|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
21-491 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 735.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 21 MDRAHSVLRSVWGYDSFRPLQADAVQDVIQGRDSLVVLPTGGGKSLCYQVPALVRDGMSVVVSPLISLMKDQVDALTSNG 100
Cdd:COG0514 2 RDDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 101 VSAALVNSTQSVEQKRETAERLRRGEIKILYLAPERLLTPKTLDFLRSLPISFFAIDEAHCVSNWGHDFRPEYRGLRILK 180
Cdd:COG0514 82 IRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGELR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 181 EQFPSASVHAFTATASEQVRDDIAEQLQLNQPNILVGDFDRPNLTYRMLR--ADGKLNQIQQCIAQHPGESGVVYCITRK 258
Cdd:COG0514 162 ERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPkpPDDKLAQLLDFLKEHPGGSGIVYCLSRK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 259 EVEQTAAALESMGVRTLPYHAGLPDDVRQANQEAFIQEKVDVIVATVAFGMGIDKSNVRFVIHAGMPKSIEHYQQESGRA 338
Cdd:COG0514 242 KVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 339 GRDGLAAECILLHSGGDLMSWKRILENG--DRSNFQSAMASVESMAALCNGVQCRHASLVEYFGQEYdSDNCNACDVCLG 416
Cdd:COG0514 322 GRDGLPAEALLLYGPEDVAIQRFFIEQSppDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFGEEL-AEPCGNCDNCLG 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1818934875 417 ELDVVDDPItLAQKILSCVVRLKERYGAGHTVKVLTGSRDQKVIQAGHDQLSTYNLLSSEGATAVRTWIEQLISQ 491
Cdd:COG0514 401 PPETFDGTE-AAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLLAQ 474
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
24-613 |
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: 684.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 24 AHSVLRSVWGYDSFRPLQADAVQDVIQGRDSLVVLPTGGGKSLCYQVPALVRDGMSVVVSPLISLMKDQVDALTSNGVSA 103
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 104 ALVNSTQSVEQKRETAERLRRGEIKILYLAPERLLTPKTLDFLRSLPISFFAIDEAHCVSNWGHDFRPEYRGLRILKEQF 183
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 184 PSASVHAFTATASEQVRDDIAEQLQLNQPNILVGDFDRPNLTYRMLRADGKLNQIQQCIAQHPGESGVVYCITRKEVEQT 263
Cdd:TIGR01389 161 PQVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 264 AAALESMGVRTLPYHAGLPDDVRQANQEAFIQEKVDVIVATVAFGMGIDKSNVRFVIHAGMPKSIEHYQQESGRAGRDGL 343
Cdd:TIGR01389 241 AERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 344 AAECILLHSGGDLMSWKRILENGDRSNF--QSAMASVESMAALCNGVQCRHASLVEYFGQEYdSDNCNACDVCLGELDVV 421
Cdd:TIGR01389 321 PAEAILLYSPADIALLKRRIEQSEADDDykQIEREKLRAMIAYCETQTCRRAYILRYFGENE-VEPCGNCDNCLDPPKSY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 422 DdpIT-LAQKILSCVVRLKERYGAGHTVKVLTGSRDQKVIQAGHDQLSTYNLLSSEGATAVRTWIEQLISQNHLIRTGE- 499
Cdd:TIGR01389 400 D--ATvEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEi 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 500 FQSLRLTESGRALLKREGEVTLTKVSAKSSSRRPAANESWEGVDRKLFDHLRSLRSEMASERGVPAYVIFGDAVLRELAR 579
Cdd:TIGR01389 478 YIGLQLTEAARKVLKNEVEVLLRPFKVVAKEKTRVQKNLSVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAE 557
|
570 580 590
....*....|....*....|....*....|....
gi 1818934875 580 VRPTSIEKLTNIRGIGDRKREEFGQLFLDSIDQY 613
Cdd:TIGR01389 558 KRPATLNALLKIKGVGQNKLDRYGEAFLEVIREY 591
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
24-610 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 594.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 24 AHSVLRSVWGYDSFRPLQADAVQDVIQGRDSLVVLPTGGGKSLCYQVPALVRDGMSVVVSPLISLMKDQVDALTSNGVSA 103
Cdd:PRK11057 13 AKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 104 ALVNSTQSVEQKRETAERLRRGEIKILYLAPERLLTPKTLDFLRSLPISFFAIDEAHCVSNWGHDFRPEYRGLRILKEQF 183
Cdd:PRK11057 93 ACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQRF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 184 PSASVHAFTATASEQVRDDIAEQLQLNQPNILVGDFDRPNLTYRMLRADGKLNQIQQCIAQHPGESGVVYCITRKEVEQT 263
Cdd:PRK11057 173 PTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVEDT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 264 AAALESMGVRTLPYHAGLPDDVRQANQEAFIQEKVDVIVATVAFGMGIDKSNVRFVIHAGMPKSIEHYQQESGRAGRDGL 343
Cdd:PRK11057 253 AARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 344 AAECILLHSGGDlMSW-KRILENGDrsnfQSAMASVES-----MAALCNGVQCRHASLVEYFGqEYDSDNCNACDVCLge 417
Cdd:PRK11057 333 PAEAMLFYDPAD-MAWlRRCLEEKP----AGQQQDIERhklnaMGAFAEAQTCRRLVLLNYFG-EGRQEPCGNCDICL-- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 418 ldvvdDP------ITLAQKILSCVVRLKERYGAGHTVKVLTGSRDQKVIQAGHDQLSTYNL---LSSEGATAVrtwIEQL 488
Cdd:PRK11057 405 -----DPpkqydgLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIgrdKSHEHWVSV---IRQL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 489 I-----SQNhlirTGEFQSLRLTESGRALLKreGEVTLTKVSAKSSSRRPAANESWEG--VDRKLFDHLRSLRSEMASER 561
Cdd:PRK11057 477 IhlglvTQN----IAQHSALQLTEAARPVLR--GEVSLQLAVPRIVALKPRAMQKSFGgnYDRKLFAKLRKLRKSIADEE 550
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1818934875 562 GVPAYVIFGDAVLRELARVRPTSIEKLTNIRGIGDRKREEFGQLFLDSI 610
Cdd:PRK11057 551 NIPPYVVFNDATLIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMALI 599
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
26-470 |
6.71e-166 |
|
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: 486.58 E-value: 6.71e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 26 SVLRSVWGYDSFRPLQADAVQDVIQGRDSLVVLPTGGGKSLCYQVPALVRDGMSVVVSPLISLMKDQVDALTSNGVSAAL 105
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 106 VNSTQSVEQKRETAERLRRGEIKILYLAPERLLtpKTLDFLRSLP----ISFFAIDEAHCVSNWGHDFRPEYRGLRILKE 181
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKIS--ASNRLLQTLEerkgITLIAVDEAHCISQWGHDFRPDYKALGSLKQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 182 QFPSASVHAFTATASEQVRDDIAEQLQLNQPNILVGDFDRPNLTYRMLRADGK-LNQIQQCI-AQHPGESGVVYCITRKE 259
Cdd:TIGR00614 159 KFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTPKiLEDLLRFIrKEFEGKSGIIYCPSRKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 260 VEQTAAALESMGVRTLPYHAGLPDDVRQANQEAFIQEKVDVIVATVAFGMGIDKSNVRFVIHAGMPKSIEHYQQESGRAG 339
Cdd:TIGR00614 239 VEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 340 RDGLAAECILLHSGGDLMSWKRILENGDRSNFQSAMASVESMAALC-NGVQCRHASLVEYFGQ---------EYDSDNCN 409
Cdd:TIGR00614 319 RDGLPSECHLFYAPADMNRLRRLLMEEPDGNFRTYKLKLYEMMEYClNSSTCRRLILLSYFGEkgfnksfciMGTEKCCD 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1818934875 410 ACDVCLGEL-----DVVDDPITLAQKILSCVVRLKERYGAGHTVKVLTGSRDQKVIQAGHDQLSTY 470
Cdd:TIGR00614 399 NCCKRLDYKtkdvtDKVYDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLY 464
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
29-644 |
1.84e-110 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 362.68 E-value: 1.84e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 29 RSVWGYDSFRPLQADAVQDVIQGRDSLVVLPTGGGKSLCYQVPALVRDGMSVVVSPLISLMKDQVDALTSNGVSAALVNS 108
Cdd:PLN03137 453 KKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSA 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 109 TQSVEQKRETAERL--RRGEIKILYLAPERLLTPKTLdfLRSLPI-------SFFAIDEAHCVSNWGHDFRPEYRGLRIL 179
Cdd:PLN03137 533 GMEWAEQLEILQELssEYSKYKLLYVTPEKVAKSDSL--LRHLENlnsrgllARFVIDEAHCVSQWGHDFRPDYQGLGIL 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 180 KEQFPSASVHAFTATASEQVRDDIAEQLQLNQPNILVGDFDRPNLTYRMLRADGK-LNQIQQCIAQ-HPGESGVVYCITR 257
Cdd:PLN03137 611 KQKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKKcLEDIDKFIKEnHFDECGIIYCLSR 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 258 KEVEQTAAALESMGVRTLPYHAGLpddvrQANQEAFIQ-----EKVDVIVATVAFGMGIDKSNVRFVIHAGMPKSIEHYQ 332
Cdd:PLN03137 691 MDCEKVAERLQEFGHKAAFYHGSM-----DPAQRAFVQkqwskDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYH 765
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 333 QESGRAGRDGLAAECILLHSGGDLMSWKRILENG--DRSNFQSAMASVES--------------MAALC-NGVQCRHASL 395
Cdd:PLN03137 766 QECGRAGRDGQRSSCVLYYSYSDYIRVKHMISQGgvEQSPMAMGYNRMASsgriletntenllrMVSYCeNEVDCRRFLQ 845
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 396 VEYFGQEYDSDNC-NACDVCLGELDVVDDPITLAQKILSCVVRL-KERYGAGHTVKVLTGSRDQKVIQAGHDQLSTY--- 470
Cdd:PLN03137 846 LVHFGEKFDSTNCkKTCDNCSSSKSLIDKDVTEIARQLVELVKLtGERFSSAHILEVYRGSLNQYVKKHRHETLSLHgag 925
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 471 -NLLSSEGATAVRTWIEQLI------------SQNHLIRTGEFQSLRLTESGRALLKR-----------EGEVTLTKVSA 526
Cdd:PLN03137 926 kHLSKGEASRILHYLVTEDIlaedvkksdlygSVSSLLKVNESKAYKLFSGGQTIIMRfpssvkaskpsKFEATPAKGPL 1005
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 527 KSS--SRRPAANESWEGVD----RKLFDHLRSLRSEMASE--RGVPAYVIFGDAVLRELARVRPTSIEKLTNIRGIGDRK 598
Cdd:PLN03137 1006 TSGkqSTLPMATPAQPPVDlnlsAILYTALRKLRTALVKEagDGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAK 1085
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1818934875 599 REEFGQLFLDSIDQYCEE-NPLDR-DQTANTTSATISKPR-ANATPNAA 644
Cdd:PLN03137 1086 VSKYGDRLLETIESTINEyYKTDKnSSSSNDSPDSGKRRRdENINPNVA 1134
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
25-220 |
3.98e-104 |
|
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: 317.17 E-value: 3.98e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 25 HSVLRSVWGYDSFRPLQADAVQDVIQGRDSLVVLPTGGGKSLCYQVPALVRDGMSVVVSPLISLMKDQVDALTSNGVSAA 104
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 105 LVNSTQSVEQKRETAERLRRGEIKILYLAPERLLTPKTLDFLRSLP----ISFFAIDEAHCVSNWGHDFRPEYRGLRILK 180
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1818934875 181 EQFPSASVHAFTATASEQVRDDIAEQLQLNQPNILVGDFD 220
Cdd:cd17920 161 RALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
25-220 |
2.15e-74 |
|
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: 239.47 E-value: 2.15e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 25 HSVLRSVWGYDSFRPLQADAVQDVIQGRDSLVVLPTGGGKSLCYQVPALV----RDGMSVVVSPLISLMKDQVDALTSnG 100
Cdd:cd18018 1 LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALPR-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 101 VSAALVNSTQSVEQKRETAERLRRGEIKILYLAPERLLTPKTLDFLRSL-PISFFAIDEAHCVSNWGHDFRPEYRGL-RI 178
Cdd:cd18018 80 IKAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTpPISLLVVDEAHCISEWSHNFRPDYLRLcRV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1818934875 179 LKEQFPSASVHAFTATASEQVRDDIAEQLQLNQPNILVGDFD 220
Cdd:cd18018 160 LRELLGAPPVLALTATATKRVVEDIASHLGIPESGVVRGPLY 201
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
22-220 |
5.88e-64 |
|
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: 211.84 E-value: 5.88e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 22 DRAHSVLRSVWGYDSFRPLQADAVQDVIQGRDSLVVLPTGGGKSLCYQVPALVRDGMSVVVSPLISLMKDQVDALTSNGV 101
Cdd:cd18015 4 GKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 102 SAALVNSTQSVEQKRETAERLRRG--EIKILYLAPERLLTPKTldFLRSLP-------ISFFAIDEAHCVSNWGHDFRPE 172
Cdd:cd18015 84 SATMLNASSSKEHVKWVHAALTDKnsELKLLYVTPEKIAKSKR--FMSKLEkaynagrLARIAIDEVHCCSQWGHDFRPD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1818934875 173 YRGLRILKEQFPSASVHAFTATASEQVRDDIAEQLQLNQPNILVGDFD 220
Cdd:cd18015 162 YKKLGILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
221-350 |
2.61e-56 |
|
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: 188.57 E-value: 2.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 221 RPNLTYRMLRADGKLNQIQQCIAQ---HPGESGVVYCITRKEVEQTAAALESMGVRTLPYHAGLPDDVRQANQEAFIQEK 297
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLKRIkveHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1818934875 298 VDVIVATVAFGMGIDKSNVRFVIHAGMPKSIEHYQQESGRAGRDGLAAECILL 350
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
26-220 |
3.90e-56 |
|
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: 190.37 E-value: 3.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 26 SVLRSVWGYDSFRPLQADAVQDVIQ-GRDSLVVLPTGGGKSLCYQVPALVRDGMSVVVSPLISLMKDQVDALTSNGVSAA 104
Cdd:cd18017 2 NALNEYFGHSSFRPVQWKVIRSVLEeRRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPAC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 105 LVNStqsvEQKRETAERLRRGEIKILYLAPERLLtpKTLDFLRSLP--ISFFAIDEAHCVSNWGHDFRPEYRGLRILKEQ 182
Cdd:cd18017 82 FLGS----AQSQNVLDDIKMGKIRVIYVTPEFVS--KGLELLQQLRngITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNR 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 1818934875 183 FPSASVHAFTATASEQVRDDIAEQLQLNQPNILVGDFD 220
Cdd:cd18017 156 LPNVPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
25-212 |
4.63e-56 |
|
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: 190.38 E-value: 4.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 25 HSVLRSVWGYDSFR-PLQADAVQDVIQGR-DSLVVLPTGGGKSLCYQVPALVRDGMSVVVSPLISLMKDQVDALTSNGVS 102
Cdd:cd18014 1 RSTLKKVFGHSDFKsPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 103 AALVNSTQSVEQKRETAERLRRG--EIKILYLAPERLLTPKTLDFLRSL----PISFFAIDEAHCVSNWGHDFRPEYRGL 176
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADLESEkpQTKFLYITPEMAATSSFQPLLSSLvsrnLLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1818934875 177 RILKEQFPSASVHAFTATASEQVRDDIAEQLQLNQP 212
Cdd:cd18014 161 GALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKP 196
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
27-220 |
6.43e-52 |
|
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: 179.25 E-value: 6.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 27 VLRSVWGYDSFRPLQADAVQDVIQGRDSLVVLPTGGGKSLCYQVPALVRDGMSVVVSPLISLMKDQVDALTSNGVSAALV 106
Cdd:cd18016 8 IFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 107 NSTQSVEQKRETAERLRRGE--IKILYLAPE------RLLTpkTLDFL--RSLpISFFAIDEAHCVSNWGHDFRPEYRGL 176
Cdd:cd18016 88 TGDKTDAEATKIYLQLSKKDpiIKLLYVTPEkisasnRLIS--TLENLyeRKL-LARFVIDEAHCVSQWGHDFRPDYKRL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1818934875 177 RILKEQFPSASVHAFTATASEQVRDDIAEQLQLNQPNILVGDFD 220
Cdd:cd18016 165 NMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| DpdF |
NF041063 |
protein DpdF; |
27-356 |
9.42e-51 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 190.51 E-value: 9.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 27 VLRSVWGYDSFR-PLQADAVQDVI---QGRDSLVVLPTGGGKSLCYQVPALV---RDGMSVVVSPLISLMKDQVDALTS- 98
Cdd:NF041063 130 FLAEALGFTHYRsPGQREAVRAALlapPGSTLIVNLPTGSGKSLVAQAPALLasrQGGLTLVVVPTVALAIDQERRAREl 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 99 -NGVSAALVNST-----QSVEQKRETAERLRRGEIKILYLAPERLLTPktldfLRSL--------PISFFAIDEAHCVSN 164
Cdd:NF041063 210 lRRAGPDLGGPLawhggLSAEERAAIRQRIRDGTQRILFTSPESLTGS-----LRPAlfdaaeagLLRYLVVDEAHLVDQ 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 165 WGHDFRPEY-------RGLRILkeqfpSASVHAF-----TATASEQVRDDIAEQLQLNQPNILV-GDFDRPNLTYRMLRA 231
Cdd:NF041063 285 WGDGFRPEFqllaglrRSLLRL-----APSGRPFrtlllSATLTESTLDTLETLFGPPGPFIVVsAVQLRPEPAYWVAKC 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 232 DG---KLNQIQQCIAQHPGESgVVYCITRKEVEQTAAALESMG---VRTLpyHAGLPDDVRQANQEAFIQEKVDVIVATV 305
Cdd:NF041063 360 DSeeeRRERVLEALRHLPRPL-ILYVTKVEDAEAWLQRLRAAGfrrVALF--HGDTPDAERERLIEQWRENELDIVVATS 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1818934875 306 AFGMGIDKSNVRFVIHAGMPKSIEHYQQESGRAGRDGLAAECILLHSGGDL 356
Cdd:NF041063 437 AFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDL 487
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
423-524 |
1.17e-30 |
|
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: 116.10 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 423 DPITLAQKILSCVVRLKERYGAGHTVKVLTGSRDQKVIQAGHDQLSTYNLLSSEGATAVRTWIEQLISQNHLIRTGEF-Q 501
Cdd:pfam09382 6 DVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVDIEFyS 85
|
90 100
....*....|....*....|...
gi 1818934875 502 SLRLTESGRALLKREGEVTLTKV 524
Cdd:pfam09382 86 VLKLTPKAREVLKGEEKVMLRVP 108
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
428-513 |
1.19e-26 |
|
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: 104.09 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 428 AQKILSCVVRLKERYGAGHTVKVLTGSRDQKVIQAGHDQLSTYNLLSSEGATAVRTWIEQLISQNHLIRTGEFQS-LRLT 506
Cdd:smart00956 6 AQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYPyLKLT 85
|
....*..
gi 1818934875 507 ESGRALL 513
Cdd:smart00956 86 EKARPVL 92
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
38-201 |
5.03e-26 |
|
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: 105.02 E-value: 5.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 38 RPLQADAVQDVIQGRDSLVVLPTGGGKSLCYQVPALVR------DGMSVVVSPLISLMKDQVDALTSNGVSAAL-VNSTQ 110
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAldkldnGPQALVLAPTRELAEQIYEELKKLGKGLGLkVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 111 SVEQKRETAERLRRgeIKILYLAPERLLTPKTLD-FLRSLpiSFFAIDEAHCVSNWGhdFRPEYRG-LRILKEQFPSAsv 188
Cdd:pfam00270 81 GGDSRKEQLEKLKG--PDILVGTPGRLLDLLQERkLLKNL--KLLVLDEAHRLLDMG--FGPDLEEiLRRLPKKRQIL-- 152
|
170
....*....|...
gi 1818934875 189 hAFTATASEQVRD 201
Cdd:pfam00270 153 -LLSATLPRNLED 164
|
|
| HTH_40 |
pfam14493 |
Helix-turn-helix domain; This presumed domain is found at the C-terminus of a large number of ... |
645-731 |
4.74e-24 |
|
Helix-turn-helix domain; This presumed domain is found at the C-terminus of a large number of helicase proteins.
Pssm-ID: 464189 Cd Length: 89 Bit Score: 96.42 E-value: 4.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 645 TVQAS-QLFREGCSVEEVASKMGRAESTVNKYLSDYIQAEKITDPSQWVSNEEAEAIRAALMAVEDERLRPVFEALGEEV 723
Cdd:pfam14493 1 SAEITlELYKEGLSIEEIAEERGLKESTIEGHLAELIEAGEPVDIERLVSEEEQKEILDAIEKLGSESLKPIKEALPEEI 80
|
....*...
gi 1818934875 724 SYEKIRIV 731
Cdd:pfam14493 81 SYFEIRLV 88
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
33-227 |
7.11e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 99.87 E-value: 7.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 33 GYDSFRPLQADAVQDVIQG-RDSLVVLPTGGGKSLCYQVPAL-----VRDGMSVVVSPLISLMKDQVDALTSNGVSAALV 106
Cdd:smart00487 5 GFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALealkrGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 107 NSTQSV-EQKRETAERLRRGEIKILYLAPERLLTPKTLDFLRSLPISFFAIDEAHCVSNWGhdFRPEYRglRILKEQFPS 185
Cdd:smart00487 85 VVGLYGgDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLE--KLLKLLPKN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1818934875 186 ASVHAFTATASEQVRDDIAEQLQLNQpNILVGDFDRPNLTYR 227
Cdd:smart00487 161 VQLLLLSATPPEEIENLLELFLNDPV-FIDVGFTPLEPIEQF 201
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
261-342 |
1.86e-21 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 88.81 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 261 EQTAAALESMGVRTLPYHAGLPDDVRQANQEAFIQEKVDVIVATVAFGMGIDKSNVRFVIHAGMPKSIEHYQQESGRAGR 340
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1818934875 341 DG 342
Cdd:smart00490 81 AG 82
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
233-342 |
2.66e-21 |
|
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: 89.58 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 233 GKLNQIQQCIAQHPGESGVVYCITRKEVEqTAAALESMGVRTLPYHAGLPDDVRQANQEAFIQEKVDVIVATVAFGMGID 312
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 1818934875 313 KSNVRFVIHAGMPKSIEHYQQESGRAGRDG 342
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
33-364 |
8.21e-21 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 95.60 E-value: 8.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 33 GYDSFRPLQADAVQDVIQGRDSLVVLPTGGGKSLCYQVPAL----------VRdgmSVVVSP---LISLMKDQVDALTSN 99
Cdd:COG0513 21 GYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLqrldpsrpraPQ---ALILAPtreLALQVAEELRKLAKY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 100 -GVSAALVNSTQSVE-QKRetaeRLRRGeIKILYLAPERLL---TPKTLDFLRslpISFFAIDEAhcvsnwghD------ 168
Cdd:COG0513 98 lGLRVATVYGGVSIGrQIR----ALKRG-VDIVVATPGRLLdliERGALDLSG---VETLVLDEA--------Drmldmg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 169 FRPEYRglRILKeQFPSASVHA-FTATASEQVRDdIAEQLqLNQP---NILVGDFDRPNLTYRMLRADG--KLNQIQQCI 242
Cdd:COG0513 162 FIEDIE--RILK-LLPKERQTLlFSATMPPEIRK-LAKRY-LKNPvriEVAPENATAETIEQRYYLVDKrdKLELLRRLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 243 AQHPGESGVVYCITRKEVEQTAAALESMGVRTLPYHAGLPDDVRQANQEAFIQEKVDVIVAT-VAfGMGIDKSNVRFVIH 321
Cdd:COG0513 237 RDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATdVA-ARGIDIDDVSHVIN 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1818934875 322 AGMPKSIEHYQQESG---RAGRDGLAaecILLHSGGDLMSWKRILE 364
Cdd:COG0513 316 YDLPEDPEDYVHRIGrtgRAGAEGTA---ISLVTPDERRLLRAIEK 358
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
543-610 |
2.87e-20 |
|
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: 84.89 E-value: 2.87e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1818934875 543 DRKLFDHLRSLRSEMASERGVPAYVIFGDAVLRELARVRPTSIEKLTNIRGIGDRKREEFGQLFLDSI 610
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
41-342 |
3.17e-18 |
|
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: 89.51 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 41 QADAVQDVIQGRDSLVVLPTGGGKSLCYQVPAL-----VRDGMSVVVSPLISLMKDQVDALTS------NGVSAALVNST 109
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLealleDPGATALYLYPTKALARDQLRRLRElaealgLGVRVATYDGD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 110 QSVEQKRETaerLRRGEIkilylaperLLT-------------PKTLDFLRSLpiSFFAIDEAHcvsnwghdfrpEYRG- 175
Cdd:COG1205 141 TPPEERRWI---REHPDI---------VLTnpdmlhygllphhTRWARFFRNL--RYVVIDEAH-----------TYRGv 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 176 ------------LRILKE-----QFPSASvhaftATASEQVrdDIAEQLqLNQPNILVGD-----------FDRPNLTYR 227
Cdd:COG1205 196 fgshvanvlrrlRRICRHygsdpQFILAS-----ATIGNPA--EHAERL-TGRPVTVVDEdgsprgertfvLWNPPLVDD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 228 MLRADGkLNQIQQCIAQHpGESGV---VYCITRKEVEQTAAALESM------GVRTLPYHAGLPDDVRQANQEAFIQEKV 298
Cdd:COG1205 268 GIRRSA-LAEAARLLADL-VREGLrtlVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEERREIERGLRSGEL 345
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1818934875 299 DVIVATVAFGMGIDKSNVRFVIHAGMPKSIEHYQQESGRAGRDG 342
Cdd:COG1205 346 LGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRG 389
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
234-344 |
3.10e-16 |
|
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: 75.62 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 234 KLNQIQQCIAQHPGESGVVYCITRKEVEQTAAALESMGVRTLPYHAGLPDDVRQANQEAFIQEKVDVIVAT-VAfGMGID 312
Cdd:cd18787 14 KLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATdVA-ARGLD 92
|
90 100 110
....*....|....*....|....*....|....*
gi 1818934875 313 KSNVRFVIHAGMPKSIEHYQQESGR---AGRDGLA 344
Cdd:cd18787 93 IPGVDHVINYDLPRDAEDYVHRIGRtgrAGRKGTA 127
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
38-340 |
1.46e-13 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 73.91 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 38 RPLQADAVQDVIQGRDS-----LVVLPTGGGKSL----CYQvpALVRDGMSVVVSPLISLMKDQVDALtsngvsaalvns 108
Cdd:COG1061 82 RPYQQEALEALLAALERgggrgLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEEL------------ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 109 tQSVEQKRETAERLRRGEIKILYLAPERLLTPKTLDFLRSLpISFFAIDEAHcvsnwgHDFRPEYRglRILkEQFPSASV 188
Cdd:COG1061 148 -RRFLGDPLAGGGKKDSDAPITVATYQSLARRAHLDELGDR-FGLVIIDEAH------HAGAPSYR--RIL-EAFPAAYR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 189 HAFTATAseqVRDDIAEQLQLNQPNILVG----------------------DFDRPNLTYRMLR----------ADGKLN 236
Cdd:COG1061 217 LGLTATP---FRSDGREILLFLFDGIVYEyslkeaiedgylappeyygirvDLTDERAEYDALSerlrealaadAERKDK 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 237 QIQQCIAQHPGES-GVVYCITRKEVEQTAAALESMGVRTLPYHAGLPDDVRQANQEAFIQEKVDVIVATVAFGMGIDKSN 315
Cdd:COG1061 294 ILRELLREHPDDRkTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPR 373
|
330 340
....*....|....*....|....*
gi 1818934875 316 VRFVIHAGMPKSIEHYQQesgRAGR 340
Cdd:COG1061 374 LDVAILLRPTGSPREFIQ---RLGR 395
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
33-342 |
1.89e-13 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 73.67 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 33 GYDSFRPLQADAVQDVIQGRDSLVVLPTGGGKSLCYQVP-----ALVRDG--------MSVVVSP---LISLMKDQVDAL 96
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPiisrcCTIRSGhpseqrnpLAMVLTPtreLCVQVEDQAKVL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 97 tSNGV--SAALVNSTQSVEQKretAERLRRGeIKILYLAPERLLTPKTLDFLRSLPISFFAIDEAHCVSNWGhdFRPEYr 174
Cdd:PLN00206 220 -GKGLpfKTALVVGGDAMPQQ---LYRIQQG-VELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERG--FRDQV- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 175 gLRILKeQFPSASVHAFTATASEQVrDDIAEQLQLNQPNILVGDFDRPNLTYRML-------RADGKLNQIQQCiAQHPG 247
Cdd:PLN00206 292 -MQIFQ-ALSQPQVLLFSATVSPEV-EKFASSLAKDIILISIGNPNRPNKAVKQLaiwvetkQKKQKLFDILKS-KQHFK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 248 ESGVVYCITRKEVEQTAAALE-SMGVRTLPYHAGLPDDVRQANQEAFIQEKVDVIVATVAFGMGIDKSNVRFVIHAGMPK 326
Cdd:PLN00206 368 PPAVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPN 447
|
330
....*....|....*.
gi 1818934875 327 SIEHYQQESGRAGRDG 342
Cdd:PLN00206 448 TIKEYIHQIGRASRMG 463
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
354-415 |
1.97e-13 |
|
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: 65.39 E-value: 1.97e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1818934875 354 GDLMSWKRILENG--DRSNFQSAMASVESMAALC-NGVQCRHASLVEYFGQEYDSDNCNACDVCL 415
Cdd:pfam16124 2 QDVVRLRFLIEQSeaDEERKEVELQKLQAMVAYCeNTTDCRRKQLLRYFGEEFDSEPCGNCDNCL 66
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
252-350 |
2.67e-13 |
|
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: 67.67 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 252 VYCITRKEVEQTAAALESMGVRTLP-------YHAGLPDDVRQANQEAFIQEKVDVIVATVAFGMGIDKSNVRFVIHAGM 324
Cdd:cd18797 40 VFCRSRKLAELLLRYLKARLVEEGPlaskvasYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAGY 119
|
90 100
....*....|....*....|....*.
gi 1818934875 325 PKSIEHYQQESGRAGRDGLAAECILL 350
Cdd:cd18797 120 PGSLASLWQQAGRAGRRGKDSLVILV 145
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
55-194 |
2.87e-13 |
|
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: 67.81 E-value: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 55 LVVLPTGGGKSLCYQVPALVRD----GMSVVVSPLISLMKDQ---VDALTSNGVSAALVNSTQSVEQKRetaeRLRRGEI 127
Cdd:cd00046 5 LITAPTGSGKTLAALLAALLLLlkkgKKVLVLVPTKALALQTaerLRELFGPGIRVAVLVGGSSAEERE----KNKLGDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1818934875 128 KILYLAPERLLTPKT-LDFLRSLPISFFAIDEAHCVSNWGHDFRPEYrgLRILKEQFPSASVHAFTAT 194
Cdd:cd00046 81 DIIIATPDMLLNLLLrEDRLFLKDLKLIIVDEAHALLIDSRGALILD--LAVRKAGLKNAQVILLSAT 146
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
33-343 |
1.73e-12 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 70.31 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 33 GYDSFRPLQADAVQDVIQGRDSLVV-LPTGGGKSLCYQVP---ALVRDGMSVVVSPLISL----MKDQVDALTSNGVSAA 104
Cdd:COG1204 19 GIEELYPPQAEALEAGLLEGKNLVVsAPTASGKTLIAELAilkALLNGGKALYIVPLRALasekYREFKRDFEELGIKVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 105 LvnSTQSVEqkrETAERLRRGEIKIlyLAPERL--LTPKTLDFLRSlpISFFAIDEAHCVSNwghdfrpEYRGLRI---- 178
Cdd:COG1204 99 V--STGDYD---SDDEWLGRYDILV--ATPEKLdsLLRNGPSWLRD--VDLVVVDEAHLIDD-------ESRGPTLevll 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 179 --LKEQFPSASVHAFTATASEQvrDDIAEQLqlnqPNILVGDFDRPN------LTYRMLR-ADG---KLNQIQQCIAQHP 246
Cdd:COG1204 163 arLRRLNPEAQIVALSATIGNA--EEIAEWL----DAELVKSDWRPVplnegvLYDGVLRfDDGsrrSKDPTLALALDLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 247 GESG--VVYCITRKEVEQTAAAL-ESMGVRTLPY------------------------------------HAGLPDDVRQ 287
Cdd:COG1204 237 EEGGqvLVFVSSRRDAESLAKKLaDELKRRLTPEereeleelaeellevseethtnekladclekgvafhHAGLPSELRR 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1818934875 288 ANQEAFIQEKVDVIVATVAFGMGIdksN--VRFVI------HAGMPKSIEHYQQESGRAGRDGL 343
Cdd:COG1204 317 LVEDAFREGLIKVLVATPTLAAGV---NlpARRVIirdtkrGGMVPIPVLEFKQMAGRAGRPGY 377
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
542-616 |
1.09e-11 |
|
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: 61.16 E-value: 1.09e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1818934875 542 VDRKLFDHLRSLRSEMASERGVPAYVIFGDAVLRELARVRPTSIEKLTNIRGIGDRKREEFGQLFLDSIDQYCEE 616
Cdd:smart00341 3 RQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEASDS 77
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
41-160 |
2.69e-10 |
|
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: 59.91 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 41 QADAVQDVIQGRDSLVVLPTGGGKSLCYQVP---ALVRDGMS--VVVSPLISLMKDQVDALTS--NGVSAALVNSTQSVE 113
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPileALLRDPGSraLYLYPTKALAQDQLRSLREllEQLGLGIRVATYDGD 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1818934875 114 QKRETAERLRRGEIKILYLAP---ERLLTP---KTLDFLRSLpiSFFAIDEAH 160
Cdd:cd17923 85 TPREERRAIIRNPPRILLTNPdmlHYALLPhhdRWARFLRNL--RYVVLDEAH 135
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
300-350 |
3.60e-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: 56.56 E-value: 3.60e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1818934875 300 VIVATVAFGMGIDKSNVRFVIHAGMPKSIEHYQQESGRAGRDG-LAAECILL 350
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILF 76
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
240-350 |
4.30e-10 |
|
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: 58.72 E-value: 4.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 240 QCIAQHPGESGV-VYCITRKEVEQTAAALESMGVrtlpYHAGLPDDVRQANQEAFIQEKVDVIVATVAFGMGID------ 312
Cdd:cd18795 35 LKIETVSEGKPVlVFCSSRKECEKTAKDLAGIAF----HHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpartv 110
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1818934875 313 --KSNVRFVIHAGMPKSIEHYQQESGRAGRDGL--AAECILL 350
Cdd:cd18795 111 iiKGTQRYDGKGYRELSPLEYLQMIGRAGRPGFdtRGEAIIM 152
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
39-342 |
8.19e-09 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 58.63 E-value: 8.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 39 PLQADAVQDVIQGRDSLVVLPTGGGKSLCYQVPALVR----------DG-MSVVVSPLISLMKDQVDALTSNGVSAALVN 107
Cdd:PTZ00110 155 PIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHinaqpllrygDGpIVLVLAPTRELAEQIREQCNKFGASSKIRN 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 108 STQ--SVEQKRETAErLRRGeIKILYLAPERLLtpktlDFLRS-----LPISFFAIDEAHCVSNWGhdFRPEYRglRILK 180
Cdd:PTZ00110 235 TVAygGVPKRGQIYA-LRRG-VEILIACPGRLI-----DFLESnvtnlRRVTYLVLDEADRMLDMG--FEPQIR--KIVS 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 181 EQFPSASVHAFTATASEQVRDdIAEQLQLNQP-NILVGDFDrpnLT-------YRMLRAD----GKLNQIQQCIAQhPGE 248
Cdd:PTZ00110 304 QIRPDRQTLMWSATWPKEVQS-LARDLCKEEPvHVNVGSLD---LTachnikqEVFVVEEhekrGKLKMLLQRIMR-DGD 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 249 SGVVYCITRKEVEQTAAALESMGVRTLPYHAGLPDDVRQANQEAFIQEKVDVIVATVAFGMGIDKSNVRFVIHAGMPKSI 328
Cdd:PTZ00110 379 KILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQI 458
|
330
....*....|....
gi 1818934875 329 EHYQQESGRAGRDG 342
Cdd:PTZ00110 459 EDYVHRIGRTGRAG 472
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
33-348 |
2.40e-08 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 57.27 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 33 GYDSFRPLQADAVQDVIQGRDSLVVLPTGGGKSLCYQV---------PALV----RDGMSVVVSPL----ISLMKDQVDA 95
Cdd:PRK04537 28 GFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVavmnrllsrPALAdrkpEDPRALILAPTrelaIQIHKDAVKF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 96 LTSNGVSAALVNSTQSVEQKRETaerLRRGeIKILYLAPERLltpktLDFLRSLP-ISFFA-----IDEAHCVSNWGHdf 169
Cdd:PRK04537 108 GADLGLRFALVYGGVDYDKQREL---LQQG-VDVIIATPGRL-----IDYVKQHKvVSLHAceicvLDEADRMFDLGF-- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 170 rpeYRGLRILKEQFPSASVHA---FTATASEQVRDDIAEqlQLNQPNILVGDFDrpNLTYRMLRA-------DGKLNQIQ 239
Cdd:PRK04537 177 ---IKDIRFLLRRMPERGTRQtllFSATLSHRVLELAYE--HMNEPEKLVVETE--TITAARVRQriyfpadEEKQTLLL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 240 QCIAQHPGESGVVYCITRKEVEQTAAALESMGVRTLPYHAGLPDDVRQANQEAFIQEKVDVIVAT--VAFGMGIDksNVR 317
Cdd:PRK04537 250 GLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATdvAARGLHID--GVK 327
|
330 340 350
....*....|....*....|....*....|.
gi 1818934875 318 FVIHAGMPKSIEHYQQESGRAGRDGLAAECI 348
Cdd:PRK04537 328 YVYNYDLPFDAEDYVHRIGRTARLGEEGDAI 358
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
33-342 |
7.99e-08 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 55.30 E-value: 7.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 33 GYDSFRPLQADAVQDVIQGRDSLVVLPTGGGKSLCY---------QVPALVRDGM----SVVVSP----LISLMKDQVDA 95
Cdd:PRK01297 106 GFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFlisiinqllQTPPPKERYMgeprALIIAPtrelVVQIAKDAAAL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 96 LTSNGVSA-ALVNSTQSVEQKRETAERLrrgeIKILYLAPERLLtpktlDFLRSLP-----ISFFAIDEAHCVSNWGhdF 169
Cdd:PRK01297 186 TKYTGLNVmTFVGGMDFDKQLKQLEARF----CDILVATPGRLL-----DFNQRGEvhldmVEVMVLDEADRMLDMG--F 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 170 RPEYRglRILKEQFPSASVHA--FTATASEQVRDdIAEQLQLNqPNIL------VGDFDRPNLTYRMLRADgKLNQIQQC 241
Cdd:PRK01297 255 IPQVR--QIIRQTPRKEERQTllFSATFTDDVMN-LAKQWTTD-PAIVeiepenVASDTVEQHVYAVAGSD-KYKLLYNL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 242 IAQHPGESGVVYCITRKEVEQTAAALESMGVRTLPYHAGLPDDVRQANQEAFIQEKVDVIVATVAFGMGIDKSNVRFVIH 321
Cdd:PRK01297 330 VTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVIN 409
|
330 340
....*....|....*....|.
gi 1818934875 322 AGMPKSIEHYQQESGRAGRDG 342
Cdd:PRK01297 410 FTLPEDPDDYVHRIGRTGRAG 430
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
33-138 |
8.09e-07 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350699 [Multi-domain] Cd Length: 198 Bit Score: 50.37 E-value: 8.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 33 GYDSFRPLQADAVQDVIQGRDSLVVLPTGGGKSLCYQVPALVR---------DGM-SVVVSPLISLMKDQVDALTSNG-- 100
Cdd:cd17941 9 GFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKlyrerwtpeDGLgALIISPTRELAMQIFEVLRKVGky 88
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1818934875 101 --VSAALVNSTQSVEQkretaERLRRGEIKILYLAPERLL 138
Cdd:cd17941 89 hsFSAGLIIGGKDVKE-----EKERINRMNILVCTPGRLL 123
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
36-207 |
1.07e-06 |
|
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: 49.64 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 36 SFRPLQADAVQDVI-QGRDSLVVLPTGGGKSLCYQ---VPALVRDGMSVVVSPLISLMKDQVD---ALTSNGVSAALvns 108
Cdd:cd18028 1 ELYPPQAEAVRAGLlKGENLLISIPTASGKTLIAEmamVNTLLEGGKALYLVPLRALASEKYEefkKLEEIGLKVGI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 109 tqSVEQKRETAERLRRGEIKIlylaperlLTPKTLDFL-RSLP-----ISFFAIDEAHCVSNwghdfrpEYRGLRI---- 178
Cdd:cd18028 78 --STGDYDEDDEWLGDYDIIV--------ATYEKFDSLlRHSPswlrdVGVVVVDEIHLISD-------EERGPTLesiv 140
|
170 180 190
....*....|....*....|....*....|.
gi 1818934875 179 --LKEQFPSASVHAFTATASEQvrDDIAEQL 207
Cdd:cd18028 141 arLRRLNPNTQIIGLSATIGNP--DELAEWL 169
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
1-342 |
3.76e-06 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 49.82 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 1 MSSPSDSTSTLAPSNS------------SGDEMDRAHSVLRSVWGYDSFRP--LQADAVQDVIQGRDSLVVLPTGGGKSL 66
Cdd:PTZ00424 1 MATSEQKNQSEQVASTgtiesnydeivdSFDALKLNEDLLRGIYSYGFEKPsaIQQRGIKPILDGYDTIGQAQSGTGKTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 67 CYQVPALVRDGMSVVVSPLISLMKDQVDALTSNGVSAALVNSTQ----------SVeqkRETAERLRRGeIKILYLAPER 136
Cdd:PTZ00424 81 TFVIAALQLIDYDLNACQALILAPTRELAQQIQKVVLALGDYLKvrchacvggtVV---RDDINKLKAG-VHMVVGTPGR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 137 LLTPKTLDFLRSLPISFFAIDEAHCVSNWGhdFRPEYRglRILKEQFPSASVHAFTATASEQVRDdIAEQLQLNQPNILV 216
Cdd:PTZ00424 157 VYDMIDKRHLRVDDLKLFILDEADEMLSRG--FKGQIY--DVFKKLPPDVQVALFSATMPNEILE-LTTKFMRDPKRILV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 217 gdfDRPNLTYRMLRA--------DGKLNQIQQCIAQHPGESGVVYCITRKEVEQTAAALESMGVRTLPYHAGLPDDVRQA 288
Cdd:PTZ00424 232 ---KKDELTLEGIRQfyvavekeEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDL 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1818934875 289 NQEAFIQEKVDVIVATVAFGMGIDKSNVRFVIHAGMPKSIEHYQQESGRAGRDG 342
Cdd:PTZ00424 309 IMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFG 362
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
33-369 |
3.88e-06 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 50.23 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 33 GYDSFRPLQADAVQDVIQGRDSLVVLPTGGGKSLCYQVPAL------VRDGMSVVVSPLISLMKDQVDALTS-----NGV 101
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLhnldpeLKAPQILVLAPTRELAVQVAEAMTDfskhmRGV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 102 SA-ALVNSTQSVEQKREtaerLRRGEiKILYLAPERLL---TPKTLDfLRSLpiSFFAIDEAHCVSNWGHdfrpeYRGLR 177
Cdd:PRK11634 105 NVvALYGGQRYDVQLRA----LRQGP-QIVVGTPGRLLdhlKRGTLD-LSKL--SGLVLDEADEMLRMGF-----IEDVE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 178 ILKEQFPSASVHA-FTATASEQVRDdIAEQLqLNQPN---ILVGDFDRPNLTYRMLRADG--KLNQIQQCIAQHPGESGV 251
Cdd:PRK11634 172 TIMAQIPEGHQTAlFSATMPEAIRR-ITRRF-MKEPQevrIQSSVTTRPDISQSYWTVWGmrKNEALVRFLEAEDFDAAI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 252 VYCITRKEVEQTAAALESMGVRTlpyhAGLPDDVRQANQEAFIQE----KVDVIVATVAFGMGIDKSNVRFVIHAGMPKS 327
Cdd:PRK11634 250 IFVRTKNATLEVAEALERNGYNS----AALNGDMNQALREQTLERlkdgRLDILIATDVAARGLDVERISLVVNYDIPMD 325
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1818934875 328 IEHYQQESGRAGRDGLAAECILLHSGGDlmswKRILENGDRS 369
Cdd:PRK11634 326 SESYVHRIGRTGRAGRAGRALLFVENRE----RRLLRNIERT 363
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
33-217 |
8.93e-06 |
|
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350700 [Multi-domain] Cd Length: 198 Bit Score: 46.97 E-value: 8.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 33 GYDSFRPLQADAVQDVIQGRDSLVVLPTGGGKSLCYQVPAL---------VRDGMSVVV-SPLISLmkdqvdALTSNGVS 102
Cdd:cd17942 9 GFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIellyklkfkPRNGTGVIIiSPTREL------ALQIYGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 103 AALV-NSTQSV------EQKRETAERLRRGeIKILYLAPERLltpktLDFLRSLP------ISFFAIDEAHCVSNWGhdF 169
Cdd:cd17942 83 KELLkYHSQTFgiviggANRKAEAEKLGKG-VNILVATPGRL-----LDHLQNTKgflyknLQCLIIDEADRILEIG--F 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1818934875 170 RPEYRglRILKeQFPSA-SVHAFTATASEQVrDDIAeQLQLNQPNILVG 217
Cdd:cd17942 155 EEEMR--QIIK-LLPKRrQTMLFSATQTRKV-EDLA-RISLKKKPLYVG 198
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
36-194 |
9.16e-06 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 46.51 E-value: 9.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 36 SFRPLQADAVQDVIQGRDS-----LVVLPTGGGKSLCY-QVPALVRDGMS----VVVSPLISLMKDQVDALTSNGVSAAL 105
Cdd:pfam04851 3 ELRPYQIEAIENLLESIKNgqkrgLIVMATGSGKTLTAaKLIARLFKKGPikkvLFLVPRKDLLEQALEEFKKFLPNYVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 106 VNSTQSVEQKRETaerlrRGEIKILYLAPERLLTPKTLDFLRSLPISFFAI--DEAHcvsnwgHDFRPEYRGlriLKEQF 183
Cdd:pfam04851 83 IGEIISGDKKDES-----VDDNKIVVTTIQSLYKALELASLELLPDFFDVIiiDEAH------RSGASSYRN---ILEYF 148
|
170
....*....|.
gi 1818934875 184 PSASVHAFTAT 194
Cdd:pfam04851 149 KPAFLLGLTAT 159
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
550-612 |
1.34e-05 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 47.94 E-value: 1.34e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1818934875 550 LRSL---RSEMASERGVPAYVIFGDAVLRELARVRPTSIEKLTNIRGIGDRKREEFGQLFLDSIDQ 612
Cdd:COG0349 213 LRELaawREREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAVAE 278
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
39-200 |
1.45e-05 |
|
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350716 [Multi-domain] Cd Length: 197 Bit Score: 46.69 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 39 PLQADAVQDVIQGRDSLVVLPTGGGKSLCYQVPALV-----------RDGMSV-VVSP---LISLMKDQVDALTSNGVSA 103
Cdd:cd17958 15 PIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIhldlqpipreqRNGPGVlVLTPtreLALQIEAECSKYSYKGLKS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 104 ALVNSTQSveqKRETAERLRRGeIKILYLAPERLLTPKTLDFLRSLPISFFAIDEAHCVSNWGhdFRPEYRglRILKEQF 183
Cdd:cd17958 95 VCVYGGGN---RNEQIEDLSKG-VDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMG--FEPQIR--KILLDIR 166
|
170
....*....|....*..
gi 1818934875 184 PSASVHAFTATASEQVR 200
Cdd:cd17958 167 PDRQTIMTSATWPDGVR 183
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
41-342 |
2.50e-05 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 47.57 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 41 QADAVQDVIQGRDSLVVLPTGGGKSLC-----YQvpALVRDGMSVVVSPLISLMKDQVDALtSNGVSAALvNSTQSVEQK 115
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKTLIaysaiYE--TFLAGLKSIYIVPLRSLAMEKYEEL-SRLRSLGM-RVKISIGDY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 116 RETAERLRRGEIKILYLAPERLLTPKTLDFLRSlpISFFAIDEAHCVSNwghdfrpEYRG------LRILKEQFPSASVH 189
Cdd:PRK01172 103 DDPPDFIKRYDVVILTSEKADSLIHHDPYIIND--VGLIVADEIHIIGD-------EDRGptletvLSSARYVNPDARIL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 190 AFTATASEQvrDDIAEQLQlnqPNILVGDFdRP-----NLTYR-MLRADGK------LNQIQQCIAQHPGESgVVYCITR 257
Cdd:PRK01172 174 ALSATVSNA--NELAQWLN---ASLIKSNF-RPvplklGILYRkRLILDGYersqvdINSLIKETVNDGGQV-LVFVSSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 258 KEVEQTAAAL--------------------ESMGVRTLP-----YHAGLPDDVRQANQEAFIQEKVDVIVATVAFGMGID 312
Cdd:PRK01172 247 KNAEDYAEMLiqhfpefndfkvssennnvyDDSLNEMLPhgvafHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVN 326
|
330 340 350
....*....|....*....|....*....|....*...
gi 1818934875 313 --------KSNVRFVIHAGMPKSIEHYQQESGRAGRDG 342
Cdd:PRK01172 327 lparlvivRDITRYGNGGIRYLSNMEIKQMIGRAGRPG 364
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
191-342 |
3.44e-05 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 46.86 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 191 FTAT-ASEQVRDdIAEQLqLNQPNILVGD---FDRPNLTYRMLRADG---KLNQIQQCIAQHPGESGVVYCITRKEVEQT 263
Cdd:PRK11192 184 FSATlEGDAVQD-FAERL-LNDPVEVEAEpsrRERKKIHQWYYRADDlehKTALLCHLLKQPEVTRSIVFVRTRERVHEL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 264 AAALESMGVRTLPYHAGLPDDVRQANQEAFIQEKVDVIVAT-VAfGMGIDKSNVRFVIHAGMPKSIEHYQQESGRAGRDG 342
Cdd:PRK11192 262 AGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATdVA-ARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAG 340
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
257-340 |
6.96e-05 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 46.42 E-value: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 257 RKEVEQTAAALesmGVRTLPYHAGLPDDVRQANQEAFIQEKVDVIVATVAFGMGID--KSNVRFVIHAgMPK---SIEHY 331
Cdd:COG1202 437 RRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDfpASQVIFDSLA-MGIewlSVQEF 512
|
....*....
gi 1818934875 332 QQESGRAGR 340
Cdd:COG1202 513 HQMLGRAGR 521
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
39-217 |
2.75e-04 |
|
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350808 [Multi-domain] Cd Length: 271 Bit Score: 43.46 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 39 PLQADAVQDVIQGRDSLVVLPTGGGKSLCYQVPALVR----------DG-MSVVVSPLISLMKdQVDALTSNGVSAALVN 107
Cdd:cd18050 87 PIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHinhqpylergDGpICLVLAPTRELAQ-QVQQVADDYGKSSRLK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 108 ST--QSVEQKRETAERLRRGeIKILYLAPERLltpktLDFLRSLPI-----SFFAIDEAHCVSNWGhdFRPEYRglRILK 180
Cdd:cd18050 166 STciYGGAPKGPQIRDLERG-VEICIATPGRL-----IDFLEAGKTnlrrcTYLVLDEADRMLDMG--FEPQIR--KIVD 235
|
170 180 190
....*....|....*....|....*....|....*..
gi 1818934875 181 EQFPSASVHAFTATASEQVRdDIAEQLQLNQPNILVG 217
Cdd:cd18050 236 QIRPDRQTLMWSATWPKEVR-QLAEDFLRDYVQINIG 271
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
278-351 |
2.97e-04 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It 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: 350198 [Multi-domain] Cd Length: 159 Bit Score: 41.95 E-value: 2.97e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1818934875 278 HAGLPDDVRQANQEAFIQEKVDVIVATVAFGMGID--KSNVRFVIHA---GMpkSIEHyqQESGRAGRDGLAAECILLH 351
Cdd:cd18811 68 HGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDvpNATVMVIEDAerfGL--SQLH--QLRGRVGRGDHQSYCLLVY 142
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
39-210 |
3.70e-04 |
|
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350807 [Multi-domain] Cd Length: 234 Bit Score: 42.69 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 39 PLQADAVQDVIQGRDSLVVLPTGGGKSLCYQVPALVR----------DG-MSVVVSPLISLMKdQVDALTSNGVSAALVN 107
Cdd:cd18049 49 AIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHinhqpflergDGpICLVLAPTRELAQ-QVQQVAAEYGRACRLK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 108 ST--QSVEQKRETAERLRRGeIKILYLAPERLltpktLDFLRSLPI-----SFFAIDEAHCVSNWGhdFRPEYRglRILK 180
Cdd:cd18049 128 STciYGGAPKGPQIRDLERG-VEICIATPGRL-----IDFLEAGKTnlrrcTYLVLDEADRMLDMG--FEPQIR--KIVD 197
|
170 180 190
....*....|....*....|....*....|....
gi 1818934875 181 EQFPSASVHAFTATASEQVR----DDIAEQLQLN 210
Cdd:cd18049 198 QIRPDRQTLMWSATWPKEVRqlaeDFLKDYIHIN 231
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
33-159 |
3.81e-04 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 42.62 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 33 GYDSFRPLQADAVQDVIQG---------RDSLVVLPTGGGKSLCYQVPAL-------VRDGMSVVVSP---LISLMKDQV 93
Cdd:cd17956 9 GITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVqalskrvVPRLRALIVVPtkeLVQQVYKVF 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1818934875 94 DALTSN-GVSAALVNSTQSVEQKRETAERLRRGE----IKILYLAPERLL-----TPK-TLDFLRslpisFFAIDEA 159
Cdd:cd17956 89 ESLCKGtGLKVVSLSGQKSFKKEQKLLLVDTSGRylsrVDILVATPGRLVdhlnsTPGfTLKHLR-----FLVIDEA 160
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
252-346 |
4.14e-04 |
|
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene encodes a DNA and RNA helicase, which is localized in mitochondria and is a subunit of the degradosome complex involved in regulation of RNA surveillance and turnover. SUV3 exhibits DNA and RNA-dependent ATPase, DNA and RNA-binding and DNA and RNA unwinding activities. SUV3 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: 350192 [Multi-domain] Cd Length: 135 Bit Score: 41.01 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 252 VYCITRKEVEQTAAALESM-GVRTLPYHAGLPDDVRQANQEAFIQEK--VDVIVATVAFGMGIDkSNVRFVIHAGMPK-- 326
Cdd:cd18805 22 VVAFSRKDIFSLKREIEKRtGLKCAVIYGALPPETRRQQARLFNDPEsgYDVLVASDAIGMGLN-LNIRRVIFSSLSKfd 100
|
90 100
....*....|....*....|....*..
gi 1818934875 327 -------SIEHYQQESGRAGRDGLAAE 346
Cdd:cd18805 101 gnemrplSPSEVKQIAGRAGRFGSHFP 127
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
20-159 |
8.42e-04 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350697 [Multi-domain] Cd Length: 199 Bit Score: 41.16 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 20 EMDRAHSVLRSVWGYDSFRP--LQADAVQDVIQGRDSLVVLPTGGGKSLCYQVPALVRDGMSV------VVSPLISLMKD 91
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPsaIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVretqalVLAPTRELAQQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1818934875 92 QVDALTSNGV-----SAALVNSTQSveqkRETAERLRRGeIKILYLAPERLLTPKTLDFLRSLPISFFAIDEA 159
Cdd:cd17939 81 IQKVVKALGDymgvkVHACIGGTSV----REDRRKLQYG-PHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEA 148
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
256-340 |
1.11e-03 |
|
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: 39.94 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 256 TRKEVEQTAAAL------ESMGVRTLPYHAGLPDDVRQANQEAFIQEKVDVIVATVAFGMGIDKSNVRFVIHAGMPKSIE 329
Cdd:cd18796 47 TRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVA 126
|
90
....*....|.
gi 1818934875 330 HYQQESGRAGR 340
Cdd:cd18796 127 RLLQRLGRSGH 137
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
277-343 |
5.30e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 40.33 E-value: 5.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1818934875 277 YHAGLPDDVRQANQEAFIQEKVDVIVATVAFGMG--------IDKSNVRFVIHAGM-PKSIEHYQQESGRAGRDGL 343
Cdd:PRK02362 309 HHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGlnlparrvIIRDYRRYDGGAGMqPIPVLEYHQMAGRAGRPGL 384
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
51-160 |
6.46e-03 |
|
DEXH-box helicase domain of LHR; 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 from 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: 350680 [Multi-domain] Cd Length: 166 Bit Score: 37.95 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 51 GRDSLVVLPTGGGKSLCYQVPALVR------DGMSVV-VSPLISLMKDQVDALT--SNGVSAALvnstqSVEQKR-ETAE 120
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSladepeKGVQVLyISPLKALINDQERRLEepLDEIDLEI-----PVAVRHgDTSQ 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1818934875 121 RLRRGEIK----ILYLAPERL---LTPKTLDFLRSlPISFFAIDEAH 160
Cdd:cd17922 76 SEKAKQLKnppgILITTPESLellLVNKKLRELFA-GLRYVVVDEIH 121
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
33-200 |
8.46e-03 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350724 [Multi-domain] Cd Length: 197 Bit Score: 38.12 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 33 GYDSFRPLQADAVQDVIQGRDSLVVLPTGGGKSLCYQVPALVR----------DG-MSVVVSP---LISLMKDQVD--AL 96
Cdd:cd17966 9 GFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHinaqpplergDGpIVLVLAPtreLAQQIQQEANkfGG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1818934875 97 TSNGVSAALVNSTQSVEQKREtaerLRRGeIKILYLAPERLltpktLDFLRS-----LPISFFAIDEAHCVSNWGhdFRP 171
Cdd:cd17966 89 SSRLRNTCVYGGAPKGPQIRD----LRRG-VEICIATPGRL-----IDFLDQgktnlRRVTYLVLDEADRMLDMG--FEP 156
|
170 180
....*....|....*....|....*....
gi 1818934875 172 EYRglRILKEQFPSASVHAFTATASEQVR 200
Cdd:cd17966 157 QIR--KIVDQIRPDRQTLMWSATWPKEVR 183
|
|
| |
