|
Name |
Accession |
Description |
Interval |
E-value |
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
3-529 |
2.62e-105 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 328.52 E-value: 2.62e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 3 FTLRPYQQEAVDATLSHFRRHRTPAVIVLPTGAGKSLVIAELAR--VARGRVLVLAHVKELVAQNHAKYCALgleADIFA 80
Cdd:COG1061 79 FELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALAAelLRGKRVLVLVPRRELLEQWAEELRRF---LGDPL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 81 AGLKRKESQGKVVFGSVQSVARN--LDAFQEEFSLLIVDECHRIGDDedsQYQQILTHLSKVnphlRLLGLTATPFRLGK 158
Cdd:COG1061 156 AGGGKKDSDAPITVATYQSLARRahLDELGDRFGLVIIDEAHHAGAP---SYRRILEAFPAA----YRLGLTATPFRSDG 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 159 GWIYQFHYHGmvrgndnalfrdCIYELPLRYMIKHGYLTPPERLDMPVvqyDFSRLQAQSNGLfsEADLNRELKKQQRIT 238
Cdd:COG1061 229 REILLFLFDG------------IVYEYSLKEAIEDGYLAPPEYYGIRV---DLTDERAEYDAL--SERLREALAADAERK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 239 PHIISQIV-EFAQTRKgVMIFAATVEHAKEIVGLLPADD--AALITGDTPGPERDALIDNFKAQRFRYLVNVSVLTTGFD 315
Cdd:COG1061 292 DKILRELLrEHPDDRK-TLVFCSSVDHAEALAELLNEAGirAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVD 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 316 APHVDLIAILRPTESVSLYQQIVGRGLRLAPGKTDCLILDYAGNphDLYAPEVGSPKGKSDNVPvqvfcpacgfantfwg 395
Cdd:COG1061 371 VPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKEDALVYDFVGN--DVPVLEELAKDLRDLAGY---------------- 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 396 kttadgTLIEHFGRRCQGWFDDDDGHREQCDFRFRFKNCPQCNAENDIAARRCRECDAILVDPDDMLKAALRLKDALVLR 475
Cdd:COG1061 433 ------RVEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAE 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 446500276 476 CSGMTMQHGQDEKGEWLKITYYDEDGADVSERFRLHTPAQRTAFEQLFIRPHTR 529
Cdd:COG1061 507 EEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALLRLEELAALLLKELL 560
|
|
| HsdR |
COG4096 |
Type I site-specific restriction endonuclease, part of a restriction-modification system ... |
3-385 |
7.34e-37 |
|
Type I site-specific restriction endonuclease, part of a restriction-modification system [Defense mechanisms];
Pssm-ID: 443272 [Multi-domain] Cd Length: 806 Bit Score: 146.52 E-value: 7.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 3 FTLRPYQQEAVDATLSHFRRHRTPAVIVLPTGAGKSLVIAEL------ARVARgRVLVLAHVKELVAQNHAKYCALGLEA 76
Cdd:COG4096 157 IALRYYQIEAIRRVEEAIAKGQRRALLVMATGTGKTRTAIALiyrllkAGRAK-RILFLADRNALVDQAKNAFKPFLPDL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 77 DIFA---AGLKRKESQGKVVFGSVQSVARNLDAFQEE----------FSLLIVDECHR-IGddedSQYQQILTHLSKVnp 142
Cdd:COG4096 236 DAFTklyNKSKDIDKSARVYFSTYQTMMNRIDGEEEEpgyrqfppdfFDLIIIDECHRgIY----SKWRAILDYFDAL-- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 143 hlrLLGLTATPFRLGKGWIYQFhYHGMVrgndnalfrdcIYELPLRYMIKHGYLTPPE------RLDMPVVQYD-----F 211
Cdd:COG4096 310 ---QIGLTATPKDTIDRNTYEY-FNGNP-----------VYTYSLEQAVADGFLVPYKviridtKFDREGIRYDagedlS 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 212 SRLQAQ-------SNGLFSEADLNRELKKQQRITpHIISQIVEFAQTRKGV-----MIFAATVEHAKEIVGLL------P 273
Cdd:COG4096 375 DEEGEEieleeleEDREYEAKDFNRKVVNEDTTR-KVLEELMEYLDKPGGDrlgktIIFAKNDDHADRIVQALrelypeL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 274 ADDAAL-ITGDTPGPErdALIDNFK-AQRF-RYLVNVSVLTTGFDAPHVDLIAILRPTESVSLYQQIVGRGLRL----AP 346
Cdd:COG4096 454 GGDFVKkITGDDDYGK--SLIDNFKnPEKYpRIAVTVDMLDTGIDVPEVVNLVFMRPVKSRIKFEQMIGRGTRLcpdlFP 531
|
410 420 430
....*....|....*....|....*....|....*....
gi 446500276 347 GKTDCLILDYAGNpHDLYAPevgspkgksDNVPVQVFCP 385
Cdd:COG4096 532 GKTHFTIFDFVGN-TELFAD---------PSFPLRIFEP 560
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
252-356 |
6.67e-34 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350186 [Multi-domain] Cd Length: 116 Bit Score: 124.59 E-value: 6.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 252 RKGVMIFAATVEHAKEIVGLLPAD--DAALITGDTPGPERD--ALIDNFKAQ-RFRYLVNVSVLTTGFDAPHVDLIAILR 326
Cdd:cd18799 6 EIKTLIFCVSIEHAEFMAEAFNEAgiDAVALNSDYSDRERGdeALILLFFGElKPPILVTVDLLTTGVDIPEVDNVVFLR 85
|
90 100 110
....*....|....*....|....*....|
gi 446500276 327 PTESVSLYQQIVGRGLRLAPGKTDCLILDY 356
Cdd:cd18799 86 PTESRTLFLQMLGRGLRLHEGKDFFTILDF 115
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
2-155 |
3.01e-33 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 124.71 E-value: 3.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 2 IFTLRPYQQEAVDATLSHFRRHRTPAVIVLPTGAGKSLVIAELARVARG-----RVLVLAHVKELVAQNHAKYCALGLEA 76
Cdd:pfam04851 1 KLELRPYQIEAIENLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKkgpikKVLFLVPRKDLLEQALEEFKKFLPNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 77 D---IFAAGLKRKES--QGKVVFGSVQSVARNLDAFQEEFS-----LLIVDECHRIGDDedsQYQQILTHLskvnPHLRL 146
Cdd:pfam04851 81 VeigEIISGDKKDESvdDNKIVVTTIQSLYKALELASLELLpdffdVIIIDEAHRSGAS---SYRNILEYF----KPAFL 153
|
....*....
gi 446500276 147 LGLTATPFR 155
Cdd:pfam04851 154 LGLTATPER 162
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
5-164 |
4.99e-31 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350790 [Multi-domain] Cd Length: 163 Bit Score: 118.43 E-value: 4.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 5 LRPYQQEAVDATLSHFRRHRTPAVIVLPTGAGKSLVIAELARV-----ARGRVLVLAHVKELVAQNHAKYCALGLEADIF 79
Cdd:cd18032 1 PRYYQQEAIEALEEAREKGQRRALLVMATGTGKTYTAAFLIKRlleanRKKRILFLAHREELLEQAERSFKEVLPDGSFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 80 -AAGLKRKESQGKVVFGSVQSVARNLDAFQ---EEFSLLIVDECHRIGddeDSQYQQILTHLSKVnphlRLLGLTATPFR 155
Cdd:cd18032 81 nLKGGKKKPDDARVVFATVQTLNKRKRLEKfppDYFDLIIIDEAHHAI---ASSYRKILEYFEPA----FLLGLTATPER 153
|
....*....
gi 446500276 156 LGKGWIYQF 164
Cdd:cd18032 154 TDGLDTYEL 162
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
5-153 |
1.85e-29 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part 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: 350684 [Multi-domain] Cd Length: 146 Bit Score: 113.55 E-value: 1.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 5 LRPYQQEAVDATLSHFRRHRtpAVIVLPTGAGKSLVIAELAR-VARGRVLVLAHVKELVAQNHAKYCALGLEADIFAAGL 83
Cdd:cd17926 1 LRPYQEEALEAWLAHKNNRR--GILVLPTGSGKTLTALALIAyLKELRTLIVVPTDALLDQWKERFEDFLGDSSIGLIGG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446500276 84 KRKESQ--GKVVFGSVQSVAR---NLDAFQEEFSLLIVDECHRIGDDedsQYQQILTHLskvNPHLRlLGLTATP 153
Cdd:cd17926 79 GKKKDFddANVVVATYQSLSNlaeEEKDLFDQFGLLIVDEAHHLPAK---TFSEILKEL---NAKYR-LGLTATP 146
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
2-153 |
4.84e-21 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 91.40 E-value: 4.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 2 IFTLRPYQQEAVDATLSHFRRhrtpAVIVLPTGAGKSLV-----IAELARVARGRVLVLAHVKELVAQNHAKYCALGLEA 76
Cdd:smart00487 6 FEPLRPYQKEAIEALLSGLRD----VILAAPTGSGKTLAallpaLEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 77 DIFAAGL-----------KRKESQGKVVFGSVQSVARNLDA---FQEEFSLLIVDECHRIGDdeDSQYQQILTHLSKVNP 142
Cdd:smart00487 82 GLKVVGLyggdskreqlrKLESGKTDILVTTPGRLLDLLENdklSLSNVDLVILDEAHRLLD--GGFGDQLEKLLKLLPK 159
|
170
....*....|.
gi 446500276 143 HLRLLGLTATP 153
Cdd:smart00487 160 NVQLLLLSATP 170
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
3-365 |
3.28e-20 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 95.40 E-value: 3.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 3 FTLRPYQQEAVDATLSHFRRHRTPAVIVLPTGAGKS-LVIAELARVARG----RVLVLAHVKELVAQNHAKYCALGLE-- 75
Cdd:PRK11448 412 LGLRYYQEDAIQAVEKAIVEGQREILLAMATGTGKTrTAIALMYRLLKAkrfrRILFLVDRSALGEQAEDAFKDTKIEgd 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 76 ---ADIFA-AGLKRK--ESQGKVVFGSVQS-VARNLDAFQE-------EFSLLIVDECHRiG---------------DDE 126
Cdd:PRK11448 492 qtfASIYDiKGLEDKfpEDETKVHVATVQGmVKRILYSDDPmdkppvdQYDCIIVDEAHR-GytldkemsegelqfrDQL 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 127 D--SQYQQILTHLSKVNphlrlLGLTATP-------FrlGKGwIYQFHYHGMVRgnDNALFrDciYELPLRY---MIKHG 194
Cdd:PRK11448 571 DyvSKYRRVLDYFDAVK-----IGLTATPalhtteiF--GEP-VYTYSYREAVI--DGYLI-D--HEPPIRIetrLSQEG 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 195 -YLTPPERLDMpvvqYDFSRLQAQSNGL-----FSEADLNRELkkqqrITPH----IISQIV-EFAQTRKG-VMIFAATV 262
Cdd:PRK11448 638 iHFEKGEEVEV----INTQTGEIDLATLedevdFEVEDFNRRV-----ITESfnrvVCEELAkYLDPTGEGkTLIFAATD 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 263 EHAKEIVGLL---------PADDAAL--ITGDTPGPerDALIDNFKAQRF-RYLVNVSVLTTGFDAPHVDLIAILRPTES 330
Cdd:PRK11448 709 AHADMVVRLLkeafkkkygQVEDDAVikITGSIDKP--DQLIRRFKNERLpNIVVTVDLLTTGIDVPSICNLVFLRRVRS 786
|
410 420 430
....*....|....*....|....*....|....*..
gi 446500276 331 VSLYQQIVGRGLRLAP--GKTDCLILDyagnPHDLYA 365
Cdd:PRK11448 787 RILYEQMLGRATRLCPeiGKTHFRIFD----AVDIYE 819
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
6-153 |
6.08e-16 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 81.31 E-value: 6.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 6 RPYQQEAVDATLshfrrhRTPAVIVLPTGAGKS----LVIAELARVARGRVLVLAHVKELVAQnHAKYC--ALGLEADIF 79
Cdd:COG1111 5 RLYQLNLAASAL------RKNTLVVLPTGLGKTavalLVIAERLHKKGGKVLFLAPTKPLVEQ-HAEFFkeALNIPEDEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 80 AA--GL----KRKE--SQGKVVFGSVQSVARNLDA---FQEEFSLLIVDECHR-IGddeDSQYQQILTHLSKVNPHLRLL 147
Cdd:COG1111 78 VVftGEvspeKRKElwEKARIIVATPQVIENDLIAgriDLDDVSLLIFDEAHRaVG---NYAYVYIAERYHEDAKDPLIL 154
|
....*.
gi 446500276 148 GLTATP 153
Cdd:COG1111 155 GMTASP 160
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
28-152 |
4.31e-15 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 72.44 E-value: 4.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 28 VIVLPTGAGKSLV----IAELARVARGRVLVLAHVKELVAQNHA---KYCALGLEADIFAAG------LKRKESQGKVVF 94
Cdd:cd00046 5 LITAPTGSGKTLAallaALLLLLKKGKKVLVLVPTKALALQTAErlrELFGPGIRVAVLVGGssaeerEKNKLGDADIII 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446500276 95 GSVQSVARNLDA----FQEEFSLLIVDECHRIGDDEDSQYQQILTHLSKVNPHLRLLGLTAT 152
Cdd:cd00046 85 ATPDMLLNLLLRedrlFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQVILLSAT 146
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
6-155 |
4.68e-15 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 73.05 E-value: 4.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 6 RPYQQEAVDATLSHFRrhrtpAVIVLPTGAGKSLViAELARVAR-------GRVLVLAHVKELVAQNHAKYCALGLEADI 78
Cdd:pfam00270 1 TPIQAEAIPAILEGRD-----VLVQAPTGSGKTLA-FLLPALEAldkldngPQALVLAPTRELAEQIYEELKKLGKGLGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 79 FAA----GLKRKESQGK-----VVF---GSVQSVARNLDAFQEeFSLLIVDECHRIGDdeDSQYQQILTHLSKVNPHLRL 146
Cdd:pfam00270 75 KVAsllgGDSRKEQLEKlkgpdILVgtpGRLLDLLQERKLLKN-LKLLVLDEAHRLLD--MGFGPDLEEILRRLPKKRQI 151
|
....*....
gi 446500276 147 LGLTATPFR 155
Cdd:pfam00270 152 LLLSATLPR 160
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
239-343 |
3.75e-14 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 68.78 E-value: 3.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 239 PHIISQIVEFAQTRKgVMIFAATVEHAK-EIVGLLPADDAALITGDTPGPERDALIDNFKAQRFRYLVNVSVLTTGFDAP 317
Cdd:pfam00271 3 LEALLELLKKERGGK-VLIFSQTKKTLEaELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLP 81
|
90 100
....*....|....*....|....*.
gi 446500276 318 HVDLIAILRPTESVSLYQQIVGRGLR 343
Cdd:pfam00271 82 DVDLVINYDLPWNPASYIQRIGRAGR 107
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
3-159 |
1.39e-13 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer 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: 350792 [Multi-domain] Cd Length: 200 Bit Score: 69.60 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 3 FTLRPYQQEAVDATLshfrRHRTpaVIVLPTGAGKSLV----IAELARVARG------RVLVLAHVKELVAQNH------ 66
Cdd:cd18034 1 FTPRSYQLELFEAAL----KRNT--IVVLPTGSGKTLIavmlIKEMGELNRKeknpkkRAVFLVPTVPLVAQQAeairsh 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 67 -----AKYCALGLEADIFAAGLKRKESQGKVVFGSVQSVarnLDAFQ------EEFSLLIVDECHR-IGDDEDSQYQQIL 134
Cdd:cd18034 75 tdlkvGEYSGEMGVDKWTKERWKEELEKYDVLVMTAQIL---LDALRhgflslSDINLLIFDECHHaTGDHPYARIMKEF 151
|
170 180
....*....|....*....|....*
gi 446500276 135 THLSKVNPHLRLLGLTATPFRlGKG 159
Cdd:cd18034 152 YHLEGRTSRPRILGLTASPVN-GKG 175
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
3-153 |
1.49e-13 |
|
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM 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: 350791 [Multi-domain] Cd Length: 182 Bit Score: 69.27 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 3 FTLRPYQQEAVDATLSHfrrhrtPAVIVLPTGAGKSLViaelARVA---------RGRVLVLAHVKELVAQNH-AKYCAL 72
Cdd:cd18033 1 VPLRDYQFTIVQKALFQ------NTLVALPTGLGKTFI----AAVVmlnyyrwfpKGKIVFMAPTKPLVSQQIeACYKIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 73 GLEADIFA--AGLKRKESQGK------VVFGSVQSVARNL---DAFQEEFSLLIVDECHR-IGDdedSQYQQILTHLSKV 140
Cdd:cd18033 71 GIPSSQTAelTGSVPPTKRAElwaskrVFFLTPQTLENDLkegDCDPKSIVCLVIDEAHRaTGN---YAYCQVVRELMRY 147
|
170
....*....|...
gi 446500276 141 NPHLRLLGLTATP 153
Cdd:cd18033 148 NSHFRILALTATP 160
|
|
| RPL40A |
COG1552 |
Ribosomal protein L40E [Translation, ribosomal structure and biogenesis]; Ribosomal protein ... |
417-466 |
4.81e-13 |
|
Ribosomal protein L40E [Translation, ribosomal structure and biogenesis]; Ribosomal protein L40E is part of the Pathway/BioSystem: Archaeal ribosomal proteins
Pssm-ID: 441161 [Multi-domain] Cd Length: 50 Bit Score: 63.80 E-value: 4.81e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 446500276 417 DDDGHREQCDFRFRFKNCPQCNAENDIAARRCRECDAILVDPDDMLKAAL 466
Cdd:COG1552 1 DMAKFEEAEKRRLNKKICMRCGARNPIRATRCRKCGYKNLRPKKKERRAK 50
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
4-152 |
1.19e-11 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 63.82 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 4 TLRPYQQEAVDATLSHfrrhRTPAVIVLPTGAGKSLvIAELARVAR-----GRVLVLAHVKELVAQNHA------KYCAL 72
Cdd:cd17921 1 LLNPIQREALRALYLS----GDSVLVSAPTSSGKTL-IAELAILRAlatsgGKAVYIAPTRALVNQKEAdlrerfGPLGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 73 GLEADIFAAGLKRKESQGKVVFGSVQSVARNL-----DAFQEEFSLLIVDECHRIGDDEDSQ-YQQILTHLSKVNPHLRL 146
Cdd:cd17921 76 NVGLLTGDPSVNKLLLAEADILVATPEKLDLLlrnggERLIQDVRLVVVDEAHLIGDGERGVvLELLLSRLLRINKNARF 155
|
....*.
gi 446500276 147 LGLTAT 152
Cdd:cd17921 156 VGLSAT 161
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
3-153 |
1.85e-11 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part 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: 350685 [Multi-domain] Cd Length: 201 Bit Score: 63.61 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 3 FTLRPYQQEAVDATLshfRRHRTpaVIVLPTGAGKSLVIAELAR--------VARGRVLVLAHVKELVAQ---------N 65
Cdd:cd17927 1 FKPRNYQLELAQPAL---KGKNT--IICLPTGSGKTFVAVLICEhhlkkfpaGRKGKVVFLANKVPLVEQqkevfrkhfE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 66 HAKYCALGLEADIFAAGLKRKESQG-KVVFGSVQSVARNLDAFQE----EFSLLIVDECHRIgdDEDSQYQQILTH---- 136
Cdd:cd17927 76 RPGYKVTGLSGDTSENVSVEQIVESsDVIIVTPQILVNDLKSGTIvslsDFSLLVFDECHNT--TKNHPYNEIMFRyldq 153
|
170
....*....|....*...
gi 446500276 137 -LSKVNPHLRLLGLTATP 153
Cdd:cd17927 154 kLGSSGPLPQILGLTASP 171
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
4-152 |
8.00e-11 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 61.20 E-value: 8.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 4 TLRPYQQEAVDATLSHFRRhrtpAVIVLPTGAGKSLvIAELARVAR----GRVLVLAHVKELVAQNH---AKYCALGLEA 76
Cdd:cd18028 1 ELYPPQAEAVRAGLLKGEN----LLISIPTASGKTL-IAEMAMVNTllegGKALYLVPLRALASEKYeefKKLEEIGLKV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 77 DIFAAGLKRKE---SQGKVVFGS---VQSVARNLDAFQEEFSLLIVDECHRIGDDEDSQYQQ-ILTHLSKVNPHLRLLGL 149
Cdd:cd18028 76 GISTGDYDEDDewlGDYDIIVATyekFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLEsIVARLRRLNPNTQIIGL 155
|
...
gi 446500276 150 TAT 152
Cdd:cd18028 156 SAT 158
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
276-343 |
8.36e-11 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 58.38 E-value: 8.36e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446500276 276 DAALITGDTPGPERDALIDNFKAQRFRYLVNVSVLTTGFDAPHVDLIAILRPTESVSLYQQIVGRGLR 343
Cdd:smart00490 13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
|
| COG4889 |
COG4889 |
Predicted helicase [General function prediction only]; |
3-348 |
1.90e-10 |
|
Predicted helicase [General function prediction only];
Pssm-ID: 443917 [Multi-domain] Cd Length: 1571 Bit Score: 64.21 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 3 FTLRPYQQEAVDATLSHFRRH-RtpAVIVLPTGAGK---SLVIAE-LARvARGRVLVLAHVKELVAQ------NHAKY-- 69
Cdd:COG4889 168 KTLRPHQQEAIEAVLAGFKTHdR--GKLIMACGTGKtftSLRIAEeLAG-KGGRVLFLVPSISLLSQtlrewtAESEVpl 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 70 -----CA-------------------LGLEA-----DIFAAGLKRKESQG-KVVFGSVQSVARNLDAFQ---EEFSLLIV 116
Cdd:COG4889 245 rsfavCSdskvgkrrkkddedtsahdLAYPAttdaeKLAAAAQKRHDADRmTVVFSTYQSIDVVADAQKlglPEFDLIIC 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 117 DECHR-----IGDDEDSQYQQIltH-LSKVNPHLRLLgLTATPfRLgkgwiyqfhYHGMVRG------------NDNALF 178
Cdd:COG4889 325 DEAHRttgatLAGEDESAFVRV--HdNDYIKAKKRLY-MTATP-RI---------YGDDAKKkakeasavlasmDDEALF 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 179 RDCIYELPLRYMIKHGYLTPPERLDMPVVQYDFSR-----LQAQSNGLfSEAD-----------LNRELKKQQRITPHII 242
Cdd:COG4889 392 GPEFHRLGFGEAVERGLLTDYKVIVLAVDESHVSRrlqqlLADNGNEL-KLDDaakivgcwnglAKRGGEEDGTDDPAPM 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 243 SQIVEFAQTRK----GVMIFAATVEHAKEIVGLLPADDAALIT-------GDTPGPERDALIDNFKAQ----RFRYLVNV 307
Cdd:COG4889 471 KRAVAFCQTIKeskrIAEHFVSVVNIYLMFQDDEAEEDAPSLRceaehvdGTMNALERNEKLDWLKAEtpenTCRILSNA 550
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 446500276 308 SVLTTGFDAPHVDLIAILRPTESVSLYQQIVGRGLRLAPGK 348
Cdd:COG4889 551 RCLSEGVDVPALDAVLFLTPRKSQVDVVQSVGRVMRKAPGK 591
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
2-152 |
2.26e-10 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 63.38 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 2 IFTLRPYQQEAVDATLshFRRHRtpAVIVLPTGAGKSLvIAELA---RVARG-RVLVLAHVKELVAQNHAK----YCALG 73
Cdd:COG1204 20 IEELYPPQAEALEAGL--LEGKN--LVVSAPTASGKTL-IAELAilkALLNGgKALYIVPLRALASEKYREfkrdFEELG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 74 LEADI----FAAGLKRKESQGKVVFGS--VQSVARNLDAFQEEFSLLIVDECHRIGDDEDS-QYQQILTHLSKVNPHLRL 146
Cdd:COG1204 95 IKVGVstgdYDSDDEWLGRYDILVATPekLDSLLRNGPSWLRDVDLVVVDEAHLIDDESRGpTLEVLLARLRRLNPEAQI 174
|
....*.
gi 446500276 147 LGLTAT 152
Cdd:COG1204 175 VALSAT 180
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
3-153 |
3.24e-10 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) 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: 350794 [Multi-domain] Cd Length: 204 Bit Score: 60.18 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 3 FTLRPYQQEAVDATLshfrRHRTpAVIVLPTGAGKSLVIAELAR---------VARGRVLVLAHVKELVAQN---HAKYC 70
Cdd:cd18036 1 LELRNYQLELVLPAL----RGKN-TIICAPTGSGKTRVAVYICRhhlekrrsaGEKGRVVVLVNKVPLVEQQlekFFKYF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 71 ALGLEADIFAAGLKRKESQGKVVFGS-------------VQSVARNLDAFQEEFSLLIVDECHRIgdDEDSQYQQIL--- 134
Cdd:cd18036 76 RKGYKVTGLSGDSSHKVSFGQIVKASdviictpqilinnLLSGREEERVYLSDFSLLIFDECHHT--QKEHPYNKIMrmy 153
|
170 180
....*....|....*....|.
gi 446500276 135 --THLSKVNPHLRLLGLTATP 153
Cdd:cd18036 154 ldKKLSSQGPLPQILGLTASP 174
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
6-153 |
3.73e-10 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 62.97 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 6 RPYQQEAVDATLshfrrhRTPAVIVLPTGAGKS----LVIAELARVARGRVLVLAHVKELVAQnHAKYC--ALGLEADIF 79
Cdd:PRK13766 17 RLYQQLLAATAL------KKNTLVVLPTGLGKTaialLVIAERLHKKGGKVLILAPTKPLVEQ-HAEFFrkFLNIPEEKI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 80 AA--G----LKRKE--SQGKVVFGSVQSVARNLDAFQ---EEFSLLIVDECHR-IGDdedsqYQqiLTHLSKV------N 141
Cdd:PRK13766 90 VVftGevspEKRAElwEKAKVIVATPQVIENDLIAGRislEDVSLLIFDEAHRaVGN-----YA--YVYIAERyhedakN 162
|
170
....*....|..
gi 446500276 142 PHlrLLGLTATP 153
Cdd:PRK13766 163 PL--VLGLTASP 172
|
|
| DEXHc_RLR-3 |
cd18075 |
DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of ... |
5-153 |
5.58e-10 |
|
DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of genetics and physiology 2 or LGP2 and DHX58) appears to positively and negatively regulate MDA5 and RIG-I signaling, respectively. RLR-3 resembles a chimera combining a MDA5-like helicase domain and RIG-I like CTD supporting both stem and end binding. RNA binding is required for RLR-3-mediated enhancement of MDA5 activation. RLR-3 end-binding may promote nucleation of MDA5 oligomerization on dsRNA. RLR-3 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: 350833 [Multi-domain] Cd Length: 200 Bit Score: 59.10 E-value: 5.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 5 LRPYQQEAVDATLshfrRHRTpAVIVLPTGAGKSLVIAELAR-----VARGRVLVLAHVKELVAQNHA--------KYCA 71
Cdd:cd18075 3 LHGYQWEVVAPAL----RGKN-SIIWLPTGAGKTRAAVYVARrhletKRGAKVAVLVNKVHLVDQHLEkefhvlldKYTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 72 LGLEADI-FAAGLKRKESQGKVVFGSVQSVARNLDAFQEE-------FSLLIVDECHRIgdDEDSQYQQILTH-----LS 138
Cdd:cd18075 78 TAISGDSsHKCFFGQLARGSDVVICTAQILQNALLSGEEEahveltdFSLLVIDECHHT--HKEAVYNKIMLSylekkLS 155
|
170
....*....|....*
gi 446500276 139 KVNPHLRLLGLTATP 153
Cdd:cd18075 156 RQGDLPQILGLTASP 170
|
|
| DEXHc_RE_I_HsdR |
cd18030 |
DEXH-box helicase domain of type I restriction enzyme HdsR subunit; The HdsR motor subunit of ... |
5-153 |
1.59e-09 |
|
DEXH-box helicase domain of type I restriction enzyme HdsR subunit; The HdsR motor subunit of type I restriction-modification enzymes contains the DNA cleavage and ATP-dependent DNA translocation activities of the heteromeric complex. 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: 350788 [Multi-domain] Cd Length: 208 Bit Score: 58.01 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 5 LRPYQQEAVDATLSHFRRHRTPA------VIVLPTGAGKSLVIAELARVARG-----RVLVLAHVKELVAQNHAKYCALG 73
Cdd:cd18030 22 ARYYQYYAVEAALERIKTATNKDgdkkggYIWHTQGSGKSLTMFKAAKLLIEdpknpKVVFVVDRKDLDYQTSSTFSRFA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 74 LEADIFA---AGLKR--KESQGKVVFGSVQSVARNLDAFQEEFSLL------IVDECHRigddedSQYQQILTHLSKVNP 142
Cdd:cd18030 102 AEDVVRAnstKELKEllKNLSGGIIVTTIQKFNNAVKEESKPVLIYrknivvIVDEAHR------SQFGELAKALKKALP 175
|
170
....*....|.
gi 446500276 143 HLRLLGLTATP 153
Cdd:cd18030 176 NATFIGFTGTP 186
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
4-152 |
6.59e-09 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 56.00 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 4 TLRPYQQEAVDATLSHfrrhrTPAVIVLPTGAGKSLvIAEL-ARVARGRVLV----LAHVKELV---AQNHAKYCALGLE 75
Cdd:cd17920 12 EFRPGQLEAINAVLAG-----RDVLVVMPTGGGKSL-CYQLpALLLDGVTLVvsplISLMQDQVdrlQQLGIRAAALNST 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 76 ADIF---AAGLKRKESQGKVVF--------GSVQSVARNLDAFQeEFSLLIVDECHRI---GDDEDSQYQQiLTHLSKVN 141
Cdd:cd17920 86 LSPEekrEVLLRIKNGQYKLLYvtperllsPDFLELLQRLPERK-RLALIVVDEAHCVsqwGHDFRPDYLR-LGRLRRAL 163
|
170
....*....|.
gi 446500276 142 PHLRLLGLTAT 152
Cdd:cd17920 164 PGVPILALTAT 174
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
6-153 |
1.48e-08 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef 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: 350793 [Multi-domain] Cd Length: 181 Bit Score: 54.83 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 6 RPYQQEAVDATLShfrrhRTPAVIVLPTGAGKS----LVIAELARVARGRVLVLAHVKELVAQNHAKYCALGLEADIFAA 81
Cdd:cd18035 3 RRLYQVLIAAVAL-----NGNTLIVLPTGLGKTiiaiLVAADRLTKKGGKVLILAPSRPLVEQHAENLKRVLNIPDKITS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 82 --GLKRKESQ------GKVVFGSVQSVARNLDAFQ---EEFSLLIVDECHRIGDDEDSQYQQILTHLSKVNPHlrLLGLT 150
Cdd:cd18035 78 ltGEVKPEERaerwdaSKIIVATPQVIENDLLAGRitlDDVSLLIFDEAHHAVGNYAYVYIAHRYKREANNPL--ILGLT 155
|
...
gi 446500276 151 ATP 153
Cdd:cd18035 156 ASP 158
|
|
| DEXHc_XPB |
cd18029 |
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ... |
5-155 |
5.49e-08 |
|
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription factor complex helicase XPB subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB 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: 350787 [Multi-domain] Cd Length: 169 Bit Score: 52.69 E-value: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 5 LRPYQQEAVDATLSHfRRHRTpAVIVLPTGAGKSLV-IAELARVaRGRVLVLAHVKELVAQNHA---KYCALGLEA-DIF 79
Cdd:cd18029 9 LRPYQEKALSKMFGN-GRARS-GVIVLPCGAGKTLVgITAACTI-KKSTLVLCTSAVSVEQWRRqflDWTTIDDEQiGRF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 80 AAGLKRKESQGKVVFGSVQSVARNLDAFQE-----------EFSLLIVDECHRIGDDedsQYQQILThLSKVNphlRLLG 148
Cdd:cd18029 86 TSDKKEIFPEAGVTVSTYSMLANTRKRSPEsekfmefiterEWGLIILDEVHVVPAP---MFRRVLT-LQKAH---CKLG 158
|
....*..
gi 446500276 149 LTATPFR 155
Cdd:cd18029 159 LTATLVR 165
|
|
| uvsW |
PHA02558 |
UvsW helicase; Provisional |
6-292 |
5.97e-08 |
|
UvsW helicase; Provisional
Pssm-ID: 222875 [Multi-domain] Cd Length: 501 Bit Score: 55.40 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 6 RPYQQEAVDATLSHFRRhrtpaVIVLPTGAGKSLVIAELAR----VARGRVLVLAHVKELVAQNHAKYCALGLEADIFAA 81
Cdd:PHA02558 116 HWYQYDAVYEGLKNNRR-----LLNLPTSAGKSLIQYLLSRyyleNYEGKVLIIVPTTSLVTQMIDDFVDYRLFPREAMH 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 82 GL---KRKESQGKVVFGSVQSVARNLDAFQEEFSLLIVDECHRigddedSQYQQILTHLSKVNPHLRLLGLTATPfRLGK 158
Cdd:PHA02558 191 KIysgTAKDTDAPIVVSTWQSAVKQPKEWFDQFGMVIVDECHL------FTGKSLTSIITKLDNCKFKFGLTGSL-RDGK 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 159 GWIYQfhYHGMvrgndnalFRDCIYELPLRYMIKHGYLTppeRLDMPVVQYDFS---RLQAQSNGLFSEADLNRELKKQQ 235
Cdd:PHA02558 264 ANILQ--YVGL--------FGDIFKPVTTSQLMEEGQVT---DLKINSIFLRYPdedRVKLKGEDYQEEIKYITSHTKRN 330
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446500276 236 RItphIISQIVEFAQTRKGVMIFAATVEHAKEIVGLLPA--DDAALITGDTPGPERDAL 292
Cdd:PHA02558 331 KW---IANLALKLAKKGENTFVMFKYVEHGKPLYEMLKKvyDKVYYVSGEVDTEDRNEM 386
|
|
| COG0610 |
COG0610 |
Type I site-specific restriction-modification system, R (restriction) subunit and related ... |
5-363 |
1.10e-07 |
|
Type I site-specific restriction-modification system, R (restriction) subunit and related helicases ... [Defense mechanisms];
Pssm-ID: 440375 [Multi-domain] Cd Length: 936 Bit Score: 54.87 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 5 LRPYQQEAVDATLSHFRRHRTPA---VIVLPTGAGKSLVIAELARVARG-------RVLVLahV--KELVAQNHAKYCAL 72
Cdd:COG0610 256 ARYHQYFAVRKAVERVKEAEGDGkggVIWHTQGSGKSLTMVFLAQKLARlpdldnpTVVVV--TdrKDLDDQLFDTFKAF 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 73 GLEADIFA---AGLKR--KESQGKVVFGSVQSVARNLDAFQEEFSL------LIVDECHRigddedSQYQQILTHLSKVN 141
Cdd:COG0610 334 GRESVVQAesrADLREllESDSGGIIVTTIQKFPEALDEIKYPELSdrkniiVIVDEAHR------SQYGGLAKNMRDAL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 142 PHLRLLGLTATP-----------FrlGKgwiyQFHYHGMVRG-NDNALfrdciyeLPLRYmikhgYLTPPErldmpvVQY 209
Cdd:COG0610 408 PNASFFGFTGTPifkedrttlevF--GD----YIHTYTITQAiEDGAT-------LPLLY-----EYRLAK------LKL 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 210 DFSRLQAQSNGLFSEADLNRELKKQQRIT--------PHIISQIVEF------AQTRKGV---MIFAATVEHA----KEI 268
Cdd:COG0610 464 DKEKIDEEFDELTEGLDDEEKEKLKAKWAlleevlgaPERIEQIAEDivehfeERTRPGKgkaMVVTSSREAAvryyEAF 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 269 VGLLPADD------AALITG---DTPGP--------ERDALIDNFK--AQRFRYLVNVSVLTTGFDAP--H---VDliai 324
Cdd:COG0610 544 DKLRPEWGykplkiAVVFSGsanDDPEElkehgnkeYEKDLAKRFKdpDDPLKLLIVVDMLLTGFDAPslHtlyVD---- 619
|
410 420 430
....*....|....*....|....*....|....*....
gi 446500276 325 lRPTESVSLYQQIvGRGLRLAPGKTDCLILDYAGNPHDL 363
Cdd:COG0610 620 -KPLKGHNLMQAI-SRVNRVFPGKPYGLIVDYRGIFENL 656
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
254-356 |
1.94e-07 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 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: 350172 [Multi-domain] Cd Length: 77 Bit Score: 48.47 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 254 GVMIFAATVEHAKEIvgllpaddaalitgdtpgperdalidnfkAQRFRYLVNVSVLTTGFDAPHVDLIAILRPTESVSL 333
Cdd:cd18785 5 KIIVFTNSIEHAEEI-----------------------------ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAAS 55
|
90 100
....*....|....*....|...
gi 446500276 334 YQQIVGRGLRlaPGKTDCLILDY 356
Cdd:cd18785 56 YIQRVGRAGR--GGKDEGEVILF 76
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
5-153 |
2.17e-07 |
|
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350677 [Multi-domain] Cd Length: 182 Bit Score: 51.41 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 5 LRPYQQEAVdATLSHFRRHRTPAVIVLPTGAGKSL-VIAELA-----RVARGRVLV------LAH-VKELvaQNHAKYCA 71
Cdd:cd17919 1 LRPYQLEGL-NFLLELYENGPGGILADEMGLGKTLqAIAFLAyllkeGKERGPVLVvcplsvLENwEREF--EKWTPDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 72 L----GLEADIFAAGLKRKESQGKVVFGSVQSVARNLDAFQE-EFSLLIVDECHRIgDDEDSQYQQiltHLSKVNPHLRL 146
Cdd:cd17919 78 VvvyhGSQRERAQIRAKEKLDKFDVVLTTYETLRRDKASLRKfRWDLVVVDEAHRL-KNPKSQLSK---ALKALRAKRRL 153
|
....*..
gi 446500276 147 LgLTATP 153
Cdd:cd17919 154 L-LTGTP 159
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
5-155 |
5.59e-07 |
|
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part 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: 350769 [Multi-domain] Cd Length: 207 Bit Score: 50.37 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 5 LRPYQQEAVdatlSHFRRHRTPAVI----VlptGAGKS----LVIAEL-ARVARGRVLVLAhVKELVAQ-NHAKYCALGL 74
Cdd:cd18011 1 PLPHQIDAV----LRALRKPPVRLLladeV---GLGKTieagLIIKELlLRGDAKRVLILC-PASLVEQwQDELQDKFGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 75 EADIF-AAGLKRKESQGKVVFG-------SVQSVARN---LDAFQ-EEFSLLIVDECHRI---GDDEDSQYQQILTHLSK 139
Cdd:cd18011 73 PFLILdRETAAQLRRLIGNPFEefpivivSLDLLKRSeerRGLLLsEEWDLVVVDEAHKLrnsGGGKETKRYKLGRLLAK 152
|
170
....*....|....*.
gi 446500276 140 VNPHlrLLGLTATPFR 155
Cdd:cd18011 153 RARH--VLLLTATPHN 166
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
4-152 |
1.25e-06 |
|
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350773 [Multi-domain] Cd Length: 209 Bit Score: 49.67 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 4 TLRPYQQEAVDATLShfrrhRTPAVIVLPTGAGKSLVIAELARVARGRVLVLAHVKELVaQNHAKYC-ALGLEADIFAA- 81
Cdd:cd18015 18 KFRPLQLETINATMA-----GRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLM-EDQLMALkKLGISATMLNAs 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 82 -----------GLKRKESQGKVVFGSVQSVARN---LDAFQE-----EFSLLIVDE---CHRIGDDEDSQYQQiLTHLSK 139
Cdd:cd18015 92 sskehvkwvhaALTDKNSELKLLYVTPEKIAKSkrfMSKLEKaynagRLARIAIDEvhcCSQWGHDFRPDYKK-LGILKR 170
|
170
....*....|...
gi 446500276 140 VNPHLRLLGLTAT 152
Cdd:cd18015 171 QFPNVPILGLTAT 183
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
4-299 |
3.00e-06 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 50.22 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 4 TLRPYQQEAVdATLSHFRRHRTPAVI---VlptGAGKSL-VIA----ELARVARGRVLVLA--HVKELVAQNHAKYcALG 73
Cdd:COG0553 241 TLRPYQLEGA-AWLLFLRRLGLGGLLaddM---GLGKTIqALAllleLKERGLARPVLIVAptSLVGNWQRELAKF-APG 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 74 LEADIFAAGLKRKE-----SQGKVVFGSVQSVARNLDAFQE-EFSLLIVDECHRIGDDEDSQYQQILthlsKVNPHLRLL 147
Cdd:COG0553 316 LRVLVLDGTRERAKganpfEDADLVITSYGLLRRDIELLAAvDWDLVILDEAQHIKNPATKRAKAVR----ALKARHRLA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 148 gLTATPF--RLGKGW-IYQFHYHGM---------------VRGNDNAL--FRDCIYELPLRYMIKHGYLTPPERLDMpVV 207
Cdd:COG0553 392 -LTGTPVenRLEELWsLLDFLNPGLlgslkafrerfarpiEKGDEEALerLRRLLRPFLLRRTKEDVLKDLPEKTEE-TL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 208 QYDFSRLQAQ----------SNGLFSEADLNR-----ELKKQQRITPH--------------------IISQIVEFAQTR 252
Cdd:COG0553 470 YVELTPEQRAlyeavleylrRELEGAEGIRRRglilaALTRLRQICSHpallleegaelsgrsakleaLLELLEELLAEG 549
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 446500276 253 KGVMIFAATVEHAKEIVGLLPA--DDAALITGDTPGPERDALIDNFKAQ 299
Cdd:COG0553 550 EKVLVFSQFTDTLDLLEERLEErgIEYAYLHGGTSAEERDELVDRFQEG 598
|
|
| DEXHc_RLR-2 |
cd18074 |
DEXH-box helicase domain of RLR-2; RIG-I-like receptor 2 (RLR-2, also known as melanoma ... |
4-153 |
3.45e-06 |
|
DEXH-box helicase domain of RLR-2; RIG-I-like receptor 2 (RLR-2, also known as melanoma differentiation-associated protein 5 or Mda5 and IFIH1) is a viral double-stranded RNA (dsRNA) receptor that shares sequence similarity and signaling pathways with RIG-I, yet plays essential functions in antiviral immunity through distinct specificity for viral RNA. RLR-2 recognizes the internal duplex structure, whereas RIG-I recognizes the terminus of dsRNA. RLR-2 uses direct protein-protein contacts to stack along dsRNA in a head-to-tail arrangement. The signaling domain (tandem CARD), which decorates the outside of the core RLR-2 filament, also has an intrinsic propensity to oligomerize into an elongated structure that activates the signaling adaptor, MAVS. RLR-2 uses long dsRNA as a signaling platform to cooperatively assemble the core filament, which in turn promotes stochastic assembly of the tandem CARD oligomers for signaling. LGP2 appears to positively and negatively regulate RLR-2 and RIG-I signaling, respectively. RLR-2 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: 350832 [Multi-domain] Cd Length: 216 Bit Score: 48.32 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 4 TLRPYQQEAVDATLSHfrrhrTPAVIVLPTGAGKSLVIAELAR---------VARGRVLVLAHVKELVAQNHAK------ 68
Cdd:cd18074 2 TLRDYQMEVAKPALEG-----KNIIICLPTGSGKTRVAVYITKdhldkkrkaSEPGKVIVLVNKVPLVEQHYRKefnpfl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 69 ---YCALGLEADI-----FAAGLKRKEsqgkVVFGSVQSVARNLDAFQEE---------FSLLIVDECHRIgdDEDSQYQ 131
Cdd:cd18074 77 khwYQVIGLSGDSqlkisFPEVVKRYD----VIICTAQILENSLLNATEEedegvqlsdFSLIIIDECHHT--QKEAVYN 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 446500276 132 QILTH----------LSKVN----PHLRLLGLTATP 153
Cdd:cd18074 151 NIMRRylkqkiknrkQKKENkpliPLPQILGLTASP 186
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
255-322 |
1.33e-05 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, 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: 350174 [Multi-domain] Cd Length: 131 Bit Score: 44.81 E-value: 1.33e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 255 VMIFAATVEHAKEIVGLLPAD--DAALITGDTPGPERDALIDNFKAQRFRYLVNVSVLTTGFDAPHVDLI 322
Cdd:cd18787 30 AIIFVNTKKRVDRLAELLEELgiKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAARGLDIPGVDHV 99
|
|
| SWI2_SNF2 |
pfam18766 |
SWI2/SNF2 ATPase; A SWi2/SNF2 ATPase found in polyvalent proteins. |
33-153 |
4.95e-05 |
|
SWI2/SNF2 ATPase; A SWi2/SNF2 ATPase found in polyvalent proteins.
Pssm-ID: 465860 [Multi-domain] Cd Length: 222 Bit Score: 44.73 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 33 TGAGKSLVIAELAR-VARG----RVLVLAHVKELVAQNHAKYCALGLEADIFA---AGLKRK-ESQGKVVFGSVQSVARN 103
Cdd:pfam18766 28 QGSGKSLTMVFLARkLRRElknpTVVVVTDRNDLDDQLTKTFAACGREVPVQAesrKDLRELlRGSGGIIFTTIQKFGET 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 446500276 104 LDAFQEEFS-----LLIVDECHRigddedSQYQQILTHLSKVNPHLRLLGLTATP 153
Cdd:pfam18766 108 PDEGFPVLSdrrniIVLVDEAHR------SQYGGLAANMRDALPNAAFIGFTGTP 156
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
222-343 |
7.50e-05 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350176 [Multi-domain] Cd Length: 153 Bit Score: 43.39 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 222 FSEADLNRELKKQQRI---TPHIIsQIVEF-----AQTRKgVMIFAATVEHAKEIVGLLpadDAALITGDTPGPERDALI 293
Cdd:cd18789 13 YREYLGLGAHRKRRLLaamNPNKL-RALEEllkrhEQGDK-IIVFTDNVEALYRYAKRL---LKPFITGETPQSEREEIL 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446500276 294 DNFKAQRFRYLVNVSVLTTGFDAPHVDLIAILRPTE-SVSLYQQIVGRGLR 343
Cdd:cd18789 88 QNFREGEYNTLVVSKVGDEGIDLPEANVAIQISGHGgSRRQEAQRLGRILR 138
|
|
| DEXHc_UvsW |
cd18031 |
DEXH-box helicase domain of bacteriophage UvsW; Bacteriophage UvsW is part of the WXY system ... |
8-153 |
9.39e-05 |
|
DEXH-box helicase domain of bacteriophage UvsW; Bacteriophage UvsW is part of the WXY system that repairs DNA damage by a process that involves homologous recombination. UvsW 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: 350789 [Multi-domain] Cd Length: 161 Bit Score: 43.19 E-value: 9.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 8 YQQEAVDATLSHFRRhrtpaVIVLPTGAGKSLVIAELARV----ARGRVLVLAHVKELVAQ---NHAKYCALGLEA--DI 78
Cdd:cd18031 4 YQKDAVFEGLVNRRR-----ILNLPTSAGRSLIQALLARYylenYEGKILIIVPTTALTTQmadDFVDYRLFSHAMikKI 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446500276 79 FAAGLKRKESQGK--VVFGSVQSVARNLDAFQEEFSLLIVDECHRigddedSQYQQILTHLSKVNPHLRLLGLTATP 153
Cdd:cd18031 79 GGGASKDDKYKNDapVVVGTWQTVVKQPKEWFSQFGMMMNDECHL------ATGKSISSIISGLNNCMFKFGLSGSL 149
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
4-152 |
1.19e-04 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 45.09 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 4 TLRPYQQEAVDATLSHfrrhrTPAVIVLPTGAGKSLVIAELARVARGRVLVLAHVKELVAQNHAKYCALGLEADIFAAGL 83
Cdd:PRK11057 25 QFRPGQQEIIDAVLSG-----RDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAAACLNSTQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 84 KRKESQG----------KVVFGSVQSVArnLDAFQEEF-----SLLIVDECHRI---GDDEDSQYQQiLTHLSKVNPHLR 145
Cdd:PRK11057 100 TREQQLEvmagcrtgqiKLLYIAPERLM--MDNFLEHLahwnpALLAVDEAHCIsqwGHDFRPEYAA-LGQLRQRFPTLP 176
|
....*..
gi 446500276 146 LLGLTAT 152
Cdd:PRK11057 177 FMALTAT 183
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
7-152 |
1.52e-04 |
|
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350772 [Multi-domain] Cd Length: 205 Bit Score: 43.23 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 7 PYQQEAVDATLshfrRHRTPAVIVLPTGAGKSLVIAELARVARGRVLV----LAHVKELVaqNHAKycALGLEADIFAAG 82
Cdd:cd18014 16 PLQEKATMAVV----KGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVisplIALIQDQV--DHLK--TLKIRVDSLNSK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 83 LKRKESqgKVVFGSVQSVARNL------------DAFQEEF---------SLLIVDECHRI---GDDEDSQYQQiLTHLS 138
Cdd:cd18014 88 LSAQER--KRIIADLESEKPQTkflyitpemaatSSFQPLLsslvsrnllSYLVVDEAHCVsqwGHDFRPDYLR-LGALR 164
|
170
....*....|....
gi 446500276 139 KVNPHLRLLGLTAT 152
Cdd:cd18014 165 SRYGHVPWVALTAT 178
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
232-348 |
1.97e-04 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350188 [Multi-domain] Cd Length: 143 Bit Score: 41.96 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 232 KKQQRITP------HIISQIVEFAQTRKG--VMIFAATVEHAKEIVGLLPADD----AALITGDTPGP--------ERDA 291
Cdd:cd18801 2 RKVEKIHPklekleEIVKEHFKKKQEGSDtrVIIFSEFRDSAEEIVNFLSKIRpgirATRFIGQASGKsskgmsqkEQKE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 446500276 292 LIDNFKAQRFRYLVNVSVLTTGFDAPHVDLIAILRPTESVSLYQQIVGRGLRLAPGK 348
Cdd:cd18801 82 VIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGRKRQGR 138
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
1-152 |
2.11e-04 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 42.63 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 1 MIFTLRPYQQEAVDATLSHfrrhrTPAVIVLPTGAGKSLV--IAELARVARGRVLVLAhVKELVA----QNHAkycalgL 74
Cdd:cd18018 9 GHPSFRPGQEEAIARLLSG-----RSTLVVLPTGAGKSLCyqLPALLLRRRGPGLTLV-VSPLIAlmkdQVDA------L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 75 EADIFAAGL-------KRKESQGKVVFGSVQ----SVARnldAFQEEF----------SLLIVDECHRI---GDDEDSQY 130
Cdd:cd18018 77 PRAIKAAALnssltreERRRILEKLRAGEVKilyvSPER---LVNESFrellrqtppiSLLVVDEAHCIsewSHNFRPDY 153
|
170 180
....*....|....*....|..
gi 446500276 131 QQILTHLSKVNPHLRLLGLTAT 152
Cdd:cd18018 154 LRLCRVLRELLGAPPVLALTAT 175
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
4-152 |
2.24e-04 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 44.50 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 4 TLRPYQQEAVDATLSHFRrhrtpaVIVL-PTGAGKSLVIAELARVARGRVLVLAHVKELV---------AQNHAKYCALG 73
Cdd:PLN03137 460 SFRPNQREIINATMSGYD------VFVLmPTGGGKSLTYQLPALICPGITLVISPLVSLIqdqimnllqANIPAASLSAG 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 74 LE----ADIFAAgLKRKESQGKVVFGSVQSVA------RNLDAF--QEEFSLLIVDECHRI---GDDEDSQYQQiLTHLS 138
Cdd:PLN03137 534 MEwaeqLEILQE-LSSEYSKYKLLYVTPEKVAksdsllRHLENLnsRGLLARFVIDEAHCVsqwGHDFRPDYQG-LGILK 611
|
170
....*....|....
gi 446500276 139 KVNPHLRLLGLTAT 152
Cdd:PLN03137 612 QKFPNIPVLALTAT 625
|
|
| rad25 |
TIGR00603 |
DNA repair helicase rad25; All proteins in this family for which functions are known are ... |
5-155 |
2.47e-04 |
|
DNA repair helicase rad25; All proteins in this family for which functions are known are DNA-DNA helicases used for the initiation of nucleotide excision repair and transacription as part of the TFIIH complex.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273168 [Multi-domain] Cd Length: 732 Bit Score: 44.02 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 5 LRPYQQEAVDATLSHfRRHRTpAVIVLPTGAGKSLVIAELARVARGRVLVLAHVKELVAQNHAKYcalGLEADIFAAGLK 84
Cdd:TIGR00603 256 IRPYQEKSLSKMFGN-GRARS-GIIVLPCGAGKSLVGVTAACTVKKSCLVLCTSAVSVEQWKQQF---KMWSTIDDSQIC 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 85 RKESQGKVVFGSVQSVA------------RNLDAFQ-------EEFSLLIVDECHRIgddEDSQYQQILThlsKVNPHLR 145
Cdd:TIGR00603 331 RFTSDAKERFHGEAGVVvstysmvahtgkRSYESEKvmewltnREWGLILLDEVHVV---PAAMFRRVLT---IVQAHCK 404
|
170
....*....|
gi 446500276 146 lLGLTATPFR 155
Cdd:TIGR00603 405 -LGLTATLVR 413
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
3-152 |
3.44e-04 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 43.77 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 3 FTLRPYQQEAVDATLShfRRHrtpaVIVL-PTGAGKSLViAELA---RVARGRVLV-LAHVKELVAQNHAKYCAL----- 72
Cdd:COG4581 24 FELDPFQEEAILALEA--GRS----VLVAaPTGSGKTLV-AEFAiflALARGRRSFyTAPIKALSNQKFFDLVERfgaen 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 73 -GL---------EADIfaaglkrkesqgkVVfgSVQSVARNLdAFQEEFSLL-----IVDECHRIGD-DEDSQYQQILTH 136
Cdd:COG4581 97 vGLltgdasvnpDAPI-------------VV--MTTEILRNM-LYREGADLEdvgvvVMDEFHYLADpDRGWVWEEPIIH 160
|
170
....*....|....*.
gi 446500276 137 LSkvnPHLRLLGLTAT 152
Cdd:COG4581 161 LP---ARVQLVLLSAT 173
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
6-152 |
4.39e-04 |
|
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations in RecQ2 cause Bloom syndrome.
Pssm-ID: 350774 [Multi-domain] Cd Length: 208 Bit Score: 41.74 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 6 RPYQQEAVDATLSHfrrhrTPAVIVLPTGAGKSLVIAELARVARGRVLVLAHVKELVAQNHAKY-----CALGLEADIFA 80
Cdd:cd18016 19 RTNQLEAINAALLG-----EDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLtsldiPATYLTGDKTD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 81 AG-------LKRKESQGKVVFGS---VQSVARNLDAFQE--EFSLL---IVDECHRI---GDDEDSQYQQiLTHLSKVNP 142
Cdd:cd18016 94 AEatkiylqLSKKDPIIKLLYVTpekISASNRLISTLENlyERKLLarfVIDEAHCVsqwGHDFRPDYKR-LNMLRQKFP 172
|
170
....*....|
gi 446500276 143 HLRLLGLTAT 152
Cdd:cd18016 173 SVPMMALTAT 182
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
3-152 |
8.83e-04 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 42.18 E-value: 8.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 3 FTLRPYQQEAVDatlsHFRRHRTPAVIVlPTGAGKSLVIAELARVARGRVLVLAHVKELVAQNHAKYCALGLEADIfaaG 82
Cdd:PRK01172 21 FELYDHQRMAIE----QLRKGENVIVSV-PTAAGKTLIAYSAIYETFLAGLKSIYIVPLRSLAMEKYEELSRLRSL---G 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 83 LKRKESQGKvvFGSVQSVARNLDA-----------------FQEEFSLLIVDECHRIGD-DEDSQYQQILTHLSKVNPHL 144
Cdd:PRK01172 93 MRVKISIGD--YDDPPDFIKRYDVviltsekadslihhdpyIINDVGLIVADEIHIIGDeDRGPTLETVLSSARYVNPDA 170
|
....*...
gi 446500276 145 RLLGLTAT 152
Cdd:PRK01172 171 RILALSAT 178
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
3-153 |
1.08e-03 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 40.48 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 3 FTLRPYQQEAVDATLSHFRR-HRTPAVIVLPTGAGKSLV--IAELARVARGRVLVLAHVKELVAQNHAKYcALGLEADI- 78
Cdd:cd17918 14 FSLTKDQAQAIKDIEKDLHSpEPMDRLLSGDVGSGKTLValGAALLAYKNGKQVAILVPTEILAHQHYEE-ARKFLPFIn 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446500276 79 ---FAAGLKRKESQGK-VVFGSVQSVARnlDAFQEEFSLLIVDECHRIGddedSQYQQILTHLSKVNphlrLLGLTATP 153
Cdd:cd17918 93 velVTGGTKAQILSGIsLLVGTHALLHL--DVKFKNLDLVIVDEQHRFG----VAQREALYNLGATH----FLEATATP 161
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
4-40 |
1.25e-03 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 41.67 E-value: 1.25e-03
10 20 30
....*....|....*....|....*....|....*..
gi 446500276 4 TLRPYQQEAVDATLSHfRRhrtpAVIVLPTGAGKSLV 40
Cdd:COG0514 17 SFRPGQEEIIEAVLAG-RD----ALVVMPTGGGKSLC 48
|
|
| rpl40e |
PRK04136 |
50S ribosomal protein L40e; Provisional |
428-451 |
4.20e-03 |
|
50S ribosomal protein L40e; Provisional
Pssm-ID: 179746 Cd Length: 48 Bit Score: 35.28 E-value: 4.20e-03
10 20
....*....|....*....|....
gi 446500276 428 RFRFKNCPQCNAENDIAARRCREC 451
Cdd:PRK04136 11 VFNKKICMRCNARNPWRATKCRKC 34
|
|
| PRK04914 |
PRK04914 |
RNA polymerase-associated protein RapA; |
106-157 |
4.91e-03 |
|
RNA polymerase-associated protein RapA;
Pssm-ID: 235319 [Multi-domain] Cd Length: 956 Bit Score: 39.82 E-value: 4.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446500276 106 AFQEEFSLLIVDECHRIGDDEDSQ---YqQILTHLSKVNPHLrLLgLTATPFRLG 157
Cdd:PRK04914 268 ALAAEWDLLVVDEAHHLVWSEEAPsreY-QVVEQLAEVIPGV-LL-LTATPEQLG 319
|
|
| Cas3_I |
cd09696 |
CRISPR/Cas system-associated protein Cas3; Distinct Cas3 family with HD domain fused to ... |
232-353 |
5.35e-03 |
|
CRISPR/Cas system-associated protein Cas3; Distinct Cas3 family with HD domain fused to C-termus of Helicase domain; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DNA helicase Cas3; This protein includes both DEAH and HD motifs; signature gene for Type I
Pssm-ID: 187827 [Multi-domain] Cd Length: 843 Bit Score: 39.62 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 232 KKQQRITPHIISQIVEFAQTRKGVMIFAATVEHAKEIVGLLPADDAALITGDTPGPERDALIDNFKAQRFR--------- 302
Cdd:cd09696 251 SDEKFLSTMVKELNLLMKDSGGAILVFCRTVKHVRKVFAKLPKEKFELLTGTLRGAERDDLVKKEIFNRFLpqmlsgsra 330
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 446500276 303 -------YLVNVSVLTTGFDAPHVDLIAILRPTESVslyQQIVGRGLRLAPgKTDCLI 353
Cdd:cd09696 331 rpqqgtvYLVCTSAGEVGVNISADHLVCDLAPFESM---QQRFGRVNRFGE-LQACQI 384
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
32-139 |
6.91e-03 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 38.38 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 32 PTGAGKSL-----VIAEL--ARVARGRVLVLAHVKELVAQNHAKYCALGLEADIFAAGL----KRKESQGKVVFGSVQS- 99
Cdd:cd17956 44 PTGSGKTLayvlpIVQALskRVVPRLRALIVVPTKELVQQVYKVFESLCKGTGLKVVSLsgqkSFKKEQKLLLVDTSGRy 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 446500276 100 -------VA---RNLDAFQ--EEFSL-----LIVDECHRIGddeDSQYQQILTHLSK 139
Cdd:cd17956 124 lsrvdilVAtpgRLVDHLNstPGFTLkhlrfLVIDEADRLL---NQSFQDWLETVMK 177
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
255-322 |
7.08e-03 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 38.97 E-value: 7.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446500276 255 VMIFAATVEHAKEIVGLLPAD--DAALITGDTPGPERDALIDNFKAQRFRYLVnvsvlTT-----GFDAPHVDLI 322
Cdd:COG0513 244 AIVFCNTKRGADRLAEKLQKRgiSAAALHGDLSQGQRERALDAFRNGKIRVLV-----ATdvaarGIDIDDVSHV 313
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-150 |
8.31e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 37.35 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446500276 32 PTGAGKSLVIAELARvargrvlvlahvkeLVAQNHAKYCALGLEADIFAAGLKRKESQGKVVFGSVQSVARNLDAF---- 107
Cdd:smart00382 10 PPGSGKTTLARALAR--------------ELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALalar 75
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446500276 108 QEEFSLLIVDECHRIGDDEDSQYQQILTHLSKVNPHLRLLGLT 150
Cdd:smart00382 76 KLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLT 118
|
|
| UPF0547 |
pfam10571 |
Uncharacterized protein family UPF0547; This domain contains a zinc-ribbon motif. |
432-451 |
9.40e-03 |
|
Uncharacterized protein family UPF0547; This domain contains a zinc-ribbon motif.
Pssm-ID: 402278 [Multi-domain] Cd Length: 26 Bit Score: 34.09 E-value: 9.40e-03
|
| |
