions. SF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438706 [Multi-domain]  Cd Length: 121  Bit Score: 50.95  E-value: 3.08e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 672069624  680 PVLIIGPYGTGKTFTLAQAVKHILQQQETS--RILICTHSNSAAD 722
Cdd:cd17914     1 LSLIQGPPGTGKTRVLVKIVAALMQNKNGEpgRILLVTPTNKAAA 45
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
649-1090 4.79e-07

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 54.60  E-value: 4.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  649 RQWDEQLDPRLNAKQKEAV--LAITTPLCIqlppvlIIGPYGTGKTFTLAQAVKHILQQQEtsRILICTHSNSAAD-LYi 725
Cdd:COG0507   115 AALEPRAGITLSDEQREAValALTTRRVSV------LTGGAGTGKTTTLRALLAALEALGL--RVALAAPTGKAAKrLS- 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  726 kdylhpyvEAGNAQARplrvyfrnrwvkTVHPVVHqyclISSAHSTFQMPQKEDILKHRVVVVtlntsqylcqldlepgf 805
Cdd:COG0507   186 --------ESTGIEAR------------TIHRLLG----LRPDSGRFRHNRDNPLTPADLLVV----------------- 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  806 fthillDEA--------AQAMEcetimplALATKNTRIVLAGDHMQLSP----FVYSEFARERNLHVSLLDrlyehypae 873
Cdd:COG0507   225 ------DEAsmvdtrlmAALLE-------ALPRAGARLILVGDPDQLPSvgagAVLRDLIESGTVPVVELT--------- 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  874 fpcrillcENYRSHEAI-INYTSELFYEGKlMASGKQPAHKDFYPL----------------TFFTARGEDVQ-----EK 931
Cdd:COG0507   283 --------EVYRQADDSrIIELAHAIREGD-APEALNARYADVVFVeaedaeeaaeaivelyADRPAGGEDIQvlaptNA 353
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  932 nSTAFYN-------NAEVFEVVERVEELRRKW----PV-------AWGkLDDGSIGVVTPYADQVFRIRAELRKKRLSDV 993
Cdd:COG0507   354 -GVDALNqairealNPAGELERELAEDGELELyvgdRVmftrndyDLG-VFNGDIGTVLSIDEDEGRLTVRFDGREIVTY 431
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  994 NVERVLNV-----------QGKQF-RVLFLSTvrtrhtckhkqtpikkkeqlledsteDLDYGFLSNyKLLNTAITRAQS 1061
Cdd:COG0507   432 DPSELDQLelayaitvhksQGSTFdRVILVLP--------------------------SEHSPLLSR-ELLYTALTRARE 484
                         490       500
                  ....*....|....*....|....*....
gi 672069624 1062 LVAVVGDPVALCSIgrCRKFWERFIALCH 1090
Cdd:COG0507   485 LLTLVGDRDALARA--VRRDTARATGLAE 511
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
662-846 6.02e-07

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


Pssm-ID: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 51.02  E-value: 6.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  662 KQKEAVLAITT-PLCIqlppvlIIGPYGTGKTFTLAQAVKHIlqQQETSRILICTHSNSAADlyikdylhpyvEAGNAQA 740
Cdd:cd17933     1 EQKAAVRLVLRnRVSV------LTGGAGTGKTTTLKALLAAL--EAEGKRVVLAAPTGKAAK-----------RLSESTG 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  741 RPlrvyfrnrwVKTVHPVvhqycLISSAHSTFQMPQKEDILKHRVVVVtlntsqylcqldlepgffthillDEAaqAMec 820
Cdd:cd17933    62 IE---------ASTIHRL-----LGINPGGGGFYYNEENPLDADLLIV-----------------------DEA--SM-- 100
                         170       180       190
                  ....*....|....*....|....*....|...
gi 672069624  821 etiMPLALATK-------NTRIVLAGDHMQLSP 846
Cdd:cd17933   101 ---VDTRLMAAllsaipaGARLILVGDPDQLPS 130
UvrD COG0210
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
658-721 2.02e-06

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


Pssm-ID: 439980 [Multi-domain]  Cd Length: 721  Bit Score: 53.02  E-value: 2.02e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672069624  658 RLNAKQKEAVLAITTPLciqlppvLII-GPyGTGKTFTLAQAVKHILQQQETS--RILICTHSNSAA 721
Cdd:COG0210     6 GLNPEQRAAVEHPEGPL-------LVLaGA-GSGKTRVLTHRIAYLIAEGGVDpeQILAVTFTNKAA 64
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
181-205 6.87e-06

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


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 44.11  E-value: 6.87e-06
                           10        20
                   ....*....|....*....|....*
gi 672069624   181 YTLCKRFLEQGICRYGAQCTSAHSQ 205
Cdd:pfam00642    3 TELCRFFLRTGYCKYGDRCKFAHGQ 27
UvrD-helicase pfam00580
UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural ...
659-722 7.15e-06

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


Pssm-ID: 395462 [Multi-domain]  Cd Length: 267  Bit Score: 49.94  E-value: 7.15e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672069624   659 LNAKQKEAVLAITTPLciqlppvLIIGPYGTGKTFTLAQAVKHILQQQETS--RILICTHSNSAAD 722
Cdd:pfam00580    1 LNPEQRKAVTHLGGPL-------LVLAGAGSGKTRVLTERIAYLILEGGIDpeEILAVTFTNKAAR 59
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1336-1430 8.85e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 47.77  E-value: 8.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624 1336 PESRPGVVYSNTKFPRKDNLNPRHINLPLPAPHTQYAIPSRHFHPLPQLPRPPFPISQQHTLLNQQQnnlPEQPNQMTPQ 1415
Cdd:PRK10263  743 PLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQ---PVAPQPQYQQ 819
                          90
                  ....*....|....*.
gi 672069624 1416 PNQ-VAPQPNQMAPQP 1430
Cdd:PRK10263  820 PQQpVAPQPQYQQPQQ 835
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
658-846 1.27e-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: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624   658 RLNAKQKEAVLAITT-PLCIQLppvlIIGPYGTGKTFTLAQAVKHIlqQQETSRILICTHSNSAADLYIKDYlhpyveag 736
Cdd:pfam13604    1 TLNAEQAAAVRALLTsGDRVAV----LVGPAGTGKTTALKALREAW--EAAGYRVIGLAPTGRAAKVLGEEL-------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624   737 NAQARplrvyfrnrwvkTVHPVVHQYclissahstfqmPQKEDILKHRVVVVtlntsqylcqldlepgffthillDEAAQ 816
Cdd:pfam13604   67 GIPAD------------TIAKLLHRL------------GGRAGLDPGTLLIV-----------------------DEAGM 99
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 672069624   817 A----MEcetiMPLALATK-NTRIVLAGDHMQLSP 846
Cdd:pfam13604  100 VgtrqMA----RLLKLAEDaGARVILVGDPRQLPS 130
ResIII pfam04851
Type III restriction enzyme, res subunit;
659-814 1.67e-04

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 44.20  E-value: 1.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624   659 LNAKQKEAVLAITTPLCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETSRILICTHSNsaaDLY------IKDYLHPY 732
Cdd:pfam04851    4 LRPYQIEAIENLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRK---DLLeqaleeFKKFLPNY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624   733 VEAGNaqarPLRVYFRNRWVKTVHPVVhqyclissahSTFQmpqkedilkhrvvvvTLNTSQYLCQLDLEPGFFTHILLD 812
Cdd:pfam04851   81 VEIGE----IISGDKKDESVDDNKIVV----------TTIQ---------------SLYKALELASLELLPDFFDVIIID 131

                   ..
gi 672069624   813 EA 814
Cdd:pfam04851  132 EA 133
AAA_19 pfam13245
AAA domain;
663-722 1.77e-04

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 43.36  E-value: 1.77e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672069624   663 QKEAVLAITTPlciqlPPVLIIGPYGTGKTFTLAQAVKHILQQQETS-RILICTHSNSAAD 722
Cdd:pfam13245    1 QREAVRTALPS-----KVVLLTGGPGTGKTTTIRHIVALLVALGGVSfPILLAAPTGRAAK 56
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1261-1536 5.65e-04

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: 45.14  E-value: 5.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  1261 HGRGSPIPYglghhpPVNLGQPQNQHAEKDQQEQNRNGKTDTNNP-GPEINKIRTPEKKPTEPKqidlesnPQNRSPESR 1339
Cdd:pfam03154  272 HGQMPPMPH------SLQTGPSHMQHPVPPQPFPLTPQSSQSQVPpGPSPAAPGQSQQRIHTPP-------SQSQLQSQQ 338
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  1340 PgvvysntkfPRKDNLNPRhinlPLPAPHTQyaipsrhfhPLPQLPRPPFPISQQHTLLN--------QQQNNLPEQP-- 1409
Cdd:pfam03154  339 P---------PREQPLPPA----PLSMPHIK---------PPPTTPIPQLPNPQSHKHPPhlsgpspfQMNSNLPPPPal 396
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  1410 ----NQMTPQPNQVAPQPNQMAPQPNQMAPQPNQVVQQQNQAPPQAPQPAPQLSPAFQAGPTNAFFnnavahrPQSP--- 1482
Cdd:pfam03154  397 kplsSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPF-------PQHPfvp 469
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 672069624  1483 -AAEAVGPEQQVPPGLSDGHSPLRAITQPGPILASPLNNFVDESSPGLPI-EEALD 1536
Cdd:pfam03154  470 gGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIkEEALD 525
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
654-747 2.17e-03

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 43.09  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624  654 QLDPRLNAKQKEAVLAITTPLCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQetsRILICTHS----NSAADLyIKDYL 729
Cdd:COG1061    76 GTSFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGK---RVLVLVPRrellEQWAEE-LRRFL 151
                          90
                  ....*....|....*...
gi 672069624  730 HPYVEAGNAQARPLRVYF 747
Cdd:COG1061   152 GDPLAGGGKKDSDAPITV 169
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
1348-1433 3.62e-03

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: 40.16  E-value: 3.62e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624   1348 KFPRKDNLNPRHINLPLPAPHTqyAIPSRHFHP-LPQLPRPPFpisqqhtllnQQQNNLPEQPNQMTPQPNQVAPQPNQM 1426
Cdd:smart00818   60 VLPAQQPVVPQQPLMPVPGQHS--MTPTQHHQPnLPQPAQQPF----------QPQPLQPPQPQQPMQPQPPVHPIPPLP 127

                    ....*..
gi 672069624   1427 APQPNQM 1433
Cdd:smart00818  128 PQPPLPP 134
AAA_22 pfam13401
AAA domain;
681-726 4.91e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 39.25  E-value: 4.91e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 672069624   681 VLIIGPYGTGKTfTLAQAVKHILQQQETSRILI-CTHSNSAADLYIK 726
Cdd:pfam13401    8 LVLTGESGTGKT-TLLRRLLEQLPEVRDSVVFVdLPSGTSPKDLLRA 53
dnaA PRK14086
chromosomal replication initiator protein DnaA;
1314-1517 6.19e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 41.35  E-value: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624 1314 TPEKKPTEPKQIDLESNPQNRSPESRPGVVYSNTKFPRKDNLNPRHINLPLPAPhtqyAIPSRHFHPLP-QLPRPPFPIS 1392
Cdd:PRK14086   91 SAGEPAPPPPHARRTSEPELPRPGRRPYEGYGGPRADDRPPGLPRQDQLPTARP----AYPAYQQRPEPgAWPRAADDYG 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672069624 1393 QQHTLLNQQQNNLPEQPNQMTPQPNQVAPQPNQMAPQPNQMAPQPNQvvqqqnqappqapqpapqlsPAFQAGPTNAFFN 1472
Cdd:PRK14086  167 WQQQRLGFPPRAPYASPASYAPEQERDREPYDAGRPEYDQRRRDYDH--------------------PRPDWDRPRRDRT 226
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 672069624 1473 NavahRPQ-SPAAEAVGPEQQVPPGLSDGHSPLRAITQPGPILASP 1517
Cdd:PRK14086  227 D----RPEpPPGAGHVHRGGPGPPERDDAPVVPIRPSAPGPLAAQP 268
 
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