|
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 ... |
6-599 |
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: 930.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 6 AHDLLRRVFGYDDFRGPQQDIVEHVAAGHDALVLMPTGGGKSLCYQVPALLRDGCGIVISPLIALMQDQVEALRQLGVRA 85
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 86 EFLNSTLDAETAGRVERELLAGELDMLYVAPERLLTGRFLSLLSRSRIALFAIDEAHCVSQWGHDFRPEYRQLTVLHERW 165
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 166 PEIPRIALTATADPPTQREIAERLDLAEARHFVSSFDRPNIRYTVVQKDNARKQLSDFLRSHRSEAGIVYCMSRRKVEET 245
Cdd:TIGR01389 161 PQVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 246 AEFLCTQGFNALPYHAGLPAEVRANNQRRFLREDGIVMCATIAFGMGIDKPDVRFVAHTDLPKSMEGYYQETGRAGRDGE 325
Cdd:TIGR01389 241 AERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 326 AAEAWLCYGLGDVVLLKQMIEQSEASEERKQLERSKLDHLLGYCESMQCRRQVLLAGFGETYPKPCGNCDNCLTPPAAWD 405
Cdd:TIGR01389 321 PAEAILLYSPADIALLKRRIEQSEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENEVEPCGNCDNCLDPPKSYD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 406 ATIPAQKALSCVYRSGQRFGVGHLIDVLRGSENEKVKQQGHDKLSTYAIGRDLDARTWRSVFRQLVAASLLEVDSEGHGG 485
Cdd:TIGR01389 401 ATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIYIG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 486 LRLTDASRDVLTGRRQISMRRDAVSAsagRERSAQRTGLSVLPQDlALFNALRGLRAELAREQNVPAFVIFHDSTLRNIA 565
Cdd:TIGR01389 481 LQLTEAARKVLKNEVEVLLRPFKVVA---KEKTRVQKNLSVGVDN-ALFEALRELRKEQADEQNVPPYVIFSDSTLREMA 556
|
570 580 590
....*....|....*....|....*....|....
gi 647598048 566 EQRPTSLDELARVGGIGGTKLSRYGPRLVEIVRE 599
Cdd:TIGR01389 557 EKRPATLNALLKIKGVGQNKLDRYGEAFLEVIRE 590
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
2-473 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 862.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 2 ASRPAHDLLRRVFGYDDFRGPQQDIVEHVAAGHDALVLMPTGGGKSLCYQVPALLRDGCGIVISPLIALMQDQVEALRQL 81
Cdd:COG0514 1 LRDDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 82 GVRAEFLNSTLDAETAGRVERELLAGELDMLYVAPERLLTGRFLSLLSRSRIALFAIDEAHCVSQWGHDFRPEYRQLTVL 161
Cdd:COG0514 81 GIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 162 HERWPEIPRIALTATADPPTQREIAERLDLAEARHFVSSFDRPNIRYTVVQK--DNARKQLSDFLRSHRSEAGIVYCMSR 239
Cdd:COG0514 161 RERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKppDDKLAQLLDFLKEHPGGSGIVYCLSR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 240 RKVEETAEFLCTQGFNALPYHAGLPAEVRANNQRRFLREDGIVMCATIAFGMGIDKPDVRFVAHTDLPKSMEGYYQETGR 319
Cdd:COG0514 241 KKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 320 AGRDGEAAEAWLCYGLGDVVLLKQMIEQSEASEERKQLERSKLDHLLGYCESMQCRRQVLLAGFGETYPKPCGNCDNCLT 399
Cdd:COG0514 321 AGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFGEELAEPCGNCDNCLG 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647598048 400 PPAAWDATIPAQKALSCVYRSGQRFGVGHLIDVLRGSENEKVKQQGHDKLSTYAIGRDLDARTWRSVFRQLVAA 473
Cdd:COG0514 401 PPETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLLAQ 474
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
5-599 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 669.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 5 PAHDLLRRVFGYDDFRGPQQDIVEHVAAGHDALVLMPTGGGKSLCYQVPALLRDGCGIVISPLIALMQDQVEALRQLGVR 84
Cdd:PRK11057 12 LAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 85 AEFLNSTLDAETAGRVERELLAGELDMLYVAPERLLTGRFLSLLSRSRIALFAIDEAHCVSQWGHDFRPEYRQLTVLHER 164
Cdd:PRK11057 92 AACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 165 WPEIPRIALTATADPPTQREIAERLDLAEARHFVSSFDRPNIRYTVVQKDNARKQLSDFLRSHRSEAGIVYCMSRRKVEE 244
Cdd:PRK11057 172 FPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVED 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 245 TAEFLCTQGFNALPYHAGLPAEVRANNQRRFLREDGIVMCATIAFGMGIDKPDVRFVAHTDLPKSMEGYYQETGRAGRDG 324
Cdd:PRK11057 252 TAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 325 EAAEAWLCYGLGDVVLLKQMIEQSEASEErKQLERSKLDHLLGYCESMQCRRQVLLAGFGETYPKPCGNCDNCLTPPAAW 404
Cdd:PRK11057 332 LPAEAMLFYDPADMAWLRRCLEEKPAGQQ-QDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNCDICLDPPKQY 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 405 DATIPAQKALSCVYRSGQRFGVGHLIDVLRGSENEKVKQQGHDKLSTYAIGRDLDARTWRSVFRQLVAASLLEVDSEGHG 484
Cdd:PRK11057 411 DGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQNIAQHS 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 485 GLRLTDASRDVLTGR--------RQISMRRDAVSASAGRErsaqrtglsvlpQDLALFNALRGLRAELAREQNVPAFVIF 556
Cdd:PRK11057 491 ALQLTEAARPVLRGEvslqlavpRIVALKPRAMQKSFGGN------------YDRKLFAKLRKLRKSIADEENIPPYVVF 558
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 647598048 557 HDSTLRNIAEQRPTSLDELARVGGIGGTKLSRYGPRLVEIVRE 599
Cdd:PRK11057 559 NDATLIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMALIRA 601
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
8-457 |
0e+00 |
|
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: 523.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 8 DLLRRVFGYDDFRGPQQDIVEHVAAGHDALVLMPTGGGKSLCYQVPALLRDGCGIVISPLIALMQDQVEALRQLGVRAEF 87
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 88 LNSTLDAETAGRVERELLAGELDMLYVAPERLLTG-RFLSLL-SRSRIALFAIDEAHCVSQWGHDFRPEYRQLTVLHERW 165
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKISASnRLLQTLeERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 166 PEIPRIALTATADPPTQREIAERLDLAEARHFVSSFDRPNIRYTVVQK-DNARKQLSDFLRS-HRSEAGIVYCMSRRKVE 243
Cdd:TIGR00614 161 PNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKtPKILEDLLRFIRKeFEGKSGIIYCPSRKKVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 244 ETAEFLCTQGFNALPYHAGLPAEVRANNQRRFLREDGIVMCATIAFGMGIDKPDVRFVAHTDLPKSMEGYYQETGRAGRD 323
Cdd:TIGR00614 241 QVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGRD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 324 GEAAEAWLCYGLGDVVLLKQMIEqsEASEERKQLERSKLDHLLGYC-ESMQCRRQVLLAGFGETYP----------KPCG 392
Cdd:TIGR00614 321 GLPSECHLFYAPADMNRLRRLLM--EEPDGNFRTYKLKLYEMMEYClNSSTCRRLILLSYFGEKGFnksfcimgteKCCD 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647598048 393 NCDNCL------TPPAAWDATIPAQKALSCVYRSGQRFGVGHLIDVLRGSENEKVKQQGHDKLSTYAIGRD 457
Cdd:TIGR00614 399 NCCKRLdyktkdVTDKVYDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGRGKD 469
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
11-597 |
3.70e-134 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 421.23 E-value: 3.70e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 11 RRVFGYDDFRGPQQDIVEHVAAGHDALVLMPTGGGKSLCYQVPALLRDGCGIVISPLIALMQDQVEALRQLGVRAEFLNS 90
Cdd:PLN03137 453 KKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSA 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 91 TLDAETAGRVERELLAG--ELDMLYVAPERLLTGRFL-----SLLSRSRIALFAIDEAHCVSQWGHDFRPEYRQLTVLHE 163
Cdd:PLN03137 533 GMEWAEQLEILQELSSEysKYKLLYVTPEKVAKSDSLlrhleNLNSRGLLARFVIDEAHCVSQWGHDFRPDYQGLGILKQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 164 RWPEIPRIALTATADPPTQREIAERLDLAEARHFVSSFDRPNIRYTVVQKdnARKQLSD---FLR-SHRSEAGIVYCMSR 239
Cdd:PLN03137 613 KFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPK--TKKCLEDidkFIKeNHFDECGIIYCLSR 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 240 RKVEETAEFLCTQGFNALPYHAGLPAEVRANNQRRFLREDGIVMCATIAFGMGIDKPDVRFVAHTDLPKSMEGYYQETGR 319
Cdd:PLN03137 691 MDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGR 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 320 AGRDGEAAEAWLCYGLGDVVLLKQMI-----EQSE--------ASEERkQLERS--KLDHLLGYCES-MQCRRQVLLAGF 383
Cdd:PLN03137 771 AGRDGQRSSCVLYYSYSDYIRVKHMIsqggvEQSPmamgynrmASSGR-ILETNteNLLRMVSYCENeVDCRRFLQLVHF 849
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 384 GETYPKP-CGN-CDNCLTPPA--AWDATIPAQKALSCVYRSGQRFGVGHLIDVLRGSENEKVKQQGHDKLSTYAIGRDLD 459
Cdd:PLN03137 850 GEKFDSTnCKKtCDNCSSSKSliDKDVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSLHGAGKHLS 929
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 460 ARTWRSVFRQLVAASLLEVD---SEGHGG----LRLTDA-SRDVLTGRRQISMR------------RDA----VSASAGR 515
Cdd:PLN03137 930 KGEASRILHYLVTEDILAEDvkkSDLYGSvsslLKVNESkAYKLFSGGQTIIMRfpssvkaskpskFEAtpakGPLTSGK 1009
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 516 ERSAQRTGLSVLPQDL----ALFNALRGLRAELARE--QNVPAFVIFHDSTLRNIAEQRPTSLDELARVGGIGGTKLSRY 589
Cdd:PLN03137 1010 QSTLPMATPAQPPVDLnlsaILYTALRKLRTALVKEagDGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAKVSKY 1089
|
....*...
gi 647598048 590 GPRLVEIV 597
Cdd:PLN03137 1090 GDRLLETI 1097
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
7-202 |
4.33e-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: 312.93 E-value: 4.33e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 7 HDLLRRVFGYDDFRGPQQDIVEHVAAGHDALVLMPTGGGKSLCYQVPALLRDGCGIVISPLIALMQDQVEALRQLGVRAE 86
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 87 FLNSTLDAETAGRVERELLAGELDMLYVAPERLLTGRFLSLLSR----SRIALFAIDEAHCVSQWGHDFRPEYRQLTVLH 162
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRlperKRLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 647598048 163 ERWPEIPRIALTATADPPTQREIAERLDLAEARHFVSSFD 202
Cdd:cd17920 161 RALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
7-193 |
2.98e-71 |
|
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: 227.91 E-value: 2.98e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 7 HDLLRRVFGYDDFRGPQQDIVEHVAAGHDALVLMPTGGGKSLCYQVPALL----RDGCGIVISPLIALMQDQVEALRQLg 82
Cdd:cd18018 1 LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALPRA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 83 VRAEFLNSTLDAETAGRVERELLAGELDMLYVAPERLLTGRFLSLL-SRSRIALFAIDEAHCVSQWGHDFRPEYRQL-TV 160
Cdd:cd18018 80 IKAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLrQTPPISLLVVDEAHCISEWSHNFRPDYLRLcRV 159
|
170 180 190
....*....|....*....|....*....|...
gi 647598048 161 LHERWPEIPRIALTATADPPTQREIAERLDLAE 193
Cdd:cd18018 160 LRELLGAPPVLALTATATKRVVEDIASHLGIPE 192
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
3-202 |
4.44e-70 |
|
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: 225.32 E-value: 4.44e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 3 SRPAHDLLRRVFGYDDFRGPQQDIVEHVAAGHDALVLMPTGGGKSLCYQVPALLRDGCGIVISPLIALMQDQVEALRQLG 82
Cdd:cd18015 3 SGKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 83 VRAEFLNSTLDAETAGRVERELLAG--ELDMLYVAPERLL-TGRFLSLLSRS----RIALFAIDEAHCVSQWGHDFRPEY 155
Cdd:cd18015 83 ISATMLNASSSKEHVKWVHAALTDKnsELKLLYVTPEKIAkSKRFMSKLEKAynagRLARIAIDEVHCCSQWGHDFRPDY 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 647598048 156 RQLTVLHERWPEIPRIALTATADPPTQREIAERLDLAEARHFVSSFD 202
Cdd:cd18015 163 KKLGILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
8-202 |
6.45e-62 |
|
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: 203.91 E-value: 6.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 8 DLLRRVFGYDDFRGPQQDIVEHVAAGHDALVLMPTGGGKSLCYQVPALLRDGCGIVISPLIALMQDQVEALRQLGVRAEF 87
Cdd:cd18016 7 KIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 88 LNSTLDAETAGRVERELLAGE--LDMLYVAPERL-LTGRFLSLL----SRSRIALFAIDEAHCVSQWGHDFRPEYRQLTV 160
Cdd:cd18016 87 LTGDKTDAEATKIYLQLSKKDpiIKLLYVTPEKIsASNRLISTLenlyERKLLARFVIDEAHCVSQWGHDFRPDYKRLNM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 647598048 161 LHERWPEIPRIALTATADPPTQREIAERLDLAEARHFVSSFD 202
Cdd:cd18016 167 LRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
203-333 |
3.21e-58 |
|
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: 191.27 E-value: 3.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 203 RPNIRYTVVQKDNARKQLSDFLRS---HRSEAGIVYCMSRRKVEETAEFLCTQGFNALPYHAGLPAEVRANNQRRFLRED 279
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLKRIkveHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 647598048 280 GIVMCATIAFGMGIDKPDVRFVAHTDLPKSMEGYYQETGRAGRDGEAAEAWLCY 333
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
7-191 |
1.89e-57 |
|
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: 191.92 E-value: 1.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 7 HDLLRRVFGYDDFRGP-QQDIVEHVAAGH-DALVLMPTGGGKSLCYQVPALLRDGCGIVISPLIALMQDQVEALRQLGVR 84
Cdd:cd18014 1 RSTLKKVFGHSDFKSPlQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 85 AEFLNSTLDAETAGRVERELLAG--ELDMLYVAPERLLTGRFL----SLLSRSRIALFAIDEAHCVSQWGHDFRPEYRQL 158
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADLESEkpQTKFLYITPEMAATSSFQpllsSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190
....*....|....*....|....*....|...
gi 647598048 159 TVLHERWPEIPRIALTATADPPTQREIAERLDL 191
Cdd:cd18014 161 GALRSRYGHVPWVALTATATPQVQEDIFAQLRL 193
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
8-202 |
5.63e-53 |
|
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: 179.59 E-value: 5.63e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 8 DLLRRVFGYDDFRGPQQDIVEHV-AAGHDALVLMPTGGGKSLCYQVPALLRDGCGIVISPLIALMQDQVEALRQLGVRAE 86
Cdd:cd18017 2 NALNEYFGHSSFRPVQWKVIRSVlEERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPAC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 87 FLNStldaETAGRVERELLAGELDMLYVAPERLLTGRFLSLLSRSRIALFAIDEAHCVSQWGHDFRPEYRQLTVLHERWP 166
Cdd:cd18017 82 FLGS----AQSQNVLDDIKMGKIRVIYVTPEFVSKGLELLQQLRNGITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRLP 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 647598048 167 EIPRIALTATADPPTQREIAERLDLAEARHFVSSFD 202
Cdd:cd18017 158 NVPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
400-507 |
8.33e-48 |
|
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: 162.32 E-value: 8.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 400 PPAAWDATIPAQKALSCVYRSGQRFGVGHLIDVLRGSENEKVKQQGHDKLSTYAIGRDLDARTWRSVFRQLVAASLLEVD 479
Cdd:pfam09382 1 PPETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVD 80
|
90 100
....*....|....*....|....*...
gi 647598048 480 SEGHGGLRLTDASRDVLTGRRQISMRRD 507
Cdd:pfam09382 81 IEFYSVLKLTPKAREVLKGEEKVMLRVP 108
|
|
| DpdF |
NF041063 |
protein DpdF; |
4-344 |
9.25e-44 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 167.40 E-value: 9.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 4 RPAHD-LLRRVFGYDDFRGP-QQDIVEHVA---AGHDALVLMPTGGGKSLCYQVPALL---RDGCGIVISPLIALMQDQV 75
Cdd:NF041063 124 PVPGDpFLAEALGFTHYRSPgQREAVRAALlapPGSTLIVNLPTGSGKSLVAQAPALLasrQGGLTLVVVPTVALAIDQE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 76 EALRQLGVRAEFLNST-------LDAETAGRVERELLAGELDMLYVAPERLlTGRFLSLL----SRSRIALFAIDEAHCV 144
Cdd:NF041063 204 RRARELLRRAGPDLGGplawhggLSAEERAAIRQRIRDGTQRILFTSPESL-TGSLRPALfdaaEAGLLRYLVVDEAHLV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 145 SQWGHDFRPEYRQLTVLHERW------PEIPR-IALTATAdppTQREIA--ERLdLAEARHFV---SSFDRPNIRYTVVQ 212
Cdd:NF041063 283 DQWGDGFRPEFQLLAGLRRSLlrlapsGRPFRtLLLSATL---TESTLDtlETL-FGPPGPFIvvsAVQLRPEPAYWVAK 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 213 KDNA---RKQLSDFLRsHRSEAGIVYCMSRRKVEETAEFLCTQGFNALP-YHAGLPAEVRannqRRFL---REDGI-VMC 284
Cdd:NF041063 359 CDSEeerRERVLEALR-HLPRPLILYVTKVEDAEAWLQRLRAAGFRRVAlFHGDTPDAER----ERLIeqwRENELdIVV 433
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 285 ATIAFGMGIDKPDVRFVAHTDLPKSMEGYYQETGRAGRDGEAAEAWLCYGLGDVVLLKQM 344
Cdd:NF041063 434 ATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDIAKSL 493
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
405-496 |
4.42e-43 |
|
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: 149.16 E-value: 4.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 405 DATIPAQKALSCVYRSGQRFGVGHLIDVLRGSENEKVKQQGHDKLSTYAIGRDLDARTWRSVFRQLVAASLLEVDSEGHG 484
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYP 80
|
90
....*....|..
gi 647598048 485 GLRLTDASRDVL 496
Cdd:smart00956 81 YLKLTEKARPVL 92
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
23-183 |
9.21e-27 |
|
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: 106.56 E-value: 9.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 23 QQDIVEHVAAGHDALVLMPTGGGKSLCYQVPAL--LRDGCG----IVISPLIALMQDQVEALRQLGvraEFLNSTLDAET 96
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALeaLDKLDNgpqaLVLAPTRELAEQIYEELKKLG---KGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 97 AG---RVERELLAGeLDMLYVAPERLLTgrFLSLLSR-SRIALFAIDEAHCVSQWGhdFRPEYRQ-LTVLHerwPEIPRI 171
Cdd:pfam00270 81 GGdsrKEQLEKLKG-PDILVGTPGRLLD--LLQERKLlKNLKLLVLDEAHRLLDMG--FGPDLEEiLRRLP---KKRQIL 152
|
170
....*....|..
gi 647598048 172 ALTATADPPTQR 183
Cdd:pfam00270 153 LLSATLPRNLED 164
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
14-211 |
7.72e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 102.18 E-value: 7.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 14 FGYDDFRGPQQDIVEHVAAG-HDALVLMPTGGGKSLCYQVPALLR-----DGCGIVISPLIALMQDQVEALRQLGVRAEF 87
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 88 LNSTL-DAETAGRVERELLAGELDMLYVAPERLLTGRFLSLLSRSRIALFAIDEAHCVSQWGhdFRPEYRQLtvLHERWP 166
Cdd:smart00487 84 KVVGLyGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKL--LKLLPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 647598048 167 EIPRIALTATADPPTQREIAERLDLAearHFVSSFDRPNIRYTVV 211
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDP---VFIDVGFTPLEPIEQF 201
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
335-398 |
2.10e-23 |
|
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: 93.51 E-value: 2.10e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 647598048 335 LGDVVLLKQMIEQSEASEERKQLERSKLDHLLGYCES-MQCRRQVLLAGFGETY-PKPCGNCDNCL 398
Cdd:pfam16124 1 YQDVVRLRFLIEQSEADEERKEVELQKLQAMVAYCENtTDCRRKQLLRYFGEEFdSEPCGNCDNCL 66
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
530-597 |
1.35e-21 |
|
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: 88.36 E-value: 1.35e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647598048 530 DLALFNALRGLRAELAREQNVPAFVIFHDSTLRNIAEQRPTSLDELARVGGIGGTKLSRYGPRLVEIV 597
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
243-324 |
6.83e-19 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 81.49 E-value: 6.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 243 EETAEFLCTQGFNALPYHAGLPAEVRANNQRRFLREDGIVMCATIAFGMGIDKPDVRFVAHTDLPKSMEGYYQETGRAGR 322
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 647598048 323 DG 324
Cdd:smart00490 81 AG 82
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
220-324 |
7.50e-19 |
|
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: 82.26 E-value: 7.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 220 LSDFLRSHRSEAGIVYCMSRRKVEETaEFLCTQGFNALPYHAGLPAEVRANNQRRFLREDGIVMCATIAFGMGIDKPDVR 299
Cdd:pfam00271 6 LLELLKKERGGKVLIFSQTKKTLEAE-LLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVD 84
|
90 100
....*....|....*....|....*
gi 647598048 300 FVAHTDLPKSMEGYYQETGRAGRDG 324
Cdd:pfam00271 85 LVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
23-327 |
3.18e-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: 88.74 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 23 QQDIVEHVAAGHDALVLMPTGGGKSLCYQVPALL-----RDGCGIVISPLIALMQDQVEALRQL------GVRAeflnST 91
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEalledPGATALYLYPTKALARDQLRRLRELaealglGVRV----AT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 92 LDAETAGRVERELLAG------ELDMLYVAperLL--TGRFLSLLSRSRiaLFAIDEAHcvsqwghdfrpEY-------- 155
Cdd:COG1205 137 YDGDTPPEERRWIREHpdivltNPDMLHYG---LLphHTRWARFFRNLR--YVVIDEAH-----------TYrgvfgshv 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 156 ----RQLTVLHERWPEIPR-IALTAT-ADPptqREIAERLdlaearhfvssFDRPnirYTVVQKDNARKQLSDFL----- 224
Cdd:COG1205 201 anvlRRLRRICRHYGSDPQfILASATiGNP---AEHAERL-----------TGRP---VTVVDEDGSPRGERTFVlwnpp 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 225 -------RSHRSEA-------------GIVYCMSRRKVE----ETAEFLCTQGF--NALPYHAGLPAEVRANNQRRfLRE 278
Cdd:COG1205 264 lvddgirRSALAEAarlladlvreglrTLVFTRSRRGAEllarYARRALREPDLadRVAAYRAGYLPEERREIERG-LRS 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 647598048 279 ---DGIVmcATIAFGMGIDKPDVRFVAHTDLPKSMEGYYQETGRAGRDGEAA 327
Cdd:COG1205 343 gelLGVV--STNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDS 392
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
33-176 |
1.60e-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: 79.75 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 33 GHDALVLMPTGGGKSLCYQVPALLRD---GCGI-VISPLIALMQDQVEALRQL---GVRAEFLNSTLDAETagrvERELL 105
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLlkkGKKVlVLVPTKALALQTAERLRELfgpGIRVAVLVGGSSAEE----REKNK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647598048 106 AGELDMLYVAPERLLT-GRFLSLLSRSRIALFAIDEAHCVSQWGHDFRPEYRQLTVLHErwPEIPRIALTAT 176
Cdd:cd00046 77 LGDADIIIATPDMLLNlLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGL--KNAQVILLSAT 146
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
8-322 |
1.15e-14 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 76.86 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 8 DLLRRvFGYDDFRGPQQDIVE-HVAAGHDALVLMPTGGGKSLCYQVP---ALLRDGCGIVISPLIALmQDQVE-----AL 78
Cdd:COG1204 13 EFLKE-RGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAilkALLNGGKALYIVPLRAL-ASEKYrefkrDF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 79 RQLGVRAEFLnstldaeTAGRVERELLAGELDMLYVAPErlltgRFLSLLSRS-----RIALFAIDEAHCVsqwGHDFR- 152
Cdd:COG1204 91 EELGIKVGVS-------TGDYDSDDEWLGRYDILVATPE-----KLDSLLRNGpswlrDVDLVVVDEAHLI---DDESRg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 153 PEYRQ-LTVLHERWPEIPRIALTATADPPtqREIAERLDlaeARHFVSSFdRPNIRYTVVQKDNA----------RKQLS 221
Cdd:COG1204 156 PTLEVlLARLRRLNPEAQIVALSATIGNA--EEIAEWLD---AELVKSDW-RPVPLNEGVLYDGVlrfddgsrrsKDPTL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 222 DFLRSHRSEAG--IVYCMSRRKVEETA------------------------EFLCTQGFNALPY-------------HAG 262
Cdd:COG1204 230 ALALDLLEEGGqvLVFVSSRRDAESLAkkladelkrrltpeereeleelaeELLEVSEETHTNEkladclekgvafhHAG 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 647598048 263 LPAEVRAnnqrrfLREDGI------VMCAT--IAfgMGIDKP-------DVRFVAHTDLPkSMEgYYQETGRAGR 322
Cdd:COG1204 310 LPSELRR------LVEDAFreglikVLVATptLA--AGVNLParrviirDTKRGGMVPIP-VLE-FKQMAGRAGR 374
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
23-142 |
1.43e-14 |
|
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: 72.23 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 23 QQDIVEHVAAGHDALVLMPTGGGKSLCYQVP---ALLRD--GCGIVISPLIALMQDQVEALRQLGVR--AEFLNSTLDAE 95
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPileALLRDpgSRALYLYPTKALAQDQLRSLRELLEQlgLGIRVATYDGD 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 647598048 96 TAGRVERELLAGEL-------DMLYVA--PERLLTGRFLSLLsrsriALFAIDEAH 142
Cdd:cd17923 85 TPREERRAIIRNPPrilltnpDMLHYAllPHHDRWARFLRNL-----RYVVLDEAH 135
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
528-599 |
8.86e-14 |
|
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: 66.94 E-value: 8.86e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647598048 528 PQDLALFNALRGLRAELAREQNVPAFVIFHDSTLRNIAEQRPTSLDELARVGGIGGTKLSRYGPRLVEIVRE 599
Cdd:smart00341 2 ERQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQE 73
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
15-351 |
9.23e-14 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 74.05 E-value: 9.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 15 GYDDFRGPQQDIVEHVAAGHDALVLMPTGGGKSLCYQVPALLRdgCGIVIS--------PLIALMQDQVEALRQLGVRAE 86
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISR--CCTIRSghpseqrnPLAMVLTPTRELCVQVEDQAK 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 87 FLNSTLDAETAGRVERELLAGELDMLYVAPERLL--TGRFLSLLSRSRIAL-----FAIDEAHCVSQWGhdFRPEYRQLT 159
Cdd:PLN00206 218 VLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVgtPGRLIDLLSKHDIELdnvsvLVLDEVDCMLERG--FRDQVMQIF 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 160 vlheRWPEIPRIALTATADPPTQREIAErlDLAEARHFVS--SFDRPN--IRYTV--VQKDNARKQLSDFLRS--HRSEA 231
Cdd:PLN00206 296 ----QALSQPQVLLFSATVSPEVEKFAS--SLAKDIILISigNPNRPNkaVKQLAiwVETKQKKQKLFDILKSkqHFKPP 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 232 GIVYCMSRRKVEETAEFLC-TQGFNALPYHAGLPAEVRANNQRRFLREDGIVMCATIAFGMGIDKPDVRFVAHTDLPKSM 310
Cdd:PLN00206 370 AVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTI 449
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 647598048 311 EGYYQETGRAGRDGEAAEAWLCYGLGDVVLLKQMIEQSEAS 351
Cdd:PLN00206 450 KEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSS 490
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
207-326 |
1.50e-13 |
|
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: 67.53 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 207 RYTVV-QKDNARKQLSDFLRSHRSEAGIVYCMSRRKVEETAEFLCTQGFNALPYHAGLPAEVRANNQRRFLREDGIVMCA 285
Cdd:cd18787 4 LYVVVeEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVA 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 647598048 286 TIAFGMGIDKPDVRFVAHTDLPKSMEGYYQ---ETGRAGRDGEA 326
Cdd:cd18787 84 TDVAARGLDIPGVDHVINYDLPRDAEDYVHrigRTGRAGRKGTA 127
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
23-326 |
3.05e-13 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 71.72 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 23 QQDIVEHVAAGHDALVLMPTGGGKSLCYQVPA---LLRDGCG----IVISP---LIAlmqdQV-EALRQLGvRAEFLNST 91
Cdd:COG0513 29 QAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLlqrLDPSRPRapqaLILAPtreLAL----QVaEELRKLA-KYLGLRVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 92 L-----DAETagrvERELLAGELDMLyVA-PerlltGRFLSLLSRSRIALFAI-----DEAhcvsqwghD------FRPE 154
Cdd:COG0513 104 TvyggvSIGR----QIRALKRGVDIV-VAtP-----GRLLDLIERGALDLSGVetlvlDEA--------DrmldmgFIED 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 155 YRQLtvlHERWPEIPRIAL-TATAdPPTQREIAERLdLAEARHfVS----SFDRPNIRYTVVQKDNARKQ--LSDFLRSH 227
Cdd:COG0513 166 IERI---LKLLPKERQTLLfSATM-PPEIRKLAKRY-LKNPVR-IEvapeNATAETIEQRYYLVDKRDKLelLRRLLRDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 228 RSEAGIVYCMSRRKVEETAEFLCTQGFNALPYHAGLPAEVRANNQRRFlREDGI-VMCAT-IAfGMGIDKPDVRFVAHTD 305
Cdd:COG0513 240 DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAF-RNGKIrVLVATdVA-ARGIDIDDVSHVINYD 317
|
330 340
....*....|....*....|....*
gi 647598048 306 LPKSMEgYYQ----ETGRAGRDGEA 326
Cdd:COG0513 318 LPEDPE-DYVhrigRTGRAGAEGTA 341
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
20-320 |
8.71e-13 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 71.21 E-value: 8.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 20 RGPQQDIVEHVAA-----GHDALVLMPTGGGKSL----CYQvpALLRDGCGIVISPLIALMQDQVEALRqlgvraEFLNS 90
Cdd:COG1061 82 RPYQQEALEALLAalergGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEELR------RFLGD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 91 TLDAETAGRVERELLAGELDMLYVAPERLLTGRFLSLLsrsrialfAIDEAHcvsqwgHDFRPEYRQLTvlhERWPEIPR 170
Cdd:COG1061 154 PLAGGGKKDSDAPITVATYQSLARRAHLDELGDRFGLV--------IIDEAH------HAGAPSYRRIL---EAFPAAYR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 171 IALTATADPPTQREIAE--------RLDLAEA--------RHFVS---SFDRPNIRYTVVQK----------DNARKQLS 221
Cdd:COG1061 217 LGLTATPFRSDGREILLflfdgivyEYSLKEAiedgylapPEYYGirvDLTDERAEYDALSErlrealaadaERKDKILR 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 222 DFLRSHRS-EAGIVYCMSRRKVEETAEFLCTQGFNALPYHAGLPAEVRANNQRRFLREDGIVMCATIAFGMGIDKPDVRF 300
Cdd:COG1061 297 ELLREHPDdRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDV 376
|
330 340
....*....|....*....|
gi 647598048 301 VAHTDLPKSMEGYYQETGRA 320
Cdd:COG1061 377 AILLRPTGSPREFIQRLGRG 396
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
8-324 |
6.11e-11 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 64.46 E-value: 6.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 8 DLLRRVFGYDdFRGP---QQDIVEHVAAGHDALVLMPTGGGKSLCYQVPALLR-----DGCGIVI-SPLIALMQDQVEAL 78
Cdd:PTZ00424 38 DLLRGIYSYG-FEKPsaiQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLidydlNACQALIlAPTRELAQQIQKVV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 79 RQLGvraEFLNSTLDAETAGRVERE----LLAGeLDMLYVAPER---LLTGRFLSLlsrSRIALFAIDEAHCVSQWG--- 148
Cdd:PTZ00424 117 LALG---DYLKVRCHACVGGTVVRDdinkLKAG-VHMVVGTPGRvydMIDKRHLRV---DDLKLFILDEADEMLSRGfkg 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 149 --HD-FR--PEYRQLTVLHERWP-EIPRIALTATADPPTQREIAERLDLAEARHFvssfdrpnirYTVVQKDNAR-KQLS 221
Cdd:PTZ00424 190 qiYDvFKklPPDVQVALFSATMPnEILELTTKFMRDPKRILVKKDELTLEGIRQF----------YVAVEKEEWKfDTLC 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 222 DFLRSHRSEAGIVYCMSRRKVEETAEFLCTQGFNALPYHAGLPAEVRANNQRRFLREDGIVMCATIAFGMGIDKPDVRFV 301
Cdd:PTZ00424 260 DLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLV 339
|
330 340
....*....|....*....|...
gi 647598048 302 AHTDLPKSMEGYYQETGRAGRDG 324
Cdd:PTZ00424 340 INYDLPASPENYIHRIGRSGRFG 362
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
528-599 |
1.63e-10 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 62.97 E-value: 1.63e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647598048 528 PQDLALFNALRGLRAELAREQNVPAFVIFHDSTLRNIAEQRPTSLDELARVGGIGGTKLSRYGPRLVEIVRE 599
Cdd:COG0349 207 PRQLAVLRELAAWREREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAVAE 278
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
32-324 |
1.89e-08 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 57.09 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 32 AGHDALVLMPTGGGKSLCYQVPA--------LLRDGCG---IVISPLIALMQDQVEALRQLGVRAEFLNSTLDAETAGRV 100
Cdd:PTZ00110 166 SGRDMIGIAETGSGKTLAFLLPAivhinaqpLLRYGDGpivLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRG 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 101 ERELLAGELDMLYVAPERLLTgrFL--SLLSRSRIALFAIDEA-------------HCVSQwghdFRPEyRQLTVLHERW 165
Cdd:PTZ00110 246 QIYALRRGVEILIACPGRLID--FLesNVTNLRRVTYLVLDEAdrmldmgfepqirKIVSQ----IRPD-RQTLMWSATW 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 166 P-EIPRIALTATADPPTQREIAErLDLAEARhfvssfdrpNIRYTV--VQKDNARKQLSDFLRSHRSEAG--IVYCMSRR 240
Cdd:PTZ00110 319 PkEVQSLARDLCKEEPVHVNVGS-LDLTACH---------NIKQEVfvVEEHEKRGKLKMLLQRIMRDGDkiLIFVETKK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 241 KVEETAEFLCTQGFNALPYHAGLPAEVRANNQRRFLREDGIVMCATIAFGMGIDKPDVRFVAHTDLPKSMEGYYQETGRA 320
Cdd:PTZ00110 389 GADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRT 468
|
....
gi 647598048 321 GRDG 324
Cdd:PTZ00110 469 GRAG 472
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
15-331 |
2.24e-07 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 53.70 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 15 GYDDFRGPQQDIVEHVAAGHDALVLMPTGGGKSLCYQVPAL------LRDGCGIVISPLIALMQDQVEA-------LRQL 81
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLhnldpeLKAPQILVLAPTRELAVQVAEAmtdfskhMRGV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 82 GVRAEFLNSTLDAE-TAGRVERELLAGeldmlyvAPERLLTGRFLSLLSRSRIALFAIDEAHCVSQWG--HDFRPEYRQL 158
Cdd:PRK11634 105 NVVALYGGQRYDVQlRALRQGPQIVVG-------TPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGfiEDVETIMAQI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 159 tvlherwPEIPRIALTATADPPTQREIAERL--DLAEARHFVSSFDRPNIR--YTVVQKDNARKQLSDFLRSHRSEAGIV 234
Cdd:PRK11634 178 -------PEGHQTALFSATMPEAIRRITRRFmkEPQEVRIQSSVTTRPDISqsYWTVWGMRKNEALVRFLEAEDFDAAII 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 235 YCMSRRKVEETAEFLCTQGFNALPYHAGLPAEVRANNQRRFlrEDGI--VMCATIAFGMGIDKPDVRFVAHTDLPKSMEG 312
Cdd:PRK11634 251 FVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERL--KDGRldILIATDVAARGLDVERISLVVNYDIPMDSES 328
|
330
....*....|....*....
gi 647598048 313 YYQETGRAGRDGEAAEAWL 331
Cdd:PRK11634 329 YVHRIGRTGRAGRAGRALL 347
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
22-197 |
2.52e-07 |
|
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: 51.11 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 22 PQQDIVEHVAAGHDALVL-MPTGGGKSLCYQ---VPALLRDGCGIV-ISPLIALMqDQVEalRQLGVRAEFLNSTLDAET 96
Cdd:cd17921 5 IQREALRALYLSGDSVLVsAPTSSGKTLIAElaiLRALATSGGKAVyIAPTRALV-NQKE--ADLRERFGPLGKNVGLLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 97 AGRVERELLAGELDMLYVAPERLLT-GRFLSLLSRSRIALFAIDEAHCVSQwghdfrPEY-----RQLTVLHERWPEIPR 170
Cdd:cd17921 82 GDPSVNKLLLAEADILVATPEKLDLlLRNGGERLIQDVRLVVVDEAHLIGD------GERgvvleLLLSRLLRINKNARF 155
|
170 180
....*....|....*....|....*..
gi 647598048 171 IALTATADPPtqREIAERLDLAEARHF 197
Cdd:cd17921 156 VGLSATLPNA--EDLAEWLGVEDLIRF 180
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
233-327 |
2.55e-07 |
|
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: 50.33 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 233 IVYCMSRRKVEETAEFLCT--QGFNALP-----YHAGLPAEVRANNQRRFLRED--GIVmcATIAFGMGIDKPDVRFVAH 303
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKArlVEEGPLAskvasYRAGYLAEDRREIEAELFNGEllGVV--ATNALELGIDIGGLDAVVL 116
|
90 100
....*....|....*....|....
gi 647598048 304 TDLPKSMEGYYQETGRAGRDGEAA 327
Cdd:cd18797 117 AGYPGSLASLWQQAGRAGRRGKDS 140
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
282-325 |
6.39e-07 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 47.31 E-value: 6.39e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 647598048 282 VMCATIAFGMGIDKPDVRFVAHTDLPKSMEGYYQETGRAGRDGE 325
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK 68
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
33-182 |
1.09e-06 |
|
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: 48.73 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 33 GHDALVLMPTGGGKSLCYQVPALLR------DGCGIV-ISPLIALMQDQVEALR------QLGVRAEFLNStldaETAGR 99
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSladepeKGVQVLyISPLKALINDQERRLEepldeiDLEIPVAVRHG----DTSQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 100 VERELLAGELDMLYVAPERLltgrFLSLLSRSRIALFA------IDEAHCV--SQWGhdfrpeyRQLTVLHERW-----P 166
Cdd:cd17922 77 EKAKQLKNPPGILITTPESL----ELLLVNKKLRELFAglryvvVDEIHALlgSKRG-------VQLELLLERLrkltgR 145
|
170
....*....|....*.
gi 647598048 167 EIPRIALTATADPPTQ 182
Cdd:cd17922 146 PLRRIGLSATLGNLEE 161
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
220-326 |
1.33e-05 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 48.01 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 220 LSDFLRSHRSEAGIVYCMSRRKVEETAEFLCTQGFNALPYHAGLPAEVRANNQRRFLREDGIVMCATIAFGMGIDKPDVR 299
Cdd:PRK11192 236 LCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVS 315
|
90 100 110
....*....|....*....|....*....|
gi 647598048 300 FVAHTDLPKSMEGYYQ---ETGRAGRDGEA 326
Cdd:PRK11192 316 HVINFDMPRSADTYLHrigRTGRAGRKGTA 345
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
23-120 |
4.06e-05 |
|
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: 44.97 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 23 QQDIVEHVAAGHDALVLMPTGGGKSLCYQVPALLR---------DGCG-IVISPLIALMQDQVEALRQLGVRAEFLNSTL 92
Cdd:cd17941 17 QRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKlyrerwtpeDGLGaLIISPTRELAMQIFEVLRKVGKYHSFSAGLI 96
|
90 100
....*....|....*....|....*...
gi 647598048 93 DAETAGRVERELLaGELDMLYVAPERLL 120
Cdd:cd17941 97 IGGKDVKEEKERI-NRMNILVCTPGRLL 123
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
22-190 |
5.26e-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: 44.25 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 22 PQQDIVEH-VAAGHDALVLMPTGGGKSLCYQ---VPALLRDGCGIVISPLIALMQDQVE---ALRQLGVRAEFlnSTLDA 94
Cdd:cd18028 5 PQAEAVRAgLLKGENLLISIPTASGKTLIAEmamVNTLLEGGKALYLVPLRALASEKYEefkKLEEIGLKVGI--STGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 95 EtagrvERELLAGELDMLYVAPErlltgRFLSLLsRSRIA------LFAIDEAHCVSQWGHDFRPEYrQLTVLHERWPEI 168
Cdd:cd18028 83 D-----EDDEWLGDYDIIVATYE-----KFDSLL-RHSPSwlrdvgVVVVDEIHLISDEERGPTLES-IVARLRRLNPNT 150
|
170 180
....*....|....*....|..
gi 647598048 169 PRIALTATADPPTqrEIAERLD 190
Cdd:cd18028 151 QIIGLSATIGNPD--ELAEWLN 170
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
233-324 |
6.80e-05 |
|
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: 43.31 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 233 IVYCMSRRKVEETAEFLCTQGFnalpYHAGLPAEVRANNQRRFlREDGI-VMCATIAFGMGIDKPdvrfvAHT------- 304
Cdd:cd18795 47 LVFCSSRKECEKTAKDLAGIAF----HHAGLTREDRELVEELF-REGLIkVLVATSTLAAGVNLP-----ARTviikgtq 116
|
90 100
....*....|....*....|....*...
gi 647598048 305 --------DLPKSMegYYQETGRAGRDG 324
Cdd:cd18795 117 rydgkgyrELSPLE--YLQMIGRAGRPG 142
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
19-142 |
9.61e-05 |
|
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: 43.96 E-value: 9.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 19 FRGPQQDIVEHVAAGHDALVLMPTGGGKS-----LC----YQVPAlLRDGCGIVISPLIALMQDQVEALRQLGVRAEFLN 89
Cdd:cd17927 3 PRNYQLELAQPALKGKNTIICLPTGSGKTfvavlICehhlKKFPA-GRKGKVVFLANKVPLVEQQKEVFRKHFERPGYKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 647598048 90 STLDAETAGRVERELLAGELDMLYVAPE----RLLTGRFLSLlsrSRIALFAIDEAH 142
Cdd:cd17927 82 TGLSGDTSENVSVEQIVESSDVIIVTPQilvnDLKSGTIVSL---SDFSLLVFDECH 135
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
226-353 |
1.32e-04 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 44.88 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 226 SHRSEAG-----IVYCMSRRKVEETAEFLctqGFNALPYHAGLPAEVRANNQRRFLREDGIVMCATIAFGMGIDKP--DV 298
Cdd:COG1202 419 DTKSSKGyrgqtIIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPasQV 495
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647598048 299 RFvahtD--------LpkSMEGYYQETGRAGRDGeaaeawlcY-GLGDVVLL----KQMIEQSEASEE 353
Cdd:COG1202 496 IF----DslamgiewL--SVQEFHQMLGRAGRPD--------YhDRGKVYLLvepgKSYHRSMEMTED 549
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
41-204 |
2.31e-03 |
|
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.
Pssm-ID: 350784 [Multi-domain] Cd Length: 202 Bit Score: 39.51 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 41 PTGGGKSLCYQVPALLRDGC----GIVISPLIALMQDQVEALRQLGVRAEFLNSTL--DAETAGRVERellaGELDMLYV 114
Cdd:cd18026 41 PTSGGKTLVAEILMLKRLLErrkkALFVLPYVSIVQEKVDALSPLFEELGFRVEGYagNKGRSPPKRR----KSLSVAVC 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 115 APERL--LTGRFLSLLSRSRIALFAIDEAHCVsqwGHDFRPEYRQLT---VLHERWPEIPRIALTATAdpPTQREIAERL 189
Cdd:cd18026 117 TIEKAnsLVNSLIEEGRLDELGLVVVDELHML---GDGHRGALLELLltkLLYAAQKNIQIVGMSATL--PNLEELASWL 191
|
170
....*....|....*
gi 647598048 190 DlaeARHFVSSFdRP 204
Cdd:cd18026 192 R---AELYTTNF-RP 202
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
8-141 |
5.23e-03 |
|
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: 38.46 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 8 DLLRRVFGYDdFRGP---QQDIVEHVAAGHDALVLMPTGGGKSLCYQVPALLR------DGCGIVISPLIALMQDQVEAL 78
Cdd:cd17939 7 DLLRGIYAYG-FEKPsaiQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRidttvrETQALVLAPTRELAQQIQKVV 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647598048 79 RQLGvraEFLNSTLDAETAG---RVERELLAGELDMLYVAPerlltGRFLSLLSRSR-----IALFAIDEA 141
Cdd:cd17939 86 KALG---DYMGVKVHACIGGtsvREDRRKLQYGPHIVVGTP-----GRVFDMLQRRSlrtdkIKMFVLDEA 148
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
8-329 |
8.26e-03 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 39.02 E-value: 8.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 8 DLLRRVF--GYDDFRGPQQDIVEHVAAGHDALVLMPTGGGKSLCYQVPALLRdgcgivispliaLMQDQVEALRQLGVRA 85
Cdd:PRK10590 11 DILRAVAeqGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQH------------LITRQPHAKGRRPVRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 86 EFLNST--LDAETAGRVE--------REL--------------LAGELDMLYVAPERLLTGRFLSLLSRSRIALFAIDEA 141
Cdd:PRK10590 79 LILTPTreLAAQIGENVRdyskylniRSLvvfggvsinpqmmkLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 142 HCVSQWG--HDFR------PEYRQLTVLHERWP-EIPRIAlTATADPPTQREIAERLDLAEA----RHFVSsfdrpniry 208
Cdd:PRK10590 159 DRMLDMGfiHDIRrvlaklPAKRQNLLFSATFSdDIKALA-EKLLHNPLEIEVARRNTASEQvtqhVHFVD--------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647598048 209 tvvqKDNARKQLSDFLRSHRSEAGIVYCMSRRKVEETAEFLCTQGFNALPYHAGLPAEVRANNQRRFLREDGIVMCATIA 288
Cdd:PRK10590 229 ----KKRKRELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDI 304
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 647598048 289 FGMGIDKPDVRFVAHTDLPKSMEGYYQETGRAGRDGEAAEA 329
Cdd:PRK10590 305 AARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEA 345
|
|
| |
