|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
1-483 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 841.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 1 MREQALRILKDVFGYDAFRGNQARIIERVAEGGDALVLMPTGGGKSLCFQVPALLREGLTVVVSPLIALMEDQVATLDEL 80
Cdd:COG0514 1 LRDDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 81 GVPAVALNSTLNPEQQRDIAERLQRGEIKLLYLAPERLVQPRMLAFLQRLPVGLFAIDEAHCVSQWGHDFRPEYLQLGQL 160
Cdd:COG0514 81 GIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 161 AELFPQVPRIALTATADMRTREEMIQRLHLQNAEQFLSSFDRPNIFYRIVPK--EQPRKQLLGFLSERRGDAGIVYCLSR 238
Cdd:COG0514 161 RERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKppDDKLAQLLDFLKEHPGGSGIVYCLSR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 239 KKVEEVAEFLGNQGFPALPYHAGLSNELRAHHQKRFLNEEGLIMVATIAFGMGIDKPNVRFVAHLDLPKSLEAYYQETGR 318
Cdd:COG0514 241 KKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 319 AGRDGLPADAWMAYGLQDVLLLRQMMQSSEGDERHKRVERHKLEAMLALCEETRCRRQALLAYFDEEMPQPCGHCDNCVD 398
Cdd:COG0514 321 AGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFGEELAEPCGNCDNCLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 399 GVETWDATESARQALSAIYRSGQRYGVGHLVDILLGRETEKIRSLGHQHLAVFGIGKGRGEDEWRTLFRQLVARGLADVD 478
Cdd:COG0514 401 PPETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLLAQLFGERK 480
|
....*
gi 489182275 479 LDGFG 483
Cdd:COG0514 481 LERYG 485
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
8-597 |
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: 825.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 8 ILKDVFGYDAFRGNQARIIERVAEGGDALVLMPTGGGKSLCFQVPALLREGLTVVVSPLIALMEDQVATLDELGVPAVAL 87
Cdd:TIGR01389 4 VLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAAAYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 88 NSTLNPEQQRDIAERLQRGEIKLLYLAPERLVQPRMLAFLQRLPVGLFAIDEAHCVSQWGHDFRPEYLQLGQLAELFPQV 167
Cdd:TIGR01389 84 NSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERFPQV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 168 PRIALTATADMRTREEMIQRLHLQNAEQFLSSFDRPNIFYRIVPKEQPRKQLLGFLSERRGDAGIVYCLSRKKVEEVAEF 247
Cdd:TIGR01389 164 PRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEELAER 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 248 LGNQGFPALPYHAGLSNELRAHHQKRFLNEEGLIMVATIAFGMGIDKPNVRFVAHLDLPKSLEAYYQETGRAGRDGLPAD 327
Cdd:TIGR01389 244 LESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDGLPAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 328 AWMAYGLQDVLLLRQMMQSSEGDERHKRVERHKLEAMLALCEETRCRRQALLAYFDEEMPQPCGHCDNCVDGVETWDATE 407
Cdd:TIGR01389 324 AILLYSPADIALLKRRIEQSEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENEVEPCGNCDNCLDPPKSYDATV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 408 SARQALSAIYRSGQRYGVGHLVDILLGRETEKIRSLGHQHLAVFGIGKGRGEDEWRTLFRQLVARGLADVDLDGFGGLRL 487
Cdd:TIGR01389 404 EAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIYIGLQL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 488 TEACRPLLRGEVRLELRRDlkpqraKGSSSGGASAASQLVRSEEREMWEALRALRRKLAEEHSVPPYVIFPDATLLEMLR 567
Cdd:TIGR01389 484 TEAARKVLKNEVEVLLRPF------KVVAKEKTRVQKNLSVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAE 557
|
570 580 590
....*....|....*....|....*....|
gi 489182275 568 SQPRSLSDMAQVSGVGARKLERYGQAFLDV 597
Cdd:TIGR01389 558 KRPATLNALLKIKGVGQNKLDRYGEAFLEV 587
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
4-600 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 686.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 4 QALRILKDVFGYDAFRGNQARIIERVAEGGDALVLMPTGGGKSLCFQVPALLREGLTVVVSPLIALMEDQVATLDELGVP 83
Cdd:PRK11057 12 LAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 84 AVALNSTLNPEQQRDIAERLQRGEIKLLYLAPERLVQPRMLAFLQRLPVGLFAIDEAHCVSQWGHDFRPEYLQLGQLAEL 163
Cdd:PRK11057 92 AACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 164 FPQVPRIALTATADMRTREEMIQRLHLQNAEQFLSSFDRPNIFYRIVPKEQPRKQLLGFLSERRGDAGIVYCLSRKKVEE 243
Cdd:PRK11057 172 FPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVED 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 244 VAEFLGNQGFPALPYHAGLSNELRAHHQKRFLNEEGLIMVATIAFGMGIDKPNVRFVAHLDLPKSLEAYYQETGRAGRDG 323
Cdd:PRK11057 252 TAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 324 LPADAWMAYGLQDVLLLRQMMQSSEGDERhKRVERHKLEAMLALCEETRCRRQALLAYFDEEMPQPCGHCDNCVDGVETW 403
Cdd:PRK11057 332 LPAEAMLFYDPADMAWLRRCLEEKPAGQQ-QDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNCDICLDPPKQY 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 404 DATESARQALSAIYRSGQRYGVGHLVDILLGRETEKIRSLGHQHLAVFGIGKGRGEDEWRTLFRQLVARGLADVDLDGFG 483
Cdd:PRK11057 411 DGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQNIAQHS 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 484 GLRLTEACRPLLRGEVRLELR--RDLKPQRAKGSSSGGasaasqlvRSEEREMWEALRALRRKLAEEHSVPPYVIFPDAT 561
Cdd:PRK11057 491 ALQLTEAARPVLRGEVSLQLAvpRIVALKPRAMQKSFG--------GNYDRKLFAKLRKLRKSIADEENIPPYVVFNDAT 562
|
570 580 590
....*....|....*....|....*....|....*....
gi 489182275 562 LLEMLRSQPRSLSDMAQVSGVGARKLERYGQAFLDVLTD 600
Cdd:PRK11057 563 LIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMALIRA 601
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
6-201 |
1.54e-103 |
|
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: 314.47 E-value: 1.54e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 6 LRILKDVFGYDAFRGNQARIIERVAEGGDALVLMPTGGGKSLCFQVPALLREGLTVVVSPLIALMEDQVATLDELGVPAV 85
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 86 ALNSTLNPEQQRDIAERLQRGEIKLLYLAPERLVQPRMLAFLQRLP----VGLFAIDEAHCVSQWGHDFRPEYLQLGQLA 161
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489182275 162 ELFPQVPRIALTATADMRTREEMIQRLHLQNAEQFLSSFD 201
Cdd:cd17920 161 RALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DpdF |
NF041063 |
protein DpdF; |
8-343 |
2.29e-42 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 165.08 E-value: 2.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 8 ILKDVFGYDAFRGN-QARIIERV--AEGGDALVL-MPTGGGKSLCFQVPALL---REGLTVVVSPLIAL---MEDQVATL 77
Cdd:NF041063 130 FLAEALGFTHYRSPgQREAVRAAllAPPGSTLIVnLPTGSGKSLVAQAPALLasrQGGLTLVVVPTVALaidQERRAREL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 78 ----DELGVPAVALNSTLNPEQQRDIAERLQRGEIKLLYLAPERLVQP-----RMLAFLQRLpvGLFAIDEAHCVSQWGH 148
Cdd:NF041063 210 lrraGPDLGGPLAWHGGLSAEERAAIRQRIRDGTQRILFTSPESLTGSlrpalFDAAEAGLL--RYLVVDEAHLVDQWGD 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 149 DFRPEYLQL-GQLAELF-----PQVPR-IALTATADMRTReEMIQRL--HLQNAEQFLSSFDRPNI---FYRIVPKEQPR 216
Cdd:NF041063 288 GFRPEFQLLaGLRRSLLrlapsGRPFRtLLLSATLTESTL-DTLETLfgPPGPFIVVSAVQLRPEPaywVAKCDSEEERR 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 217 KQLLGFLSERRGDAgIVYCLSRKKVEEVAEFLGNQGFPALP-YHAGLSNELRaHHQKRFLNEEGL-IMVATIAFGMGIDK 294
Cdd:NF041063 367 ERVLEALRHLPRPL-ILYVTKVEDAEAWLQRLRAAGFRRVAlFHGDTPDAER-ERLIEQWRENELdIVVATSAFGLGMDK 444
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 489182275 295 PNVRFVAHLDLPKSLEAYYQETGRAGRDGLPADAWMAYGLQDVLLLRQM 343
Cdd:NF041063 445 SDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDIAKSL 493
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
400-506 |
4.90e-41 |
|
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: 145.37 E-value: 4.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 400 VETWDATESARQALSAIYRSGQRYGVGHLVDILLGRETEKIRSLGHQHLAVFGIGKGRGEDEWRTLFRQLVARGLADVDL 479
Cdd:pfam09382 2 PETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVDI 81
|
90 100
....*....|....*....|....*..
gi 489182275 480 DGFGGLRLTEACRPLLRGEVRLELRRD 506
Cdd:pfam09382 82 EFYSVLKLTPKAREVLKGEEKVMLRVP 108
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
404-495 |
1.14e-35 |
|
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: 129.52 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 404 DATESARQALSAIYRSGQRYGVGHLVDILLGRETEKIRSLGHQHLAVFGIGKGRGEDEWRTLFRQLVARGLADVDLDGFG 483
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYP 80
|
90
....*....|..
gi 489182275 484 GLRLTEACRPLL 495
Cdd:smart00956 81 YLKLTEKARPVL 92
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
531-598 |
5.35e-19 |
|
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: 81.43 E-value: 5.35e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489182275 531 EREMWEALRALRRKLAEEHSVPPYVIFPDATLLEMLRSQPRSLSDMAQVSGVGARKLERYGQAFLDVL 598
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
528-598 |
8.35e-17 |
|
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: 75.41 E-value: 8.35e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489182275 528 RSEEREMWEALRALRRKLAEEHSVPPYVIFPDATLLEMLRSQPRSLSDMAQVSGVGARKLERYGQAFLDVL 598
Cdd:smart00341 1 RERQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVI 71
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
528-598 |
5.94e-06 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 49.10 E-value: 5.94e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489182275 528 RSEEREMWEALRALRRKLAEEHSVPPYVIFPDATLLEMLRSQPRSLSDMAQVSGVGARKLERYGQAFLDVL 598
Cdd:COG0349 206 NPRQLAVLRELAAWREREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAV 276
|
|
| HTH_40 |
pfam14493 |
Helix-turn-helix domain; This presumed domain is found at the C-terminus of a large number of ... |
623-703 |
6.48e-04 |
|
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: 39.03 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 623 GMTPAQIARQLNCSEKNVYAMLAEAI-AGQQVSLEQAldLPEELLGEIQDAFLE-EDGELPPvaaLEERFGKRVPSGVLH 700
Cdd:pfam14493 12 GLSIEEIAEERGLKESTIEGHLAELIeAGEPVDIERL--VSEEEQKEILDAIEKlGSESLKP---IKEALPEEISYFEIR 86
|
...
gi 489182275 701 CVR 703
Cdd:pfam14493 87 LVL 89
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
1-483 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 841.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 1 MREQALRILKDVFGYDAFRGNQARIIERVAEGGDALVLMPTGGGKSLCFQVPALLREGLTVVVSPLIALMEDQVATLDEL 80
Cdd:COG0514 1 LRDDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 81 GVPAVALNSTLNPEQQRDIAERLQRGEIKLLYLAPERLVQPRMLAFLQRLPVGLFAIDEAHCVSQWGHDFRPEYLQLGQL 160
Cdd:COG0514 81 GIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 161 AELFPQVPRIALTATADMRTREEMIQRLHLQNAEQFLSSFDRPNIFYRIVPK--EQPRKQLLGFLSERRGDAGIVYCLSR 238
Cdd:COG0514 161 RERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKppDDKLAQLLDFLKEHPGGSGIVYCLSR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 239 KKVEEVAEFLGNQGFPALPYHAGLSNELRAHHQKRFLNEEGLIMVATIAFGMGIDKPNVRFVAHLDLPKSLEAYYQETGR 318
Cdd:COG0514 241 KKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 319 AGRDGLPADAWMAYGLQDVLLLRQMMQSSEGDERHKRVERHKLEAMLALCEETRCRRQALLAYFDEEMPQPCGHCDNCVD 398
Cdd:COG0514 321 AGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFGEELAEPCGNCDNCLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 399 GVETWDATESARQALSAIYRSGQRYGVGHLVDILLGRETEKIRSLGHQHLAVFGIGKGRGEDEWRTLFRQLVARGLADVD 478
Cdd:COG0514 401 PPETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLLAQLFGERK 480
|
....*
gi 489182275 479 LDGFG 483
Cdd:COG0514 481 LERYG 485
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
8-597 |
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: 825.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 8 ILKDVFGYDAFRGNQARIIERVAEGGDALVLMPTGGGKSLCFQVPALLREGLTVVVSPLIALMEDQVATLDELGVPAVAL 87
Cdd:TIGR01389 4 VLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAAAYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 88 NSTLNPEQQRDIAERLQRGEIKLLYLAPERLVQPRMLAFLQRLPVGLFAIDEAHCVSQWGHDFRPEYLQLGQLAELFPQV 167
Cdd:TIGR01389 84 NSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERFPQV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 168 PRIALTATADMRTREEMIQRLHLQNAEQFLSSFDRPNIFYRIVPKEQPRKQLLGFLSERRGDAGIVYCLSRKKVEEVAEF 247
Cdd:TIGR01389 164 PRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEELAER 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 248 LGNQGFPALPYHAGLSNELRAHHQKRFLNEEGLIMVATIAFGMGIDKPNVRFVAHLDLPKSLEAYYQETGRAGRDGLPAD 327
Cdd:TIGR01389 244 LESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDGLPAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 328 AWMAYGLQDVLLLRQMMQSSEGDERHKRVERHKLEAMLALCEETRCRRQALLAYFDEEMPQPCGHCDNCVDGVETWDATE 407
Cdd:TIGR01389 324 AILLYSPADIALLKRRIEQSEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENEVEPCGNCDNCLDPPKSYDATV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 408 SARQALSAIYRSGQRYGVGHLVDILLGRETEKIRSLGHQHLAVFGIGKGRGEDEWRTLFRQLVARGLADVDLDGFGGLRL 487
Cdd:TIGR01389 404 EAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIYIGLQL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 488 TEACRPLLRGEVRLELRRDlkpqraKGSSSGGASAASQLVRSEEREMWEALRALRRKLAEEHSVPPYVIFPDATLLEMLR 567
Cdd:TIGR01389 484 TEAARKVLKNEVEVLLRPF------KVVAKEKTRVQKNLSVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAE 557
|
570 580 590
....*....|....*....|....*....|
gi 489182275 568 SQPRSLSDMAQVSGVGARKLERYGQAFLDV 597
Cdd:TIGR01389 558 KRPATLNALLKIKGVGQNKLDRYGEAFLEV 587
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
4-600 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 686.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 4 QALRILKDVFGYDAFRGNQARIIERVAEGGDALVLMPTGGGKSLCFQVPALLREGLTVVVSPLIALMEDQVATLDELGVP 83
Cdd:PRK11057 12 LAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 84 AVALNSTLNPEQQRDIAERLQRGEIKLLYLAPERLVQPRMLAFLQRLPVGLFAIDEAHCVSQWGHDFRPEYLQLGQLAEL 163
Cdd:PRK11057 92 AACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 164 FPQVPRIALTATADMRTREEMIQRLHLQNAEQFLSSFDRPNIFYRIVPKEQPRKQLLGFLSERRGDAGIVYCLSRKKVEE 243
Cdd:PRK11057 172 FPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVED 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 244 VAEFLGNQGFPALPYHAGLSNELRAHHQKRFLNEEGLIMVATIAFGMGIDKPNVRFVAHLDLPKSLEAYYQETGRAGRDG 323
Cdd:PRK11057 252 TAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 324 LPADAWMAYGLQDVLLLRQMMQSSEGDERhKRVERHKLEAMLALCEETRCRRQALLAYFDEEMPQPCGHCDNCVDGVETW 403
Cdd:PRK11057 332 LPAEAMLFYDPADMAWLRRCLEEKPAGQQ-QDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNCDICLDPPKQY 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 404 DATESARQALSAIYRSGQRYGVGHLVDILLGRETEKIRSLGHQHLAVFGIGKGRGEDEWRTLFRQLVARGLADVDLDGFG 483
Cdd:PRK11057 411 DGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQNIAQHS 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 484 GLRLTEACRPLLRGEVRLELR--RDLKPQRAKGSSSGGasaasqlvRSEEREMWEALRALRRKLAEEHSVPPYVIFPDAT 561
Cdd:PRK11057 491 ALQLTEAARPVLRGEVSLQLAvpRIVALKPRAMQKSFG--------GNYDRKLFAKLRKLRKSIADEENIPPYVVFNDAT 562
|
570 580 590
....*....|....*....|....*....|....*....
gi 489182275 562 LLEMLRSQPRSLSDMAQVSGVGARKLERYGQAFLDVLTD 600
Cdd:PRK11057 563 LIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMALIRA 601
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
8-455 |
1.43e-175 |
|
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: 510.08 E-value: 1.43e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 8 ILKDVFGYDAFRGNQARIIERVAEGGDALVLMPTGGGKSLCFQVPALLREGLTVVVSPLIALMEDQVATLDELGVPAVAL 87
Cdd:TIGR00614 2 ILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 88 NSTLNPEQQRDIAERLQRGEIKLLYLAPERLVQPRMlaFLQRLP----VGLFAIDEAHCVSQWGHDFRPEYLQLGQLAEL 163
Cdd:TIGR00614 82 NSAQTKEQQLNVLTDLKDGKIKLLYVTPEKISASNR--LLQTLEerkgITLIAVDEAHCISQWGHDFRPDYKALGSLKQK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 164 FPQVPRIALTATADMRTREEMIQRLHLQNAEQFLSSFDRPNIFYRIVPK-EQPRKQLLGFL-SERRGDAGIVYCLSRKKV 241
Cdd:TIGR00614 160 FPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKtPKILEDLLRFIrKEFEGKSGIIYCPSRKKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 242 EEVAEFLGNQGFPALPYHAGLSNELRAHHQKRFLNEEGLIMVATIAFGMGIDKPNVRFVAHLDLPKSLEAYYQETGRAGR 321
Cdd:TIGR00614 240 EQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 322 DGLPADAWMAYGLQDVLLLRQMMQsSEGDERHKRVERHKLEAMLALCEETRCRRQALLAYFDEEMPQ----------PCG 391
Cdd:TIGR00614 320 DGLPSECHLFYAPADMNRLRRLLM-EEPDGNFRTYKLKLYEMMEYCLNSSTCRRLILLSYFGEKGFNksfcimgtekCCD 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 392 HCDNCVDGV------ETWDATESARQALSAIYRSGQRYGVGHLVDILLGRETEKIRSLGHQHLAVFGIGK 455
Cdd:TIGR00614 399 NCCKRLDYKtkdvtdKVYDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGRGK 468
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
10-598 |
2.41e-115 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 374.62 E-value: 2.41e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 10 KDVFGYDAFRGNQARIIERVAEGGDALVLMPTGGGKSLCFQVPALLREGLTVVVSPLIALMEDQVATLDELGVPAVALNS 89
Cdd:PLN03137 453 KKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSA 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 90 TLNPEQQRDIAERL--QRGEIKLLYLAPERLVQP----RMLAFLQ-RLPVGLFAIDEAHCVSQWGHDFRPEYLQLGQLAE 162
Cdd:PLN03137 533 GMEWAEQLEILQELssEYSKYKLLYVTPEKVAKSdsllRHLENLNsRGLLARFVIDEAHCVSQWGHDFRPDYQGLGILKQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 163 LFPQVPRIALTATADMRTREEMIQRLHLQNAEQFLSSFDRPNIFYRIVPKEqpRKQLLG---FLSERRGD-AGIVYCLSR 238
Cdd:PLN03137 613 KFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKT--KKCLEDidkFIKENHFDeCGIIYCLSR 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 239 KKVEEVAEFLGNQGFPALPYHAGLSNELRAHHQKRFLNEEGLIMVATIAFGMGIDKPNVRFVAHLDLPKSLEAYYQETGR 318
Cdd:PLN03137 691 MDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGR 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 319 AGRDGLPADAWMAYGLQDVLLLRQMM--------QSSEGDERHKRVER------HKLEAMLALCE-ETRCRRQALLAYFD 383
Cdd:PLN03137 771 AGRDGQRSSCVLYYSYSDYIRVKHMIsqggveqsPMAMGYNRMASSGRiletntENLLRMVSYCEnEVDCRRFLQLVHFG 850
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 384 EEMPQP-CGH-CDNCVDG---VETwDATESARQALSAIYRSGQRYGVGHLVDILLGRETEKIRSLGHQHLAVFGIGKGRG 458
Cdd:PLN03137 851 EKFDSTnCKKtCDNCSSSkslIDK-DVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSLHGAGKHLS 929
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 459 EDEWRTLFRQLVARGLADVDL---DGFGG----LRLTEA-CRPLLRGEVRLELR-----RDLKPQR-----AKGSSSGGA 520
Cdd:PLN03137 930 KGEASRILHYLVTEDILAEDVkksDLYGSvsslLKVNESkAYKLFSGGQTIIMRfpssvKASKPSKfeatpAKGPLTSGK 1009
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 521 SAASQLVRSEERE--------MWEALRALRRKLAEEHS--VPPYVIFPDATLLEMLRSQPRSLSDMAQVSGVGARKLERY 590
Cdd:PLN03137 1010 QSTLPMATPAQPPvdlnlsaiLYTALRKLRTALVKEAGdgVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAKVSKY 1089
|
....*...
gi 489182275 591 GQAFLDVL 598
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 ... |
6-201 |
1.54e-103 |
|
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: 314.47 E-value: 1.54e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 6 LRILKDVFGYDAFRGNQARIIERVAEGGDALVLMPTGGGKSLCFQVPALLREGLTVVVSPLIALMEDQVATLDELGVPAV 85
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 86 ALNSTLNPEQQRDIAERLQRGEIKLLYLAPERLVQPRMLAFLQRLP----VGLFAIDEAHCVSQWGHDFRPEYLQLGQLA 161
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489182275 162 ELFPQVPRIALTATADMRTREEMIQRLHLQNAEQFLSSFD 201
Cdd:cd17920 161 RALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
6-192 |
1.87e-72 |
|
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: 233.69 E-value: 1.87e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 6 LRILKDVFGYDAFRGNQARIIERVAEGGDALVLMPTGGGKSLCFQVPALLRE----GLTVVVSPLIALMEDQVATLdELG 81
Cdd:cd18018 1 LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRrrgpGLTLVVSPLIALMKDQVDAL-PRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 82 VPAVALNSTLNPEQQRDIAERLQRGEIKLLYLAPERLVQPRMLAFL-QRLPVGLFAIDEAHCVSQWGHDFRPEYLQLGQL 160
Cdd:cd18018 80 IKAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLrQTPPISLLVVDEAHCISEWSHNFRPDYLRLCRV 159
|
170 180 190
....*....|....*....|....*....|...
gi 489182275 161 AELFPQVPRI-ALTATADMRTREEMIQRLHLQN 192
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 ... |
3-201 |
1.20e-67 |
|
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: 221.09 E-value: 1.20e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 3 EQALRILKDVFGYDAFRGNQARIIERVAEGGDALVLMPTGGGKSLCFQVPALLREGLTVVVSPLIALMEDQVATLDELGV 82
Cdd:cd18015 4 GKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 83 PAVALNSTLNPEQQRDIAERLQRG--EIKLLYLAPERLVQP-RMLAFLQR-LPVG---LFAIDEAHCVSQWGHDFRPEYL 155
Cdd:cd18015 84 SATMLNASSSKEHVKWVHAALTDKnsELKLLYVTPEKIAKSkRFMSKLEKaYNAGrlaRIAIDEVHCCSQWGHDFRPDYK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489182275 156 QLGQLAELFPQVPRIALTATADMRTREEMIQRLHLQNAEQFLSSFD 201
Cdd:cd18015 164 KLGILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
1-201 |
8.73e-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: 205.45 E-value: 8.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 1 MREQALRILKDVFGYDAFRGNQARIIERVAEGGDALVLMPTGGGKSLCFQVPALLREGLTVVVSPLIALMEDQVATLDEL 80
Cdd:cd18016 1 HSKEMMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 81 GVPAVALNSTLNPEQQRDIAERLQRGE--IKLLYLAPERL-VQPRMLAFLQRLP----VGLFAIDEAHCVSQWGHDFRPE 153
Cdd:cd18016 81 DIPATYLTGDKTDAEATKIYLQLSKKDpiIKLLYVTPEKIsASNRLISTLENLYerklLARFVIDEAHCVSQWGHDFRPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489182275 154 YLQLGQLAELFPQVPRIALTATADMRTREEMIQRLHLQNAEQFLSSFD 201
Cdd:cd18016 161 YKRLNMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
9-201 |
2.49e-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: 2.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 9 LKDVFGYDAFRGNQARIIERVAEGG-DALVLMPTGGGKSLCFQVPALLREGLTVVVSPLIALMEDQVATLDELGVPAVAL 87
Cdd:cd18017 4 LNEYFGHSSFRPVQWKVIRSVLEERrDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 88 NStlnpEQQRDIAERLQRGEIKLLYLAPErLVQpRMLAFLQ--RLPVGLFAIDEAHCVSQWGHDFRPEYLQLGQLAELFP 165
Cdd:cd18017 84 GS----AQSQNVLDDIKMGKIRVIYVTPE-FVS-KGLELLQqlRNGITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRLP 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 489182275 166 QVPRIALTATADMRTREEMIQRLHLQNAEQFLSSFD 201
Cdd:cd18017 158 NVPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
202-332 |
4.11e-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: 187.42 E-value: 4.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 202 RPNIFYRIVPKEQPRKQLLG---FLSERRGDAGIVYCLSRKKVEEVAEFLGNQGFPALPYHAGLSNELRAHHQKRFLNEE 278
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLlkrIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 489182275 279 GLIMVATIAFGMGIDKPNVRFVAHLDLPKSLEAYYQETGRAGRDGLPADAWMAY 332
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 ... |
6-196 |
2.98e-54 |
|
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: 184.98 E-value: 2.98e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 6 LRILKDVFGYDAFRGN-QARIIERVAEG-GDALVLMPTGGGKSLCFQVPALLREGLTVVVSPLIALMEDQVATLDELGVP 83
Cdd:cd18014 1 RSTLKKVFGHSDFKSPlQEKATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 84 AVALNSTLNPEQQRDIAERLQRG--EIKLLYLAPERL----VQPRMLAFLQRLPVGLFAIDEAHCVSQWGHDFRPEYLQL 157
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADLESEkpQTKFLYITPEMAatssFQPLLSSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489182275 158 GQLAELFPQVPRIALTATADMRTREEMIQRLHL-QNAEQF 196
Cdd:cd18014 161 GALRSRYGHVPWVALTATATPQVQEDIFAQLRLkKPVAIF 200
|
|
| DpdF |
NF041063 |
protein DpdF; |
8-343 |
2.29e-42 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 165.08 E-value: 2.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 8 ILKDVFGYDAFRGN-QARIIERV--AEGGDALVL-MPTGGGKSLCFQVPALL---REGLTVVVSPLIAL---MEDQVATL 77
Cdd:NF041063 130 FLAEALGFTHYRSPgQREAVRAAllAPPGSTLIVnLPTGSGKSLVAQAPALLasrQGGLTLVVVPTVALaidQERRAREL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 78 ----DELGVPAVALNSTLNPEQQRDIAERLQRGEIKLLYLAPERLVQP-----RMLAFLQRLpvGLFAIDEAHCVSQWGH 148
Cdd:NF041063 210 lrraGPDLGGPLAWHGGLSAEERAAIRQRIRDGTQRILFTSPESLTGSlrpalFDAAEAGLL--RYLVVDEAHLVDQWGD 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 149 DFRPEYLQL-GQLAELF-----PQVPR-IALTATADMRTReEMIQRL--HLQNAEQFLSSFDRPNI---FYRIVPKEQPR 216
Cdd:NF041063 288 GFRPEFQLLaGLRRSLLrlapsGRPFRtLLLSATLTESTL-DTLETLfgPPGPFIVVSAVQLRPEPaywVAKCDSEEERR 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 217 KQLLGFLSERRGDAgIVYCLSRKKVEEVAEFLGNQGFPALP-YHAGLSNELRaHHQKRFLNEEGL-IMVATIAFGMGIDK 294
Cdd:NF041063 367 ERVLEALRHLPRPL-ILYVTKVEDAEAWLQRLRAAGFRRVAlFHGDTPDAER-ERLIEQWRENELdIVVATSAFGLGMDK 444
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 489182275 295 PNVRFVAHLDLPKSLEAYYQETGRAGRDGLPADAWMAYGLQDVLLLRQM 343
Cdd:NF041063 445 SDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDIAKSL 493
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
400-506 |
4.90e-41 |
|
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: 145.37 E-value: 4.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 400 VETWDATESARQALSAIYRSGQRYGVGHLVDILLGRETEKIRSLGHQHLAVFGIGKGRGEDEWRTLFRQLVARGLADVDL 479
Cdd:pfam09382 2 PETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVDI 81
|
90 100
....*....|....*....|....*..
gi 489182275 480 DGFGGLRLTEACRPLLRGEVRLELRRD 506
Cdd:pfam09382 82 EFYSVLKLTPKAREVLKGEEKVMLRVP 108
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
404-495 |
1.14e-35 |
|
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: 129.52 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 404 DATESARQALSAIYRSGQRYGVGHLVDILLGRETEKIRSLGHQHLAVFGIGKGRGEDEWRTLFRQLVARGLADVDLDGFG 483
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYP 80
|
90
....*....|..
gi 489182275 484 GLRLTEACRPLL 495
Cdd:smart00956 81 YLKLTEKARPVL 92
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
22-177 |
1.95e-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: 106.17 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 22 QARIIERVAEGGDALVLMPTGGGKSLCFQVPAL------LREGLTVVVSPLIALMEDQVATLDELGVP-AVALNSTLNPE 94
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGlGLKVASLLGGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 95 QQRDIAERLQRGEIklLYLAPERLVQprMLAFLQRLP-VGLFAIDEAHCVSQWGhdFRPEYLQLgqLAELFPQVPRIALT 173
Cdd:pfam00270 84 SRKEQLEKLKGPDI--LVGTPGRLLD--LLQERKLLKnLKLLVLDEAHRLLDMG--FGPDLEEI--LRRLPKKRQILLLS 155
|
....
gi 489182275 174 ATAD 177
Cdd:pfam00270 156 ATLP 159
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
13-210 |
1.22e-23 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 99.10 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 13 FGYDAFRGNQARIIERVAEG-GDALVLMPTGGGKSLCFQVPALLR-----EGLTVVVSPLIALMEDQVATLDELGVPAVA 86
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 87 LNSTL-NPEQQRDIAERLQRGEIKLLYLAPERLVQPRMLAFLQRLPVGLFAIDEAHCVSQWGhdFRPEYLQLgqLAELFP 165
Cdd:smart00487 84 KVVGLyGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKL--LKLLPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489182275 166 QVPRIALTATadMRTREEMIQRLHLQNaEQFLSSFDRPNIFYRIV 210
Cdd:smart00487 160 NVQLLLLSAT--PPEEIENLLELFLND-PVFIDVGFTPLEPIEQF 201
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
334-396 |
1.57e-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: 94.28 E-value: 1.57e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489182275 334 LQDVLLLRQMMQSSEGDERHKRVERHKLEAMLALCEET-RCRRQALLAYFDEE-MPQPCGHCDNC 396
Cdd:pfam16124 1 YQDVVRLRFLIEQSEADEERKEVELQKLQAMVAYCENTtDCRRKQLLRYFGEEfDSEPCGNCDNC 65
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
242-323 |
1.33e-20 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 86.50 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 242 EEVAEFLGNQGFPALPYHAGLSNELRAHHQKRFLNEEGLIMVATIAFGMGIDKPNVRFVAHLDLPKSLEAYYQETGRAGR 321
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 489182275 322 DG 323
Cdd:smart00490 81 AG 82
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
219-323 |
7.09e-20 |
|
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: 85.34 E-value: 7.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 219 LLGFLSERRGDAGIVYCLSRKKVEEvAEFLGNQGFPALPYHAGLSNELRAHHQKRFLNEEGLIMVATIAFGMGIDKPNVR 298
Cdd:pfam00271 6 LLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVD 84
|
90 100
....*....|....*....|....*
gi 489182275 299 FVAHLDLPKSLEAYYQETGRAGRDG 323
Cdd:pfam00271 85 LVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
531-598 |
5.35e-19 |
|
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: 81.43 E-value: 5.35e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489182275 531 EREMWEALRALRRKLAEEHSVPPYVIFPDATLLEMLRSQPRSLSDMAQVSGVGARKLERYGQAFLDVL 598
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
206-324 |
2.49e-17 |
|
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: 78.70 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 206 FYRIVPKEQPRKQLLG-FLSERRGDAGIVYCLSRKKVEEVAEFLGNQGFPALPYHAGLSNELRAHHQKRFLNEEGLIMVA 284
Cdd:cd18787 4 LYVVVEEEEKKLLLLLlLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVA 83
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 489182275 285 TIAFGMGIDKPNVRFVAHLDLPKSLEAYYQ---ETGRAGRDGL 324
Cdd:cd18787 84 TDVAARGLDIPGVDHVINYDLPRDAEDYVHrigRTGRAGRKGT 126
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
528-598 |
8.35e-17 |
|
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: 75.41 E-value: 8.35e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489182275 528 RSEEREMWEALRALRRKLAEEHSVPPYVIFPDATLLEMLRSQPRSLSDMAQVSGVGARKLERYGQAFLDVL 598
Cdd:smart00341 1 RERQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVI 71
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
32-175 |
3.97e-16 |
|
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: 75.90 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 32 GGDALVLMPTGGGKSLCFQVPALLR----EGLTVVVSPLIALMEDQVATLDEL---GVPAVALNSTLNPEQQRDIAERlq 104
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLllkkGKKVLVLVPTKALALQTAERLRELfgpGIRVAVLVGGSSAEEREKNKLG-- 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489182275 105 rgEIKLLYLAPERLVQPRMLAFLQRLP-VGLFAIDEAHCVSQWGHDFRPEYLQLGQLAelFPQVPRIALTAT 175
Cdd:cd00046 79 --DADIIIATPDMLLNLLLREDRLFLKdLKLIIVDEAHALLIDSRGALILDLAVRKAG--LKNAQVILLSAT 146
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
203-324 |
1.01e-11 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 67.48 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 203 PNI--FYRIVPKEQPRKQLLGFLSERRGDAGIVYCLSRKKVEEVAEFLGNQGFPALPYHAGLSNELRAHHQKRFLNEEGL 280
Cdd:COG0513 214 ETIeqRYYLVDKRDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIR 293
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 489182275 281 IMVAT-IAfGMGIDKPNVRFVAHLDLPKSLEAYyq---eTGRAGRDGL 324
Cdd:COG0513 294 VLVATdVA-ARGIDIDDVSHVINYDLPEDPEDYvhrigrTGRAGAEGT 340
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
22-319 |
1.32e-11 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 67.74 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 22 QARIIERV-----AEGGDALVLMPTGGGKSLCFQVPA--LLREGLTVVVSPLIALMEDQVATLDElgVPAVALNSTLNPE 94
Cdd:COG1061 85 QQEALEALlaaleRGGGRGLVVAPTGTGKTVLALALAaeLLRGKRVLVLVPRRELLEQWAEELRR--FLGDPLAGGGKKD 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 95 QQRDIaerlqrgeiklLYLAPERLVQPRMLAFLQRLPvGLFAIDEAHcvsqwgHDFRPEYLQLgqlAELFPQVPRIALTA 174
Cdd:COG1061 163 SDAPI-----------TVATYQSLARRAHLDELGDRF-GLVIIDEAH------HAGAPSYRRI---LEAFPAAYRLGLTA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 175 T---ADMRTRE--------------EMIQRLHLQNAEQFLSSFDRPNIFYRIVPKEQPRKQLLGFLSER----------- 226
Cdd:COG1061 222 TpfrSDGREILlflfdgivyeyslkEAIEDGYLAPPEYYGIRVDLTDERAEYDALSERLREALAADAERkdkilrellre 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 227 --RGDAGIVYCLSRKKVEEVAEFLGNQGFPALPYHAGLSNELRAHHQKRFLNEEGLIMVATIAFGMGIDKPNVRFVAHLD 304
Cdd:COG1061 302 hpDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLR 381
|
330
....*....|....*
gi 489182275 305 LPKSLEAYYQETGRA 319
Cdd:COG1061 382 PTGSPREFIQRLGRG 396
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
14-328 |
1.84e-11 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 67.12 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 14 GYDAFRGNQARIIERVAEGGDALVLMPTGGGKSLCFQVP-----ALLREG--------LTVVVSP---LIALMEDQVATL 77
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPiisrcCTIRSGhpseqrnpLAMVLTPtreLCVQVEDQAKVL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 78 DElGVP---AVALNSTLNPEQqrdiAERLQRGeIKLLYLAPERLVQPRMLAFLQRLPVGLFAIDEAHCVSQWGhdFRPEY 154
Cdd:PLN00206 220 GK-GLPfktALVVGGDAMPQQ----LYRIQQG-VELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERG--FRDQV 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 155 LQLGQlAELFPQVprIALTATAdmrtreemiqrlhLQNAEQFLSSFDRPNIFYRIVPKEQP----------------RKQ 218
Cdd:PLN00206 292 MQIFQ-ALSQPQV--LLFSATV-------------SPEVEKFASSLAKDIILISIGNPNRPnkavkqlaiwvetkqkKQK 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 219 LLGFL--SERRGDAGIVYCLSRKKveevAEFLGN-----QGFPALPYHAGLSNELRAHHQKRFLNEEGLIMVATIAFGMG 291
Cdd:PLN00206 356 LFDILksKQHFKPPAVVFVSSRLG----ADLLANaitvvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRG 431
|
330 340 350
....*....|....*....|....*....|....*..
gi 489182275 292 IDKPNVRFVAHLDLPKSLEAYYQETGRAGRDGLPADA 328
Cdd:PLN00206 432 VDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTA 468
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
22-323 |
3.16e-10 |
|
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: 63.70 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 22 QARIIERVAEGGDALVLMPTGGGKSLCFQVPALL-----REGLTVVVSPLIALMEDQVATLDEL------GVPAVALNST 90
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEalledPGATALYLYPTKALARDQLRRLRELaealglGVRVATYDGD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 91 LNPEQQRDIaerLQRGEIkllylapeRLVQPRML------------AFLQRLpvGLFAIDEAHC---V--SQWGHDFRpe 153
Cdd:COG1205 141 TPPEERRWI---REHPDI--------VLTNPDMLhygllphhtrwaRFFRNL--RYVVIDEAHTyrgVfgSHVANVLR-- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 154 ylQLGQLAELF---PQVprIALTATadmrtreemiqrlhLQNAEQFLSS-FDRP---------------NIFYRIVPKEQ 214
Cdd:COG1205 206 --RLRRICRHYgsdPQF--ILASAT--------------IGNPAEHAERlTGRPvtvvdedgsprgertFVLWNPPLVDD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 215 PR--------KQLLGFLSeRRGDAGIVYCLSRKKVEEVA----EFLGNQGFPA--LPYHAGLSNELRAHHQKRFLNEEGL 280
Cdd:COG1205 268 GIrrsalaeaARLLADLV-REGLRTLVFTRSRRGAELLAryarRALREPDLADrvAAYRAGYLPEERREIERGLRSGELL 346
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 489182275 281 IMVATIAFGMGIDkpnvrfVAHLDL------PKSLEAYYQETGRAGRDG 323
Cdd:COG1205 347 GVVSTNALELGID------IGGLDAvvlagyPGTRASFWQQAGRAGRRG 389
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
232-323 |
1.26e-08 |
|
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: 52.32 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 232 IVYCLSRKKVEEVAEFLGnqgfpalpyhaglsnelrahhqkrflneeglIMVATIAFGMGIDKPNVRFVAHLDLPKSLEA 311
Cdd:cd18785 7 IVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSAAS 55
|
90
....*....|..
gi 489182275 312 YYQETGRAGRDG 323
Cdd:cd18785 56 YIQRVGRAGRGG 67
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
32-323 |
5.89e-08 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 55.94 E-value: 5.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 32 GGDALVLMPTGGGKSLCFQVPA--------LLREG---LTVVVSPLIALMEDQVATLDELGVPAVALNSTLN---PEQQR 97
Cdd:PTZ00110 167 GRDMIGIAETGSGKTLAFLLPAivhinaqpLLRYGdgpIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYggvPKRGQ 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 98 DIAerLQRGeIKLLYLAPERLVQprmlaFLQR-----LPVGLFAIDEAHCVSQWGhdFRPEYLQLgqLAELFPQVPRIAL 172
Cdd:PTZ00110 247 IYA--LRRG-VEILIACPGRLID-----FLESnvtnlRRVTYLVLDEADRMLDMG--FEPQIRKI--VSQIRPDRQTLMW 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 173 TAT--------ADMRTREEMIQ----RLHL---QNAEQflssfdrpNIFyrIVPKEQPRKQLLGFLSERRGDAG--IVYC 235
Cdd:PTZ00110 315 SATwpkevqslARDLCKEEPVHvnvgSLDLtacHNIKQ--------EVF--VVEEHEKRGKLKMLLQRIMRDGDkiLIFV 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 236 LSRKKVEEVAEFLGNQGFPALPYHAGLSNELRAHHQKRFLNEEGLIMVATIAFGMGIDKPNVRFVAHLDLPKSLEAYYQE 315
Cdd:PTZ00110 385 ETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHR 464
|
....*...
gi 489182275 316 TGRAGRDG 323
Cdd:PTZ00110 465 IGRTGRAG 472
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
22-83 |
3.24e-07 |
|
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: 51.05 E-value: 3.24e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489182275 22 QARIIERVAEGGDALVLMPTGGGKSLCFQVP---ALLREGLT--VVVSPLIALMEDQVATLDELGVP 83
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPileALLRDPGSraLYLYPTKALAQDQLRSLRELLEQ 71
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
16-323 |
4.56e-07 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 53.35 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 16 DAFRGN-------QARIIERVAEGGDALVLMPTGGGKSLCFQ---VPALLREGLTVVVSPLIAL-ME--DQVATLDELGv 82
Cdd:PRK01172 14 NLFTGNdfelydhQRMAIEQLRKGENVIVSVPTAAGKTLIAYsaiYETFLAGLKSIYIVPLRSLaMEkyEELSRLRSLG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 83 pavaLNSTLNPEQQRDIAERLQRGEIklLYLAPER---LVQ--PRMLAflqrlPVGLFAIDEAHCVsqwGHDFRPEYLQ- 156
Cdd:PRK01172 93 ----MRVKISIGDYDDPPDFIKRYDV--VILTSEKadsLIHhdPYIIN-----DVGLIVADEIHII---GDEDRGPTLEt 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 157 -LGQLAELFPQVPRIALTATadMRTREEMIQRLhlqNAEQFLSSFdRP-----NIFY--RIVPKEQPRKQL--LGFLSER 226
Cdd:PRK01172 159 vLSSARYVNPDARILALSAT--VSNANELAQWL---NASLIKSNF-RPvplklGILYrkRLILDGYERSQVdiNSLIKET 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 227 RGDAG--IVYCLSRKKVEEVAEFLG---------------NQGFP-----ALP-----YHAGLSNELRAHHQKRFLNEEG 279
Cdd:PRK01172 233 VNDGGqvLVFVSSRKNAEDYAEMLIqhfpefndfkvssenNNVYDdslneMLPhgvafHHAGLSNEQRRFIEEMFRNRYI 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489182275 280 LIMVATIAFGMGIDKPnVRFVAHLDLPKSLEAYY---------QETGRAGRDG 323
Cdd:PRK01172 313 KVIVATPTLAAGVNLP-ARLVIVRDITRYGNGGIrylsnmeikQMIGRAGRPG 364
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
206-323 |
1.06e-06 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 51.75 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 206 FYRIVPKEQPRKQLLGFLSERRG-DAGIVYCLSRKKVEEVAEFLGNQGFPALPYHAGLSNELRAHHQKRFLNEEGLIMVA 284
Cdd:PTZ00424 244 FYVAVEKEEWKFDTLCDLYETLTiTQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLIT 323
|
90 100 110
....*....|....*....|....*....|....*....
gi 489182275 285 TIAFGMGIDKPNVRFVAHLDLPKSLEAYYQETGRAGRDG 323
Cdd:PTZ00424 324 TDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFG 362
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
14-323 |
1.88e-06 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 51.39 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 14 GYDAFRGNQARIIERVAEGGDALVLMPTGGGKSLCFQVPAL------LREGLTVVVSPLIALMEDQVATLDEL-----GV 82
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLhnldpeLKAPQILVLAPTRELAVQVAEAMTDFskhmrGV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 83 PAVALNSTlnpeQQRDIAERLQRGEIKLLYLAPERLvqprmLAFLQRLPVGL-----FAIDEAHcvsqwghdfrpEYLQL 157
Cdd:PRK11634 105 NVVALYGG----QRYDVQLRALRQGPQIVVGTPGRL-----LDHLKRGTLDLsklsgLVLDEAD-----------EMLRM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 158 G---QLAELFPQVPRIALTA--TADMRTREEMIQRLHLQNAEQFL---SSFDRPNIF--YRIVPKEQPRKQLLGFLSERR 227
Cdd:PRK11634 165 GfieDVETIMAQIPEGHQTAlfSATMPEAIRRITRRFMKEPQEVRiqsSVTTRPDISqsYWTVWGMRKNEALVRFLEAED 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 228 GDAGIVYCLSRKKVEEVAEFLGNQGFPALPYHAGLSNELRAHHQKRFLNEEGLIMVATIAFGMGIDKPNVRFVAHLDLPK 307
Cdd:PRK11634 245 FDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPM 324
|
330
....*....|....*.
gi 489182275 308 SLEAYYQETGRAGRDG 323
Cdd:PRK11634 325 DSESYVHRIGRTGRAG 340
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
196-321 |
2.75e-06 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 50.66 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 196 FLSSFDRPNIFYRIVPKEQPRKQLLGFlserRGDAgIVYCLSRKKVEEVAEFLGnqgFPALPYHAGLSNELRAHHQKRFL 275
Cdd:COG1202 400 FADGREKIRIINKLVKREFDTKSSKGY----RGQT-IIFTNSRRRCHEIARALG---YKAAPYHAGLDYGERKKVERRFA 471
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 489182275 276 NEEGLIMVATIAFGMGIDKP--NVRFvahldlpKSL---------EAYYQETGRAGR 321
Cdd:COG1202 472 DQELAAVVTTAALAAGVDFPasQVIF-------DSLamgiewlsvQEFHQMLGRAGR 521
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
22-207 |
3.83e-06 |
|
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: 48.03 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 22 QARIIERVAEGGDALVL-MPTGGGKSLCFQ---VPALLREGLTVV-VSPLIALMEDQVATLDELGVPA---VAL---NST 90
Cdd:cd17921 6 QREALRALYLSGDSVLVsAPTSSGKTLIAElaiLRALATSGGKAVyIAPTRALVNQKEADLRERFGPLgknVGLltgDPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 91 LNPEQ--QRDI----AERLQrgeiKLLYLAPERLVQPrmlaflqrlpVGLFAIDEAHCVSQwghdfrPEY-----LQLGQ 159
Cdd:cd17921 86 VNKLLlaEADIlvatPEKLD----LLLRNGGERLIQD----------VRLVVVDEAHLIGD------GERgvvleLLLSR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489182275 160 LAELFPQVPRIALTATadmrtreemiqrlhLQNAEQFLSSFDRPNIFY 207
Cdd:cd17921 146 LLRINKNARFVGLSAT--------------LPNAEDLAEWLGVEDLIR 179
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
528-598 |
5.94e-06 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 49.10 E-value: 5.94e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489182275 528 RSEEREMWEALRALRRKLAEEHSVPPYVIFPDATLLEMLRSQPRSLSDMAQVSGVGARKLERYGQAFLDVL 598
Cdd:COG0349 206 NPRQLAVLRELAAWREREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAV 276
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
232-326 |
7.68e-06 |
|
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: 46.10 E-value: 7.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 232 IVYCLSRKKVEEVAEFLGN--QGFPALP-----YHAGLSNELRAHHQKRFLNEEGLIMVATIAFGMGIDKPNVRFVAHLD 304
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKArlVEEGPLAskvasYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|..
gi 489182275 305 LPKSLEAYYQETGRAGRDGLPA 326
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDS 140
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
206-323 |
4.10e-05 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 46.47 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 206 FYRIVPKEQPRKQLLGFLSERRGDAGIVYCLSRKKVEEVAEFLGNQGFPAlpyhAGLSNEL----RAHHQKRFLNEEGLI 281
Cdd:PRK11192 223 YYRADDLEHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINC----CYLEGEMvqakRNEAIKRLTDGRVNV 298
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 489182275 282 MVATIAFGMGIDKPNVRFVAHLDLPKSLEAYYQ---ETGRAGRDG 323
Cdd:PRK11192 299 LVATDVAARGIDIDDVSHVINFDMPRSADTYLHrigRTGRAGRKG 343
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
232-324 |
7.30e-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: 43.70 E-value: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 232 IVYCLSRKKVEEVAEFLGNQGFpalpYHAGLSNELRAHHQKRFLneEGLIMV--ATIAFGMGIDKPnvrfvAHL------ 303
Cdd:cd18795 47 LVFCSSRKECEKTAKDLAGIAF----HHAGLTREDRELVEELFR--EGLIKVlvATSTLAAGVNLP-----ARTviikgt 115
|
90 100 110
....*....|....*....|....*....|
gi 489182275 304 ---------DLPkSLEaYYQETGRAGRDGL 324
Cdd:cd18795 116 qrydgkgyrELS-PLE-YLQMIGRAGRPGF 143
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
22-246 |
7.72e-05 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 46.04 E-value: 7.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 22 QARIIERVAEGGDALVL-MPTGGGKSLCFQVPAL--LREGLTVV-VSPLIAL----MEDQVATLDELGVPAVAlnSTLNP 93
Cdd:COG1204 27 QAEALEAGLLEGKNLVVsAPTASGKTLIAELAILkaLLNGGKALyIVPLRALasekYREFKRDFEELGIKVGV--STGDY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 94 EqqrDIAERLQRGEIklLYLAPERLVQprML----AFLQRlpVGLFAIDEAHCVsqwGHDFR-PEY-LQLGQLAELFPQV 167
Cdd:COG1204 105 D---SDDEWLGRYDI--LVATPEKLDS--LLrngpSWLRD--VDLVVVDEAHLI---DDESRgPTLeVLLARLRRLNPEA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 168 PRIALTATadmrtreemiqrlhLQNAEQFLSSFDRPNIF--YRIVPK----------------EQPRKQLLGFLSERRGD 229
Cdd:COG1204 173 QIVALSAT--------------IGNAEEIAEWLDAELVKsdWRPVPLnegvlydgvlrfddgsRRSKDPTLALALDLLEE 238
|
250
....*....|....*....
gi 489182275 230 AG--IVYCLSRKKVEEVAE 246
Cdd:COG1204 239 GGqvLVFVSSRRDAESLAK 257
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
219-328 |
4.08e-04 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 43.79 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 219 LLGFLSERRGDAGIVYCLSRKKVEEVAEFLGNQGFPALPYHAGLSNELRAHHQKRFLNEEGLIMVATIAFGMGIDKPNVR 298
Cdd:PRK04537 248 LLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVK 327
|
90 100 110
....*....|....*....|....*....|
gi 489182275 299 FVAHLDLPKSLEAYYQETGRAGRDGLPADA 328
Cdd:PRK04537 328 YVYNYDLPFDAEDYVHRIGRTARLGEEGDA 357
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
22-175 |
5.72e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 41.12 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 22 QARIIERVAEG-----GDALVLMPTGGGKSLC-FQVPALLREGL----TVVVSPLIALMEDQVATLDELGVPAVALNSTL 91
Cdd:pfam04851 8 QIEAIENLLESikngqKRGLIVMATGSGKTLTaAKLIARLFKKGpikkVLFLVPRKDLLEQALEEFKKFLPNYVEIGEII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 92 NPEqqrdiAERLQRGEIKLLYLAPERLVQPRMLAFLQRLP--VGLFAIDEAHcvsqwgHDFRPEYlqlGQLAELFPQVPR 169
Cdd:pfam04851 88 SGD-----KKDESVDDNKIVVTTIQSLYKALELASLELLPdfFDVIIIDEAH------RSGASSY---RNILEYFKPAFL 153
|
....*.
gi 489182275 170 IALTAT 175
Cdd:pfam04851 154 LGLTAT 159
|
|
| HTH_40 |
pfam14493 |
Helix-turn-helix domain; This presumed domain is found at the C-terminus of a large number of ... |
623-703 |
6.48e-04 |
|
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: 39.03 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 623 GMTPAQIARQLNCSEKNVYAMLAEAI-AGQQVSLEQAldLPEELLGEIQDAFLE-EDGELPPvaaLEERFGKRVPSGVLH 700
Cdd:pfam14493 12 GLSIEEIAEERGLKESTIEGHLAELIeAGEPVDIERL--VSEEEQKEILDAIEKlGSESLKP---IKEALPEEISYFEIR 86
|
...
gi 489182275 701 CVR 703
Cdd:pfam14493 87 LVL 89
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
216-327 |
1.44e-03 |
|
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: 39.46 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 216 RKQLLGFLSERRGDAgiVYCLSRKKVEEVAEFL-GNQGFPALPYHAGLSNELRAHHQKRFL--NEEGLIMVATIAFGMGI 292
Cdd:cd18805 7 SKPLGSLRNLRPGDC--VVAFSRKDIFSLKREIeKRTGLKCAVIYGALPPETRRQQARLFNdpESGYDVLVASDAIGMGL 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 489182275 293 DKpNVRFVAHLDLPK---------SLEAYYQETGRAGRDGLPAD 327
Cdd:cd18805 85 NL-NIRRVIFSSLSKfdgnemrplSPSEVKQIAGRAGRFGSHFP 127
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
231-321 |
3.83e-03 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 37.92 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 231 GIVYCLSRKKVEEVAEFLGNQGFPALPYHAGLSNELRAHHQKRFLNEEGL---IMVATIAFGMGIDKPNVRFVAHLDLPK 307
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEALILLFFGELkppILVTVDLLTTGVDIPEVDNVVFLRPTE 88
|
90
....*....|....
gi 489182275 308 SLEAYYQETGRAGR 321
Cdd:cd18799 89 SRTLFLQMLGRGLR 102
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
32-175 |
4.81e-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: 38.33 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 32 GGDALVLMPTGGGKSLCFQVPALLR------EGLTVV-VSPLIALMEDQVATLDE------LGVPAVALNSTLNPEQQRD 98
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSladepeKGVQVLyISPLKALINDQERRLEEpldeidLEIPVAVRHGDTSQSEKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182275 99 IAERLQrgeiKLLYLAPERL----VQPR---MLAFLQRLpvglfAIDEAHCV--SQWGHDFRpeyLQLGQLAELF-PQVP 168
Cdd:cd17922 81 QLKNPP----GILITTPESLelllVNKKlreLFAGLRYV-----VVDEIHALlgSKRGVQLE---LLLERLRKLTgRPLR 148
|
....*..
gi 489182275 169 RIALTAT 175
Cdd:cd17922 149 RIGLSAT 155
|
|
| |
