|
Name |
Accession |
Description |
Interval |
E-value |
| DEXXc_HELZ2-C |
cd18040 |
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
1583-1857 |
1.89e-151 |
|
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: 468.54 E-value: 1.89e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1583 KLNPSQNVAVREALEKPFTVIQGPPGTGKTIVGLHIVFWFHKSNQEQVQPGGpprgeKRLGGPCILYCGPSNKSVDVLAG 1662
Cdd:cd18040 1 KLNPSQNHAVRTALTKPFTLIQGPPGTGKTVTGVHIAYWFAKQNREIQSVSG-----EGDGGPCVLYCGPSNKSVDVVAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1663 LLLRRMELKPLRVYSEQAEASEFPVPRVGSRKLlRKSPREGRPNQSLRSITLHHRIRQAPNPYSSEIKAFDTRLQR-GEL 1741
Cdd:cd18040 76 LLLKVPGLKILRVYSEQIETTEYPIPNEPRHPN-KKSERESKPNSELSSITLHHRIRQPSNPHSQQIKAFEARFERtQEK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1742 FSREDLVWYKKVLWEARKFELDRHEVILCTCSCAASASLK-ILDVRQILVDEAGMATEPETLIPLVQFPQAEKVVLLGDH 1820
Cdd:cd18040 155 ITEEDIKTYKILIWEARFEELETVDVILCTCSEAASQKMRtHANVKQCIVDECGMCTEPESLIPIVSAPRAEQVVLIGDH 234
|
250 260 270
....*....|....*....|....*....|....*..
gi 156105695 1821 KQLRPVVKNERLQNLGLDRSLFERYHEDAHMLDTQYR 1857
Cdd:cd18040 235 KQLRPVVQNKEAQKLGLGRSLFERYAEKACMLDTQYR 271
|
|
| DEXXQc_HELZ2-N |
cd18076 |
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
6-175 |
4.93e-106 |
|
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: 338.40 E-value: 4.93e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 6 SRSAADIYIREYFHSHVSGGHPEATPLRVMYTDRPLSQTDPVTLQYCCLTDDRQAFRPPTRAELARHRVVVTTTSQAREL 85
Cdd:cd18076 61 TNSAADIYIREYFHPYVDKGHPEARPLRIKATDRPNAITDPDTITYCCLTKDRQCFRLPTRDELDFHNIVITTTAMAFNL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 86 RVPVGFFSHILIDEAAQMLECEALTPLAYASHGTRLVLAGDHMQVTPRLFSVARARAAEHTLLHRLFLCYQQETHEVARQ 165
Cdd:cd18076 141 HVLSGFFTHIFIDEAAQMLECEALIPLSYAGPKTRVVLAGDHMQMTPKLFSVADYNRANHTLLNRLFHYYQGEKHEVAVK 220
|
170
....*....|
gi 156105695 166 SRLVFHENYR 175
Cdd:cd18076 221 SRVIFSENYR 230
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1837-2042 |
1.53e-61 |
|
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: 209.33 E-value: 1.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1837 LDRSLFER----YHEDAHMLDTQYRMHEGICAFPSVAFYKSKLKTWQGLR-RPPSVLGHAGKESCPVIFGHVQGHErsll 1911
Cdd:pfam13087 1 LDRSLFERlqelGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAeRPLPDDFHLPDPLGPLVFIDVDGSE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1912 vSTDEGNENSKANLEEVAEVVRITKQLTLGRTVEPQDIAVLTPYNAQASEISKALRRE--GIAGVAVSSITKSQGSEWRY 1989
Cdd:pfam13087 77 -EEESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSDIGVITPYRAQVRLIRKLLKRKlgGKLEIEVNTVDGFQGREKDV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 156105695 1990 VLVSTVRTCAKSDldqrptkswlkkfLGFVVDPNQVNVAVTRAQEGLCLIGDH 2042
Cdd:pfam13087 156 IIFSCVRSNEKGG-------------IGFLSDPRRLNVALTRAKRGLIIVGNA 195
|
|
| RNB |
smart00955 |
This domain is the catalytic domain of ribonuclease II; |
765-1124 |
4.65e-60 |
|
This domain is the catalytic domain of ribonuclease II;
Pssm-ID: 214935 [Multi-domain] Cd Length: 286 Bit Score: 208.66 E-value: 4.65e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 765 REDCRAFLTFTVDPQGACNLDDALSVRDLGP-RCEVAVHITDVASFVPRDGVLDVEARRQGAAFYAPGRePVPMLPASLC 843
Cdd:smart00955 1 RVDLRDLPLFTIDPEDAKDIDDAVSVEKLDNgGYRLGVHIADVSHYVKPGSALDREARKRGTSVYLPDR-VIPMLPEELS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 844 QDVLSLLPGRDRLAISLFLTMEKASGQLKSLRFAPSVVQSDRQLSYEEAEEVIRQHpgagrelparldsvdacvvaacyf 923
Cdd:smart00955 80 NGLCSLNPGEDRLALSVEMTLDADGGEILDYEFYRSVIRSKARLTYEEVDAILEKI------------------------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 924 srllrrhrlrsdcfyeQPDEDGTLG------FRAAHIMVKEYMIQFNRLVAEFLVGSECTrtvTPLRWQPAPR----SQQ 993
Cdd:smart00955 136 ----------------VLDEEGKIEdivpreRNDAHSLVEEFMILANEAVARFLAKNGIP---GLYRVHEGPDpeklAEL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 994 LKALCEKHGDRVPLSlhlghhlhggggsppDTRLHLLASLWKqvqfaARTQDYEQMVDLVttddmhpflapagrdLRKAL 1073
Cdd:smart00955 197 LKEFLALLGLLLLGG---------------DGPKALAKLLEK-----IRDSPEERLLELL---------------LLRSM 241
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 156105695 1074 ERSAFGRcarghqQQGGHYSLQVDWYTWATSPIRRYLDVVLQRQILLALGH 1124
Cdd:smart00955 242 PHAEYSV------DNSGHFGLALDAYTHFTSPIRRYPDLIVHRQLKAALRG 286
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
1533-2068 |
2.30e-54 |
|
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: 202.74 E-value: 2.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1533 RKEEAVRGLEEASPLVTSIALGRPVPQPLCRVIPSRFLERQtynipggrhkLNPSQNVAVREAL-EKPFTVIQGPPGTGK 1611
Cdd:TIGR00376 117 RMKEALRALTENHSRLLEFLLGREAPSKASEIHDFQFFDPN----------LNESQKEAVLFALsSKDLFLIHGPPGTGK 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1612 TIVGLHIVfwfhksnQEQVQpggppRGEKrlggpcILYCGPSNKSVDVlaglLLRRMELKPLRVYseqaeasefpvpRVG 1691
Cdd:TIGR00376 187 TRTVVELI-------RQLVK-----RGLR------VLVTAPSNIAVDN----LLERLALCDQKIV------------RLG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1692 SRKLLRKSPREgrpnQSLRSITLHHRIRQAPNPYSSEIKAF-------------------DTRLQRGELFSRE-----DL 1747
Cdd:TIGR00376 233 HPARLLKSNKQ----HSLDYLIENHPKYQIVADIREKIDELieernkktkpspqkrrglsDIKILRKALKKREargieSL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1748 VWYKKVLWEARKFELDR----------------HEVILCTCSCAASASLKILDVRQILVDEAGMATEPETLIPLVqfpQA 1811
Cdd:TIGR00376 309 KIASMAEWIETNKSIDRllkllpeseerimneiLAESDATNSMAGSEILNGQYFDVAVIDEASQAMEPSCLIPLL---KA 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1812 EKVVLLGDHKQLRPVVKNErlQNLGLDRSLFER----YHEDAHMLDTQYRMHEGICAFPSVAFYKSKLK-----TWQGLR 1882
Cdd:TIGR00376 386 RKLILAGDHKQLPPTILSH--DAEELSLTLFERlikeYPERSRTLNVQYRMNQKIMEFPSREFYNGKLTahesvANILLR 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1883 RPPSVlgHAGKESC------PVIFGHVQGHERSLLvstDEGNENSKANLEEVAEVVRITKQLtLGRTVEPQDIAVLTPYN 1956
Cdd:TIGR00376 464 DLPKV--EATESEDdletgiPLLFIDTSGCELFEL---KEADSTSKYNPGEAELVSEIIQAL-VKMGVPANDIGVITPYD 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1957 AQASEISKALRREGIaGVAVSSITKSQGSEWRYVLVSTVRTCAKSDldqrptkswlkkfLGFVVDPNQVNVAVTRAQEGL 2036
Cdd:TIGR00376 538 AQVDLLRQLLEHRHI-DIEVSSVDGFQGREKEVIIISFVRSNRKGE-------------VGFLKDLRRLNVALTRARRKL 603
|
570 580 590
....*....|....*....|....*....|..
gi 156105695 2037 CLIGDHLLLRCCPLWRSLLDFCEAQQTLVPAG 2068
Cdd:TIGR00376 604 IVIGDSRTLSNHKFYKRLIEWCKQHGEVREAF 635
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
1657-2061 |
1.74e-51 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 197.27 E-value: 1.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1657 VDVLAGLLLRRMELKPLRVYSEQAEASEFPVPRVGSRKLLRKSPREGRPNQSLRSITLHHRIRQAPNPYSSEIKAFDTRL 1736
Cdd:COG1112 428 LLALALLAALLALLLLLAAALAALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPEELEKLIAELREAA 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1737 QRGELFSREdLVWYKKVLWEARKFELDRHEVILCTC-SCAASASLKILDVRQILVDEAGMATEPETLIPLVQfpqAEKVV 1815
Cdd:COG1112 508 RLRRALRRE-LKKRRELRKLLWDALLELAPVVGMTPaSVARLLPLGEGSFDLVIIDEASQATLAEALGALAR---AKRVV 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1816 LLGDHKQLRPVVKNER---LQNLGLDRSLFER----YHEDAHMLDTQYRMHEGICAFPSVAFYKSKLKTwqgLRRPPSVl 1888
Cdd:COG1112 584 LVGDPKQLPPVVFGEEaeeVAEEGLDESLLDRllarLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVP---LPSPKAR- 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1889 gHAGKESCPVIFGHVQGhersllvsTDEGNENSKANLEEVAEVVRITKQLtLGRTVEPQDIAVLTPYNAQASEISKALRR 1968
Cdd:COG1112 660 -RLADPDSPLVFIDVDG--------VYERRGGSRTNPEEAEAVVELVREL-LEDGPDGESIGVITPYRAQVALIRELLRE 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1969 E---GIAGVAVSSITKSQGSEWRYVLVSTVRTcakSDLDQRPTKSWLKKflgfvvDPNQVNVAVTRAQEGLCLIGDHLLL 2045
Cdd:COG1112 730 AlgdGLEPVFVGTVDRFQGDERDVIIFSLVYS---NDEDVPRNFGFLNG------GPRRLNVAVSRARRKLIVVGSRELL 800
|
410
....*....|....*....
gi 156105695 2046 RCCP---LWRSLLDFCEAQ 2061
Cdd:COG1112 801 DSDPstpALKRLLEYLERA 819
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
1858-2059 |
5.85e-50 |
|
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: 175.50 E-value: 5.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1858 MHEGICAFPSVAFYKSKLKTWQGLRRPPSVLgHAGKESCPVIFGHVQGHERSllvstdEGNENSKANLEEVAEVVRITKQ 1937
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKAGVSVAARLNPP-PLPGPSKPLVFVDVSGGEER------EESGTSKSNEAEAELVVELVKY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1938 LtLGRTVEPQDIAVLTPYNAQASEISKALRREGIA--GVAVSSITKSQGSEWRYVLVSTVRTCAKsdldqrptkswlKKF 2015
Cdd:cd18808 74 L-LKSGVKPSSIGVITPYRAQVALIRELLRKRGGLleDVEVGTVDNFQGREKDVIILSLVRSNES------------GGS 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 156105695 2016 LGFVVDPNQVNVAVTRAQEGLCLIGDHLLLRCCPLWRSLLDFCE 2059
Cdd:cd18808 141 IGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1587-1830 |
7.33e-49 |
|
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: 174.84 E-value: 7.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1587 SQNVAVREALEKP-FTVIQGPPGTGKTivgLHIVFWFHKSNQeqvqpggpPRGEKRLGGPCILYCGPSNKSVDVLAGLLL 1665
Cdd:pfam13086 1 SQREAIRSALSSShFTLIQGPPGTGKT---TTIVELIRQLLS--------YPATSAAAGPRILVCAPSNAAVDNILERLL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1666 RRME---LKPLRVYSEQAEASEfpvprvgSRKLLRKSPREGRPNQSlRSITLHHRIRQAPNPYSSEIKAF-----DTRLQ 1737
Cdd:pfam13086 70 RKGQkygPKIVRIGHPAAISEA-------VLPVSLDYLVESKLNNE-EDAQIVKDISKELEKLAKALRAFekeiiVEKLL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1738 RGELFSREDLVWYKKVLWEARK---------------FELDRHEVILCTCSCAASASLKILD-VRQILVDEAGMATEPET 1801
Cdd:pfam13086 142 KSRNKDKSKLEQERRKLRSERKelrkelrrreqslerEILDEAQIVCSTLSGAGSRLLSSLAnFDVVIIDEAAQALEPST 221
|
250 260
....*....|....*....|....*....
gi 156105695 1802 LIPLVQfpQAEKVVLLGDHKQLRPVVKNE 1830
Cdd:pfam13086 222 LIPLLR--GPKKVVLVGDPKQLPPTVISK 248
|
|
| RNB |
pfam00773 |
RNB domain; This domain is the catalytic domain of ribonuclease II. |
765-1122 |
1.18e-48 |
|
RNB domain; This domain is the catalytic domain of ribonuclease II.
Pssm-ID: 459934 [Multi-domain] Cd Length: 314 Bit Score: 176.71 E-value: 1.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 765 REDCRAFLTFTVDPQGACNLDDALSVRDLGP-RCEVAVHITDVASFVPRDGVLDVEARRQGAAFYAPGREpVPMLPASLC 843
Cdd:pfam00773 1 RKDLRDLPFITIDPADAKDLDDAISVEKLPNgGYRLGVHIADVSHYVPPGSPLDREARKRGTSVYLPDRV-IPMLPEKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 844 QDVLSLLPGRDRLAISLFLTMEKaSGQLKSLRFAPSVVQSDRQLSYEEAEEVIRQHPGAGRELP--ARLDSVDACV---- 917
Cdd:pfam00773 80 NDLCSLNPGEDRLALSVEITIDA-DGEVTSYEIYPSVIRSKARLTYEEVDDLLEGKDAEKDKPDlaEDLRLLYELAkilr 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 918 ---VAACYFSRLLRRHRLRSDcfYEQPDEDGTLGFRAAHIMVKEYMIQFNRLVAEFLvgsECTRTVTPLRWQPAPRSQQL 994
Cdd:pfam00773 159 akrLQRGALDLDTPENKLILD--EEGVIDILIQERTDAHSLIEEFMLLANEAVARHL---QELGIPALYRVHPEPDLEKL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 995 kalcekhgdrvplslhlghhlhggggsppdtrlhllASLWKQVQFAARTQDYEQmvDLVTTDDMHPFLAPAgrdLRKALE 1074
Cdd:pfam00773 234 ------------------------------------NSLIKLLQLLPDDKGLSK--SLEKIKDDERLLSIL---LLRTMP 272
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 156105695 1075 RSAFGrcarghQQQGGHYSLQVDWYTWATSPIRRYLDVVLQRQILLAL 1122
Cdd:pfam00773 273 RAEYS------PEPLGHFGLGLDIYTHFTSPIRRYPDLIVHRQLKALL 314
|
|
| VacB |
COG0557 |
Exoribonuclease R [Transcription]; |
597-1139 |
2.37e-39 |
|
Exoribonuclease R [Transcription];
Pssm-ID: 440323 [Multi-domain] Cd Length: 711 Bit Score: 158.35 E-value: 2.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 597 AFAGDEVLVQLLSGDKapEGRLRGRVLGVLKRKRHElaFVCRMDTWDPR-IMVPINGSVTK-IFVAELKdpsqvpiyslr 674
Cdd:COG0557 103 ALHGDRVLVRVTKEDR--RGRPEGRVVEILERANTR--VVGRFEKEKGFgFVVPDDKRLLQdIFIPPDD----------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 675 kgrlqrvglerlTAEARHSRLFWVQIVLWRQGFYYPLGIVREVLPEAStwEQGLRILGL--EYSLRV--PPS--DQA-TI 747
Cdd:COG0557 168 ------------LNGAKDGDLVVVEITRYPERRGPPEGRVVEVLGSPG--DPGAEILIAirKHGLPHefPEEvlAEAeAL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 748 TKVLQKyhTELGRvagrREDCRAFLTFTVDPQGACNLDDALSVRDLGPRC-EVAVHITDVASFVPRDGVLDVEARRQGAA 826
Cdd:COG0557 234 PDEVPE--ADLKG----RRDLRDLPLVTIDGEDAKDFDDAVSAEKLDNGGwRLGVHIADVSHYVRPGSALDREARKRGTS 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 827 FYAPGRePVPMLPASLCQDVLSLLPGRDRLAISLFLTMEkASGQLKSLRFAPSVVQSDRQLSYEEAEEVIRQHPGAGREL 906
Cdd:COG0557 308 VYLPDR-VIPMLPERLSNGLCSLNPGEDRLAMSCEMEID-AKGEVVSYEFYRSVIRSDARLTYEEVQAILDGKDEELREE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 907 P-------------------AR-------LDSVDACVVaacyFsrllrrhrlrsdcfyeqpDEDGTLG---FRA---AHI 954
Cdd:COG0557 386 YadlvpmleelyelakilrkARekrgaidFDLPETKII----L------------------DEEGKPEdivPRErndAHK 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 955 MVKEYMIQFNRLVAEFLVGSECTrtvTPLRWQPAP---RSQQLKALCEKHGdrvplslhlghhlhggggsppdtrLHLla 1031
Cdd:COG0557 444 LIEEFMLLANEAVAEFLEKLKLP---FLYRVHEEPdpeKLEALREFLANLG------------------------LKL-- 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1032 SLWKQVQfaarTQDYEQMVDLVttddmhpflapAGRD----LRKALERSafgrcarghQQQ-------GGHYSLQVDWYT 1100
Cdd:COG0557 495 KGGDEPT----PKDLQKLLEQV-----------KGRPeeelLNTLLLRS---------MKQavyspenIGHFGLALEAYT 550
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 156105695 1101 WATSPIRRYLDVVLQRQILLALGHGGSA----YSARDIDGLCQ 1139
Cdd:COG0557 551 HFTSPIRRYPDLLVHRALKAYLEGKRSPglqeYLEEELEEIAE 593
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
146-346 |
8.46e-38 |
|
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: 141.15 E-value: 8.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 146 TLLHRLFLCYQQethevarqSRLVFHENYRCTDAIVSFISRHFYVAK-GNPIHARGKVPPHPRH-----YPLMFCHVAGS 219
Cdd:pfam13087 4 SLFERLQELGPS--------AVVMLDTQYRMHPEIMEFPSKLFYGGKlKDGPSVAERPLPDDFHlpdplGPLVFIDVDGS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 220 PDRDM-SMASWLNLAEIAQVVEKVQEAYNTWPSCWggreqRCICVVS-HGAQVSALRQELRRRDLG--QVSVGSFEILPG 295
Cdd:pfam13087 76 EEEESdGGTSYSNEAEAELVVQLVEKLIKSGPEEP-----SDIGVITpYRAQVRLIRKLLKRKLGGklEIEVNTVDGFQG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 156105695 296 RQFRVVVLSTVHTCQSllspGALApeFFTDARVLNTVLTRAQSQLVVVGDA 346
Cdd:pfam13087 151 REKDVIIFSCVRSNEK----GGIG--FLSDPRRLNVALTRAKRGLIIVGNA 195
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
179-363 |
1.60e-35 |
|
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: 134.28 E-value: 1.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 179 AIVSFISRHFY----VAKGNPIHARGKVPPHPRHYPLMFCHVAGSPDRDMSMASWLNLAEIAQVVEKVQEAYNTwpscwg 254
Cdd:cd18808 4 EISEFPSKLFYegklKAGVSVAARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKS------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 255 GREQRCICVVSH-GAQVSALRQELRRR--DLGQVSVGSFEILPGRQFRVVVLSTVHTCQSLLSPGalapeFFTDARVLNT 331
Cdd:cd18808 78 GVKPSSIGVITPyRAQVALIRELLRKRggLLEDVEVGTVDNFQGREKDVIILSLVRSNESGGSIG-----FLSDPRRLNV 152
|
170 180 190
....*....|....*....|....*....|..
gi 156105695 332 VLTRAQSQLVVVGDAVALCSFGACGKLWESFI 363
Cdd:cd18808 153 ALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
54-346 |
1.92e-31 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 134.49 E-value: 1.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 54 LTDDRQAFRPPTRAELARHRVVVTTTSQ-ARELRVPVGFFSHILIDEAAQMLECEALTPLAYAShgtRLVLAGDHMQVTP 132
Cdd:COG1112 517 LKKRRELRKLLWDALLELAPVVGMTPASvARLLPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPP 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 133 RLFSVARARAAEH----TLLHRLFLCYQQethevaRQSRLVFHenYRCTDAIVSFISRHFYvakGNPIHARGKVPPHPR- 207
Cdd:COG1112 594 VVFGEEAEEVAEEgldeSLLDRLLARLPE------RGVMLREH--YRMHPEIIAFSNRLFY---DGKLVPLPSPKARRLa 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 208 --HYPLMFCHVAGSPDRDMSmaSWLNLAEIAQVVEKVQEAYNTWPscwggrEQRCICVVS-HGAQVSALRQELRRRDLG- 283
Cdd:COG1112 663 dpDSPLVFIDVDGVYERRGG--SRTNPEEAEAVVELVRELLEDGP------DGESIGVITpYRAQVALIRELLREALGDg 734
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156105695 284 --QVSVGSFEILPGRQFRVVVLSTVhtcqslLSPGALAPEFF----TDARVLNTVLTRAQSQLVVVGDA 346
Cdd:COG1112 735 lePVFVGTVDRFQGDERDVIIFSLV------YSNDEDVPRNFgflnGGPRRLNVAVSRARRKLIVVGSR 797
|
|
| 3_prime_RNase |
TIGR00358 |
VacB and RNase II family 3'-5' exoribonucleases; This model is defined to identify a pair of ... |
765-1156 |
1.28e-22 |
|
VacB and RNase II family 3'-5' exoribonucleases; This model is defined to identify a pair of paralogous 3-prime exoribonucleases in E. coli, plus the set of proteins apparently orthologous to one or the other in other eubacteria. VacB was characterized originally as required for the expression of virulence genes, but is now recognized as the exoribonuclease RNase R (Rnr). Its paralog in E. coli and H. influenzae is designated exoribonuclease II (Rnb). Both are involved in the degradation of mRNA, and consequently have strong pleiotropic effects that may be difficult to disentangle. Both these proteins share domain-level similarity (RNB, S1) with a considerable number of other proteins, and full-length similarity scoring below the trusted cutoff to proteins associated with various phenotypes but uncertain biochemistry; it may be that these latter proteins are also 3-prime exoribonucleases. [Transcription, Degradation of RNA]
Pssm-ID: 273033 [Multi-domain] Cd Length: 654 Bit Score: 105.18 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 765 REDCRAFLTFTVDPQGACNLDDALSVRDLGPR-CEVAVHITDVASFVPRDGVLDVEARRQGAAFYAPGREpVPMLPASLC 843
Cdd:TIGR00358 194 REDLTDLAFVTIDGADAKDLDDAVYVKKLPDGgWKLYVAIADVSYYVAENSPLDKEAKHRGFSVYLPGFV-IPMLPEELS 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 844 QDVLSLLPGRDRLAISLFLTMEkASGQLKSLRFAPSVVQSDRQLSYEEAEEVIRQHPGAGRELPARLDSVDAcvvAACYF 923
Cdd:TIGR00358 273 NGLCSLNPNEDRLVLVCEMTIS-AQGRITDNEFYPATIESKARLTYDKVNDWLENDDELQPEYETLVEQLKA---LHQLS 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 924 SRLLRRHRLRSDCFYEQP------DEDG------TLGFRAAHIMVKEYMIQFNRLVAEFLvgsECTRTVTPLRWQPAPRS 991
Cdd:TIGR00358 349 QALGEWRHKRGLIDFEHPetkfivDEEGrvidivAEVRRIAEKIIEEAMIVANICAARFL---HNHKVPGIYRVHPGPSK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 992 QQLKALCE---KHGDRVPLSLHLGHHLHGgggsppdtrlhlLASLWKQVqfaARTQDYEQMVDLvttddmhpflapagrd 1068
Cdd:TIGR00358 426 KKLQSLLEflaELGLTLPGGNAENVTTLD------------GACWLREV---KDRPEYEILVTR---------------- 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1069 LRKALERSAFgrcargHQQQGGHYSLQVDWYTWATSPIRRYLDVVLQRQILLALGHG----GSAYSARDIDGLCQAFSlq 1144
Cdd:TIGR00358 475 LLRSLSQAEY------SPEPLGHFGLGLEHYAHFTSPIRRYPDLTNHRLIKAVLAKEqtdtERYQPQDELLQIAEHCS-- 546
|
410
....*....|..
gi 156105695 1145 halaqSYQRRAR 1156
Cdd:TIGR00358 547 -----DTERRAR 553
|
|
| PRK11642 |
PRK11642 |
ribonuclease R; |
765-899 |
5.01e-09 |
|
ribonuclease R;
Pssm-ID: 236944 [Multi-domain] Cd Length: 813 Bit Score: 61.68 E-value: 5.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 765 REDCRAFLTFTVDPQGACNLDDALSV---RDLGPRCEVAvhITDVASFVPRDGVLDVEARRQGAAFYAPGrEPVPMLPAS 841
Cdd:PRK11642 260 RVDLRDLPLVTIDGEDARDFDDAVYCekkRGGGWRLWVA--IADVSYYVRPPTPLDREARNRGTSVYFPS-QVVPMLPEV 336
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156105695 842 LCQDVLSLLPGRDRLAISLFLTMEkASGQLKSLRFAPSVVQSDRQLSYE------EAEEVIRQH 899
Cdd:PRK11642 337 LSNGLCSLNPQVDRLCMVCEMTIS-SKGRLTGYKFYEAVMSSHARLTYTkvwhilQGDQDLREQ 399
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
65-136 |
3.43e-06 |
|
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: 50.81 E-value: 3.43e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156105695 65 TRAELARHRVVVTT--TSQARELRVPVGFFShILIDEAAQMLECEALTPLAYASHgtRLVLAGDHMQVTPRLFS 136
Cdd:pfam13086 177 EREILDEAQIVCSTlsGAGSRLLSSLANFDV-VIIDEAAQALEPSTLIPLLRGPK--KVVLVGDPKQLPPTVIS 247
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
1578-1988 |
2.72e-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: 49.20 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1578 PGGRHKLNPSQNVAVREALEK-PFTVIQGPPGTGKTIVGLHIVFWFHKSNQEqvqpggpprgekrlggpcILYCGPSNKS 1656
Cdd:COG0507 119 PRAGITLSDEQREAVALALTTrRVSVLTGGAGTGKTTTLRALLAALEALGLR------------------VALAAPTGKA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1657 VDVLaglllrrmelkplrvyseqAEASEFPvprvgsrkllrkspregrpnqslrSITLHHRIRQAPNpysseikafdtrl 1736
Cdd:COG0507 181 AKRL-------------------SESTGIE------------------------ARTIHRLLGLRPD------------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1737 qrgelfsredlvwykkvlweARKFELDRHEVilctcscaasasLKILDVrqILVDEAGMATEP--ETLIPLVQFPQAeKV 1814
Cdd:COG0507 205 --------------------SGRFRHNRDNP------------LTPADL--LVVDEASMVDTRlmAALLEALPRAGA-RL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1815 VLLGDHKQLRPVVKNERLqnlgldRSLFERYHEDAHMLDTQYRMHEGIcAFPSVAfyksklktwQGLR--RPPSVLGHAG 1892
Cdd:COG0507 250 ILVGDPDQLPSVGAGAVL------RDLIESGTVPVVELTEVYRQADDS-RIIELA---------HAIRegDAPEALNARY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1893 KEscpVIFGHVQGHERSllvstdegnenskanLEEVAEVVRitkqltlGRTVEPQDIAVLTPYNAQASEISKALRRE-GI 1971
Cdd:COG0507 314 AD---VVFVEAEDAEEA---------------AEAIVELYA-------DRPAGGEDIQVLAPTNAGVDALNQAIREAlNP 368
|
410
....*....|....*..
gi 156105695 1972 AGVAVSSITKSQGSEWR 1988
Cdd:COG0507 369 AGELERELAEDGELELY 385
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1481-1631 |
2.77e-03 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 42.45 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1481 DWDQERRADRQEAPRRVHLFVHH-MGMEKVPEEVLRPGTLFTVELLPKQLPDLRKEEAVRGLEEASPLVTSIALGRPVPQ 1559
Cdd:COG1401 102 EELYELEADSEIEAVGLLLELAErSDALEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAEL 181
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156105695 1560 PLCRVIPSRFLERQTYNIPGGRHKLNPSQNVAVREALE-KPFTVIQGPPGTGKTIVGLHIVFWFHKSNQEQVQ 1631
Cdd:COG1401 182 SAAEELYSEDLESEDDYLKDLLREKFEETLEAFLAALKtKKNVILAGPPGTGKTYLARRLAEALGGEDNGRIE 254
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DEXXc_HELZ2-C |
cd18040 |
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
1583-1857 |
1.89e-151 |
|
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: 468.54 E-value: 1.89e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1583 KLNPSQNVAVREALEKPFTVIQGPPGTGKTIVGLHIVFWFHKSNQEQVQPGGpprgeKRLGGPCILYCGPSNKSVDVLAG 1662
Cdd:cd18040 1 KLNPSQNHAVRTALTKPFTLIQGPPGTGKTVTGVHIAYWFAKQNREIQSVSG-----EGDGGPCVLYCGPSNKSVDVVAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1663 LLLRRMELKPLRVYSEQAEASEFPVPRVGSRKLlRKSPREGRPNQSLRSITLHHRIRQAPNPYSSEIKAFDTRLQR-GEL 1741
Cdd:cd18040 76 LLLKVPGLKILRVYSEQIETTEYPIPNEPRHPN-KKSERESKPNSELSSITLHHRIRQPSNPHSQQIKAFEARFERtQEK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1742 FSREDLVWYKKVLWEARKFELDRHEVILCTCSCAASASLK-ILDVRQILVDEAGMATEPETLIPLVQFPQAEKVVLLGDH 1820
Cdd:cd18040 155 ITEEDIKTYKILIWEARFEELETVDVILCTCSEAASQKMRtHANVKQCIVDECGMCTEPESLIPIVSAPRAEQVVLIGDH 234
|
250 260 270
....*....|....*....|....*....|....*..
gi 156105695 1821 KQLRPVVKNERLQNLGLDRSLFERYHEDAHMLDTQYR 1857
Cdd:cd18040 235 KQLRPVVQNKEAQKLGLGRSLFERYAEKACMLDTQYR 271
|
|
| DEXXQc_HELZ2-N |
cd18076 |
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
6-175 |
4.93e-106 |
|
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: 338.40 E-value: 4.93e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 6 SRSAADIYIREYFHSHVSGGHPEATPLRVMYTDRPLSQTDPVTLQYCCLTDDRQAFRPPTRAELARHRVVVTTTSQAREL 85
Cdd:cd18076 61 TNSAADIYIREYFHPYVDKGHPEARPLRIKATDRPNAITDPDTITYCCLTKDRQCFRLPTRDELDFHNIVITTTAMAFNL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 86 RVPVGFFSHILIDEAAQMLECEALTPLAYASHGTRLVLAGDHMQVTPRLFSVARARAAEHTLLHRLFLCYQQETHEVARQ 165
Cdd:cd18076 141 HVLSGFFTHIFIDEAAQMLECEALIPLSYAGPKTRVVLAGDHMQMTPKLFSVADYNRANHTLLNRLFHYYQGEKHEVAVK 220
|
170
....*....|
gi 156105695 166 SRLVFHENYR 175
Cdd:cd18076 221 SRVIFSENYR 230
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1837-2042 |
1.53e-61 |
|
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: 209.33 E-value: 1.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1837 LDRSLFER----YHEDAHMLDTQYRMHEGICAFPSVAFYKSKLKTWQGLR-RPPSVLGHAGKESCPVIFGHVQGHErsll 1911
Cdd:pfam13087 1 LDRSLFERlqelGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAeRPLPDDFHLPDPLGPLVFIDVDGSE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1912 vSTDEGNENSKANLEEVAEVVRITKQLTLGRTVEPQDIAVLTPYNAQASEISKALRRE--GIAGVAVSSITKSQGSEWRY 1989
Cdd:pfam13087 77 -EEESDGGTSYSNEAEAELVVQLVEKLIKSGPEEPSDIGVITPYRAQVRLIRKLLKRKlgGKLEIEVNTVDGFQGREKDV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 156105695 1990 VLVSTVRTCAKSDldqrptkswlkkfLGFVVDPNQVNVAVTRAQEGLCLIGDH 2042
Cdd:pfam13087 156 IIFSCVRSNEKGG-------------IGFLSDPRRLNVALTRAKRGLIIVGNA 195
|
|
| RNB |
smart00955 |
This domain is the catalytic domain of ribonuclease II; |
765-1124 |
4.65e-60 |
|
This domain is the catalytic domain of ribonuclease II;
Pssm-ID: 214935 [Multi-domain] Cd Length: 286 Bit Score: 208.66 E-value: 4.65e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 765 REDCRAFLTFTVDPQGACNLDDALSVRDLGP-RCEVAVHITDVASFVPRDGVLDVEARRQGAAFYAPGRePVPMLPASLC 843
Cdd:smart00955 1 RVDLRDLPLFTIDPEDAKDIDDAVSVEKLDNgGYRLGVHIADVSHYVKPGSALDREARKRGTSVYLPDR-VIPMLPEELS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 844 QDVLSLLPGRDRLAISLFLTMEKASGQLKSLRFAPSVVQSDRQLSYEEAEEVIRQHpgagrelparldsvdacvvaacyf 923
Cdd:smart00955 80 NGLCSLNPGEDRLALSVEMTLDADGGEILDYEFYRSVIRSKARLTYEEVDAILEKI------------------------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 924 srllrrhrlrsdcfyeQPDEDGTLG------FRAAHIMVKEYMIQFNRLVAEFLVGSECTrtvTPLRWQPAPR----SQQ 993
Cdd:smart00955 136 ----------------VLDEEGKIEdivpreRNDAHSLVEEFMILANEAVARFLAKNGIP---GLYRVHEGPDpeklAEL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 994 LKALCEKHGDRVPLSlhlghhlhggggsppDTRLHLLASLWKqvqfaARTQDYEQMVDLVttddmhpflapagrdLRKAL 1073
Cdd:smart00955 197 LKEFLALLGLLLLGG---------------DGPKALAKLLEK-----IRDSPEERLLELL---------------LLRSM 241
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 156105695 1074 ERSAFGRcarghqQQGGHYSLQVDWYTWATSPIRRYLDVVLQRQILLALGH 1124
Cdd:smart00955 242 PHAEYSV------DNSGHFGLALDAYTHFTSPIRRYPDLIVHRQLKAALRG 286
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
1533-2068 |
2.30e-54 |
|
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: 202.74 E-value: 2.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1533 RKEEAVRGLEEASPLVTSIALGRPVPQPLCRVIPSRFLERQtynipggrhkLNPSQNVAVREAL-EKPFTVIQGPPGTGK 1611
Cdd:TIGR00376 117 RMKEALRALTENHSRLLEFLLGREAPSKASEIHDFQFFDPN----------LNESQKEAVLFALsSKDLFLIHGPPGTGK 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1612 TIVGLHIVfwfhksnQEQVQpggppRGEKrlggpcILYCGPSNKSVDVlaglLLRRMELKPLRVYseqaeasefpvpRVG 1691
Cdd:TIGR00376 187 TRTVVELI-------RQLVK-----RGLR------VLVTAPSNIAVDN----LLERLALCDQKIV------------RLG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1692 SRKLLRKSPREgrpnQSLRSITLHHRIRQAPNPYSSEIKAF-------------------DTRLQRGELFSRE-----DL 1747
Cdd:TIGR00376 233 HPARLLKSNKQ----HSLDYLIENHPKYQIVADIREKIDELieernkktkpspqkrrglsDIKILRKALKKREargieSL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1748 VWYKKVLWEARKFELDR----------------HEVILCTCSCAASASLKILDVRQILVDEAGMATEPETLIPLVqfpQA 1811
Cdd:TIGR00376 309 KIASMAEWIETNKSIDRllkllpeseerimneiLAESDATNSMAGSEILNGQYFDVAVIDEASQAMEPSCLIPLL---KA 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1812 EKVVLLGDHKQLRPVVKNErlQNLGLDRSLFER----YHEDAHMLDTQYRMHEGICAFPSVAFYKSKLK-----TWQGLR 1882
Cdd:TIGR00376 386 RKLILAGDHKQLPPTILSH--DAEELSLTLFERlikeYPERSRTLNVQYRMNQKIMEFPSREFYNGKLTahesvANILLR 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1883 RPPSVlgHAGKESC------PVIFGHVQGHERSLLvstDEGNENSKANLEEVAEVVRITKQLtLGRTVEPQDIAVLTPYN 1956
Cdd:TIGR00376 464 DLPKV--EATESEDdletgiPLLFIDTSGCELFEL---KEADSTSKYNPGEAELVSEIIQAL-VKMGVPANDIGVITPYD 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1957 AQASEISKALRREGIaGVAVSSITKSQGSEWRYVLVSTVRTCAKSDldqrptkswlkkfLGFVVDPNQVNVAVTRAQEGL 2036
Cdd:TIGR00376 538 AQVDLLRQLLEHRHI-DIEVSSVDGFQGREKEVIIISFVRSNRKGE-------------VGFLKDLRRLNVALTRARRKL 603
|
570 580 590
....*....|....*....|....*....|..
gi 156105695 2037 CLIGDHLLLRCCPLWRSLLDFCEAQQTLVPAG 2068
Cdd:TIGR00376 604 IVIGDSRTLSNHKFYKRLIEWCKQHGEVREAF 635
|
|
| DEXXQc_UPF1 |
cd18039 |
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ... |
1583-1857 |
9.94e-53 |
|
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: 185.53 E-value: 9.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1583 KLNPSQNVAVREALEKPFTVIQGPPGTGKTIVGLHIVFWFHKSNQEQVqpggpprgekrlggpciLYCGPSNKSVDVLAg 1662
Cdd:cd18039 1 ELNHSQVDAVKTALQRPLSLIQGPPGTGKTVTSATIVYHLVKQGNGPV-----------------LVCAPSNVAVDQLT- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1663 LLLRRMELKPLRVYSEQAEASEFPVPrvgsrkllrkspregrpnqslrSITLHHRIRQAPNPYSSEIKAFdTRLQRGELf 1742
Cdd:cd18039 63 EKIHQTGLKVVRLCAKSREAVESPVS----------------------FLALHNQVRNLDSAEKLELLKL-LKLETGEL- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1743 SREDLVWYKKVLWEARKFELDRHEVILCTCSCAASASLKILDVRQILVDEAGMATEPETLIPLVQfpQAEKVVLLGDHKQ 1822
Cdd:cd18039 119 SSADEKRYRKLKRKAERELLRNADVICCTCVGAGDPRLSKMKFRTVLIDEATQATEPECLIPLVH--GAKQVILVGDHCQ 196
|
250 260 270
....*....|....*....|....*....|....*...
gi 156105695 1823 LRPVVKNERLQNLGLDRSLFERYHEDAH---MLDTQYR 1857
Cdd:cd18039 197 LGPVVMCKKAAKAGLSQSLFERLVQLGIrpiRLQVQYR 234
|
|
| DEXXQc_HELZ |
cd18077 |
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ... |
6-175 |
1.03e-51 |
|
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: 182.30 E-value: 1.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 6 SRSAADIYIREYFHSHVSGGHPEATPLRVMYTDRPLSQTDPVTLQYCcLTDDRQAFRPPTRAELARHRVVVTTTSQAREL 85
Cdd:cd18077 59 SNSAADLYIKEYLHPYVETGNPRARPLRVYYRNRWVKTVHPVVQKYC-LIDEHGTFRMPTREDVMRHRVVVVTLSTSQYL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 86 ---RVPVGFFSHILIDEAAQMLECEALTPLAYASHGTRLVLAGDHMQVTPRLFSV-ARARAAEHTLLHRLFLCYQQEthe 161
Cdd:cd18077 138 cqlDLEPGFFTHILLDEAAQAMECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEfARERNLHISLLERLYEHYPSE--- 214
|
170
....*....|....
gi 156105695 162 vaRQSRLVFHENYR 175
Cdd:cd18077 215 --HPCRILLCENYR 226
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
1657-2061 |
1.74e-51 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 197.27 E-value: 1.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1657 VDVLAGLLLRRMELKPLRVYSEQAEASEFPVPRVGSRKLLRKSPREGRPNQSLRSITLHHRIRQAPNPYSSEIKAFDTRL 1736
Cdd:COG1112 428 LLALALLAALLALLLLLAAALAALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPEELEKLIAELREAA 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1737 QRGELFSREdLVWYKKVLWEARKFELDRHEVILCTC-SCAASASLKILDVRQILVDEAGMATEPETLIPLVQfpqAEKVV 1815
Cdd:COG1112 508 RLRRALRRE-LKKRRELRKLLWDALLELAPVVGMTPaSVARLLPLGEGSFDLVIIDEASQATLAEALGALAR---AKRVV 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1816 LLGDHKQLRPVVKNER---LQNLGLDRSLFER----YHEDAHMLDTQYRMHEGICAFPSVAFYKSKLKTwqgLRRPPSVl 1888
Cdd:COG1112 584 LVGDPKQLPPVVFGEEaeeVAEEGLDESLLDRllarLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVP---LPSPKAR- 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1889 gHAGKESCPVIFGHVQGhersllvsTDEGNENSKANLEEVAEVVRITKQLtLGRTVEPQDIAVLTPYNAQASEISKALRR 1968
Cdd:COG1112 660 -RLADPDSPLVFIDVDG--------VYERRGGSRTNPEEAEAVVELVREL-LEDGPDGESIGVITPYRAQVALIRELLRE 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1969 E---GIAGVAVSSITKSQGSEWRYVLVSTVRTcakSDLDQRPTKSWLKKflgfvvDPNQVNVAVTRAQEGLCLIGDHLLL 2045
Cdd:COG1112 730 AlgdGLEPVFVGTVDRFQGDERDVIIFSLVYS---NDEDVPRNFGFLNG------GPRRLNVAVSRARRKLIVVGSRELL 800
|
410
....*....|....*....
gi 156105695 2046 RCCP---LWRSLLDFCEAQ 2061
Cdd:COG1112 801 DSDPstpALKRLLEYLERA 819
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
1858-2059 |
5.85e-50 |
|
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: 175.50 E-value: 5.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1858 MHEGICAFPSVAFYKSKLKTWQGLRRPPSVLgHAGKESCPVIFGHVQGHERSllvstdEGNENSKANLEEVAEVVRITKQ 1937
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKAGVSVAARLNPP-PLPGPSKPLVFVDVSGGEER------EESGTSKSNEAEAELVVELVKY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1938 LtLGRTVEPQDIAVLTPYNAQASEISKALRREGIA--GVAVSSITKSQGSEWRYVLVSTVRTCAKsdldqrptkswlKKF 2015
Cdd:cd18808 74 L-LKSGVKPSSIGVITPYRAQVALIRELLRKRGGLleDVEVGTVDNFQGREKDVIILSLVRSNES------------GGS 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 156105695 2016 LGFVVDPNQVNVAVTRAQEGLCLIGDHLLLRCCPLWRSLLDFCE 2059
Cdd:cd18808 141 IGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1587-1830 |
7.33e-49 |
|
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: 174.84 E-value: 7.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1587 SQNVAVREALEKP-FTVIQGPPGTGKTivgLHIVFWFHKSNQeqvqpggpPRGEKRLGGPCILYCGPSNKSVDVLAGLLL 1665
Cdd:pfam13086 1 SQREAIRSALSSShFTLIQGPPGTGKT---TTIVELIRQLLS--------YPATSAAAGPRILVCAPSNAAVDNILERLL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1666 RRME---LKPLRVYSEQAEASEfpvprvgSRKLLRKSPREGRPNQSlRSITLHHRIRQAPNPYSSEIKAF-----DTRLQ 1737
Cdd:pfam13086 70 RKGQkygPKIVRIGHPAAISEA-------VLPVSLDYLVESKLNNE-EDAQIVKDISKELEKLAKALRAFekeiiVEKLL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1738 RGELFSREDLVWYKKVLWEARK---------------FELDRHEVILCTCSCAASASLKILD-VRQILVDEAGMATEPET 1801
Cdd:pfam13086 142 KSRNKDKSKLEQERRKLRSERKelrkelrrreqslerEILDEAQIVCSTLSGAGSRLLSSLAnFDVVIIDEAAQALEPST 221
|
250 260
....*....|....*....|....*....
gi 156105695 1802 LIPLVQfpQAEKVVLLGDHKQLRPVVKNE 1830
Cdd:pfam13086 222 LIPLLR--GPKKVVLVGDPKQLPPTVISK 248
|
|
| RNB |
pfam00773 |
RNB domain; This domain is the catalytic domain of ribonuclease II. |
765-1122 |
1.18e-48 |
|
RNB domain; This domain is the catalytic domain of ribonuclease II.
Pssm-ID: 459934 [Multi-domain] Cd Length: 314 Bit Score: 176.71 E-value: 1.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 765 REDCRAFLTFTVDPQGACNLDDALSVRDLGP-RCEVAVHITDVASFVPRDGVLDVEARRQGAAFYAPGREpVPMLPASLC 843
Cdd:pfam00773 1 RKDLRDLPFITIDPADAKDLDDAISVEKLPNgGYRLGVHIADVSHYVPPGSPLDREARKRGTSVYLPDRV-IPMLPEKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 844 QDVLSLLPGRDRLAISLFLTMEKaSGQLKSLRFAPSVVQSDRQLSYEEAEEVIRQHPGAGRELP--ARLDSVDACV---- 917
Cdd:pfam00773 80 NDLCSLNPGEDRLALSVEITIDA-DGEVTSYEIYPSVIRSKARLTYEEVDDLLEGKDAEKDKPDlaEDLRLLYELAkilr 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 918 ---VAACYFSRLLRRHRLRSDcfYEQPDEDGTLGFRAAHIMVKEYMIQFNRLVAEFLvgsECTRTVTPLRWQPAPRSQQL 994
Cdd:pfam00773 159 akrLQRGALDLDTPENKLILD--EEGVIDILIQERTDAHSLIEEFMLLANEAVARHL---QELGIPALYRVHPEPDLEKL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 995 kalcekhgdrvplslhlghhlhggggsppdtrlhllASLWKQVQFAARTQDYEQmvDLVTTDDMHPFLAPAgrdLRKALE 1074
Cdd:pfam00773 234 ------------------------------------NSLIKLLQLLPDDKGLSK--SLEKIKDDERLLSIL---LLRTMP 272
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 156105695 1075 RSAFGrcarghQQQGGHYSLQVDWYTWATSPIRRYLDVVLQRQILLAL 1122
Cdd:pfam00773 273 RAEYS------PEPLGHFGLGLDIYTHFTSPIRRYPDLIVHRQLKALL 314
|
|
| DEXXQc_Helz-like |
cd18038 |
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ... |
5-175 |
8.72e-45 |
|
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: 162.40 E-value: 8.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 5 PSRSAADIYIREYFHShvsgGHPEATPLRVMYTDRPLSQTDPVTLQYCCLTDDRqAFRPPTRAELARHRVVVTTTSQA-- 82
Cdd:cd18038 58 PSNSAADLLAERLLNA----LVTKREILRLNAPSRDRASVPPELLPYCNSKAEG-TFRLPSLEELKKYRIVVCTLMTAgr 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 83 -RELRVPVGFFSHILIDEAAQMLECEALTPLAY-ASHGTRLVLAGDHMQVTPRLFS-VARARAAEHTLLHRLFLCYQ-QE 158
Cdd:cd18038 133 lVQAGVPNGHFTHIFIDEAGQATEPEALIPLSElASKNTQIVLAGDPKQLGPVVRSpLARKYGLGKSLLERLMERPLyYK 212
|
170
....*....|....*..
gi 156105695 159 THEVARQSRLVFHENYR 175
Cdd:cd18038 213 DGEYNPSYITKLLKNYR 229
|
|
| VacB |
COG0557 |
Exoribonuclease R [Transcription]; |
597-1139 |
2.37e-39 |
|
Exoribonuclease R [Transcription];
Pssm-ID: 440323 [Multi-domain] Cd Length: 711 Bit Score: 158.35 E-value: 2.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 597 AFAGDEVLVQLLSGDKapEGRLRGRVLGVLKRKRHElaFVCRMDTWDPR-IMVPINGSVTK-IFVAELKdpsqvpiyslr 674
Cdd:COG0557 103 ALHGDRVLVRVTKEDR--RGRPEGRVVEILERANTR--VVGRFEKEKGFgFVVPDDKRLLQdIFIPPDD----------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 675 kgrlqrvglerlTAEARHSRLFWVQIVLWRQGFYYPLGIVREVLPEAStwEQGLRILGL--EYSLRV--PPS--DQA-TI 747
Cdd:COG0557 168 ------------LNGAKDGDLVVVEITRYPERRGPPEGRVVEVLGSPG--DPGAEILIAirKHGLPHefPEEvlAEAeAL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 748 TKVLQKyhTELGRvagrREDCRAFLTFTVDPQGACNLDDALSVRDLGPRC-EVAVHITDVASFVPRDGVLDVEARRQGAA 826
Cdd:COG0557 234 PDEVPE--ADLKG----RRDLRDLPLVTIDGEDAKDFDDAVSAEKLDNGGwRLGVHIADVSHYVRPGSALDREARKRGTS 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 827 FYAPGRePVPMLPASLCQDVLSLLPGRDRLAISLFLTMEkASGQLKSLRFAPSVVQSDRQLSYEEAEEVIRQHPGAGREL 906
Cdd:COG0557 308 VYLPDR-VIPMLPERLSNGLCSLNPGEDRLAMSCEMEID-AKGEVVSYEFYRSVIRSDARLTYEEVQAILDGKDEELREE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 907 P-------------------AR-------LDSVDACVVaacyFsrllrrhrlrsdcfyeqpDEDGTLG---FRA---AHI 954
Cdd:COG0557 386 YadlvpmleelyelakilrkARekrgaidFDLPETKII----L------------------DEEGKPEdivPRErndAHK 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 955 MVKEYMIQFNRLVAEFLVGSECTrtvTPLRWQPAP---RSQQLKALCEKHGdrvplslhlghhlhggggsppdtrLHLla 1031
Cdd:COG0557 444 LIEEFMLLANEAVAEFLEKLKLP---FLYRVHEEPdpeKLEALREFLANLG------------------------LKL-- 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1032 SLWKQVQfaarTQDYEQMVDLVttddmhpflapAGRD----LRKALERSafgrcarghQQQ-------GGHYSLQVDWYT 1100
Cdd:COG0557 495 KGGDEPT----PKDLQKLLEQV-----------KGRPeeelLNTLLLRS---------MKQavyspenIGHFGLALEAYT 550
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 156105695 1101 WATSPIRRYLDVVLQRQILLALGHGGSA----YSARDIDGLCQ 1139
Cdd:COG0557 551 HFTSPIRRYPDLLVHRALKAYLEGKRSPglqeYLEEELEEIAE 593
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
146-346 |
8.46e-38 |
|
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: 141.15 E-value: 8.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 146 TLLHRLFLCYQQethevarqSRLVFHENYRCTDAIVSFISRHFYVAK-GNPIHARGKVPPHPRH-----YPLMFCHVAGS 219
Cdd:pfam13087 4 SLFERLQELGPS--------AVVMLDTQYRMHPEIMEFPSKLFYGGKlKDGPSVAERPLPDDFHlpdplGPLVFIDVDGS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 220 PDRDM-SMASWLNLAEIAQVVEKVQEAYNTWPSCWggreqRCICVVS-HGAQVSALRQELRRRDLG--QVSVGSFEILPG 295
Cdd:pfam13087 76 EEEESdGGTSYSNEAEAELVVQLVEKLIKSGPEEP-----SDIGVITpYRAQVRLIRKLLKRKLGGklEIEVNTVDGFQG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 156105695 296 RQFRVVVLSTVHTCQSllspGALApeFFTDARVLNTVLTRAQSQLVVVGDA 346
Cdd:pfam13087 151 REKDVIIFSCVRSNEK----GGIG--FLSDPRRLNVALTRAKRGLIIVGNA 195
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
179-363 |
1.60e-35 |
|
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: 134.28 E-value: 1.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 179 AIVSFISRHFY----VAKGNPIHARGKVPPHPRHYPLMFCHVAGSPDRDMSMASWLNLAEIAQVVEKVQEAYNTwpscwg 254
Cdd:cd18808 4 EISEFPSKLFYegklKAGVSVAARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKS------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 255 GREQRCICVVSH-GAQVSALRQELRRR--DLGQVSVGSFEILPGRQFRVVVLSTVHTCQSLLSPGalapeFFTDARVLNT 331
Cdd:cd18808 78 GVKPSSIGVITPyRAQVALIRELLRKRggLLEDVEVGTVDNFQGREKDVIILSLVRSNESGGSIG-----FLSDPRRLNV 152
|
170 180 190
....*....|....*....|....*....|..
gi 156105695 332 VLTRAQSQLVVVGDAVALCSFGACGKLWESFI 363
Cdd:cd18808 153 ALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
|
|
| DEXXQc_SETX |
cd18042 |
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ... |
1584-1857 |
1.06e-34 |
|
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: 133.11 E-value: 1.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1584 LNPSQNVAVREAL--EKPFTVIQGPPGTGKT--IVGL--HIVFWFHKSNQEQVQPGGPPRGEK---RLGGPCILYCGPSN 1654
Cdd:cd18042 1 LNESQLEAIASALqnSPGITLIQGPPGTGKTktIVGIlsVLLAGKYRKYYEKVKKKLRKLQRNlnnKKKKNRILVCAPSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1655 KSVDvlaGLLLRrmeLKPLRVYSEQAEASEFPVPRVGSRKLlRKSpregrpnqslrsitlhhrirqapnpysseikafdt 1734
Cdd:cd18042 81 AAVD---EIVLR---LLSEGFLDGDGRSYKPNVVRVGRQEL-RAS----------------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1735 rlqrgelfsredlvwykkVLWEArkfeldrhEVILCTCSCAASASLKILDVR--QILVDEAGMATEPETLIPLvQFpQAE 1812
Cdd:cd18042 119 ------------------ILNEA--------DIVCTTLSSSGSDLLESLPRGfdTVIIDEAAQAVELSTLIPL-RL-GCK 170
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 156105695 1813 KVVLLGDHKQLRPVVKNERLQNLGLDRSLFERYHE---DAHMLDTQYR 1857
Cdd:cd18042 171 RLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQLagyPVLMLTTQYR 218
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
54-346 |
1.92e-31 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 134.49 E-value: 1.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 54 LTDDRQAFRPPTRAELARHRVVVTTTSQ-ARELRVPVGFFSHILIDEAAQMLECEALTPLAYAShgtRLVLAGDHMQVTP 132
Cdd:COG1112 517 LKKRRELRKLLWDALLELAPVVGMTPASvARLLPLGEGSFDLVIIDEASQATLAEALGALARAK---RVVLVGDPKQLPP 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 133 RLFSVARARAAEH----TLLHRLFLCYQQethevaRQSRLVFHenYRCTDAIVSFISRHFYvakGNPIHARGKVPPHPR- 207
Cdd:COG1112 594 VVFGEEAEEVAEEgldeSLLDRLLARLPE------RGVMLREH--YRMHPEIIAFSNRLFY---DGKLVPLPSPKARRLa 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 208 --HYPLMFCHVAGSPDRDMSmaSWLNLAEIAQVVEKVQEAYNTWPscwggrEQRCICVVS-HGAQVSALRQELRRRDLG- 283
Cdd:COG1112 663 dpDSPLVFIDVDGVYERRGG--SRTNPEEAEAVVELVRELLEDGP------DGESIGVITpYRAQVALIRELLREALGDg 734
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156105695 284 --QVSVGSFEILPGRQFRVVVLSTVhtcqslLSPGALAPEFF----TDARVLNTVLTRAQSQLVVVGDA 346
Cdd:COG1112 735 lePVFVGTVDRFQGDERDVIIFSLV------YSNDEDVPRNFgflnGGPRRLNVAVSRARRKLIVVGSR 797
|
|
| DEXXQc_Helz-like |
cd18038 |
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ... |
1584-1844 |
1.77e-29 |
|
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: 118.49 E-value: 1.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1584 LNPSQNVAVREALEKPFT----VIQGPPGTGKTIVglhIVfwfhksnqE---QVqpggpprgEKRLGGPCILYCGPSNKS 1656
Cdd:cd18038 2 LNDEQKLAVRNIVTGTSRpppyIIFGPPGTGKTVT---LV--------EailQV--------LRQPPEARILVCAPSNSA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1657 VDVLAGLLLRRMELK--PLRVYSEQAEASEFPVPrvgsrkllrkspregrpnqslrsitlhhrirqaPNPYSSEIKAFDT 1734
Cdd:cd18038 63 ADLLAERLLNALVTKreILRLNAPSRDRASVPPE---------------------------------LLPYCNSKAEGTF 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1735 RLqrgelFSREdlvwykkvlwearkfELDRHEVILCTCSCAASasLKILDVRQ-----ILVDEAGMATEPETLIPLVQFP 1809
Cdd:cd18038 110 RL-----PSLE---------------ELKKYRIVVCTLMTAGR--LVQAGVPNghfthIFIDEAGQATEPEALIPLSELA 167
|
250 260 270
....*....|....*....|....*....|....*.
gi 156105695 1810 QAE-KVVLLGDHKQLRPVVKNERLQNLGLDRSLFER 1844
Cdd:cd18038 168 SKNtQIVLAGDPKQLGPVVRSPLARKYGLGKSLLER 203
|
|
| DEXXQc_SMUBP2 |
cd18044 |
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ... |
1583-1857 |
3.78e-25 |
|
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: 104.61 E-value: 3.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1583 KLNPSQNVAVREALE-KPFTVIQGPPGTGKTIVGLHIVfwfhksnQEQVQpggppRGEKrlggpcILYCGPSNKSVDVLA 1661
Cdd:cd18044 1 NLNDSQKEAVKFALSqKDVALIHGPPGTGKTTTVVEII-------LQAVK-----RGEK------VLACAPSNIAVDNLV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1662 GLLLRRMeLKPLRVyseqaeasefpvprvgsrkllrkspreGRPNQSLRSITLHhrirqapnpysseikAFDTRLQrgel 1741
Cdd:cd18044 63 ERLVALK-VKVVRI---------------------------GHPARLLESVLDH---------------SLDALVA---- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1742 fsredlvwykkvlweARkfeldrheVILCTCSCAASASLKIL---DVrqILVDEAGMATEPETLIPLVQFPqaeKVVLLG 1818
Cdd:cd18044 96 ---------------AQ--------VVLATNTGAGSRQLLPNelfDV--VVIDEAAQALEASCWIPLLKAR---RCILAG 147
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 156105695 1819 DHKQLRPVVKNERLQNLGLDRSLFER----YHEDAH-MLDTQYR 1857
Cdd:cd18044 148 DHKQLPPTILSDKAARGGLGVTLFERlvnlYGESVVrMLTVQYR 191
|
|
| 3_prime_RNase |
TIGR00358 |
VacB and RNase II family 3'-5' exoribonucleases; This model is defined to identify a pair of ... |
765-1156 |
1.28e-22 |
|
VacB and RNase II family 3'-5' exoribonucleases; This model is defined to identify a pair of paralogous 3-prime exoribonucleases in E. coli, plus the set of proteins apparently orthologous to one or the other in other eubacteria. VacB was characterized originally as required for the expression of virulence genes, but is now recognized as the exoribonuclease RNase R (Rnr). Its paralog in E. coli and H. influenzae is designated exoribonuclease II (Rnb). Both are involved in the degradation of mRNA, and consequently have strong pleiotropic effects that may be difficult to disentangle. Both these proteins share domain-level similarity (RNB, S1) with a considerable number of other proteins, and full-length similarity scoring below the trusted cutoff to proteins associated with various phenotypes but uncertain biochemistry; it may be that these latter proteins are also 3-prime exoribonucleases. [Transcription, Degradation of RNA]
Pssm-ID: 273033 [Multi-domain] Cd Length: 654 Bit Score: 105.18 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 765 REDCRAFLTFTVDPQGACNLDDALSVRDLGPR-CEVAVHITDVASFVPRDGVLDVEARRQGAAFYAPGREpVPMLPASLC 843
Cdd:TIGR00358 194 REDLTDLAFVTIDGADAKDLDDAVYVKKLPDGgWKLYVAIADVSYYVAENSPLDKEAKHRGFSVYLPGFV-IPMLPEELS 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 844 QDVLSLLPGRDRLAISLFLTMEkASGQLKSLRFAPSVVQSDRQLSYEEAEEVIRQHPGAGRELPARLDSVDAcvvAACYF 923
Cdd:TIGR00358 273 NGLCSLNPNEDRLVLVCEMTIS-AQGRITDNEFYPATIESKARLTYDKVNDWLENDDELQPEYETLVEQLKA---LHQLS 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 924 SRLLRRHRLRSDCFYEQP------DEDG------TLGFRAAHIMVKEYMIQFNRLVAEFLvgsECTRTVTPLRWQPAPRS 991
Cdd:TIGR00358 349 QALGEWRHKRGLIDFEHPetkfivDEEGrvidivAEVRRIAEKIIEEAMIVANICAARFL---HNHKVPGIYRVHPGPSK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 992 QQLKALCE---KHGDRVPLSLHLGHHLHGgggsppdtrlhlLASLWKQVqfaARTQDYEQMVDLvttddmhpflapagrd 1068
Cdd:TIGR00358 426 KKLQSLLEflaELGLTLPGGNAENVTTLD------------GACWLREV---KDRPEYEILVTR---------------- 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1069 LRKALERSAFgrcargHQQQGGHYSLQVDWYTWATSPIRRYLDVVLQRQILLALGHG----GSAYSARDIDGLCQAFSlq 1144
Cdd:TIGR00358 475 LLRSLSQAEY------SPEPLGHFGLGLEHYAHFTSPIRRYPDLTNHRLIKAVLAKEqtdtERYQPQDELLQIAEHCS-- 546
|
410
....*....|..
gi 156105695 1145 halaqSYQRRAR 1156
Cdd:TIGR00358 547 -----DTERRAR 553
|
|
| DEXXQc_DNA2 |
cd18041 |
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ... |
1583-1857 |
2.21e-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: 91.53 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1583 KLNPSQNVAVREALE-KPFTVIQGPPGTGKTIVGLHIVFWFHKSNQeqvqpggpprgekrlggpCILYCGPSNKSVDvla 1661
Cdd:cd18041 1 GLNKDQRQAIKKVLNaKDYALILGMPGTGKTTTIAALVRILVALGK------------------SVLLTSYTHSAVD--- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1662 GLLLRrmeLKPLRVyseqaeasefPVPRVGsrkllrkspregrpnqslRSITLHHRIRQapnpysseikafdtrlqrgel 1741
Cdd:cd18041 60 NILLK---LKKFGV----------NFLRLG------------------RLKKIHPDVQE--------------------- 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1742 FSREDLVWYKKVLWEARKFeLDRHEVILCTCSCAASASL--KILDVrqILVDEAGMATEPETLIPLVQfpqAEKVVLLGD 1819
Cdd:cd18041 88 FTLEAILKSCKSVEELESK-YESVSVVATTCLGINHPIFrrRTFDY--CIVDEASQITLPICLGPLRL---AKKFVLVGD 161
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 156105695 1820 HKQLRPVVKNERLQNLGLDRSLFERY---HEDAH-MLDTQYR 1857
Cdd:cd18041 162 HYQLPPLVKSREARELGMDESLFKRLseaHPDAVvQLTIQYR 203
|
|
| DEXXQc_Upf1-like |
cd17934 |
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ... |
1600-1857 |
1.23e-18 |
|
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: 83.44 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1600 FTVIQGPPGTGKTIVGLHIVFWFHKsnqeqvqpggpprgekRLGGPCILYCGPSNKSVDVlaglllrrmelkplrvyseq 1679
Cdd:cd17934 1 ISLIQGPPGTGKTTTIAAIVLQLLK----------------GLRGKRVLVTAQSNVAVDN-------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1680 aeasefpvprvgsrkllrkspregrpnqslrsitlhhrirqapnpysseikafdtrlqrgelfsredlvwykkvlweark 1759
Cdd:cd17934 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1760 feldrhevilctcscaasaslkildVRQILVDEAGMATEPETLIPLvqfPQAEKVVLLGDHKQLRPVVKNERLQNLG--- 1836
Cdd:cd17934 45 -------------------------VDVVIIDEASQITEPELLIAL---IRAKKVVLVGDPKQLPPVVQEDHAALLGlsf 96
|
250 260
....*....|....*....|....*
gi 156105695 1837 ----LDRSLFERYHEDAHMLDTQYR 1857
Cdd:cd17934 97 ilslLLLFRLLLPGSPKVMLDTQYR 121
|
|
| DEXXQc_Mov10L1 |
cd18078 |
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ... |
1583-1844 |
2.85e-17 |
|
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: 83.19 E-value: 2.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1583 KLNPSQNVAVREALEK-----PFtVIQGPPGTGKTIVGLHIVFwfhksnqeQVQpggpprgeKRLGGPCILYCGPSNKSV 1657
Cdd:cd18078 1 DLNELQKEAVKRILGGecrplPY-ILFGPPGTGKTVTIIEAIL--------QVV--------YNLPRSRILVCAPSNSAA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1658 DVLAgllLRRMELKPLRvyseqaeasefpvprvgsrkllrkspregrPNQSLRSITLHHRIRQapnpYSSEIKAFDTRLQ 1737
Cdd:cd18078 64 DLVT---SRLHESKVLK------------------------------PGDMVRLNAVNRFEST----VIDARKLYCRLGE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1738 RgelfsredlvwykkvLWEArkfelDRHEVILCTCScaASASLKILDVR-----QILVDEAGMATEPETLIPLVQFPQAE 1812
Cdd:cd18078 107 D---------------LSKA-----SRHRIVISTCS--TAGLLYQMGLPvghftHVFVDEAGQATEPESLIPLGLISSRD 164
|
250 260 270
....*....|....*....|....*....|...
gi 156105695 1813 -KVVLLGDHKQLRPVVKNERLQNLGLDRSLFER 1844
Cdd:cd18078 165 gQIILAGDPMQLGPVIKSRLASAYGLGVSFLER 197
|
|
| EEXXEc_NFX1 |
cd17936 |
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ... |
1584-1844 |
5.48e-17 |
|
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: 80.67 E-value: 5.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1584 LNPSQNVAVREALEKPFTVIQGPPGTGKTIVGLHIVF-WFHKSNQEQVQPggpprgekrlggpcILYCGPSNKSVDVLAG 1662
Cdd:cd17936 2 LDPSQLEALKHALTSELALIQGPPGTGKTFLGVKLVRaLLQNQDLSITGP--------------ILVVCYTNHALDQFLE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1663 LLLRRMELKplrvyseqaeasefpVPRVGsrkllrkspregrpnqslrsitlhhrirqapnpysseikafdtrlqrgelf 1742
Cdd:cd17936 68 GLLDFGPTK---------------IVRLG--------------------------------------------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1743 sredlvwykkvlwearkfeldrHEVILCTCSCAASAS--LKILDVRQILVDEAGMATEPETLIPLvqFPQAEKVVLLGDH 1820
Cdd:cd17936 82 ----------------------ARVIGMTTTGAAKYRelLQALGPKVVIVEEAAEVLEAHILAAL--TPSTEHLILIGDH 137
|
250 260
....*....|....*....|....*.
gi 156105695 1821 KQLRPVVKNERLQNLG--LDRSLFER 1844
Cdd:cd17936 138 KQLRPKVNVYELTAKKynLDVSLFER 163
|
|
| DEXXQc_Mov10L1 |
cd18078 |
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ... |
5-175 |
3.33e-13 |
|
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: 71.25 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 5 PSRSAADIYIREYfhsHVSGGHPEATPLRVMYTDRPLSQTDPVTLQYCCLTDDRQAfrpptraeLARHRVVVTTTSQA-- 82
Cdd:cd18078 58 PSNSAADLVTSRL---HESKVLKPGDMVRLNAVNRFESTVIDARKLYCRLGEDLSK--------ASRHRIVISTCSTAgl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 83 -RELRVPVGFFSHILIDEAAQMLECEALTPLAYASHGT-RLVLAGDHMQVTPRLFS-VARARAAEHTLLHRLFL--CYQQ 157
Cdd:cd18078 127 lYQMGLPVGHFTHVFVDEAGQATEPESLIPLGLISSRDgQIILAGDPMQLGPVIKSrLASAYGLGVSFLERLMNrpLYLR 206
|
170 180
....*....|....*....|....
gi 156105695 158 ET----HEVARQSRLVFH--ENYR 175
Cdd:cd18078 207 DPnrfgESGGYNPLLVTKlvDNYR 230
|
|
| EEXXQc_AQR |
cd17935 |
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ... |
1767-1864 |
1.37e-12 |
|
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: 68.99 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1767 VILCTCSCAAS--ASLKILDVR--QILVDEAGMATEPETLIPL-VQFPQAE-----KVVLLGDHKQLRPVVKNERLQNLG 1836
Cdd:cd17935 89 IIAMTCTHAALkrGELVELGFKydNILMEEAAQILEIETFIPLlLQNPEDGpnrlkRLIMIGDHHQLPPVIKNMAFQKYS 168
|
90 100 110
....*....|....*....|....*....|..
gi 156105695 1837 -LDRSLFERYHE---DAHMLDTQYRMHEGICA 1864
Cdd:cd17935 169 nMEQSLFTRLVRlgvPTVDLDAQGRARASISS 200
|
|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
1751-1844 |
4.89e-12 |
|
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: 64.81 E-value: 4.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1751 KKVLWEARKFELDRHEVILCTCSCAASASLkildvRQILVDEAGMATEPETLIPLVQFPQAEKVVLLGDHKQLRPVVKNE 1830
Cdd:cd17914 18 KIVAALMQNKNGEPGRILLVTPTNKAAAQL-----DNILVDEAAQILEPETSRLIDLALDQGRVILVGDHDQLGPVWRGA 92
|
90
....*....|....
gi 156105695 1831 RLQNLGLDRSLFER 1844
Cdd:cd17914 93 VLAKICNEQSLFTR 106
|
|
| PRK11642 |
PRK11642 |
ribonuclease R; |
765-899 |
5.01e-09 |
|
ribonuclease R;
Pssm-ID: 236944 [Multi-domain] Cd Length: 813 Bit Score: 61.68 E-value: 5.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 765 REDCRAFLTFTVDPQGACNLDDALSV---RDLGPRCEVAvhITDVASFVPRDGVLDVEARRQGAAFYAPGrEPVPMLPAS 841
Cdd:PRK11642 260 RVDLRDLPLVTIDGEDARDFDDAVYCekkRGGGWRLWVA--IADVSYYVRPPTPLDREARNRGTSVYFPS-QVVPMLPEV 336
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156105695 842 LCQDVLSLLPGRDRLAISLFLTMEkASGQLKSLRFAPSVVQSDRQLSYE------EAEEVIRQH 899
Cdd:PRK11642 337 LSNGLCSLNPQVDRLCMVCEMTIS-SKGRLTGYKFYEAVMSSHARLTYTkvwhilQGDQDLREQ 399
|
|
| SF1_C |
cd18786 |
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ... |
1948-2036 |
1.02e-08 |
|
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Similar to SF2 helicases, they do not form toroidal, predominantly hexameric structures like SF3-6. SF1 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. 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. The 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: 350173 [Multi-domain] Cd Length: 89 Bit Score: 54.37 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1948 DIAVLTPYNAQASEISKALRREGI-----AGVAVSSITKSQGSEWRYVLVSTVRtcAKSDldqrptkswlkkflgfvvDP 2022
Cdd:cd18786 12 KGVVLTPYHRDRAYLNQYLQGLSLdefdlQLVGAITIDSSQGLTFDVVTLYLPT--ANSL------------------TP 71
|
90
....*....|....
gi 156105695 2023 NQVNVAVTRAQEGL 2036
Cdd:cd18786 72 RRLYVALTRARKRL 85
|
|
| DEXXQc_UPF1 |
cd18039 |
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ... |
74-156 |
1.58e-08 |
|
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: 57.26 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 74 VVVTTTSQARELRVPVGFFSHILIDEAAQMLECEALTPLAYASHgtRLVLAGDHMQVTPRLFS--VARARAAeHTLLHRL 151
Cdd:cd18039 143 VICCTCVGAGDPRLSKMKFRTVLIDEATQATEPECLIPLVHGAK--QVILVGDHCQLGPVVMCkkAAKAGLS-QSLFERL 219
|
90
....*....|...
gi 156105695 152 --------FLCYQ 156
Cdd:cd18039 220 vqlgirpiRLQVQ 232
|
|
| DEXXQc_HELZ |
cd18077 |
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ... |
1761-1847 |
2.34e-08 |
|
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: 56.72 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1761 ELDRHEVI---LCTCSCAASASLKILDVRQILVDEAGMATEPETLIPLVQFPQAEKVVLLGDHKQLRPVVKNERLQNLGL 1837
Cdd:cd18077 120 DVMRHRVVvvtLSTSQYLCQLDLEPGFFTHILLDEAAQAMECEAIMPLALATKSTRIVLAGDHMQLSPEVYSEFARERNL 199
|
90
....*....|
gi 156105695 1838 DRSLFERYHE 1847
Cdd:cd18077 200 HISLLERLYE 209
|
|
| DEXXQc_SMUBP2 |
cd18044 |
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ... |
73-151 |
1.18e-07 |
|
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: 54.15 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 73 RVVVTTTSQA--RELRVPVgFFSHILIDEAAQMLECEALTPLAYAShgtRLVLAGDHMQVTPRLFSVARARAA-EHTLLH 149
Cdd:cd18044 97 QVVLATNTGAgsRQLLPNE-LFDVVVIDEAAQALEASCWIPLLKAR---RCILAGDHKQLPPTILSDKAARGGlGVTLFE 172
|
..
gi 156105695 150 RL 151
Cdd:cd18044 173 RL 174
|
|
| DEXXQc_SETX |
cd18042 |
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ... |
65-154 |
2.03e-07 |
|
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: 53.76 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 65 TRAELARH-RVVVTTTSQA--RELRVPVGFFSHILIDEAAQMLECEALTPLAYASHgtRLVLAGDHMQVTPRLFS-VARA 140
Cdd:cd18042 115 LRASILNEaDIVCTTLSSSgsDLLESLPRGFDTVIIDEAAQAVELSTLIPLRLGCK--RLILVGDPKQLPATVFSkVAQK 192
|
90
....*....|....
gi 156105695 141 RAAEHTLLHRLFLC 154
Cdd:cd18042 193 LGYDRSLFERLQLA 206
|
|
| DEXXQc_HELZ2-N |
cd18076 |
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
1759-1858 |
2.43e-06 |
|
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: 50.66 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1759 KFELDRHEVILCTCSCAASASLKILDVRQILVDEAGMATEPETLIPLVQFPQAEKVVLLGDHKQLRP---VVKNERLQNL 1835
Cdd:cd18076 121 RDELDFHNIVITTTAMAFNLHVLSGFFTHIFIDEAAQMLECEALIPLSYAGPKTRVVLAGDHMQMTPklfSVADYNRANH 200
|
90 100
....*....|....*....|...
gi 156105695 1836 GLDRSLFERYHEDAHMLDTQYRM 1858
Cdd:cd18076 201 TLLNRLFHYYQGEKHEVAVKSRV 223
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
65-136 |
3.43e-06 |
|
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: 50.81 E-value: 3.43e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156105695 65 TRAELARHRVVVTT--TSQARELRVPVGFFShILIDEAAQMLECEALTPLAYASHgtRLVLAGDHMQVTPRLFS 136
Cdd:pfam13086 177 EREILDEAQIVCSTlsGAGSRLLSSLANFDV-VIIDEAAQALEPSTLIPLLRGPK--KVVLVGDPKQLPPTVIS 247
|
|
| DEXXQc_SF1 |
cd18043 |
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ... |
1585-1616 |
5.14e-06 |
|
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: 47.58 E-value: 5.14e-06
10 20 30
....*....|....*....|....*....|....
gi 156105695 1585 NPSQNVAVREALEKPFTVIQGPPGTGK--TIVGL 1616
Cdd:cd18043 1 DSSQEAAIISARNGKNVVIQGPPGTGKsqTIANI 34
|
|
| DEXXc_HELZ2-C |
cd18040 |
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
68-167 |
2.05e-05 |
|
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: 48.68 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 68 ELARHRVVVTTTSQA--RELRVPVGFfSHILIDEAAQMLECEALTPLAYASHGTRLVLAGDHMQVTPrlfSVARARAAEH 145
Cdd:cd18040 174 ELETVDVILCTCSEAasQKMRTHANV-KQCIVDECGMCTEPESLIPIVSAPRAEQVVLIGDHKQLRP---VVQNKEAQKL 249
|
90 100
....*....|....*....|..
gi 156105695 146 TLLHRLFLCYQQETHEVARQSR 167
Cdd:cd18040 250 GLGRSLFERYAEKACMLDTQYR 271
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
1578-1988 |
2.72e-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: 49.20 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1578 PGGRHKLNPSQNVAVREALEK-PFTVIQGPPGTGKTIVGLHIVFWFHKSNQEqvqpggpprgekrlggpcILYCGPSNKS 1656
Cdd:COG0507 119 PRAGITLSDEQREAVALALTTrRVSVLTGGAGTGKTTTLRALLAALEALGLR------------------VALAAPTGKA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1657 VDVLaglllrrmelkplrvyseqAEASEFPvprvgsrkllrkspregrpnqslrSITLHHRIRQAPNpysseikafdtrl 1736
Cdd:COG0507 181 AKRL-------------------SESTGIE------------------------ARTIHRLLGLRPD------------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1737 qrgelfsredlvwykkvlweARKFELDRHEVilctcscaasasLKILDVrqILVDEAGMATEP--ETLIPLVQFPQAeKV 1814
Cdd:COG0507 205 --------------------SGRFRHNRDNP------------LTPADL--LVVDEASMVDTRlmAALLEALPRAGA-RL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1815 VLLGDHKQLRPVVKNERLqnlgldRSLFERYHEDAHMLDTQYRMHEGIcAFPSVAfyksklktwQGLR--RPPSVLGHAG 1892
Cdd:COG0507 250 ILVGDPDQLPSVGAGAVL------RDLIESGTVPVVELTEVYRQADDS-RIIELA---------HAIRegDAPEALNARY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1893 KEscpVIFGHVQGHERSllvstdegnenskanLEEVAEVVRitkqltlGRTVEPQDIAVLTPYNAQASEISKALRRE-GI 1971
Cdd:COG0507 314 AD---VVFVEAEDAEEA---------------AEAIVELYA-------DRPAGGEDIQVLAPTNAGVDALNQAIREAlNP 368
|
410
....*....|....*..
gi 156105695 1972 AGVAVSSITKSQGSEWR 1988
Cdd:COG0507 369 AGELERELAEDGELELY 385
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
1588-1612 |
9.48e-05 |
|
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: 44.85 E-value: 9.48e-05
10 20
....*....|....*....|....*
gi 156105695 1588 QNVAVREALEKPFTVIQGPPGTGKT 1612
Cdd:cd17933 2 QKAAVRLVLRNRVSVLTGGAGTGKT 26
|
|
| SF1_C_UvrD |
cd18807 |
C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase ... |
1899-1990 |
1.33e-04 |
|
C-terminal helicase domain of UvrD family helicases; 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. This family also includes ATP-dependent helicase/nuclease AddA and helicase/nuclease RecBCD subunit RecB, among others. UvrD family helicases 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: 350194 [Multi-domain] Cd Length: 150 Bit Score: 44.14 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1899 IFGHVQGHERSLLVStdeGNENSKA-----NLEEVAEVVRIT---KQLTLGRTVEPQDIAVLTPYNAQASEISKALRreg 1970
Cdd:cd18807 12 LIKQNKNRPKKPLKA---GNKSGGPvelllAKDEADEAKAIAdeiKRLIESGPVQYSDIAILVRTNRQARVIEEALR--- 85
|
90 100
....*....|....*....|
gi 156105695 1971 iagVAVSSITKSQGSEWRYV 1990
Cdd:cd18807 86 ---VTLMTIHASKGLEFPVV 102
|
|
| CoV_Nsp13-helicase |
cd21718 |
helicase domain of coronavirus non-structural protein 13; This model represents the helicase ... |
1788-2039 |
3.32e-04 |
|
helicase domain of coronavirus non-structural protein 13; This model represents the helicase domain of non-structural protein 13 (Nsp13) from alpha-, beta-, gamma-, and deltacoronavirus, including pathogenic human viruses such as Severe acute respiratory syndrome coronavirus (SARS-CoV), SARS-CoV2 (also called 2019 novel CoV or 2019-nCoV), and Middle East respiratory syndrome-related (MERS) CoV. Helicases catalyze NTP-dependent unwinding of nucleic acid duplexes into single strands and are classified based on the arrangement of conserved motifs into six superfamilies. CoV Nsp13 is a member of the helicase superfamily 1 (SF1); SF1 and SF2 helicases do not form toroidal structures, while SF3-6 helicases do. Nsp13 is a component of the viral RNA synthesis replication and transcription complex (RTC). It is a multidomain protein containing a Cys/His rich zinc-binding domain (CH/ZBD), a stalk domain, a 1B domain involved in nucleic acid substrate binding, and a SF1 helicase core.
Pssm-ID: 409652 [Multi-domain] Cd Length: 341 Bit Score: 45.21 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1788 ILVDEAGMATEPEtLIPLVQFPQAEKVVLLGDHKQL---RPVVKNERLQNLGLDRSLFERYHEDAH-MLDTQYRMHEGIC 1863
Cdd:cd21718 121 VVVDEVSMCTNYD-LSVVNARLKYKHIVYVGDPAQLpapRTLLTEGSLEPKDYNVVTRLMVGSGPDvFLSKCYRCPKEIV 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1864 AFPSVAFYKSKLKTwqglrrppsvlGHAGKESCPVIFGhvqghersllvSTDEGNENSKANLEEVAEVVRitkqLTLGRT 1943
Cdd:cd21718 200 DTVSKLVYDNKLKA-----------IKPKSRQCFKTFG-----------KGDVRHDNGSAINRPQLEFVK----RFLDRN 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1944 VEPQDIAVLTPYNAQASEISKalrregIAGVAVSSITKSQGSEWRYVLVstvrtCAKSDLDQrptkswlkkflgfVVDPN 2023
Cdd:cd21718 254 PRWRKAVFISPYNAMNNRASR------LLGLSTQTVDSSQGSEYDYVIF-----CQTTDTAH-------------ALNIN 309
|
250
....*....|....*.
gi 156105695 2024 QVNVAVTRAQEGLCLI 2039
Cdd:cd21718 310 RFNVAITRAKHGILVI 325
|
|
| betaCoV_Nsp13-helicase |
cd21722 |
helicase domain of betacoronavirus non-structural protein 13; This model represents the ... |
1952-2044 |
6.37e-04 |
|
helicase domain of betacoronavirus non-structural protein 13; This model represents the helicase domain of non-structural protein 13 (Nsp13) from betacoronavirus, including pathogenic human viruses such as Severe acute respiratory syndrome coronavirus (SARS-CoV), SARS-CoV2 (also called 2019 novel CoV or 2019-nCoV), and Middle East respiratory syndrome-related (MERS) CoV. Helicases catalyze NTP-dependent unwinding of nucleic acid duplexes into single strands and are classified based on the arrangement of conserved motifs into six superfamilies. CoV Nsp13 is a member of the helicase superfamily 1 (SF1); SF1 and SF2 helicases do not form toroidal structures, while SF3-6 helicases do. Nsp13 is a component of the viral RNA synthesis replication and transcription complex (RTC). It is a multidomain protein containing a Cys/His rich zinc-binding domain (CH/ZBD), a stalk domain, a 1B domain involved in nucleic acid substrate binding, and a SF1 helicase core.
Pssm-ID: 409655 [Multi-domain] Cd Length: 340 Bit Score: 44.41 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1952 LTPYNAQASEISKALrregiaGVAVSSITKSQGSEWRYVLVSTVRTCAKSdldqrptkswlkkflgfvVDPNQVNVAVTR 2031
Cdd:cd21722 262 ISPYNSQNAVARRVL------GLQTQTVDSSQGSEYDYVIYCQTAETAHS------------------VNVNRFNVAITR 317
|
90
....*....|....
gi 156105695 2032 AQEG-LCLIGDHLL 2044
Cdd:cd21722 318 AKKGiLCVMSSMQL 331
|
|
| EEXXQc_AQR |
cd17935 |
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ... |
74-151 |
6.75e-04 |
|
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: 43.18 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 74 VVVTTTSQARELR--VPVGF-FSHILIDEAAQMLECEALTPLAYASHGT------RLVLAGDHMQVTPRLFSVARARAA- 143
Cdd:cd17935 90 IAMTCTHAALKRGelVELGFkYDNILMEEAAQILEIETFIPLLLQNPEDgpnrlkRLIMIGDHHQLPPVIKNMAFQKYSn 169
|
....*....
gi 156105695 144 -EHTLLHRL 151
Cdd:cd17935 170 mEQSLFTRL 178
|
|
| HelD |
COG3973 |
DNA helicase IV [Replication, recombination and repair]; |
1588-1617 |
1.57e-03 |
|
DNA helicase IV [Replication, recombination and repair];
Pssm-ID: 443173 [Multi-domain] Cd Length: 699 Bit Score: 43.70 E-value: 1.57e-03
10 20 30
....*....|....*....|....*....|
gi 156105695 1588 QNVAVREALEKPfTVIQGPPGTGKTIVGLH 1617
Cdd:COG3973 196 QDRIIRADLRGV-LVVQGGAGSGKTAVALH 224
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
1481-1631 |
2.77e-03 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 42.45 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 1481 DWDQERRADRQEAPRRVHLFVHH-MGMEKVPEEVLRPGTLFTVELLPKQLPDLRKEEAVRGLEEASPLVTSIALGRPVPQ 1559
Cdd:COG1401 102 EELYELEADSEIEAVGLLLELAErSDALEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAEL 181
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156105695 1560 PLCRVIPSRFLERQTYNIPGGRHKLNPSQNVAVREALE-KPFTVIQGPPGTGKTIVGLHIVFWFHKSNQEQVQ 1631
Cdd:COG1401 182 SAAEELYSEDLESEDDYLKDLLREKFEETLEAFLAALKtKKNVILAGPPGTGKTYLARRLAEALGGEDNGRIE 254
|
|
| EEXXEc_NFX1 |
cd17936 |
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ... |
72-134 |
3.55e-03 |
|
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: 40.61 E-value: 3.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105695 72 HRVV-VTTTSQAR------ELRVPVgffshILIDEAAQMLECEALTPLayASHGTRLVLAGDHMQVTPRL 134
Cdd:cd17936 82 ARVIgMTTTGAAKyrellqALGPKV-----VIVEEAAEVLEAHILAAL--TPSTEHLILIGDHKQLRPKV 144
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
1781-1826 |
5.86e-03 |
|
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: 39.46 E-value: 5.86e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 156105695 1781 KILDVRQILVDEAGMATEP--ETLIPLVqfPQAEKVVLLGDHKQLRPV 1826
Cdd:cd17933 86 NPLDADLLIVDEASMVDTRlmAALLSAI--PAGARLILVGDPDQLPSV 131
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