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Conserved domains on  [gi|310616720|ref|NP_001099396|]
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probable ATP-dependent RNA helicase DHX37 [Rattus norvegicus]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 1000776)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; similar to ATP-dependent RNA helicase that is involved in translation initiation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HrpA super family cl34328
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
248-1036 8.45e-130

HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG1643:

Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 416.79  E-value: 8.45e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEDSIIgVTEPRRVAAVAMSQRVAKEmnLSHRV--- 324
Cdd:COG1643    10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRIG-MLEPRRLAARAAAERMAEE--LGEPVget 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  325 VSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIV-ALRakrhlP-LKLLI 402
Cdd:COG1643    87 VGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQpALR-----PdLKLLV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  403 MSATLRVEDFtqnQRLFTtPPPVIKVESRQFPVTVHFNKRTPLD-DYSGECFRKVCKIHRMlPAGGILVFLTGQAEVHAL 481
Cdd:COG1643   162 MSATLDAERF---ARLLG-DAPVIESSGRTYPVEVRYRPLPADErDLEDAVADAVREALAE-EPGDILVFLPGEREIRRT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  482 CRRLRKAfpircsqpqemeedsaegmrrfkksrtrarkaqamalpqinldnysvlpagegdedreaemddeeeaLGSDLD 561
Cdd:COG1643   237 AEALRGR-------------------------------------------------------------------LPPDTE 249
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  562 ldlgdseanegeqpdaslplhVLPLYSLLAPEKQAQVFKPPPEGTRLCVIATNVAETSLTIPGIKYVVDCGKVKKRYYDR 641
Cdd:COG1643   250 ---------------------ILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDP 308
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  642 VTGVSSFRVTWVSQASADQRAGRAGRTEPGHCYRLYSSAVFGDFEQFPPPEITRrpvEDL---ILQMKALNIEKVINFPF 718
Cdd:COG1643   309 RSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARRPAFTDPEILR---ADLaslILELAAWGLGDPEDLPF 385
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  719 PTPPSVEALIAAEELLIALGALQAPPKqermkklqmsqlscpITALGRTMSTFPVAPRYAKMLALSQQHGCLPYTIAIVA 798
Cdd:COG1643   386 LDPPPARAIADARALLQELGALDADGR---------------LTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAA 450
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  799 AMTVRELFeeldRPAASeeelaelkgrrtrvaqmkrtwagqgaslklGDLMVLLGAVGACEYAgcspqfcQANGLRYKAM 878
Cdd:COG1643   451 LLSERDPR----RGAAG------------------------------SDLLARLNLWRRLREQ-------QREFLSYLRL 489
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  879 LEIRRLRGQLTTAVNavcpeaglfldpkmQPPTESQVTYLR--QIMAAGLGDHLARRVQsedlldpkwknayktpllDDP 956
Cdd:COG1643   490 REWRDLARQLRRLLG--------------EGANEEPADYEAigLLLALAYPDRIARRRG------------------EGG 537
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  957 VF---------IHPSSVLFRElpEFVVYQEIVET---TKMYMkgVSTVEIQWIPSLLPSYCQfdaplEEPAPTYCPESGR 1024
Cdd:COG1643   538 RYllargrgaaLFPGSPLAKK--EWLVAAELVGGaaeARIRL--AAPIDPEWLEELAAHLIK-----RYSEPHWDKKRGR 608
                         810
                  ....*....|..
gi 310616720 1025 VLCHRASVFYRV 1036
Cdd:COG1643   609 VVARERVRLGAL 620
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
248-1036 8.45e-130

HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 416.79  E-value: 8.45e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEDSIIgVTEPRRVAAVAMSQRVAKEmnLSHRV--- 324
Cdd:COG1643    10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRIG-MLEPRRLAARAAAERMAEE--LGEPVget 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  325 VSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIV-ALRakrhlP-LKLLI 402
Cdd:COG1643    87 VGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQpALR-----PdLKLLV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  403 MSATLRVEDFtqnQRLFTtPPPVIKVESRQFPVTVHFNKRTPLD-DYSGECFRKVCKIHRMlPAGGILVFLTGQAEVHAL 481
Cdd:COG1643   162 MSATLDAERF---ARLLG-DAPVIESSGRTYPVEVRYRPLPADErDLEDAVADAVREALAE-EPGDILVFLPGEREIRRT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  482 CRRLRKAfpircsqpqemeedsaegmrrfkksrtrarkaqamalpqinldnysvlpagegdedreaemddeeeaLGSDLD 561
Cdd:COG1643   237 AEALRGR-------------------------------------------------------------------LPPDTE 249
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  562 ldlgdseanegeqpdaslplhVLPLYSLLAPEKQAQVFKPPPEGTRLCVIATNVAETSLTIPGIKYVVDCGKVKKRYYDR 641
Cdd:COG1643   250 ---------------------ILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDP 308
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  642 VTGVSSFRVTWVSQASADQRAGRAGRTEPGHCYRLYSSAVFGDFEQFPPPEITRrpvEDL---ILQMKALNIEKVINFPF 718
Cdd:COG1643   309 RSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARRPAFTDPEILR---ADLaslILELAAWGLGDPEDLPF 385
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  719 PTPPSVEALIAAEELLIALGALQAPPKqermkklqmsqlscpITALGRTMSTFPVAPRYAKMLALSQQHGCLPYTIAIVA 798
Cdd:COG1643   386 LDPPPARAIADARALLQELGALDADGR---------------LTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAA 450
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  799 AMTVRELFeeldRPAASeeelaelkgrrtrvaqmkrtwagqgaslklGDLMVLLGAVGACEYAgcspqfcQANGLRYKAM 878
Cdd:COG1643   451 LLSERDPR----RGAAG------------------------------SDLLARLNLWRRLREQ-------QREFLSYLRL 489
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  879 LEIRRLRGQLTTAVNavcpeaglfldpkmQPPTESQVTYLR--QIMAAGLGDHLARRVQsedlldpkwknayktpllDDP 956
Cdd:COG1643   490 REWRDLARQLRRLLG--------------EGANEEPADYEAigLLLALAYPDRIARRRG------------------EGG 537
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  957 VF---------IHPSSVLFRElpEFVVYQEIVET---TKMYMkgVSTVEIQWIPSLLPSYCQfdaplEEPAPTYCPESGR 1024
Cdd:COG1643   538 RYllargrgaaLFPGSPLAKK--EWLVAAELVGGaaeARIRL--AAPIDPEWLEELAAHLIK-----RYSEPHWDKKRGR 608
                         810
                  ....*....|..
gi 310616720 1025 VLCHRASVFYRV 1036
Cdd:COG1643   609 VVARERVRLGAL 620
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
248-428 8.73e-118

DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the human nervous system and has been linked to schizophrenia. It also negatively regulates poxviruses such as Myxoma virus. DEAH-box helicase 37 (DHX37) belongs to 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: 350740 [Multi-domain]  Cd Length: 191  Bit Score: 361.67  E-value: 8.73e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEDS----IIGVTEPRRVAAVAMSQRVAKEMNLSHR 323
Cdd:cd17982     1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSPESdnpgMIGITQPRRVAAVSMAKRVAEELNVFGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  324 VVSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAK------RHLP 397
Cdd:cd17982    81 EVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdqTVKP 160
                         170       180       190
                  ....*....|....*....|....*....|.
gi 310616720  398 LKLLIMSATLRVEDFTQNQRLFTTPPPVIKV 428
Cdd:cd17982   161 LKLVIMSATLRVEDFTENKLLFPRPPPVIKV 191
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
248-1002 2.38e-99

RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria and a few high-GC Gram-positive bacteria. HrpA is about 1300 amino acids long, while its paralog HrpB, also uncharacterized, is about 800 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. The HrpA/B homolog from Borrelia is 500 amino acids shorter but appears to be derived from HrpA rather than HrpB. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273900 [Multi-domain]  Cd Length: 1283  Bit Score: 343.67  E-value: 2.38e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEdSIIGVTEPRRVAAVAMSQRVAKEMNLS-HRVVS 326
Cdd:TIGR01967   66 LPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRGSH-GLIGHTQPRRLAARTVAQRIAEELGTPlGEKVG 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   327 YQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIValraKRHLPLKLLIMSAT 406
Cdd:TIGR01967  145 YKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLL----PRRPDLKIIITSAT 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   407 LRVEDFTqnqRLFTTPPpVIKVESRQFPVTVHFNkrtPLDDYSGE--------CFRKVCKIHRMLPaGGILVFLTGQAEv 478
Cdd:TIGR01967  221 IDPERFS---RHFNNAP-IIEVSGRTYPVEVRYR---PLVEEQEDddldqleaILDAVDELFAEGP-GDILIFLPGERE- 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   479 halcrrlrkafpIRcsqpqemeeDSAEGMRRfkksrtrarkaqamalpqinldnysvlpagegdedreaemddeeealgs 558
Cdd:TIGR01967  292 ------------IR---------DAAEILRK------------------------------------------------- 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   559 dldLDLGDSEanegeqpdaslplhVLPLYSLLAPEKQAQVFKPppEGTRLCVIATNVAETSLTIPGIKYVVDCGKVKKRY 638
Cdd:TIGR01967  302 ---RNLRHTE--------------ILPLYARLSNKEQQRVFQP--HSGRRIVLATNVAETSLTVPGIHYVIDTGTARISR 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   639 YDRVTGVSSFRVTWVSQASADQRAGRAGRTEPGHCYRLYSSAVFGDFEQFPPPEITRRPVEDLILQMKALNIEKVINFPF 718
Cdd:TIGR01967  363 YSYRTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPEFTDPEILRTNLASVILQMLALRLGDIAAFPF 442
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   719 PTPPSVEALIAAEELLIALGALQappKQERMKKLqmsqlscpiTALGRTMSTFPVAPRYAKMLALSQQHGCLPYTIAIVA 798
Cdd:TIGR01967  443 IEAPDPRAIRDGFRLLEELGALD---DDEAEPQL---------TPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIAS 510
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   799 AMTVRELFEE-LDRPAASEEELAELKGRRTRVAQMKRTWAGqgaslklgdlmvllgaVGACEYAGCSPQFCQANGLRYKA 877
Cdd:TIGR01967  511 ALSIQDPRERpMEKQQAADQAHARFKDPRSDFLSRVNLWRH----------------IEEQRQALSANQFRNACRKQYLN 574
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   878 MLEIRRLRgQLTTAVNAVCPEAGLFLDpkmQPPTESQVtyLRQIMAAGLGDHLARRVQSEDLLDPKWKNayktpllddpV 957
Cdd:TIGR01967  575 YLRVREWQ-DIYRQLTQVVKELGLKLN---EEPADYDA--IHKALLSGLLSQIGMKDEKHEYDGARGRK----------F 638
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....*
gi 310616720   958 FIHPSSVLFRELPEFVVYQEIVETTKMYMKGVSTVEIQWIPSLLP 1002
Cdd:TIGR01967  639 HIFPGSPLFKKPPKWVMAAELVETSKLYARLVAKIEPEWVEPVAG 683
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
248-1000 2.68e-96

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 334.72  E-value: 2.68e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEdSIIGVTEPRRVAAVAMSQRVAKEMNLS-HRVVS 326
Cdd:PRK11131   73 LPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVK-GLIGHTQPRRLAARTVANRIAEELETElGGCVG 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  327 YQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKrhlpLKLLIMSAT 406
Cdd:PRK11131  152 YKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPD----LKVIITSAT 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  407 LRVEDFTqnqRLFTTpPPVIKVESRQFPVTVHFNKRTPLDDYSGE-----CFRKVCKIHRMLPaGGILVFLTGQAEvhal 481
Cdd:PRK11131  228 IDPERFS---RHFNN-APIIEVSGRTYPVEVRYRPIVEEADDTERdqlqaIFDAVDELGREGP-GDILIFMSGERE---- 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  482 crrlrkafpIRcsqpqemeeDSAEGMRRfkksrtrarkaqamalpqinldnysvlpagegdedreaemddeeealgsdld 561
Cdd:PRK11131  299 ---------IR---------DTADALNK---------------------------------------------------- 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  562 LDLGDSEanegeqpdaslplhVLPLYSLLAPEKQAQVFKppPEGTRLCVIATNVAETSLTIPGIKYVVDCGKVKKRYYDR 641
Cdd:PRK11131  309 LNLRHTE--------------ILPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSY 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  642 VTGVSSFRVTWVSQASADQRAGRAGRTEPGHCYRLYSSAVFGDFEQFPPPEITRRPVEDLILQMKALNIEKVINFPFPTP 721
Cdd:PRK11131  373 RTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLSRPEFTDPEILRTNLASVILQMTALGLGDIAAFPFVEA 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  722 PSVEALIAAEELLIALGALQAPPKQERMKklqmsqlscpITALGRTMSTFPVAPRYAKMLALSQQHGCLPYTIAIVAAMT 801
Cdd:PRK11131  453 PDKRNIQDGVRLLEELGAITTDEQASAYK----------LTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALS 522
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  802 VRELFEE-LDRPAASEEelaelKGRRTrvaqmkrtwagqgaSLKLGDLMVLLGA---VGACEYAGCSPQF---CQANGLR 874
Cdd:PRK11131  523 IQDPRERpMDKQQASDE-----KHRRF--------------ADKESDFLAFVNLwnyLQEQQKALSSNQFrrlCRTDYLN 583
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  875 YKAMLEIRRLRGQLTTAVNavcpEAGLfldpkmqpPTESQVTYLRQIMAA---GLGDHLARRVQSedlldpkwKNAYkTP 951
Cdd:PRK11131  584 YLRVREWQDIYTQLRQVVK----ELGI--------PVNSEPAEYREIHTAlltGLLSHIGMKDAE--------KQEY-TG 642
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....*....
gi 310616720  952 LLDDPVFIHPSSVLFRELPEFVVYQEIVETTKMYMKGVSTVEIQWIPSL 1000
Cdd:PRK11131  643 ARNARFSIFPGSGLFKKPPKWVMVAELVETSRLWGRIAARIEPEWIEPL 691
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
730-851 9.44e-29

Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 461295 [Multi-domain]  Cd Length: 104  Bit Score: 111.18  E-value: 9.44e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   730 AEELLIALGALQAPPKqermkklqmsqlscpITALGRTMSTFPVAPRYAKMLALSQQHGCLPYTIAIVAAMTVRELFEEL 809
Cdd:pfam04408    1 ALELLYYLGALDEDGE---------------LTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQP 65
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 310616720   810 DRPAASEEELAELKGRRTRVAQMKRTWAGQGaslKLGDLMVL 851
Cdd:pfam04408   66 NFLDPRSAAKAARRRRRAADEKARAKFARLD---LEGDHLTL 104
DEXDc smart00487
DEAD-like helicases superfamily;
254-414 3.31e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 104.50  E-value: 3.31e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720    254 EQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEDSIIGVTEPRRVAAVAMSQRVAKEMNLSHRVV-------S 326
Cdd:smart00487   14 KEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVvglyggdS 93
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720    327 YQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLL-KYKVVIIDEAHERS--VYTDILLGLLSRivaLRAKRHlplkLLIM 403
Cdd:smart00487   94 KREQLRKLESGKTDILVTTPGRLLDLLENDKLSLsNVDLVILDEAHRLLdgGFGDQLEKLLKL---LPKNVQ----LLLL 166
                           170
                    ....*....|...
gi 310616720    404 SATL--RVEDFTQ 414
Cdd:smart00487  167 SATPpeEIENLLE 179
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
248-1036 8.45e-130

HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 416.79  E-value: 8.45e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEDSIIgVTEPRRVAAVAMSQRVAKEmnLSHRV--- 324
Cdd:COG1643    10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRIG-MLEPRRLAARAAAERMAEE--LGEPVget 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  325 VSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIV-ALRakrhlP-LKLLI 402
Cdd:COG1643    87 VGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQpALR-----PdLKLLV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  403 MSATLRVEDFtqnQRLFTtPPPVIKVESRQFPVTVHFNKRTPLD-DYSGECFRKVCKIHRMlPAGGILVFLTGQAEVHAL 481
Cdd:COG1643   162 MSATLDAERF---ARLLG-DAPVIESSGRTYPVEVRYRPLPADErDLEDAVADAVREALAE-EPGDILVFLPGEREIRRT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  482 CRRLRKAfpircsqpqemeedsaegmrrfkksrtrarkaqamalpqinldnysvlpagegdedreaemddeeeaLGSDLD 561
Cdd:COG1643   237 AEALRGR-------------------------------------------------------------------LPPDTE 249
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  562 ldlgdseanegeqpdaslplhVLPLYSLLAPEKQAQVFKPPPEGTRLCVIATNVAETSLTIPGIKYVVDCGKVKKRYYDR 641
Cdd:COG1643   250 ---------------------ILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDP 308
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  642 VTGVSSFRVTWVSQASADQRAGRAGRTEPGHCYRLYSSAVFGDFEQFPPPEITRrpvEDL---ILQMKALNIEKVINFPF 718
Cdd:COG1643   309 RSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARRPAFTDPEILR---ADLaslILELAAWGLGDPEDLPF 385
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  719 PTPPSVEALIAAEELLIALGALQAPPKqermkklqmsqlscpITALGRTMSTFPVAPRYAKMLALSQQHGCLPYTIAIVA 798
Cdd:COG1643   386 LDPPPARAIADARALLQELGALDADGR---------------LTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAA 450
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  799 AMTVRELFeeldRPAASeeelaelkgrrtrvaqmkrtwagqgaslklGDLMVLLGAVGACEYAgcspqfcQANGLRYKAM 878
Cdd:COG1643   451 LLSERDPR----RGAAG------------------------------SDLLARLNLWRRLREQ-------QREFLSYLRL 489
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  879 LEIRRLRGQLTTAVNavcpeaglfldpkmQPPTESQVTYLR--QIMAAGLGDHLARRVQsedlldpkwknayktpllDDP 956
Cdd:COG1643   490 REWRDLARQLRRLLG--------------EGANEEPADYEAigLLLALAYPDRIARRRG------------------EGG 537
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  957 VF---------IHPSSVLFRElpEFVVYQEIVET---TKMYMkgVSTVEIQWIPSLLPSYCQfdaplEEPAPTYCPESGR 1024
Cdd:COG1643   538 RYllargrgaaLFPGSPLAKK--EWLVAAELVGGaaeARIRL--AAPIDPEWLEELAAHLIK-----RYSEPHWDKKRGR 608
                         810
                  ....*....|..
gi 310616720 1025 VLCHRASVFYRV 1036
Cdd:COG1643   609 VVARERVRLGAL 620
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
248-428 8.73e-118

DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the human nervous system and has been linked to schizophrenia. It also negatively regulates poxviruses such as Myxoma virus. DEAH-box helicase 37 (DHX37) belongs to 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: 350740 [Multi-domain]  Cd Length: 191  Bit Score: 361.67  E-value: 8.73e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEDS----IIGVTEPRRVAAVAMSQRVAKEMNLSHR 323
Cdd:cd17982     1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSPESdnpgMIGITQPRRVAAVSMAKRVAEELNVFGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  324 VVSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAK------RHLP 397
Cdd:cd17982    81 EVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdqTVKP 160
                         170       180       190
                  ....*....|....*....|....*....|.
gi 310616720  398 LKLLIMSATLRVEDFTQNQRLFTTPPPVIKV 428
Cdd:cd17982   161 LKLVIMSATLRVEDFTENKLLFPRPPPVIKV 191
DEAH_box_HrpA TIGR01967
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ...
248-1002 2.38e-99

RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria and a few high-GC Gram-positive bacteria. HrpA is about 1300 amino acids long, while its paralog HrpB, also uncharacterized, is about 800 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. The HrpA/B homolog from Borrelia is 500 amino acids shorter but appears to be derived from HrpA rather than HrpB. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273900 [Multi-domain]  Cd Length: 1283  Bit Score: 343.67  E-value: 2.38e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEdSIIGVTEPRRVAAVAMSQRVAKEMNLS-HRVVS 326
Cdd:TIGR01967   66 LPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRGSH-GLIGHTQPRRLAARTVAQRIAEELGTPlGEKVG 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   327 YQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIValraKRHLPLKLLIMSAT 406
Cdd:TIGR01967  145 YKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLL----PRRPDLKIIITSAT 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   407 LRVEDFTqnqRLFTTPPpVIKVESRQFPVTVHFNkrtPLDDYSGE--------CFRKVCKIHRMLPaGGILVFLTGQAEv 478
Cdd:TIGR01967  221 IDPERFS---RHFNNAP-IIEVSGRTYPVEVRYR---PLVEEQEDddldqleaILDAVDELFAEGP-GDILIFLPGERE- 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   479 halcrrlrkafpIRcsqpqemeeDSAEGMRRfkksrtrarkaqamalpqinldnysvlpagegdedreaemddeeealgs 558
Cdd:TIGR01967  292 ------------IR---------DAAEILRK------------------------------------------------- 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   559 dldLDLGDSEanegeqpdaslplhVLPLYSLLAPEKQAQVFKPppEGTRLCVIATNVAETSLTIPGIKYVVDCGKVKKRY 638
Cdd:TIGR01967  302 ---RNLRHTE--------------ILPLYARLSNKEQQRVFQP--HSGRRIVLATNVAETSLTVPGIHYVIDTGTARISR 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   639 YDRVTGVSSFRVTWVSQASADQRAGRAGRTEPGHCYRLYSSAVFGDFEQFPPPEITRRPVEDLILQMKALNIEKVINFPF 718
Cdd:TIGR01967  363 YSYRTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPEFTDPEILRTNLASVILQMLALRLGDIAAFPF 442
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   719 PTPPSVEALIAAEELLIALGALQappKQERMKKLqmsqlscpiTALGRTMSTFPVAPRYAKMLALSQQHGCLPYTIAIVA 798
Cdd:TIGR01967  443 IEAPDPRAIRDGFRLLEELGALD---DDEAEPQL---------TPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIAS 510
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   799 AMTVRELFEE-LDRPAASEEELAELKGRRTRVAQMKRTWAGqgaslklgdlmvllgaVGACEYAGCSPQFCQANGLRYKA 877
Cdd:TIGR01967  511 ALSIQDPRERpMEKQQAADQAHARFKDPRSDFLSRVNLWRH----------------IEEQRQALSANQFRNACRKQYLN 574
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   878 MLEIRRLRgQLTTAVNAVCPEAGLFLDpkmQPPTESQVtyLRQIMAAGLGDHLARRVQSEDLLDPKWKNayktpllddpV 957
Cdd:TIGR01967  575 YLRVREWQ-DIYRQLTQVVKELGLKLN---EEPADYDA--IHKALLSGLLSQIGMKDEKHEYDGARGRK----------F 638
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....*
gi 310616720   958 FIHPSSVLFRELPEFVVYQEIVETTKMYMKGVSTVEIQWIPSLLP 1002
Cdd:TIGR01967  639 HIFPGSPLFKKPPKWVMAAELVETSKLYARLVAKIEPEWVEPVAG 683
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
248-1000 2.68e-96

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 334.72  E-value: 2.68e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEdSIIGVTEPRRVAAVAMSQRVAKEMNLS-HRVVS 326
Cdd:PRK11131   73 LPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVK-GLIGHTQPRRLAARTVANRIAEELETElGGCVG 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  327 YQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKrhlpLKLLIMSAT 406
Cdd:PRK11131  152 YKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPD----LKVIITSAT 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  407 LRVEDFTqnqRLFTTpPPVIKVESRQFPVTVHFNKRTPLDDYSGE-----CFRKVCKIHRMLPaGGILVFLTGQAEvhal 481
Cdd:PRK11131  228 IDPERFS---RHFNN-APIIEVSGRTYPVEVRYRPIVEEADDTERdqlqaIFDAVDELGREGP-GDILIFMSGERE---- 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  482 crrlrkafpIRcsqpqemeeDSAEGMRRfkksrtrarkaqamalpqinldnysvlpagegdedreaemddeeealgsdld 561
Cdd:PRK11131  299 ---------IR---------DTADALNK---------------------------------------------------- 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  562 LDLGDSEanegeqpdaslplhVLPLYSLLAPEKQAQVFKppPEGTRLCVIATNVAETSLTIPGIKYVVDCGKVKKRYYDR 641
Cdd:PRK11131  309 LNLRHTE--------------ILPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSY 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  642 VTGVSSFRVTWVSQASADQRAGRAGRTEPGHCYRLYSSAVFGDFEQFPPPEITRRPVEDLILQMKALNIEKVINFPFPTP 721
Cdd:PRK11131  373 RTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLSRPEFTDPEILRTNLASVILQMTALGLGDIAAFPFVEA 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  722 PSVEALIAAEELLIALGALQAPPKQERMKklqmsqlscpITALGRTMSTFPVAPRYAKMLALSQQHGCLPYTIAIVAAMT 801
Cdd:PRK11131  453 PDKRNIQDGVRLLEELGAITTDEQASAYK----------LTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALS 522
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  802 VRELFEE-LDRPAASEEelaelKGRRTrvaqmkrtwagqgaSLKLGDLMVLLGA---VGACEYAGCSPQF---CQANGLR 874
Cdd:PRK11131  523 IQDPRERpMDKQQASDE-----KHRRF--------------ADKESDFLAFVNLwnyLQEQQKALSSNQFrrlCRTDYLN 583
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  875 YKAMLEIRRLRGQLTTAVNavcpEAGLfldpkmqpPTESQVTYLRQIMAA---GLGDHLARRVQSedlldpkwKNAYkTP 951
Cdd:PRK11131  584 YLRVREWQDIYTQLRQVVK----ELGI--------PVNSEPAEYREIHTAlltGLLSHIGMKDAE--------KQEY-TG 642
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....*....
gi 310616720  952 LLDDPVFIHPSSVLFRELPEFVVYQEIVETTKMYMKGVSTVEIQWIPSL 1000
Cdd:PRK11131  643 ARNARFSIFPGSGLFKKPPKWVMVAELVETSRLWGRIAARIEPEWIEPL 691
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
264-428 2.32e-67

DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family belongs to 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: 438707 [Multi-domain]  Cd Length: 159  Bit Score: 223.49  E-value: 2.32e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  264 HPIVIVCGETGSGKTTQVPQFLYEAGYSS-EDSIIGVTEPRRVAAVAMSQRVAKEMNLSH-RVVSYQIRYEGNVTEETRI 341
Cdd:cd17917     1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKgGKGRIVCTQPRRIAAISVAERVAEERGEKLgEEVGYQIRFESKTSSKTRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  342 KFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIValraKRHLPLKLLIMSATLRVEDFTQnqrlFTT 421
Cdd:cd17917    81 KFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLL----RKRPDLKVILMSATLDAEKFSS----YFG 152

                  ....*..
gi 310616720  422 PPPVIKV 428
Cdd:cd17917   153 GAPVIHI 159
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
248-414 1.39e-65

DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA polymerase I transcription of the 47S precursor rRNA. DHX33 belongs to 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: 438710 [Multi-domain]  Cd Length: 178  Bit Score: 219.15  E-value: 1.39e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSsEDSIIGVTEPRRVAAVAMSQRVAKEMNLSH-RVVS 326
Cdd:cd17978     1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFA-RGGMIGITQPRRVAAVSVAKRVAEEMGVELgQLVG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  327 YQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKRHL-PLKLLIMSA 405
Cdd:cd17978    80 YSVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRKEQKLsPLKVIIMSA 159

                  ....*....
gi 310616720  406 TLRVEDFTQ 414
Cdd:cd17978   160 TLDADLFSE 168
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
433-677 4.72e-60

C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members 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: 350178 [Multi-domain]  Cd Length: 171  Bit Score: 203.15  E-value: 4.72e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  433 FPVTVHFNKRT----------PLDDYSGECFRKVCKIHRMLPAGGILVFLTGQAEVHALCRRLRKafpircsqpqemeed 502
Cdd:cd18791     1 FPVEVYYLEDIlellgissekEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLRE--------------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  503 saegmrrfkksrtrarkaqamalpqinldnysvlpagegdedreaemddeeealgsdldldlgdsEANEGEQPDaslpLH 582
Cdd:cd18791    66 -----------------------------------------------------------------ELLSPDLGK----LL 76
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  583 VLPLYSLLAPEKQAQVFKPPPEGTRLCVIATNVAETSLTIPGIKYVVDCGKVKKRYYDRVTGVSSFRVTWVSQASADQRA 662
Cdd:cd18791    77 VLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRA 156
                         250
                  ....*....|....*
gi 310616720  663 GRAGRTEPGHCYRLY 677
Cdd:cd18791   157 GRAGRTRPGKCYRLY 171
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
248-800 3.29e-59

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 219.41  E-value: 3.29e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVP-QFLYEAGYSSEdsIIgVTEPRRVAAVAMSQRVAKEMNlsHRV-- 324
Cdd:PRK11664    4 LPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPlQLLQHGGINGK--II-MLEPRRLAARNVAQRLAEQLG--EKPge 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  325 -VSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRI-VALRAKrhlpLKLLI 402
Cdd:PRK11664   79 tVGYRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLDVqQGLRDD----LKLLI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  403 MSATLrvedftQNQRLFTTPP--PVIKVESRQFPVTVHF---NKRTPLDDysgecfrKVCK-IHRML--PAGGILVFLTG 474
Cdd:PRK11664  155 MSATL------DNDRLQQLLPdaPVIVSEGRSFPVERRYqplPAHQRFDE-------AVARaTAELLrqESGSLLLFLPG 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  475 QAEVHALCRRLRkafpircsqpqemeedsaegmrrfkksrtrarkaqamalpqinldnysvlpagegdedreaemddeeE 554
Cdd:PRK11664  222 VGEIQRVQEQLA-------------------------------------------------------------------S 234
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  555 ALGSDLDLdlgdseanegeqpdaslplhvLPLYSLLAPEKQAQVFKPPPEGTRLCVIATNVAETSLTIPGIKYVVDCGKV 634
Cdd:PRK11664  235 RVASDVLL---------------------CPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLE 293
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  635 KKRYYDRVTGVSSFRVTWVSQASADQRAGRAGRTEPGHCYRLYSSAVFGDFEQFPPPEITRRPVEDLIL----------- 703
Cdd:PRK11664  294 RVARFDPKTGLTRLVTQRISQASMTQRAGRAGRLEPGICLHLYSKEQAERAAAQSEPEILHSDLSGLLLellqwgchdpa 373
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  704 QMKALNIekvinfpfptPPSVeALIAAEELLIALGALQappkqermkklQMSQLscpiTALGRTMSTFPVAPRYAKMLAL 783
Cdd:PRK11664  374 QLSWLDQ----------PPAA-ALAAAKRLLQQLGALD-----------GQGRL----TARGRKMAALGNDPRLAAMLVA 427
                         570
                  ....*....|....*...
gi 310616720  784 SQQHG-CLPYTIAIVAAM 800
Cdd:PRK11664  428 AKEDDeAALATAAKLAAI 445
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
248-410 2.69e-54

DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to 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: 350742 [Multi-domain]  Cd Length: 178  Bit Score: 186.98  E-value: 2.69e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSsEDSIIGVTEPRRVAAVAMSQRVAKEMNLS-HRVVS 326
Cdd:cd17984     1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFS-QHGMIGVTQPRRVAAISVAQRVAEEMKCTlGSKVG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  327 YQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAK-RHLPLKLLIMSA 405
Cdd:cd17984    80 YQVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSPnRKEHLKVVVMSA 159

                  ....*
gi 310616720  406 TLRVE 410
Cdd:cd17984   160 TLELA 164
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
248-412 5.56e-54

DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and seems to be associated with risk to thyroid cancers. It also has been shown to positively regulate poxviruses, such as Myxoma virus. DEAH-box helicase 35 (DHX35) belongs to 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: 350738 [Multi-domain]  Cd Length: 185  Bit Score: 186.52  E-value: 5.56e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEDSIIGVTEPRRVAAVAMSQRVAKEM--NLSHRvV 325
Cdd:cd17980     1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAGGRVVGCTQPRRVAAVTVAGRVAEEMgaVLGHE-V 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  326 SYQIRYEGNVTE-ETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKrhlpLKLLIMS 404
Cdd:cd17980    80 GYCIRFDDCTDPqATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGD----LRLIVAS 155

                  ....*...
gi 310616720  405 ATLRVEDF 412
Cdd:cd17980   156 ATLDAEKF 163
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
243-422 8.43e-52

DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as pre-mRNA-splicing factor ATP-dependent RNA helicase PRP22) acts late in the splicing of pre-mRNA and mediates the release of the spliced mRNA from spliceosomes. DHX8 belongs to 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: 350729 [Multi-domain]  Cd Length: 179  Bit Score: 179.99  E-value: 8.43e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  243 EERLKLPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEdSIIGVTEPRRVAAVAMSQRVAKEMN--L 320
Cdd:cd17971     1 EQRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSR-GKIGCTQPRRVAAMSVAKRVAEEFGccL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  321 SHRVvSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIValraKRHLPLKL 400
Cdd:cd17971    80 GQEV-GYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTV----QKRPDLKL 154
                         170       180
                  ....*....|....*....|....*
gi 310616720  401 LIMSATLRVEDFTQ---NQRLFTTP 422
Cdd:cd17971   155 IVTSATLDAVKFSQyfyEAPIFTIP 179
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
248-413 1.55e-51

DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably involved in pre-mRNA splicing. DHX16 belongs to 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: 350732 [Multi-domain]  Cd Length: 174  Bit Score: 178.85  E-value: 1.55e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEDSIIGVTEPRRVAAVAMSQRVAKEMN--LSHRvV 325
Cdd:cd17974     1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKGGGKIGCTQPRRVAAMSVAARVAEEMGvkLGNE-V 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  326 SYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKrhlpLKLLIMSA 405
Cdd:cd17974    80 GYSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPD----LKLLISSA 155

                  ....*...
gi 310616720  406 TLRVEDFT 413
Cdd:cd17974   156 TMDAEKFS 163
DEXHc_DHX38 cd17983
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ...
248-413 2.74e-51

DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as PRP16) is involved in pre-mRNA splicing. DHX38 belongs to 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: 350741 [Multi-domain]  Cd Length: 173  Bit Score: 178.04  E-value: 2.74e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSeDSIIGVTEPRRVAAVAMSQRVAKEMNLS-HRVVS 326
Cdd:cd17983     1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTD-YGMIGCTQPRRVAAMSVAKRVSEEMGVElGEEVG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  327 YQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKrhlpLKLLIMSAT 406
Cdd:cd17983    80 YAIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRD----LKLIVTSAT 155

                  ....*..
gi 310616720  407 LRVEDFT 413
Cdd:cd17983   156 MDADKFA 162
DEXHc_DHX15 cd17973
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ...
236-423 4.01e-51

DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA. DHX15 belongs to 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: 438709 [Multi-domain]  Cd Length: 187  Bit Score: 178.38  E-value: 4.01e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  236 NRTPEMQEERLKLPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYS-SEDSIIGVTEPRRVAAVAMSQRV 314
Cdd:cd17973     1 QRYFEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPhQPKKLVACTQPRRVAAMSVAQRV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  315 AKEMNLS-HRVVSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAK 393
Cdd:cd17973    81 AEEMDVKlGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRPD 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 310616720  394 rhlpLKLLIMSATLRVEDFtqnQRLFTTPP 423
Cdd:cd17973   161 ----LKLIVMSATLDAGKF---QKYFDNAP 183
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
248-413 4.72e-47

DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in the nonsense-mediated decay (NMD), a surveillance mechanism that degrades aberrant mRNAs. DHX34 belongs to 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: 350737 [Multi-domain]  Cd Length: 170  Bit Score: 166.08  E-value: 4.72e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSedsiIGVTEPRRVAAVAMSQRVAKE-MNLSHRVVS 326
Cdd:cd17979     1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRH----IACTQPRRIACISLAKRVAFEsLNQYGSKVA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  327 YQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKrhlpLKLLIMSAT 406
Cdd:cd17979    77 YQIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPD----LKLILMSAT 152

                  ....*..
gi 310616720  407 LRVEDFT 413
Cdd:cd17979   153 INIELFS 159
DEXHc_HrpA cd17989
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ...
248-428 5.84e-47

DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpA belongs to 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: 350747 [Multi-domain]  Cd Length: 173  Bit Score: 165.71  E-value: 5.84e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEdSIIGVTEPRRVAAVAMSQRVAKEMNLS-HRVVS 326
Cdd:cd17989     1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRGIR-GLIGHTQPRRLAARSVAERIAEELKTElGGAVG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  327 YQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIValraKRHLPLKLLIMSAT 406
Cdd:cd17989    80 YKVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLL----PRRPDLKVIITSAT 155
                         170       180
                  ....*....|....*....|..
gi 310616720  407 LRVEDFTQNqrlFTTpPPVIKV 428
Cdd:cd17989   156 IDAERFSRH---FNN-APIIEV 173
DEXHc_DHX29 cd17975
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ...
248-428 3.07e-39

DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of the 43S pre-initiation complex involved in translation initiation of mRNAs with structured 5'-UTRs. DHX29 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: 350733 [Multi-domain]  Cd Length: 183  Bit Score: 144.29  E-value: 3.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYE----AGYSSEDSIIGVTEPRRVAAVAMSQRVAKEMNLS-- 321
Cdd:cd17975     1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEdlllNGGTAQKCNIVCTQPRRISAMSLATRVCEELGCEsg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  322 ----HRVVSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKRHlp 397
Cdd:cd17975    81 pggkNSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLH-- 158
                         170       180       190
                  ....*....|....*....|....*....|.
gi 310616720  398 lkLLIMSATLRVEDFTQnqrlFTTPPPVIKV 428
Cdd:cd17975   159 --LILMSATVDCEKFSS----YFTHCPILRI 183
DEXHc_DHX36 cd17981
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ...
248-414 2.61e-36

DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as G4-resolvase 1 or G4R1, MLE-like protein 1 and RNA helicase associated with AU-rich element or RHAU) unwinds a G4-quadruplex in human telomerase RNA. DHX36 belongs to 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: 350739 [Multi-domain]  Cd Length: 180  Bit Score: 135.74  E-value: 2.61e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLY----EAGYSSEDSIIgVTEPRRVAAVAMSQRVAKEMNLSH- 322
Cdd:cd17981     1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILddaiERGKGSSCRIV-CTQPRRISAISVAERVAAERAESCg 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  323 --RVVSYQIRYEGNVT-EETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRakrhLPLK 399
Cdd:cd17981    80 lgNSTGYQIRLESRKPrKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFR----SDLK 155
                         170
                  ....*....|....*
gi 310616720  400 LLIMSATLRVEDFTQ 414
Cdd:cd17981   156 VILMSATLNAEKFSD 170
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
248-428 1.42e-34

DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also known as HIG-1or NET54 or C14orf75) is a part of the nuclear PIWI-interacting RNA (piRNA) pathway essential for transposon silencing and male fertility TDRD9 belongs to 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: 350746 [Multi-domain]  Cd Length: 180  Bit Score: 130.70  E-value: 1.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGY-SSEDSIIGVTEPRRVAAVAMSQRVAKEMNLS-HRVV 325
Cdd:cd17988     1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYkRGKYCNIVVTQPRRIAAISIARRVSQEREWTlGSLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  326 SYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAkRHlpLKLLIMSA 405
Cdd:cd17988    81 GYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNS-RH--VKIILMSA 157
                         170       180
                  ....*....|....*....|...
gi 310616720  406 TLRVEDFTQNQRLFTTPPPVIKV 428
Cdd:cd17988   158 TISCKEFADYFTTPNNPAYVFEV 180
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
248-414 3.12e-34

DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to 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: 350743 [Multi-domain]  Cd Length: 177  Bit Score: 129.58  E-value: 3.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEA---GYSSEDSIIGVTEPRRVAAVAMSQRVAKEMnlSHRV 324
Cdd:cd17985     1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNslqGPPLPVANIICTQPRRISAISVAERVAQER--AERV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  325 ---VSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKrhlpLKLL 401
Cdd:cd17985    79 gqsVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPD----LKVI 154
                         170
                  ....*....|...
gi 310616720  402 IMSATLRVEDFTQ 414
Cdd:cd17985   155 LMSATLNAELFSD 167
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
248-428 3.77e-33

DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) regulates mRNA translation and stability via binding to N6-methyladenosine, a modified RNA nucleotide enriched in the stop codons and 3' UTRs of eukaryotic messenger RNAs. YTHDC2 belongs to 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: 350745 [Multi-domain]  Cd Length: 176  Bit Score: 126.48  E-value: 3.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEDSI-IGVTEPRRVAAVAMSQRVAKEMNLS-HRVV 325
Cdd:cd17987     1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANGIPCrIFCTQPRRLAAIAVAERVAAERGEKiGQTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  326 SYQIRYEGNVTEETRIKFMTDGVLLKEIQ-KDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIValraKRHLPLKLLIMS 404
Cdd:cd17987    81 GYQIRLESRVSPKTLLTFCTNGVLLRTLMaGDSALSTVTHVIVDEVHERDRFSDFLLTKLRDIL----QKHPNLKLILSS 156
                         170       180
                  ....*....|....*....|....
gi 310616720  405 ATLRVEDFTqnqRLFTTpPPVIKV 428
Cdd:cd17987   157 AALDVNLFI---RYFGS-CPVIYI 176
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
248-428 4.79e-33

DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an important role in the assembly of the mitochondrial large ribosomal subunit. DHX30 belongs to 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: 350734 [Multi-domain]  Cd Length: 178  Bit Score: 126.06  E-value: 4.79e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYE----AGYSSEDSIIgVTEPRRVAAVAMSQRVAKEM--NLS 321
Cdd:cd17976     1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEdyvlRGRGARCNVV-ITQPRRISAVSVAQRVAHELgpNLR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  322 HRvVSYQIRYEGNVTEE-TRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKrhlpLKL 400
Cdd:cd17976    80 RN-VGYQVRLESRPPPRgGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPE----LRV 154
                         170       180
                  ....*....|....*....|....*...
gi 310616720  401 LIMSATLRVEDFTQnqrlFTTPPPVIKV 428
Cdd:cd17976   155 VLMSATGDNQRLSR----YFGGCPVVRV 178
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
248-410 3.25e-30

DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to 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: 438711 [Multi-domain]  Cd Length: 174  Bit Score: 117.82  E-value: 3.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEDSIIgVTEPRRVAAVAMSQRVAKEMNLS-HRVVS 326
Cdd:cd17990     1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGGKII-VLEPRRVAARAAARRLATLLGEApGETVG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  327 YQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRivaLRAKRHLPLKLLIMSAT 406
Cdd:cd17990    80 YRVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLE---VQQLLRDDLRLLAMSAT 156

                  ....
gi 310616720  407 LRVE 410
Cdd:cd17990   157 LDGD 160
DEXHc_DHX32 cd17977
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ...
248-405 8.49e-29

DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to 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: 350735 [Multi-domain]  Cd Length: 176  Bit Score: 113.77  E-value: 8.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSS--EDSIIGVTEPRRVAAVAMSQRVAKEM--NLSHR 323
Cdd:cd17977     1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEYCLSAhyQHGVVVCTQVHKQTAVWLALRVADEMdvNIGHE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  324 VvSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKrhlpLKLLIM 403
Cdd:cd17977    81 V-GYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPE----LKLVII 155

                  ..
gi 310616720  404 SA 405
Cdd:cd17977   156 TC 157
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
730-851 9.44e-29

Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 461295 [Multi-domain]  Cd Length: 104  Bit Score: 111.18  E-value: 9.44e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   730 AEELLIALGALQAPPKqermkklqmsqlscpITALGRTMSTFPVAPRYAKMLALSQQHGCLPYTIAIVAAMTVRELFEEL 809
Cdd:pfam04408    1 ALELLYYLGALDEDGE---------------LTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQP 65
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 310616720   810 DRPAASEEELAELKGRRTRVAQMKRTWAGQGaslKLGDLMVL 851
Cdd:pfam04408   66 NFLDPRSAAKAARRRRRAADEKARAKFARLD---LEGDHLTL 104
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
243-428 2.15e-28

DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ATP-dependent RNA helicase A or RHA and leukophysin or LKP) plays an important role in many cellular processes, including regulation of DNA replication, transcription, translation, microRNA biogenesis, RNA processing and transport, and maintenance of genomic stability. DHX9 belongs to 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: 350730 [Multi-domain]  Cd Length: 234  Bit Score: 114.55  E-value: 2.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  243 EERLKLPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYE----AGYSSEDSIIgVTEPRRVAAVAMSQRVAKEM 318
Cdd:cd17972    54 QERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDdfiqNDRAAECNIV-VTQPRRISAVSVAERVAFER 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  319 NLS-HRVVSYQIRYEGNVTE-ETRIKFMTDGVLLKEIQKDFLLLKYkvVIIDEAHERSVYTDILLGLLSRIValraKRHL 396
Cdd:cd17972   133 GEEvGKSCGYSVRFESVLPRpHASILFCTVGVLLRKLEAGIRGISH--VIVDEIHERDINTDFLLVVLRDVV----QAYP 206
                         170       180       190
                  ....*....|....*....|....*....|..
gi 310616720  397 PLKLLIMSATLRVEDFTQnqrlFTTPPPVIKV 428
Cdd:cd17972   207 DLRVILMSATIDTSMFCE----YFFNCPVIEV 234
DEXDc smart00487
DEAD-like helicases superfamily;
254-414 3.31e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 104.50  E-value: 3.31e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720    254 EQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEDSIIGVTEPRRVAAVAMSQRVAKEMNLSHRVV-------S 326
Cdd:smart00487   14 KEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVvglyggdS 93
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720    327 YQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLL-KYKVVIIDEAHERS--VYTDILLGLLSRivaLRAKRHlplkLLIM 403
Cdd:smart00487   94 KREQLRKLESGKTDILVTTPGRLLDLLENDKLSLsNVDLVILDEAHRLLdgGFGDQLEKLLKL---LPKNVQ----LLLL 166
                           170
                    ....*....|...
gi 310616720    404 SATL--RVEDFTQ 414
Cdd:smart00487  167 SATPpeEIENLLE 179
DEXQc_DQX1 cd17986
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ...
248-428 3.51e-25

DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 (DQX1) belongs to 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: 350744 [Multi-domain]  Cd Length: 177  Bit Score: 103.44  E-value: 3.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  248 LPILAEEQAIMEAV-AEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEDS--IIGVTEPRRVAAVAMSQRVAKEM--NLSH 322
Cdd:cd17986     1 LPIWAAKFTFLEQLeSPSGIVLVSGEPGSGKSTQVPQWCAEFALSRGFQkgQVTVTQPHPLAARSLALRVADEMdlNLGH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  323 RVvSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKrhlpLKLLI 402
Cdd:cd17986    81 EV-GYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPE----LRVVV 155
                         170       180
                  ....*....|....*....|....*.
gi 310616720  403 MSATLRVEDFtqnqRLFTTPPPVIKV 428
Cdd:cd17986   156 VTSPALEPKL----RAFWGNPPVVHV 177
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
918-1004 1.86e-22

Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus of the DEAD-box helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. There do seem to be a couple of instances where it occurs by itself -. The structure PDB:3i4u adopts an OB-fold. helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. This C-terminal domain of the yeast helicase contains an oligonucleotide/oligosaccharide-binding (OB)-fold which seems to be placed at the entrance of the putative nucleic acid cavity. It also constitutes the binding site for the G-patch-containing domain of Pfa1p. When found on DEAH/RHA helicases, this domain is central to the regulation of the helicase activity through its binding of both RNA and G-patch domain proteins.


Pssm-ID: 400182 [Multi-domain]  Cd Length: 82  Bit Score: 92.32  E-value: 1.86e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   918 LRQIMAAGLGDHLARRvqsedllDPKWKNaYKTPLLDDPVFIHPSSVLFREL---PEFVVYQEIVETTKMYMKGVSTVEI 994
Cdd:pfam07717    1 LRAALAAGLYPNVARR-------DPKGKG-YTTLSDNQRVFIHPSSVLFNEKtfpPEWVVYQELVETTKVYIRTVTAISP 72
                           90
                   ....*....|
gi 310616720   995 QWIPSLLPSY 1004
Cdd:pfam07717   73 EWLLLFAPHI 82
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
761-852 1.61e-14

Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 214852 [Multi-domain]  Cd Length: 82  Bit Score: 69.60  E-value: 1.61e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720    761 ITALGRTMSTFPVAPRYAKMLALSQQHGCLPYTIAIVAAMTVRELFEeldrpaaseeelaelKGRRTRVAQMKRTWAGQG 840
Cdd:smart00847   11 LTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPRP---------------KEKREDADAARRRFADPE 75
                            90
                    ....*....|..
gi 310616720    841 aslklGDLMVLL 852
Cdd:smart00847   76 -----SDHLTLL 82
HELICc smart00490
helicase superfamily c-terminal domain;
578-667 1.51e-11

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 61.46  E-value: 1.51e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720    578 SLPLHVLPLYSLLAPEKQAQVFKPPPEGTRLCVIATNVAETSLTIPGIKYVVDCGkvkkryydrvtgvssfrvTWVSQAS 657
Cdd:smart00490    9 ELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYD------------------LPWSPAS 70
                            90
                    ....*....|
gi 310616720    658 ADQRAGRAGR 667
Cdd:smart00490   71 YIQRIGRAGR 80
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
581-667 4.02e-09

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: 55.29  E-value: 4.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   581 LHVLPLYSLLAPEKQAQVFKPPPEGTRLCVIATNVAETSLTIPGIKYVVDcgkvkkryYDRVTGVSSFRvtwvsqasadQ 660
Cdd:pfam00271   39 IKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVIN--------YDLPWNPASYI----------Q 100

                   ....*..
gi 310616720   661 RAGRAGR 667
Cdd:pfam00271  101 RIGRAGR 107
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
254-407 1.02e-08

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: 55.71  E-value: 1.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   254 EQAIMEAVAEHPiVIVCGETGSGKTT--QVPqFLYEAGYSSEDSIIGVTEPRRVAAVAMSQRVAKEMNLSHRVVSY---- 327
Cdd:pfam00270    5 AEAIPAILEGRD-VLVQAPTGSGKTLafLLP-ALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASllgg 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   328 -QIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHErsvytdiLLGLLSRIVALRAKRHLPLK--LLIMS 404
Cdd:pfam00270   83 dSRKEQLEKLKGPDILVGTPGRLLDLLQERKLLKNLKLLVLDEAHR-------LLDMGFGPDLEEILRRLPKKrqILLLS 155

                   ...
gi 310616720   405 ATL 407
Cdd:pfam00270  156 ATL 158
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
267-406 1.81e-08

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: 54.33  E-value: 1.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  267 VIVCGETGSGKTTQVPQFLYEAGYSSEDSIIgVTEPRRVAAVAMSQRVAKEMNLSHRVVSYQIRY-----EGNVTEETRI 341
Cdd:cd00046     4 VLITAPTGSGKTLAALLAALLLLLKKGKKVL-VLVPTKALALQTAERLRELFGPGIRVAVLVGGSsaeerEKNKLGDADI 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 310616720  342 KFMTDGVLLKEIQKD--FLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKrhlPLKLLIMSAT 406
Cdd:cd00046    83 IIATPDMLLNLLLREdrLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLK---NAQVILLSAT 146
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
254-491 5.13e-07

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 53.83  E-value: 5.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  254 EQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYE-----AGYSSEDSIIGVTEPR-------RVAAV-AMSQRVAKEM-- 318
Cdd:PHA02653  169 QLKIFEAWISRKPVVLTGGTGVGKTSQVPKLLLWfnylfGGFDNLDKIDPNFIERpivlslpRVALVrLHSITLLKSLgf 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  319 -NLSHRVVSyqIRYeGNVTEETR-IKFMTDGVLLK----EIQKdflLLKYKVVIIDEAHERSVYTDILlgllsrIVALRA 392
Cdd:PHA02653  249 dEIDGSPIS--LKY-GSIPDELInTNPKPYGLVFSthklTLNK---LFDYGTVIIDEVHEHDQIGDII------IAVARK 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  393 KRHLPLKLLIMSATLrvEDFTQNQRLFTTPPPVIKVE-SRQFPVTVHF--NKRTPLDDYS-GECFRK-VCKIHRML--PA 465
Cdd:PHA02653  317 HIDKIRSLFLMTATL--EDDRDRIKEFFPNPAFVHIPgGTLFPISEVYvkNKYNPKNKRAyIEEEKKnIVTALKKYtpPK 394
                         250       260
                  ....*....|....*....|....*...
gi 310616720  466 G--GIlVFLTGQAEVHALCRRLRKAFPI 491
Cdd:PHA02653  395 GssGI-VFVASVSQCEEYKKYLEKRLPI 421
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
266-434 1.04e-04

CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 45.88  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  266 IVIVCGETGSGKTTQVPQF-LYEAGYSSEDSIIgVTEPRRVAAVAMSQR---VAKEMNLSHRVVSYQIRYEGNVTEE--- 338
Cdd:cd09639     1 LLVIEAPTGYGKTEAALLWaLHSLKSQKADRVI-IALPTRATINAMYRRakeAFGETGLYHSSILSSRIKEMGDSEEfeh 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  339 --------------TRIKFMTDGVLLKEIQKDF-------LLLKYKVVIIDEAHersVYTDILLGLLsrIVALRAKRHLP 397
Cdd:cd09639    80 lfplyihsndtlflDPITVCTIDQVLKSVFGEFghyeftlASIANSLLIFDEVH---FYDEYTLALI--LAVLEVLKDND 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 310616720  398 LKLLIMSATL--RVEDFTQNQRL--FTTPPPVIKVESRQFP 434
Cdd:cd09639   155 VPILLMSATLpkFLKEYAEKIGYveENEPLDLKPNERAPFI 195
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
610-670 3.14e-04

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: 40.38  E-value: 3.14e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 310616720  610 VIATNVAETSLTIPGIKYVVDCGKVKkryydrvtgvssfrvtwvSQASADQRAGRAGRTEP 670
Cdd:cd18785    26 LVATNVLGEGIDVPSLDTVIFFDPPS------------------SAASYIQRVGRAGRGGK 68
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
264-412 7.58e-04

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 41.20  E-value: 7.58e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720    264 HPIVIVCGETGSGKTTQVPQFLYEAGYSSEDSIIGVTEPRRvaavamsqrvakemnlshrvvsYQIRYEGNVTEETRIKF 343
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDIL----------------------EEVLDQLLLIIVGGKKA 59
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720    344 MTDGVLLKEIQKDFLL-LKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKRHLPLKLLIMSATLRVEDF 412
Cdd:smart00382   60 SGSGELRLRLALALARkLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDL 129
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
266-407 8.01e-04

CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 43.21  E-value: 8.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   266 IVIVCGETGSGKTTQVPQF-LYEAGYSSEDSIIgVTEPRRVAAVAMSQRvAKEMNLSHRVV----SYQIRYEGNVTEE-- 338
Cdd:TIGR01587    1 LLVIEAPTGYGKTEAALLWaLHSIKSQKADRVI-IALPTRATINAMYRR-AKELFGSELVGlhhsSSFSRIKEMGDSEef 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   339 ----------------TRIKFMTDGVLLKEIQKDF-------LLLKYKVVIIDEAHersVYTDILLGLLsrIVALRAKRH 395
Cdd:TIGR01587   79 ehlfplyihsndklflDPITVCTIDQVLKSVFGEFghyeftlASIANSLLIFDEVH---FYDEYTLALI--LAVLEVLKD 153
                          170
                   ....*....|..
gi 310616720   396 LPLKLLIMSATL 407
Cdd:TIGR01587  154 NDVPILLMSATL 165
DEXHc_viral_Ns3 cd17931
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ...
273-406 9.56e-04

DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional protein found in pestiviruses that contains an N-terminal protease and a C-terminal helicase. The N-terminal domain is a chymotrypsin-like serine protease, which is responsible for most of the maturation cleavages of the polyprotein precursor in the cytosolic side of the endoplasmic reticulum membrane. The C-terminal domain, about two-thirds of NS3, is a helicase belonging to superfamily 2 (SF2) thought to be important for unwinding highly structured regions of the RNA genome during replication. NS3 plays an essential role in viral polyprotein processing and genome replication. NS3 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: 350689 [Multi-domain]  Cd Length: 151  Bit Score: 41.00  E-value: 9.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  273 TGSGKTTQVPQFLYEAGYSSEDSIIgVTEPRRVAAVAMSQRvakemnLSHRVVSYQIryeGNVTEETR----IKFMTDGV 348
Cdd:cd17931    10 PGAGKTTRVLPQIIREAIKKRLRTL-VLAPTRVVAAEMYEA------LRGLPIRYRT---GAVKEEHGgneiVDYMCHGT 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 310616720  349 LLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKRhlplkLLIMSAT 406
Cdd:cd17931    80 FTCRLLSPKRVPNYNLIIMDEAHFTDPASIAARGYIHTRVEMGEAA-----VIFMTAT 132
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
253-387 1.53e-03

DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD 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: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 40.23  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  253 EEQAIMEAVAEHPIVIVCGETGSGKTTQVpQFLYEAGYSSEDSIIGVTePRRVAAVAMSQRVAKEMNLSHRVVsyqirye 332
Cdd:cd17933     1 EQKAAVRLVLRNRVSVLTGGAGTGKTTTL-KALLAALEAEGKRVVLAA-PTGKAAKRLSESTGIEASTIHRLL------- 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 310616720  333 gnvteetRIKFMTDGVLLKEIQkdflLLKYKVVIIDEAherS-VYTDILLGLLSRI 387
Cdd:cd17933    72 -------GINPGGGGFYYNEEN----PLDADLLIVDEA---SmVDTRLMAALLSAI 113
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
252-434 1.72e-03

CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system


Pssm-ID: 440816 [Multi-domain]  Cd Length: 535  Bit Score: 42.38  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  252 AEEQAIMEAVAEHPIVIVCGETGSGKTtqvpqflyEAGYS---------SEDSIIgVTEPRRVAAVAMSQRVAKEMNLS- 321
Cdd:COG1203   135 ALELALEAAEEEPGLFILTAPTGGGKT--------EAALLfalrlaakhGGRRII-YALPFTSIINQTYDRLRDLFGEDv 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  322 ----HRVVSYQIRYEGNVTEETRIKFMTDGVLLKEI------Q-------------KDFLLLKYKVVIIDEAHersVYTD 378
Cdd:COG1203   206 llhhSLADLDLLEEEEEYESEARWLKLLKELWDAPVvvttidQlfeslfsnrkgqeRRLHNLANSVIILDEVQ---AYPP 282
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 310616720  379 ILLGLLSRivALRAKRHLPLKLLIMSATL---RVEDFTQNQRLFTTPPPVIKVESRQFP 434
Cdd:COG1203   283 YMLALLLR--LLEWLKNLGGSVILMTATLpplLREELLEAYELIPDEPEELPEYFRAFV 339
AAA_22 pfam13401
AAA domain;
266-371 3.40e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.86  E-value: 3.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720   266 IVIVCGETGSGKTTQVPQFLYEAGySSEDSIIGVTEPRRVAAVAMSQRVAKEmnlshrvvsYQIRYEGNVTEETRIKFMT 345
Cdd:pfam13401    7 ILVLTGESGTGKTTLLRRLLEQLP-EVRDSVVFVDLPSGTSPKDLLRALLRA---------LGLPLSGRLSKEELLAALQ 76
                           90       100
                   ....*....|....*....|....*.
gi 310616720   346 DgvLLKEIQKDflllkyKVVIIDEAH 371
Cdd:pfam13401   77 Q--LLLALAVA------VVLIIDEAQ 94
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
255-414 4.74e-03

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: 39.55  E-value: 4.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  255 QAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEDSIIgVTEPRRvaavAMSQRvaKEMNLSHRVVSYQ---IRY 331
Cdd:cd17921     8 EALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGKAV-YIAPTR----ALVNQ--KEADLRERFGPLGknvGLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  332 EGNVTE------ETRIKFMT----DGVLLKEIQKDFLLLKYkvVIIDEAH-----ERSVytdILLGLLSRIvaLRAKRHl 396
Cdd:cd17921    81 TGDPSVnklllaEADILVATpeklDLLLRNGGERLIQDVRL--VVVDEAHligdgERGV---VLELLLSRL--LRINKN- 152
                         170
                  ....*....|....*....
gi 310616720  397 pLKLLIMSATLR-VEDFTQ 414
Cdd:cd17921   153 -ARFVGLSATLPnAEDLAE 170
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
265-407 6.73e-03

DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 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: 350688 [Multi-domain]  Cd Length: 186  Bit Score: 39.20  E-value: 6.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  265 PIVIVCGETGSGKTtqvpqflyEAGY---------SSEDSIIgVTEPRRVAAVAMSQRVAKemNLSHRVVSYQIR-YEGN 334
Cdd:cd17930     2 GLVILEAPTGSGKT--------EAALlwalklaarGGKRRII-YALPTRATINQMYERIRE--ILGRLDDEDKVLlLHSK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310616720  335 VTEETRIKFMTDGVLLKEIQKDFLLLK---------------------------------YKVVIIDEAHERSV-YTDIL 380
Cdd:cd17930    71 AALELLESDEEPDDDPVEAVDWALLLKrswlapivvttidqllesllkykhferrlhglaNSVVVLDEVQAYDPeYMALL 150
                         170       180
                  ....*....|....*....|....*..
gi 310616720  381 LGLLSRIValrakRHLPLKLLIMSATL 407
Cdd:cd17930   151 LKALLELL-----GELGGPVVLMTATL 172
 
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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