|
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 1046848940 658 RLNAKQKEAVLAITTPLCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETsRILICTHSNSAADLYIKDYLHPYVEAGN 737
Cdd:cd18077 1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPET-RILICTHSNSAADLYIKEYLHPYVETGN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 738 AQARPLRVYFRNRWVKTVHPVVHQYCLISsAHSTFQMPQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQA 817
Cdd:cd18077 80 PRARPLRVYYRNRWVKTVHPVVQKYCLID-EHGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046848940 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 1046848940 783 HRVVVVTLNTSQYLcqLDLEPGFFTHILLDEAAQAMECETIMPLALATkntRIVLAGDHMQLSPFV---YSEFARERNLH 859
Cdd:COG1112 535 APVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVfgeEAEEVAEEGLD 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 860 VSLLDRLYEHYPaefPCRILLCENYRSHEAIINYTSELFYEGKLMA---SGKQPAHKDFYPLTFFTARGedVQEKNSTAF 936
Cdd:COG1112 610 ESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDG--VYERRGGSR 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 937 YNnaevfevverveelrrkwP------VAW------GKLDDGSIGVVTPYADQVFRIRAELRKKRLSDV------NVERv 998
Cdd:COG1112 685 TN------------------PeeaeavVELvrelleDGPDGESIGVITPYRAQVALIRELLREALGDGLepvfvgTVDR- 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 999 lnVQGKQFRVLFLSTVRTRhtckhkqtpikkkeqlleDSTEDLDYGFLS-NYKLLNTAITRAQSLVAVVGDPvALCSIGR 1077
Cdd:COG1112 746 --FQGDERDVIIFSLVYSN------------------DEDVPRNFGFLNgGPRRLNVAVSRARRKLIVVGSR-ELLDSDP 804
|
330
....*....|....*
gi 1046848940 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 1046848940 886 SHEAIINYTSELFYEGKLMAS-------GKQPAHKDFYPLTFFTARGEDVQEKNSTAFYNNAEVFEVVERVEELRRKWpv 958
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKAGvsvaarlNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 959 awgkLDDGSIGVVTPYADQVFRIRAELRKKR--LSDVNVERVLNVQGKQFRVLFLSTVRTRHTCKHkqtpikkkeqlled 1036
Cdd:cd18808 79 ----VKPSSIGVITPYRAQVALIRELLRKRGglLEDVEVGTVDNFQGREKDVIILSLVRSNESGGS-------------- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1046848940 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 1046848940 858 LHVSLLDRLYEHYPAefpCRILLCENYRSHEAIINYTSELFYEGKLMASGKQPAH---------KDFYPLTFF-TARGED 927
Cdd:pfam13087 1 LDRSLFERLQELGPS---AVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERplpddfhlpDPLGPLVFIdVDGSEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 928 VQEKNSTAFYNNAEVFEVVERVEELRRKWPVAWGKlddgsIGVVTPYADQVFRIRAELRKKRLSDVNVErVLNV---QGK 1004
Cdd:pfam13087 78 EESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSD-----IGVITPYRAQVRLIRKLLKRKLGGKLEIE-VNTVdgfQGR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046848940 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 1046848940 663 QKEAVLAIttplCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETS-----RILICTHSNSAAD----LYIKDYLHPyv 733
Cdd:pfam13086 2 QREAIRSA----LSSSHFTLIQGPPGTGKTTTIVELIRQLLSYPATSaaagpRILVCAPSNAAVDnileRLLRKGQKY-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 734 eagnaQARPLRVYFRnrwvKTVHPVVHQYCLISSAHSTFQMPQKEDILK------------------------------- 782
Cdd:pfam13086 76 -----GPKIVRIGHP----AAISEAVLPVSLDYLVESKLNNEEDAQIVKdiskeleklakalrafekeiivekllksrnk 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 783 -------------------------------------HRVVVVTLNTS--QYLCQLDlepGFFThILLDEAAQAMECETI 823
Cdd:pfam13086 147 dkskleqerrklrserkelrkelrrreqslereildeAQIVCSTLSGAgsRLLSSLA---NFDV-VIIDEAAQALEPSTL 222
|
250 260
....*....|....*....|....*...
gi 1046848940 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 1046848940 649 RQWDEQLDPRLNAKQKEAV--LAITTPLCIqlppvlIIGPYGTGKTFTLAQAVKHILQQQEtsRILICTHSNSAAD-LYi 725
Cdd:COG0507 115 AALEPRAGITLSDEQREAValALTTRRVSV------LTGGAGTGKTTTLRALLAALEALGL--RVALAAPTGKAAKrLS- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 726 kdylhpyvEAGNAQARplrvyfrnrwvkTVHPVVHqyclISSAHSTFQMPQKEDILKHRVVVVtlntsqylcqldlepgf 805
Cdd:COG0507 186 --------ESTGIEAR------------TIHRLLG----LRPDSGRFRHNRDNPLTPADLLVV----------------- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 806 fthillDEA--------AQAMEcetimplALATKNTRIVLAGDHMQLSP----FVYSEFARERNLHVSLLDrlyehypae 873
Cdd:COG0507 225 ------DEAsmvdtrlmAALLE-------ALPRAGARLILVGDPDQLPSvgagAVLRDLIESGTVPVVELT--------- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 874 fpcrillcENYRSHEAI-INYTSELFYEGKlMASGKQPAHKDFYPL----------------TFFTARGEDVQ-----EK 931
Cdd:COG0507 283 --------EVYRQADDSrIIELAHAIREGD-APEALNARYADVVFVeaedaeeaaeaivelyADRPAGGEDIQvlaptNA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 932 nSTAFYN-------NAEVFEVVERVEELRRKW----PV-------AWGkLDDGSIGVVTPYADQVFRIRAELRKKRLSDV 993
Cdd:COG0507 354 -GVDALNqairealNPAGELERELAEDGELELyvgdRVmftrndyDLG-VFNGDIGTVLSIDEDEGRLTVRFDGREIVTY 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 994 NVERVLNV-----------QGKQF-RVLFLSTvrtrhtckhkqtpikkkeqlledsteDLDYGFLSNyKLLNTAITRAQS 1061
Cdd:COG0507 432 DPSELDQLelayaitvhksQGSTFdRVILVLP--------------------------SEHSPLLSR-ELLYTALTRARE 484
|
490 500
....*....|....*....|....*....
gi 1046848940 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
|
| 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 1046848940 1336 PESRPGVVYSNTKFPRKDNLNPRHINLPLPAPHTQYAIPSRHFHPLPQLPRPPFPISQQHTLLNQQQnnlPEQPNQMTPQ 1415
Cdd:PRK10263 743 PLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQ---PVAPQPQYQQ 819
|
90
....*....|....*.
gi 1046848940 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 1046848940 1261 HGRGSPIPYglghhpPVNLGQPQNQHAEKDQQEQNRNGKTDTNNP-GPEINKIRTPEKKPTEPKqidlesnPQNRSPESR 1339
Cdd:pfam03154 272 HGQMPPMPH------SLQTGPSHMQHPVPPQPFPLTPQSSQSQVPpGPSPAAPGQSQQRIHTPP-------SQSQLQSQQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 1340 PgvvysntkfPRKDNLNPRhinlPLPAPHTQyaipsrhfhPLPQLPRPPFPISQQHTLLN--------QQQNNLPEQP-- 1409
Cdd:pfam03154 339 P---------PREQPLPPA----PLSMPHIK---------PPPTTPIPQLPNPQSHKHPPhlsgpspfQMNSNLPPPPal 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 1410 ----NQMTPQPNQVAPQPNQMAPQPNQMAPQPNQVVQQQNQAPPQAPQPAPQLSPAFQAGPTNAFFnnavahrPQSP--- 1482
Cdd:pfam03154 397 kplsSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPF-------PQHPfvp 469
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1046848940 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 1046848940 1348 KFPRKDNLNPRHINLPLPAPHTqyAIPSRHFHP-LPQLPRPPFpisqqhtllnQQQNNLPEQPNQMTPQPNQVAPQPNQM 1426
Cdd:smart00818 60 VLPAQQPVVPQQPLMPVPGQHS--MTPTQHHQPnLPQPAQQPF----------QPQPLQPPQPQQPMQPQPPVHPIPPLP 127
|
....*..
gi 1046848940 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 1046848940 1314 TPEKKPTEPKQIDLESNPQNRSPESRPGVVYSNTKFPRKDNLNPRHINLPLPAPhtqyAIPSRHFHPLP-QLPRPPFPIS 1392
Cdd:PRK14086 91 SAGEPAPPPPHARRTSEPELPRPGRRPYEGYGGPRADDRPPGLPRQDQLPTARP----AYPAYQQRPEPgAWPRAADDYG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 1393 QQHTLLNQQQNNLPEQPNQMTPQPNQVAPQPNQMAPQPNQMAPQPNQvvqqqnqappqapqpapqlsPAFQAGPTNAFFN 1472
Cdd:PRK14086 167 WQQQRLGFPPRAPYASPASYAPEQERDREPYDAGRPEYDQRRRDYDH--------------------PRPDWDRPRRDRT 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1046848940 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 1046848940 658 RLNAKQKEAVLAITTPLCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETsRILICTHSNSAADLYIKDYLHPYVEAGN 737
Cdd:cd18077 1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPET-RILICTHSNSAADLYIKEYLHPYVETGN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 738 AQARPLRVYFRNRWVKTVHPVVHQYCLISsAHSTFQMPQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQA 817
Cdd:cd18077 80 PRARPLRVYYRNRWVKTVHPVVQKYCLID-EHGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046848940 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 1046848940 658 RLNAKQKEAVLAITTPLCiQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETSRILICTHSNSAADLYIKDYLHPYVEagn 737
Cdd:cd18038 1 ELNDEQKLAVRNIVTGTS-RPPPYIIFGPPGTGKTVTLVEAILQVLRQPPEARILVCAPSNSAADLLAERLLNALVT--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 738 aQARPLRVYFRNRWVKTVHPVVHQYClISSAHSTFQMPQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQA 817
Cdd:cd18038 77 -KREILRLNAPSRDRASVPPELLPYC-NSKAEGTFRLPSLEELKKYRIVVCTLMTAGRLVQAGVPNGHFTHIFIDEAGQA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046848940 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 1046848940 658 RLNAKQKEAVLAIT--TPLCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETsRILICTHSNSAADLYIKDYLHPYVEA 735
Cdd:cd18076 1 AGNNKQQLAFNFIAgkPSEARFVPPLLIYGPFGTGKTFTLAMAALEVIREPGT-KVLICTHTNSAADIYIREYFHPYVDK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 736 GNAQARPLRVYFRNRWVKTVHPVVHQYCLISSAHSTFQMPQKEDILKHRVVVVTLNTSQylcQLDLEPGFFTHILLDEAA 815
Cdd:cd18076 80 GHPEARPLRIKATDRPNAITDPDTITYCCLTKDRQCFRLPTRDELDFHNIVITTTAMAF---NLHVLSGFFTHIFIDEAA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046848940 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 1046848940 659 LNAKQKEAVLAITTPLCIQLPPVlIIGPYGTGKTFTLAQAVKHILQQQETSRILICTHSNSAADLYIKDyLHPYVEAGNA 738
Cdd:cd18078 2 LNELQKEAVKRILGGECRPLPYI-LFGPPGTGKTVTIIEAILQVVYNLPRSRILVCAPSNSAADLVTSR-LHESKVLKPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 739 QARPLRVYfrNRWVKTVHPVVHQYCLISSahstfqmpQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQAM 818
Cdd:cd18078 80 DMVRLNAV--NRFESTVIDARKLYCRLGE--------DLSKASRHRIVISTCSTAGLLYQMGLPVGHFTHVFVDEAGQAT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 819 ECETIMPLALATKNT-RIVLAGDHMQLSPFVYSEFARERNLHVSLLDRL-----YEHYPAEFP-CRIL-------LCENY 884
Cdd:cd18078 150 EPESLIPLGLISSRDgQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLmnrplYLRDPNRFGeSGGYnpllvtkLVDNY 229
|
.
gi 1046848940 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 1046848940 783 HRVVVVTLNTSQYLcqLDLEPGFFTHILLDEAAQAMECETIMPLALATkntRIVLAGDHMQLSPFV---YSEFARERNLH 859
Cdd:COG1112 535 APVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVfgeEAEEVAEEGLD 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 860 VSLLDRLYEHYPaefPCRILLCENYRSHEAIINYTSELFYEGKLMA---SGKQPAHKDFYPLTFFTARGedVQEKNSTAF 936
Cdd:COG1112 610 ESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDG--VYERRGGSR 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 937 YNnaevfevverveelrrkwP------VAW------GKLDDGSIGVVTPYADQVFRIRAELRKKRLSDV------NVERv 998
Cdd:COG1112 685 TN------------------PeeaeavVELvrelleDGPDGESIGVITPYRAQVALIRELLREALGDGLepvfvgTVDR- 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 999 lnVQGKQFRVLFLSTVRTRhtckhkqtpikkkeqlleDSTEDLDYGFLS-NYKLLNTAITRAQSLVAVVGDPvALCSIGR 1077
Cdd:COG1112 746 --FQGDERDVIIFSLVYSN------------------DEDVPRNFGFLNgGPRRLNVAVSRARRKLIVVGSR-ELLDSDP 804
|
330
....*....|....*
gi 1046848940 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 1046848940 886 SHEAIINYTSELFYEGKLMAS-------GKQPAHKDFYPLTFFTARGEDVQEKNSTAFYNNAEVFEVVERVEELRRKWpv 958
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKAGvsvaarlNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 959 awgkLDDGSIGVVTPYADQVFRIRAELRKKR--LSDVNVERVLNVQGKQFRVLFLSTVRTRHTCKHkqtpikkkeqlled 1036
Cdd:cd18808 79 ----VKPSSIGVITPYRAQVALIRELLRKRGglLEDVEVGTVDNFQGREKDVIILSLVRSNESGGS-------------- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1046848940 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 1046848940 858 LHVSLLDRLYEHYPAefpCRILLCENYRSHEAIINYTSELFYEGKLMASGKQPAH---------KDFYPLTFF-TARGED 927
Cdd:pfam13087 1 LDRSLFERLQELGPS---AVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERplpddfhlpDPLGPLVFIdVDGSEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 928 VQEKNSTAFYNNAEVFEVVERVEELRRKWPVAWGKlddgsIGVVTPYADQVFRIRAELRKKRLSDVNVErVLNV---QGK 1004
Cdd:pfam13087 78 EESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSD-----IGVITPYRAQVRLIRKLLKRKLGGKLEIE-VNTVdgfQGR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046848940 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 1046848940 658 RLNAKQKEAVLAITTPLCIqlppVLIIGPYGTGKTFTLAQAVKhILQQQETSrILICTHSNSAAD---LYIKDYLHPYVE 734
Cdd:cd18041 1 GLNKDQRQAIKKVLNAKDY----ALILGMPGTGKTTTIAALVR-ILVALGKS-VLLTSYTHSAVDnilLKLKKFGVNFLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 735 AGNAqarplrvyfrnrwvKTVHPVVHQYCLISSAHSTFQMPQKEDIL-KHRVVVVTL--NTSQYLCQldlepGFFTHILL 811
Cdd:cd18041 75 LGRL--------------KKIHPDVQEFTLEAILKSCKSVEELESKYeSVSVVATTClgINHPIFRR-----RTFDYCIV 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 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 1046848940 658 RLNAKQKEAVLaittpLCIQLPPVLII-GPYGTGKTFTLAQAVKHILQQQEtsRILICTHSNSAADlYIKDYLhpyveag 736
Cdd:cd18044 1 NLNDSQKEAVK-----FALSQKDVALIhGPPGTGKTTTVVEIILQAVKRGE--KVLACAPSNIAVD-NLVERL------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 737 naQARPLRVyfrnrwVKTVHPV-----VHQYCLissahstfqmpqkEDILKHRVVVVTLNTSqylCQLDLEPG-FFTHIL 810
Cdd:cd18044 66 --VALKVKV------VRIGHPArllesVLDHSL-------------DALVAAQVVLATNTGA---GSRQLLPNeLFDVVV 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046848940 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 1046848940 659 LNAKQKEAV-LAITTPLCiqlppvLIIGPYGTGKTFTLAQAVKHILQQQEtSRILICTHSNSAADlYIKDYLHpyveagN 737
Cdd:cd18039 2 LNHSQVDAVkTALQRPLS------LIQGPPGTGKTVTSATIVYHLVKQGN-GPVLVCAPSNVAVD-QLTEKIH------Q 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 738 AQARPLRVYFRNRW-----VK--TVHPVVHQY-----------------CLISSAHSTFQM----PQKEDILKHRVVVVT 789
Cdd:cd18039 68 TGLKVVRLCAKSREavespVSflALHNQVRNLdsaeklellkllkletgELSSADEKRYRKlkrkAERELLRNADVICCT 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046848940 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 1046848940 659 LNAKQKEAVLAIttplCIQLPPV-LIIGPYGTGKTFTL---------------AQAVKHILQQQETS--------RILIC 714
Cdd:cd18042 1 LNESQLEAIASA----LQNSPGItLIQGPPGTGKTKTIvgilsvllagkyrkyYEKVKKKLRKLQRNlnnkkkknRILVC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 715 THSNSAADLYIKDYLHPYVEAGNAQARPLRVyfrnrwVKTVHpvvhqyclissahstfQMPQKEDILKHRVVVVTLNTSQ 794
Cdd:cd18042 77 APSNAAVDEIVLRLLSEGFLDGDGRSYKPNV------VRVGR----------------QELRASILNEADIVCTTLSSSG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 795 YLcQLDLEPGFFTHILLDEAAQAMECETIMPLALATKntRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEhypAEF 874
Cdd:cd18042 135 SD-LLESLPRGFDTVIIDEAAQAVELSTLIPLRLGCK--RLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQL---AGY 208
|
250
....*....|.
gi 1046848940 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 1046848940 681 VLIIGPYGTGKTFTLAQAVKHILQQQETSRILICTHSNSAADlyikdylhpyveagNAqarplrvyfrnrwvktvhpvvh 760
Cdd:cd17934 2 SLIQGPPGTGKTTTIAAIVLQLLKGLRGKRVLVTAQSNVAVD--------------NV---------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 761 qyclissahstfqmpqkedilkhRVVVVtlntsqylcqldlepgffthillDEAAQAMECETIMPLALATKntrIVLAGD 840
Cdd:cd17934 46 -----------------------DVVII-----------------------DEASQITEPELLIALIRAKK---VVLVGD 76
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1046848940 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 1046848940 663 QKEAVLAIttplCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETS-----RILICTHSNSAAD----LYIKDYLHPyv 733
Cdd:pfam13086 2 QREAIRSA----LSSSHFTLIQGPPGTGKTTTIVELIRQLLSYPATSaaagpRILVCAPSNAAVDnileRLLRKGQKY-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 734 eagnaQARPLRVYFRnrwvKTVHPVVHQYCLISSAHSTFQMPQKEDILK------------------------------- 782
Cdd:pfam13086 76 -----GPKIVRIGHP----AAISEAVLPVSLDYLVESKLNNEEDAQIVKdiskeleklakalrafekeiivekllksrnk 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 783 -------------------------------------HRVVVVTLNTS--QYLCQLDlepGFFThILLDEAAQAMECETI 823
Cdd:pfam13086 147 dkskleqerrklrserkelrkelrrreqslereildeAQIVCSTLSGAgsRLLSSLA---NFDV-VIIDEAAQALEPSTL 222
|
250 260
....*....|....*....|....*...
gi 1046848940 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 1046848940 658 RLNAKQKEA-VLAITTPLciqlppVLIIGPYGTGKTFTLAQAVKHILQ---QQETSRILICTHSNSAADLYIKDYLhpyv 733
Cdd:cd17936 1 TLDPSQLEAlKHALTSEL------ALIQGPPGTGKTFLGVKLVRALLQnqdLSITGPILVVCYTNHALDQFLEGLL---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 734 EAGNAQArpLRVYFRnrwvktvhpVVHqyCLISSAHSTFQMPQKediLKHRVVVVtlntsqylcqldlepgffthillDE 813
Cdd:cd17936 71 DFGPTKI--VRLGAR---------VIG--MTTTGAAKYRELLQA---LGPKVVIV-----------------------EE 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1046848940 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 1046848940 659 LNAKQKEAVL-AITTPLciqlppVLIIGPYGTGKTFTLAQAVKHILQQQETSR-----------ILICTHSNSAADL--- 723
Cdd:cd18040 2 LNPSQNHAVRtALTKPF------TLIQGPPGTGKTVTGVHIAYWFAKQNREIQsvsgegdggpcVLYCGPSNKSVDVvae 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 724 YIKDY-----LHPYVEAGNAQARPLRVYFRNRWVK--------------TVHPVVHQ----YC-LISSAHSTFQMPQ--- 776
Cdd:cd18040 76 LLLKVpglkiLRVYSEQIETTEYPIPNEPRHPNKKsereskpnselssiTLHHRIRQpsnpHSqQIKAFEARFERTQeki 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 777 -KEDILKHRVVV------------VTLNTsqylCQLDLEPGFFTH-----ILLDEAAQAMECETIMPLALATKNTRIVLA 838
Cdd:cd18040 156 tEEDIKTYKILIwearfeeletvdVILCT----CSEAASQKMRTHanvkqCIVDECGMCTEPESLIPIVSAPRAEQVVLI 231
|
250 260 270
....*....|....*....|....*....|
gi 1046848940 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 1046848940 658 RLNAKQKEAVLAITTPLCiqlppVLIIGPYGTGKTFTLAQAVKHILQQQETSRILICTHSNSAA-DLYIKdylhpyVEAg 736
Cdd:cd17935 5 KFTPTQIEAIRSGMQPGL-----TMVVGPPGTGKTDVAVQIISNLYHNFPNQRTLIVTHSNQALnQLFEK------IMA- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 737 naqarpLRVYFRNrwvktvhpvvhqycLISSAHSTfqmpqkedilkhRVVVVTLnTSQYLCQLDL-EPGF-FTHILLDEA 814
Cdd:cd17935 73 ------LDIDERH--------------LLRLGHGA------------KIIAMTC-THAALKRGELvELGFkYDNILMEEA 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1046848940 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 1046848940 660 NAKQKEAVLAITTPLCIqlppvlIIGPyGTGKTFTLAQAVKHILQQQET--SRILICTHSNSAADlYIKDYLHPYVeaGN 737
Cdd:cd17932 1 NPEQREAVTHPDGPLLV------LAGA-GSGKTRVLTHRIAYLILEGGVppERILAVTFTNKAAK-EMRERLRKLL--GE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 738 AQARPLrvyfrnrWVKTVHPVvhqyCL-ISSAHSTFqmpqkEDILkHRVVVVtLNTSQYLCQLDLEPgfFTHILLDEA-- 814
Cdd:cd17932 71 QLASGV-------WIGTFHSF----ALrILRRYGDF-----DDLL-LYALEL-LEENPDVREKLQSR--FRYILVDEYqd 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046848940 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 1046848940 660 NAKQKEAVLAIttplcIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQEtsRILICTHSNSAADlyikdylhpyveagnaq 739
Cdd:cd18043 1 DSSQEAAIISA-----RNGKNVVIQGPPGTGKSQTIANIIANALARGK--RVLFVSEKKAALD----------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 740 arplrvyfrnrwvktvhpVVHQYCLISSAHSTFQMpqkedilkhrvvvvtlntsqylcqLDLEPGFFTHILLDEAAQAME 819
Cdd:cd18043 57 ------------------VVRFPCWIMSPLSVSQY------------------------LPLNRNLFDLVIFDEASQIPI 94
|
170 180 190
....*....|....*....|....*....|
gi 1046848940 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 1046848940 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 1046848940 649 RQWDEQLDPRLNAKQKEAV--LAITTPLCIqlppvlIIGPYGTGKTFTLAQAVKHILQQQEtsRILICTHSNSAAD-LYi 725
Cdd:COG0507 115 AALEPRAGITLSDEQREAValALTTRRVSV------LTGGAGTGKTTTLRALLAALEALGL--RVALAAPTGKAAKrLS- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 726 kdylhpyvEAGNAQARplrvyfrnrwvkTVHPVVHqyclISSAHSTFQMPQKEDILKHRVVVVtlntsqylcqldlepgf 805
Cdd:COG0507 186 --------ESTGIEAR------------TIHRLLG----LRPDSGRFRHNRDNPLTPADLLVV----------------- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 806 fthillDEA--------AQAMEcetimplALATKNTRIVLAGDHMQLSP----FVYSEFARERNLHVSLLDrlyehypae 873
Cdd:COG0507 225 ------DEAsmvdtrlmAALLE-------ALPRAGARLILVGDPDQLPSvgagAVLRDLIESGTVPVVELT--------- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 874 fpcrillcENYRSHEAI-INYTSELFYEGKlMASGKQPAHKDFYPL----------------TFFTARGEDVQ-----EK 931
Cdd:COG0507 283 --------EVYRQADDSrIIELAHAIREGD-APEALNARYADVVFVeaedaeeaaeaivelyADRPAGGEDIQvlaptNA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 932 nSTAFYN-------NAEVFEVVERVEELRRKW----PV-------AWGkLDDGSIGVVTPYADQVFRIRAELRKKRLSDV 993
Cdd:COG0507 354 -GVDALNqairealNPAGELERELAEDGELELyvgdRVmftrndyDLG-VFNGDIGTVLSIDEDEGRLTVRFDGREIVTY 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 994 NVERVLNV-----------QGKQF-RVLFLSTvrtrhtckhkqtpikkkeqlledsteDLDYGFLSNyKLLNTAITRAQS 1061
Cdd:COG0507 432 DPSELDQLelayaitvhksQGSTFdRVILVLP--------------------------SEHSPLLSR-ELLYTALTRARE 484
|
490 500
....*....|....*....|....*....
gi 1046848940 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 1046848940 662 KQKEAVLAITT-PLCIqlppvlIIGPYGTGKTFTLAQAVKHIlqQQETSRILICTHSNSAADlyikdylhpyvEAGNAQA 740
Cdd:cd17933 1 EQKAAVRLVLRnRVSV------LTGGAGTGKTTTLKALLAAL--EAEGKRVVLAAPTGKAAK-----------RLSESTG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 741 RPlrvyfrnrwVKTVHPVvhqycLISSAHSTFQMPQKEDILKHRVVVVtlntsqylcqldlepgffthillDEAaqAMec 820
Cdd:cd17933 62 IE---------ASTIHRL-----LGINPGGGGFYYNEENPLDADLLIV-----------------------DEA--SM-- 100
|
170 180 190
....*....|....*....|....*....|...
gi 1046848940 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 1046848940 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
|
| 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 1046848940 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 1046848940 1336 PESRPGVVYSNTKFPRKDNLNPRHINLPLPAPHTQYAIPSRHFHPLPQLPRPPFPISQQHTLLNQQQnnlPEQPNQMTPQ 1415
Cdd:PRK10263 743 PLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQ---PVAPQPQYQQ 819
|
90
....*....|....*.
gi 1046848940 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 1046848940 658 RLNAKQKEAVLAITT-PLCIQLppvlIIGPYGTGKTFTLAQAVKHIlqQQETSRILICTHSNSAADLYIKDYlhpyveag 736
Cdd:pfam13604 1 TLNAEQAAAVRALLTsGDRVAV----LVGPAGTGKTTALKALREAW--EAAGYRVIGLAPTGRAAKVLGEEL-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 737 NAQARplrvyfrnrwvkTVHPVVHQYclissahstfqmPQKEDILKHRVVVVtlntsqylcqldlepgffthillDEAAQ 816
Cdd:pfam13604 67 GIPAD------------TIAKLLHRL------------GGRAGLDPGTLLIV-----------------------DEAGM 99
|
170 180 190
....*....|....*....|....*....|....*
gi 1046848940 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 1046848940 659 LNAKQKEAVLAITTPLCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETSRILICTHSNsaaDLY------IKDYLHPY 732
Cdd:pfam04851 4 LRPYQIEAIENLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRK---DLLeqaleeFKKFLPNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 733 VEAGNaqarPLRVYFRNRWVKTVHPVVhqyclissahSTFQmpqkedilkhrvvvvTLNTSQYLCQLDLEPGFFTHILLD 812
Cdd:pfam04851 81 VEIGE----IISGDKKDESVDDNKIVV----------TTIQ---------------SLYKALELASLELLPDFFDVIIID 131
|
..
gi 1046848940 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 1046848940 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 1046848940 1261 HGRGSPIPYglghhpPVNLGQPQNQHAEKDQQEQNRNGKTDTNNP-GPEINKIRTPEKKPTEPKqidlesnPQNRSPESR 1339
Cdd:pfam03154 272 HGQMPPMPH------SLQTGPSHMQHPVPPQPFPLTPQSSQSQVPpGPSPAAPGQSQQRIHTPP-------SQSQLQSQQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 1340 PgvvysntkfPRKDNLNPRhinlPLPAPHTQyaipsrhfhPLPQLPRPPFPISQQHTLLN--------QQQNNLPEQP-- 1409
Cdd:pfam03154 339 P---------PREQPLPPA----PLSMPHIK---------PPPTTPIPQLPNPQSHKHPPhlsgpspfQMNSNLPPPPal 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 1410 ----NQMTPQPNQVAPQPNQMAPQPNQMAPQPNQVVQQQNQAPPQAPQPAPQLSPAFQAGPTNAFFnnavahrPQSP--- 1482
Cdd:pfam03154 397 kplsSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPF-------PQHPfvp 469
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1046848940 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 1046848940 654 QLDPRLNAKQKEAVLAITTPLCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQetsRILICTHS----NSAADLyIKDYL 729
Cdd:COG1061 76 GTSFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGK---RVLVLVPRrellEQWAEE-LRRFL 151
|
90
....*....|....*...
gi 1046848940 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 1046848940 1348 KFPRKDNLNPRHINLPLPAPHTqyAIPSRHFHP-LPQLPRPPFpisqqhtllnQQQNNLPEQPNQMTPQPNQVAPQPNQM 1426
Cdd:smart00818 60 VLPAQQPVVPQQPLMPVPGQHS--MTPTQHHQPnLPQPAQQPF----------QPQPLQPPQPQQPMQPQPPVHPIPPLP 127
|
....*..
gi 1046848940 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 1046848940 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 1046848940 1314 TPEKKPTEPKQIDLESNPQNRSPESRPGVVYSNTKFPRKDNLNPRHINLPLPAPhtqyAIPSRHFHPLP-QLPRPPFPIS 1392
Cdd:PRK14086 91 SAGEPAPPPPHARRTSEPELPRPGRRPYEGYGGPRADDRPPGLPRQDQLPTARP----AYPAYQQRPEPgAWPRAADDYG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046848940 1393 QQHTLLNQQQNNLPEQPNQMTPQPNQVAPQPNQMAPQPNQMAPQPNQvvqqqnqappqapqpapqlsPAFQAGPTNAFFN 1472
Cdd:PRK14086 167 WQQQRLGFPPRAPYASPASYAPEQERDREPYDAGRPEYDQRRRDYDH--------------------PRPDWDRPRRDRT 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1046848940 1473 NavahRPQ-SPAAEAVGPEQQVPPGLSDGHSPLRAITQPGPILASP 1517
Cdd:PRK14086 227 D----RPEpPPGAGHVHRGGPGPPERDDAPVVPIRPSAPGPLAAQP 268
|
|
| |
