|
Name |
Accession |
Description |
Interval |
E-value |
| DEXXQc_HELZ |
cd18077 |
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ... |
641-868 |
2.48e-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: 465.42 E-value: 2.48e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 641 RLNAKQKEAVLAITTPLCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETsRILICTHSNSAADLYIKDYLHPYVEAGN 720
Cdd:cd18077 1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPET-RILICTHSNSAADLYIKEYLHPYVETGN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 721 AQARPLRVYFRNRWVKTVHPVVHQYCLISsAHSTFQMPQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQA 800
Cdd:cd18077 80 PRARPLRVYYRNRWVKTVHPVVQKYCLID-EHGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164663913 801 MECETIMPLALATKNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEFPCRILLCENYR 868
Cdd:cd18077 159 MECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSEHPCRILLCENYR 226
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
766-1075 |
9.20e-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: 9.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 766 HRVVVVTLNTSQYLcqLDLEPGFFTHILLDEAAQAMECETIMPLALATkntRIVLAGDHMQLSPFV---YSEFARERNLH 842
Cdd:COG1112 535 APVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVfgeEAEEVAEEGLD 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 843 VSLLDRLYEHYPaefPCRILLCENYRSHEAIINYTSELFYEGKLMA---SGKQPAHKDFYPLTFFTARGedVQEKNSTAF 919
Cdd:COG1112 610 ESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDG--VYERRGGSR 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 920 YNnaevfevverveelrrkwP------VAW------GKLDDGSIGVVTPYADQVFRIRAELRKKRLSDV------NVERv 981
Cdd:COG1112 685 TN------------------PeeaeavVELvrelleDGPDGESIGVITPYRAQVALIRELLREALGDGLepvfvgTVDR- 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 982 lnVQGKQFRVLFLSTVRTRhtckhkqtpikkkeqlleDSTEDLDYGFLS-NYKLLNTAITRAQSLVAVVGDPvALCSIGR 1060
Cdd:COG1112 746 --FQGDERDVIIFSLVYSN------------------DEDVPRNFGFLNgGPRRLNVAVSRARRKLIVVGSR-ELLDSDP 804
|
330
....*....|....*
gi 164663913 1061 CRKFWERFIALCHEN 1075
Cdd:COG1112 805 STPALKRLLEYLERA 819
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
869-1069 |
6.36e-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: 6.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 869 SHEAIINYTSELFYEGKLMAS-------GKQPAHKDFYPLTFFTARGEDVQEKNSTAFYNNAEVFEVVERVEELRRKWpv 941
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKAGvsvaarlNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 942 awgkLDDGSIGVVTPYADQVFRIRAELRKKR--LSDVNVERVLNVQGKQFRVLFLSTVRTRHTCKHkqtpikkkeqlled 1019
Cdd:cd18808 79 ----VKPSSIGVITPYRAQVALIRELLRKRGglLEDVEVGTVDNFQGREKDVIILSLVRSNESGGS-------------- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 164663913 1020 stedldYGFLSNYKLLNTAITRAQSLVAVVGDPVALCSIGRCRKFWERFI 1069
Cdd:cd18808 141 ------IGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
841-1052 |
4.88e-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 164663913 841 LHVSLLDRLYEHYPAefpCRILLCENYRSHEAIINYTSELFYEGKLMASGKQPAH---------KDFYPLTFF-TARGED 910
Cdd:pfam13087 1 LDRSLFERLQELGPS---AVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERplpddfhlpDPLGPLVFIdVDGSEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 911 VQEKNSTAFYNNAEVFEVVERVEELRRKWPVAWGKlddgsIGVVTPYADQVFRIRAELRKKRLSDVNVErVLNV---QGK 987
Cdd:pfam13087 78 EESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSD-----IGVITPYRAQVRLIRKLLKRKLGGKLEIE-VNTVdgfQGR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164663913 988 QFRVLFLSTVRtrhtckhkqtpikkkeqlledSTEDLDYGFLSNYKLLNTAITRAQSLVAVVGDP 1052
Cdd:pfam13087 152 EKDVIIFSCVR---------------------SNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNA 195
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
646-834 |
3.05e-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: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 646 QKEAVLAIttplCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETS-----RILICTHSNSAAD----LYIKDYLHPyv 716
Cdd:pfam13086 2 QREAIRSA----LSSSHFTLIQGPPGTGKTTTIVELIRQLLSYPATSaaagpRILVCAPSNAAVDnileRLLRKGQKY-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 717 eagnaQARPLRVYFRnrwvKTVHPVVHQYCLISSAHSTFQMPQKEDILK------------------------------- 765
Cdd:pfam13086 76 -----GPKIVRIGHP----AAISEAVLPVSLDYLVESKLNNEEDAQIVKdiskeleklakalrafekeiivekllksrnk 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 766 -------------------------------------HRVVVVTLNTS--QYLCQLDlepGFFThILLDEAAQAMECETI 806
Cdd:pfam13086 147 dkskleqerrklrserkelrkelrrreqslereildeAQIVCSTLSGAgsRLLSSLA---NFDV-VIIDEAAQALEPSTL 222
|
250 260
....*....|....*....|....*...
gi 164663913 807 MPLALATKntRIVLAGDHMQLSPFVYSE 834
Cdd:pfam13086 223 IPLLRGPK--KVVLVGDPKQLPPTVISK 248
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
632-1073 |
4.70e-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: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 632 RQWDEQLDPRLNAKQKEAV--LAITTPLCIqlppvlIIGPYGTGKTFTLAQAVKHILQQQEtsRILICTHSNSAAD-LYi 708
Cdd:COG0507 115 AALEPRAGITLSDEQREAValALTTRRVSV------LTGGAGTGKTTTLRALLAALEALGL--RVALAAPTGKAAKrLS- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 709 kdylhpyvEAGNAQARplrvyfrnrwvkTVHPVVHqyclISSAHSTFQMPQKEDILKHRVVVVtlntsqylcqldlepgf 788
Cdd:COG0507 186 --------ESTGIEAR------------TIHRLLG----LRPDSGRFRHNRDNPLTPADLLVV----------------- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 789 fthillDEA--------AQAMEcetimplALATKNTRIVLAGDHMQLSP----FVYSEFARERNLHVSLLDrlyehypae 856
Cdd:COG0507 225 ------DEAsmvdtrlmAALLE-------ALPRAGARLILVGDPDQLPSvgagAVLRDLIESGTVPVVELT--------- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 857 fpcrillcENYRSHEAI-INYTSELFYEGKlMASGKQPAHKDFYPL----------------TFFTARGEDVQ-----EK 914
Cdd:COG0507 283 --------EVYRQADDSrIIELAHAIREGD-APEALNARYADVVFVeaedaeeaaeaivelyADRPAGGEDIQvlaptNA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 915 nSTAFYN-------NAEVFEVVERVEELRRKW----PV-------AWGkLDDGSIGVVTPYADQVFRIRAELRKKRLSDV 976
Cdd:COG0507 354 -GVDALNqairealNPAGELERELAEDGELELyvgdRVmftrndyDLG-VFNGDIGTVLSIDEDEGRLTVRFDGREIVTY 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 977 NVERVLNV-----------QGKQF-RVLFLSTvrtrhtckhkqtpikkkeqlledsteDLDYGFLSNyKLLNTAITRAQS 1044
Cdd:COG0507 432 DPSELDQLelayaitvhksQGSTFdRVILVLP--------------------------SEHSPLLSR-ELLYTALTRARE 484
|
490 500
....*....|....*....|....*....
gi 164663913 1045 LVAVVGDPVALCSIgrCRKFWERFIALCH 1073
Cdd:COG0507 485 LLTLVGDRDALARA--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 |
1319-1413 |
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 164663913 1319 PESRPGVVYSNTKFPRKDNLNPRHINLPLPAPHTQYAIPSRHFHPLPQLPRPPFPISQQHTLLNQQQnnlPEQPNQMTPQ 1398
Cdd:PRK10263 743 PLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQ---PVAPQPQYQQ 819
|
90
....*....|....*.
gi 164663913 1399 PNQ-VAPQPNQMAPQP 1413
Cdd:PRK10263 820 PQQpVAPQPQYQQPQQ 835
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1244-1519 |
6.68e-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: 44.76 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 1244 HGRGSPIPYglghhpPVNLGQPQNQHAEKDQQEQNRNGKTDTNNP-GPEINKIRTPEKKPTEPKqidlesnPQNRSPESR 1322
Cdd:pfam03154 272 HGQMPPMPH------SLQTGPSHMQHPVPPQPFPLTPQSSQSQVPpGPSPAAPGQSQQRIHTPP-------SQSQLQSQQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 1323 PgvvysntkfPRKDNLNPRhinlPLPAPHTQyaipsrhfhPLPQLPRPPFPISQQHTLLN--------QQQNNLPEQP-- 1392
Cdd:pfam03154 339 P---------PREQPLPPA----PLSMPHIK---------PPPTTPIPQLPNPQSHKHPPhlsgpspfQMNSNLPPPPal 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 1393 ----NQMTPQPNQVAPQPNQMAPQPNQMAPQPNQVVQQQNQAPPQAPQPAPQLSPAFQAGPTNAFFnnavahrPQSP--- 1465
Cdd:pfam03154 397 kplsSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPF-------PQHPfvp 469
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 164663913 1466 -AAEAVGPEQQVPPGLSDGHSPLRAITQPGPILASPLNNFVDESSPGLPI-EEALD 1519
Cdd:pfam03154 470 gGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIkEEALD 525
|
|
| Amelogenin |
smart00818 |
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
1331-1416 |
3.69e-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: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 1331 KFPRKDNLNPRHINLPLPAPHTqyAIPSRHFHP-LPQLPRPPFpisqqhtllnQQQNNLPEQPNQMTPQPNQVAPQPNQM 1409
Cdd:smart00818 60 VLPAQQPVVPQQPLMPVPGQHS--MTPTQHHQPnLPQPAQQPF----------QPQPLQPPQPQQPMQPQPPVHPIPPLP 127
|
....*..
gi 164663913 1410 APQPNQM 1416
Cdd:smart00818 128 PQPPLPP 134
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
1297-1500 |
6.46e-03 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 41.35 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 1297 TPEKKPTEPKQIDLESNPQNRSPESRPGVVYSNTKFPRKDNLNPRHINLPLPAPhtqyAIPSRHFHPLP-QLPRPPFPIS 1375
Cdd:PRK14086 91 SAGEPAPPPPHARRTSEPELPRPGRRPYEGYGGPRADDRPPGLPRQDQLPTARP----AYPAYQQRPEPgAWPRAADDYG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 1376 QQHTLLNQQQNNLPEQPNQMTPQPNQVAPQPNQMAPQPNQMAPQPNQvvqqqnqappqapqpapqlsPAFQAGPTNAFFN 1455
Cdd:PRK14086 167 WQQQRLGFPPRAPYASPASYAPEQERDREPYDAGRPEYDQRRRDYDH--------------------PRPDWDRPRRDRT 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 164663913 1456 NavahRPQ-SPAAEAVGPEQQVPPGLSDGHSPLRAITQPGPILASP 1500
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 ... |
641-868 |
2.48e-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: 465.42 E-value: 2.48e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 641 RLNAKQKEAVLAITTPLCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETsRILICTHSNSAADLYIKDYLHPYVEAGN 720
Cdd:cd18077 1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPET-RILICTHSNSAADLYIKEYLHPYVETGN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 721 AQARPLRVYFRNRWVKTVHPVVHQYCLISsAHSTFQMPQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQA 800
Cdd:cd18077 80 PRARPLRVYYRNRWVKTVHPVVQKYCLID-EHGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164663913 801 MECETIMPLALATKNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEFPCRILLCENYR 868
Cdd:cd18077 159 MECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSEHPCRILLCENYR 226
|
|
| DEXXQc_Helz-like |
cd18038 |
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ... |
641-868 |
9.17e-95 |
|
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: 9.17e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 641 RLNAKQKEAVLAITTPLCiQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETSRILICTHSNSAADLYIKDYLHPYVEagn 720
Cdd:cd18038 1 ELNDEQKLAVRNIVTGTS-RPPPYIIFGPPGTGKTVTLVEAILQVLRQPPEARILVCAPSNSAADLLAERLLNALVT--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 721 aQARPLRVYFRNRWVKTVHPVVHQYClISSAHSTFQMPQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQA 800
Cdd:cd18038 77 -KREILRLNAPSRDRASVPPELLPYC-NSKAEGTFRLPSLEELKKYRIVVCTLMTAGRLVQAGVPNGHFTHIFIDEAGQA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164663913 801 MECETIMPLA-LATKNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYP------AEFPCRILLCENYR 868
Cdd:cd18038 155 TEPEALIPLSeLASKNTQIVLAGDPKQLGPVVRSPLARKYGLGKSLLERLMERPLyykdgeYNPSYITKLLKNYR 229
|
|
| DEXXQc_HELZ2-N |
cd18076 |
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
641-868 |
3.86e-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: 3.86e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 641 RLNAKQKEAVLAIT--TPLCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETsRILICTHSNSAADLYIKDYLHPYVEA 718
Cdd:cd18076 1 AGNNKQQLAFNFIAgkPSEARFVPPLLIYGPFGTGKTFTLAMAALEVIREPGT-KVLICTHTNSAADIYIREYFHPYVDK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 719 GNAQARPLRVYFRNRWVKTVHPVVHQYCLISSAHSTFQMPQKEDILKHRVVVVTLNTSQylcQLDLEPGFFTHILLDEAA 798
Cdd:cd18076 80 GHPEARPLRIKATDRPNAITDPDTITYCCLTKDRQCFRLPTRDELDFHNIVITTTAMAF---NLHVLSGFFTHIFIDEAA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164663913 799 QAMECETIMPLALATKNTRIVLAGDHMQLSPFVYSeFARERNLHVSLLDRLYEHYPAE-----FPCRILLCENYR 868
Cdd:cd18076 157 QMLECEALIPLSYAGPKTRVVLAGDHMQMTPKLFS-VADYNRANHTLLNRLFHYYQGEkhevaVKSRVIFSENYR 230
|
|
| DEXXQc_Mov10L1 |
cd18078 |
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ... |
642-868 |
7.36e-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: 7.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 642 LNAKQKEAVLAITTPLCIQLPPVlIIGPYGTGKTFTLAQAVKHILQQQETSRILICTHSNSAADLYIKDyLHPYVEAGNA 721
Cdd:cd18078 2 LNELQKEAVKRILGGECRPLPYI-LFGPPGTGKTVTIIEAILQVVYNLPRSRILVCAPSNSAADLVTSR-LHESKVLKPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 722 QARPLRVYfrNRWVKTVHPVVHQYCLISSahstfqmpQKEDILKHRVVVVTLNTSQYLCQLDLEPGFFTHILLDEAAQAM 801
Cdd:cd18078 80 DMVRLNAV--NRFESTVIDARKLYCRLGE--------DLSKASRHRIVISTCSTAGLLYQMGLPVGHFTHVFVDEAGQAT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 802 ECETIMPLALATKNT-RIVLAGDHMQLSPFVYSEFARERNLHVSLLDRL-----YEHYPAEFP-CRIL-------LCENY 867
Cdd:cd18078 150 EPESLIPLGLISSRDgQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLmnrplYLRDPNRFGeSGGYnpllvtkLVDNY 229
|
.
gi 164663913 868 R 868
Cdd:cd18078 230 R 230
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
766-1075 |
9.20e-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: 9.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 766 HRVVVVTLNTSQYLcqLDLEPGFFTHILLDEAAQAMECETIMPLALATkntRIVLAGDHMQLSPFV---YSEFARERNLH 842
Cdd:COG1112 535 APVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVfgeEAEEVAEEGLD 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 843 VSLLDRLYEHYPaefPCRILLCENYRSHEAIINYTSELFYEGKLMA---SGKQPAHKDFYPLTFFTARGedVQEKNSTAF 919
Cdd:COG1112 610 ESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDG--VYERRGGSR 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 920 YNnaevfevverveelrrkwP------VAW------GKLDDGSIGVVTPYADQVFRIRAELRKKRLSDV------NVERv 981
Cdd:COG1112 685 TN------------------PeeaeavVELvrelleDGPDGESIGVITPYRAQVALIRELLREALGDGLepvfvgTVDR- 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 982 lnVQGKQFRVLFLSTVRTRhtckhkqtpikkkeqlleDSTEDLDYGFLS-NYKLLNTAITRAQSLVAVVGDPvALCSIGR 1060
Cdd:COG1112 746 --FQGDERDVIIFSLVYSN------------------DEDVPRNFGFLNgGPRRLNVAVSRARRKLIVVGSR-ELLDSDP 804
|
330
....*....|....*
gi 164663913 1061 CRKFWERFIALCHEN 1075
Cdd:COG1112 805 STPALKRLLEYLERA 819
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
869-1069 |
6.36e-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: 6.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 869 SHEAIINYTSELFYEGKLMAS-------GKQPAHKDFYPLTFFTARGEDVQEKNSTAFYNNAEVFEVVERVEELRRKWpv 941
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKAGvsvaarlNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 942 awgkLDDGSIGVVTPYADQVFRIRAELRKKR--LSDVNVERVLNVQGKQFRVLFLSTVRTRHTCKHkqtpikkkeqlled 1019
Cdd:cd18808 79 ----VKPSSIGVITPYRAQVALIRELLRKRGglLEDVEVGTVDNFQGREKDVIILSLVRSNESGGS-------------- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 164663913 1020 stedldYGFLSNYKLLNTAITRAQSLVAVVGDPVALCSIGRCRKFWERFI 1069
Cdd:cd18808 141 ------IGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
841-1052 |
4.88e-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 164663913 841 LHVSLLDRLYEHYPAefpCRILLCENYRSHEAIINYTSELFYEGKLMASGKQPAH---------KDFYPLTFF-TARGED 910
Cdd:pfam13087 1 LDRSLFERLQELGPS---AVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERplpddfhlpDPLGPLVFIdVDGSEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 911 VQEKNSTAFYNNAEVFEVVERVEELRRKWPVAWGKlddgsIGVVTPYADQVFRIRAELRKKRLSDVNVErVLNV---QGK 987
Cdd:pfam13087 78 EESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSD-----IGVITPYRAQVRLIRKLLKRKLGGKLEIE-VNTVdgfQGR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164663913 988 QFRVLFLSTVRtrhtckhkqtpikkkeqlledSTEDLDYGFLSNYKLLNTAITRAQSLVAVVGDP 1052
Cdd:pfam13087 152 EKDVIIFSCVR---------------------SNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNA 195
|
|
| DEXXQc_DNA2 |
cd18041 |
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ... |
641-854 |
2.23e-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: 105.78 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 641 RLNAKQKEAVLAITTPLCIqlppVLIIGPYGTGKTFTLAQAVKhILQQQETSrILICTHSNSAAD---LYIKDYLHPYVE 717
Cdd:cd18041 1 GLNKDQRQAIKKVLNAKDY----ALILGMPGTGKTTTIAALVR-ILVALGKS-VLLTSYTHSAVDnilLKLKKFGVNFLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 718 AGNAqarplrvyfrnrwvKTVHPVVHQYCLISSAHSTFQMPQKEDIL-KHRVVVVTL--NTSQYLCQldlepGFFTHILL 794
Cdd:cd18041 75 LGRL--------------KKIHPDVQEFTLEAILKSCKSVEELESKYeSVSVVATTClgINHPIFRR-----RTFDYCIV 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 795 DEAAQAMECETIMPLALATKntrIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYP 854
Cdd:cd18041 136 DEASQITLPICLGPLRLAKK---FVLVGDHYQLPPLVKSREARELGMDESLFKRLSEAHP 192
|
|
| DEXXQc_SMUBP2 |
cd18044 |
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ... |
641-868 |
9.40e-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: 100.76 E-value: 9.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 641 RLNAKQKEAVLaittpLCIQLPPVLII-GPYGTGKTFTLAQAVKHILQQQEtsRILICTHSNSAADlYIKDYLhpyveag 719
Cdd:cd18044 1 NLNDSQKEAVK-----FALSQKDVALIhGPPGTGKTTTVVEIILQAVKRGE--KVLACAPSNIAVD-NLVERL------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 720 naQARPLRVyfrnrwVKTVHPV-----VHQYCLissahstfqmpqkEDILKHRVVVVTLNTSqylCQLDLEPG-FFTHIL 793
Cdd:cd18044 66 --VALKVKV------VRIGHPArllesVLDHSL-------------DALVAAQVVLATNTGA---GSRQLLPNeLFDVVV 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164663913 794 LDEAAQAMECETIMPLalaTKNTRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEHYPAEfpCRILLCENYR 868
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 ... |
642-849 |
1.43e-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: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 642 LNAKQKEAV-LAITTPLCiqlppvLIIGPYGTGKTFTLAQAVKHILQQQEtSRILICTHSNSAADlYIKDYLHpyveagN 720
Cdd:cd18039 2 LNHSQVDAVkTALQRPLS------LIQGPPGTGKTVTSATIVYHLVKQGN-GPVLVCAPSNVAVD-QLTEKIH------Q 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 721 AQARPLRVYFRNRW-----VK--TVHPVVHQY-----------------CLISSAHSTFQM----PQKEDILKHRVVVVT 772
Cdd:cd18039 68 TGLKVVRLCAKSREavespVSflALHNQVRNLdsaeklellkllkletgELSSADEKRYRKlkrkAERELLRNADVICCT 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164663913 773 LNTSqylcqLD--LEPGFFTHILLDEAAQAMECETIMPLALATKntRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRL 849
Cdd:cd18039 148 CVGA-----GDprLSKMKFRTVLIDEATQATEPECLIPLVHGAK--QVILVGDHCQLGPVVMCKKAAKAGLSQSLFERL 219
|
|
| DEXXQc_SETX |
cd18042 |
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ... |
642-868 |
2.91e-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: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 642 LNAKQKEAVLAIttplCIQLPPV-LIIGPYGTGKTFTL---------------AQAVKHILQQQETS--------RILIC 697
Cdd:cd18042 1 LNESQLEAIASA----LQNSPGItLIQGPPGTGKTKTIvgilsvllagkyrkyYEKVKKKLRKLQRNlnnkkkknRILVC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 698 THSNSAADLYIKDYLHPYVEAGNAQARPLRVyfrnrwVKTVHpvvhqyclissahstfQMPQKEDILKHRVVVVTLNTSQ 777
Cdd:cd18042 77 APSNAAVDEIVLRLLSEGFLDGDGRSYKPNV------VRVGR----------------QELRASILNEADIVCTTLSSSG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 778 YLcQLDLEPGFFTHILLDEAAQAMECETIMPLALATKntRIVLAGDHMQLSPFVYSEFARERNLHVSLLDRLYEhypAEF 857
Cdd:cd18042 135 SD-LLESLPRGFDTVIIDEAAQAVELSTLIPLRLGCK--RLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQL---AGY 208
|
250
....*....|.
gi 164663913 858 PCrILLCENYR 868
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, ... |
664-868 |
1.05e-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: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 664 VLIIGPYGTGKTFTLAQAVKHILQQQETSRILICTHSNSAADlyikdylhpyveagNAqarplrvyfrnrwvktvhpvvh 743
Cdd:cd17934 2 SLIQGPPGTGKTTTIAAIVLQLLKGLRGKRVLVTAQSNVAVD--------------NV---------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 744 qyclissahstfqmpqkedilkhRVVVVtlntsqylcqldlepgffthillDEAAQAMECETIMPLALATKntrIVLAGD 823
Cdd:cd17934 46 -----------------------DVVII-----------------------DEASQITEPELLIALIRAKK---VVLVGD 76
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 164663913 824 HMQLSPFVYSEFARE--RNLHVSLLDRLYEHYPAEFPcrILLCENYR 868
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 ... |
646-834 |
3.05e-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: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 646 QKEAVLAIttplCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETS-----RILICTHSNSAAD----LYIKDYLHPyv 716
Cdd:pfam13086 2 QREAIRSA----LSSSHFTLIQGPPGTGKTTTIVELIRQLLSYPATSaaagpRILVCAPSNAAVDnileRLLRKGQKY-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 717 eagnaQARPLRVYFRnrwvKTVHPVVHQYCLISSAHSTFQMPQKEDILK------------------------------- 765
Cdd:pfam13086 76 -----GPKIVRIGHP----AAISEAVLPVSLDYLVESKLNNEEDAQIVKdiskeleklakalrafekeiivekllksrnk 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 766 -------------------------------------HRVVVVTLNTS--QYLCQLDlepGFFThILLDEAAQAMECETI 806
Cdd:pfam13086 147 dkskleqerrklrserkelrkelrrreqslereildeAQIVCSTLSGAgsRLLSSLA---NFDV-VIIDEAAQALEPSTL 222
|
250 260
....*....|....*....|....*...
gi 164663913 807 MPLALATKntRIVLAGDHMQLSPFVYSE 834
Cdd:pfam13086 223 IPLLRGPK--KVVLVGDPKQLPPTVISK 248
|
|
| EEXXEc_NFX1 |
cd17936 |
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ... |
641-849 |
8.55e-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: 74.50 E-value: 8.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 641 RLNAKQKEA-VLAITTPLciqlppVLIIGPYGTGKTFTLAQAVKHILQ---QQETSRILICTHSNSAADLYIKDYLhpyv 716
Cdd:cd17936 1 TLDPSQLEAlKHALTSEL------ALIQGPPGTGKTFLGVKLVRALLQnqdLSITGPILVVCYTNHALDQFLEGLL---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 717 EAGNAQArpLRVYFRnrwvktvhpVVHqyCLISSAHSTFQMPQKediLKHRVVVVtlntsqylcqldlepgffthillDE 796
Cdd:cd17936 71 DFGPTKI--VRLGAR---------VIG--MTTTGAAKYRELLQA---LGPKVVIV-----------------------EE 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 164663913 797 AAQAMECETIMPLalaTKNTR-IVLAGDHMQLSPFV--YSEFARERNLHVSLLDRL 849
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 ... |
642-851 |
3.03e-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: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 642 LNAKQKEAVL-AITTPLciqlppVLIIGPYGTGKTFTLAQAVKHILQQQETSR-----------ILICTHSNSAADL--- 706
Cdd:cd18040 2 LNPSQNHAVRtALTKPF------TLIQGPPGTGKTVTGVHIAYWFAKQNREIQsvsgegdggpcVLYCGPSNKSVDVvae 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 707 YIKDY-----LHPYVEAGNAQARPLRVYFRNRWVK--------------TVHPVVHQ----YC-LISSAHSTFQMPQ--- 759
Cdd:cd18040 76 LLLKVpglkiLRVYSEQIETTEYPIPNEPRHPNKKsereskpnselssiTLHHRIRQpsnpHSqQIKAFEARFERTQeki 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 760 -KEDILKHRVVV------------VTLNTsqylCQLDLEPGFFTH-----ILLDEAAQAMECETIMPLALATKNTRIVLA 821
Cdd:cd18040 156 tEEDIKTYKILIwearfeeletvdVILCT----CSEAASQKMRTHanvkqCIVDECGMCTEPESLIPIVSAPRAEQVVLI 231
|
250 260 270
....*....|....*....|....*....|
gi 164663913 822 GDHMQLSPFVYSEFARERNLHVSLLDRLYE 851
Cdd:cd18040 232 GDHKQLRPVVQNKEAQKLGLGRSLFERYAE 261
|
|
| EEXXQc_AQR |
cd17935 |
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ... |
641-849 |
7.64e-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: 7.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 641 RLNAKQKEAVLAITTPLCiqlppVLIIGPYGTGKTFTLAQAVKHILQQQETSRILICTHSNSAA-DLYIKdylhpyVEAg 719
Cdd:cd17935 5 KFTPTQIEAIRSGMQPGL-----TMVVGPPGTGKTDVAVQIISNLYHNFPNQRTLIVTHSNQALnQLFEK------IMA- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 720 naqarpLRVYFRNrwvktvhpvvhqycLISSAHSTfqmpqkedilkhRVVVVTLnTSQYLCQLDL-EPGF-FTHILLDEA 797
Cdd:cd17935 73 ------LDIDERH--------------LLRLGHGA------------KIIAMTC-THAALKRGELvELGFkYDNILMEEA 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 164663913 798 AQAMECETIMPLALATKNT------RIVLAGDHMQLSPFVYS-EFARERNLHVSLLDRL 849
Cdd:cd17935 120 AQILEIETFIPLLLQNPEDgpnrlkRLIMIGDHHQLPPVIKNmAFQKYSNMEQSLFTRL 178
|
|
| DEXQc_UvrD |
cd17932 |
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch ... |
643-867 |
4.19e-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: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 643 NAKQKEAVLAITTPLCIqlppvlIIGPyGTGKTFTLAQAVKHILQQQET--SRILICTHSNSAADlYIKDYLHPYVeaGN 720
Cdd:cd17932 1 NPEQREAVTHPDGPLLV------LAGA-GSGKTRVLTHRIAYLILEGGVppERILAVTFTNKAAK-EMRERLRKLL--GE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 721 AQARPLrvyfrnrWVKTVHPVvhqyCL-ISSAHSTFqmpqkEDILkHRVVVVtLNTSQYLCQLDLEPgfFTHILLDEA-- 797
Cdd:cd17932 71 QLASGV-------WIGTFHSF----ALrILRRYGDF-----DDLL-LYALEL-LEENPDVREKLQSR--FRYILVDEYqd 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164663913 798 ---AQamecETIMpLALATKNTRIVLAGDHMQlSpfVYSeFareRNLHVSLLDRLYEHYPAefPCRILLCENY 867
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 ... |
643-832 |
2.54e-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: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 643 NAKQKEAVLAIttplcIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQEtsRILICTHSNSAADlyikdylhpyveagnaq 722
Cdd:cd18043 1 DSSQEAAIISA-----RNGKNVVIQGPPGTGKSQTIANIIANALARGK--RVLFVSEKKAALD----------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 723 arplrvyfrnrwvktvhpVVHQYCLISSAHSTFQMpqkedilkhrvvvvtlntsqylcqLDLEPGFFTHILLDEAAQAME 802
Cdd:cd18043 57 ------------------VVRFPCWIMSPLSVSQY------------------------LPLNRNLFDLVIFDEASQIPI 94
|
170 180 190
....*....|....*....|....*....|
gi 164663913 803 CETImPLALATKntRIVLAGDHMQLSPFVY 832
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 ... |
663-705 |
3.05e-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: 3.05e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 164663913 663 PVLIIGPYGTGKTFTLAQAVKHILQQQETS--RILICTHSNSAAD 705
Cdd:cd17914 1 LSLIQGPPGTGKTRVLVKIVAALMQNKNGEpgRILLVTPTNKAAA 45
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
632-1073 |
4.70e-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: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 632 RQWDEQLDPRLNAKQKEAV--LAITTPLCIqlppvlIIGPYGTGKTFTLAQAVKHILQQQEtsRILICTHSNSAAD-LYi 708
Cdd:COG0507 115 AALEPRAGITLSDEQREAValALTTRRVSV------LTGGAGTGKTTTLRALLAALEALGL--RVALAAPTGKAAKrLS- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 709 kdylhpyvEAGNAQARplrvyfrnrwvkTVHPVVHqyclISSAHSTFQMPQKEDILKHRVVVVtlntsqylcqldlepgf 788
Cdd:COG0507 186 --------ESTGIEAR------------TIHRLLG----LRPDSGRFRHNRDNPLTPADLLVV----------------- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 789 fthillDEA--------AQAMEcetimplALATKNTRIVLAGDHMQLSP----FVYSEFARERNLHVSLLDrlyehypae 856
Cdd:COG0507 225 ------DEAsmvdtrlmAALLE-------ALPRAGARLILVGDPDQLPSvgagAVLRDLIESGTVPVVELT--------- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 857 fpcrillcENYRSHEAI-INYTSELFYEGKlMASGKQPAHKDFYPL----------------TFFTARGEDVQ-----EK 914
Cdd:COG0507 283 --------EVYRQADDSrIIELAHAIREGD-APEALNARYADVVFVeaedaeeaaeaivelyADRPAGGEDIQvlaptNA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 915 nSTAFYN-------NAEVFEVVERVEELRRKW----PV-------AWGkLDDGSIGVVTPYADQVFRIRAELRKKRLSDV 976
Cdd:COG0507 354 -GVDALNqairealNPAGELERELAEDGELELyvgdRVmftrndyDLG-VFNGDIGTVLSIDEDEGRLTVRFDGREIVTY 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 977 NVERVLNV-----------QGKQF-RVLFLSTvrtrhtckhkqtpikkkeqlledsteDLDYGFLSNyKLLNTAITRAQS 1044
Cdd:COG0507 432 DPSELDQLelayaitvhksQGSTFdRVILVLP--------------------------SEHSPLLSR-ELLYTALTRARE 484
|
490 500
....*....|....*....|....*....
gi 164663913 1045 LVAVVGDPVALCSIgrCRKFWERFIALCH 1073
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. ... |
645-829 |
5.97e-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: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 645 KQKEAVLAITT-PLCIqlppvlIIGPYGTGKTFTLAQAVKHIlqQQETSRILICTHSNSAADlyikdylhpyvEAGNAQA 723
Cdd:cd17933 1 EQKAAVRLVLRnRVSV------LTGGAGTGKTTTLKALLAAL--EAEGKRVVLAAPTGKAAK-----------RLSESTG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 724 RPlrvyfrnrwVKTVHPVvhqycLISSAHSTFQMPQKEDILKHRVVVVtlntsqylcqldlepgffthillDEAaqAMec 803
Cdd:cd17933 62 IE---------ASTIHRL-----LGINPGGGGFYYNEENPLDADLLIV-----------------------DEA--SM-- 100
|
170 180 190
....*....|....*....|....*....|...
gi 164663913 804 etiMPLALATK-------NTRIVLAGDHMQLSP 829
Cdd:cd17933 101 ---VDTRLMAAllsaipaGARLILVGDPDQLPS 130
|
|
| UvrD |
COG0210 |
Superfamily I DNA or RNA helicase [Replication, recombination and repair]; |
641-704 |
2.00e-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: 2.00e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164663913 641 RLNAKQKEAVLAITTPLciqlppvLII-GPyGTGKTFTLAQAVKHILQQQETS--RILICTHSNSAA 704
Cdd:COG0210 6 GLNPEQRAAVEHPEGPL-------LVLaGA-GSGKTRVLTHRIAYLIAEGGVDpeQILAVTFTNKAA 64
|
|
| zf-CCCH |
pfam00642 |
Zinc finger C-x8-C-x5-C-x3-H type (and similar); |
181-205 |
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 ... |
642-705 |
7.35e-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: 49.55 E-value: 7.35e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164663913 642 LNAKQKEAVLAITTPLciqlppvLIIGPYGTGKTFTLAQAVKHILQQQETS--RILICTHSNSAAD 705
Cdd:pfam00580 1 LNPEQRKAVTHLGGPL-------LVLAGAGSGKTRVLTERIAYLILEGGIDpeEILAVTFTNKAAR 59
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
1319-1413 |
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 164663913 1319 PESRPGVVYSNTKFPRKDNLNPRHINLPLPAPHTQYAIPSRHFHPLPQLPRPPFPISQQHTLLNQQQnnlPEQPNQMTPQ 1398
Cdd:PRK10263 743 PLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQ---PVAPQPQYQQ 819
|
90
....*....|....*.
gi 164663913 1399 PNQ-VAPQPNQMAPQP 1413
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 ... |
641-829 |
1.26e-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: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 641 RLNAKQKEAVLAITT-PLCIQLppvlIIGPYGTGKTFTLAQAVKHIlqQQETSRILICTHSNSAADLYIKDYlhpyveag 719
Cdd:pfam13604 1 TLNAEQAAAVRALLTsGDRVAV----LVGPAGTGKTTALKALREAW--EAAGYRVIGLAPTGRAAKVLGEEL-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 720 NAQARplrvyfrnrwvkTVHPVVHQYclissahstfqmPQKEDILKHRVVVVtlntsqylcqldlepgffthillDEAAQ 799
Cdd:pfam13604 67 GIPAD------------TIAKLLHRL------------GGRAGLDPGTLLIV-----------------------DEAGM 99
|
170 180 190
....*....|....*....|....*....|....*
gi 164663913 800 A----MEcetiMPLALATK-NTRIVLAGDHMQLSP 829
Cdd:pfam13604 100 VgtrqMA----RLLKLAEDaGARVILVGDPRQLPS 130
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
642-797 |
1.65e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 44.20 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 642 LNAKQKEAVLAITTPLCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQETSRILICTHSNsaaDLY------IKDYLHPY 715
Cdd:pfam04851 4 LRPYQIEAIENLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRK---DLLeqaleeFKKFLPNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 716 VEAGNaqarPLRVYFRNRWVKTVHPVVhqyclissahSTFQmpqkedilkhrvvvvTLNTSQYLCQLDLEPGFFTHILLD 795
Cdd:pfam04851 81 VEIGE----IISGDKKDESVDDNKIVV----------TTIQ---------------SLYKALELASLELLPDFFDVIIID 131
|
..
gi 164663913 796 EA 797
Cdd:pfam04851 132 EA 133
|
|
| AAA_19 |
pfam13245 |
AAA domain; |
646-705 |
1.76e-04 |
|
AAA domain;
Pssm-ID: 433059 [Multi-domain] Cd Length: 136 Bit Score: 43.36 E-value: 1.76e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164663913 646 QKEAVLAITTPlciqlPPVLIIGPYGTGKTFTLAQAVKHILQQQETS-RILICTHSNSAAD 705
Cdd:pfam13245 1 QREAVRTALPS-----KVVLLTGGPGTGKTTTIRHIVALLVALGGVSfPILLAAPTGRAAK 56
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1244-1519 |
6.68e-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: 44.76 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 1244 HGRGSPIPYglghhpPVNLGQPQNQHAEKDQQEQNRNGKTDTNNP-GPEINKIRTPEKKPTEPKqidlesnPQNRSPESR 1322
Cdd:pfam03154 272 HGQMPPMPH------SLQTGPSHMQHPVPPQPFPLTPQSSQSQVPpGPSPAAPGQSQQRIHTPP-------SQSQLQSQQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 1323 PgvvysntkfPRKDNLNPRhinlPLPAPHTQyaipsrhfhPLPQLPRPPFPISQQHTLLN--------QQQNNLPEQP-- 1392
Cdd:pfam03154 339 P---------PREQPLPPA----PLSMPHIK---------PPPTTPIPQLPNPQSHKHPPhlsgpspfQMNSNLPPPPal 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 1393 ----NQMTPQPNQVAPQPNQMAPQPNQMAPQPNQVVQQQNQAPPQAPQPAPQLSPAFQAGPTNAFFnnavahrPQSP--- 1465
Cdd:pfam03154 397 kplsSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPF-------PQHPfvp 469
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 164663913 1466 -AAEAVGPEQQVPPGLSDGHSPLRAITQPGPILASPLNNFVDESSPGLPI-EEALD 1519
Cdd:pfam03154 470 gGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIkEEALD 525
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
637-730 |
2.15e-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: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 637 QLDPRLNAKQKEAVLAITTPLCIQLPPVLIIGPYGTGKTFTLAQAVKHILQQQetsRILICTHS----NSAADLyIKDYL 712
Cdd:COG1061 76 GTSFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGK---RVLVLVPRrellEQWAEE-LRRFL 151
|
90
....*....|....*...
gi 164663913 713 HPYVEAGNAQARPLRVYF 730
Cdd:COG1061 152 GDPLAGGGKKDSDAPITV 169
|
|
| Amelogenin |
smart00818 |
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
1331-1416 |
3.69e-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: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 1331 KFPRKDNLNPRHINLPLPAPHTqyAIPSRHFHP-LPQLPRPPFpisqqhtllnQQQNNLPEQPNQMTPQPNQVAPQPNQM 1409
Cdd:smart00818 60 VLPAQQPVVPQQPLMPVPGQHS--MTPTQHHQPnLPQPAQQPF----------QPQPLQPPQPQQPMQPQPPVHPIPPLP 127
|
....*..
gi 164663913 1410 APQPNQM 1416
Cdd:smart00818 128 PQPPLPP 134
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
664-709 |
4.86e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 39.25 E-value: 4.86e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 164663913 664 VLIIGPYGTGKTfTLAQAVKHILQQQETSRILI-CTHSNSAADLYIK 709
Cdd:pfam13401 8 LVLTGESGTGKT-TLLRRLLEQLPEVRDSVVFVdLPSGTSPKDLLRA 53
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
1297-1500 |
6.46e-03 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 41.35 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 1297 TPEKKPTEPKQIDLESNPQNRSPESRPGVVYSNTKFPRKDNLNPRHINLPLPAPhtqyAIPSRHFHPLP-QLPRPPFPIS 1375
Cdd:PRK14086 91 SAGEPAPPPPHARRTSEPELPRPGRRPYEGYGGPRADDRPPGLPRQDQLPTARP----AYPAYQQRPEPgAWPRAADDYG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663913 1376 QQHTLLNQQQNNLPEQPNQMTPQPNQVAPQPNQMAPQPNQMAPQPNQvvqqqnqappqapqpapqlsPAFQAGPTNAFFN 1455
Cdd:PRK14086 167 WQQQRLGFPPRAPYASPASYAPEQERDREPYDAGRPEYDQRRRDYDH--------------------PRPDWDRPRRDRT 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 164663913 1456 NavahRPQ-SPAAEAVGPEQQVPPGLSDGHSPLRAITQPGPILASP 1500
Cdd:PRK14086 227 D----RPEpPPGAGHVHRGGPGPPERDDAPVVPIRPSAPGPLAAQP 268
|
|
| |
