|
Name |
Accession |
Description |
Interval |
E-value |
| COG4951 |
COG4951 |
Uncharacterized conserved protein [Function unknown]; |
8-783 |
0e+00 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443978 [Multi-domain] Cd Length: 793 Bit Score: 959.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 8 DELAALRAENARLVSLLEAHGIEWRRKPQTPVQRV-SVLSTDEKVALFRRLFRGRDDVWALRWESKTSGKSGYSPACANE 86
Cdd:COG4951 11 ARLAELEAENARLRNLLEAHGIPPDPPPATQPELVtSSSSPEEKIALFRSLFKGRTDVYAKRWESKKTGKSGYSPACANE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 87 WQARICGKPRIKCGDCAHRQLIPVSDLVIYHHLAGTHTVGMYPLLEDDSCYFLAVDFDEAEWQKDASAFMRSCDELGVPA 166
Cdd:COG4951 91 WRKGICNKPRIKCKDCKNRSYLPLTDSVIYDHLRGKDVIGIYPLLEDNTCWFLAADFDKAGWQEDARAFVEVCREFGIPA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 167 ALEISRSRQGAHVWIFFASRVSAREARRLGTAIISYTCSRTRQLRLGSYDRLFPNQDTMPKGGFGNLIALPLQKRPRELG 246
Cdd:COG4951 171 ALERSRSGNGAHVWIFFEEPVSARLARKLGTALLTEAMERRPELSFSSYDRLFPNQDTLPKGGFGNLIALPLQKKARENG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 247 GSVFVDMNLQPYPDQWAFLVSVTPMNVQDIEPTILRATGSIHPLDVNfiNEEDLGTPWeEKKSSGNRLNISIAEPLKITL 326
Cdd:COG4951 251 NSVFVDEDFEPYPDQWAFLSSIKKLSEQDLESLILKLEGGAELLDVR--DDEDDSKPW-ERPRRTKLLKGDFPKTLTITL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 327 ANQIYFEKAQLPQVLINRLIRLAAFPNPEFYKAQAMRMSVWNKPRVIGCAENYPQHIALPRGCLDSVLSFLRDNNIAAEL 406
Cdd:COG4951 328 ANMIYIPKSGLPQALLNRLKRLAAFQNPEFYKAQAMRLSTFGKPRIISCAEETPGYLALPRGCDDDLILLLKHGKIEILD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 407 IDKRFAGTECNAVFMGNLRAEQEEAVSALLRYDTGVLCAPTAFGKTVTAAAVIAKRKVNTLILVHRTELLKQWQERLAvF 486
Cdd:COG4951 408 DDRRGGGKNIEVFFFGLLRDQQQAAAAALLKHDGGVLAAATAFGKTVVAAIIIARKKVNTLILVHRRLLLQQWKRRLL-F 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 487 LQAGDSIGIIGGGKHKPCGNIDIAVVQSISRQGEVEPLVRN--YGQIIVDECHHIGAVSFSAILKETNARYLLGLTATPI 564
Cdd:COG4951 487 FLLINEEGPIGGGGGKKKGKKDIIITQQLSRSRSGLDIDDIiaYGQVIVDEDHHHSAAAFEAVEVRAKAAVVYGLTATAT 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 565 RRDGLHPIIFMYCGAIRHTAvrPKESPHNLEVLIRSRFTSGHLPSDARIQDIFREIALDHDRTVAIAEEAMKAFGQGRKV 644
Cdd:COG4951 567 RKRKNHDVILMFVGPGRHHA--RHKAQAQFEGPVRRVRIRSTKPPEPPIPEDDPRRTTVPRRRRLQAEAKLRIIAERDEV 644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 645 LVLTERTDHLDEIASVMNSLKLSPFILHGRLSKKKRAMLISGLNALPPDSPRILLS--TGRLIGEGFDHPPLDTLILAMP 722
Cdd:COG4951 645 VNLLERRIILLEREEVALLLLRLLLVLLRIVLKLEKASGLLKRKLASLELAAGGVLttTGKVIGEGGDPLILLFLLLILA 724
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830559 723 VSWKGTLQQYAGRLHREHTGKSDVRIIDFVDTAYPVLLRMWDKRQRGYKAMGYRIIADGDE 783
Cdd:COG4951 725 TGFKGGLIQYRGRLHRLALAKVRVAYRDYVVHGLVLLRDKVLKRRYGYKRYAYRKRGRLES 785
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
424-563 |
7.52e-46 |
|
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: 160.55 E-value: 7.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 424 LRAEQEEAVSALL---RYDTGVLCAPTAFGKTVTAAAVIAKRKV-NTLILVHRTELLKQWQERLAVFLQAGDSIGI-IGG 498
Cdd:cd17926 1 LRPYQEEALEAWLahkNNRRGILVLPTGSGKTLTALALIAYLKElRTLIVVPTDALLDQWKERFEDFLGDSSIGLIgGGK 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830559 499 GKHKPCGNIDIAVVQSISRQGEVE-PLVRNYGQIIVDECHHIGAVSFSAILKETNARYLLGLTATP 563
Cdd:cd17926 81 KKDFDDANVVVATYQSLSNLAEEEkDLFDQFGLLIVDEAHHLPAKTFSEILKELNAKYRLGLTATP 146
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
423-565 |
1.88e-24 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 100.44 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 423 NLRAEQEEAVSALLRY-----DTGVLCAPTAFGKTVTAAAVIAK-----RKVNTLILVHRTELLKQWQERLAVFLQAGDS 492
Cdd:pfam04851 3 ELRPYQIEAIENLLESikngqKRGLIVMATGSGKTLTAAKLIARlfkkgPIKKVLFLVPRKDLLEQALEEFKKFLPNYVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 493 IGIIGGGKHKP----CGNIDIAVVQSISR---QGEVEPLVRNYGQIIVDECHHIGAVSFSAILKETNARYLLGLTATPIR 565
Cdd:pfam04851 83 IGEIISGDKKDesvdDNKIVVTTIQSLYKaleLASLELLPDFFDVIIIDEAHRSGASSYRNILEYFKPAFLLGLTATPER 162
|
|
| PrimPol_Msp |
NF040561 |
CRISPR-associated primase-polymerase type A1; |
26-277 |
3.24e-22 |
|
CRISPR-associated primase-polymerase type A1;
Pssm-ID: 468537 [Multi-domain] Cd Length: 515 Bit Score: 101.31 E-value: 3.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 26 AHGIEWRRKPQTPVQRVSVLSTDekVALFRRLFRGRDDVWALRWESKTsGKSGYSPAcanewqaricgkprikcgdcaHR 105
Cdd:NF040561 102 AGIEKEEELLKEPFFTFRLREED--LSRFMELFSGREDCFARQWNDRE-EKQGYSPV---------------------RR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 106 qliPVSDLVIYHHLAGTHTVGMYPLLEDDSCYFLAVDFDEAE---------------WQKDASAFMRSCD---ELGVPAA 167
Cdd:NF040561 158 ---PMTEEDVLEHLNGKRTYGIYLLRKDNRVRFAVLDIDIKKslrarqltpknkqsvRREAVYVALRIPEllkDEGLKCL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 168 LEISRSRqGAHVWIFFASRVSAREARRlgtaiISYTCSRTRQLRLGSYDR-LFPNQDTMPKGGFGNLIALPLQKRPRELG 246
Cdd:NF040561 235 VEFSGGK-GYHFWFFFDEPVPAYKVRE-----FLKTILNKIEPDLSCINLeVFPKQDRLGGKGLGNLVKLPLGIHRLTGK 308
|
250 260 270
....*....|....*....|....*....|.
gi 15830559 247 GSVFVDMNLQPYPDQWAFLVSVTPMNVQDIE 277
Cdd:NF040561 309 RSLFVDENGEPVENQLEFLLKIRPNSKEAIE 339
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
420-596 |
9.67e-19 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 85.24 E-value: 9.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 420 FMGNLRAEQEEAVSALLR-YDTGVLCAPTAFGKTVTAAAVIAKR-----KVNTLILVHRTELLKQWQERLAVFLQA---- 489
Cdd:smart00487 5 GFEPLRPYQKEAIEALLSgLRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLGPSlglk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 490 ------GDSIGIIGGGKHKPCGNIDIAVVQSISRQGEVEPL-VRNYGQIIVDECHHIGAVSFSAILKE-----TNARYLL 557
Cdd:smart00487 85 vvglygGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLsLSNVDLVILDEAHRLLDGGFGDQLEKllkllPKNVQLL 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 15830559 558 GLTATPIRRdgLHPIIFMYCGAIRHTAVRPKeSPHNLEV 596
Cdd:smart00487 165 LLSATPPEE--IENLLELFLNDPVFIDVGFT-PLEPIEQ 200
|
|
| uvsW |
PHA02558 |
UvsW helicase; Provisional |
428-753 |
2.45e-07 |
|
UvsW helicase; Provisional
Pssm-ID: 222875 [Multi-domain] Cd Length: 501 Bit Score: 54.25 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 428 QEEAVSALLRYDTGVLCAPTAFGKTVTAAAV----IAKRKVNTLILVHRTELLKQ---------WQERLAVflqagdsig 494
Cdd:PHA02558 119 QYDAVYEGLKNNRRLLNLPTSAGKSLIQYLLsryyLENYEGKVLIIVPTTSLVTQmiddfvdyrLFPREAM--------- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 495 iigggkHKPCG----NIDIAVV----QSISRQGEvePLVRNYGQIIVDECHHIGAVSFSAILKE-TNARYLLGLTATPir 565
Cdd:PHA02558 190 ------HKIYSgtakDTDAPIVvstwQSAVKQPK--EWFDQFGMVIVDECHLFTGKSLTSIITKlDNCKFKFGLTGSL-- 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 566 RDG-LHPIIFM-YCGAIRH--TAVRPKESPHNLEVLIRSRFTsGHlPSDARIQDIFR------EIALDHD-RTVAIAEEA 634
Cdd:PHA02558 260 RDGkANILQYVgLFGDIFKpvTTSQLMEEGQVTDLKINSIFL-RY-PDEDRVKLKGEdyqeeiKYITSHTkRNKWIANLA 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 635 MKAFGQGRKVLVLTERTDHLDEIASVMNSLKLSPFILHGRLSKKKR----AMLISGLNALppdsprILLSTGrLIGEGFD 710
Cdd:PHA02558 338 LKLAKKGENTFVMFKYVEHGKPLYEMLKKVYDKVYYVSGEVDTEDRnemkKIAEGGKGII------IVASYG-VFSTGIS 410
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 15830559 711 HPPLDTLILAMPVSWKGTLQQYAGRLHREHTGKSDVRIIDFVD 753
Cdd:PHA02558 411 IKNLHHVIFAHPSKSKIIVLQSIGRVLRKHGSKSIATVWDIID 453
|
|
| rad25 |
TIGR00603 |
DNA repair helicase rad25; All proteins in this family for which functions are known are ... |
424-567 |
5.45e-07 |
|
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: 53.26 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 424 LRAEQEEAVSALL---RYDTGVLCAPTAFGKT---VTAAAVIAKRkvnTLILVHRTELLKQWQERLAVFLQAGDSIGII- 496
Cdd:TIGR00603 256 IRPYQEKSLSKMFgngRARSGIIVLPCGAGKSlvgVTAACTVKKS---CLVLCTSAVSVEQWKQQFKMWSTIDDSQICRf 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 497 -GGGKHKPCGNIDIAV------VQSISRQGEVEPLV-----RNYGQIIVDECHHIGAVSFSAILKETNARYLLGLTATPI 564
Cdd:TIGR00603 333 tSDAKERFHGEAGVVVstysmvAHTGKRSYESEKVMewltnREWGLILLDEVHVVPAAMFRRVLTIVQAHCKLGLTATLV 412
|
...
gi 15830559 565 RRD 567
Cdd:TIGR00603 413 RED 415
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG4951 |
COG4951 |
Uncharacterized conserved protein [Function unknown]; |
8-783 |
0e+00 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443978 [Multi-domain] Cd Length: 793 Bit Score: 959.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 8 DELAALRAENARLVSLLEAHGIEWRRKPQTPVQRV-SVLSTDEKVALFRRLFRGRDDVWALRWESKTSGKSGYSPACANE 86
Cdd:COG4951 11 ARLAELEAENARLRNLLEAHGIPPDPPPATQPELVtSSSSPEEKIALFRSLFKGRTDVYAKRWESKKTGKSGYSPACANE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 87 WQARICGKPRIKCGDCAHRQLIPVSDLVIYHHLAGTHTVGMYPLLEDDSCYFLAVDFDEAEWQKDASAFMRSCDELGVPA 166
Cdd:COG4951 91 WRKGICNKPRIKCKDCKNRSYLPLTDSVIYDHLRGKDVIGIYPLLEDNTCWFLAADFDKAGWQEDARAFVEVCREFGIPA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 167 ALEISRSRQGAHVWIFFASRVSAREARRLGTAIISYTCSRTRQLRLGSYDRLFPNQDTMPKGGFGNLIALPLQKRPRELG 246
Cdd:COG4951 171 ALERSRSGNGAHVWIFFEEPVSARLARKLGTALLTEAMERRPELSFSSYDRLFPNQDTLPKGGFGNLIALPLQKKARENG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 247 GSVFVDMNLQPYPDQWAFLVSVTPMNVQDIEPTILRATGSIHPLDVNfiNEEDLGTPWeEKKSSGNRLNISIAEPLKITL 326
Cdd:COG4951 251 NSVFVDEDFEPYPDQWAFLSSIKKLSEQDLESLILKLEGGAELLDVR--DDEDDSKPW-ERPRRTKLLKGDFPKTLTITL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 327 ANQIYFEKAQLPQVLINRLIRLAAFPNPEFYKAQAMRMSVWNKPRVIGCAENYPQHIALPRGCLDSVLSFLRDNNIAAEL 406
Cdd:COG4951 328 ANMIYIPKSGLPQALLNRLKRLAAFQNPEFYKAQAMRLSTFGKPRIISCAEETPGYLALPRGCDDDLILLLKHGKIEILD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 407 IDKRFAGTECNAVFMGNLRAEQEEAVSALLRYDTGVLCAPTAFGKTVTAAAVIAKRKVNTLILVHRTELLKQWQERLAvF 486
Cdd:COG4951 408 DDRRGGGKNIEVFFFGLLRDQQQAAAAALLKHDGGVLAAATAFGKTVVAAIIIARKKVNTLILVHRRLLLQQWKRRLL-F 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 487 LQAGDSIGIIGGGKHKPCGNIDIAVVQSISRQGEVEPLVRN--YGQIIVDECHHIGAVSFSAILKETNARYLLGLTATPI 564
Cdd:COG4951 487 FLLINEEGPIGGGGGKKKGKKDIIITQQLSRSRSGLDIDDIiaYGQVIVDEDHHHSAAAFEAVEVRAKAAVVYGLTATAT 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 565 RRDGLHPIIFMYCGAIRHTAvrPKESPHNLEVLIRSRFTSGHLPSDARIQDIFREIALDHDRTVAIAEEAMKAFGQGRKV 644
Cdd:COG4951 567 RKRKNHDVILMFVGPGRHHA--RHKAQAQFEGPVRRVRIRSTKPPEPPIPEDDPRRTTVPRRRRLQAEAKLRIIAERDEV 644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 645 LVLTERTDHLDEIASVMNSLKLSPFILHGRLSKKKRAMLISGLNALPPDSPRILLS--TGRLIGEGFDHPPLDTLILAMP 722
Cdd:COG4951 645 VNLLERRIILLEREEVALLLLRLLLVLLRIVLKLEKASGLLKRKLASLELAAGGVLttTGKVIGEGGDPLILLFLLLILA 724
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830559 723 VSWKGTLQQYAGRLHREHTGKSDVRIIDFVDTAYPVLLRMWDKRQRGYKAMGYRIIADGDE 783
Cdd:COG4951 725 TGFKGGLIQYRGRLHRLALAKVRVAYRDYVVHGLVLLRDKVLKRRYGYKRYAYRKRGRLES 785
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
376-768 |
2.52e-83 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 276.52 E-value: 2.52e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 376 AENYPQHIALPRGCLDSVLSFLRDNNIAAELIDKRFAGTECNAVFMGNLRAEQEEAVSALLRY-----DTGVLCAPTAFG 450
Cdd:COG1061 33 NLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFELRPYQQEALEALLAAlerggGRGLVVAPTGTG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 451 KTVTAAAVIAK--RKVNTLILVHRTELLKQWQERLAVFLqagdSIGIIGGGKHKPCGNIDIAVVQSISRQGEVEPLVRNY 528
Cdd:COG1061 113 KTVLALALAAEllRGKRVLVLVPRRELLEQWAEELRRFL----GDPLAGGGKKDSDAPITVATYQSLARRAHLDELGDRF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 529 GQIIVDECHHIGAVSFSAILKETNARYLLGLTATPIRRDGLHPIIFMYCGaIRHTaVRPKE-------SPHNLEVlIRSR 601
Cdd:COG1061 189 GLVIIDEAHHAGAPSYRRILEAFPAAYRLGLTATPFRSDGREILLFLFDG-IVYE-YSLKEaiedgylAPPEYYG-IRVD 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 602 FTSGHLPSDARIQDIFREIALDHDRTVAIAEEAMKAFGQGRKVLVLTERTDHLDEIASVMNSLKLSPFILHGRLSKKKRA 681
Cdd:COG1061 266 LTDERAEYDALSERLREALAADAERKDKILRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKERE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 682 MLISGLNAlppDSPRILLsTGRLIGEGFDHPPLDTLILAMPVSWKGTLQQYAGRLHREHTGKSDVRIIDFVDTAYPVLLR 761
Cdd:COG1061 346 EILEAFRD---GELRILV-TVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKEDALVYDFVGNDVPVLEE 421
|
....*..
gi 15830559 762 MWDKRQR 768
Cdd:COG1061 422 LAKDLRD 428
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
424-563 |
7.52e-46 |
|
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: 160.55 E-value: 7.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 424 LRAEQEEAVSALL---RYDTGVLCAPTAFGKTVTAAAVIAKRKV-NTLILVHRTELLKQWQERLAVFLQAGDSIGI-IGG 498
Cdd:cd17926 1 LRPYQEEALEAWLahkNNRRGILVLPTGSGKTLTALALIAYLKElRTLIVVPTDALLDQWKERFEDFLGDSSIGLIgGGK 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830559 499 GKHKPCGNIDIAVVQSISRQGEVE-PLVRNYGQIIVDECHHIGAVSFSAILKETNARYLLGLTATP 563
Cdd:cd17926 81 KKDFDDANVVVATYQSLSNLAEEEkDLFDQFGLLIVDEAHHLPAKTFSEILKELNAKYRLGLTATP 146
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
424-570 |
2.33e-25 |
|
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: 103.02 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 424 LRAEQEEAVSALLR-----YDTGVLCAPTAFGKTVTAAAVI-----AKRKVNTLILVHRTELLKQWQERLAVFLQAGDSI 493
Cdd:cd18032 1 PRYYQQEAIEALEEarekgQRRALLVMATGTGKTYTAAFLIkrlleANRKKRILFLAHREELLEQAERSFKEVLPDGSFG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830559 494 GIIGGGKHKPCGNIDIAVVQSISRQGEVEPLVRNY-GQIIVDECHHIGAVSFSAILKETNARYLLGLTATPIRRDGLH 570
Cdd:cd18032 81 NLKGGKKKPDDARVVFATVQTLNKRKRLEKFPPDYfDLIIIDEAHHAIASSYRKILEYFEPAFLLGLTATPERTDGLD 158
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
423-565 |
1.88e-24 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 100.44 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 423 NLRAEQEEAVSALLRY-----DTGVLCAPTAFGKTVTAAAVIAK-----RKVNTLILVHRTELLKQWQERLAVFLQAGDS 492
Cdd:pfam04851 3 ELRPYQIEAIENLLESikngqKRGLIVMATGSGKTLTAAKLIARlfkkgPIKKVLFLVPRKDLLEQALEEFKKFLPNYVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 493 IGIIGGGKHKP----CGNIDIAVVQSISR---QGEVEPLVRNYGQIIVDECHHIGAVSFSAILKETNARYLLGLTATPIR 565
Cdd:pfam04851 83 IGEIISGDKKDesvdDNKIVVTTIQSLYKaleLASLELLPDFFDVIIIDEAHRSGASSYRNILEYFKPAFLLGLTATPER 162
|
|
| PrimPol_Msp |
NF040561 |
CRISPR-associated primase-polymerase type A1; |
26-277 |
3.24e-22 |
|
CRISPR-associated primase-polymerase type A1;
Pssm-ID: 468537 [Multi-domain] Cd Length: 515 Bit Score: 101.31 E-value: 3.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 26 AHGIEWRRKPQTPVQRVSVLSTDekVALFRRLFRGRDDVWALRWESKTsGKSGYSPAcanewqaricgkprikcgdcaHR 105
Cdd:NF040561 102 AGIEKEEELLKEPFFTFRLREED--LSRFMELFSGREDCFARQWNDRE-EKQGYSPV---------------------RR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 106 qliPVSDLVIYHHLAGTHTVGMYPLLEDDSCYFLAVDFDEAE---------------WQKDASAFMRSCD---ELGVPAA 167
Cdd:NF040561 158 ---PMTEEDVLEHLNGKRTYGIYLLRKDNRVRFAVLDIDIKKslrarqltpknkqsvRREAVYVALRIPEllkDEGLKCL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 168 LEISRSRqGAHVWIFFASRVSAREARRlgtaiISYTCSRTRQLRLGSYDR-LFPNQDTMPKGGFGNLIALPLQKRPRELG 246
Cdd:NF040561 235 VEFSGGK-GYHFWFFFDEPVPAYKVRE-----FLKTILNKIEPDLSCINLeVFPKQDRLGGKGLGNLVKLPLGIHRLTGK 308
|
250 260 270
....*....|....*....|....*....|.
gi 15830559 247 GSVFVDMNLQPYPDQWAFLVSVTPMNVQDIE 277
Cdd:NF040561 309 RSLFVDENGEPVENQLEFLLKIRPNSKEAIE 339
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
420-596 |
9.67e-19 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 85.24 E-value: 9.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 420 FMGNLRAEQEEAVSALLR-YDTGVLCAPTAFGKTVTAAAVIAKR-----KVNTLILVHRTELLKQWQERLAVFLQA---- 489
Cdd:smart00487 5 GFEPLRPYQKEAIEALLSgLRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLGPSlglk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 490 ------GDSIGIIGGGKHKPCGNIDIAVVQSISRQGEVEPL-VRNYGQIIVDECHHIGAVSFSAILKE-----TNARYLL 557
Cdd:smart00487 85 vvglygGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLsLSNVDLVILDEAHRLLDGGFGDQLEKllkllPKNVQLL 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 15830559 558 GLTATPIRRdgLHPIIFMYCGAIRHTAVRPKeSPHNLEV 596
Cdd:smart00487 165 LLSATPPEE--IENLLELFLNDPVFIDVGFT-PLEPIEQ 200
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
642-752 |
6.55e-12 |
|
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: 61.57 E-value: 6.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 642 RKVLVLTERTDHLDEIASVMNslklspfilhgrlskkkramlisglnalppdspriLLSTGRLIGEGFDHPPLDTLILAM 721
Cdd:cd18785 4 VKIIVFTNSIEHAEEIASSLE-----------------------------------ILVATNVLGEGIDVPSLDTVIFFD 48
|
90 100 110
....*....|....*....|....*....|.
gi 15830559 722 PVSWKGTLQQYAGRLHRehTGKSDVRIIDFV 752
Cdd:cd18785 49 PPSSAASYIQRVGRAGR--GGKDEGEVILFV 77
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
441-562 |
1.84e-10 |
|
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: 59.72 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 441 GVLCAPTAFGKTVTAAAVIA----KRKVNTLILVHRTELLKQWQERLAVFLQAG------DSIGIIGGGKHKPCGNIDIA 510
Cdd:cd00046 4 VLITAPTGSGKTLAALLAALllllKKGKKVLVLVPTKALALQTAERLRELFGPGirvavlVGGSSAEEREKNKLGDADII 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830559 511 VV--QSI--SRQGEVEPLVRNYGQIIVDECHHI---GAVSFSAILKETNARY----LLGLTAT 562
Cdd:cd00046 84 IAtpDMLlnLLLREDRLFLKDLKLIIVDEAHALlidSRGALILDLAVRKAGLknaqVILLSAT 146
|
|
| DEXHc_XPB |
cd18029 |
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ... |
424-568 |
3.96e-09 |
|
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: 56.54 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 424 LRAEQEEAVSALL---RYDTGVLCAPTAFGKTVTAAAVIAKRKVNTLILVHRTELLKQWQ-----------ERLAVFlqA 489
Cdd:cd18029 9 LRPYQEKALSKMFgngRARSGVIVLPCGAGKTLVGITAACTIKKSTLVLCTSAVSVEQWRrqfldwttiddEQIGRF--T 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 490 GDSIGIIgggkHKPCgnIDIAVVQSISRQGEVEPL---------VRNYGQIIVDECHHIGAVSFSAILKETNARYLLGLT 560
Cdd:cd18029 87 SDKKEIF----PEAG--VTVSTYSMLANTRKRSPEsekfmefitEREWGLIILDEVHVVPAPMFRRVLTLQKAHCKLGLT 160
|
....*...
gi 15830559 561 ATPIRRDG 568
Cdd:cd18029 161 ATLVREDD 168
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
643-752 |
2.00e-07 |
|
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: 50.25 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 643 KVLVLTERTDHLDEIASVMNSLKLSPFILHGRLSKKKRAMLISGLNALPPDSPRILLSTGrLIGEGFDHPPLDTLILAMP 722
Cdd:cd18799 8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEALILLFFGELKPPILVTVD-LLTTGVDIPEVDNVVFLRP 86
|
90 100 110
....*....|....*....|....*....|
gi 15830559 723 VSWKGTLQQYAGRLHREHTGKSDVRIIDFV 752
Cdd:cd18799 87 TESRTLFLQMLGRGLRLHEGKDFFTILDFI 116
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
628-738 |
2.10e-07 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They 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: 350180 [Multi-domain] Cd Length: 135 Bit Score: 50.55 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 628 VAIAEEAMKAFGQGRKVLVLTERTDHLDEIASVMNSLKLSPFILHGRLSKKKRAMLISGLNAlPPDSPRILLSTgRLIGE 707
Cdd:cd18793 14 EALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNE-DPDIRVFLLST-KAGGV 91
|
90 100 110
....*....|....*....|....*....|..
gi 15830559 708 GFDHPPLDTLILAMPvSWK-GTLQQYAGRLHR 738
Cdd:cd18793 92 GLNLTAANRVILYDP-WWNpAVEEQAIDRAHR 122
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
450-567 |
2.29e-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: 51.91 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 450 GKTVTAAAVIA-------KRKVntLILVHRTeLLKQWQE------RLAVFLQAGDSIGIIGGGKHKPCGNIDIAVV--QS 514
Cdd:cd18011 29 GKTIEAGLIIKelllrgdAKRV--LILCPAS-LVEQWQDelqdkfGLPFLILDRETAAQLRRLIGNPFEEFPIVIVslDL 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830559 515 ISRQGEVEPLV--RNYGQIIVDECHHIGAvsfSAILKETN-----------ARYLLGLTATPIRRD 567
Cdd:cd18011 106 LKRSEERRGLLlsEEWDLVVVDEAHKLRN---SGGGKETKryklgrllakrARHVLLLTATPHNGK 168
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
428-565 |
2.40e-07 |
|
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: 51.09 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 428 QEEAVSALLRYDTGVLCAPTAFGKTvtAAAVIA--------KRKVNTLILVHRTELLKQ----WQERLA------VFLQA 489
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKT--LAFLLPalealdklDNGPQALVLAPTRELAEQiyeeLKKLGKglglkvASLLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 490 GDSIGIIGGGKHKPcgniDIAV-----VQSISRQgevEPLVRNYGQIIVDECHHIGAVSFSAILKE-----TNARYLLGL 559
Cdd:pfam00270 82 GDSRKEQLEKLKGP----DILVgtpgrLLDLLQE---RKLLKNLKLLVLDEAHRLLDMGFGPDLEEilrrlPKKRQILLL 154
|
....*.
gi 15830559 560 TATPIR 565
Cdd:pfam00270 155 SATLPR 160
|
|
| uvsW |
PHA02558 |
UvsW helicase; Provisional |
428-753 |
2.45e-07 |
|
UvsW helicase; Provisional
Pssm-ID: 222875 [Multi-domain] Cd Length: 501 Bit Score: 54.25 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 428 QEEAVSALLRYDTGVLCAPTAFGKTVTAAAV----IAKRKVNTLILVHRTELLKQ---------WQERLAVflqagdsig 494
Cdd:PHA02558 119 QYDAVYEGLKNNRRLLNLPTSAGKSLIQYLLsryyLENYEGKVLIIVPTTSLVTQmiddfvdyrLFPREAM--------- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 495 iigggkHKPCG----NIDIAVV----QSISRQGEvePLVRNYGQIIVDECHHIGAVSFSAILKE-TNARYLLGLTATPir 565
Cdd:PHA02558 190 ------HKIYSgtakDTDAPIVvstwQSAVKQPK--EWFDQFGMVIVDECHLFTGKSLTSIITKlDNCKFKFGLTGSL-- 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 566 RDG-LHPIIFM-YCGAIRH--TAVRPKESPHNLEVLIRSRFTsGHlPSDARIQDIFR------EIALDHD-RTVAIAEEA 634
Cdd:PHA02558 260 RDGkANILQYVgLFGDIFKpvTTSQLMEEGQVTDLKINSIFL-RY-PDEDRVKLKGEdyqeeiKYITSHTkRNKWIANLA 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 635 MKAFGQGRKVLVLTERTDHLDEIASVMNSLKLSPFILHGRLSKKKR----AMLISGLNALppdsprILLSTGrLIGEGFD 710
Cdd:PHA02558 338 LKLAKKGENTFVMFKYVEHGKPLYEMLKKVYDKVYYVSGEVDTEDRnemkKIAEGGKGII------IVASYG-VFSTGIS 410
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 15830559 711 HPPLDTLILAMPVSWKGTLQQYAGRLHREHTGKSDVRIIDFVD 753
Cdd:PHA02558 411 IKNLHHVIFAHPSKSKIIVLQSIGRVLRKHGSKSIATVWDIID 453
|
|
| rad25 |
TIGR00603 |
DNA repair helicase rad25; All proteins in this family for which functions are known are ... |
424-567 |
5.45e-07 |
|
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: 53.26 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 424 LRAEQEEAVSALL---RYDTGVLCAPTAFGKT---VTAAAVIAKRkvnTLILVHRTELLKQWQERLAVFLQAGDSIGII- 496
Cdd:TIGR00603 256 IRPYQEKSLSKMFgngRARSGIIVLPCGAGKSlvgVTAACTVKKS---CLVLCTSAVSVEQWKQQFKMWSTIDDSQICRf 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 497 -GGGKHKPCGNIDIAV------VQSISRQGEVEPLV-----RNYGQIIVDECHHIGAVSFSAILKETNARYLLGLTATPI 564
Cdd:TIGR00603 333 tSDAKERFHGEAGVVVstysmvAHTGKRSYESEKVMewltnREWGLILLDEVHVVPAAMFRRVLTIVQAHCKLGLTATLV 412
|
...
gi 15830559 565 RRD 567
Cdd:TIGR00603 413 RED 415
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
450-701 |
2.53e-06 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 50.99 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 450 GKTVTAAAVIAKRKVN-----TLILVhRTELLKQWQERLAVFLQAGDSI----GIIGGGKHKPCGNIDIAVV--QSISRq 518
Cdd:COG0553 272 GKTIQALALLLELKERglarpVLIVA-PTSLVGNWQRELAKFAPGLRVLvldgTRERAKGANPFEDADLVITsyGLLRR- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 519 gEVEPLVR-NYGQIIVDECHHI---GAVSFSAIlKETNARYLLGLTATPI--RRDGLHPII-FMYCG------AIRHTAV 585
Cdd:COG0553 350 -DIELLAAvDWDLVILDEAQHIknpATKRAKAV-RALKARHRLALTGTPVenRLEELWSLLdFLNPGllgslkAFRERFA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 586 RPKE--SPHNLEVLIR------SRFTSGH----LPS------------------DARIQDIFREIALDH----------- 624
Cdd:COG0553 428 RPIEkgDEEALERLRRllrpflLRRTKEDvlkdLPEkteetlyveltpeqralyEAVLEYLRRELEGAEgirrrglilaa 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 625 ----------------------------DRTVAIAEEAMKAfgqGRKVLVLTERTDHLDEIASVMNSLKLSPFILHGRLS 676
Cdd:COG0553 508 ltrlrqicshpallleegaelsgrsaklEALLELLEELLAE---GEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTS 584
|
330 340
....*....|....*....|....*
gi 15830559 677 KKKRAMLISGLNAlPPDSPRILLST 701
Cdd:COG0553 585 AEERDELVDRFQE-GPEAPVFLISL 608
|
|
| HsdR |
COG4096 |
Type I site-specific restriction endonuclease, part of a restriction-modification system ... |
450-570 |
5.37e-06 |
|
Type I site-specific restriction endonuclease, part of a restriction-modification system [Defense mechanisms];
Pssm-ID: 443272 [Multi-domain] Cd Length: 806 Bit Score: 50.23 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 450 GKTVTAAAVI-----AKRKVNTLILVHRTELLKQWQERLAVFLQAGDSIGIIGGGKHKPCGN--IDIAVVQ---SISRQG 519
Cdd:COG4096 190 GKTRTAIALIyrllkAGRAKRILFLADRNALVDQAKNAFKPFLPDLDAFTKLYNKSKDIDKSarVYFSTYQtmmNRIDGE 269
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 15830559 520 EVEPLVRNYGQ-----IIVDECHHIGAVSFSAILKETNArYLLGLTATPIRRDGLH 570
Cdd:COG4096 270 EEEPGYRQFPPdffdlIIIDECHRGIYSKWRAILDYFDA-LQIGLTATPKDTIDRN 324
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
531-753 |
1.31e-05 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 48.54 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 531 IIVDECHHIGAVSFSAI------LKETNARYLLgLTAT--PIRRDGLHPIIFMYCGAirhtavrPKESPHNLEVLIRSRF 602
Cdd:COG1203 272 IILDEVQAYPPYMLALLlrllewLKNLGGSVIL-MTATlpPLLREELLEAYELIPDE-------PEELPEYFRAFVRKRV 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 603 TsghlpsdariqdiFREIALDHDrtvAIAEEAMKAFGQGRKVLVLTERTDHLDEIASVMNSLKLSP--FILHGRLSKKKR 680
Cdd:COG1203 344 E-------------LKEGPLSDE---ELAELILEALHKGKSVLVIVNTVKDAQELYEALKEKLPDEevYLLHSRFCPADR 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 681 AMLISGL-NALPPDSPRILLSTgRLIGEGFDH---------PPLDTLIlampvswkgtlqQYAGRLHRE--HTGKSDVRI 748
Cdd:COG1203 408 SEIEKEIkERLERGKPCILVST-QVVEAGVDIdfdvvirdlAPLDSLI------------QRAGRCNRHgrKEEEGNVYV 474
|
....*
gi 15830559 749 IDFVD 753
Cdd:COG1203 475 FDPED 479
|
|
| DEXHc_RLR-3 |
cd18075 |
DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of ... |
424-563 |
4.39e-05 |
|
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: 45.23 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 424 LRAEQEEAVSALLRYDTGVLCAPTAFGKTvTAAAVIAKRKVNT------LILVHRTELLKQWQE--------RLAVFLQA 489
Cdd:cd18075 3 LHGYQWEVVAPALRGKNSIIWLPTGAGKT-RAAVYVARRHLETkrgakvAVLVNKVHLVDQHLEkefhvlldKYTVTAIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 490 GDSIGIIGGGKHKPCGNIDIAVVQ-------SISRQGEVEplVRNYGQIIVDECHHIGAvsfSAILKETNARYL------ 556
Cdd:cd18075 82 GDSSHKCFFGQLARGSDVVICTAQilqnallSGEEEAHVE--LTDFSLLVIDECHHTHK---EAVYNKIMLSYLekklsr 156
|
170
....*....|....
gi 15830559 557 -------LGLTATP 563
Cdd:cd18075 157 qgdlpqiLGLTASP 170
|
|
| DNA_primase_S |
pfam01896 |
DNA primase small subunit; DNA primase synthesizes the RNA primers for the Okazaki fragments ... |
130-289 |
9.42e-05 |
|
DNA primase small subunit; DNA primase synthesizes the RNA primers for the Okazaki fragments in lagging strand DNA synthesis. DNA primase is a heterodimer of large and small subunits. This family also includes baculovirus late expression factor 1 or LEF-1 proteins. Baculovirus LEF-1 is a DNA primase enzyme. The family also contains many bacterial DNA primases.
Pssm-ID: 460377 [Multi-domain] Cd Length: 158 Bit Score: 43.36 E-value: 9.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 130 LLEDDSCYFLAVDFDEAEWQKDASAFMRSC--DELGVPAALEISRSRQGAHVWIFFASRVSAREARRLGTAiisytcsrt 207
Cdd:pfam01896 5 MDDYDDPRIADVCEKCWRFVEVAVKLLDELlrEDFGFPDTLWVFSGRRGFHVWVPDKDARFLTDEERAAIA--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 208 rqlrlgSYDRLFPNQDTMPKGgfGNLIALPLQKRPRELGGSVFVDMNLQPYPDQWAFLVSVTPMNV-QDIEPTIlRATGS 286
Cdd:pfam01896 76 ------NYLNLHGTLDQLIVT--EKDLFNDFDELIKKLLDRLPDKSLGERLRKKWKYLYPRIDENVtKGIRHLL-KAPFS 146
|
...
gi 15830559 287 IHP 289
Cdd:pfam01896 147 IHG 149
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
425-563 |
2.51e-04 |
|
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: 42.50 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 425 RAEQEEAVSALLRYDTgVLCAPTAFGKTVTAAAVIA----KRKVNTLILVHRTELLKQWQERLAVFLQAGDSIGIIGGGK 500
Cdd:cd18035 4 RLYQVLIAAVALNGNT-LIVLPTGLGKTIIAILVAAdrltKKGGKVLILAPSRPLVEQHAENLKRVLNIPDKITSLTGEV 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830559 501 hKP--------CGNIDIAVVQSISRQ---GEVEplVRNYGQIIVDECHH-IGAVSFSAI----LKETNARYLLGLTATP 563
Cdd:cd18035 83 -KPeeraerwdASKIIVATPQVIENDllaGRIT--LDDVSLLIFDEAHHaVGNYAYVYIahryKREANNPLILGLTASP 158
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
428-562 |
8.20e-04 |
|
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: 41.09 E-value: 8.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 428 QEEAVSALLRYDTGVL-CAPTAFGKTVTAAAVIAK--RKVNTLILV---HR---TELLKQWQERLA-----VFLQAGDSI 493
Cdd:cd17921 6 QREALRALYLSGDSVLvSAPTSSGKTLIAELAILRalATSGGKAVYiapTRalvNQKEADLRERFGplgknVGLLTGDPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 494 GIIGGGKHKpcgniDIAVV-----QSISRQGEvEPLVRNYGQIIVDECHHIGAVSFSAILKET---------NARYlLGL 559
Cdd:cd17921 86 VNKLLLAEA-----DILVAtpeklDLLLRNGG-ERLIQDVRLVVVDEAHLIGDGERGVVLELLlsrllrinkNARF-VGL 158
|
...
gi 15830559 560 TAT 562
Cdd:cd17921 159 SAT 161
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
424-564 |
3.82e-03 |
|
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: 39.09 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 424 LRAEQEEAVSALL-RYDT---GVLCAPTAFGKTVTAAAVIA------KRKVNTLILV------H-RTELLKqWQERLAVF 486
Cdd:cd17919 1 LRPYQLEGLNFLLeLYENgpgGILADEMGLGKTLQAIAFLAyllkegKERGPVLVVCplsvleNwEREFEK-WTPDLRVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 487 LQAGDSIGIIGGGKHKPCGNIDIAVV--QSISRQGEVEPLVRnYGQIIVDECHHI--GAVSFSAILKETNARYLLGLTAT 562
Cdd:cd17919 80 VYHGSQRERAQIRAKEKLDKFDVVLTtyETLRRDKASLRKFR-WDLVVVDEAHRLknPKSQLSKALKALRAKRRLLLTGT 158
|
..
gi 15830559 563 PI 564
Cdd:cd17919 159 PL 160
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
428-562 |
5.84e-03 |
|
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: 38.47 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 428 QEEAVSA-LLRYDTGVLCAPTAFGKTVTAAAVIAKRKVN---TLILV-------HRTELLKQWQER-LAVFLQAGDsigi 495
Cdd:cd18028 6 QAEAVRAgLLKGENLLISIPTASGKTLIAEMAMVNTLLEggkALYLVplralasEKYEEFKKLEEIgLKVGISTGD---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 496 iGGGKHKPCGNIDIAV-----VQSISRQGEvePLVRNYGQIIVDECHHIGAVSFSAILKETNARY--------LLGLTAT 562
Cdd:cd18028 82 -YDEDDEWLGDYDIIVatyekFDSLLRHSP--SWLRDVGVVVVDEIHLISDEERGPTLESIVARLrrlnpntqIIGLSAT 158
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
424-563 |
7.31e-03 |
|
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: 38.61 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 424 LRAEQEEAVSALLRYDTGVLCAPTAFGKTVTAAAVI---------AKRKVNTLILVHRTELLKQWQERLAVFLQ------ 488
Cdd:cd18036 3 LRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICrhhlekrrsAGEKGRVVVLVNKVPLVEQQLEKFFKYFRkgykvt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830559 489 --AGDSIGIIGGGKHKPCGNIDIAVVQSI------SRQGEvEPLVRNYGQIIVDECHHIGA------VSFSAILKETNAR 554
Cdd:cd18036 83 glSGDSSHKVSFGQIVKASDVIICTPQILinnllsGREEE-RVYLSDFSLLIFDECHHTQKehpynkIMRMYLDKKLSSQ 161
|
170
....*....|...
gi 15830559 555 Y----LLGLTATP 563
Cdd:cd18036 162 GplpqILGLTASP 174
|
|
| |
