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Conserved domains on  [gi|2157343983|ref|WP_230470295|]
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helicase-related protein [Lujinxingia vulgaris]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DISARM_DrmD super family cl45761
DISARM system SNF2-like helicase DrmD, long form; DrmD, a SNF2-like helicase, is a component ...
1-437 1.11e-57

DISARM system SNF2-like helicase DrmD, long form; DrmD, a SNF2-like helicase, is a component of class 1 DISARM (Defence Island System Associated with Restriction Modification), which contains a DNA adenine N6 methyltransferase.


The actual alignment was detected with superfamily member NF038317:

Pssm-ID: 468471 [Multi-domain]  Cd Length: 1023  Bit Score: 213.17  E-value: 1.11e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983    1 MLT-QFQKELWSRFTIPLVRLDSTGLQRIRRKIPTNQNPFHYFDRAIISVDTLKQNNEFRHYLE--------QAHWDVIV 71
Cdd:NF038317   165 SLQeKWRDEMREKFGLDFRIVDSEYVAQLRRERGLHANPWTSFPRLIVSMDWLRGERAQRLLRDvlpahadtPRAFDLLI 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983   72 IDEAHNVAVRGHDR----SQRARLAQLLSRRSDALIMLSATPHDGRAQSFASLMNMLDPTAIADEENYTPEDIEGLFIRR 147
Cdd:NF038317   245 VDEAHNVAPASPSKyavdSQRTRLIRDLAPHFEHRLFLSATPHNGYSESFTALLELLDPQRFARGVPPDEKQLDEVMVRR 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  148 FKGDVADQLGDKI-PSRELHRLNAQASLVEEQVFDAFAEldFSALDSPNAKSTGGR---MLFKTSLEKGLLSSPAAAMET 223
Cdd:NF038317   325 LKSDLVDRDGSPRfPERELEALPVDYSADEREIHELLDE--YTELRRKRLAGKRGRraaDFVTLLLKKRLFSSPAAFART 402
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  224 IDNRIKTIESR---------------------------------------ETADRY-----KDDVAQLQHLRRVLERVAP 259
Cdd:NF038317   403 LEVHRATLERGaarggplsdderllrddvlddeedyaddelleeaedealEEASELsppltAEERALLERLRAWAERAEA 482
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  260 EDFSKFQLLVDTLtddDSPFKFSGHFKDDRLVIFTERIATMRWLASHLPAAlGLDEKKVACLYGGMSDLDQQQVVEDF-- 337
Cdd:NF038317   483 RPDSKARALIDWL---RANLRPGGRWTNERVIVFTEYRDTLRWLVELLAAE-GYGGDRLALLHGGMDDDERERIKAAFqa 558
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  338 GRESSDIRLLIASDVASEGINLHYYCHRMVHFDIPWSLMVFQQRNGRVDRYGQTRTP-HIAYLSTLAQNERIYSDTRILE 416
Cdd:NF038317   559 DPSEHPVRILLATDAASEGIDLQNHCHRLIHYDIPWNPNRLEQRNGRIDRHGQRADPvLIWHFVGKGTEGAAEGDLEFLD 638
                          490       500
                   ....*....|....*....|.
gi 2157343983  417 ILVEKDDQASRNIGDPSALMG 437
Cdd:NF038317   639 RLARKVATIREDLGSVNPVIA 659
 
Name Accession Description Interval E-value
DISARM_DrmD NF038317
DISARM system SNF2-like helicase DrmD, long form; DrmD, a SNF2-like helicase, is a component ...
1-437 1.11e-57

DISARM system SNF2-like helicase DrmD, long form; DrmD, a SNF2-like helicase, is a component of class 1 DISARM (Defence Island System Associated with Restriction Modification), which contains a DNA adenine N6 methyltransferase.


Pssm-ID: 468471 [Multi-domain]  Cd Length: 1023  Bit Score: 213.17  E-value: 1.11e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983    1 MLT-QFQKELWSRFTIPLVRLDSTGLQRIRRKIPTNQNPFHYFDRAIISVDTLKQNNEFRHYLE--------QAHWDVIV 71
Cdd:NF038317   165 SLQeKWRDEMREKFGLDFRIVDSEYVAQLRRERGLHANPWTSFPRLIVSMDWLRGERAQRLLRDvlpahadtPRAFDLLI 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983   72 IDEAHNVAVRGHDR----SQRARLAQLLSRRSDALIMLSATPHDGRAQSFASLMNMLDPTAIADEENYTPEDIEGLFIRR 147
Cdd:NF038317   245 VDEAHNVAPASPSKyavdSQRTRLIRDLAPHFEHRLFLSATPHNGYSESFTALLELLDPQRFARGVPPDEKQLDEVMVRR 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  148 FKGDVADQLGDKI-PSRELHRLNAQASLVEEQVFDAFAEldFSALDSPNAKSTGGR---MLFKTSLEKGLLSSPAAAMET 223
Cdd:NF038317   325 LKSDLVDRDGSPRfPERELEALPVDYSADEREIHELLDE--YTELRRKRLAGKRGRraaDFVTLLLKKRLFSSPAAFART 402
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  224 IDNRIKTIESR---------------------------------------ETADRY-----KDDVAQLQHLRRVLERVAP 259
Cdd:NF038317   403 LEVHRATLERGaarggplsdderllrddvlddeedyaddelleeaedealEEASELsppltAEERALLERLRAWAERAEA 482
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  260 EDFSKFQLLVDTLtddDSPFKFSGHFKDDRLVIFTERIATMRWLASHLPAAlGLDEKKVACLYGGMSDLDQQQVVEDF-- 337
Cdd:NF038317   483 RPDSKARALIDWL---RANLRPGGRWTNERVIVFTEYRDTLRWLVELLAAE-GYGGDRLALLHGGMDDDERERIKAAFqa 558
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  338 GRESSDIRLLIASDVASEGINLHYYCHRMVHFDIPWSLMVFQQRNGRVDRYGQTRTP-HIAYLSTLAQNERIYSDTRILE 416
Cdd:NF038317   559 DPSEHPVRILLATDAASEGIDLQNHCHRLIHYDIPWNPNRLEQRNGRIDRHGQRADPvLIWHFVGKGTEGAAEGDLEFLD 638
                          490       500
                   ....*....|....*....|.
gi 2157343983  417 ILVEKDDQASRNIGDPSALMG 437
Cdd:NF038317   639 RLARKVATIREDLGSVNPVIA 659
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
2-430 1.58e-39

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 156.15  E-value: 1.58e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983   2 LTQFQKELwSRFT--IPLVRLDSTglqRIRRKiptNQNPFHYFDRAIISVDTLKQNnefRHYLEQAHWDVIVIDEAHNVA 79
Cdd:COG0553   302 VGNWQREL-AKFApgLRVLVLDGT---RERAK---GANPFEDADLVITSYGLLRRD---IELLAAVDWDLVILDEAQHIK 371
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  80 VRghdRSQRARLAQLLsrRSDALIMLSATPHDGRAQSFASLMNMLDP-----------TAIADEENYTPEDIEGL----- 143
Cdd:COG0553   372 NP---ATKRAKAVRAL--KARHRLALTGTPVENRLEELWSLLDFLNPgllgslkafreRFARPIEKGDEEALERLrrllr 446
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 144 --FIRRFKGDVADQLGDKIPSRELHRLNAQaslvEEQVFDAFAELDFSALDSPNAKSTGGRMLFKTSLEKGLLSSPAAAM 221
Cdd:COG0553   447 pfLLRRTKEDVLKDLPEKTEETLYVELTPE----QRALYEAVLEYLRRELEGAEGIRRRGLILAALTRLRQICSHPALLL 522
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 222 EtiDNRIKTIESretadrykddvaqlqhlrrvlervapedfSKFQLLVDTLTDDDSpfkfsghfKDDRLVIFTERIATMR 301
Cdd:COG0553   523 E--EGAELSGRS-----------------------------AKLEALLELLEELLA--------EGEKVLVFSQFTDTLD 563
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 302 WLASHLpAALGLdekKVACLYGGMSDLDQQQVVEDFGRESSDIRLLIASDVASEGINLHyYCHRMVHFDIPWSLMVFQQR 381
Cdd:COG0553   564 LLEERL-EERGI---EYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLT-AADHVIHYDLWWNPAVEEQA 638
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 2157343983 382 NGRVDRYGQTRTPHIAYLstLAQNERiysDTRILEILVEKDDQASRNIG 430
Cdd:COG0553   639 IDRAHRIGQTRDVQVYKL--VAEGTI---EEKILELLEEKRALAESVLG 682
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
1-147 4.82e-33

DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 126.63  E-value: 4.82e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983   1 MLTQFQKELWSRFTIPLVRLDSTGLQRIRRKIptnQNPFHYFDRAIISVDTLKQNNEFRHYLEQAHWDVIVIDEAHNVAV 80
Cdd:cd18011    58 LVEQWQDELQDKFGLPFLILDRETAAQLRRLI---GNPFEEFPIVIVSLDLLKRSEERRGLLLSEEWDLVVVDEAHKLRN 134
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2157343983  81 R-GHDRSQRARLAQLLSRRSDALIMLSATPHDGRAQSFASLMNMLDPTAIAD-----EENYTPEDIEGLFIRR 147
Cdd:cd18011   135 SgGGKETKRYKLGRLLAKRARHVLLLTATPHNGKEEDFRALLSLLDPGRFAVlgrflRLDGLREVLAKVLLRR 207
DpdE NF041062
protein DpdE;
68-395 1.21e-18

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 91.19  E-value: 1.21e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983   68 DVIVIDEAHN-VAVRGHDRS-QRARLAQL--LSRRSDALIMLSATPHDGRAQSFASLMNMLDPtaiadeENYTPEDIEGl 143
Cdd:NF041062   252 DLLVVDEAHQlARLAWSGDPpERARYRELaaLAHAAPRLLLLSATPVLGNEETFLALLHLLDP------DLYPLDDLEA- 324
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  144 FIRRFK---------------------GDVADQLGDKIPS-RELHRL----------------NAQASLV---------- 175
Cdd:NF041062   325 FRERLEereelgrlvlgldpdnpnfllRQALDELRALFPEdEELQELaeellplldefddeepEERARAVsalrahiset 404
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  176 -------------------------------------EEQVFDAFAELDFSALDSPNAKSTGGRMLFKTSLekGLLSSPA 218
Cdd:NF041062   405 yrlhrrmirnrrssvlgadylvpgragprvlvwespaREAADEALEDWREEAALLDAESDPAARAAYARAL--AWLVARL 482
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  219 AAMETIDNRIKT-IESRETADRYKDDVAQLQHLRRVLERVApEDFSKFQLLVDTLTDddspfkfsgHFKDD-RLVIFTER 296
Cdd:NF041062   483 GGPDDLAALLRWrLRGDAASADLAGERELLEALIAALEDEA-KDADLLAALADWLLP---------LLRGSgKAVVFCGD 552
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  297 iatmRWLASHLPAALG-LDEKKVACLYGGMSDLDQQQVVEDFgRESSDIRLLIASDVASEGINLHYYChRMVHFDIPWSL 375
Cdd:NF041062   553 ----GSLADHLAAALArLGAGSVERHLSGQGADQAERAVRAF-RQDPSARVLVCDRSGEEGLNLQGAD-RLVHLDLPWSP 626
                          410       420
                   ....*....|....*....|
gi 2157343983  376 MVFQQRNGRVDRYGQTRTPH 395
Cdd:NF041062   627 NRLEQRIGRLDRYASLRGGR 646
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
286-389 1.57e-15

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: 73.01  E-value: 1.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 286 KDDRLVIFTERIATMRwlASHLPAALGLdekKVACLYGGMSDLDQQQVVEDFgrESSDIRLLIASDVASEGINLHYyCHR 365
Cdd:pfam00271  14 RGGKVLIFSQTKKTLE--AELLLEKEGI---KVARLHGDLSQEEREEILEDF--RKGKIDVLVATDVAERGLDLPD-VDL 85
                          90       100
                  ....*....|....*....|....
gi 2157343983 366 MVHFDIPWSLMVFQQRNGRVDRYG 389
Cdd:pfam00271  86 VINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
307-389 2.90e-14

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 68.39  E-value: 2.90e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  307 LPAALGLDEKKVACLYGGMSDLDQQQVVEDFgrESSDIRLLIASDVASEGINLHYyCHRMVHFDIPWSLMVFQQRNGRVD 386
Cdd:smart00490   3 LAELLKELGIKVARLHGGLSQEEREEILDKF--NNGKIKVLVATDVAERGLDLPG-VDLVIIYDLPWSPASYIQRIGRAG 79

                   ...
gi 2157343983  387 RYG 389
Cdd:smart00490  80 RAG 82
PRK04914 PRK04914
RNA polymerase-associated protein RapA;
37-404 4.10e-09

RNA polymerase-associated protein RapA;


Pssm-ID: 235319 [Multi-domain]  Cd Length: 956  Bit Score: 60.24  E-value: 4.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  37 NPFHYFDRAIISVDTLKQNNEFRHYLEQAHWDVIVIDEAHNVAVRGHDRSQRARLAQLLSRRSDALIMLSATPHD-GRAQ 115
Cdd:PRK04914  243 NPFETEQLVICSLDFLRRNKQRLEQALAAEWDLLVVDEAHHLVWSEEAPSREYQVVEQLAEVIPGVLLLTATPEQlGQES 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 116 SFASLmNMLDP-------TAIADEENYTPedieglfirrfkgdVADQ----LGDKIPSRELHrlNAQASLVEEQ-VFDAF 183
Cdd:PRK04914  323 HFARL-RLLDPdrfhdyeAFVEEQQQYRP--------------VADAvqalLAGEKLSDDAL--NALGELLGEQdIEPLL 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 184 AELDFSALDSPNAKST---------G-GRMLFKTSLE--KGL---------LSSPAAAMETIDnriKTIESRETADRYKD 242
Cdd:PRK04914  386 QAANSDSEEAQAARQEliselldrhGtGRVLFRNTRAavKGFpkrelhpipLPLPEQYQTAIK---VSLEARARDMLYPE 462
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 243 DVAQLQhlrrvlERVAP--EDFSKFQLLVDTLTDddspfkfsgHFKDDRLVIfteriatmrwlASHLPAALGLDEK---- 316
Cdd:PRK04914  463 QIYQEF------EDNATwwNFDPRVEWLIDFLKS---------HRSEKVLVI-----------CAKAATALQLEQAlrer 516
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 317 ---KVACLYGGMSDLDQQQVVEDFGRESSDIRLLIASDVASEGINLHyYCHRMVHFDIPWSLMVFQQRNGRVDRYGQTRT 393
Cdd:PRK04914  517 egiRAAVFHEGMSIIERDRAAAYFADEEDGAQVLLCSEIGSEGRNFQ-FASHLVLFDLPFNPDLLEQRIGRLDRIGQKHD 595
                         410
                  ....*....|...
gi 2157343983 394 P--HIAYLSTLAQ 404
Cdd:PRK04914  596 IqiHVPYLEGTAQ 608
recQ_fam TIGR00614
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ...
55-156 7.49e-04

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: 42.83  E-value: 7.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  55 NNEFRHYLEqAHWDV--IVIDEAHNVAVRGHD-RSQRARLAQLLSRRSDALIM-LSATPHDGRAQSFASLMNMLDP---T 127
Cdd:TIGR00614 115 SNRLLQTLE-ERKGItlIAVDEAHCISQWGHDfRPDYKALGSLKQKFPNVPVMaLTATASPSVREDILRQLNLLNPqifC 193
                          90       100
                  ....*....|....*....|....*....
gi 2157343983 128 AIADEENYTpediegLFIRRFKGDVADQL 156
Cdd:TIGR00614 194 TSFDRPNLY------YEVRRKTPKILEDL 216
 
Name Accession Description Interval E-value
DISARM_DrmD NF038317
DISARM system SNF2-like helicase DrmD, long form; DrmD, a SNF2-like helicase, is a component ...
1-437 1.11e-57

DISARM system SNF2-like helicase DrmD, long form; DrmD, a SNF2-like helicase, is a component of class 1 DISARM (Defence Island System Associated with Restriction Modification), which contains a DNA adenine N6 methyltransferase.


Pssm-ID: 468471 [Multi-domain]  Cd Length: 1023  Bit Score: 213.17  E-value: 1.11e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983    1 MLT-QFQKELWSRFTIPLVRLDSTGLQRIRRKIPTNQNPFHYFDRAIISVDTLKQNNEFRHYLE--------QAHWDVIV 71
Cdd:NF038317   165 SLQeKWRDEMREKFGLDFRIVDSEYVAQLRRERGLHANPWTSFPRLIVSMDWLRGERAQRLLRDvlpahadtPRAFDLLI 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983   72 IDEAHNVAVRGHDR----SQRARLAQLLSRRSDALIMLSATPHDGRAQSFASLMNMLDPTAIADEENYTPEDIEGLFIRR 147
Cdd:NF038317   245 VDEAHNVAPASPSKyavdSQRTRLIRDLAPHFEHRLFLSATPHNGYSESFTALLELLDPQRFARGVPPDEKQLDEVMVRR 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  148 FKGDVADQLGDKI-PSRELHRLNAQASLVEEQVFDAFAEldFSALDSPNAKSTGGR---MLFKTSLEKGLLSSPAAAMET 223
Cdd:NF038317   325 LKSDLVDRDGSPRfPERELEALPVDYSADEREIHELLDE--YTELRRKRLAGKRGRraaDFVTLLLKKRLFSSPAAFART 402
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  224 IDNRIKTIESR---------------------------------------ETADRY-----KDDVAQLQHLRRVLERVAP 259
Cdd:NF038317   403 LEVHRATLERGaarggplsdderllrddvlddeedyaddelleeaedealEEASELsppltAEERALLERLRAWAERAEA 482
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  260 EDFSKFQLLVDTLtddDSPFKFSGHFKDDRLVIFTERIATMRWLASHLPAAlGLDEKKVACLYGGMSDLDQQQVVEDF-- 337
Cdd:NF038317   483 RPDSKARALIDWL---RANLRPGGRWTNERVIVFTEYRDTLRWLVELLAAE-GYGGDRLALLHGGMDDDERERIKAAFqa 558
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  338 GRESSDIRLLIASDVASEGINLHYYCHRMVHFDIPWSLMVFQQRNGRVDRYGQTRTP-HIAYLSTLAQNERIYSDTRILE 416
Cdd:NF038317   559 DPSEHPVRILLATDAASEGIDLQNHCHRLIHYDIPWNPNRLEQRNGRIDRHGQRADPvLIWHFVGKGTEGAAEGDLEFLD 638
                          490       500
                   ....*....|....*....|.
gi 2157343983  417 ILVEKDDQASRNIGDPSALMG 437
Cdd:NF038317   639 RLARKVATIREDLGSVNPVIA 659
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
2-430 1.58e-39

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 156.15  E-value: 1.58e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983   2 LTQFQKELwSRFT--IPLVRLDSTglqRIRRKiptNQNPFHYFDRAIISVDTLKQNnefRHYLEQAHWDVIVIDEAHNVA 79
Cdd:COG0553   302 VGNWQREL-AKFApgLRVLVLDGT---RERAK---GANPFEDADLVITSYGLLRRD---IELLAAVDWDLVILDEAQHIK 371
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  80 VRghdRSQRARLAQLLsrRSDALIMLSATPHDGRAQSFASLMNMLDP-----------TAIADEENYTPEDIEGL----- 143
Cdd:COG0553   372 NP---ATKRAKAVRAL--KARHRLALTGTPVENRLEELWSLLDFLNPgllgslkafreRFARPIEKGDEEALERLrrllr 446
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 144 --FIRRFKGDVADQLGDKIPSRELHRLNAQaslvEEQVFDAFAELDFSALDSPNAKSTGGRMLFKTSLEKGLLSSPAAAM 221
Cdd:COG0553   447 pfLLRRTKEDVLKDLPEKTEETLYVELTPE----QRALYEAVLEYLRRELEGAEGIRRRGLILAALTRLRQICSHPALLL 522
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 222 EtiDNRIKTIESretadrykddvaqlqhlrrvlervapedfSKFQLLVDTLTDDDSpfkfsghfKDDRLVIFTERIATMR 301
Cdd:COG0553   523 E--EGAELSGRS-----------------------------AKLEALLELLEELLA--------EGEKVLVFSQFTDTLD 563
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 302 WLASHLpAALGLdekKVACLYGGMSDLDQQQVVEDFGRESSDIRLLIASDVASEGINLHyYCHRMVHFDIPWSLMVFQQR 381
Cdd:COG0553   564 LLEERL-EERGI---EYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLT-AADHVIHYDLWWNPAVEEQA 638
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 2157343983 382 NGRVDRYGQTRTPHIAYLstLAQNERiysDTRILEILVEKDDQASRNIG 430
Cdd:COG0553   639 IDRAHRIGQTRDVQVYKL--VAEGTI---EEKILELLEEKRALAESVLG 682
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
1-147 4.82e-33

DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 126.63  E-value: 4.82e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983   1 MLTQFQKELWSRFTIPLVRLDSTGLQRIRRKIptnQNPFHYFDRAIISVDTLKQNNEFRHYLEQAHWDVIVIDEAHNVAV 80
Cdd:cd18011    58 LVEQWQDELQDKFGLPFLILDRETAAQLRRLI---GNPFEEFPIVIVSLDLLKRSEERRGLLLSEEWDLVVVDEAHKLRN 134
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2157343983  81 R-GHDRSQRARLAQLLSRRSDALIMLSATPHDGRAQSFASLMNMLDPTAIAD-----EENYTPEDIEGLFIRR 147
Cdd:cd18011   135 SgGGKETKRYKLGRLLAKRARHVLLLTATPHNGKEEDFRALLSLLDPGRFAVlgrflRLDGLREVLAKVLLRR 207
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
263-399 3.55e-26

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 104.48  E-value: 3.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 263 SKFQLLVDTLTDDDSPfkfsghfkDDRLVIFTERIATMRWLASHLPAALgldeKKVACLYGGMSDLDQQQVVEDFGRESS 342
Cdd:cd18793    11 GKLEALLELLEELREP--------GEKVLIFSQFTDTLDILEEALRERG----IKYLRLDGSTSSKERQKLVDRFNEDPD 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2157343983 343 DIRLLIASDVASEGINLHYyCHRMVHFDIPWSLMVFQQRNGRVDRYGQTRTPHIAYL 399
Cdd:cd18793    79 IRVFLLSTKAGGVGLNLTA-ANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRL 134
DpdE NF041062
protein DpdE;
68-395 1.21e-18

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 91.19  E-value: 1.21e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983   68 DVIVIDEAHN-VAVRGHDRS-QRARLAQL--LSRRSDALIMLSATPHDGRAQSFASLMNMLDPtaiadeENYTPEDIEGl 143
Cdd:NF041062   252 DLLVVDEAHQlARLAWSGDPpERARYRELaaLAHAAPRLLLLSATPVLGNEETFLALLHLLDP------DLYPLDDLEA- 324
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  144 FIRRFK---------------------GDVADQLGDKIPS-RELHRL----------------NAQASLV---------- 175
Cdd:NF041062   325 FRERLEereelgrlvlgldpdnpnfllRQALDELRALFPEdEELQELaeellplldefddeepEERARAVsalrahiset 404
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  176 -------------------------------------EEQVFDAFAELDFSALDSPNAKSTGGRMLFKTSLekGLLSSPA 218
Cdd:NF041062   405 yrlhrrmirnrrssvlgadylvpgragprvlvwespaREAADEALEDWREEAALLDAESDPAARAAYARAL--AWLVARL 482
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  219 AAMETIDNRIKT-IESRETADRYKDDVAQLQHLRRVLERVApEDFSKFQLLVDTLTDddspfkfsgHFKDD-RLVIFTER 296
Cdd:NF041062   483 GGPDDLAALLRWrLRGDAASADLAGERELLEALIAALEDEA-KDADLLAALADWLLP---------LLRGSgKAVVFCGD 552
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  297 iatmRWLASHLPAALG-LDEKKVACLYGGMSDLDQQQVVEDFgRESSDIRLLIASDVASEGINLHYYChRMVHFDIPWSL 375
Cdd:NF041062   553 ----GSLADHLAAALArLGAGSVERHLSGQGADQAERAVRAF-RQDPSARVLVCDRSGEEGLNLQGAD-RLVHLDLPWSP 626
                          410       420
                   ....*....|....*....|
gi 2157343983  376 MVFQQRNGRVDRYGQTRTPH 395
Cdd:NF041062   627 NRLEQRIGRLDRYASLRGGR 646
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
286-389 1.57e-15

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: 73.01  E-value: 1.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 286 KDDRLVIFTERIATMRwlASHLPAALGLdekKVACLYGGMSDLDQQQVVEDFgrESSDIRLLIASDVASEGINLHYyCHR 365
Cdd:pfam00271  14 RGGKVLIFSQTKKTLE--AELLLEKEGI---KVARLHGDLSQEEREEILEDF--RKGKIDVLVATDVAERGLDLPD-VDL 85
                          90       100
                  ....*....|....*....|....
gi 2157343983 366 MVHFDIPWSLMVFQQRNGRVDRYG 389
Cdd:pfam00271  86 VINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
307-389 2.90e-14

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 68.39  E-value: 2.90e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  307 LPAALGLDEKKVACLYGGMSDLDQQQVVEDFgrESSDIRLLIASDVASEGINLHYyCHRMVHFDIPWSLMVFQQRNGRVD 386
Cdd:smart00490   3 LAELLKELGIKVARLHGGLSQEEREEILDKF--NNGKIKVLVATDVAERGLDLPG-VDLVIIYDLPWSPASYIQRIGRAG 79

                   ...
gi 2157343983  387 RYG 389
Cdd:smart00490  80 RAG 82
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
261-384 2.10e-09

C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 56.45  E-value: 2.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 261 DFSKFQLLVDTLtddDSPFKFSGHFkddRLVIFTERIATMRWLaSHLPAALGLDEKKVACLY------------GGMSDL 328
Cdd:cd18802     5 VIPKLQKLIEIL---REYFPKTPDF---RGIIFVERRATAVVL-SRLLKEHPSTLAFIRCGFligrgnssqrkrSLMTQR 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2157343983 329 DQQQVVEDFgrESSDIRLLIASDVASEGINLHyYCHRMVHFDIPWSLMVFQQRNGR 384
Cdd:cd18802    78 KQKETLDKF--RDGELNLLIATSVLEEGIDVP-ACNLVIRFDLPKTLRSYIQSRGR 130
PRK04914 PRK04914
RNA polymerase-associated protein RapA;
37-404 4.10e-09

RNA polymerase-associated protein RapA;


Pssm-ID: 235319 [Multi-domain]  Cd Length: 956  Bit Score: 60.24  E-value: 4.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  37 NPFHYFDRAIISVDTLKQNNEFRHYLEQAHWDVIVIDEAHNVAVRGHDRSQRARLAQLLSRRSDALIMLSATPHD-GRAQ 115
Cdd:PRK04914  243 NPFETEQLVICSLDFLRRNKQRLEQALAAEWDLLVVDEAHHLVWSEEAPSREYQVVEQLAEVIPGVLLLTATPEQlGQES 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 116 SFASLmNMLDP-------TAIADEENYTPedieglfirrfkgdVADQ----LGDKIPSRELHrlNAQASLVEEQ-VFDAF 183
Cdd:PRK04914  323 HFARL-RLLDPdrfhdyeAFVEEQQQYRP--------------VADAvqalLAGEKLSDDAL--NALGELLGEQdIEPLL 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 184 AELDFSALDSPNAKST---------G-GRMLFKTSLE--KGL---------LSSPAAAMETIDnriKTIESRETADRYKD 242
Cdd:PRK04914  386 QAANSDSEEAQAARQEliselldrhGtGRVLFRNTRAavKGFpkrelhpipLPLPEQYQTAIK---VSLEARARDMLYPE 462
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 243 DVAQLQhlrrvlERVAP--EDFSKFQLLVDTLTDddspfkfsgHFKDDRLVIfteriatmrwlASHLPAALGLDEK---- 316
Cdd:PRK04914  463 QIYQEF------EDNATwwNFDPRVEWLIDFLKS---------HRSEKVLVI-----------CAKAATALQLEQAlrer 516
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 317 ---KVACLYGGMSDLDQQQVVEDFGRESSDIRLLIASDVASEGINLHyYCHRMVHFDIPWSLMVFQQRNGRVDRYGQTRT 393
Cdd:PRK04914  517 egiRAAVFHEGMSIIERDRAAAYFADEEDGAQVLLCSEIGSEGRNFQ-FASHLVLFDLPFNPDLLEQRIGRLDRIGQKHD 595
                         410
                  ....*....|...
gi 2157343983 394 P--HIAYLSTLAQ 404
Cdd:PRK04914  596 IqiHVPYLEGTAQ 608
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
260-391 4.39e-09

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: 55.21  E-value: 4.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 260 EDFSKFQLLVDTLTDDDSPFKFsghfkddrlVIFTERIATMRWLAshlpAALGLDEKKVACLYGGMSDLDQQQVVEDFgr 339
Cdd:cd18787     9 EEEEKKLLLLLLLLEKLKPGKA---------IIFVNTKKRVDRLA----ELLEELGIKVAALHGDLSQEERERALKKF-- 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2157343983 340 ESSDIRLLIASDVASEGI---NLHYychrMVHFDIPWSLMVFQQRNGRVDRYGQT 391
Cdd:cd18787    74 RSGKVRVLVATDVAARGLdipGVDH----VINYDLPRDAEDYVHRIGRTGRAGRK 124
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
256-391 6.51e-08

Superfamily II DNA and RNA helicase [Replication, recombination and repair];


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 55.54  E-value: 6.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 256 RVAPEDfsKFQLLVDTLTDDDspfkfsghfkDDRLVIFTERIATMRWLASHLPAAlGLdekKVACLYGGMSDLDQQQVVE 335
Cdd:COG0513   222 LVDKRD--KLELLRRLLRDED----------PERAIVFCNTKRGADRLAEKLQKR-GI---SAAALHGDLSQGQRERALD 285
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 336 DFgrESSDIRLLIASDVASEGINL----HyychrMVHFDIPWSLMVFQQRNGRVDRYGQT 391
Cdd:COG0513   286 AF--RNGKIRVLVATDVAARGIDIddvsH-----VINYDLPEDPEDYVHRIGRTGRAGAE 338
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
2-126 2.90e-07

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 51.41  E-value: 2.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983   2 LTQFQKELwSRFT--IPLVRLDSTGLQRIRRKIPTNQNPFHYFdraIISVDTLKQNnefRHYLEQAHWDVIVIDEAHNVa 79
Cdd:cd17919    62 LENWEREF-EKWTpdLRVVVYHGSQRERAQIRAKEKLDKFDVV---LTTYETLRRD---KASLRKFRWDLVVVDEAHRL- 133
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2157343983  80 vrghdRSQRARLAQLLSR-RSDALIMLSATPHDGRAQSFASLMNMLDP 126
Cdd:cd17919   134 -----KNPKSQLSKALKAlRAKRRLLLTGTPLQNNLEELWALLDFLDP 176
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
2-542 2.34e-06

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 51.18  E-value: 2.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983   2 LTQFQKELWSRFTIPLVrldSTGLQRIRRKIptnqnpfhyfdrAIISVDTLKQNNEFRHYleQAHWDVIVIDEAHNVAvr 81
Cdd:COG1061   140 LEQWAEELRRFLGDPLA---GGGKKDSDAPI------------TVATYQSLARRAHLDEL--GDRFGLVIIDEAHHAG-- 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  82 ghdRSQRARLAQLLSRRsdALIMLSATPH--DGRaqsfaslmnmldptaiadeenytpedieGLFIRRFKGDVADqlgdk 159
Cdd:COG1061   201 ---APSYRRILEAFPAA--YRLGLTATPFrsDGR----------------------------EILLFLFDGIVYE----- 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 160 IPSRELhrlnaqaslveeqvfdafaeldfsaldspnakstggrmlfktsLEKGLLSSPaaametidnRIKTIESRETADR 239
Cdd:COG1061   243 YSLKEA-------------------------------------------IEDGYLAPP---------EYYGIRVDLTDER 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 240 YKDDVAQlQHLRRVLERVAPEDFSKFQLLVDTltdddspfkfsgHFKDDRLVIFTERIATMRWLASHLPAAlgldEKKVA 319
Cdd:COG1061   271 AEYDALS-ERLREALAADAERKDKILRELLRE------------HPDDRKTLVFCSSVDHAEALAELLNEA----GIRAA 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 320 CLYGGMSDLDQQQVVEDFgrESSDIRLLIASDVASEGinlhyychrmvhFDIPW-----------SLMVFQQRNGRV--D 386
Cdd:COG1061   334 VVTGDTPKKEREEILEAF--RDGELRILVTVDVLNEG------------VDVPRldvaillrptgSPREFIQRLGRGlrP 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 387 RYGQTR-------TPHIAYLSTLAQNERIYSDTRIlEILVEKDDQASRNIGDPSALMGTYDVEEQELQTAEAIEGGASPD 459
Cdd:COG1061   400 APGKEDalvydfvGNDVPVLEELAKDLRDLAGYRV-EFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLL 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 460 AFLAAFETDNPLEALLKLSAASQQDQKRGEGPATDHLPALFANDYDYLREALYFLKSRYGFEVSFDDDAQRIDLRLNKTL 539
Cdd:COG1061   479 VLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALLRLEELAALLLKE 558

                  ...
gi 2157343983 540 RRA 542
Cdd:COG1061   559 LLR 561
DEXDc smart00487
DEAD-like helicases superfamily;
1-141 8.35e-06

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 47.49  E-value: 8.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983    1 MLTQFQKELWSRFTIPLVRLDSTGLQRIRRKIPTNQnpfhyFDRAIISVDTLKqNNEFRHYLEQAHWDVIVIDEAHNVav 80
Cdd:smart00487  70 WAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGK-----TDILVTTPGRLL-DLLENDKLSLSNVDLVILDEAHRL-- 141
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2157343983   81 rgHDRSQRARLAQLLSRRSDA--LIMLSATPHDGRAQSFASLMNMLDPTaiaDEENYTPEDIE 141
Cdd:smart00487 142 --LDGGFGDQLEKLLKLLPKNvqLLLLSATPPEEIENLLELFLNDPVFI---DVGFTPLEPIE 199
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
346-391 2.67e-05

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: 43.08  E-value: 2.67e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2157343983 346 LLIASDVASEGINLHYyCHRMVHFDIPWSLMVFQQRNGRVDRYGQT 391
Cdd:cd18785    25 ILVATNVLGEGIDVPS-LDTVIFFDPPSSAASYIQRVGRAGRGGKD 69
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
54-108 6.55e-04

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: 41.75  E-value: 6.55e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2157343983  54 QNNEFRHYLEQAHW----DVIVIDEAHNVAVRGHD-RSQRARLAQLLSRRSDALIM-LSAT 108
Cdd:cd17920   114 LSPDFLELLQRLPErkrlALIVVDEAHCVSQWGHDfRPDYLRLGRLRRALPGVPILaLTAT 174
recQ_fam TIGR00614
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ...
55-156 7.49e-04

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: 42.83  E-value: 7.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  55 NNEFRHYLEqAHWDV--IVIDEAHNVAVRGHD-RSQRARLAQLLSRRSDALIM-LSATPHDGRAQSFASLMNMLDP---T 127
Cdd:TIGR00614 115 SNRLLQTLE-ERKGItlIAVDEAHCISQWGHDfRPDYKALGSLKQKFPNVPVMaLTATASPSVREDILRQLNLLNPqifC 193
                          90       100
                  ....*....|....*....|....*....
gi 2157343983 128 AIADEENYTpediegLFIRRFKGDVADQL 156
Cdd:TIGR00614 194 TSFDRPNLY------YEVRRKTPKILEDL 216
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
59-126 1.30e-03

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 42.39  E-value: 1.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2157343983  59 RHYLEQ-AHWD--VIVIDEAHNVAVRGHD-RSQRARLAQLLSRRSDALIM-LSATPHDGRAQSFASLMNMLDP 126
Cdd:PRK11057  129 DNFLEHlAHWNpaLLAVDEAHCISQWGHDfRPEYAALGQLRQRFPTLPFMaLTATADDTTRQDIVRLLGLNDP 201
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
62-138 1.91e-03

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; Chromodomain-helicase-DNA-binding protein 6 (CHD6) is a DNA-dependent ATPase that plays a role in chromatin remodeling. It regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin. It activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2.2 and acts as a transcriptional repressor of different viruses including influenza virus or papillomavirus. During influenza virus infection, the viral polymerase complex localizes CHD6 to inactive chromatin where it gets degraded in a proteasome independent-manner. CHD6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350816 [Multi-domain]  Cd Length: 222  Bit Score: 40.41  E-value: 1.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2157343983  62 LEQAHWDVIVIDEAHNVAVRGHDRSQRARLAQLLSRrsdalIMLSATPHDGRAQSFASLMNMLDPTAIADEENYTPE 138
Cdd:cd18058   127 LKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALEHK-----VLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEE 198
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
62-133 1.96e-03

DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; Chromodomain-helicase-DNA-binding protein 6-9 (CHD6, CHD7, CHD8, and CHD9) are members of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350753 [Multi-domain]  Cd Length: 223  Bit Score: 40.69  E-value: 1.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2157343983  62 LEQAHWDVIVIDEAHNVavrghdRSQRARLAQ-LLSRRSDALIMLSATPHDGRAQSFASLMNMLDPTAIADEE 133
Cdd:cd17995   128 LRKIPWRVVVVDEAHRL------KNRNSKLLQgLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSE 194
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
46-136 3.11e-03

DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a like 1, also known as HARP) is recruited to stalled replication forks to promote repair and helps restart replication. It plays a role in DNA repair, telomere maintenance and replication fork stability in response to DNA replication stress. Mutations cause Schimke Immunoosseous Dysplasia. SMARCAL1 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: 350768 [Multi-domain]  Cd Length: 213  Bit Score: 39.88  E-value: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  46 IISVDTLKQNNEfrhYLEQAHWDVIVIDEAHNVAVRghdRSQRARLAQLLSRRSDALIMLSATPHDGRAQSFASLMNMLD 125
Cdd:cd18010    93 IVSYDLLRRLEK---QLLARKFKVVICDESHYLKNS---KAKRTKAALPLLKRAKRVILLSGTPALSRPIELFTQLDALD 166
                          90
                  ....*....|.
gi 2157343983 126 PTAIADEENYT 136
Cdd:cd18010   167 PKLFGRFHDFG 177
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
223-389 3.24e-03

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 40.67  E-value: 3.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 223 TIDNRIKTIESRETADrykDDVAQLQHLrrvlerVAPEDfsKFQLLVDTLTDDdspfkfsghfKDDRLVIFTERIATMRW 302
Cdd:PRK01297  292 TTDPAIVEIEPENVAS---DTVEQHVYA------VAGSD--KYKLLYNLVTQN----------PWERVMVFANRKDEVRR 350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983 303 LASHLPAalglDEKKVACLYGGMSDLDQQQVVEDFgRESSdIRLLIASDVASEGINLHYYCHrMVHFDIPWSLMVFQQRN 382
Cdd:PRK01297  351 IEERLVK----DGINAAQLSGDVPQHKRIKTLEGF-REGK-IRVLVATDVAGRGIHIDGISH-VINFTLPEDPDDYVHRI 423

                  ....*..
gi 2157343983 383 GRVDRYG 389
Cdd:PRK01297  424 GRTGRAG 430
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
61-168 5.46e-03

DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, also known as ALC1) is involved in DNA repair by regulating chromatin relaxation following DNA damage. CHD1L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350764 [Multi-domain]  Cd Length: 216  Bit Score: 38.96  E-value: 5.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983  61 YLEQAHWDVIVIDEAHNVavrghdRSQRARLAQLLSRRS-DALIMLSATPHDGRAQSFASLMNMLDPtaiadeeNYTPED 139
Cdd:cd18006   117 FLKSFPWASLVVDEAHRL------KNQNSLLHKTLSEFSvDFRLLLTGTPIQNSLQELYALLSFIEP-------NVFPKD 183
                          90       100
                  ....*....|....*....|....*....
gi 2157343983 140 IEGLFIRRFKgDVADQLGdkiPSRELHRL 168
Cdd:cd18006   184 KLDDFIKAYS-ETDDESE---TVEELHLL 208
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
3-126 5.74e-03

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 39.59  E-value: 5.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343983   3 TQFQKElWSRFTIPLVRLDSTGLQRIRRKIPTNQnpFHYFDRAIISVDTLKqnnefRHY--LEQAHWDVIVIDEAHNVav 80
Cdd:pfam00176  66 NEFERW-VSPPALRVVVLHGNKRPQERWKNDPNF--LADFDVVITTYETLR-----KHKelLKKVHWHRIVLDEGHRL-- 135
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2157343983  81 rghdRSQRARLAQ-LLSRRSDALIMLSATPHDGRAQSFASLMNMLDP 126
Cdd:pfam00176 136 ----KNSKSKLSKaLKSLKTRNRWILTGTPLQNNLEELWALLNFLRP 178
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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