|
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 ... |
805-1030 |
7.35e-144 |
|
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: 445.39 E-value: 7.35e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 805 KLNAKQREAVNAITTALSIKLPPILLIGPFGTGKTYTLAQAIKQLLTQPEAKILICTHSNSAADLYIKEYLHPWIEEGLK 884
Cdd:cd18077 1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPETRILICTHSNSAADLYIKEYLHPYVETGNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 885 EATPLRVYYHKRWSATVNGVVQKYCITDGVGNFLRPTVEDIMRHRIVVVTLSISMELATLGLPKGLFTHIFLDEAAQAME 964
Cdd:cd18077 81 RARPLRVYYRNRWVKTVHPVVQKYCLIDEHGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQAME 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442632370 965 CEAIMPLALANDSTRIVLAGDHMQMSPELFSAFAKERKLHISLLERLYDHYPSNFPCKILLCENYR 1030
Cdd:cd18077 161 CEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSEHPCRILLCENYR 226
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
925-1236 |
4.35e-49 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 189.95 E-value: 4.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 925 IMRHRIVVVTL-SISmelATLGLPKGLFTHIFLDEAAQAMECEAIMPLALANdstRIVLAGDHMQMSPELFS---AFAKE 1000
Cdd:COG1112 532 LELAPVVGMTPaSVA---RLLPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVFGeeaEEVAE 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 1001 RKLHISLLERLYDHYPsnfPCKILLCENYRAHEAIIRFTSELFYEQKLVA---SGKQPRHDRFYPLTFFTTRGEDVQDKN 1077
Cdd:COG1112 606 EGLDESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDGVYERRGG 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 1078 STafYNNAEVYEVVERVSELRKRWPsawgklNDTSIGIMTPYSDQVFRIRSELRKRRMGGISVERVLNV---QGKQFRAV 1154
Cdd:COG1112 683 SR--TNPEEAEAVVELVRELLEDGP------DGESIGVITPYRAQVALIRELLREALGDGLEPVFVGTVdrfQGDERDVI 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 1155 FLSTVRTRRTCMPQGsapgsasttsigdadadYGFLSNS-KLLNTAITRAQSLVAVVGDPvALCSIGRCRKVWERFIEIC 1233
Cdd:COG1112 755 IFSLVYSNDEDVPRN-----------------FGFLNGGpRRLNVAVSRARRKLIVVGSR-ELLDSDPSTPALKRLLEYL 816
|
...
gi 442632370 1234 DEH 1236
Cdd:COG1112 817 ERA 819
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1003-1213 |
1.84e-47 |
|
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: 168.88 E-value: 1.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 1003 LHISLLERLYDHYPSnfpCKILLCENYRAHEAIIRFTSELFYEQKLVASGKQPRH---------DRFYPLTFF-TTRGED 1072
Cdd:pfam13087 1 LDRSLFERLQELGPS---AVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERplpddfhlpDPLGPLVFIdVDGSEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 1073 VQDKNSTAFYNNAEVYEVVERVSELRKRWPSAWGKlndtsIGIMTPYSDQVFRIRSELRKRRMG--GISVERVLNVQGKQ 1150
Cdd:pfam13087 78 EESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSD-----IGVITPYRAQVRLIRKLLKRKLGGklEIEVNTVDGFQGRE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442632370 1151 FRAVFLSTVRTRRtcmpqgsapgsasttsigdaDADYGFLSNSKLLNTAITRAQSLVAVVGDP 1213
Cdd:pfam13087 153 KDVIIFSCVRSNE--------------------KGGIGFLSDPRRLNVALTRAKRGLIIVGNA 195
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
1032-1233 |
2.16e-47 |
|
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: 168.18 E-value: 2.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 1032 HEAIIRFTSELFYEQKLVAS-------GKQPRHDRFYPLTFFTTRGEDVQDKNSTAFYNNAEVYEVVERVSELRKRWpsa 1104
Cdd:cd18808 2 HPEISEFPSKLFYEGKLKAGvsvaarlNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 1105 wgkLNDTSIGIMTPYSDQVFRIRSELRKRRMG--GISVERVLNVQGKQFRAVFLSTVRTRRTCMPqgsapgsasttsigd 1182
Cdd:cd18808 79 ---VKPSSIGVITPYRAQVALIRELLRKRGGLleDVEVGTVDNFQGREKDVIILSLVRSNESGGS--------------- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 442632370 1183 adadYGFLSNSKLLNTAITRAQSLVAVVGDPVALCSigrcRKVWERFIEIC 1233
Cdd:cd18808 141 ----IGFLSDPRRLNVALTRAKRGLIIVGNPDTLSK----DPLWKKLLEYL 183
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
657-1236 |
2.44e-42 |
|
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273041 [Multi-domain] Cd Length: 636 Bit Score: 166.53 E-value: 2.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 657 AGMATSTAKYSLAGEL--FALMRLGKDISEDT--SPGRLILSncssvyiskpedpdSKADPTKRAVYEALIEdKGKNVIY 732
Cdd:TIGR00376 25 RGRAILNLQGKIRGGLlgFLLVRFGRRKAIATeiSVGDIVLV--------------SRGNPLQSDLTGVVTR-VGKRFIT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 733 LKLSAKcVEAMALQadtelEVDIQFQLNRMPYCEWHNAVDKITDFR---LIFPATELEPS-IPWTPKKQWADSCepkLNA 808
Cdd:TIGR00376 90 VALEES-VPQWSLK-----RVRIDLYANDVTFKRMKEALRALTENHsrlLEFLLGREAPSkASEIHDFQFFDPN---LNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 809 KQREAVNAittALSIKlpPILLI-GPFGTGKTYTLAQAIKQLLTQPEaKILICTHSNSAADlYIKEYL-----------H 876
Cdd:TIGR00376 161 SQKEAVLF---ALSSK--DLFLIhGPPGTGKTRTVVELIRQLVKRGL-RVLVTAPSNIAVD-NLLERLalcdqkivrlgH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 877 P-----------------------------------------------WIEEGLKEATPLRVYYHKRWSATVNGVVQKYC 909
Cdd:TIGR00376 234 ParllksnkqhsldylienhpkyqivadirekidelieernkktkpspQKRRGLSDIKILRKALKKREARGIESLKIASM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 910 I--------TDGVGNFLRPTVEDIMRHRIVVVTLSISMElATLGLPKGLFTHIFLDEAAQAMECEAIMPLALANdstRIV 981
Cdd:TIGR00376 314 AewietnksIDRLLKLLPESEERIMNEILAESDATNSMA-GSEILNGQYFDVAVIDEASQAMEPSCLIPLLKAR---KLI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 982 LAGDHMQMSPELFSAFAKErkLHISLLERLYDHYPSNfpCKILLCEnYRAHEAIIRFTSELFYEQKLVASGKQPRH---- 1057
Cdd:TIGR00376 390 LAGDHKQLPPTILSHDAEE--LSLTLFERLIKEYPER--SRTLNVQ-YRMNQKIMEFPSREFYNGKLTAHESVANIllrd 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 1058 -------------DRFYPLTFFTTRG---EDVQDKNSTAFYNNAEVYEVVERVSELRKRwpsawgKLNDTSIGIMTPYSD 1121
Cdd:TIGR00376 465 lpkveateseddlETGIPLLFIDTSGcelFELKEADSTSKYNPGEAELVSEIIQALVKM------GVPANDIGVITPYDA 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 1122 QVFRIRsELRKRRMGGISVERVLNVQGKQFRAVFLSTVRTRRtcmpqgsapgsasttsigdaDADYGFLSNSKLLNTAIT 1201
Cdd:TIGR00376 539 QVDLLR-QLLEHRHIDIEVSSVDGFQGREKEVIIISFVRSNR--------------------KGEVGFLKDLRRLNVALT 597
|
650 660 670
....*....|....*....|....*....|....*
gi 442632370 1202 RAQSLVAVVGDPVALcsigRCRKVWERFIEICDEH 1236
Cdd:TIGR00376 598 RARRKLIVIGDSRTL----SNHKFYKRLIEWCKQH 628
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
815-995 |
8.60e-11 |
|
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: 64.29 E-value: 8.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 815 NAITTALSikLPPILLI-GPFGTGKTYTLAQAIKQLLTQPEA------KILICTHSNSAAD----LYIKEYL-------- 875
Cdd:pfam13086 4 EAIRSALS--SSHFTLIqGPPGTGKTTTIVELIRQLLSYPATsaaagpRILVCAPSNAAVDnileRLLRKGQkygpkivr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 876 --HP-WIEEGLKEAT---PLRVYYHKRWSAT---------------------VNGVVQKYCITDGVGNFLRPTVEDIM-- 926
Cdd:pfam13086 82 igHPaAISEAVLPVSldyLVESKLNNEEDAQivkdiskeleklakalrafekEIIVEKLLKSRNKDKSKLEQERRKLRse 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 927 ---------------------RHRIVVVTLSISMELATLGLPKglFTHIFLDEAAQAMECEAIMPLALAndSTRIVLAGD 985
Cdd:pfam13086 162 rkelrkelrrreqslereildEAQIVCSTLSGAGSRLLSSLAN--FDVVIIDEAAQALEPSTLIPLLRG--PKKVVLVGD 237
|
250
....*....|
gi 442632370 986 HMQMSPELFS 995
Cdd:pfam13086 238 PKQLPPTVIS 247
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
803-959 |
5.96e-07 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 54.65 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 803 EPKLNAKQREAVNAITTALSIKLPPILLIGPFGTGKTYTLAQAIKQLLTQPeaKILICTHSnsaadlyiKEYLHPWIEEg 882
Cdd:COG1061 78 SFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGK--RVLVLVPR--------RELLEQWAEE- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 883 LKEATPLRVYYHKRWSATvngvvqkycitdgvgnflrptvedimrHRIVVVT---LSISMELATLGlpkGLFTHIFLDEA 959
Cdd:COG1061 147 LRRFLGDPLAGGGKKDSD---------------------------APITVATyqsLARRAHLDELG---DRFGLVIIDEA 196
|
|
| zf-CCCH |
pfam00642 |
Zinc finger C-x8-C-x5-C-x3-H type (and similar); |
329-353 |
1.71e-04 |
|
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
Pssm-ID: 459885 [Multi-domain] Cd Length: 27 Bit Score: 40.25 E-value: 1.71e-04
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
824-883 |
1.47e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.20 E-value: 1.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 824 KLPPILLIGPFGTGKTyTLAQAIKQLLTQPEAKILICTHSNSAADLYIKEYLHPWIEEGL 883
Cdd:smart00382 1 PGEVILIVGPPGSGKT-TLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKA 59
|
|
| |
|
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 ... |
805-1030 |
7.35e-144 |
|
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: 445.39 E-value: 7.35e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 805 KLNAKQREAVNAITTALSIKLPPILLIGPFGTGKTYTLAQAIKQLLTQPEAKILICTHSNSAADLYIKEYLHPWIEEGLK 884
Cdd:cd18077 1 RLNAKQKEAVLAITTPLSIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPETRILICTHSNSAADLYIKEYLHPYVETGNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 885 EATPLRVYYHKRWSATVNGVVQKYCITDGVGNFLRPTVEDIMRHRIVVVTLSISMELATLGLPKGLFTHIFLDEAAQAME 964
Cdd:cd18077 81 RARPLRVYYRNRWVKTVHPVVQKYCLIDEHGTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQAME 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442632370 965 CEAIMPLALANDSTRIVLAGDHMQMSPELFSAFAKERKLHISLLERLYDHYPSNFPCKILLCENYR 1030
Cdd:cd18077 161 CEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEHYPSEHPCRILLCENYR 226
|
|
| DEXXQc_Helz-like |
cd18038 |
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ... |
806-1030 |
5.77e-78 |
|
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: 257.93 E-value: 5.77e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 806 LNAKQREAVNAITTALSiKLPPILLIGPFGTGKTYTLAQAIKQLL-TQPEAKILICTHSNSAADLYIKEYLHpwieEGLK 884
Cdd:cd18038 2 LNDEQKLAVRNIVTGTS-RPPPYIIFGPPGTGKTVTLVEAILQVLrQPPEARILVCAPSNSAADLLAERLLN----ALVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 885 EATPLRVYYHKRWSATVNGVVQKYCITDGVGNFLRPTVEDIMRHRIVVVTLSISMELATLGLPKGLFTHIFLDEAAQAME 964
Cdd:cd18038 77 KREILRLNAPSRDRASVPPELLPYCNSKAEGTFRLPSLEELKKYRIVVCTLMTAGRLVQAGVPNGHFTHIFIDEAGQATE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442632370 965 CEAIMPLA-LANDSTRIVLAGDHMQMSPELFSAFAKERKLHISLLERLYDHYPS------NFPCKILLCENYR 1030
Cdd:cd18038 157 PEALIPLSeLASKNTQIVLAGDPKQLGPVVRSPLARKYGLGKSLLERLMERPLYykdgeyNPSYITKLLKNYR 229
|
|
| DEXXQc_HELZ2-N |
cd18076 |
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
806-1030 |
8.61e-70 |
|
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB, and RXRA. It belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350834 [Multi-domain] Cd Length: 230 Bit Score: 234.40 E-value: 8.61e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 806 LNAKQREAVNAITTALS--IKLPPILLIGPFGTGKTYTLAQAIKQLLTQPEAKILICTHSNSAADLYIKEYLHPWIEEGL 883
Cdd:cd18076 2 GNNKQQLAFNFIAGKPSeaRFVPPLLIYGPFGTGKTFTLAMAALEVIREPGTKVLICTHTNSAADIYIREYFHPYVDKGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 884 KEATPLRVYYHKRWSATVNGVVQKY-CITDGVGNFLRPTVEDIMRHRIVVVTLSISMELATlglPKGLFTHIFLDEAAQA 962
Cdd:cd18076 82 PEARPLRIKATDRPNAITDPDTITYcCLTKDRQCFRLPTRDELDFHNIVITTTAMAFNLHV---LSGFFTHIFIDEAAQM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442632370 963 MECEAIMPLALANDSTRIVLAGDHMQMSPELFSAfAKERKLHISLLERLYDHYPSN-----FPCKILLCENYR 1030
Cdd:cd18076 159 LECEALIPLSYAGPKTRVVLAGDHMQMTPKLFSV-ADYNRANHTLLNRLFHYYQGEkhevaVKSRVIFSENYR 230
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
925-1236 |
4.35e-49 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 189.95 E-value: 4.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 925 IMRHRIVVVTL-SISmelATLGLPKGLFTHIFLDEAAQAMECEAIMPLALANdstRIVLAGDHMQMSPELFS---AFAKE 1000
Cdd:COG1112 532 LELAPVVGMTPaSVA---RLLPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPPVVFGeeaEEVAE 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 1001 RKLHISLLERLYDHYPsnfPCKILLCENYRAHEAIIRFTSELFYEQKLVA---SGKQPRHDRFYPLTFFTTRGEDVQDKN 1077
Cdd:COG1112 606 EGLDESLLDRLLARLP---ERGVMLREHYRMHPEIIAFSNRLFYDGKLVPlpsPKARRLADPDSPLVFIDVDGVYERRGG 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 1078 STafYNNAEVYEVVERVSELRKRWPsawgklNDTSIGIMTPYSDQVFRIRSELRKRRMGGISVERVLNV---QGKQFRAV 1154
Cdd:COG1112 683 SR--TNPEEAEAVVELVRELLEDGP------DGESIGVITPYRAQVALIRELLREALGDGLEPVFVGTVdrfQGDERDVI 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 1155 FLSTVRTRRTCMPQGsapgsasttsigdadadYGFLSNS-KLLNTAITRAQSLVAVVGDPvALCSIGRCRKVWERFIEIC 1233
Cdd:COG1112 755 IFSLVYSNDEDVPRN-----------------FGFLNGGpRRLNVAVSRARRKLIVVGSR-ELLDSDPSTPALKRLLEYL 816
|
...
gi 442632370 1234 DEH 1236
Cdd:COG1112 817 ERA 819
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1003-1213 |
1.84e-47 |
|
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: 168.88 E-value: 1.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 1003 LHISLLERLYDHYPSnfpCKILLCENYRAHEAIIRFTSELFYEQKLVASGKQPRH---------DRFYPLTFF-TTRGED 1072
Cdd:pfam13087 1 LDRSLFERLQELGPS---AVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERplpddfhlpDPLGPLVFIdVDGSEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 1073 VQDKNSTAFYNNAEVYEVVERVSELRKRWPSAWGKlndtsIGIMTPYSDQVFRIRSELRKRRMG--GISVERVLNVQGKQ 1150
Cdd:pfam13087 78 EESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSD-----IGVITPYRAQVRLIRKLLKRKLGGklEIEVNTVDGFQGRE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442632370 1151 FRAVFLSTVRTRRtcmpqgsapgsasttsigdaDADYGFLSNSKLLNTAITRAQSLVAVVGDP 1213
Cdd:pfam13087 153 KDVIIFSCVRSNE--------------------KGGIGFLSDPRRLNVALTRAKRGLIIVGNA 195
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
1032-1233 |
2.16e-47 |
|
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: 168.18 E-value: 2.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 1032 HEAIIRFTSELFYEQKLVAS-------GKQPRHDRFYPLTFFTTRGEDVQDKNSTAFYNNAEVYEVVERVSELRKRWpsa 1104
Cdd:cd18808 2 HPEISEFPSKLFYEGKLKAGvsvaarlNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 1105 wgkLNDTSIGIMTPYSDQVFRIRSELRKRRMG--GISVERVLNVQGKQFRAVFLSTVRTRRTCMPqgsapgsasttsigd 1182
Cdd:cd18808 79 ---VKPSSIGVITPYRAQVALIRELLRKRGGLleDVEVGTVDNFQGREKDVIILSLVRSNESGGS--------------- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 442632370 1183 adadYGFLSNSKLLNTAITRAQSLVAVVGDPVALCSigrcRKVWERFIEIC 1233
Cdd:cd18808 141 ----IGFLSDPRRLNVALTRAKRGLIIVGNPDTLSK----DPLWKKLLEYL 183
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
657-1236 |
2.44e-42 |
|
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273041 [Multi-domain] Cd Length: 636 Bit Score: 166.53 E-value: 2.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 657 AGMATSTAKYSLAGEL--FALMRLGKDISEDT--SPGRLILSncssvyiskpedpdSKADPTKRAVYEALIEdKGKNVIY 732
Cdd:TIGR00376 25 RGRAILNLQGKIRGGLlgFLLVRFGRRKAIATeiSVGDIVLV--------------SRGNPLQSDLTGVVTR-VGKRFIT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 733 LKLSAKcVEAMALQadtelEVDIQFQLNRMPYCEWHNAVDKITDFR---LIFPATELEPS-IPWTPKKQWADSCepkLNA 808
Cdd:TIGR00376 90 VALEES-VPQWSLK-----RVRIDLYANDVTFKRMKEALRALTENHsrlLEFLLGREAPSkASEIHDFQFFDPN---LNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 809 KQREAVNAittALSIKlpPILLI-GPFGTGKTYTLAQAIKQLLTQPEaKILICTHSNSAADlYIKEYL-----------H 876
Cdd:TIGR00376 161 SQKEAVLF---ALSSK--DLFLIhGPPGTGKTRTVVELIRQLVKRGL-RVLVTAPSNIAVD-NLLERLalcdqkivrlgH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 877 P-----------------------------------------------WIEEGLKEATPLRVYYHKRWSATVNGVVQKYC 909
Cdd:TIGR00376 234 ParllksnkqhsldylienhpkyqivadirekidelieernkktkpspQKRRGLSDIKILRKALKKREARGIESLKIASM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 910 I--------TDGVGNFLRPTVEDIMRHRIVVVTLSISMElATLGLPKGLFTHIFLDEAAQAMECEAIMPLALANdstRIV 981
Cdd:TIGR00376 314 AewietnksIDRLLKLLPESEERIMNEILAESDATNSMA-GSEILNGQYFDVAVIDEASQAMEPSCLIPLLKAR---KLI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 982 LAGDHMQMSPELFSAFAKErkLHISLLERLYDHYPSNfpCKILLCEnYRAHEAIIRFTSELFYEQKLVASGKQPRH---- 1057
Cdd:TIGR00376 390 LAGDHKQLPPTILSHDAEE--LSLTLFERLIKEYPER--SRTLNVQ-YRMNQKIMEFPSREFYNGKLTAHESVANIllrd 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 1058 -------------DRFYPLTFFTTRG---EDVQDKNSTAFYNNAEVYEVVERVSELRKRwpsawgKLNDTSIGIMTPYSD 1121
Cdd:TIGR00376 465 lpkveateseddlETGIPLLFIDTSGcelFELKEADSTSKYNPGEAELVSEIIQALVKM------GVPANDIGVITPYDA 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 1122 QVFRIRsELRKRRMGGISVERVLNVQGKQFRAVFLSTVRTRRtcmpqgsapgsasttsigdaDADYGFLSNSKLLNTAIT 1201
Cdd:TIGR00376 539 QVDLLR-QLLEHRHIDIEVSSVDGFQGREKEVIIISFVRSNR--------------------KGEVGFLKDLRRLNVALT 597
|
650 660 670
....*....|....*....|....*....|....*
gi 442632370 1202 RAQSLVAVVGDPVALcsigRCRKVWERFIEICDEH 1236
Cdd:TIGR00376 598 RARRKLIVIGDSRTL----SNHKFYKRLIEWCKQH 628
|
|
| DEXXQc_Mov10L1 |
cd18078 |
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ... |
805-1030 |
2.47e-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: 155.60 E-value: 2.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 805 KLNAKQREAVNAITTALSIKLPPILLiGPFGTGKTYTLAQAIKQLLTQ-PEAKILICTHSNSAADLyIKEYLHP--WIEE 881
Cdd:cd18078 1 DLNELQKEAVKRILGGECRPLPYILF-GPPGTGKTVTIIEAILQVVYNlPRSRILVCAPSNSAADL-VTSRLHEskVLKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 882 GlkeaTPLRVYYHKRWSATVNGVVQKYCItdgvgnfLRPTVEDIMRHRIVVVTLSISMELATLGLPKGLFTHIFLDEAAQ 961
Cdd:cd18078 79 G----DMVRLNAVNRFESTVIDARKLYCR-------LGEDLSKASRHRIVISTCSTAGLLYQMGLPVGHFTHVFVDEAGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 962 AMECEAIMPLALANDST-RIVLAGDHMQMSPELFSAFAKERKLHISLLERL-----YDHYPSNFPCKIL--------LCE 1027
Cdd:cd18078 148 ATEPESLIPLGLISSRDgQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLmnrplYLRDPNRFGESGGynpllvtkLVD 227
|
...
gi 442632370 1028 NYR 1030
Cdd:cd18078 228 NYR 230
|
|
| DEXXQc_SMUBP2 |
cd18044 |
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ... |
805-1030 |
5.36e-26 |
|
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, or IGHMBP2) is a 5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction. It is a DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence (5'-GGGCT-3') related to the immunoglobulin mu chain switch region. The IGHMBP2 gene is responsible for Charcot-Marie-Tooth disease (CMT) type 2S and spinal muscular atrophy with respiratory distress type 1 (SMARD1). It is also thought to play a role in frontotemporal dementia (FTD) with amyotrophic lateral sclerosis (ALS) and major depressive disorder (MDD). SMUBP2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350802 [Multi-domain] Cd Length: 191 Bit Score: 107.31 E-value: 5.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 805 KLNAKQREAVNaittaLSIKLPPILLI-GPFGTGKTYTLAQAIKQLLtQPEAKILICTHSNSAADlYIKEYLhpwIEEGL 883
Cdd:cd18044 1 NLNDSQKEAVK-----FALSQKDVALIhGPPGTGKTTTVVEIILQAV-KRGEKVLACAPSNIAVD-NLVERL---VALKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 884 KeatPLRVYYHKRwsatVNGVVQKYCItdgvgnflrptvEDIMRHRIVVVTLSISMelATLGLPKGLFTHIFLDEAAQAM 963
Cdd:cd18044 71 K---VVRIGHPAR----LLESVLDHSL------------DALVAAQVVLATNTGAG--SRQLLPNELFDVVVIDEAAQAL 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442632370 964 ECEAIMPLALANdstRIVLAGDHMQMSPELFSAFAKERKLHISLLERLYDHYPSNfpCKILLCENYR 1030
Cdd:cd18044 130 EASCWIPLLKAR---RCILAGDHKQLPPTILSDKAARGGLGVTLFERLVNLYGES--VVRMLTVQYR 191
|
|
| DEXXQc_DNA2 |
cd18041 |
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ... |
805-1030 |
9.32e-20 |
|
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: 89.60 E-value: 9.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 805 KLNAKQREAVNAITTALSIKLppILliGPFGTGKTYTLAQAIKQLLTQPEaKILICTHSNSAAD-LYIKeyLHPWIEEGL 883
Cdd:cd18041 1 GLNKDQRQAIKKVLNAKDYAL--IL--GMPGTGKTTTIAALVRILVALGK-SVLLTSYTHSAVDnILLK--LKKFGVNFL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 884 KEATPLRVyyHKRwsatvngvVQKYCITDGVGNFlrPTVEDI----MRHRIVVVT-LSISMELatlgLPKGLFTHIFLDE 958
Cdd:cd18041 74 RLGRLKKI--HPD--------VQEFTLEAILKSC--KSVEELeskyESVSVVATTcLGINHPI----FRRRTFDYCIVDE 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442632370 959 AAQAMECEAIMPLALANdstRIVLAGDHMQMSPELFSAFAKERKLHISLLERLYDHYPSNFpckILLCENYR 1030
Cdd:cd18041 138 ASQITLPICLGPLRLAK---KFVLVGDHYQLPPLVKSREARELGMDESLFKRLSEAHPDAV---VQLTIQYR 203
|
|
| DEXXQc_UPF1 |
cd18039 |
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ... |
805-1030 |
8.88e-19 |
|
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: 87.69 E-value: 8.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 805 KLNAKQreaVNAITTALSiklPPILLI-GPFGTGKTYTLAQAIKQLLTQPEAKILICTHSNSAADlYIKEYLHpwiEEGL 883
Cdd:cd18039 1 ELNHSQ---VDAVKTALQ---RPLSLIqGPPGTGKTVTSATIVYHLVKQGNGPVLVCAPSNVAVD-QLTEKIH---QTGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 884 K---------EATPLRVYY---HK--RWSATVNGVVQKYCITDGVGNF----------LRPTVE-DIMRHRIVVVTLSIS 938
Cdd:cd18039 71 KvvrlcaksrEAVESPVSFlalHNqvRNLDSAEKLELLKLLKLETGELssadekryrkLKRKAErELLRNADVICCTCVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 939 MelATLGLPKGLFTHIFLDEAAQAMECEAIMPLALAndSTRIVLAGDHMQMSPELFSAFAKERKLHISLLERLYD--HYP 1016
Cdd:cd18039 151 A--GDPRLSKMKFRTVLIDEATQATEPECLIPLVHG--AKQVILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVQlgIRP 226
|
250
....*....|....
gi 442632370 1017 snfpckILLCENYR 1030
Cdd:cd18039 227 ------IRLQVQYR 234
|
|
| DEXXQc_SETX |
cd18042 |
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ... |
806-1030 |
4.56e-17 |
|
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: 82.26 E-value: 4.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 806 LNAKQREAVNAITtalsIKLPPILLI-GPFGTGKTYTL------------------------AQAIKQLLTQPEAKILIC 860
Cdd:cd18042 1 LNESQLEAIASAL----QNSPGITLIqGPPGTGKTKTIvgilsvllagkyrkyyekvkkklrKLQRNLNNKKKKNRILVC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 861 THSNSAADlyikEYLHPWIEEGLKeatplrvyyhkrwsatvngvvqkycitDGVGNFLRPTV-----EDIMRH-----RI 930
Cdd:cd18042 77 APSNAAVD----EIVLRLLSEGFL---------------------------DGDGRSYKPNVvrvgrQELRASilneaDI 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 931 VVVTLSIS--MELATLGLPkglFTHIFLDEAAQAMECEAIMPLALanDSTRIVLAGDHMQMSPELFSAFAKERKLHISLL 1008
Cdd:cd18042 126 VCTTLSSSgsDLLESLPRG---FDTVIIDEAAQAVELSTLIPLRL--GCKRLILVGDPKQLPATVFSKVAQKLGYDRSLF 200
|
250 260
....*....|....*....|..
gi 442632370 1009 ERLYDHypsNFPCkILLCENYR 1030
Cdd:cd18042 201 ERLQLA---GYPV-LMLTTQYR 218
|
|
| EEXXEc_NFX1 |
cd17936 |
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ... |
806-1024 |
1.74e-12 |
|
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: 67.95 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 806 LNAKQREA-VNAITTALSIklppilLIGPFGTGKTYTLAQAIKQLLT----QPEAKILICTHSNSAADlyikEYLhpwie 880
Cdd:cd17936 2 LDPSQLEAlKHALTSELAL------IQGPPGTGKTFLGVKLVRALLQnqdlSITGPILVVCYTNHALD----QFL----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 881 EGLKEATPlrvyyhkrwsatvngvvqkycitdgvgnflrptvEDIMRH--RIVVVTLSISMELATLgLPKGLFTHIFLDE 958
Cdd:cd17936 67 EGLLDFGP----------------------------------TKIVRLgaRVIGMTTTGAAKYREL-LQALGPKVVIVEE 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632370 959 AAQAMECEAIMplALANDSTRIVLAGDHMQMSP--ELFSAFAKERKLHISLLERLYDhypSNFPCKIL 1024
Cdd:cd17936 112 AAEVLEAHILA--ALTPSTEHLILIGDHKQLRPkvNVYELTAKKYNLDVSLFERLVK---NGLPFVTL 174
|
|
| DEXXQc_Upf1-like |
cd17934 |
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ... |
829-1030 |
7.88e-12 |
|
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: 64.18 E-value: 7.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 829 LLIGPFGTGKTYTLAQAIKQLLTQ-PEAKILICTHSNSAADlyikeylhpwieeglkeatplrvyyhkrwsatvNgvvqk 907
Cdd:cd17934 3 LIQGPPGTGKTTTIAAIVLQLLKGlRGKRVLVTAQSNVAVD---------------------------------N----- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 908 ycitdgvgnflrptvedimrhrivvvtlsismelatlglpkglFTHIFLDEAAQAMECEAIMPLALAndsTRIVLAGDHM 987
Cdd:cd17934 45 -------------------------------------------VDVVIIDEASQITEPELLIALIRA---KKVVLVGDPK 78
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 442632370 988 QMSPELFS--AFAKERKLHISLLERLYDHYPsNFPcKILLCENYR 1030
Cdd:cd17934 79 QLPPVVQEdhAALLGLSFILSLLLLFRLLLP-GSP-KVMLDTQYR 121
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
815-995 |
8.60e-11 |
|
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: 64.29 E-value: 8.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 815 NAITTALSikLPPILLI-GPFGTGKTYTLAQAIKQLLTQPEA------KILICTHSNSAAD----LYIKEYL-------- 875
Cdd:pfam13086 4 EAIRSALS--SSHFTLIqGPPGTGKTTTIVELIRQLLSYPATsaaagpRILVCAPSNAAVDnileRLLRKGQkygpkivr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 876 --HP-WIEEGLKEAT---PLRVYYHKRWSAT---------------------VNGVVQKYCITDGVGNFLRPTVEDIM-- 926
Cdd:pfam13086 82 igHPaAISEAVLPVSldyLVESKLNNEEDAQivkdiskeleklakalrafekEIIVEKLLKSRNKDKSKLEQERRKLRse 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 927 ---------------------RHRIVVVTLSISMELATLGLPKglFTHIFLDEAAQAMECEAIMPLALAndSTRIVLAGD 985
Cdd:pfam13086 162 rkelrkelrrreqslereildEAQIVCSTLSGAGSRLLSSLAN--FDVVIIDEAAQALEPSTLIPLLRG--PKKVVLVGD 237
|
250
....*....|
gi 442632370 986 HMQMSPELFS 995
Cdd:pfam13086 238 PKQLPPTVIS 247
|
|
| EEXXQc_AQR |
cd17935 |
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ... |
805-1011 |
5.57e-09 |
|
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds precursor-mRNA introns at a defined position and is part of a pentameric intron-binding complex (IBC). It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350693 [Multi-domain] Cd Length: 207 Bit Score: 58.21 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 805 KLNAKQreaVNAITTALSIKLppILLIGPFGTGKTYTLAQAIKQLL-TQPEAKILICTHSNSAA-DLYIKeylhpwIEEg 882
Cdd:cd17935 5 KFTPTQ---IEAIRSGMQPGL--TMVVGPPGTGKTDVAVQIISNLYhNFPNQRTLIVTHSNQALnQLFEK------IMA- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 883 lkeatpLRVYyhkrwsatvngvvQKYCITDGVGNflrptvedimrhRIVVVT-LSISMELATLgLPKGL-FTHIFLDEAA 960
Cdd:cd17935 73 ------LDID-------------ERHLLRLGHGA------------KIIAMTcTHAALKRGEL-VELGFkYDNILMEEAA 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442632370 961 QAMECEAIMPLALANDST------RIVLAGDHMQMSPELFS-AFAKERKLHISLLERL 1011
Cdd:cd17935 121 QILEIETFIPLLLQNPEDgpnrlkRLIMIGDHHQLPPVIKNmAFQKYSNMEQSLFTRL 178
|
|
| DEXXc_HELZ2-C |
cd18040 |
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
805-1011 |
1.05e-07 |
|
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: 55.61 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 805 KLNAKQREAV-NAITTalsiklPPILLIGPFGTGKTYT----------LAQAIKQLLTQPEAK--ILICTHSNSAADLyI 871
Cdd:cd18040 1 KLNPSQNHAVrTALTK------PFTLIQGPPGTGKTVTgvhiaywfakQNREIQSVSGEGDGGpcVLYCGPSNKSVDV-V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 872 KEYLHPwiEEGLKeatPLRVY----------------------------YHKRWSATVNGVVQK----YC--ITDGVGNF 917
Cdd:cd18040 74 AELLLK--VPGLK---ILRVYseqietteypipneprhpnkksereskpNSELSSITLHHRIRQpsnpHSqqIKAFEARF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 918 LRP----TVEDIMRHRIVVVTLSISmELATLGL---------PKGLFTH-----IFLDEAAQAMECEAIMPLALANDSTR 979
Cdd:cd18040 149 ERTqekiTEEDIKTYKILIWEARFE-ELETVDVilctcseaaSQKMRTHanvkqCIVDECGMCTEPESLIPIVSAPRAEQ 227
|
250 260 270
....*....|....*....|....*....|..
gi 442632370 980 IVLAGDHMQMSPELFSAFAKERKLHISLLERL 1011
Cdd:cd18040 228 VVLIGDHKQLRPVVQNKEAQKLGLGRSLFERY 259
|
|
| DEXXQc_SF1 |
cd18043 |
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ... |
807-994 |
5.92e-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: 50.27 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 807 NAKQREAVNAITTALSIklppiLLIGPFGTGKTYTLAQAIKQLLTQPEaKILICTHSNSAADlyikeylhpwieeglkea 886
Cdd:cd18043 1 DSSQEAAIISARNGKNV-----VIQGPPGTGKSQTIANIIANALARGK-RVLFVSEKKAALD------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 887 tplrvyyhkrwsatvngVVQKYCItdgvgnflrptvedIMRHRIVvvtlsismeLATLGLPKGLFTHIFLDEAAQAMECE 966
Cdd:cd18043 57 -----------------VVRFPCW--------------IMSPLSV---------SQYLPLNRNLFDLVIFDEASQIPIEE 96
|
170 180
....*....|....*....|....*...
gi 442632370 967 AIMPLALANdstRIVLAGDHMQMSPELF 994
Cdd:cd18043 97 ALPALFRGK---QVVVVGDDKQLPPSIL 121
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
803-959 |
5.96e-07 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 54.65 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 803 EPKLNAKQREAVNAITTALSIKLPPILLIGPFGTGKTYTLAQAIKQLLTQPeaKILICTHSnsaadlyiKEYLHPWIEEg 882
Cdd:COG1061 78 SFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGK--RVLVLVPR--------RELLEQWAEE- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 883 LKEATPLRVYYHKRWSATvngvvqkycitdgvgnflrptvedimrHRIVVVT---LSISMELATLGlpkGLFTHIFLDEA 959
Cdd:COG1061 147 LRRFLGDPLAGGGKKDSD---------------------------APITVATyqsLARRAHLDELG---DRFGLVIIDEA 196
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
809-991 |
3.19e-06 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350691 [Multi-domain] Cd Length: 155 Bit Score: 49.09 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 809 KQREAVNAITTAlsiklPPILLIGPFGTGKTYTLAQAIKqLLTQPEAKILICTHSNSAADlyikeylhpwieeGLKEATP 888
Cdd:cd17933 1 EQKAAVRLVLRN-----RVSVLTGGAGTGKTTTLKALLA-ALEAEGKRVVLAAPTGKAAK-------------RLSESTG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 889 LRVYyhkrwsaTvngvVQKYCITDGVGNFLRPTVEDIMRHRIVVVTlSISMelatLGLPkgLFTHIfldeaaqameceai 968
Cdd:cd17933 62 IEAS-------T----IHRLLGINPGGGGFYYNEENPLDADLLIVD-EASM----VDTR--LMAAL-------------- 109
|
170 180
....*....|....*....|...
gi 442632370 969 mpLALANDSTRIVLAGDHMQMSP 991
Cdd:cd17933 110 --LSAIPAGARLILVGDPDQLPS 130
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
810-886 |
7.03e-06 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 47.91 E-value: 7.03e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632370 810 QREAVNAITTALSIK-LPPILLIGPFGTGKTyTLAQAIKQLLTQPEAKILICTHSNSAADLYIKEYLHPWIEEGLKEA 886
Cdd:cd00009 3 QEEAIEALREALELPpPKNLLLYGPPGTGKT-TLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFEL 79
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
803-959 |
1.87e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 46.90 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 803 EPKLNAKQREAVNAITTALSIKLPPILLIGPFGTGKTYTLAQAIKQLLTQ-PEAKILICTHSNsaaDLYIKeylhpWIEE 881
Cdd:pfam04851 1 KLELRPYQIEAIENLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKgPIKKVLFLVPRK---DLLEQ-----ALEE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 882 glkeatplrvyYHKRWSATVNGvvqkycITDGVGNFLRPTVEDImrhRIVVVT---LSISMELATLGLPKGLFTHIFLDE 958
Cdd:pfam04851 73 -----------FKKFLPNYVEI------GEIISGDKKDESVDDN---KIVVTTiqsLYKALELASLELLPDFFDVIIIDE 132
|
.
gi 442632370 959 A 959
Cdd:pfam04851 133 A 133
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
810-865 |
4.16e-05 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs 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: 350790 [Multi-domain] Cd Length: 163 Bit Score: 46.02 E-value: 4.16e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 442632370 810 QREAVNAITTALSIKLPPILLIGPFGTGKTYTLAQAIKQLL-TQPEAKILICTHSNS 865
Cdd:cd18032 5 QQEAIEALEEAREKGQRRALLVMATGTGKTYTAAFLIKRLLeANRKKRILFLAHREE 61
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
744-867 |
4.88e-05 |
|
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: 48.43 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 744 ALQADTELEVDIQFQLNRMPYCEWHNAVDKITDFRLIFPATELEPSIPWtpkkqWADSCEPKLNAKQREAVNAITTALSI 823
Cdd:COG0507 68 ALVESGPLVLDGRRYLTRLLEAEQRLARRLRRLARPALDEADVEAALAA-----LEPRAGITLSDEQREAVALALTTRRV 142
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 442632370 824 klppILLIGPFGTGKTYTLAqAIKQLLTQPEAKILICTHSNSAA 867
Cdd:COG0507 143 ----SVLTGGAGTGKTTTLR-ALLAALEALGLRVALAAPTGKAA 181
|
|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
827-868 |
6.15e-05 |
|
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: 44.40 E-value: 6.15e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 442632370 827 PILLIGPFGTGKTYTLAQAIKQLLTQ---PEAKILICTHSNSAAD 868
Cdd:cd17914 1 LSLIQGPPGTGKTRVLVKIVAALMQNkngEPGRILLVTPTNKAAA 45
|
|
| UvrD-helicase |
pfam00580 |
UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural ... |
806-868 |
8.36e-05 |
|
UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural domains. The Rep family function as dimers. REP helicases catalyze ATP dependent unwinding of double stranded DNA to single stranded DNA. Swiss:P23478, Swiss:P08394 have large insertions near to the carboxy-terminus relative to other members of the family.
Pssm-ID: 395462 [Multi-domain] Cd Length: 267 Bit Score: 46.47 E-value: 8.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442632370 806 LNAKQREAVNAITTalsiklpPILLIGPFGTGKTYTLAQAIKQLLTQ----PEaKILICTHSNSAAD 868
Cdd:pfam00580 1 LNPEQRKAVTHLGG-------PLLVLAGAGSGKTRVLTERIAYLILEggidPE-EILAVTFTNKAAR 59
|
|
| DEXQc_UvrD |
cd17932 |
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch ... |
807-1029 |
1.08e-04 |
|
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: 45.20 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 807 NAKQREAVNAITTalsiklpPILLI-GPfGTGKTYTLAQAIKQLL----TQPEaKILICTHSNSAADlYIKEYLHPWIee 881
Cdd:cd17932 1 NPEQREAVTHPDG-------PLLVLaGA-GSGKTRVLTHRIAYLIleggVPPE-RILAVTFTNKAAK-EMRERLRKLL-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 882 GLKEATPLRVY-YHkrwsATVNGVVQKYcitdgvGNFlrptvEDIMRHrivvvTLSIsMELATLGLPK--GLFTHIFLDE 958
Cdd:cd17932 69 GEQLASGVWIGtFH----SFALRILRRY------GDF-----DDLLLY-----ALEL-LEENPDVREKlqSRFRYILVDE 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632370 959 A-----AQamecEAIMpLALANDSTRIVLAGDHMQmspelfS--AFakeRKLHISLLERLYDHYPSnfPCKILLCENY 1029
Cdd:cd17932 128 YqdtnpLQ----YELL-KLLAGDGKNLFVVGDDDQ------SiyGF---RGADPENILDFEKDFPD--AKVIKLEENY 189
|
|
| zf-CCCH |
pfam00642 |
Zinc finger C-x8-C-x5-C-x3-H type (and similar); |
329-353 |
1.71e-04 |
|
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
Pssm-ID: 459885 [Multi-domain] Cd Length: 27 Bit Score: 40.25 E-value: 1.71e-04
|
| UvrD |
COG0210 |
Superfamily I DNA or RNA helicase [Replication, recombination and repair]; |
805-867 |
3.31e-04 |
|
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
Pssm-ID: 439980 [Multi-domain] Cd Length: 721 Bit Score: 45.70 E-value: 3.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632370 805 KLNAKQREAVNAIttalsikLPPILLI-GPfGTGKTYTLAQAIKQLLTQ----PEaKILICTHSNSAA 867
Cdd:COG0210 6 GLNPEQRAAVEHP-------EGPLLVLaGA-GSGKTRVLTHRIAYLIAEggvdPE-QILAVTFTNKAA 64
|
|
| AAA_19 |
pfam13245 |
AAA domain; |
810-868 |
5.36e-04 |
|
AAA domain;
Pssm-ID: 433059 [Multi-domain] Cd Length: 136 Bit Score: 42.21 E-value: 5.36e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442632370 810 QREAVNAITTAlsiklPPILLIGPFGTGKTYTLAQAIKQLLT--QPEAKILICTHSNSAAD 868
Cdd:pfam13245 1 QREAVRTALPS-----KVVLLTGGPGTGKTTTIRHIVALLVAlgGVSFPILLAAPTGRAAK 56
|
|
| AAA_30 |
pfam13604 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
806-991 |
7.02e-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: 42.94 E-value: 7.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 806 LNAKQREAVNAITT---ALSIklppilLIGPFGTGKTYTLAqAIKQLLTQPEAKILICTHSNSAADlyikeylhpwieeG 882
Cdd:pfam13604 2 LNAEQAAAVRALLTsgdRVAV------LVGPAGTGKTTALK-ALREAWEAAGYRVIGLAPTGRAAK-------------V 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 883 LKEATPLRvyyhkrwSATVNGVVqkYCITDGVgnflrptveDIMRHRIVVVtlsismelatlglpkglfthiflDEAAQA 962
Cdd:pfam13604 62 LGEELGIP-------ADTIAKLL--HRLGGRA---------GLDPGTLLIV-----------------------DEAGMV 100
|
170 180 190
....*....|....*....|....*....|
gi 442632370 963 MECEAIMPLALANDS-TRIVLAGDHMQMSP 991
Cdd:pfam13604 101 GTRQMARLLKLAEDAgARVILVGDPRQLPS 130
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
824-883 |
1.47e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.20 E-value: 1.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632370 824 KLPPILLIGPFGTGKTyTLAQAIKQLLTQPEAKILICTHSNSAADLYIKEYLHPWIEEGL 883
Cdd:smart00382 1 PGEVILIVGPPGSGKT-TLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKA 59
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
828-872 |
2.00e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 40.40 E-value: 2.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 442632370 828 ILLIGPFGTGKTYTLAQAIKQLLTQPEAKILI-CTHSNSAADLYIK 872
Cdd:pfam13401 8 LVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVdLPSGTSPKDLLRA 53
|
|
| DEAD-like_helicase_N |
cd17912 |
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ... |
828-867 |
5.60e-03 |
|
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase superfamily is a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. The N-terminal domain contains the ATP-binding region.
Pssm-ID: 350670 [Multi-domain] Cd Length: 81 Bit Score: 37.88 E-value: 5.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 442632370 828 ILLIGPFGTGKTYTLAQAIKQLLTQPEaKILICTHSNSAA 867
Cdd:cd17912 2 ILHLGPTGSGKTLVAIQKIASAMSSGK-SVLVVTPTKLLA 40
|
|
| |
