|
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 |
5.77e-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: 5.77e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 641 RLNAKQKEAVLAITTPLCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETRILICTHSNSAADLYIKDYLHPYVEAGNA 720
Cdd:cd18077 1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPETRILICTHSNSAADLYIKEYLHPYVETGNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 721 QARPLRVYFRNRWVKTVHPVVHQYCLISsAHSTFQMPQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQAM 800
Cdd:cd18077 81 RARPLRVYYRNRWVKTVHPVVQKYCLID-EHGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQAM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564374816 801 ECETIMPLALATKNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEFPCRILLCENYR 867
Cdd:cd18077 160 ECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSEHPCRILLCENYR 226
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
765-1074 |
9.19e-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: 9.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 765 HRVVVVTLNTSQYLcqLDLEPGFFTHILLDEAAQAMECETIMPLALATkntRIVLAGDHMQLSPFV---YSEFARERNLH 841
Cdd:COG1112 535 APVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVfgeEAEEVAEEGLD 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 842 VSLLDRLYEHYPaefPCRILLCENYRSHEAIINYTSELFYEGKLMA---SGKQPAHKDFYPLTFFTARGedVQEKNSTAF 918
Cdd:COG1112 610 ESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDG--VYERRGGSR 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 919 YNnaevfevverveelrrkwP------VAW------GKLDDGSIGVVTPYADQVFRIRAELRKKRLSDV------NVERv 980
Cdd:COG1112 685 TN------------------PeeaeavVELvrelleDGPDGESIGVITPYRAQVALIRELLREALGDGLepvfvgTVDR- 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 981 lnVQGKQFRVLFLSTVRTRhtckhkqtpikkkeqlleDSTEDLDYGFLS-NYKLLNTAITRAQSLVAVVGDPvALCSIGR 1059
Cdd:COG1112 746 --FQGDERDVIIFSLVYSN------------------DEDVPRNFGFLNgGPRRLNVAVSRARRKLIVVGSR-ELLDSDP 804
|
330
....*....|....*
gi 564374816 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 |
6.35e-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: 6.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 868 SHEAIINYTSELFYEGKLMAS-------GKQPAHKDFYPLTFFTARGEDVQEKNSTAFYNNAEVFEVVERVEELRRKWpv 940
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKAGvsvaarlNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 941 awgkLDDGSIGVVTPYADQVFRIRAELRKKR--LSDVNVERVLNVQGKQFRVLFLSTVRTRHTCKHkqtpikkkeqlled 1018
Cdd:cd18808 79 ----VKPSSIGVITPYRAQVALIRELLRKRGglLEDVEVGTVDNFQGREKDVIILSLVRSNESGGS-------------- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 564374816 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 |
4.83e-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: 4.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 840 LHVSLLDRLYEHYPAefpCRILLCENYRSHEAIINYTSELFYEGKLMASGKQPAH---------KDFYPLTFF-TARGED 909
Cdd:pfam13087 1 LDRSLFERLQELGPS---AVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERplpddfhlpDPLGPLVFIdVDGSEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 910 VQEKNSTAFYNNAEVFEVVERVEELRRKWPVAWGKlddgsIGVVTPYADQVFRIRAELRKKRLSDVNVErVLNV---QGK 986
Cdd:pfam13087 78 EESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSD-----IGVITPYRAQVRLIRKLLKRKLGGKLEIE-VNTVdgfQGR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564374816 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 ... |
646-833 |
6.11e-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: 76.61 E-value: 6.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 646 QKEAVLAIttplCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQET------RILICTHSNSAAD----LYIKDYLHPyv 715
Cdd:pfam13086 2 QREAIRSA----LSSSHFTLIQGPPGTGKTTTIVELIRQLLSYPATsaaagpRILVCAPSNAAVDnileRLLRKGQKY-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 716 eagnaQARPLRVYFRnrwvKTVHPVVHQYCLISSAHSTFQMPQKEDILK------------------------------- 764
Cdd:pfam13086 76 -----GPKIVRIGHP----AAISEAVLPVSLDYLVESKLNNEEDAQIVKdiskeleklakalrafekeiivekllksrnk 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 765 -------------------------------------HRVVVVTLNTS--QYLCQLDlepGFFThILLDEAAQAMECETI 805
Cdd:pfam13086 147 dkskleqerrklrserkelrkelrrreqslereildeAQIVCSTLSGAgsRLLSSLA---NFDV-VIIDEAAQALEPSTL 222
|
250 260
....*....|....*....|....*...
gi 564374816 806 MPLALATKntRIVLAGDHMQLSPFVYSE 833
Cdd:pfam13086 223 IPLLRGPK--KVVLVGDPKQLPPTVISK 248
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
632-1072 |
4.10e-08 |
|
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: 58.06 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 632 RQWDEQLDPRLNAKQKEAV--LAITTPLCIqlppvlIIGPYGTGKTFTLAqAVKHILQQQETRILICTHSNSAAD-LYik 708
Cdd:COG0507 115 AALEPRAGITLSDEQREAValALTTRRVSV------LTGGAGTGKTTTLR-ALLAALEALGLRVALAAPTGKAAKrLS-- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 709 dylhpyvEAGNAQARplrvyfrnrwvkTVHPVVHqyclISSAHSTFQMPQKEDILKHRVVVVtlntsqylcqldlepgff 788
Cdd:COG0507 186 -------ESTGIEAR------------TIHRLLG----LRPDSGRFRHNRDNPLTPADLLVV------------------ 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 789 thillDEA--------AQAMEcetimplALATKNTRIVLAGDHMQLSP----FVYSEFARERNLHVSLLDrlyehypaef 856
Cdd:COG0507 225 -----DEAsmvdtrlmAALLE-------ALPRAGARLILVGDPDQLPSvgagAVLRDLIESGTVPVVELT---------- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 857 pcrillcENYRSHEAI-INYTSELFYEGKlMASGKQPAHKDFYPL----------------TFFTARGEDVQ-----EKn 914
Cdd:COG0507 283 -------EVYRQADDSrIIELAHAIREGD-APEALNARYADVVFVeaedaeeaaeaivelyADRPAGGEDIQvlaptNA- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 915 STAFYN-------NAEVFEVVERVEELRRKW----PV-------AWGkLDDGSIGVVTPYADQVFRIRAELRKKRLSDVN 976
Cdd:COG0507 354 GVDALNqairealNPAGELERELAEDGELELyvgdRVmftrndyDLG-VFNGDIGTVLSIDEDEGRLTVRFDGREIVTYD 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 977 VERVLNV-----------QGKQF-RVLFLSTvrtrhtckhkqtpikkkeqlledsteDLDYGFLSNyKLLNTAITRAQSL 1044
Cdd:COG0507 433 PSELDQLelayaitvhksQGSTFdRVILVLP--------------------------SEHSPLLSR-ELLYTALTRAREL 485
|
490 500
....*....|....*....|....*...
gi 564374816 1045 VAVVGDPVALCSIgrCRKFWERFIALCH 1072
Cdd:COG0507 486 LTLVGDRDALARA--VRRDTARATGLAE 511
|
|
| zf-CCCH |
pfam00642 |
Zinc finger C-x8-C-x5-C-x3-H type (and similar); |
181-205 |
6.11e-06 |
|
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
Pssm-ID: 459885 [Multi-domain] Cd Length: 27 Bit Score: 44.49 E-value: 6.11e-06
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
1318-1412 |
9.14e-05 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 47.77 E-value: 9.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 1318 PESRPGVVYSNTKFPRKDNLNPRHINLPLPAPHTQYAIPSRHFHPLPQLPRPPFPISQQHTLLNQQQnnlPEQPNQMTPQ 1397
Cdd:PRK10263 743 PLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQ---PVAPQPQYQQ 819
|
90
....*....|....*.
gi 564374816 1398 PNQ-VAPQPNQMAPQP 1412
Cdd:PRK10263 820 PQQpVAPQPQYQQPQQ 835
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1243-1518 |
5.64e-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: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 1243 HGRGSPIPYglghhpPVNLGQPQNQHAEKDQQEQNRNGKTDTNNP-GPEINKIRTPEKKPTEPKqidlesnPQNRSPESR 1321
Cdd:pfam03154 272 HGQMPPMPH------SLQTGPSHMQHPVPPQPFPLTPQSSQSQVPpGPSPAAPGQSQQRIHTPP-------SQSQLQSQQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 1322 PgvvysntkfPRKDNLNPRhinlPLPAPHTQyaipsrhfhPLPQLPRPPFPISQQHTLLN--------QQQNNLPEQP-- 1391
Cdd:pfam03154 339 P---------PREQPLPPA----PLSMPHIK---------PPPTTPIPQLPNPQSHKHPPhlsgpspfQMNSNLPPPPal 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 1392 ----NQMTPQPNQVAPQPNQMAPQPNQMAPQPNQVVQQQNQAPPQAPQPAPQLSPAFQAGPTNAFFnnavahrPQSP--- 1464
Cdd:pfam03154 397 kplsSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPF-------PQHPfvp 469
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 564374816 1465 -AAEAVGPEQQVPPGLSDGHSPLRAITQPGPILASPLNNFVDESSPGLPI-EEALD 1518
Cdd:pfam03154 470 gGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIkEEALD 525
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
663-741 |
1.86e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.82 E-value: 1.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564374816 663 PVLIIGPYGTGKTfTLAQAVKHILQQQETRILICTHSNSAADLYIKDYLHPYVEAGNAQARPLRVYFRNRWVKTVHPVV 741
Cdd:smart00382 4 VILIVGPPGSGKT-TLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDV 81
|
|
| Amelogenin |
smart00818 |
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
1330-1415 |
3.72e-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: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 1330 KFPRKDNLNPRHINLPLPAPHTqyAIPSRHFHP-LPQLPRPPFpisqqhtllnQQQNNLPEQPNQMTPQPNQVAPQPNQM 1408
Cdd:smart00818 60 VLPAQQPVVPQQPLMPVPGQHS--MTPTQHHQPnLPQPAQQPF----------QPQPLQPPQPQQPMQPQPPVHPIPPLP 127
|
....*..
gi 564374816 1409 APQPNQM 1415
Cdd:smart00818 128 PQPPLPP 134
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
1296-1499 |
6.45e-03 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 41.35 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 1296 TPEKKPTEPKQIDLESNPQNRSPESRPGVVYSNTKFPRKDNLNPRHINLPLPAPhtqyAIPSRHFHPLP-QLPRPPFPIS 1374
Cdd:PRK14086 91 SAGEPAPPPPHARRTSEPELPRPGRRPYEGYGGPRADDRPPGLPRQDQLPTARP----AYPAYQQRPEPgAWPRAADDYG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 1375 QQHTLLNQQQNNLPEQPNQMTPQPNQVAPQPNQMAPQPNQMAPQPNQvvqqqnqappqapqpapqlsPAFQAGPTNAFFN 1454
Cdd:PRK14086 167 WQQQRLGFPPRAPYASPASYAPEQERDREPYDAGRPEYDQRRRDYDH--------------------PRPDWDRPRRDRT 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564374816 1455 NavahRPQ-SPAAEAVGPEQQVPPGLSDGHSPLRAITQPGPILASP 1499
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 ... |
641-867 |
5.77e-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: 5.77e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 641 RLNAKQKEAVLAITTPLCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETRILICTHSNSAADLYIKDYLHPYVEAGNA 720
Cdd:cd18077 1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPETRILICTHSNSAADLYIKEYLHPYVETGNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 721 QARPLRVYFRNRWVKTVHPVVHQYCLISsAHSTFQMPQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQAM 800
Cdd:cd18077 81 RARPLRVYYRNRWVKTVHPVVQKYCLID-EHGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQAM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564374816 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 |
8.31e-94 |
|
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and similar proteins. Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. All are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350796 [Multi-domain] Cd Length: 229 Bit Score: 303.00 E-value: 8.31e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 641 RLNAKQKEAVLAITTPLCiQLPPVLIIGPYGTGKTFTLAQAVKHIL-QQQETRILICTHSNSAADLYIKDYLHPYVEagn 719
Cdd:cd18038 1 ELNDEQKLAVRNIVTGTS-RPPPYIIFGPPGTGKTVTLVEAILQVLrQPPEARILVCAPSNSAADLLAERLLNALVT--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 720 aQARPLRVYFRNRWVKTVHPVVHQYClISSAHSTFQMPQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQA 799
Cdd:cd18038 77 -KREILRLNAPSRDRASVPPELLPYC-NSKAEGTFRLPSLEELKKYRIVVCTLMTAGRLVQAGVPNGHFTHIFIDEAGQA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564374816 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 |
9.36e-68 |
|
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB, and RXRA. It belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350834 [Multi-domain] Cd Length: 230 Bit Score: 228.62 E-value: 9.36e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 641 RLNAKQKEAVLAIT--TPLCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETRILICTHSNSAADLYIKDYLHPYVEAG 718
Cdd:cd18076 1 AGNNKQQLAFNFIAgkPSEARFVPPLLIYGPFGTGKTFTLAMAALEVIREPGTKVLICTHTNSAADIYIREYFHPYVDKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 719 NAQARPLRVYFRNRWVKTVHPVVHQYCLISSAHSTFQMPQKEDILKHRVVVVTLNTSQylcQLDLEPGFFTHILLDEAAQ 798
Cdd:cd18076 81 HPEARPLRIKATDRPNAITDPDTITYCCLTKDRQCFRLPTRDELDFHNIVITTTAMAF---NLHVLSGFFTHIFIDEAAQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564374816 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 |
9.19e-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: 9.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 765 HRVVVVTLNTSQYLcqLDLEPGFFTHILLDEAAQAMECETIMPLALATkntRIVLAGDHMQLSPFV---YSEFARERNLH 841
Cdd:COG1112 535 APVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVfgeEAEEVAEEGLD 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 842 VSLLDRLYEHYPaefPCRILLCENYRSHEAIINYTSELFYEGKLMA---SGKQPAHKDFYPLTFFTARGedVQEKNSTAF 918
Cdd:COG1112 610 ESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDG--VYERRGGSR 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 919 YNnaevfevverveelrrkwP------VAW------GKLDDGSIGVVTPYADQVFRIRAELRKKRLSDV------NVERv 980
Cdd:COG1112 685 TN------------------PeeaeavVELvrelleDGPDGESIGVITPYRAQVALIRELLREALGDGLepvfvgTVDR- 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 981 lnVQGKQFRVLFLSTVRTRhtckhkqtpikkkeqlleDSTEDLDYGFLS-NYKLLNTAITRAQSLVAVVGDPvALCSIGR 1059
Cdd:COG1112 746 --FQGDERDVIIFSLVYSN------------------DEDVPRNFGFLNgGPRRLNVAVSRARRKLIVVGSR-ELLDSDP 804
|
330
....*....|....*
gi 564374816 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 |
4.72e-41 |
|
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. Mov10L1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350836 [Multi-domain] Cd Length: 230 Bit Score: 151.75 E-value: 4.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 642 LNAKQKEAVLAITTPLCIQLPPVlIIGPYGTGKTFTLAQAvkhILQQQ----ETRILICTHSNSAADLYIKDyLHPYVEA 717
Cdd:cd18078 2 LNELQKEAVKRILGGECRPLPYI-LFGPPGTGKTVTIIEA---ILQVVynlpRSRILVCAPSNSAADLVTSR-LHESKVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 718 GNAQARPLRVYfrNRWVKTVHPVVHQYCLISSahstfqmpQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAA 797
Cdd:cd18078 77 KPGDMVRLNAV--NRFESTVIDARKLYCRLGE--------DLSKASRHRIVISTCSTAGLLYQMGLPVGHFTHVFVDEAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 798 QAMECETIMPLALATKNT-RIVLAGDHMQLSPFVYSEFARERNLHVSLLDRL-----YEHYPAEFP-CRIL-------LC 863
Cdd:cd18078 147 QATEPESLIPLGLISSRDgQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLmnrplYLRDPNRFGeSGGYnpllvtkLV 226
|
....
gi 564374816 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 |
6.35e-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: 6.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 868 SHEAIINYTSELFYEGKLMAS-------GKQPAHKDFYPLTFFTARGEDVQEKNSTAFYNNAEVFEVVERVEELRRKWpv 940
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKAGvsvaarlNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 941 awgkLDDGSIGVVTPYADQVFRIRAELRKKR--LSDVNVERVLNVQGKQFRVLFLSTVRTRHTCKHkqtpikkkeqlled 1018
Cdd:cd18808 79 ----VKPSSIGVITPYRAQVALIRELLRKRGglLEDVEVGTVDNFQGREKDVIILSLVRSNESGGS-------------- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 564374816 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 |
4.83e-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: 4.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 840 LHVSLLDRLYEHYPAefpCRILLCENYRSHEAIINYTSELFYEGKLMASGKQPAH---------KDFYPLTFF-TARGED 909
Cdd:pfam13087 1 LDRSLFERLQELGPS---AVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERplpddfhlpDPLGPLVFIdVDGSEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 910 VQEKNSTAFYNNAEVFEVVERVEELRRKWPVAWGKlddgsIGVVTPYADQVFRIRAELRKKRLSDVNVErVLNV---QGK 986
Cdd:pfam13087 78 EESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSD-----IGVITPYRAQVRLIRKLLKRKLGGKLEIE-VNTVdgfQGR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564374816 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 |
1.81e-26 |
|
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5-3 helicase, and endonuclease activities, and is involved in DNA replication and DNA repair in the nucleus and mitochondrion. It is involved in Okazaki fragment processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. It is also involved in 5-end resection of DNA during double-strand break (DSB) repair; it is recruited by BLM and mediates the cleavage of 5-ssDNA, while the 3-ssDNA cleavage is prevented by the presence of RPA. DNA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350799 [Multi-domain] Cd Length: 203 Bit Score: 108.86 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 641 RLNAKQKEAVLAITTPLCIqlppVLIIGPYGTGKTFTLAQAVKhILQQQETRILICTHSNSAAD---LYIKDYLHPYVEA 717
Cdd:cd18041 1 GLNKDQRQAIKKVLNAKDY----ALILGMPGTGKTTTIAALVR-ILVALGKSVLLTSYTHSAVDnilLKLKKFGVNFLRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 718 GNAqarplrvyfrnrwvKTVHPVVHQYCLISSAHSTFQMPQKEDIL-KHRVVVVTL--NTSQYLCQldlepGFFTHILLD 794
Cdd:cd18041 76 GRL--------------KKIHPDVQEFTLEAILKSCKSVEELESKYeSVSVVATTClgINHPIFRR-----RTFDYCIVD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564374816 795 EAAQAMECETIMPLALATKntrIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYP 853
Cdd:cd18041 137 EASQITLPICLGPLRLAKK---FVLVGDHYQLPPLVKSREARELGMDESLFKRLSEAHP 192
|
|
| DEXXQc_SMUBP2 |
cd18044 |
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ... |
641-867 |
4.93e-24 |
|
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: 101.53 E-value: 4.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 641 RLNAKQKEAVLaittpLCIQLPPVLII-GPYGTGKTFTLAQAvkhILQ--QQETRILICTHSNSAADlYIKDYLhpyvea 717
Cdd:cd18044 1 NLNDSQKEAVK-----FALSQKDVALIhGPPGTGKTTTVVEI---ILQavKRGEKVLACAPSNIAVD-NLVERL------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 718 gnaQARPLRVyfrnrwVKTVHPV-----VHQYCLissahstfqmpqkEDILKHRVVVVTLNTSqylCQLDLEPG-FFTHI 791
Cdd:cd18044 66 ---VALKVKV------VRIGHPArllesVLDHSL-------------DALVAAQVVLATNTGA---GSRQLLPNeLFDVV 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564374816 792 LLDEAAQAMECETIMPLalaTKNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEfpCRILLCENYR 867
Cdd:cd18044 121 VIDEAAQALEASCWIPL---LKARRCILAGDHKQLPPTILSDKAARGGLGVTLFERLVNLYGES--VVRMLTVQYR 191
|
|
| DEXXQc_UPF1 |
cd18039 |
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ... |
642-848 |
6.13e-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: 96.55 E-value: 6.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 642 LNAKQKEAV-LAITTPLCiqlppvLIIGPYGTGKTFTLAQAVKHILQQQETRILICTHSNSAADlYIKDYLHpyveagNA 720
Cdd:cd18039 2 LNHSQVDAVkTALQRPLS------LIQGPPGTGKTVTSATIVYHLVKQGNGPVLVCAPSNVAVD-QLTEKIH------QT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 721 QARPLRVYFRNRW-----VK--TVHPVVHQY-----------------CLISSAHSTFQM----PQKEDILKHRVVVVTL 772
Cdd:cd18039 69 GLKVVRLCAKSREavespVSflALHNQVRNLdsaeklellkllkletgELSSADEKRYRKlkrkAERELLRNADVICCTC 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564374816 773 NTSqylcqLD--LEPGFFTHILLDEAAQAMECETIMPLALATKntRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRL 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 |
6.37e-19 |
|
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in transcription, neurogenesis, and antiviral response. SEXT is an R-loop-associated protein that is thought to function as an RNA/DNA helicase. R-loops consist of RNA/DNA hybrids, formed during transcription when nascent RNA hybridizes to the DNA template strand, displacing the non-template DNA strand. Mutations in SETX are linked to two neurodegenerative disorders: ataxia with oculomotor apraxia type 2 (AOA2) and amyotrophic lateral sclerosis type 4 (ALS4). S. cerevisiae homolog splicing endonuclease 1 (Sen1) is an exclusively nuclear protein, important for nucleolar organization. S. cerevisiae Sen1 and its ortholog, the Schizosaccharomyces pombe Sen1, share conserved domains and belong to the family I class of helicases. Both proteins translocate 5' to 3' and unwind both DNA and RNA duplexes and also RNA/DNA hybrids in vitro. SETX is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438712 [Multi-domain] Cd Length: 218 Bit Score: 87.65 E-value: 6.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 642 LNAKQKEAVLAIttplCIQLPPV-LIIGPYGTGKTFTL---------------AQAVKHILQQQET---------RILIC 696
Cdd:cd18042 1 LNESQLEAIASA----LQNSPGItLIQGPPGTGKTKTIvgilsvllagkyrkyYEKVKKKLRKLQRnlnnkkkknRILVC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 697 THSNSAADLYIKDYLHPYVEAGNAQARPLRVyfrnrwVKTVHpvvhqyclissahstfQMPQKEDILKHRVVVVTLNTSQ 776
Cdd:cd18042 77 APSNAAVDEIVLRLLSEGFLDGDGRSYKPNV------VRVGR----------------QELRASILNEADIVCTTLSSSG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 777 YLcQLDLEPGFFTHILLDEAAQAMECETIMPLALATKntRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEhypAEF 856
Cdd:cd18042 135 SD-LLESLPRGFDTVIIDEAAQAVELSTLIPLRLGCK--RLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQL---AGY 208
|
250
....*....|.
gi 564374816 857 PCrILLCENYR 867
Cdd:cd18042 209 PV-LMLTTQYR 218
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
646-833 |
6.11e-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: 76.61 E-value: 6.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 646 QKEAVLAIttplCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQET------RILICTHSNSAAD----LYIKDYLHPyv 715
Cdd:pfam13086 2 QREAIRSA----LSSSHFTLIQGPPGTGKTTTIVELIRQLLSYPATsaaagpRILVCAPSNAAVDnileRLLRKGQKY-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 716 eagnaQARPLRVYFRnrwvKTVHPVVHQYCLISSAHSTFQMPQKEDILK------------------------------- 764
Cdd:pfam13086 76 -----GPKIVRIGHP----AAISEAVLPVSLDYLVESKLNNEEDAQIVKdiskeleklakalrafekeiivekllksrnk 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 765 -------------------------------------HRVVVVTLNTS--QYLCQLDlepGFFThILLDEAAQAMECETI 805
Cdd:pfam13086 147 dkskleqerrklrserkelrkelrrreqslereildeAQIVCSTLSGAgsRLLSSLA---NFDV-VIIDEAAQALEPSTL 222
|
250 260
....*....|....*....|....*...
gi 564374816 806 MPLALATKntRIVLAGDHMQLSPFVYSE 833
Cdd:pfam13086 223 IPLLRGPK--KVVLVGDPKQLPPTVISK 248
|
|
| DEXXQc_Upf1-like |
cd17934 |
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ... |
664-867 |
5.21e-14 |
|
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), coronavirus Nsp13, and similar proteins. They belong to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438708 [Multi-domain] Cd Length: 121 Bit Score: 70.34 E-value: 5.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 664 VLIIGPYGTGKTFTLAQAVKHILQQQET-RILICTHSNSAADlyikdylhpyveagNAqarplrvyfrnrwvktvhpvvh 742
Cdd:cd17934 2 SLIQGPPGTGKTTTIAAIVLQLLKGLRGkRVLVTAQSNVAVD--------------NV---------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 743 qyclissahstfqmpqkedilkhRVVVVtlntsqylcqldlepgffthillDEAAQAMECETIMPLALATKntrIVLAGD 822
Cdd:cd17934 46 -----------------------DVVII-----------------------DEASQITEPELLIALIRAKK---VVLVGD 76
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564374816 823 HMQLSPFVYSEFARE--RNLHVSLLDRLYEHYPAEFPcrILLCENYR 867
Cdd:cd17934 77 PKQLPPVVQEDHAALlgLSFILSLLLLFRLLLPGSPK--VMLDTQYR 121
|
|
| EEXXEc_NFX1 |
cd17936 |
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ... |
641-848 |
9.31e-14 |
|
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: 71.42 E-value: 9.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 641 RLNAKQKEA-VLAITTPLciqlppVLIIGPYGTGKTFTLAQAVKHILQ----QQETRILICTHSNSAADLYIKDYLhpyv 715
Cdd:cd17936 1 TLDPSQLEAlKHALTSEL------ALIQGPPGTGKTFLGVKLVRALLQnqdlSITGPILVVCYTNHALDQFLEGLL---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 716 EAGNAQArpLRVYFRnrwvktvhpVVHqyCLISSAHSTFQMPQKediLKHRVVVVtlntsqylcqldlepgffthillDE 795
Cdd:cd17936 71 DFGPTKI--VRLGAR---------VIG--MTTTGAAKYRELLQA---LGPKVVIV-----------------------EE 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564374816 796 AAQAMECETIMPLalaTKNTR-IVLAGDHMQLSPFV--YSEFARERNLHVSLLDRL 848
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 ... |
642-850 |
3.72e-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: 68.71 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 642 LNAKQKEAVL-AITTPLciqlppVLIIGPYGTGKTFTLAQAVKHILQQQETR------------ILICTHSNSAADL--- 705
Cdd:cd18040 2 LNPSQNHAVRtALTKPF------TLIQGPPGTGKTVTGVHIAYWFAKQNREIqsvsgegdggpcVLYCGPSNKSVDVvae 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 706 YIKDY-----LHPYVEAGNAQARPLRVYFRNRWVK--------------TVHPVVHQ----YC-LISSAHSTFQMPQ--- 758
Cdd:cd18040 76 LLLKVpglkiLRVYSEQIETTEYPIPNEPRHPNKKsereskpnselssiTLHHRIRQpsnpHSqQIKAFEARFERTQeki 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 759 -KEDILKHRVVV------------VTLNTsqylCQLDLEPGFFTH-----ILLDEAAQAMECETIMPLALATKNTRIVLA 820
Cdd:cd18040 156 tEEDIKTYKILIwearfeeletvdVILCT----CSEAASQKMRTHanvkqCIVDECGMCTEPESLIPIVSAPRAEQVVLI 231
|
250 260 270
....*....|....*....|....*....|
gi 564374816 821 GDHMQLSPFVYSEFARERNLHVSLLDRLYE 850
Cdd:cd18040 232 GDHKQLRPVVQNKEAQKLGLGRSLFERYAE 261
|
|
| EEXXQc_AQR |
cd17935 |
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ... |
641-848 |
6.39e-10 |
|
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds precursor-mRNA introns at a defined position and is part of a pentameric intron-binding complex (IBC). It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350693 [Multi-domain] Cd Length: 207 Bit Score: 60.90 E-value: 6.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 641 RLNAKQKEAVLAITTPLCiqlppVLIIGPYGTGKTFTLAQAVKHILQQ-QETRILICTHSNSAA-DLYIKdylhpyVEAg 718
Cdd:cd17935 5 KFTPTQIEAIRSGMQPGL-----TMVVGPPGTGKTDVAVQIISNLYHNfPNQRTLIVTHSNQALnQLFEK------IMA- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 719 naqarpLRVYFRNrwvktvhpvvhqycLISSAHSTfqmpqkedilkhRVVVVTLnTSQYLCQLDL-EPGF-FTHILLDEA 796
Cdd:cd17935 73 ------LDIDERH--------------LLRLGHGA------------KIIAMTC-THAALKRGELvELGFkYDNILMEEA 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564374816 797 AQAMECETIMPLALATKNT------RIVLAGDHMQLSPFVYS-EFARERNLHVSLLDRL 848
Cdd:cd17935 120 AQILEIETFIPLLLQNPEDgpnrlkRLIMIGDHHQLPPVIKNmAFQKYSNMEQSLFTRL 178
|
|
| DEXQc_UvrD |
cd17932 |
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch ... |
643-866 |
1.05e-08 |
|
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. UvrD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350690 [Multi-domain] Cd Length: 189 Bit Score: 57.14 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 643 NAKQKEAVLAITTPLCIqlppvlIIGPyGTGKTFTLAQAVKHILQQQET---RILICTHSNSAADlYIKDYLHPYVeaGN 719
Cdd:cd17932 1 NPEQREAVTHPDGPLLV------LAGA-GSGKTRVLTHRIAYLILEGGVppeRILAVTFTNKAAK-EMRERLRKLL--GE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 720 AQARPLrvyfrnrWVKTVHPVvhqyCL-ISSAHSTFqmpqkEDILkHRVVVVtLNTSQYLCQLDLEPgfFTHILLDEA-- 796
Cdd:cd17932 71 QLASGV-------WIGTFHSF----ALrILRRYGDF-----DDLL-LYALEL-LEENPDVREKLQSR--FRYILVDEYqd 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564374816 797 ---AQamecETIMpLALATKNTRIVLAGDHMQlSpfVYSeFareRNLHVSLLDRLYEHYPAefPCRILLCENY 866
Cdd:cd17932 131 tnpLQ----YELL-KLLAGDGKNLFVVGDDDQ-S--IYG-F---RGADPENILDFEKDFPD--AKVIKLEENY 189
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
632-1072 |
4.10e-08 |
|
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: 58.06 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 632 RQWDEQLDPRLNAKQKEAV--LAITTPLCIqlppvlIIGPYGTGKTFTLAqAVKHILQQQETRILICTHSNSAAD-LYik 708
Cdd:COG0507 115 AALEPRAGITLSDEQREAValALTTRRVSV------LTGGAGTGKTTTLR-ALLAALEALGLRVALAAPTGKAAKrLS-- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 709 dylhpyvEAGNAQARplrvyfrnrwvkTVHPVVHqyclISSAHSTFQMPQKEDILKHRVVVVtlntsqylcqldlepgff 788
Cdd:COG0507 186 -------ESTGIEAR------------TIHRLLG----LRPDSGRFRHNRDNPLTPADLLVV------------------ 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 789 thillDEA--------AQAMEcetimplALATKNTRIVLAGDHMQLSP----FVYSEFARERNLHVSLLDrlyehypaef 856
Cdd:COG0507 225 -----DEAsmvdtrlmAALLE-------ALPRAGARLILVGDPDQLPSvgagAVLRDLIESGTVPVVELT---------- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 857 pcrillcENYRSHEAI-INYTSELFYEGKlMASGKQPAHKDFYPL----------------TFFTARGEDVQ-----EKn 914
Cdd:COG0507 283 -------EVYRQADDSrIIELAHAIREGD-APEALNARYADVVFVeaedaeeaaeaivelyADRPAGGEDIQvlaptNA- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 915 STAFYN-------NAEVFEVVERVEELRRKW----PV-------AWGkLDDGSIGVVTPYADQVFRIRAELRKKRLSDVN 976
Cdd:COG0507 354 GVDALNqairealNPAGELERELAEDGELELyvgdRVmftrndyDLG-VFNGDIGTVLSIDEDEGRLTVRFDGREIVTYD 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 977 VERVLNV-----------QGKQF-RVLFLSTvrtrhtckhkqtpikkkeqlledsteDLDYGFLSNyKLLNTAITRAQSL 1044
Cdd:COG0507 433 PSELDQLelayaitvhksQGSTFdRVILVLP--------------------------SEHSPLLSR-ELLYTALTRAREL 485
|
490 500
....*....|....*....|....*...
gi 564374816 1045 VAVVGDPVALCSIgrCRKFWERFIALCH 1072
Cdd:COG0507 486 LTLVGDRDALARA--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. ... |
645-828 |
1.03e-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: 53.33 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 645 KQKEAVLAITT-PLCIqlppvlIIGPYGTGKTFTLAQAVKhILQQQETRILICTHSNSAADlyikdylhpyvEAGNAQAR 723
Cdd:cd17933 1 EQKAAVRLVLRnRVSV------LTGGAGTGKTTTLKALLA-ALEAEGKRVVLAAPTGKAAK-----------RLSESTGI 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 724 PlrvyfrnrwVKTVHPVvhqycLISSAHSTFQMPQKEDILKHRVVVVtlntsqylcqldlepgffthillDEAaqAMece 803
Cdd:cd17933 63 E---------ASTIHRL-----LGINPGGGGFYYNEENPLDADLLIV-----------------------DEA--SM--- 100
|
170 180 190
....*....|....*....|....*....|..
gi 564374816 804 tiMPLALATK-------NTRIVLAGDHMQLSP 828
Cdd:cd17933 101 --VDTRLMAAllsaipaGARLILVGDPDQLPS 130
|
|
| DEXXQc_SF1 |
cd18043 |
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ... |
643-831 |
1.90e-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: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 643 NAKQKEAVLAIttplcIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQEtRILICTHSNSAADlyikdylhpyveagnaqa 722
Cdd:cd18043 1 DSSQEAAIISA-----RNGKNVVIQGPPGTGKSQTIANIIANALARGK-RVLFVSEKKAALD------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 723 rplrvyfrnrwvktvhpVVHQYCLISSAHSTFQMpqkedilkhrvvvvtlntsqylcqLDLEPGFFTHILLDEAAQAMEC 802
Cdd:cd18043 57 -----------------VVRFPCWIMSPLSVSQY------------------------LPLNRNLFDLVIFDEASQIPIE 95
|
170 180
....*....|....*....|....*....
gi 564374816 803 ETImPLALATKntRIVLAGDHMQLSPFVY 831
Cdd:cd18043 96 EAL-PALFRGK--QVVVVGDDKQLPPSIL 121
|
|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
663-704 |
6.31e-07 |
|
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. Their helicase core is surrounded by C and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains or domains engaged in protein-protein interactions. SF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438706 [Multi-domain] Cd Length: 121 Bit Score: 50.18 E-value: 6.31e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 564374816 663 PVLIIGPYGTGKTFTLAQAVKHILQQ---QETRILICTHSNSAAD 704
Cdd:cd17914 1 LSLIQGPPGTGKTRVLVKIVAALMQNkngEPGRILLVTPTNKAAA 45
|
|
| UvrD |
COG0210 |
Superfamily I DNA or RNA helicase [Replication, recombination and repair]; |
641-703 |
5.18e-06 |
|
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
Pssm-ID: 439980 [Multi-domain] Cd Length: 721 Bit Score: 51.47 E-value: 5.18e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564374816 641 RLNAKQKEAVLAITTPLciqlppvLII-GPyGTGKTFTLAQAVKHILQQQET---RILICTHSNSAA 703
Cdd:COG0210 6 GLNPEQRAAVEHPEGPL-------LVLaGA-GSGKTRVLTHRIAYLIAEGGVdpeQILAVTFTNKAA 64
|
|
| zf-CCCH |
pfam00642 |
Zinc finger C-x8-C-x5-C-x3-H type (and similar); |
181-205 |
6.11e-06 |
|
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
Pssm-ID: 459885 [Multi-domain] Cd Length: 27 Bit Score: 44.49 E-value: 6.11e-06
|
| UvrD-helicase |
pfam00580 |
UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural ... |
642-704 |
1.78e-05 |
|
UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural domains. The Rep family function as dimers. REP helicases catalyze ATP dependent unwinding of double stranded DNA to single stranded DNA. Swiss:P23478, Swiss:P08394 have large insertions near to the carboxy-terminus relative to other members of the family.
Pssm-ID: 395462 [Multi-domain] Cd Length: 267 Bit Score: 48.40 E-value: 1.78e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564374816 642 LNAKQKEAVLAITTPLciqlppvLIIGPYGTGKTFTLAQAVKHILQQ---QETRILICTHSNSAAD 704
Cdd:pfam00580 1 LNPEQRKAVTHLGGPL-------LVLAGAGSGKTRVLTERIAYLILEggiDPEEILAVTFTNKAAR 59
|
|
| AAA_30 |
pfam13604 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
641-828 |
5.38e-05 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B.
Pssm-ID: 433343 [Multi-domain] Cd Length: 191 Bit Score: 46.02 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 641 RLNAKQKEAVLAITT-PLCIQLppvlIIGPYGTGKTFTLAqAVKHILQQQETRILICTHSNSAADLYIKDYlhpyveagN 719
Cdd:pfam13604 1 TLNAEQAAAVRALLTsGDRVAV----LVGPAGTGKTTALK-ALREAWEAAGYRVIGLAPTGRAAKVLGEEL--------G 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 720 AQARplrvyfrnrwvkTVHPVVHQYclissahstfqmPQKEDILKHRVVVVtlntsqylcqldlepgffthillDEAAQA 799
Cdd:pfam13604 68 IPAD------------TIAKLLHRL------------GGRAGLDPGTLLIV-----------------------DEAGMV 100
|
170 180 190
....*....|....*....|....*....|....
gi 564374816 800 ----MEcetiMPLALATK-NTRIVLAGDHMQLSP 828
Cdd:pfam13604 101 gtrqMA----RLLKLAEDaGARVILVGDPRQLPS 130
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
1318-1412 |
9.14e-05 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 47.77 E-value: 9.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 1318 PESRPGVVYSNTKFPRKDNLNPRHINLPLPAPHTQYAIPSRHFHPLPQLPRPPFPISQQHTLLNQQQnnlPEQPNQMTPQ 1397
Cdd:PRK10263 743 PLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQ---PVAPQPQYQQ 819
|
90
....*....|....*.
gi 564374816 1398 PNQ-VAPQPNQMAPQP 1412
Cdd:PRK10263 820 PQQpVAPQPQYQQPQQ 835
|
|
| AAA_19 |
pfam13245 |
AAA domain; |
646-704 |
4.62e-04 |
|
AAA domain;
Pssm-ID: 433059 [Multi-domain] Cd Length: 136 Bit Score: 42.21 E-value: 4.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564374816 646 QKEAVLAITTPlciqlPPVLIIGPYGTGKTFTLAQAVKHILQQQET--RILICTHSNSAAD 704
Cdd:pfam13245 1 QREAVRTALPS-----KVVLLTGGPGTGKTTTIRHIVALLVALGGVsfPILLAAPTGRAAK 56
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1243-1518 |
5.64e-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: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 1243 HGRGSPIPYglghhpPVNLGQPQNQHAEKDQQEQNRNGKTDTNNP-GPEINKIRTPEKKPTEPKqidlesnPQNRSPESR 1321
Cdd:pfam03154 272 HGQMPPMPH------SLQTGPSHMQHPVPPQPFPLTPQSSQSQVPpGPSPAAPGQSQQRIHTPP-------SQSQLQSQQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 1322 PgvvysntkfPRKDNLNPRhinlPLPAPHTQyaipsrhfhPLPQLPRPPFPISQQHTLLN--------QQQNNLPEQP-- 1391
Cdd:pfam03154 339 P---------PREQPLPPA----PLSMPHIK---------PPPTTPIPQLPNPQSHKHPPhlsgpspfQMNSNLPPPPal 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 1392 ----NQMTPQPNQVAPQPNQMAPQPNQMAPQPNQVVQQQNQAPPQAPQPAPQLSPAFQAGPTNAFFnnavahrPQSP--- 1464
Cdd:pfam03154 397 kplsSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPF-------PQHPfvp 469
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 564374816 1465 -AAEAVGPEQQVPPGLSDGHSPLRAITQPGPILASPLNNFVDESSPGLPI-EEALD 1518
Cdd:pfam03154 470 gGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIkEEALD 525
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
637-729 |
1.64e-03 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 43.47 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 637 QLDPRLNAKQKEAVLAITTPLCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQetRILICTHS----NSAADLyIKDYLH 712
Cdd:COG1061 76 GTSFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGK--RVLVLVPRrellEQWAEE-LRRFLG 152
|
90
....*....|....*..
gi 564374816 713 PYVEAGNAQARPLRVYF 729
Cdd:COG1061 153 DPLAGGGKKDSDAPITV 169
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
663-741 |
1.86e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.82 E-value: 1.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564374816 663 PVLIIGPYGTGKTfTLAQAVKHILQQQETRILICTHSNSAADLYIKDYLHPYVEAGNAQARPLRVYFRNRWVKTVHPVV 741
Cdd:smart00382 4 VILIVGPPGSGKT-TLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDV 81
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
642-796 |
2.34e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 40.73 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 642 LNAKQKEAVLAITTPLCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQ-ETRILICTHSNsaaDLY------IKDYLHPY 714
Cdd:pfam04851 4 LRPYQIEAIENLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGpIKKVLFLVPRK---DLLeqaleeFKKFLPNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 715 VEAGNaqarPLRVYFRNRWVKTVHPVVhqyclissahSTFQmpqkedilkhrvvvvTLNTSQYLCQLDLEPGFFTHILLD 794
Cdd:pfam04851 81 VEIGE----IISGDKKDESVDDNKIVV----------TTIQ---------------SLYKALELASLELLPDFFDVIIID 131
|
..
gi 564374816 795 EA 796
Cdd:pfam04851 132 EA 133
|
|
| Amelogenin |
smart00818 |
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
1330-1415 |
3.72e-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: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 1330 KFPRKDNLNPRHINLPLPAPHTqyAIPSRHFHP-LPQLPRPPFpisqqhtllnQQQNNLPEQPNQMTPQPNQVAPQPNQM 1408
Cdd:smart00818 60 VLPAQQPVVPQQPLMPVPGQHS--MTPTQHHQPnLPQPAQQPF----------QPQPLQPPQPQQPMQPQPPVHPIPPLP 127
|
....*..
gi 564374816 1409 APQPNQM 1415
Cdd:smart00818 128 PQPPLPP 134
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
1296-1499 |
6.45e-03 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 41.35 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 1296 TPEKKPTEPKQIDLESNPQNRSPESRPGVVYSNTKFPRKDNLNPRHINLPLPAPhtqyAIPSRHFHPLP-QLPRPPFPIS 1374
Cdd:PRK14086 91 SAGEPAPPPPHARRTSEPELPRPGRRPYEGYGGPRADDRPPGLPRQDQLPTARP----AYPAYQQRPEPgAWPRAADDYG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374816 1375 QQHTLLNQQQNNLPEQPNQMTPQPNQVAPQPNQMAPQPNQMAPQPNQvvqqqnqappqapqpapqlsPAFQAGPTNAFFN 1454
Cdd:PRK14086 167 WQQQRLGFPPRAPYASPASYAPEQERDREPYDAGRPEYDQRRRDYDH--------------------PRPDWDRPRRDRT 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564374816 1455 NavahRPQ-SPAAEAVGPEQQVPPGLSDGHSPLRAITQPGPILASP 1499
Cdd:PRK14086 227 D----RPEpPPGAGHVHRGGPGPPERDDAPVVPIRPSAPGPLAAQP 268
|
|
| |
