NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1371547147|ref|XP_001350899|]
View 

ATP-dependent RNA helicase DRS1, putative [Plasmodium falciparum 3D7]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11423521)

DEAD/DEAH box-containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA

EC:  3.6.4.-
Gene Ontology:  GO:0016887|GO:0003676|GO:0005524
PubMed:  20206133
SCOP:  4000282|3002019

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
90-507 2.11e-108

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 335.19  E-value: 2.11e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  90 SDLYISRPFLKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLQSVNIKMRrnnmkgsynit 169
Cdd:COG0513     5 ADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQ----------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 170 kALILLPTRELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDFiNYLEIVVF 249
Cdd:COG0513    74 -ALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDL-SGVETLVL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 250 DEADKLLELGFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFIQsgmsfdknVDGKNTynayntcntynd 329
Cdd:COG0513   152 DEADRMLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIE--------VAPENA------------ 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 330 ndnnnivvnniisnsflkisnkasfkISENLKQEFVNIiqEKYRKASLLY--LCNNIYKNhCIIFFKTKRETHlmyLLFD 407
Cdd:COG0513   212 --------------------------TAETIEQRYYLV--DKRDKLELLRrlLRDEDPER-AIVFCNTKRGAD---RLAE 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 408 LLN---LRCAELHGSMSQKKRIESIMKFKKAEVDFLLTTELASRGIDIDHVLYVINYNVPSNVIKYVHRIGRTARIGKEG 484
Cdd:COG0513   260 KLQkrgISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEG 339
                         410       420
                  ....*....|....*....|...
gi 1371547147 485 IASTLYLQKEKIEVKKIVKGLKK 507
Cdd:COG0513   340 TAISLVTPDERRLLRAIEKLIGQ 362
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
90-507 2.11e-108

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 335.19  E-value: 2.11e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  90 SDLYISRPFLKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLQSVNIKMRrnnmkgsynit 169
Cdd:COG0513     5 ADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQ----------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 170 kALILLPTRELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDFiNYLEIVVF 249
Cdd:COG0513    74 -ALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDL-SGVETLVL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 250 DEADKLLELGFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFIQsgmsfdknVDGKNTynayntcntynd 329
Cdd:COG0513   152 DEADRMLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIE--------VAPENA------------ 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 330 ndnnnivvnniisnsflkisnkasfkISENLKQEFVNIiqEKYRKASLLY--LCNNIYKNhCIIFFKTKRETHlmyLLFD 407
Cdd:COG0513   212 --------------------------TAETIEQRYYLV--DKRDKLELLRrlLRDEDPER-AIVFCNTKRGAD---RLAE 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 408 LLN---LRCAELHGSMSQKKRIESIMKFKKAEVDFLLTTELASRGIDIDHVLYVINYNVPSNVIKYVHRIGRTARIGKEG 484
Cdd:COG0513   260 KLQkrgISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEG 339
                         410       420
                  ....*....|....*....|...
gi 1371547147 485 IASTLYLQKEKIEVKKIVKGLKK 507
Cdd:COG0513   340 TAISLVTPDERRLLRAIEKLIGQ 362
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
99-303 1.24e-78

DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350705 [Multi-domain]  Cd Length: 196  Bit Score: 249.48  E-value: 1.24e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  99 LKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLqsvnikmRRNNMKGSyniTKALILLPTR 178
Cdd:cd17947     2 LRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLL-------YRPKKKAA---TRVLVLVPTR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 179 ELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDFINYLEIVVFDEADKLLEL 258
Cdd:cd17947    72 ELAMQCFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEE 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1371547147 259 GFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFIQ 303
Cdd:cd17947   152 GFADELKEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
89-536 2.37e-65

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 222.51  E-value: 2.37e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  89 WSDLYISRPFLKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLQSVnikmRRNNmkGSYNI 168
Cdd:PRK11192    3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFP----RRKS--GPPRI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 169 tkaLILLPTRELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDfINYLEIVV 248
Cdd:PRK11192   77 ---LILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFD-CRAVETLI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 249 FDEADKLLELGFKEECLKILDVCKFKKQILFFSATLTSD-IKQLANFSLKNPVFIQSgmsfdknvdgkntynayntcnty 327
Cdd:PRK11192  153 LDEADRMLDMGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEA----------------------- 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 328 ndndnnnivvnniisnsflKISNKASFKIsenlkQEFVNIIQEKYRKASLlyLCNNIYKNHC---IIFFKTKRETHlmyL 404
Cdd:PRK11192  210 -------------------EPSRRERKKI-----HQWYYRADDLEHKTAL--LCHLLKQPEVtrsIVFVRTRERVH---E 260
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 405 LFDLL---NLRCAELHGSMSQKKRIESIMKFKKAEVDFLLTTELASRGIDIDHVLYVINYNVPSNVIKYVHRIGRTARIG 481
Cdd:PRK11192  261 LAGWLrkaGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAG 340
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371547147 482 KEGIASTL-----YLQKEKIE------VK-KIVKGLK-KSKNLKILKRTIAENNVLVWYKIIKENKQK 536
Cdd:PRK11192  341 RKGTAISLveahdHLLLGKIEryieepLKaRVIDELRpKTKAPSEKKTGKPSKKVLAKRAEKKEKEKE 408
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
111-291 1.74e-47

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: 165.11  E-value: 1.74e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 111 TYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLlqsvnikmrRNNMKGsyniTKALILLPTRELSLQCYDVIRS 190
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL---------DKLDNG----PQALVLAPTRELAEQIYEELKK 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 191 LTKYVTITYSLFCGGIDIKQQEYEFKKrNDIFVCTPGRILDLLLNSSsdFINYLEIVVFDEADKLLELGFKEECLKILDV 270
Cdd:pfam00270  68 LGKGLGLKVASLLGGDSRKEQLEKLKG-PDILVGTPGRLLDLLQERK--LLKNLKLLVLDEAHRLLDMGFGPDLEEILRR 144
                         170       180
                  ....*....|....*....|.
gi 1371547147 271 CKFKKQILFFSATLTSDIKQL 291
Cdd:pfam00270 145 LPKKRQILLLSATLPRNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
102-313 1.38e-40

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 147.25  E-value: 1.38e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  102 LYEQKFSNPTYIQRDVIPLALEG-KSILANSETGSGKTLAFVLPILERLLQSVNIKmrrnnmkgsynitkALILLPTREL 180
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGGR--------------VLVLVPTREL 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  181 SLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRN-DIFVCTPGRILDLLLNSSSDFINYlEIVVFDEADKLLELG 259
Cdd:smart00487  67 AEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNV-DLVILDEAHRLLDGG 145
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1371547147  260 FKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFIQSGMSFDKNVD 313
Cdd:smart00487 146 FGDQLEKLLKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPLEPIE 199
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
90-507 2.11e-108

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 335.19  E-value: 2.11e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  90 SDLYISRPFLKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLQSVNIKMRrnnmkgsynit 169
Cdd:COG0513     5 ADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQ----------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 170 kALILLPTRELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDFiNYLEIVVF 249
Cdd:COG0513    74 -ALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDL-SGVETLVL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 250 DEADKLLELGFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFIQsgmsfdknVDGKNTynayntcntynd 329
Cdd:COG0513   152 DEADRMLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIE--------VAPENA------------ 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 330 ndnnnivvnniisnsflkisnkasfkISENLKQEFVNIiqEKYRKASLLY--LCNNIYKNhCIIFFKTKRETHlmyLLFD 407
Cdd:COG0513   212 --------------------------TAETIEQRYYLV--DKRDKLELLRrlLRDEDPER-AIVFCNTKRGAD---RLAE 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 408 LLN---LRCAELHGSMSQKKRIESIMKFKKAEVDFLLTTELASRGIDIDHVLYVINYNVPSNVIKYVHRIGRTARIGKEG 484
Cdd:COG0513   260 KLQkrgISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEG 339
                         410       420
                  ....*....|....*....|...
gi 1371547147 485 IASTLYLQKEKIEVKKIVKGLKK 507
Cdd:COG0513   340 TAISLVTPDERRLLRAIEKLIGQ 362
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
99-303 1.24e-78

DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350705 [Multi-domain]  Cd Length: 196  Bit Score: 249.48  E-value: 1.24e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  99 LKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLqsvnikmRRNNMKGSyniTKALILLPTR 178
Cdd:cd17947     2 LRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLL-------YRPKKKAA---TRVLVLVPTR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 179 ELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDFINYLEIVVFDEADKLLEL 258
Cdd:cd17947    72 ELAMQCFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEE 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1371547147 259 GFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFIQ 303
Cdd:cd17947   152 GFADELKEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
99-303 1.25e-71

DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 231.18  E-value: 1.25e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  99 LKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLQSVNIKMRRnnmkgsyniTKALILLPTR 178
Cdd:cd00268     2 LKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRG---------PQALVLAPTR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 179 ELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDFiNYLEIVVFDEADKLLEL 258
Cdd:cd00268    73 ELAMQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDL-SNVKYLVLDEADRMLDM 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1371547147 259 GFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFIQ 303
Cdd:cd00268   152 GFEEDVEKILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
89-536 2.37e-65

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 222.51  E-value: 2.37e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  89 WSDLYISRPFLKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLQSVnikmRRNNmkGSYNI 168
Cdd:PRK11192    3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFP----RRKS--GPPRI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 169 tkaLILLPTRELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDfINYLEIVV 248
Cdd:PRK11192   77 ---LILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFD-CRAVETLI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 249 FDEADKLLELGFKEECLKILDVCKFKKQILFFSATLTSD-IKQLANFSLKNPVFIQSgmsfdknvdgkntynayntcnty 327
Cdd:PRK11192  153 LDEADRMLDMGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEA----------------------- 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 328 ndndnnnivvnniisnsflKISNKASFKIsenlkQEFVNIIQEKYRKASLlyLCNNIYKNHC---IIFFKTKRETHlmyL 404
Cdd:PRK11192  210 -------------------EPSRRERKKI-----HQWYYRADDLEHKTAL--LCHLLKQPEVtrsIVFVRTRERVH---E 260
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 405 LFDLL---NLRCAELHGSMSQKKRIESIMKFKKAEVDFLLTTELASRGIDIDHVLYVINYNVPSNVIKYVHRIGRTARIG 481
Cdd:PRK11192  261 LAGWLrkaGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAG 340
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371547147 482 KEGIASTL-----YLQKEKIE------VK-KIVKGLK-KSKNLKILKRTIAENNVLVWYKIIKENKQK 536
Cdd:PRK11192  341 RKGTAISLveahdHLLLGKIEryieepLKaRVIDELRpKTKAPSEKKTGKPSKKVLAKRAEKKEKEKE 408
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
92-507 4.76e-62

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 214.29  E-value: 4.76e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  92 LYISRPFLKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLQS-VNIKMRRNnmkgsyniTK 170
Cdd:PRK10590    6 LGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRqPHAKGRRP--------VR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 171 ALILLPTRELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDfINYLEIVVFD 250
Cdd:PRK10590   78 ALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVK-LDQVEILVLD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 251 EADKLLELGFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFIQsgmsfdknVDGKNTynayntcntyndn 330
Cdd:PRK10590  157 EADRMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIE--------VARRNT------------- 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 331 dnnnivvnniisnsflkisnkASFKISENLkqEFVniiqEKYRKASLL-YLCNNIYKNHCIIFFKTKretHLMYLLFDLL 409
Cdd:PRK10590  216 ---------------------ASEQVTQHV--HFV----DKKRKRELLsQMIGKGNWQQVLVFTRTK---HGANHLAEQL 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 410 N---LRCAELHGSMSQKKRIESIMKFKKAEVDFLLTTELASRGIDIDHVLYVINYNVPSNVIKYVHRIGRTARIGKEGIA 486
Cdd:PRK10590  266 NkdgIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEA 345
                         410       420
                  ....*....|....*....|.
gi 1371547147 487 STLYLQKEKIEVKKIVKGLKK 507
Cdd:PRK10590  346 LSLVCVDEHKLLRDIEKLLKK 366
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
99-302 1.13e-54

DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350699 [Multi-domain]  Cd Length: 198  Bit Score: 185.96  E-value: 1.13e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  99 LKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLQsvnikmrrnNMKGSYNITKALILLPTR 178
Cdd:cd17941     2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYR---------ERWTPEDGLGALIISPTR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 179 ELSLQCYDVIRSLTKYVTITYSLFCGGIDIKqQEYEFKKRNDIFVCTPGRILDLLLNSSSDFINYLEIVVFDEADKLLEL 258
Cdd:cd17941    73 ELAMQIFEVLRKVGKYHSFSAGLIIGGKDVK-EEKERINRMNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILDM 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1371547147 259 GFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFI 302
Cdd:cd17941   152 GFKETLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
90-501 4.45e-50

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 181.54  E-value: 4.45e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  90 SDLYISRPFLKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPilerLLQSVNIKMRRnnmkgsyniT 169
Cdd:PRK11776    7 STLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLG----LLQKLDVKRFR---------V 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 170 KALILLPTRELSLQCYDVIRSL------TKYVTItyslfCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDFINy 243
Cdd:PRK11776   74 QALVLCPTRELADQVAKEIRRLarfipnIKVLTL-----CGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDA- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 244 LEIVVFDEADKLLELGFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFIQsgmsfdknVDGKNTYNAynt 323
Cdd:PRK11776  148 LNTLVLDEADRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVK--------VESTHDLPA--- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 324 cntyndndnnnivvnniISNSFlkisnkasFKISENLKQEFVNIIQEKYRKASllylcnniyknhCIIFFKTKRETHlmy 403
Cdd:PRK11776  217 -----------------IEQRF--------YEVSPDERLPALQRLLLHHQPES------------CVVFCNTKKECQ--- 256
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 404 LLFDLLNLR---CAELHGSMSQKKRIESIMKF--KKAEVdfLLTTELASRGIDIDHVLYVINYNVPSNVIKYVHRIGRTA 478
Cdd:PRK11776  257 EVADALNAQgfsALALHGDLEQRDRDQVLVRFanRSCSV--LVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTG 334
                         410       420
                  ....*....|....*....|...
gi 1371547147 479 RIGKEGIASTLYLQKEKIEVKKI 501
Cdd:PRK11776  335 RAGSKGLALSLVAPEEMQRANAI 357
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
99-302 6.03e-50

DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350700 [Multi-domain]  Cd Length: 198  Bit Score: 172.93  E-value: 6.03e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  99 LKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILErLLQSVNIKMRrnnmkgsyNITKALILLPTR 178
Cdd:cd17942     2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIE-LLYKLKFKPR--------NGTGVIIISPTR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 179 ELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDFINYLEIVVFDEADKLLEL 258
Cdd:cd17942    73 ELALQIYGVAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEI 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1371547147 259 GFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKN-PVFI 302
Cdd:cd17942   153 GFEEEMRQIIKLLPKRRQTMLFSATQTRKVEDLARISLKKkPLYV 197
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
94-303 8.43e-50

DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350717 [Multi-domain]  Cd Length: 205  Bit Score: 172.87  E-value: 8.43e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  94 ISRPFLKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLlqsvnikMRRNNMKGsyniTKALI 173
Cdd:cd17959     8 LSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL-------KAHSPTVG----ARALI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 174 LLPTRELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDFINyLEIVVFDEAD 253
Cdd:cd17959    77 LSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSS-VEYVVFDEAD 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1371547147 254 KLLELGFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFIQ 303
Cdd:cd17959   156 RLFEMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
106-302 5.30e-49

DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350707 [Multi-domain]  Cd Length: 214  Bit Score: 171.23  E-value: 5.30e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 106 KFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERlLQSVNIKMRRNnmKGSYnitkALILLPTRELSLQCY 185
Cdd:cd17949    10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQR-LLSLEPRVDRS--DGTL----ALVLVPTRELALQIY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 186 DVIRSLTKYVT-ITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDFINYLEIVVFDEADKLLELGFKEEC 264
Cdd:cd17949    83 EVLEKLLKPFHwIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDI 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1371547147 265 LKILD-------------VCKFKKQILFFSATLTSDIKQLANFSLKNPVFI 302
Cdd:cd17949   163 TKILEllddkrskaggekSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
91-486 7.53e-49

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 178.57  E-value: 7.53e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  91 DLYISRPFLKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLQSVNIKMRrnnMKGSyniTK 170
Cdd:PRK01297   91 DFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKER---YMGE---PR 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 171 ALILLPTRELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRN-DIFVCTPGRILDllLNSSSD-FINYLEIVV 248
Cdd:PRK01297  165 ALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARFcDILVATPGRLLD--FNQRGEvHLDMVEVMV 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 249 FDEADKLLELGFKEECLKILDVC--KFKKQILFFSATLTSDIKQLANFSLKNPVFIQsgmsfdknvdgkntynayntcnt 326
Cdd:PRK01297  243 LDEADRMLDMGFIPQVRQIIRQTprKEERQTLLFSATFTDDVMNLAKQWTTDPAIVE----------------------- 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 327 yndndnnnivvnniisnsfLKISNKAsfkiSENLKQE-FVNIIQEKYRkasLLYlcNNIYKN---HCIIFFKTKRETHLM 402
Cdd:PRK01297  300 -------------------IEPENVA----SDTVEQHvYAVAGSDKYK---LLY--NLVTQNpweRVMVFANRKDEVRRI 351
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 403 YLLFDLLNLRCAELHGSMSQKKRIESIMKFKKAEVDFLLTTELASRGIDIDHVLYVINYNVPSNVIKYVHRIGRTARIGK 482
Cdd:PRK01297  352 EERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGA 431

                  ....
gi 1371547147 483 EGIA 486
Cdd:PRK01297  432 SGVS 435
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
89-303 1.40e-48

DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350712 [Multi-domain]  Cd Length: 203  Bit Score: 169.42  E-value: 1.40e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  89 WSDLYISRPFLKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLqsvnikmrrNNMKGSYni 168
Cdd:cd17954     2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALL---------ENPQRFF-- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 169 tkALILLPTRELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDFINYLEIVV 248
Cdd:cd17954    71 --ALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGFSLKSLKFLV 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1371547147 249 FDEADKLLELGFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFIQ 303
Cdd:cd17954   149 MDEADRLLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
90-303 2.91e-48

DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350713 [Multi-domain]  Cd Length: 204  Bit Score: 168.56  E-value: 2.91e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  90 SDLYISRPFLKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLlqsvnikmrrnnMKGSYNIT 169
Cdd:cd17955     2 EDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL------------SEDPYGIF 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 170 kALILLPTRELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDlLLNSSSDFINYLEIV-- 247
Cdd:cd17955    70 -ALVLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLAD-HLRSSDDTTKVLSRVkf 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1371547147 248 -VFDEADKLLELGFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFIQ 303
Cdd:cd17955   148 lVLDEADRLLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
99-300 7.08e-48

DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350719 [Multi-domain]  Cd Length: 206  Bit Score: 167.76  E-value: 7.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  99 LKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLqsvnikmRRNNMKGSYNITKALILLPTR 178
Cdd:cd17961     6 LKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIL-------KAKAESGEEQGTRALILVPTR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 179 ELSLQCYDVIRSLTKYVTITYSLfcggIDIKQQEYEFKKRN------DIFVCTPGRILDLLLNSSSDFINYLEIVVFDEA 252
Cdd:cd17961    79 ELAQQVSKVLEQLTAYCRKDVRV----VNLSASSSDSVQRAllaekpDIVVSTPARLLSHLESGSLLLLSTLKYLVIDEA 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1371547147 253 DKLLELGFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPV 300
Cdd:cd17961   155 DLVLSYGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
110-508 1.64e-47

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 175.75  E-value: 1.64e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 110 PTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILER--LLQSVNIKMRRNNMkgsynitkALILLPTRELSLQCYDV 187
Cdd:PLN00206  144 PTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRccTIRSGHPSEQRNPL--------AMVLTPTRELCVQVEDQ 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 188 IRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDfINYLEIVVFDEADKLLELGFKEECLKI 267
Cdd:PLN00206  216 AKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIE-LDNVSVLVLDEVDCMLERGFRDQVMQI 294
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 268 LDVCKfKKQILFFSATLTSDIKQLANFSLKNPVFIQSGMSFDKNVDGKNTynayntcntyndndnnnivvnniisnsflk 347
Cdd:PLN00206  295 FQALS-QPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQL------------------------------ 343
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 348 isnkASFKISENLKQEFVNIIQEKYRkasllylcnniYKNHCIIFFKTKrethlmyLLFDLLN--------LRCAELHGS 419
Cdd:PLN00206  344 ----AIWVETKQKKQKLFDILKSKQH-----------FKPPAVVFVSSR-------LGADLLAnaitvvtgLKALSIHGE 401
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 420 MSQKKRIESIMKFKKAEVDFLLTTELASRGIDIDHVLYVINYNVPSNVIKYVHRIGRTARIGKEGIASTLYLQKEKIEVK 499
Cdd:PLN00206  402 KSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFP 481

                  ....*....
gi 1371547147 500 KIVKGLKKS 508
Cdd:PLN00206  482 ELVALLKSS 490
PTZ00110 PTZ00110
helicase; Provisional
93-509 1.66e-47

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 176.50  E-value: 1.66e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  93 YISRP--FLKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILerllqsVNIKMRRNNMKGSYNItk 170
Cdd:PTZ00110  134 YTSFPdyILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAI------VHINAQPLLRYGDGPI-- 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 171 ALILLPTRELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDF--INYLeivV 248
Cdd:PTZ00110  206 VLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLrrVTYL---V 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 249 FDEADKLLELGFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKN-PVFIQSGmSFDknvdgkntynayntcnty 327
Cdd:PTZ00110  283 LDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVG-SLD------------------ 343
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 328 ndndnnnivvnniisnsflkisnkasFKISENLKQEfVNIIQEKYRKASLLYLCNNIYKN--HCIIFFKTKRETHLMYLL 405
Cdd:PTZ00110  344 --------------------------LTACHNIKQE-VFVVEEHEKRGKLKMLLQRIMRDgdKILIFVETKKGADFLTKE 396
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 406 FDLLNLRCAELHGSMSQKKRIESIMKFKKAEVDFLLTTELASRGIDIDHVLYVINYNVPSNVIKYVHRIGRTARIGKEGI 485
Cdd:PTZ00110  397 LRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGA 476
                         410       420
                  ....*....|....*....|....*
gi 1371547147 486 ASTlYLQKEKIEV-KKIVKGLKKSK 509
Cdd:PTZ00110  477 SYT-FLTPDKYRLaRDLVKVLREAK 500
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
111-291 1.74e-47

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: 165.11  E-value: 1.74e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 111 TYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLlqsvnikmrRNNMKGsyniTKALILLPTRELSLQCYDVIRS 190
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL---------DKLDNG----PQALVLAPTRELAEQIYEELKK 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 191 LTKYVTITYSLFCGGIDIKQQEYEFKKrNDIFVCTPGRILDLLLNSSsdFINYLEIVVFDEADKLLELGFKEECLKILDV 270
Cdd:pfam00270  68 LGKGLGLKVASLLGGDSRKEQLEKLKG-PDILVGTPGRLLDLLQERK--LLKNLKLLVLDEAHRLLDMGFGPDLEEILRR 144
                         170       180
                  ....*....|....*....|.
gi 1371547147 271 CKFKKQILFFSATLTSDIKQL 291
Cdd:pfam00270 145 LPKKRQILLLSATLPRNLEDL 165
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
99-302 4.71e-47

DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350718 [Multi-domain]  Cd Length: 202  Bit Score: 165.44  E-value: 4.71e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  99 LKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLqsvnikmrrnnmKGSYNITK----ALIL 174
Cdd:cd17960     2 LDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILL------------KRKANLKKgqvgALII 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 175 LPTRELSLQCYDVIRSLTKYVT--ITYSLFCGGIDIKQQEYEFKKRN-DIFVCTPGRILDlLLNSSSDFINY--LEIVVF 249
Cdd:cd17960    70 SPTRELATQIYEVLQSFLEHHLpkLKCQLLIGGTNVEEDVKKFKRNGpNILVGTPGRLEE-LLSRKADKVKVksLEVLVL 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1371547147 250 DEADKLLELGFKEECLKILDvcKFKKQ--ILFFSATLTSDIKQLANFSLKNPVFI 302
Cdd:cd17960   149 DEADRLLDLGFEADLNRILS--KLPKQrrTGLFSATQTDAVEELIKAGLRNPVRV 201
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
102-302 2.10e-44

DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350715 [Multi-domain]  Cd Length: 198  Bit Score: 157.75  E-value: 2.10e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 102 LYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLqsvnikmRRNNMKGsyniTKALILLPTRELS 181
Cdd:cd17957     5 LEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLG-------KPRKKKG----LRALILAPTRELA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 182 LQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRN-DIFVCTPGRILDLLLNSSSDFINyLEIVVFDEADKLLELGF 260
Cdd:cd17957    74 SQIYRELLKLSKGTGLRIVLLSKSLEAKAKDGPKSITKyDILVSTPLRLVFLLKQGPIDLSS-VEYLVLDEADKLFEPGF 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1371547147 261 KEECLKILDVCKFKK-QILFFSATLTSDIKQLANFSLKNPVFI 302
Cdd:cd17957   153 REQTDEILAACTNPNlQRSLFSATIPSEVEELARSVMKDPIRI 195
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
90-486 2.69e-44

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 164.37  E-value: 2.69e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  90 SDLYISRPFLKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLQSVNIKMRRNNMKgsynit 169
Cdd:PRK04837   11 SDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDRKVNQP------ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 170 KALILLPTRELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDFiNYLEIVVF 249
Cdd:PRK04837   85 RALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINL-GAIQVVVL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 250 DEADKLLELGFKEECLKILDVCKFKKQIL--FFSATLTSDIKQLANFSLKNPVFIQsgmsfdknvdgkntynayntcnty 327
Cdd:PRK04837  164 DEADRMFDLGFIKDIRWLFRRMPPANQRLnmLFSATLSYRVRELAFEHMNNPEYVE------------------------ 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 328 ndndnnnivvnniisnsfLKISNKASFKISENLkqeFVNIIQEKYRkaSLLYLCNNIYKNHCIIFFKTKR--ETHLMYLL 405
Cdd:PRK04837  220 ------------------VEPEQKTGHRIKEEL---FYPSNEEKMR--LLQTLIEEEWPDRAIIFANTKHrcEEIWGHLA 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 406 FDllNLRCAELHGSMSQKKRIESIMKFKKAEVDFLLTTELASRGIDIDHVLYVINYNVPSNVIKYVHRIGRTARIGKEGI 485
Cdd:PRK04837  277 AD--GHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGH 354

                  .
gi 1371547147 486 A 486
Cdd:PRK04837  355 S 355
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
360-490 1.38e-43

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 153.05  E-value: 1.38e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 360 LKQEFVNIIQEKYRKASLLYLCNNIYKNHCIIFFKTKRETHLMYLLFDLLNLRCAELHGSMSQKKRIESIMKFKKAEVDF 439
Cdd:cd18787     1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1371547147 440 LLTTELASRGIDIDHVLYVINYNVPSNVIKYVHRIGRTARIGKEGIASTLY 490
Cdd:cd18787    81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
89-303 9.27e-43

DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350711 [Multi-domain]  Cd Length: 222  Bit Score: 154.07  E-value: 9.27e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  89 WSDLYISRPFLKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILErllqsvNIKMRRNNMKGSYNI 168
Cdd:cd17953    14 WSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFR------HIKDQRPVKPGEGPI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 169 tkALILLPTRELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDFINYLEI-- 246
Cdd:cd17953    88 --GLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRVTNLRRVty 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1371547147 247 VVFDEADKLLELGFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFIQ 303
Cdd:cd17953   166 VVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEIT 222
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
89-302 1.72e-42

DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350698 [Multi-domain]  Cd Length: 201  Bit Score: 152.84  E-value: 1.72e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  89 WSDLYISRPFLKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLQSvnikmrrnnmkgSYNI 168
Cdd:cd17940     1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPK------------KDVI 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 169 tKALILLPTRELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDFiNYLEIVV 248
Cdd:cd17940    69 -QALILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADL-SHCKTLV 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1371547147 249 FDEADKLLELGFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFI 302
Cdd:cd17940   147 LDEADKLLSQDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
107-486 5.56e-42

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 161.27  E-value: 5.56e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 107 FSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLQSVNIKMRRNNMKgsynitKALILLPTRELSLQCYD 186
Cdd:PRK04537   29 FTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADRKPEDP------RALILAPTRELAIQIHK 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 187 VIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDFINYLEIVVFDEADKLLELGFKEECLK 266
Cdd:PRK04537  103 DAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSLHACEICVLDEADRMFDLGFIKDIRF 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 267 ILDVC--KFKKQILFFSATLTSDIKQLANFSLKNPvfiqsgmsfDKNVDGKNTYNAyntcntyndndnnnivvnniisns 344
Cdd:PRK04537  183 LLRRMpeRGTRQTLLFSATLSHRVLELAYEHMNEP---------EKLVVETETITA------------------------ 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 345 fLKISNKASFKiSENLKQEFvniiqekyrkasLLYLCNNIYKNHCIIFFKTKRETHLMYLLFDLLNLRCAELHGSMSQKK 424
Cdd:PRK04537  230 -ARVRQRIYFP-ADEEKQTL------------LLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKK 295
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371547147 425 RIESIMKFKKAEVDFLLTTELASRGIDIDHVLYVINYNVPSNVIKYVHRIGRTARIGKEGIA 486
Cdd:PRK04537  296 RESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDA 357
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
94-303 1.71e-41

DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350722 [Multi-domain]  Cd Length: 211  Bit Score: 150.43  E-value: 1.71e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  94 ISRPFLKVLYEQKFSNPTYIQRDVIPLALE-GKSILANSETGSGKTLAFVLPILERLLQSvnIKMRRNNMkgsyniTKAL 172
Cdd:cd17964     1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNT--KPAGRRSG------VSAL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 173 ILLPTRELSLQCYDVIRSLTKYVT-ITYSLFCGGIDIKQQEYEFKKRN-DIFVCTPGRILDLLLNSSS--DFINyLEIVV 248
Cdd:cd17964    73 IISPTRELALQIAAEAKKLLQGLRkLRVQSAVGGTSRRAELNRLRRGRpDILVATPGRLIDHLENPGVakAFTD-LDYLV 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 249 FDEADKLLELGFKEECLKILD----VCKFKKQILFFSATLTSDIKQLANFSL-KNPVFIQ 303
Cdd:cd17964   152 LDEADRLLDMGFRPDLEQILRhlpeKNADPRQTLLFSATVPDEVQQIARLTLkKDYKFID 211
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
89-506 2.25e-41

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 160.01  E-value: 2.25e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  89 WSDLYISRPFLKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILerllqsvnikmrrNNMKGSYNI 168
Cdd:PRK11634    8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLL-------------HNLDPELKA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 169 TKALILLPTRELSLQCYDVIRSLTKYV-TITYSLFCGGidikqQEYEFKKRN-----DIFVCTPGRILDLLLNSSSDFIN 242
Cdd:PRK11634   75 PQILVLAPTRELAVQVAEAMTDFSKHMrGVNVVALYGG-----QRYDVQLRAlrqgpQIVVGTPGRLLDHLKRGTLDLSK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 243 yLEIVVFDEADKLLELGFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNP--VFIQSGMSFDKNVDgkntyNA 320
Cdd:PRK11634  150 -LSGLVLDEADEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPqeVRIQSSVTTRPDIS-----QS 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 321 YNTCNTYNDndnnnivvnniisnsflkisNKASFKISEnlkqefvniiQEKYRKAsllylcnniyknhcIIFFKTKRETH 400
Cdd:PRK11634  224 YWTVWGMRK--------------------NEALVRFLE----------AEDFDAA--------------IIFVRTKNATL 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 401 LMYLLFDLLNLRCAELHGSMSQKKRIESIMKFKKAEVDFLLTTELASRGIDIDHVLYVINYNVPSNVIKYVHRIGRTARI 480
Cdd:PRK11634  260 EVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRA 339
                         410       420
                  ....*....|....*....|....*.
gi 1371547147 481 GKEGIASTLYLQKEKIEVKKIVKGLK 506
Cdd:PRK11634  340 GRAGRALLFVENRERRLLRNIERTMK 365
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
99-287 4.14e-41

DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.


Pssm-ID: 350704 [Multi-domain]  Cd Length: 235  Bit Score: 150.08  E-value: 4.14e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  99 LKVLYEQKFSNPTYIQRDVIPLAL-EGKSILANSETGSGKTLAFVLPILERLLQSVnikmRRNNMKGSYNITKALILLPT 177
Cdd:cd17946     2 LRALADLGFSEPTPIQALALPAAIrDGKDVIGAAETGSGKTLAFGIPILERLLSQK----SSNGVGGKQKPLRALILTPT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 178 RELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDlLLNSSSDFINYLEIV---VFDEADK 254
Cdd:cd17946    78 RELAVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWE-LIQEGNEHLANLKSLrflVLDEADR 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1371547147 255 LLELG-FKE--ECLKILDVC----KFKKQILFFSATLTSD 287
Cdd:cd17946   157 MLEKGhFAEleKILELLNKDragkKRKRQTFVFSATLTLD 196
DEXDc smart00487
DEAD-like helicases superfamily;
102-313 1.38e-40

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 147.25  E-value: 1.38e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  102 LYEQKFSNPTYIQRDVIPLALEG-KSILANSETGSGKTLAFVLPILERLLQSVNIKmrrnnmkgsynitkALILLPTREL 180
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGGR--------------VLVLVPTREL 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  181 SLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRN-DIFVCTPGRILDLLLNSSSDFINYlEIVVFDEADKLLELG 259
Cdd:smart00487  67 AEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNV-DLVILDEAHRLLDGG 145
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1371547147  260 FKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFIQSGMSFDKNVD 313
Cdd:smart00487 146 FGDQLEKLLKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPLEPIE 199
PTZ00424 PTZ00424
helicase 45; Provisional
91-501 2.80e-40

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 152.67  E-value: 2.80e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  91 DLYISRPFLKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLlqsvnikmrrnnmKGSYNITK 170
Cdd:PTZ00424   32 ALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLI-------------DYDLNACQ 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 171 ALILLPTRELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDlLLNSSSDFINYLEIVVFD 250
Cdd:PTZ00424   99 ALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYD-MIDKRHLRVDDLKLFILD 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 251 EADKLLELGFKeecLKILDVckFKK-----QILFFSATLTSDIKQLANFSLKNPVfiqsgmsfdknvdgkntynayntcn 325
Cdd:PTZ00424  178 EADEMLSRGFK---GQIYDV--FKKlppdvQVALFSATMPNEILELTTKFMRDPK------------------------- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 326 tyndndnnnivvnniisnsflKISNKASFKISENLKQEFVNIIQEKYRKASLLYLCNNIYKNHCIIFFKTKRETHLMYLL 405
Cdd:PTZ00424  228 ---------------------RILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKK 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 406 FDLLNLRCAELHGSMSQKKRiESIMK-FKKAEVDFLLTTELASRGIDIDHVLYVINYNVPSNVIKYVHRIGRTARIGKEG 484
Cdd:PTZ00424  287 MHERDFTVSCMHGDMDQKDR-DLIMReFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKG 365
                         410
                  ....*....|....*..
gi 1371547147 485 IASTLYLQKEKIEVKKI 501
Cdd:PTZ00424  366 VAINFVTPDDIEQLKEI 382
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
99-302 7.61e-40

DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350703 [Multi-domain]  Cd Length: 220  Bit Score: 145.93  E-value: 7.61e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  99 LKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLQSvNIKMRRNNMKGSYnitkALILLPTR 178
Cdd:cd17945     2 LRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRL-PPLDEETKDDGPY----ALILAPTR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 179 ELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNS--SSDFINYleiVVFDEADKLL 256
Cdd:cd17945    77 ELAQQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRllVLNQCTY---VVLDEADRMI 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371547147 257 ELGFKEECLKILD-------------------VCKFK-KQILFFSATLTSDIKQLANFSLKNPVFI 302
Cdd:cd17945   154 DMGFEPQVTKILDampvsnkkpdteeaeklaaSGKHRyRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
106-305 3.39e-39

DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes Drosophila melanogaster Vasa, which is essential for development. DEAD box protein 3 (DDX3) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DDX3 and DDX4 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350725 [Multi-domain]  Cd Length: 221  Bit Score: 144.17  E-value: 3.39e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 106 KFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLQSVNIKMRRNNMKGSyniTKALILLPTRELSLQCY 185
Cdd:cd17967    19 GYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGRRKAY---PSALILAPTRELAIQIY 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 186 DVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNS--SSDFINYLeivVFDEADKLLELGFKEE 263
Cdd:cd17967    96 EEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGriSLSSIKFL---VLDEADRMLDMGFEPQ 172
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1371547147 264 CLKILD----VCKFKKQILFFSATLTSDIKQLANFSLKNPVFIQSG 305
Cdd:cd17967   173 IRKIVEhpdmPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVG 218
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
110-302 4.59e-39

DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350696 [Multi-domain]  Cd Length: 204  Bit Score: 143.23  E-value: 4.59e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 110 PTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILErllqsvnikmrrnnmkgsynITKALILLPTRELSLQCYDVIR 189
Cdd:cd17938    22 PTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ--------------------IVVALILEPSRELAEQTYNCIE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 190 SLTKYV---TITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDlLLNSSSDFINYLEIVVFDEADKLLELGFKEECLK 266
Cdd:cd17938    82 NFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLED-LIKTGKLDLSSVRFFVLDEADRLLSQGNLETINR 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1371547147 267 IldvckFKK-----------QILFFSATLTS-DIKQLANFSLKNPVFI 302
Cdd:cd17938   161 I-----YNRipkitsdgkrlQVIVCSATLHSfEVKKLADKIMHFPTWV 203
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
99-302 5.67e-38

DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350709 [Multi-domain]  Cd Length: 206  Bit Score: 140.17  E-value: 5.67e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  99 LKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLQSvNIKMRRNNMKGSYnitkALILLPTR 178
Cdd:cd17951     2 LKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQ-EKKLPFIKGEGPY----GLIVCPSR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 179 ELSLQCYDVIRSLTKYVTIT-----YSLFC-GGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNS--SSDFINYLeivVFD 250
Cdd:cd17951    77 ELARQTHEVIEYYCKALQEGgypqlRCLLCiGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKkiNLDICRYL---CLD 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1371547147 251 EADKLLELGFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFI 302
Cdd:cd17951   154 EADRMIDMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
99-302 3.70e-37

DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor 3B-Associated 125 kDa Protein, RHELP, or RNAHP) is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase with protein displacement and RNA annealing activities. DDX42 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350710 [Multi-domain]  Cd Length: 197  Bit Score: 137.55  E-value: 3.70e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  99 LKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILerllqsVNIKMRRNNMKGSYNItkALILLPTR 178
Cdd:cd17952     2 LNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPML------VHIMDQRELEKGEGPI--AVIVAPTR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 179 ELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDFiNYLEIVVFDEADKLLEL 258
Cdd:cd17952    74 ELAQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNL-QRVTYLVLDEADRMFDM 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1371547147 259 GFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFI 302
Cdd:cd17952   153 GFEYQVRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
91-302 1.27e-36

DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350697 [Multi-domain]  Cd Length: 199  Bit Score: 136.30  E-value: 1.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  91 DLYISRPFLKVLYEQKFSNPTYI-QRDVIPLaLEGKSILANSETGSGKTLAFVLPILERLLQSVNIkmrrnnmkgsyniT 169
Cdd:cd17939     1 DMGLSEDLLRGIYAYGFEKPSAIqQRAIVPI-IKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRE-------------T 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 170 KALILLPTRELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDfINYLEIVVF 249
Cdd:cd17939    67 QALVLAPTRELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLR-TDKIKMFVL 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1371547147 250 DEADKLLELGFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFI 302
Cdd:cd17939   146 DEADEMLSRGFKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
110-302 2.24e-36

DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350720 [Multi-domain]  Cd Length: 193  Bit Score: 135.37  E-value: 2.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 110 PTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLQSVNIKMrrnnmkgsynitkALILLPTRELSLQCYDVIR 189
Cdd:cd17962    13 PTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPS-------------ALILTPTRELAVQIEDQAK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 190 SLTK-YVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDFINyLEIVVFDEADKLLELGFKEECLKIL 268
Cdd:cd17962    80 ELMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDN-IKIVVVDEADTMLKMGFQQQVLDIL 158
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1371547147 269 DVCKFKKQILFFSATLTSDIKQLANFSLKNPVFI 302
Cdd:cd17962   159 ENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
99-303 1.19e-35

DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350724 [Multi-domain]  Cd Length: 197  Bit Score: 133.26  E-value: 1.19e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  99 LKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILerllqsVNIKMRRNNMKGSYNItkALILLPTR 178
Cdd:cd17966     2 MDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAI------VHINAQPPLERGDGPI--VLVLAPTR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 179 ELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDF--INYLeivVFDEADKLL 256
Cdd:cd17966    74 ELAQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLrrVTYL---VLDEADRML 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1371547147 257 ELGFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFIQ 303
Cdd:cd17966   151 DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
98-299 1.40e-35

DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350714 [Multi-domain]  Cd Length: 231  Bit Score: 134.30  E-value: 1.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  98 FLKVLYEQKFSNPTYIQRDVIPLALEG---------KSILANSETGSGKTLAFVLPILERLLQSVNIKMRrnnmkgsyni 168
Cdd:cd17956     1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLR---------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 169 tkALILLPTRELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKK--------RNDIFVCTPGRILDLLLNSSSDF 240
Cdd:cd17956    71 --ALIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVdtsgrylsRVDILVATPGRLVDHLNSTPGFT 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371547147 241 INYLEIVVFDEADKLLELGFKEECLKILDVCK--------------------FKKQILFFSATLTSDIKQLANFSLKNP 299
Cdd:cd17956   149 LKHLRFLVIDEADRLLNQSFQDWLETVMKALGrptapdlgsfgdanllersvRPLQKLLFSATLTRDPEKLSSLKLHRP 227
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
99-302 2.76e-33

DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350716 [Multi-domain]  Cd Length: 197  Bit Score: 126.81  E-value: 2.76e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  99 LKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLQSVNIKMRRNNmkgsyniTKALILLPTR 178
Cdd:cd17958     2 MKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQRNG-------PGVLVLTPTR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 179 ELSLQCYDVIrslTKYVTITYSLFC--GGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDF--INYLeivVFDEADK 254
Cdd:cd17958    75 ELALQIEAEC---SKYSYKGLKSVCvyGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLksITYL---VLDEADR 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1371547147 255 LLELGFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFI 302
Cdd:cd17958   149 MLDMGFEPQIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
94-302 1.86e-32

DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called DEAD box RNA helicase DEAD5) and DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH)) are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350721 [Multi-domain]  Cd Length: 196  Bit Score: 124.22  E-value: 1.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  94 ISRPFLKVLYEQKFSNPTYIQRDVIPLALEG--KSILANSETGSGKTLAFVLPILERLlqSVNIKMrrnnmkgsyniTKA 171
Cdd:cd17963     1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV--DPTLKS-----------PQA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 172 LILLPTRELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEyefKKRNDIFVCTPGRILDLLLNSSSDfINYLEIVVFDE 251
Cdd:cd17963    68 LCLAPTRELARQIGEVVEKMGKFTGVKVALAVPGNDVPRGK---KITAQIVIGTPGTVLDWLKKRQLD-LKKIKILVLDE 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1371547147 252 ADKLLEL-GFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFI 302
Cdd:cd17963   144 ADVMLDTqGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
98-303 4.11e-31

DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350701 [Multi-domain]  Cd Length: 192  Bit Score: 120.45  E-value: 4.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  98 FLKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLlqsvNIKMRRnnmkgsyniTKALILLPT 177
Cdd:cd17943     1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESL----DLERRH---------PQVLILAPT 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 178 RELSLQCYDVIRSLTKYVT-ITYSLFCGGIDIKQQEYEFKKRNdIFVCTPGRILDLL----LNSSSdfinyLEIVVFDEA 252
Cdd:cd17943    68 REIAVQIHDVFKKIGKKLEgLKCEVFIGGTPVKEDKKKLKGCH-IAVGTPGRIKQLIelgaLNVSH-----VRLFVLDEA 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1371547147 253 DKLLELGFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFIQ 303
Cdd:cd17943   142 DKLMEGSFQKDVNWIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
106-305 4.44e-31

DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD box, X isoform, or DDX14) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. This protein has multiple conserved domains and is thought to play roles in both the nucleus and cytoplasm. Nuclear roles include transcriptional regulation, mRNP assembly, pre-mRNA splicing, and mRNA export. In the cytoplasm, this protein is thought to be involved in translation, cellular signaling, and viral replication. Misregulation of this gene has been implicated in tumorigenesis. Diseases associated with DDX3 include mental retardation, X-linked 102 and agenesis of the corpus callosum, with facial anomalies and robin sequence. DDX3 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350809 [Multi-domain]  Cd Length: 249  Bit Score: 122.07  E-value: 4.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 106 KFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLQ-----SVNIKMRRNNMKGSYNItkALILLPTREL 180
Cdd:cd18051    40 RYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEqgpgeSLPSESGYYGRRKQYPL--ALVLAPTREL 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 181 SLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNS--SSDFINYLeivVFDEADKLLEL 258
Cdd:cd18051   118 ASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGkiGLDYCKYL---VLDEADRMLDM 194
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1371547147 259 GFKEECLKILDVC----KFKKQILFFSATLTSDIKQLANFSLKNPVFIQSG 305
Cdd:cd18051   195 GFEPQIRRIVEQDtmppTGERQTLMFSATFPKEIQMLARDFLDNYIFLAVG 245
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
94-297 6.14e-28

DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350810 [Multi-domain]  Cd Length: 264  Bit Score: 113.52  E-value: 6.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  94 ISRPFLKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLlqsvnikMRRNNMKGSYNITK--- 170
Cdd:cd18052    50 LCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGM-------MKEGLTASSFSEVQepq 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 171 ALILLPTRELSLQCYDVIRSLTkYVTITYSLFC-GGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNS--SSDFINYLeiv 247
Cdd:cd18052   123 ALIVAPTRELANQIFLEARKFS-YGTCIRPVVVyGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGkiSLSKLKYL--- 198
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1371547147 248 VFDEADKLLELGFKEECLKILDVC----KFKKQILFFSATLTSDIKQLANFSLK 297
Cdd:cd18052   199 ILDEADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEEIQRLAAEFLK 252
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
99-305 9.13e-28

DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350808 [Multi-domain]  Cd Length: 271  Bit Score: 113.18  E-value: 9.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  99 LKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILerllqsVNIKMRRNNMKGSYNItkALILLPTR 178
Cdd:cd18050    74 MDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAI------VHINHQPYLERGDGPI--CLVLAPTR 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 179 ELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDF--INYLeivVFDEADKLL 256
Cdd:cd18050   146 ELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLrrCTYL---VLDEADRML 222
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1371547147 257 ELGFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFIQSG 305
Cdd:cd18050   223 DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
99-305 1.96e-27

DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350807 [Multi-domain]  Cd Length: 234  Bit Score: 111.25  E-value: 1.96e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  99 LKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILerllqsVNIKMRRNNMKGSYNItkALILLPTR 178
Cdd:cd18049    36 MDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAI------VHINHQPFLERGDGPI--CLVLAPTR 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 179 ELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDfINYLEIVVFDEADKLLEL 258
Cdd:cd18049   108 ELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTN-LRRCTYLVLDEADRMLDM 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1371547147 259 GFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFIQSG 305
Cdd:cd18049   187 GFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
98-291 4.58e-27

DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 110.15  E-value: 4.58e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  98 FLKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLQsvnikmRRNNMKGSYNITKALILLPT 177
Cdd:cd17948     1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLR------YKLLAEGPFNAPRGLVITPS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 178 RELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLlnsSSDFI--NYLEIVVFDEADKL 255
Cdd:cd17948    75 RELAEQIGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLL---TSRIYslEQLRHLVLDEADTL 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1371547147 256 LELGFKEECLKILDVCKFKK-------------QILFFSATLTSDIKQL 291
Cdd:cd17948   152 LDDSFNEKLSHFLRRFPLASrrsentdgldpgtQLVLVSATMPSGVGEV 200
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
377-481 8.83e-27

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: 104.99  E-value: 8.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 377 LLYLCNNIYKNHCIIFFKTKRETHLMYLLFdLLNLRCAELHGSMSQKKRIESIMKFKKAEVDFLLTTELASRGIDIDHVL 456
Cdd:pfam00271   6 LLELLKKERGGKVLIFSQTKKTLEAELLLE-KEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVD 84
                          90       100
                  ....*....|....*....|....*
gi 1371547147 457 YVINYNVPSNVIKYVHRIGRTARIG 481
Cdd:pfam00271  85 LVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
91-302 9.44e-27

DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350804 [Multi-domain]  Cd Length: 201  Bit Score: 108.30  E-value: 9.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  91 DLYISRPFLKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLQSVNIkmrrnnmkgsyniTK 170
Cdd:cd18046     3 DMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKA-------------TQ 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 171 ALILLPTRELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDlLLNSSSDFINYLEIVVFD 250
Cdd:cd18046    70 ALVLAPTRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFD-MINRRYLRTDYIKMFVLD 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1371547147 251 EADKLLELGFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFI 302
Cdd:cd18046   149 EADEMLSRGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
91-302 2.59e-25

DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350708 [Multi-domain]  Cd Length: 208  Bit Score: 104.35  E-value: 2.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  91 DLYISRPFLKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLlqsvnikmrrnnmKGSYNITK 170
Cdd:cd17950     6 DFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQL-------------EPVDGQVS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 171 ALILLPTRELSLQCYDVIRSLTKYV-TITYSLFCGGIDIKQQEYEFKKRN-DIFVCTPGRILDLLLNSSSDfINYLEIVV 248
Cdd:cd17950    73 VLVICHTRELAFQISNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLK-LSHVKHFV 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1371547147 249 FDEADKLLE-LGFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFI 302
Cdd:cd17950   152 LDECDKMLEqLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEI 206
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
113-283 4.69e-24

DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.


Pssm-ID: 350702 [Multi-domain]  Cd Length: 202  Bit Score: 100.31  E-value: 4.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 113 IQRDVIPLALEGKSILANSETGSGKTLAFVLPILERlLQSVNIKMRRNNMKgsynitKALILLPTRELSLQCYDVIRSLT 192
Cdd:cd17944    16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEK-LQEDQQPRKRGRAP------KVLVLAPTRELANQVTKDFKDIT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 193 KYVTItySLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDfINYLEIVVFDEADKLLELGFKEECLKILDVcK 272
Cdd:cd17944    89 RKLSV--ACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLD-LTKLKHVVLDEVDQMLDMGFAEQVEEILSV-S 164
                         170
                  ....*....|....*..
gi 1371547147 273 FKK------QILFFSAT 283
Cdd:cd17944   165 YKKdsednpQTLLFSAT 181
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
99-302 4.72e-24

DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor 4A-III (EIF4AIII, also known as DDX48) is part of the exon junction complex (EJC) that plays a major role in posttranscriptional regulation of mRNA. EJC consists of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. DDX48 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350803 [Multi-domain]  Cd Length: 201  Bit Score: 100.23  E-value: 4.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  99 LKVLYEQKFSNPTYIQ-RDVIPLaLEGKSILANSETGSGKTLAFVLPILerllQSVNIKMRRnnmkgsyniTKALILLPT 177
Cdd:cd18045    11 LRGIYAYGFEKPSAIQqRAIKPI-IKGRDVIAQSQSGTGKTATFSISVL----QCLDIQVRE---------TQALILSPT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 178 RELSLQCYDVIRSLTKYVTITYSLFCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDFiNYLEIVVFDEADKLLE 257
Cdd:cd18045    77 RELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRT-RHIKMLVLDEADEMLN 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1371547147 258 LGFKEEclkILDVCKF---KKQILFFSATLTSDIKQLANFSLKNPVFI 302
Cdd:cd18045   156 KGFKEQ---IYDVYRYlppATQVVLVSATLPQDILEMTNKFMTDPIRI 200
HELICc smart00490
helicase superfamily c-terminal domain;
402-481 2.95e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 93.82  E-value: 2.95e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  402 MYLLFDLLNLRCAELHGSMSQKKRIESIMKFKKAEVDFLLTTELASRGIDIDHVLYVINYNVPSNVIKYVHRIGRTARIG 481
Cdd:smart00490   3 LAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
132-284 7.28e-19

DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350723 [Multi-domain]  Cd Length: 251  Bit Score: 86.66  E-value: 7.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 132 ETGSGKTLAFVLPILERL----LQSVNIKMRRNNMKGSYNITKALILLPTRELSLQCYDVIRSLTKYVTI---TYSLFCG 204
Cdd:cd17965    69 ETGSGKTLAYLAPLLDYLkrqeQEPFEEAEEEYESAKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLgikTFSSGFG 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 205 GIDIKQQEYeFKKRNDIFVCTPGRILDlLLNSSSDFINYLEIVVFDEADKLLELGFKEECLKILDVCKFKKQILFFSATL 284
Cdd:cd17965   149 PSYQRLQLA-FKGRIDILVTTPGKLAS-LAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATI 226
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
124-283 5.42e-18

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: 81.30  E-value: 5.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 124 GKSILANSETGSGKTLAFVLPILERLLQsvnikmrrnnmkgsyNITKALILLPTRELSLQCYDVIRSLTKYVtITYSLFC 203
Cdd:cd00046     1 GENVLITAPTGSGKTLAALLAALLLLLK---------------KGKKVLVLVPTKALALQTAERLRELFGPG-IRVAVLV 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 204 GGIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDFINYLEIVVFDEADKLLELGFKEECLKILDVCKFKK--QILFFS 281
Cdd:cd00046    65 GGSSAEEREKNKLGDADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKnaQVILLS 144

                  ..
gi 1371547147 282 AT 283
Cdd:cd00046   145 AT 146
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
89-303 5.44e-17

DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350805 [Multi-domain]  Cd Length: 205  Bit Score: 80.15  E-value: 5.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  89 WSDLYISRPFLKVLYEQKFSNPTYIQRDVIPLALEG--KSILANSETGSGKTLAFVLPILerllqsvnikmrrNNMKGSY 166
Cdd:cd18047     3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAML-------------SQVEPAN 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 167 NITKALILLPTRELSLQCYDVIRSLTKY---VTITYSlfcggIDIKQQEYEFKKRNDIFVCTPGRILDLLLNSSSDFINY 243
Cdd:cd18047    70 KYPQCLCLSPTYELALQTGKVIEQMGKFypeLKLAYA-----VRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKK 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371547147 244 LEIVVFDEADKLLEL-GFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFIQ 303
Cdd:cd18047   145 IKVFVLDEADVMIATqGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
89-303 8.47e-17

DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350806 [Multi-domain]  Cd Length: 229  Bit Score: 80.07  E-value: 8.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147  89 WSDLYISRPFLKVLYEQKFSNPTYIQRDVIPLALEG--KSILANSETGSGKTLAFVLPILERLlqsvnikmrrnNMKGSY 166
Cdd:cd18048    20 FEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV-----------DALKLY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 167 niTKALILLPTRELSLQCYDVIRSLTKY---VTITYSLFCG----GIDIKQQeyefkkrndIFVCTPGRILDLLLNSSSD 239
Cdd:cd18048    89 --PQCLCLSPTFELALQTGKVVEEMGKFcvgIQVIYAIRGNrpgkGTDIEAQ---------IVIGTPGTVLDWCFKLRLI 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371547147 240 FINYLEIVVFDEADKLLEL-GFKEECLKILDVCKFKKQILFFSATLTSDIKQLANFSLKNPVFIQ 303
Cdd:cd18048   158 DVTNISVFVLDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIK 222
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
111-284 3.05e-14

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: 71.52  E-value: 3.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 111 TYIQRDVI-PLALEGKSILANSETGSGKTLAFVLPILERLLQSvnikmrrnnmkgsynITKALILLPTRELSLQCYDVIR 189
Cdd:cd17921     3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATS---------------GGKAVYIAPTRALVNQKEADLR 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 190 SLTKYVTITYSLFCGGIDIKQQEyefKKRNDIFVCTPGRILDLLLNSSSDFINYLEIVVFDEADKL--------LELGfk 261
Cdd:cd17921    68 ERFGPLGKNVGLLTGDPSVNKLL---LAEADILVATPEKLDLLLRNGGERLIQDVRLVVVDEAHLIgdgergvvLELL-- 142
                         170       180
                  ....*....|....*....|...
gi 1371547147 262 eeCLKILDVCKfKKQILFFSATL 284
Cdd:cd17921   143 --LSRLLRINK-NARFVGLSATL 162
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
114-252 1.72e-13

DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 69.15  E-value: 1.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 114 QRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLQSVNikmrrnnmkgsyniTKALILLPTRELSlqcYDVIRSLTK 193
Cdd:cd17923     5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPG--------------SRALYLYPTKALA---QDQLRSLRE 67
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 194 YVT-----ITYSLFCGgiDIKQQEYEFKKRN--DIFVCTPgRILDLLL----NSSSDFINYLEIVVFDEA 252
Cdd:cd17923    68 LLEqlglgIRVATYDG--DTPREERRAIIRNppRILLTNP-DMLHYALlphhDRWARFLRNLRYVVLDEA 134
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
114-293 7.61e-13

Replicative superfamily II helicase [Replication, recombination and repair];


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 71.46  E-value: 7.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 114 QRDVIPLAL-EGKSILANSETGSGKTLAFVLPILERLLQSvnikmrrnnmkgsyniTKALILLPTRELslqCYDVIRSLT 192
Cdd:COG1204    27 QAEALEAGLlEGKNLVVSAPTASGKTLIAELAILKALLNG----------------GKALYIVPLRAL---ASEKYREFK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 193 KY-------VTITYslfcGGIDIkqqEYEFKKRNDIFVCTPGRiLDLLLNSSSDFINYLEIVVFDEADKL--LELGFKEE 263
Cdd:COG1204    88 RDfeelgikVGVST----GDYDS---DDEWLGRYDILVATPEK-LDSLLRNGPSWLRDVDLVVVDEAHLIddESRGPTLE 159
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1371547147 264 CL--KILDVCKfKKQILFFSATLtSDIKQLAN 293
Cdd:COG1204   160 VLlaRLRRLNP-EAQIVALSATI-GNAEEIAE 189
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
420-566 5.72e-11

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 65.91  E-value: 5.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 420 MSQKKRIESIMKFKKAEVDFLLTTELASRGIDIDHVLYVINY-NVPSNvIKYVHRIGRTARIGK--------EGIASTLY 490
Cdd:COG1111   395 LTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYePVPSE-IRSIQRKGRTGRKREgrvvvliaKGTRDEAY 473
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 491 ----LQKEKiEVKKIVKGLKksknlKILKRTIAENNvlvwykiIKENKQKLNDIIQQEKIDKEIEMSNKSIDKIKNMITF 566
Cdd:COG1111   474 ywssRRKEK-KMKSILKKLK-----KLLDKQEKEKL-------KESAQATLDEFESIKELAEDEINEKDLDEIESSENGA 540
PRK13766 PRK13766
Hef nuclease; Provisional
420-551 4.09e-10

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 62.97  E-value: 4.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 420 MSQKKRIESIMKFKKAEVDFLLTTELASRGIDIDHVLYVINYN-VPSNvIKYVHRIGRTARiGKEGIASTLY-------- 490
Cdd:PRK13766  407 MSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSE-IRSIQRKGRTGR-QEEGRVVVLIakgtrdea 484
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371547147 491 -----LQKEKiEVKKIVKGLKksknlKILKRTIAENNVLVWYKIIKENKQKLNDIIQQEKIDKEIE 551
Cdd:PRK13766  485 yywssRRKEK-KMKEELKNLK-----GILNKKLQELDEEQKGEEEEKDEQLSLDDFVKSKGKEEEE 544
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
389-479 3.56e-09

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


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 55.68  E-value: 3.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 389 CIIFFKTKRETHLMYLLF-----DLLNLRCAELHGS----------MSQKKRIESIMKFKKAEVDFLLTTELASRGIDID 453
Cdd:cd18802    28 GIIFVERRATAVVLSRLLkehpsTLAFIRCGFLIGRgnssqrkrslMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVP 107
                          90       100
                  ....*....|....*....|....*.
gi 1371547147 454 HVLYVINYNVPSNVIKYVHRIGRtAR 479
Cdd:cd18802   108 ACNLVIRFDLPKTLRSYIQSRGR-AR 132
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
133-490 7.75e-09

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 58.88  E-value: 7.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 133 TGSGKTLAFVLpILERLLqsvnikmrrnnmkgsyNITKALILLPTRELSLQCYDVIRSLTKyvtitysLFCGGIDIKQQE 212
Cdd:COG1061   109 TGTGKTVLALA-LAAELL----------------RGKRVLVLVPRRELLEQWAEELRRFLG-------DPLAGGGKKDSD 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 213 YefkkrnDIFVCTpgriLDLLLNSSS--DFINYLEIVVFDEADKLLELGFKeeclKILDVCKFKKqILFFSATLT-SDIK 289
Cdd:COG1061   165 A------PITVAT----YQSLARRAHldELGDRFGLVIIDEAHHAGAPSYR----RILEAFPAAY-RLGLTATPFrSDGR 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 290 QLANFSLKNPVF-------IQSGM-----SFDKNVDGKNTYNAYNtcntyndndnnnivvnniisnsflkisnkasfKIS 357
Cdd:COG1061   230 EILLFLFDGIVYeyslkeaIEDGYlappeYYGIRVDLTDERAEYD--------------------------------ALS 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 358 ENLKQEFVNIIQEKYRKASLLyLCNNIYKNHCIIFFKTKRETHLMYLLFDLLNLRCAELHGSMSQKKRIESIMKFKKAEV 437
Cdd:COG1061   278 ERLREALAADAERKDKILREL-LREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGEL 356
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1371547147 438 DFLLTTELASRGIDIDHVLYVInYNVP-SNVIKYVHRIGRTARIGKEGIASTLY 490
Cdd:COG1061   357 RILVTVDVLNEGVDVPRLDVAI-LLRPtGSPREFIQRLGRGLRPAPGKEDALVY 409
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
133-252 1.08e-08

DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer 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: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 55.74  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 133 TGSGKTLAFVLPILErllqsvnikMRRNNMKGSYNITKALILLPTRELSLQCYDVIRSLTKYVTITYslfCGGIDIKQQE 212
Cdd:cd18034    25 TGSGKTLIAVMLIKE---------MGELNRKEKNPKKRAVFLVPTVPLVAQQAEAIRSHTDLKVGEY---SGEMGVDKWT 92
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1371547147 213 ----YEFKKRNDIFVCTPGRILDLLLNSssdFI--NYLEIVVFDEA 252
Cdd:cd18034    93 kerwKEELEKYDVLVMTAQILLDALRHG---FLslSDINLLIFDEC 135
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
104-151 1.40e-08

Lhr-like helicase [Replication, recombination and repair];


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 58.19  E-value: 1.40e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1371547147 104 EQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLQ 151
Cdd:COG1201    19 AARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAAFLPALDELAR 66
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
420-479 3.93e-08

C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef 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: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 52.74  E-value: 3.93e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 420 MSQKKRIESIMKFKKAEVDFLLTTELASRGIDIDHVLYVINYNVPSNVIKYVHRIGRTAR 479
Cdd:cd18801    74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
114-252 6.51e-08

ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 56.00  E-value: 6.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 114 QRDVIPLALEGKSILANSETGSGKTLAFVLPILERLLQSVNikmrrnnmkgsyniTKALILLPTRELSlqcYDVIRSLTK 193
Cdd:COG1205    61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPG--------------ATALYLYPTKALA---RDQLRRLRE 123
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371547147 194 YVT-----ITYSLFCGgiDIKQQE-YEFKKRNDIFVCTPgrilD-----LLLNSS--SDFINYLEIVVFDEA 252
Cdd:COG1205   124 LAEalglgVRVATYDG--DTPPEErRWIREHPDIVLTNP----DmlhygLLPHHTrwARFFRNLRYVVIDEA 189
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
389-479 2.67e-07

C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 50.73  E-value: 2.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 389 CIIFFKTKRETHLMYllfDLLNLRCAEL---------HGSMS--QKKRIESimKFKKAEVDFLLTT---ELasrGIDIDH 454
Cdd:cd18796    41 TLVFTNTRSQAERLA---QRLRELCPDRvppdfialhHGSLSreLREEVEA--ALKRGDLKVVVATsslEL---GIDIGD 112
                          90       100
                  ....*....|....*....|....*
gi 1371547147 455 VLYVINYNVPSNVIKYVHRIGRTAR 479
Cdd:cd18796   113 VDLVIQIGSPKSVARLLQRLGRSGH 137
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
424-484 4.03e-07

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 48.08  E-value: 4.03e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371547147 424 KRIESIMKFkkaevdfLLTTELASRGIDIDHVLYVINYNVPSNVIKYVHRIGRTARIGKEG 484
Cdd:cd18785    17 EEIASSLEI-------LVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
121-252 1.20e-05

DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 46.66  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 121 ALEGKSILANSETGSGKTLAFVLpILERLLQsvniKMRRNNMKgsynitKALILLPTRELSLQCYDVIRSLT---KYVTI 197
Cdd:cd17927    14 ALKGKNTIICLPTGSGKTFVAVL-ICEHHLK----KFPAGRKG------KVVFLANKVPLVEQQKEVFRKHFerpGYKVT 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1371547147 198 TYSlfcGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLN----SSSDFinylEIVVFDEA 252
Cdd:cd17927    83 GLS---GDTSENVSVEQIVESSDVIIVTPQILVNDLKSgtivSLSDF----SLLVFDEC 134
PRK13767 PRK13767
ATP-dependent helicase; Provisional
96-150 1.49e-05

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 48.34  E-value: 1.49e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1371547147  96 RPFLKVLYEQKFSNPTYIQRDVIPLALEGKSILANSETGSGKTLAFVLPILERLL 150
Cdd:PRK13767   19 RPYVREWFKEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELF 73
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
110-252 1.40e-04

DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef 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: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 43.27  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 110 PTYIQRDVIPLALEGKSILANSeTGSGKTLAFVLPILERLLQsvnikmrrnnmKGSynitKALILLPTRELSLQCYDVIR 189
Cdd:cd18035     3 RRLYQVLIAAVALNGNTLIVLP-TGLGKTIIAILVAADRLTK-----------KGG----KVLILAPSRPLVEQHAENLK 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371547147 190 SL----TKYVTITyslfcGGIDIKQQEyEFKKRNDIFVCTPGRILDLLLNSSSDfINYLEIVVFDEA 252
Cdd:cd18035    67 RVlnipDKITSLT-----GEVKPEERA-ERWDASKIIVATPQVIENDLLAGRIT-LDDVSLLIFDEA 126
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
127-252 2.65e-04

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: 42.66  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 127 ILANSETGSGKTLAFVLPILErllQSVNIKMRRnnmkgsynitkaLIL-LPTRELSLQCYDVIRSLTKYVTITYSL---- 201
Cdd:cd17930     4 VILEAPTGSGKTEAALLWALK---LAARGGKRR------------IIYaLPTRATINQMYERIREILGRLDDEDKVlllh 68
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371547147 202 -------------FCGGIDIKQQEYEFKKRN---DIFVCTPGRILDLLLNSSSDFINYLEI----VVFDEA 252
Cdd:cd17930    69 skaalellesdeePDDDPVEAVDWALLLKRSwlaPIVVTTIDQLLESLLKYKHFERRLHGLansvVVLDEV 139
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
389-502 4.50e-04

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 40.92  E-value: 4.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 389 CIIFFKTKRETHLMYLLFDLLNLRCAELHGSMSQKKRIESIMKFKK--AEVDFLLTTELASRGIDI---DHvlyVINYNV 463
Cdd:cd18793    30 VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEdpDIRVFLLSTKAGGVGLNLtaaNR---VILYDP 106
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1371547147 464 PSNVIKYVHRIGRTARIGkegiastlylQKEKIEVKKIV 502
Cdd:cd18793   107 WWNPAVEEQAIDRAHRIG----------QKKPVVVYRLI 135
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
389-502 8.49e-04

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 42.52  E-value: 8.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 389 CIIFfkTKRETHLMYL--LFDLLNLRCAELHGSMSQKKRIESIMKFK-KAEVD-FLLTTELASRGIDI---DHvlyVINY 461
Cdd:COG0553   552 VLVF--SQFTDTLDLLeeRLEERGIEYAYLHGGTSAEERDELVDRFQeGPEAPvFLISLKAGGEGLNLtaaDH---VIHY 626
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1371547147 462 NVPSNVIKYVHRIGRTARIGkegiastlylQKEKIEVKKIV 502
Cdd:COG0553   627 DLWWNPAVEEQAIDRAHRIG----------QTRDVQVYKLV 657
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
124-251 1.39e-03

DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 39.87  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 124 GKSILANSETGSGKTLAFVLPILERLLqsvnikmrRNNMKGsyniTKALILLPTRELSlqcYDVIRSLTKYVT-----IT 198
Cdd:cd17922     1 GRNVLIAAPTGSGKTEAAFLPALSSLA--------DEPEKG----VQVLYISPLKALI---NDQERRLEEPLDeidleIP 65
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1371547147 199 YSLFCGGIDIKQQEYEFKKRNDIFVCTPgRILDLLLNS---SSDFINyLEIVVFDE 251
Cdd:cd17922    66 VAVRHGDTSQSEKAKQLKNPPGILITTP-ESLELLLVNkklRELFAG-LRYVVVDE 119
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
370-490 1.80e-03

C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 39.11  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 370 EKYRKASLLYLCNNIYKNHC-----IIFFKTKRETHLMYLLFDLLNLRCAELHGSMSQKKRIESIMKFKKAEVDFLLTTE 444
Cdd:cd18794     9 RPKDKKDEKLDLLKRIKVEHlggsgIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATV 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1371547147 445 LASRGIDIDHVLYVINYNVPSNVIKYVHRIGRTARIGKEGIASTLY 490
Cdd:cd18794    89 AFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
DEXHc_POLQ-like cd18026
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ...
119-294 3.12e-03

DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.


Pssm-ID: 350784 [Multi-domain]  Cd Length: 202  Bit Score: 39.51  E-value: 3.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 119 PLALEGKSILANSETGSGKTL-AFVLpILERLLQsvnikMRRnnmkgsynitKALILLPtrelslqcydvirsltkYVTI 197
Cdd:cd18026    28 PGLLEGRNLVYSLPTSGGKTLvAEIL-MLKRLLE-----RRK----------KALFVLP-----------------YVSI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 198 ------TYSLFCGGIDIKQQEY---------EFKKRNDIFVCTPGRiLDLLLNS--SSDFINYLEIVVFDEAD------- 253
Cdd:cd18026    75 vqekvdALSPLFEELGFRVEGYagnkgrsppKRRKSLSVAVCTIEK-ANSLVNSliEEGRLDELGLVVVDELHmlgdghr 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1371547147 254 -KLLELGFKeeclKILDVCKFKKQILFFSATLtSDIKQLANF 294
Cdd:cd18026   154 gALLELLLT----KLLYAAQKNIQIVGMSATL-PNLEELASW 190
ResIII pfam04851
Type III restriction enzyme, res subunit;
125-283 4.13e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 38.42  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 125 KSILANSETGSGKTL-AFVlpILERLLQSVNIKmrrnnmkgsynitKALILLPTRELSLQCYDvirSLTKYVTITYSLfc 203
Cdd:pfam04851  24 KRGLIVMATGSGKTLtAAK--LIARLFKKGPIK-------------KVLFLVPRKDLLEQALE---EFKKFLPNYVEI-- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 204 gGIDIKQQEYEFKKRN-DIFVCTPGRIL-DLLLNSSSDFINYLEIVVFDEADKLLELGFKeeclKILDvcKFKKQILF-F 280
Cdd:pfam04851  84 -GEIISGDKKDESVDDnKIVVTTIQSLYkALELASLELLPDFFDVIIIDEAHRSGASSYR----NILE--YFKPAFLLgL 156

                  ...
gi 1371547147 281 SAT 283
Cdd:pfam04851 157 TAT 159
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
122-251 5.25e-03

DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 38.47  E-value: 5.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 122 LEGKSILANSETGSGKTLAFVLPILERLLqsvnikmrrnnmKGSynitKALILLPTRELSLQCYDVIRSLTKY---VTIT 198
Cdd:cd18028    15 LKGENLLISIPTASGKTLIAEMAMVNTLL------------EGG----KALYLVPLRALASEKYEEFKKLEEIglkVGIS 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1371547147 199 yslfCGGIDIKQqeyEFKKRNDIFVCTPGRiLDLLLNSSSDFINYLEIVVFDE 251
Cdd:cd18028    79 ----TGDYDEDD---EWLGDYDIIVATYEK-FDSLLRHSPSWLRDVGVVVVDE 123
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
111-186 6.80e-03

DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 38.49  E-value: 6.80e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371547147 111 TYIQRDVIPLALEG-KSILANSETGSGKTLAFVLPILeRLLQSVNIKMRRNnmkgsyniTKALILLPTRELSLQCYD 186
Cdd:cd18023     3 NRIQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAIL-RLLKERNPLPWGN--------RKVVYIAPIKALCSEKYD 70
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
114-251 7.06e-03

DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members 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: 350794 [Multi-domain]  Cd Length: 204  Bit Score: 38.61  E-value: 7.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371547147 114 QRDVIPLALEGKSILANSETGSGKTLAFVLPILERLlqsvniKMRRNNMKGSynitKALILLPTRELSLQCYDVirsLTK 193
Cdd:cd18036     7 QLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHL------EKRRSAGEKG----RVVVLVNKVPLVEQQLEK---FFK 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371547147 194 YVTITYSL--FCGGIDIKQQEYEFKKRNDIFVCTPGRILDLLLN-------SSSDFinylEIVVFDE 251
Cdd:cd18036    74 YFRKGYKVtgLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSgreeervYLSDF----SLLIFDE 136
PRK13767 PRK13767
ATP-dependent helicase; Provisional
417-476 9.26e-03

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 39.48  E-value: 9.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371547147 417 HGSMSQKKRIESIMKFKKAEVDFLLTT---ELasrGIDIDHVLYVINYNVPSNVIKYVHRIGR 476
Cdd:PRK13767  321 HSSLSREVRLEVEEKLKRGELKVVVSStslEL---GIDIGYIDLVVLLGSPKSVSRLLQRIGR 380
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH