|
Name |
Accession |
Description |
Interval |
E-value |
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
1-588 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 residues long. This model represents bacterial proteins with a high degree of similarity in domain architecture and in primary sequence to E. coli RecQ. The model excludes eukaryotic and archaeal proteins with RecQ-like regions, as well as more distantly related bacterial helicases related to RecQ. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273594 [Multi-domain] Cd Length: 591 Bit Score: 881.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 1 MEATLSHYFGYDNFRPGQKEIITKIMDHHNVLGVLPTGGGKSICYQVPGLMLGGTTIVISPLISLMKDQVDQLKAMGIKA 80
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 81 AFLNSSLTKKQQKEIEDDLMKGHIQFLYVAPERFDNQYFLSLLSRIDIHLIAFDEAHCISKWGHDFRPSYQSVIKKVFTL 160
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 161 PQNFTIvALTATATAEVQQDIMGKLNIDRRDEVKTSTKRRNLIFKVNPTYQRQKFVVDYVQKHKEQAGIIYCSTRKQVEE 240
Cdd:TIGR01389 161 PQVPRI-ALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 241 LQEALDVINVSSAIYHAGLTNKERETAQNEFVYDKVKVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDG 320
Cdd:TIGR01389 240 LAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 321 LESECILLFSERDKGLHEYFITVSQADEDYKDKMGEKLTKMIQYTKTKKCLEATVVHYFEPNEkLEECGQCSSCIQQNKT 400
Cdd:TIGR01389 320 LPAEAILLYSPADIALLKRRIEQSEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENE-VEPCGNCDNCLDPPKS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 401 YDMTQEAKMIISCIARMRQKESYSVIIQVLRGETSDYIKYNNYDKLTTHGLMKDYTTSELSHLIDELRFKGFLNENDEIL 480
Cdd:TIGR01389 399 YDATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 481 I---CDESVKKLLNNKEKVFTTPFKQKSKEK--VYINTVEGVDRALYSELVEVRRKLSEKLDIAPVSIFSDYTLEEFAKR 555
Cdd:TIGR01389 479 IglqLTEAARKVLKNEVEVLLRPFKVVAKEKtrVQKNLSVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAEK 558
|
570 580 590
....*....|....*....|....*....|...
gi 1378690484 556 KPESKQEMISIDGVGSYKLKHYCPKFLEIIHSY 588
Cdd:TIGR01389 559 RPATLNALLKIKGVGQNKLDRYGEAFLEVIREY 591
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
1-467 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 670.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 1 MEATLSHYFGYDNFRPGQKEIITKIMDHHNVLGVLPTGGGKSICYQVPGLMLGGTTIVISPLISLMKDQVDQLKAMGIKA 80
Cdd:COG0514 5 ALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 81 AFLNSSLTKKQQKEIEDDLMKGHIQFLYVAPERFDNQYFLSLLSRIDIHLIAFDEAHCISKWGHDFRPSYQ--SVIKKVF 158
Cdd:COG0514 85 AFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRrlGELRERL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 159 TlpqNFTIVALTATATAEVQQDIMGKLNIDRRDEVKTSTKRRNLIFKVNPTYQRQK--FVVDYVQKHKEQAGIIYCSTRK 236
Cdd:COG0514 165 P---NVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPPDDKlaQLLDFLKEHPGGSGIVYCLSRK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 237 QVEELQEALDVINVSSAIYHAGLTNKERETAQNEFVYDKVKVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRA 316
Cdd:COG0514 242 KVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 317 GRDGLESECILLFSERDKGLHEYFITVSQADEDYKDKMGEKLTKMIQYTKTKKCLEATVVHYF-EPNEklEECGQCSSCI 395
Cdd:COG0514 322 GRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFgEELA--EPCGNCDNCL 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1378690484 396 QQNKTYDMTQEAKMIISCIARMRQKESYSVIIQVLRGETSDYIKYNNYDKLTTHGLMKDYTTSELSHLIDEL 467
Cdd:COG0514 400 GPPETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQL 471
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
2-585 |
1.79e-159 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 469.58 E-value: 1.79e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 2 EATLSHYFGYDNFRPGQKEIITKIMDHHNVLGVLPTGGGKSICYQVPGLMLGGTTIVISPLISLMKDQVDQLKAMGIKAA 81
Cdd:PRK11057 14 KQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 82 FLNSSLTKKQQKEIEDDLMKGHIQFLYVAPERFDNQYFLSLLSRIDIHLIAFDEAHCISKWGHDFRPSYQSV--IKKVF- 158
Cdd:PRK11057 94 CLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALgqLRQRFp 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 159 TLPqnftIVALTATATAEVQQDIMGKLNIDRRDEVKTSTKRRN----LIFKVNPTYQrqkfVVDYVQKHKEQAGIIYCST 234
Cdd:PRK11057 174 TLP----FMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNirytLVEKFKPLDQ----LMRYVQEQRGKSGIIYCNS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 235 RKQVEELQEALDVINVSSAIYHAGLTNKERETAQNEFVYDKVKVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAG 314
Cdd:PRK11057 246 RAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 315 RAGRDGLESECILLFSERD-----KGLHEyfitvsQADEDYKDKMGEKLTKMIQYTKTKKCLEATVVHYFEPNEKlEECG 389
Cdd:PRK11057 326 RAGRDGLPAEAMLFYDPADmawlrRCLEE------KPAGQQQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQ-EPCG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 390 QCSSCIQQNKTYDMTQEAKMIISCIARMRQKESYSVIIQVLRGETSDYIKYNNYDKLTTHGLMKDYTTSELSHLIDELRF 469
Cdd:PRK11057 399 NCDICLDPPKQYDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 470 KGFLNEN---DEILICDESVKKLLNNKEKV-FTTP----FKQKSKEKVYINTvegVDRALYSELVEVRRKLSEKLDIAPV 541
Cdd:PRK11057 479 LGLVTQNiaqHSALQLTEAARPVLRGEVSLqLAVPrivaLKPRAMQKSFGGN---YDRKLFAKLRKLRKSIADEENIPPY 555
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1378690484 542 SIFSDYTLEEFAKRKPESKQEMISIDGVGSYKLKHYCPKFLEII 585
Cdd:PRK11057 556 VVFNDATLIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMALI 599
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
5-454 |
5.39e-141 |
|
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are known are 3'-5' DNA-DNA helicases. These proteins are used for recombination, recombinational repair, and possibly maintenance of chromosome stability. 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: 129701 [Multi-domain] Cd Length: 470 Bit Score: 417.25 E-value: 5.39e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 5 LSHYFGYDNFRPGQKEIITKIMDHHNVLGVLPTGGGKSICYQVPGLMLGGTTIVISPLISLMKDQVDQLKAMGIKAAFLN 84
Cdd:TIGR00614 3 LKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATFLN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 85 SSLTKKQQKEIEDDLMKGHIQFLYVAPERF--DNQYFLSLLSRIDIHLIAFDEAHCISKWGHDFRPSYQSV--IKKVFTl 160
Cdd:TIGR00614 83 SAQTKEQQLNVLTDLKDGKIKLLYVTPEKIsaSNRLLQTLEERKGITLIAVDEAHCISQWGHDFRPDYKALgsLKQKFP- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 161 pqNFTIVALTATATAEVQQDIMGKLNIDRRDEVKTSTKRRNLIFKV-----NPTYQRQKFVVdyvQKHKEQAGIIYCSTR 235
Cdd:TIGR00614 162 --NVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVrrktpKILEDLLRFIR---KEFEGKSGIIYCPSR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 236 KQVEELQEALDVINVSSAIYHAGLTNKERETAQNEFVYDKVKVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGR 315
Cdd:TIGR00614 237 KKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 316 AGRDGLESECILLFSERDKGLHEYFItVSQADEDYKDKMGEKLTKMIQYTKTKKCLEATVVHYFE------------PNE 383
Cdd:TIGR00614 317 AGRDGLPSECHLFYAPADMNRLRRLL-MEEPDGNFRTYKLKLYEMMEYCLNSSTCRRLILLSYFGekgfnksfcimgTEK 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1378690484 384 KLEECGQCSSCIQQNKT---YDMTQEAKMIISCIARMRQKESYSVIIQVLRGETSDYIKYNNYDKLTTHGLMKD 454
Cdd:TIGR00614 396 CCDNCCKRLDYKTKDVTdkvYDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGRGKD 469
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
1-587 |
2.26e-98 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 324.93 E-value: 2.26e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 1 MEATLSHYFGYDNFRPGQKEIITKIMDHHNVLGVLPTGGGKSICYQVPGLMLGGTTIVISPLISLMKDQVDQLKAMGIKA 80
Cdd:PLN03137 448 LEVNNKKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPA 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 81 AFLNSSLTKKQQKEIEDDLMKGHIQF--LYVAPER----------FDNQYFLSLLSRIDIhliafDEAHCISKWGHDFRP 148
Cdd:PLN03137 528 ASLSAGMEWAEQLEILQELSSEYSKYklLYVTPEKvaksdsllrhLENLNSRGLLARFVI-----DEAHCVSQWGHDFRP 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 149 SYQS--VIKKVFtlpQNFTIVALTATATAEVQQDIMGKLNIDRRDEVKTSTKRRNLIFKVNPTYQR-----QKFVVdyvQ 221
Cdd:PLN03137 603 DYQGlgILKQKF---PNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKKclediDKFIK---E 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 222 KHKEQAGIIYCSTRKQVEELQEALDVINVSSAIYHAGLTNKERETAQNEFVYDKVKVVIATNAFGMGIDKSNVRYVIHYN 301
Cdd:PLN03137 677 NHFDECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHS 756
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 302 MPGDLESYYQEAGRAGRDGLESECILLFSERDKGLHEYFITVSQADEDyKDKMG---------------EKLTKMIQYTK 366
Cdd:PLN03137 757 LPKSIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEQS-PMAMGynrmassgriletntENLLRMVSYCE 835
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 367 T----KKCLEatVVHY---FEPNEKLEECGQCSScIQQNKTYDMTQEAKMIISCIARMRQKESYSVIIQVLRGETSDYIK 439
Cdd:PLN03137 836 NevdcRRFLQ--LVHFgekFDSTNCKKTCDNCSS-SKSLIDKDVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVK 912
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 440 YNNYDKLTTHGLMKDYTTSELSHLIDELRFKGFLNEN----------DEILICDES-VKKLLNNKEKV---FTTPFKQKS 505
Cdd:PLN03137 913 KHRHETLSLHGAGKHLSKGEASRILHYLVTEDILAEDvkksdlygsvSSLLKVNESkAYKLFSGGQTIimrFPSSVKASK 992
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 506 KEKVYINTVEG-------------------VDRALYSELVEVRRKLSEKL------DIAPVSIFSDYTLEEFAKRKPESK 560
Cdd:PLN03137 993 PSKFEATPAKGpltsgkqstlpmatpaqppVDLNLSAILYTALRKLRTALvkeagdGVMAYHIFGNATLQQISKRIPRTK 1072
|
650 660
....*....|....*....|....*..
gi 1378690484 561 QEMISIDGVGSYKLKHYCPKFLEIIHS 587
Cdd:PLN03137 1073 EELLEINGLGKAKVSKYGDRLLETIES 1099
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
2-197 |
3.78e-96 |
|
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: 292.13 E-value: 3.78e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 2 EATLSHYFGYDNFRPGQKEIITKIMDHHNVLGVLPTGGGKSICYQVPGLMLGGTTIVISPLISLMKDQVDQLKAMGIKAA 81
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 82 FLNSSLTKKQQKEIEDDLMKGHIQFLYVAPERFDNQYFLSLLSRID----IHLIAFDEAHCISKWGHDFRPSYQSvIKKV 157
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLR-LGRL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1378690484 158 FTLPQNFTIVALTATATAEVQQDIMGKLNIDRRDEVKTST 197
Cdd:cd17920 160 RRALPGVPILALTATATPEVREDILKRLGLRNPVIFRASF 199
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
2-197 |
1.34e-78 |
|
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: 246.78 E-value: 1.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 2 EATLSHYFGYDNFRPGQKEIITKIMDHHNVLGVLPTGGGKSICYQVPGLML----GGTTIVISPLISLMKDQVDQLKAmG 77
Cdd:cd18018 1 LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLrrrgPGLTLVVSPLIALMKDQVDALPR-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 78 IKAAFLNSSLTKKQQKEIEDDLMKGHIQFLYVAPERFDNQYFLSLL-SRIDIHLIAFDEAHCISKWGHDFRPSYQSVIKK 156
Cdd:cd18018 80 IKAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLrQTPPISLLVVDEAHCISEWSHNFRPDYLRLCRV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1378690484 157 VFTLPQNFTIVALTATATAEVQQDIMGKLNIDRRDEVKTST 197
Cdd:cd18018 160 LRELLGAPPVLALTATATKRVVEDIASHLGIPESGVVRGPL 200
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
3-190 |
2.18e-59 |
|
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: 196.82 E-value: 2.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 3 ATLSHYFGYDNFRPGQKEIITKIMDHHNVLGVLPTGGGKSICYQVPGLMLGGTTIVISPLISLMKDQVDQLKAMGIKAAF 82
Cdd:cd18015 8 DTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISATM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 83 LNSSLTKKQQKEIEDDLMKGHIQF--LYVAPE------RFDNQ----YFLSLLSRidihlIAFDEAHCISKWGHDFRPSY 150
Cdd:cd18015 88 LNASSSKEHVKWVHAALTDKNSELklLYVTPEkiakskRFMSKlekaYNAGRLAR-----IAIDEVHCCSQWGHDFRPDY 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1378690484 151 Q--SVIKKVFtlpQNFTIVALTATATAEVQQDIMGKLNIDRR 190
Cdd:cd18015 163 KklGILKRQF---PNVPILGLTATATSKVLKDVQKILCIQKC 201
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
3-187 |
2.06e-54 |
|
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ATP-dependent helicase or WRN) 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 Werner's syndrome.
Pssm-ID: 350775 [Multi-domain] Cd Length: 193 Bit Score: 183.05 E-value: 2.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 3 ATLSHYFGYDNFRPGQKEIItkimdhHNVLG-------VLPTGGGKSICYQVPGLMLGGTTIVISPLISLMKDQVDQLKA 75
Cdd:cd18017 2 NALNEYFGHSSFRPVQWKVI------RSVLEerrdnlvVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 76 MGIKAAFLNSSltkkQQKEIEDDLMKGHIQFLYVAPERFDNQyfLSLLSRIDIH--LIAFDEAHCISKWGHDFRPSYQ-- 151
Cdd:cd18017 76 SNIPACFLGSA----QSQNVLDDIKMGKIRVIYVTPEFVSKG--LELLQQLRNGitLIAIDEAHCVSQWGHDFRSSYRhl 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 1378690484 152 SVIKKVftLPqNFTIVALTATATAEVQQDIMGKLNI 187
Cdd:cd18017 150 GSIRNR--LP-NVPIVALTATATPSVRDDIIKNLNL 182
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
199-329 |
6.22e-52 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. 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: 350181 [Multi-domain] Cd Length: 134 Bit Score: 174.32 E-value: 6.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 199 RRNLIFKV---NPTYQRQKFVVDYVQKHKEQAGIIYCSTRKQVEELQEALDVINVSSAIYHAGLTNKERETAQNEFVYDK 275
Cdd:cd18794 1 RPNLFYSVrpkDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1378690484 276 VKVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDGLESECILLF 329
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
1-189 |
1.95e-49 |
|
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: 170.39 E-value: 1.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 1 MEATLSHYFGYDNFRPGQKEIITKIMDHHNVLGVLPTGGGKSICYQVPGLMLGGTTIVISPLISLMKDQVDQLKAMGIKA 80
Cdd:cd18016 5 MMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 81 AFLNSSLTKKQQKEIEDDLMKGH--IQFLYVAPER----------FDNQYFLSLLSRIDIhliafDEAHCISKWGHDFRP 148
Cdd:cd18016 85 TYLTGDKTDAEATKIYLQLSKKDpiIKLLYVTPEKisasnrlistLENLYERKLLARFVI-----DEAHCVSQWGHDFRP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1378690484 149 SYQ--SVIKKVFtlpQNFTIVALTATATAEVQQDIMGKLNIDR 189
Cdd:cd18016 160 DYKrlNMLRQKF---PSVPMMALTATATPRVQKDILNQLKMLR 199
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
4-189 |
1.45e-46 |
|
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: 162.64 E-value: 1.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 4 TLSHYFGYDNFR-PGQKEIITKIMDHH-NVLGVLPTGGGKSICYQVPGLMLGGTTIVISPLISLMKDQVDQLKAMGIKAA 81
Cdd:cd18014 3 TLKKVFGHSDFKsPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIRVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 82 FLNSSLTKKQQKEIEDDL--MKGHIQFLYVAPER----FDNQYFLSLLSRIDIHLIAFDEAHCISKWGHDFRPSYQ---S 152
Cdd:cd18014 83 SLNSKLSAQERKRIIADLesEKPQTKFLYITPEMaatsSFQPLLSSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLrlgA 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 1378690484 153 VIKKVFTLPqnftIVALTATATAEVQQDIMGKLNIDR 189
Cdd:cd18014 163 LRSRYGHVP----WVALTATATPQVQEDIFAQLRLKK 195
|
|
| DpdF |
NF041063 |
protein DpdF; |
5-333 |
7.84e-38 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 149.68 E-value: 7.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 5 LSHYFGYDNFR-PGQKEII----------TkimdhhnVLGVLPTGGGKSICYQVPGLML---GGTTIVISPLISLMKDQV 70
Cdd:NF041063 131 LAEALGFTHYRsPGQREAVraallappgsT-------LIVNLPTGSGKSLVAQAPALLAsrqGGLTLVVVPTVALAIDQE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 71 DQLKAMGIKAAFLN-------SSLTKKQQKEIEDDLMKGHIQFLYVAPErfdnqyflSLLSRID-----------IHLIA 132
Cdd:NF041063 204 RRARELLRRAGPDLggplawhGGLSAEERAAIRQRIRDGTQRILFTSPE--------SLTGSLRpalfdaaeaglLRYLV 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 133 FDEAHCISKWGHDFRPSYQSV---IKKVFTL---PQNFTIVALTATATA---EVQQDIMGKlnIDRRDEVKTSTKRRNLI 203
Cdd:NF041063 276 VDEAHLVDQWGDGFRPEFQLLaglRRSLLRLapsGRPFRTLLLSATLTEstlDTLETLFGP--PGPFIVVSAVQLRPEPA 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 204 FKVNPT---YQRQKFVVDYVqKHKEQAGIIYCSTRKQVEE----LQEA----LDVInvssaiyHAGLTNKERETAQNEFV 272
Cdd:NF041063 354 YWVAKCdseEERRERVLEAL-RHLPRPLILYVTKVEDAEAwlqrLRAAgfrrVALF-------HGDTPDAERERLIEQWR 425
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1378690484 273 YDKVKVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDGLESECILLFSERD 333
Cdd:NF041063 426 ENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDD 486
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
15-179 |
2.83e-29 |
|
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: 113.49 E-value: 2.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 15 RPGQKEIITKIMDHHNVLGVLPTGGGKSICYQVPGL------MLGGTTIVISPLISLMKDQVDQLKAMGIKAAF-LNSSL 87
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGLkVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 88 TKKQQKEIEDDLMKGHIqfLYVAPERFDnqYFLSLLSRI-DIHLIAFDEAHCISKWGhdFRPSYQSVIKKvftLPQNFTI 166
Cdd:pfam00270 81 GGDSRKEQLEKLKGPDI--LVGTPGRLL--DLLQERKLLkNLKLLVLDEAHRLLDMG--FGPDLEEILRR---LPKKRQI 151
|
170
....*....|...
gi 1378690484 167 VALTATATAEVQQ 179
Cdd:pfam00270 152 LLLSATLPRNLED 164
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
7-181 |
2.93e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 103.34 E-value: 2.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 7 HYFGYDNFRPGQKEIITKIMDH-HNVLGVLPTGGGKSICYQVPGLML-----GGTTIVISPLISLMKDQVDQLKAMGIKA 80
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 81 AFLNSSL-TKKQQKEIEDDLMKGHIQFLYVAPERFDNQYFLSLLSRIDIHLIAFDEAHCISKWGHdfrpsYQSVIKKVFT 159
Cdd:smart00487 82 GLKVVGLyGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGF-----GDQLEKLLKL 156
|
170 180
....*....|....*....|..
gi 1378690484 160 LPQNFTIVALTATATAEVQQDI 181
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLL 178
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
214-320 |
8.72e-24 |
|
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: 96.13 E-value: 8.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 214 KFVVDYVQKHKEQAGIIYCSTRKQVEElQEALDVINVSSAIYHAGLTNKERETAQNEFVYDKVKVVIATNAFGMGIDKSN 293
Cdd:pfam00271 4 EALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPD 82
|
90 100
....*....|....*....|....*..
gi 1378690484 294 VRYVIHYNMPGDLESYYQEAGRAGRDG 320
Cdd:pfam00271 83 VDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
239-320 |
3.55e-23 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 93.43 E-value: 3.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 239 EELQEALDVINVSSAIYHAGLTNKERETAQNEFVYDKVKVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGR 318
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1378690484 319 DG 320
Cdd:smart00490 81 AG 82
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
402-490 |
1.01e-21 |
|
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix structure; The RQC domain, found only in RecQ family enzymes, is a high affinity G4 DNA binding domain.
Pssm-ID: 214936 [Multi-domain] Cd Length: 92 Bit Score: 89.84 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 402 DMTQEAKMIISCIARMRQKESYSVIIQVLRGETSDYIKYNNYDKLTTHGLMKDYTTSELSHLIDELRFKGFLNENDE--- 478
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGryp 80
|
90
....*....|..
gi 1378690484 479 ILICDESVKKLL 490
Cdd:smart00956 81 YLKLTEKARPVL 92
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
399-496 |
8.93e-21 |
|
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix structure. The RQC domain, found only in RecQ family enzymes, is a high affinity G4 DNA binding domain.
Pssm-ID: 462780 [Multi-domain] Cd Length: 108 Bit Score: 87.59 E-value: 8.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 399 KTYDMTQEAKMIISCIARMRQKESYSVIIQVLRGETSDYIKYNNYDKLTTHGLMKDYTTSELSHLIDELRFKGFLNENDE 478
Cdd:pfam09382 3 ETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVDIE 82
|
90 100
....*....|....*....|.
gi 1378690484 479 ---ILICDESVKKLLNNKEKV 496
Cdd:pfam09382 83 fysVLKLTPKAREVLKGEEKV 103
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
200-329 |
2.76e-20 |
|
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: 86.79 E-value: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 200 RNLIFKVNPTYQRQKFVVDYVQKHKEQAGIIYCSTRKQVEELQEALDVINVSSAIYHAGLTNKERETAQNEFVYDKVKVV 279
Cdd:cd18787 2 KQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVL 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1378690484 280 IATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDGLESECILLF 329
Cdd:cd18787 82 VATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
518-585 |
5.30e-18 |
|
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic acid binding. Mutations in the HRDC domain cause human disease. It is interesting to note that the RecQ helicase in Deinococcus radiodurans has three tandem HRDC domains.
Pssm-ID: 425755 [Multi-domain] Cd Length: 68 Bit Score: 78.35 E-value: 5.30e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1378690484 518 DRALYSELVEVRRKLSEKLDIAPVSIFSDYTLEEFAKRKPESKQEMISIDGVGSYKLKHYCPKFLEII 585
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
10-336 |
2.92e-17 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 84.43 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 10 GYDNFRPGQKEIITKIMDHHNVLGVLPTGGGKSICYQVPGLML-----GGTT--IVISP---LIslmkDQV-DQLKAMGi 78
Cdd:COG0513 21 GYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRldpsrPRAPqaLILAPtreLA----LQVaEELRKLA- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 79 kaAFLN-SSLT----KKQQKEIEDdLMKGhIQFLyVA-PERFdnqyfLSLLSR--IDIHLIAF---DEAhciskwghD-- 145
Cdd:COG0513 96 --KYLGlRVATvyggVSIGRQIRA-LKRG-VDIV-VAtPGRL-----LDLIERgaLDLSGVETlvlDEA--------Drm 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 146 ----FRPSYQSVIKKvftLPQNFTIVALTATATAEVQ---QDIMG---KLNIDRRDEVKTSTKRRnlIFKVNPtYQRQKF 215
Cdd:COG0513 158 ldmgFIEDIERILKL---LPKERQTLLFSATMPPEIRklaKRYLKnpvRIEVAPENATAETIEQR--YYLVDK-RDKLEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 216 VVDYVQKHKEQAGIIYCSTRKQVEELQEALDVINVSSAIYHAGLTNKERETAQNEFVYDKVKVVIATNAFGMGIDKSNVR 295
Cdd:COG0513 232 LRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVS 311
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1378690484 296 YVIHYNMPGDLESYYQEAGRAGRDGLESECILLFSERDKGL 336
Cdd:COG0513 312 HVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRL 352
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
15-316 |
5.12e-17 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 84.31 E-value: 5.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 15 RPGQKEIITKIM-----DHHNVLGVLPTGGGKSICyqvpGLML------GGTTIVISPLISLMKDQVDQLKAmgikaaFL 83
Cdd:COG1061 82 RPYQQEALEALLaalerGGGRGLVVAPTGTGKTVL----ALALaaellrGKRVLVLVPRRELLEQWAEELRR------FL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 84 NSSLTKKQQKEIEDDLMKGHIQFLYVAPErfdnqyfLSLLSRiDIHLIAFDEAHciskwgHDFRPSYQSVIKKvftLPQN 163
Cdd:COG1061 152 GDPLAGGGKKDSDAPITVATYQSLARRAH-------LDELGD-RFGLVIIDEAH------HAGAPSYRRILEA---FPAA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 164 FtIVALTAT---------------------ATAEVQQD----------IMGKLNIDRRDEVKTSTKRRNLIFKVNPtyQR 212
Cdd:COG1061 215 Y-RLGLTATpfrsdgreillflfdgivyeySLKEAIEDgylappeyygIRVDLTDERAEYDALSERLREALAADAE--RK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 213 QKFVVDYVQKHKEQ-AGIIYCSTRKQVEELQEALDVINVSSAIYHAGLTNKERETAQNEFVYDKVKVVIATNAFGMGIDK 291
Cdd:COG1061 292 DKILRELLREHPDDrKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDV 371
|
330 340
....*....|....*....|....*.
gi 1378690484 292 SNVRYVIhYNMP-GDLESYYQEAGRA 316
Cdd:COG1061 372 PRLDVAI-LLRPtGSPREFIQRLGRG 396
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
28-172 |
8.79e-17 |
|
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: 77.44 E-value: 8.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 28 HHNVLGVLPTGGGKSICYQVPGLML----GGTTIVISPLISLMKDQVDQLKA---MGIKAAFLNSSLTKKQQKEIEddlm 100
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLllkkGKKVLVLVPTKALALQTAERLRElfgPGIRVAVLVGGSSAEEREKNK---- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1378690484 101 KGHIQFLYVAPERFDNQY-FLSLLSRIDIHLIAFDEAHCISKWGHDFRPSYQSVIKKVFTLPQnftIVALTAT 172
Cdd:cd00046 77 LGDADIIIATPDMLLNLLlREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQ---VILLSAT 146
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
10-346 |
3.59e-15 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 78.29 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 10 GYDNFRPGQKEIITKIMDHHNVLGVLPTGGGKSICYQVPGLM------LGGTT-------IVISPLISLMKDQVDQLKAM 76
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrcctirSGHPSeqrnplaMVLTPTRELCVQVEDQAKVL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 77 GIKAAFlnssltkKQQKEIEDDLMKGH-------IQFLYVAPERFdnqyfLSLLSRIDIHL-----IAFDEAHCISKWGh 144
Cdd:PLN00206 220 GKGLPF-------KTALVVGGDAMPQQlyriqqgVELIVGTPGRL-----IDLLSKHDIELdnvsvLVLDEVDCMLERG- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 145 dFRpsyQSVIKKVFTLPQNfTIVALTATATAEVQ-------QDIM----GKLNidrrdevKTSTKRRNLIFKVNPTYQRQ 213
Cdd:PLN00206 287 -FR---DQVMQIFQALSQP-QVLLFSATVSPEVEkfasslaKDIIlisiGNPN-------RPNKAVKQLAIWVETKQKKQ 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 214 K-FVVDYVQKHKEQAGIIYCSTRKQVEELQEALDVIN-VSSAIYHAGLTNKERETAQNEFVYDKVKVVIATNAFGMGIDK 291
Cdd:PLN00206 355 KlFDILKSKQHFKPPAVVFVSSRLGADLLANAITVVTgLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDL 434
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1378690484 292 SNVRYVIHYNMPGDLESYYQEAGRAGRDGLESECILLFSERDKGLHEYFITVSQA 346
Cdd:PLN00206 435 LRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKS 489
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
229-328 |
3.72e-15 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases 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: 350184 [Multi-domain] Cd Length: 146 Bit Score: 72.67 E-value: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 229 IIYCSTRKQVE----ELQEALDVINVSS---AIYHAGLTNKERETAQNEFVYDKVKVVIATNAFGMGIDKSNVRYVIHYN 301
Cdd:cd18797 39 IVFCRSRKLAElllrYLKARLVEEGPLAskvASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|....*..
gi 1378690484 302 MPGDLESYYQEAGRAGRDGLESECILL 328
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDSLVILV 145
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
229-328 |
2.39e-14 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases 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: 350182 [Multi-domain] Cd Length: 154 Bit Score: 70.66 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 229 IIYCSTRKQVEELqeALDVINVssAIYHAGLTNKERETAQNEFVYDKVKVVIATNAFGMGID--------KSNVRYVIHY 300
Cdd:cd18795 47 LVFCSSRKECEKT--AKDLAGI--AFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpartviiKGTQRYDGKG 122
|
90 100 110
....*....|....*....|....*....|
gi 1378690484 301 NMPGDLESYYQEAGRAGRDGLES--ECILL 328
Cdd:cd18795 123 YRELSPLEYLQMIGRAGRPGFDTrgEAIIM 152
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
9-324 |
2.82e-14 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 75.70 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 9 FGYDNFRPGQKEIITK-IMDHHNVLGVLPTGGGKS------ICYQvpgLMLGGTTIVISPLISL----MKDQVDQLKAMG 77
Cdd:COG1204 18 RGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTliaelaILKA---LLNGGKALYIVPLRALasekYREFKRDFEELG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 78 IKAAFLNSSLTkkqqkEIEDDLMKGHIqflYVA-PERFDnqyflSLLSRI-----DIHLIAFDEAHCIskwGHDFR-PSY 150
Cdd:COG1204 95 IKVGVSTGDYD-----SDDEWLGRYDI---LVAtPEKLD-----SLLRNGpswlrDVDLVVVDEAHLI---DDESRgPTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 151 QSVIKKVFTLPQNFTIVALTATAT-AEvqqDIMGKLN----------IDRRDEVKtstKRRNLIFKvnPTYQRQKFV-VD 218
Cdd:COG1204 159 EVLLARLRRLNPEAQIVALSATIGnAE---EIAEWLDaelvksdwrpVPLNEGVL---YDGVLRFD--DGSRRSKDPtLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 219 YVQKHKEQAG--IIYCSTRKQVEELQEAL---------------------DVINVSS----------------AIYHAGL 259
Cdd:COG1204 231 LALDLLEEGGqvLVFVSSRRDAESLAKKLadelkrrltpeereeleelaeELLEVSEethtnekladclekgvAFHHAGL 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1378690484 260 TNKERETAQNEFVYDKVKVVIATNAFGMGIdksN--VRYVI------HYNMPGDLESYYQEAGRAGRDGLESE 324
Cdd:COG1204 311 PSELRRLVEDAFREGLIKVLVATPTLAAGV---NlpARRVIirdtkrGGMVPIPVLEFKQMAGRAGRPGYDPY 380
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
18-331 |
1.42e-13 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 73.72 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 18 QKEIITKIMDHHNVLGVLPTGGGKSICYQVPGL--ML---GGTTIVISPLISLMKDQVDQLKAM------GIKAAFLNSS 86
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLeaLLedpGATALYLYPTKALARDQLRRLRELaealglGVRVATYDGD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 87 LTKKQQKEIED---------DLMkgHIQFLYVAPErfdnqyFLSLLSRIDihLIAFDEAHciskwghdfrpSYQSV---- 153
Cdd:COG1205 141 TPPEERRWIREhpdivltnpDML--HYGLLPHHTR------WARFFRNLR--YVVIDEAH-----------TYRGVfgsh 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 154 -----------IKKVFTLPQnftIVALTAT-----ATAEvqqdimgKLnIDRR-DEVKTSTK---RRNLIFkVNP----T 209
Cdd:COG1205 200 vanvlrrlrriCRHYGSDPQ---FILASATignpaEHAE-------RL-TGRPvTVVDEDGSprgERTFVL-WNPplvdD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 210 YQRQ-------KFVVDYVQKhkEQAGIIYCSTRKQVE----ELQEALDVINVSSAI--YHAGLTNKERETAQNEFVYDKV 276
Cdd:COG1205 268 GIRRsalaeaaRLLADLVRE--GLRTLVFTRSRRGAEllarYARRALREPDLADRVaaYRAGYLPEERREIERGLRSGEL 345
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1378690484 277 KVVIATNAFGMGIDKSNVRYVI--HYnmPGDLESYYQEAGRAGRDGLESECILLFSE 331
Cdd:COG1205 346 LGVVSTNALELGIDIGGLDAVVlaGY--PGTRASFWQQAGRAGRRGQDSLVVLVAGD 400
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
517-585 |
2.02e-13 |
|
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the HRDC domain cause human disease.
Pssm-ID: 128635 [Multi-domain] Cd Length: 81 Bit Score: 65.78 E-value: 2.02e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1378690484 517 VDRALYSELVEVRRKLSEKLDIAPVSIFSDYTLEEFAKRKPESKQEMISIDGVGSYKLKHYCPKFLEII 585
Cdd:smart00341 3 RQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVI 71
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
127-320 |
5.61e-12 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 67.93 E-value: 5.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 127 DIHLIAFDEAHCISKWGhdFRPSYQSVIKKvftLPQNFTIVALTATataeVQQDIMGKLNIDRRDEVKTSTKRRNLI--- 203
Cdd:PTZ00424 170 DLKLFILDEADEMLSRG--FKGQIYDVFKK---LPPDVQVALFSAT----MPNEILELTTKFMRDPKRILVKKDELTleg 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 204 ---FKVNPTYQRQKF--VVDYVQKHKEQAGIIYCSTRKQVEELQEALDVINVSSAIYHAGLTNKERETAQNEFVYDKVKV 278
Cdd:PTZ00424 241 irqFYVAVEKEEWKFdtLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRV 320
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1378690484 279 VIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDG 320
Cdd:PTZ00424 321 LITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFG 362
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
272-328 |
2.07e-10 |
|
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: 56.94 E-value: 2.07e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1378690484 272 VYDKVKVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDG-LESECILL 328
Cdd:cd18785 19 IASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILF 76
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
229-320 |
6.58e-10 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 61.71 E-value: 6.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 229 IIYCSTRKQVEELQEALDVINVSSAIYHAGLTNKERETAQNEFVYDKVKVVIATNAFGMGIDKSNVRYVIHYNMPGDLES 308
Cdd:PTZ00110 381 LIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIED 460
|
90
....*....|..
gi 1378690484 309 YYQEAGRAGRDG 320
Cdd:PTZ00110 461 YVHRIGRTGRAG 472
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
7-333 |
1.05e-09 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 61.08 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 7 HYFGYDNFRPGQKEIITKIMDHHNVLGVLPTGGGKSICY---------QVP----GLMLGGTTIVISP----LISLMKDQ 69
Cdd:PRK01297 103 HDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFlisiinqllQTPppkeRYMGEPRALIIAPtrelVVQIAKDA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 70 VDQLKAMGIKA-AFLNSSLTKKQQKEIEDDlmkgHIQFLYVAPERFdnqyfLSLLSRIDIHL-----IAFDEAHCISKWG 143
Cdd:PRK01297 183 AALTKYTGLNVmTFVGGMDFDKQLKQLEAR----FCDILVATPGRL-----LDFNQRGEVHLdmvevMVLDEADRMLDMG 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 144 hdFRPSYQSVIKKVFTLPQNFTIVaLTATATAEV----QQDIMGKLNIDRRDEVKTSTKRRNLIFKVNPTyQRQKFVVDY 219
Cdd:PRK01297 254 --FIPQVRQIIRQTPRKEERQTLL-FSATFTDDVmnlaKQWTTDPAIVEIEPENVASDTVEQHVYAVAGS-DKYKLLYNL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 220 VQKHKEQAGIIYCSTRKQVEELQEALDVINVSSAIYHAGLTNKERETAQNEFVYDKVKVVIATNAFGMGIDKSNVRYVIH 299
Cdd:PRK01297 330 VTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVIN 409
|
330 340 350
....*....|....*....|....*....|....
gi 1378690484 300 YNMPGDLESYYQEAGRAGRDGLESECILLFSERD 333
Cdd:PRK01297 410 FTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDD 443
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
332-394 |
9.44e-09 |
|
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ.
Pssm-ID: 465031 [Multi-domain] Cd Length: 66 Bit Score: 51.91 E-value: 9.44e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1378690484 332 RDKGLHEYFITVSQADEDYKDKMGEKLTKMIQY-TKTKKCLEATVVHYFEPNEKLEECGQCSSC 394
Cdd:pfam16124 2 QDVVRLRFLIEQSEADEERKEVELQKLQAMVAYcENTTDCRRKQLLRYFGEEFDSEPCGNCDNC 65
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
14-173 |
1.42e-08 |
|
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: 54.58 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 14 FRPGQKEIITKIMDH-HNVLGVLPTGGGKSICYQvpgLML-------GGTTIVISPLISL----MKDQVDQLKAMGIKAA 81
Cdd:cd17921 2 LNPIQREALRALYLSgDSVLVSAPTSSGKTLIAE---LAIlralatsGGKAVYIAPTRALvnqkEADLRERFGPLGKNVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 82 FLNSSLTkkqqkeiEDDLMKGHIQFLYVAPERFDNQ-YFLSLLSRIDIHLIAFDEAHCIskwGHDFR-PSYQSVIKKVFT 159
Cdd:cd17921 79 LLTGDPS-------VNKLLLAEADILVATPEKLDLLlRNGGERLIQDVRLVVVDEAHLI---GDGERgVVLELLLSRLLR 148
|
170
....*....|....
gi 1378690484 160 LPQNFTIVALTATA 173
Cdd:cd17921 149 INKNARFVGLSATL 162
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
227-336 |
3.47e-08 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 56.40 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 227 AGIIYCSTRKQVEELQEALDVINVSSAIYHAGLTNKERETAQNEFVYDKVKVVIATNAFGMGIDKSNVRYVIHYNMPGDL 306
Cdd:PRK11634 247 AAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDS 326
|
90 100 110
....*....|....*....|....*....|
gi 1378690484 307 ESYYQEAGRAGRDGLESECILLFSERDKGL 336
Cdd:PRK11634 327 ESYVHRIGRTGRAGRAGRALLFVENRERRL 356
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
14-181 |
8.69e-07 |
|
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: 49.63 E-value: 8.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 14 FRPGQKEIITKIMdHHNVLGVLPTGGGKSICYQVpgLMLG-------GTTIVISPLISLMKDQVDQ-LKAMGIKAAfLNS 85
Cdd:cd18033 3 LRDYQFTIVQKAL-FQNTLVALPTGLGKTFIAAV--VMLNyyrwfpkGKIVFMAPTKPLVSQQIEAcYKITGIPSS-QTA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 86 SLTKKQQKEIEDDLMKgHIQFLYVAPERFDNQYFLSLLSRIDIHLIAFDEAHCISKwghdfRPSYQSVIKKVFTLPQNFT 165
Cdd:cd18033 79 ELTGSVPPTKRAELWA-SKRVFFLTPQTLENDLKEGDCDPKSIVCLVIDEAHRATG-----NYAYCQVVRELMRYNSHFR 152
|
170
....*....|....*....
gi 1378690484 166 IVALTAT---ATAEVQQDI 181
Cdd:cd18033 153 ILALTATpgsKLEAVQQVI 171
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
13-172 |
1.03e-06 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 48.82 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 13 NFRPGQKEIITKIM-----DHHNVLGVLPTGGGKS-----ICYQVPGLMLGGTTIVISPLISLMKDQVDQLKAMGIKAAF 82
Cdd:pfam04851 3 ELRPYQIEAIENLLesiknGQKRGLIVMATGSGKTltaakLIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 83 LNSSLT--KKQQKEIEDDLMKGHIQFLYVAperFDNQYFLSLLSRIDihLIAFDEAHciskwgHDFRPSYQSVIKKVftl 160
Cdd:pfam04851 83 IGEIISgdKKDESVDDNKIVVTTIQSLYKA---LELASLELLPDFFD--VIIIDEAH------RSGASSYRNILEYF--- 148
|
170
....*....|..
gi 1378690484 161 pQNFTIVALTAT 172
Cdd:pfam04851 149 -KPAFLLGLTAT 159
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
229-318 |
2.87e-06 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 50.27 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 229 IIYCSTRKQVEELQEALDVinvSSAIYHAGLTNKERETAQNEFVYDKVKVVIATNAFG----------------MGIDKS 292
Cdd:COG1202 431 IIFTNSRRRCHEIARALGY---KAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAagvdfpasqvifdslaMGIEWL 507
|
90 100
....*....|....*....|....*.
gi 1378690484 293 NVRyvihynmpgdleSYYQEAGRAGR 318
Cdd:COG1202 508 SVQ------------EFHQMLGRAGR 521
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
229-318 |
6.78e-06 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases 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: 350183 [Multi-domain] Cd Length: 150 Bit Score: 46.10 E-value: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 229 IIYCSTRKQVEELQEAL------DVINVSSAIYHAGLTNKERETAQNEFVYDKVKVVIATNAFGMGIDKSNVRYVIHYNM 302
Cdd:cd18796 42 LVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGS 121
|
90
....*....|....*.
gi 1378690484 303 PGDLESYYQEAGRAGR 318
Cdd:cd18796 122 PKSVARLLQRLGRSGH 137
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
18-320 |
1.42e-05 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 47.96 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 18 QKEIITKIMDHHNVLGVLPTGGGKS-ICYQV--PGLMLGGTTIVISPLISLMKDQVDQLKAMgikaaflnSSLTKKQQKE 94
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKTlIAYSAiyETFLAGLKSIYIVPLRSLAMEKYEELSRL--------RSLGMRVKIS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 95 IED-----DLMKGHiQFLYVAPERFD-----NQYFLSllsriDIHLIAFDEAHCIskwGHDFR-PSYQSVIKKVFTLPQN 163
Cdd:PRK01172 99 IGDyddppDFIKRY-DVVILTSEKADslihhDPYIIN-----DVGLIVADEIHII---GDEDRgPTLETVLSSARYVNPD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 164 FTIVALTATAT--AEVQQDIMG------------KLNIDRRDEVKTSTKRR-----NLIFK------------VNPTYQR 212
Cdd:PRK01172 170 ARILALSATVSnaNELAQWLNAsliksnfrpvplKLGILYRKRLILDGYERsqvdiNSLIKetvndggqvlvfVSSRKNA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 213 QKFVVDYVQKHKEQAGIIYCSTRKQV--EELQEaldVINVSSAIYHAGLTNKERETAQNEFVYDKVKVVIATNAFGMGID 290
Cdd:PRK01172 250 EDYAEMLIQHFPEFNDFKVSSENNNVydDSLNE---MLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVN 326
|
330 340 350
....*....|....*....|....*....|....*....
gi 1378690484 291 KSnVRYVIHYNMP--GDLESYY-------QEAGRAGRDG 320
Cdd:PRK01172 327 LP-ARLVIVRDITryGNGGIRYlsnmeikQMIGRAGRPG 364
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
16-172 |
3.35e-05 |
|
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: 44.63 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 16 PGQKEIITK-IMDHHNVLGVLPTGGGKSICYQ---VPGLMLGGTTIVISPLISLMKDQVDQLKA---MGIKAAflnssLT 88
Cdd:cd18028 4 PPQAEAVRAgLLKGENLLISIPTASGKTLIAEmamVNTLLEGGKALYLVPLRALASEKYEEFKKleeIGLKVG-----IS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 89 KKQQKEIEDDLMKGHIqfLYVAPERFDnqyflSLL-SRI----DIHLIAFDEAHCISKWGHDfrPSYQSVIKKVFTLPQN 163
Cdd:cd18028 79 TGDYDEDDEWLGDYDI--IVATYEKFD-----SLLrHSPswlrDVGVVVVDEIHLISDEERG--PTLESIVARLRRLNPN 149
|
....*....
gi 1378690484 164 FTIVALTAT 172
Cdd:cd18028 150 TQIIGLSAT 158
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
252-356 |
4.56e-05 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 46.49 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 252 SAIYHAGLTNKERETAQNEFVYDKVKVVIATNAFGMG--------IDKSNVRYVIHYNM-PGDLESYYQEAGRAGRDGLE 322
Cdd:PRK02362 306 AAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGlnlparrvIIRDYRRYDGGAGMqPIPVLEYHQMAGRAGRPGLD 385
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1378690484 323 --SECILL---FSERDKgLHEYFItvsQAD-EDYKDKMGE 356
Cdd:PRK02362 386 pyGEAVLLaksYDELDE-LFERYI---WADpEDVRSKLAT 421
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
123-318 |
1.29e-04 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 44.80 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 123 LSRIDIhlIAFDEAHCISKWG--HDFRpsyqSVIKKVFTLPQNftivaLTATATaeVQQDIMGKLNIDRRDEVKTSTKRR 200
Cdd:PRK10590 147 LDQVEI--LVLDEADRMLDMGfiHDIR----RVLAKLPAKRQN-----LLFSAT--FSDDIKALAEKLLHNPLEIEVARR 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 201 NlifkvNPTYQRQKFVvDYVQKHKE-------------QAGIIYCSTRKQVEELQEALDVINVSSAIYHAGLTNKERETA 267
Cdd:PRK10590 214 N-----TASEQVTQHV-HFVDKKRKrellsqmigkgnwQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRA 287
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1378690484 268 QNEFVYDKVKVVIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGR 318
Cdd:PRK10590 288 LADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGR 338
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
18-75 |
1.50e-04 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs 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: 350681 [Multi-domain] Cd Length: 182 Bit Score: 42.96 E-value: 1.50e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1378690484 18 QKEIITKIMDHHNVLGVLPTGGGKSICYQVPGL--ML---GGTTIVISPLISLMKDQVDQLKA 75
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILeaLLrdpGSRALYLYPTKALAQDQLRSLRE 67
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
214-328 |
1.95e-04 |
|
C-terminal helicase domain of the 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. Dicer exists throughout eukaryotes, and a subset has 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 helicase domains 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: 350189 [Multi-domain] Cd Length: 142 Bit Score: 41.81 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 214 KFVVDYVQKHKEQAGIIYCSTRKQV-------EELQEALDVINVSSAI--------YHAGLTNKERETAQNEFVYDKVKV 278
Cdd:cd18802 14 EILREYFPKTPDFRGIIFVERRATAvvlsrllKEHPSTLAFIRCGFLIgrgnssqrKRSLMTQRKQKETLDKFRDGELNL 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1378690484 279 VIATNAFGMGIDKSNVRYVIHYNMPGDLESYYQEAGRAGRDGleSECILL 328
Cdd:cd18802 94 LIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN--SKYILM 141
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
15-171 |
3.27e-04 |
|
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: 42.25 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 15 RPGQKEIITKIMdHHNVLGVLPTGGGKsicyqvpglmlggTTIVISpLISLMKDQVDQLKAMGIKAAFLNSS--LTKKQQ 92
Cdd:cd18034 4 RSYQLELFEAAL-KRNTIVVLPTGSGK-------------TLIAVM-LIKEMGELNRKEKNPKKRAVFLVPTvpLVAQQA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 93 KEI-------------EDDLMKGHIQFLYVAPERFD-----NQYFLSLLSRI-----DIHLIAFDEAHCISKwGHDFRps 149
Cdd:cd18034 69 EAIrshtdlkvgeysgEMGVDKWTKERWKEELEKYDvlvmtAQILLDALRHGflslsDINLLIFDECHHATG-DHPYA-- 145
|
170 180
....*....|....*....|....*.
gi 1378690484 150 yqsVIKKVFTLPQNFT----IVALTA 171
Cdd:cd18034 146 ---RIMKEFYHLEGRTsrprILGLTA 168
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
214-320 |
1.45e-03 |
|
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: 39.00 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 214 KFVVDYVQKHKEQAG--IIYCSTRKQVEELQEALDVINVSSAIYHAGLTNKERETAQNEF--VYDKVKVVIATNAFGMGI 289
Cdd:cd18793 14 EALLELLEELREPGEkvLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFneDPDIRVFLLSTKAGGVGL 93
|
90 100 110
....*....|....*....|....*....|....*
gi 1378690484 290 DKSNVRYVIHY----NmPGDLEsyyQEAGRAGRDG 320
Cdd:cd18793 94 NLTAANRVILYdpwwN-PAVEE---QAIDRAHRIG 124
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
14-172 |
3.24e-03 |
|
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: 39.34 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 14 FRPGQKEIITKIMDHHNVLGVLPTGGGKS-----IC----YQVPGLMlGGTTIVISPLISLMKDQVDQ---------LKA 75
Cdd:cd17927 3 PRNYQLELAQPALKGKNTIICLPTGSGKTfvavlICehhlKKFPAGR-KGKVVFLANKVPLVEQQKEVfrkhferpgYKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 76 MGIKAAflnSSLTKKQQKEIEDDlmkghiQFLYVAPERFDNQyFLS--LLSRIDIHLIAFDEAHCISKwGHDFRP---SY 150
Cdd:cd17927 82 TGLSGD---TSENVSVEQIVESS------DVIIVTPQILVND-LKSgtIVSLSDFSLLVFDECHNTTK-NHPYNEimfRY 150
|
170 180
....*....|....*....|..
gi 1378690484 151 QSviKKVFTLPQNFTIVALTAT 172
Cdd:cd17927 151 LD--QKLGSSGPLPQILGLTAS 170
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
236-338 |
4.33e-03 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF 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: 350197 [Multi-domain] Cd Length: 151 Bit Score: 38.09 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378690484 236 KQVEELqealdVINVSSAIYHAGLTNKERETAQNEFVYDKVKVVIATNAFGMGIDKSNVRYVI--HYNMPGdLESYYQEA 313
Cdd:cd18810 43 TQLRQL-----VPEARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieRADKFG-LAQLYQLR 116
|
90 100
....*....|....*....|....*
gi 1378690484 314 GRAGRDGLESECILLFsERDKGLHE 338
Cdd:cd18810 117 GRVGRSKERAYAYFLY-PDQKKLTE 140
|
|
| |
